data_1N45
# 
_entry.id   1N45 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1N45         
RCSB  RCSB017495   
WWPDB D_1000017495 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2002-11-13 
_pdbx_database_PDB_obs_spr.pdb_id           1n45 
_pdbx_database_PDB_obs_spr.replace_pdb_id   1qq8 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1QQ8 'X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME, 2.08 ANGSTROMS' unspecified 
PDB 1N3U 'X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME, CRYSTAL FORM B' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1N45 
_pdbx_database_status.recvd_initial_deposition_date   2002-10-30 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Schuller, D.J.'            1 
'Wilks, A.'                 2 
'Ortiz de Montellano, P.R.' 3 
'Poulos, T.L.'              4 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 'Comparison of the Heme-free and -bound Crystal Structures of Human Heme Oxygenase-1' 'To be Published' ? ?   ?   ?    ? ? 
?         0353 ? ? ?             
1       'Crystal Structure of Human Heme Oxygenase-1'                                         Nat.Struct.Biol.  6 903 905 1999 
NSBIEW US 1072-8368 2024 ? ? 10.1038/13264 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Schuller, D.J.'            1  
primary 'Wilks, A.'                 2  
primary 'Ortiz de Montellano, P.R.' 3  
primary 'Poulos, T.L.'              4  
1       'Lad, L.'                   5  
1       'Schuller, D.J.'            6  
1       'Friedman, J.P.'            7  
1       'Li, H.'                    8  
1       'Ortiz de Montellano, P.R.' 9  
1       'Poulos, T.L.'              10 
# 
_cell.entry_id           1N45 
_cell.length_a           61.441 
_cell.length_b           54.534 
_cell.length_c           70.969 
_cell.angle_alpha        90.00 
_cell.angle_beta         99.05 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1N45 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'heme oxygenase 1'                26898.615 2   1.14.99.3 ? 'Residues 1-233' ? 
2 non-polymer syn 'SULFATE ION'                     96.063    1   ?         ? ?                ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ?         ? ?                ? 
4 water       nat water                             18.015    425 ?         ? ?                ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        HO-1 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFP
EELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSS
GEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFP
EELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSS
GEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   ARG n 
1 4   PRO n 
1 5   GLN n 
1 6   PRO n 
1 7   ASP n 
1 8   SER n 
1 9   MET n 
1 10  PRO n 
1 11  GLN n 
1 12  ASP n 
1 13  LEU n 
1 14  SER n 
1 15  GLU n 
1 16  ALA n 
1 17  LEU n 
1 18  LYS n 
1 19  GLU n 
1 20  ALA n 
1 21  THR n 
1 22  LYS n 
1 23  GLU n 
1 24  VAL n 
1 25  HIS n 
1 26  THR n 
1 27  GLN n 
1 28  ALA n 
1 29  GLU n 
1 30  ASN n 
1 31  ALA n 
1 32  GLU n 
1 33  PHE n 
1 34  MET n 
1 35  ARG n 
1 36  ASN n 
1 37  PHE n 
1 38  GLN n 
1 39  LYS n 
1 40  GLY n 
1 41  GLN n 
1 42  VAL n 
1 43  THR n 
1 44  ARG n 
1 45  ASP n 
1 46  GLY n 
1 47  PHE n 
1 48  LYS n 
1 49  LEU n 
1 50  VAL n 
1 51  MET n 
1 52  ALA n 
1 53  SER n 
1 54  LEU n 
1 55  TYR n 
1 56  HIS n 
1 57  ILE n 
1 58  TYR n 
1 59  VAL n 
1 60  ALA n 
1 61  LEU n 
1 62  GLU n 
1 63  GLU n 
1 64  GLU n 
1 65  ILE n 
1 66  GLU n 
1 67  ARG n 
1 68  ASN n 
1 69  LYS n 
1 70  GLU n 
1 71  SER n 
1 72  PRO n 
1 73  VAL n 
1 74  PHE n 
1 75  ALA n 
1 76  PRO n 
1 77  VAL n 
1 78  TYR n 
1 79  PHE n 
1 80  PRO n 
1 81  GLU n 
1 82  GLU n 
1 83  LEU n 
1 84  HIS n 
1 85  ARG n 
1 86  LYS n 
1 87  ALA n 
1 88  ALA n 
1 89  LEU n 
1 90  GLU n 
1 91  GLN n 
1 92  ASP n 
1 93  LEU n 
1 94  ALA n 
1 95  PHE n 
1 96  TRP n 
1 97  TYR n 
1 98  GLY n 
1 99  PRO n 
1 100 ARG n 
1 101 TRP n 
1 102 GLN n 
1 103 GLU n 
1 104 VAL n 
1 105 ILE n 
1 106 PRO n 
1 107 TYR n 
1 108 THR n 
1 109 PRO n 
1 110 ALA n 
1 111 MET n 
1 112 GLN n 
1 113 ARG n 
1 114 TYR n 
1 115 VAL n 
1 116 LYS n 
1 117 ARG n 
1 118 LEU n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 GLY n 
1 123 ARG n 
1 124 THR n 
1 125 GLU n 
1 126 PRO n 
1 127 GLU n 
1 128 LEU n 
1 129 LEU n 
1 130 VAL n 
1 131 ALA n 
1 132 HIS n 
1 133 ALA n 
1 134 TYR n 
1 135 THR n 
1 136 ARG n 
1 137 TYR n 
1 138 LEU n 
1 139 GLY n 
1 140 ASP n 
1 141 LEU n 
1 142 SER n 
1 143 GLY n 
1 144 GLY n 
1 145 GLN n 
1 146 VAL n 
1 147 LEU n 
1 148 LYS n 
1 149 LYS n 
1 150 ILE n 
1 151 ALA n 
1 152 GLN n 
1 153 LYS n 
1 154 ALA n 
1 155 LEU n 
1 156 ASP n 
1 157 LEU n 
1 158 PRO n 
1 159 SER n 
1 160 SER n 
1 161 GLY n 
1 162 GLU n 
1 163 GLY n 
1 164 LEU n 
1 165 ALA n 
1 166 PHE n 
1 167 PHE n 
1 168 THR n 
1 169 PHE n 
1 170 PRO n 
1 171 ASN n 
1 172 ILE n 
1 173 ALA n 
1 174 SER n 
1 175 ALA n 
1 176 THR n 
1 177 LYS n 
1 178 PHE n 
1 179 LYS n 
1 180 GLN n 
1 181 LEU n 
1 182 TYR n 
1 183 ARG n 
1 184 SER n 
1 185 ARG n 
1 186 MET n 
1 187 ASN n 
1 188 SER n 
1 189 LEU n 
1 190 GLU n 
1 191 MET n 
1 192 THR n 
1 193 PRO n 
1 194 ALA n 
1 195 VAL n 
1 196 ARG n 
1 197 GLN n 
1 198 ARG n 
1 199 VAL n 
1 200 ILE n 
1 201 GLU n 
1 202 GLU n 
1 203 ALA n 
1 204 LYS n 
1 205 THR n 
1 206 ALA n 
1 207 PHE n 
1 208 LEU n 
1 209 LEU n 
1 210 ASN n 
1 211 ILE n 
1 212 GLN n 
1 213 LEU n 
1 214 PHE n 
1 215 GLU n 
1 216 GLU n 
1 217 LEU n 
1 218 GLN n 
1 219 GLU n 
1 220 LEU n 
1 221 LEU n 
1 222 THR n 
1 223 HIS n 
1 224 ASP n 
1 225 THR n 
1 226 LYS n 
1 227 ASP n 
1 228 GLN n 
1 229 SER n 
1 230 PRO n 
1 231 SER n 
1 232 ARG n 
1 233 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 'HMOX1, HO1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'DH5 alpha' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'delta 233-hHO-1' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HMOX1_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFP
EELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSS
GEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRA
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_accession          P09601 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1N45 A 1 ? 233 ? P09601 1 ? 233 ? 1 233 
2 1 1N45 B 1 ? 233 ? P09601 1 ? 233 ? 1 233 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?    'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?    'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?    'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?    'C4 H7 N O4'       133.103 
GLN 'L-peptide linking' y GLUTAMINE                         ?    'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?    'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?    'C2 H5 N O2'       75.067  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?    'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
SO4 non-polymer         . 'SULFATE ION'                     ?    'O4 S -2'          96.063  
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          1N45 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_percent_sol   40.54 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            301 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'ammonium sulfate, HEPES, 1,6-hexanediol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 301K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1999-07-27 
_diffrn_detector.details                mirror 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'curved crystal' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL7-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL7-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.08 
# 
_reflns.entry_id                     1N45 
_reflns.observed_criterion_sigma_F   0.0 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.d_resolution_high            1.50 
_reflns.d_resolution_low             50.0 
_reflns.number_all                   74389 
_reflns.number_obs                   74186 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.051 
_reflns.pdbx_netI_over_sigmaI        11.5 
_reflns.B_iso_Wilson_estimate        19.8 
_reflns.pdbx_redundancy              3.7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.50 
_reflns_shell.d_res_low              1.53 
_reflns_shell.percent_possible_all   96.8 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.484 
_reflns_shell.meanI_over_sigI_obs    2.2 
_reflns_shell.pdbx_redundancy        3 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3564 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1N45 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             50.0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     70267 
_refine.ls_number_reflns_obs                     70267 
_refine.ls_number_reflns_R_free                  3714 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_work                       0.151 
_refine.ls_R_factor_R_free                       0.217 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'SAD, SIRAS, NCS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ANISOTROPIC 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3507 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         91 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               4023 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        50.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d  0.010 ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d 0.030 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1N45 
_pdbx_refine.R_factor_all_no_cutoff                      0.151 
_pdbx_refine.R_factor_obs_no_cutoff                      0.1489 
_pdbx_refine.number_reflns_obs_no_cutoff                 ? 
_pdbx_refine.free_R_factor_no_cutoff                     ? 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            ? 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     ? 
_pdbx_refine.R_factor_all_4sig_cutoff                    ? 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  1N45 
_struct.title                     'X-RAY CRYSTAL STRUCTURE OF HUMAN HEME OXYGENASE-1 (HO-1) IN COMPLEX WITH ITS SUBSTRATE HEME' 
_struct.pdbx_descriptor           'heme oxygenase 1 (E.C.1.14.99.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1N45 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'Alpha Helices, heme-binding site, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 'the enzyme is a monomer' ? 
2 ?                         ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ASP A 12  ? THR A 21  ? ASP A 12  THR A 21  1 ? 10 
HELX_P HELX_P2  2  THR A 21  ? ALA A 31  ? THR A 21  ALA A 31  1 ? 11 
HELX_P HELX_P3  3  ALA A 31  ? LYS A 39  ? ALA A 31  LYS A 39  1 ? 9  
HELX_P HELX_P4  4  THR A 43  ? LYS A 69  ? THR A 43  LYS A 69  1 ? 27 
HELX_P HELX_P5  5  PHE A 74  ? TYR A 78  ? PHE A 74  TYR A 78  5 ? 5  
HELX_P HELX_P6  6  PHE A 79  ? HIS A 84  ? PHE A 79  HIS A 84  1 ? 6  
HELX_P HELX_P7  7  ARG A 85  ? GLY A 98  ? ARG A 85  GLY A 98  1 ? 14 
HELX_P HELX_P8  8  ARG A 100 ? VAL A 104 ? ARG A 100 VAL A 104 5 ? 5  
HELX_P HELX_P9  9  THR A 108 ? GLU A 125 ? THR A 108 GLU A 125 1 ? 18 
HELX_P HELX_P10 10 LEU A 128 ? ASP A 156 ? LEU A 128 ASP A 156 1 ? 29 
HELX_P HELX_P11 11 LEU A 164 ? THR A 168 ? LEU A 164 THR A 168 5 ? 5  
HELX_P HELX_P12 12 SER A 174 ? LEU A 189 ? SER A 174 LEU A 189 1 ? 16 
HELX_P HELX_P13 13 THR A 192 ? LEU A 221 ? THR A 192 LEU A 221 1 ? 30 
HELX_P HELX_P14 14 ASP B 12  ? ALA B 31  ? ASP B 12  ALA B 31  1 ? 20 
HELX_P HELX_P15 15 ALA B 31  ? LYS B 39  ? ALA B 31  LYS B 39  1 ? 9  
HELX_P HELX_P16 16 THR B 43  ? LYS B 69  ? THR B 43  LYS B 69  1 ? 27 
HELX_P HELX_P17 17 PHE B 74  ? TYR B 78  ? PHE B 74  TYR B 78  5 ? 5  
HELX_P HELX_P18 18 PHE B 79  ? HIS B 84  ? PHE B 79  HIS B 84  1 ? 6  
HELX_P HELX_P19 19 ARG B 85  ? GLY B 98  ? ARG B 85  GLY B 98  1 ? 14 
HELX_P HELX_P20 20 ARG B 100 ? ILE B 105 ? ARG B 100 ILE B 105 1 ? 6  
HELX_P HELX_P21 21 THR B 108 ? GLU B 125 ? THR B 108 GLU B 125 1 ? 18 
HELX_P HELX_P22 22 LEU B 128 ? ASP B 156 ? LEU B 128 ASP B 156 1 ? 29 
HELX_P HELX_P23 23 LEU B 164 ? THR B 168 ? LEU B 164 THR B 168 5 ? 5  
HELX_P HELX_P24 24 SER B 174 ? LEU B 189 ? SER B 174 LEU B 189 1 ? 16 
HELX_P HELX_P25 25 THR B 192 ? HIS B 223 ? THR B 192 HIS B 223 1 ? 32 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1 metalc ? ? B HIS 25 NE2 ? ? ? 1_555 E HEM . FE ? ? B HIS 25  B HEM 300 1_555 ? ? ? ? ? ? ? 1.900 ? 
metalc2 metalc ? ? A HIS 25 NE2 ? ? ? 1_555 D HEM . FE ? ? A HIS 25  A HEM 300 1_555 ? ? ? ? ? ? ? 1.986 ? 
metalc3 metalc ? ? D HEM .  FE  ? ? ? 1_555 F HOH . O  ? ? A HEM 300 A HOH 301 1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc4 metalc ? ? E HEM .  FE  ? ? ? 1_555 G HOH . O  ? ? B HEM 300 B HOH 301 1_555 ? ? ? ? ? ? ? 2.072 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 A 234' 
AC2 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM A 300' 
AC3 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE HEM B 300' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5  LYS A 148 ? LYS A 148 . ? 1_555 ? 
2  AC1 5  GLN A 152 ? GLN A 152 . ? 1_555 ? 
3  AC1 5  HOH F .   ? HOH A 498 . ? 1_555 ? 
4  AC1 5  SER B 160 ? SER B 160 . ? 1_555 ? 
5  AC1 5  HOH G .   ? HOH B 328 . ? 1_555 ? 
6  AC2 16 LYS A 18  ? LYS A 18  . ? 1_555 ? 
7  AC2 16 HIS A 25  ? HIS A 25  . ? 1_555 ? 
8  AC2 16 GLN A 38  ? GLN A 38  . ? 1_555 ? 
9  AC2 16 TYR A 134 ? TYR A 134 . ? 1_555 ? 
10 AC2 16 THR A 135 ? THR A 135 . ? 1_555 ? 
11 AC2 16 ARG A 136 ? ARG A 136 . ? 1_555 ? 
12 AC2 16 GLY A 139 ? GLY A 139 . ? 1_555 ? 
13 AC2 16 SER A 142 ? SER A 142 . ? 1_555 ? 
14 AC2 16 GLY A 143 ? GLY A 143 . ? 1_555 ? 
15 AC2 16 ARG A 183 ? ARG A 183 . ? 1_555 ? 
16 AC2 16 PHE A 207 ? PHE A 207 . ? 1_555 ? 
17 AC2 16 ASN A 210 ? ASN A 210 . ? 1_555 ? 
18 AC2 16 PHE A 214 ? PHE A 214 . ? 1_555 ? 
19 AC2 16 HOH F .   ? HOH A 301 . ? 1_555 ? 
20 AC2 16 HOH F .   ? HOH A 392 . ? 1_555 ? 
21 AC2 16 HOH F .   ? HOH A 510 . ? 1_555 ? 
22 AC3 14 LYS B 18  ? LYS B 18  . ? 1_555 ? 
23 AC3 14 HIS B 25  ? HIS B 25  . ? 1_555 ? 
24 AC3 14 GLU B 29  ? GLU B 29  . ? 1_555 ? 
25 AC3 14 GLN B 38  ? GLN B 38  . ? 1_555 ? 
26 AC3 14 TYR B 134 ? TYR B 134 . ? 1_555 ? 
27 AC3 14 THR B 135 ? THR B 135 . ? 1_555 ? 
28 AC3 14 GLY B 139 ? GLY B 139 . ? 1_555 ? 
29 AC3 14 ARG B 183 ? ARG B 183 . ? 1_555 ? 
30 AC3 14 PHE B 207 ? PHE B 207 . ? 1_555 ? 
31 AC3 14 ASN B 210 ? ASN B 210 . ? 1_555 ? 
32 AC3 14 PHE B 214 ? PHE B 214 . ? 1_555 ? 
33 AC3 14 HOH G .   ? HOH B 301 . ? 1_555 ? 
34 AC3 14 HOH G .   ? HOH B 409 . ? 1_555 ? 
35 AC3 14 HOH G .   ? HOH B 460 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1N45 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1N45 
_atom_sites.fract_transf_matrix[1][1]   0.016276 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002592 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018337 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.014268 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PRO A 1 10  ? 3.430   -0.136  16.885  1.00 59.27  ? 10  PRO A N   1 
ATOM   2    C  CA  . PRO A 1 10  ? 3.328   1.299   17.212  1.00 55.59  ? 10  PRO A CA  1 
ATOM   3    C  C   . PRO A 1 10  ? 2.099   1.839   16.491  1.00 47.86  ? 10  PRO A C   1 
ATOM   4    O  O   . PRO A 1 10  ? 1.649   1.128   15.594  1.00 49.44  ? 10  PRO A O   1 
ATOM   5    C  CB  . PRO A 1 10  ? 4.625   1.861   16.656  1.00 58.68  ? 10  PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 10  ? 5.603   0.743   16.799  1.00 61.06  ? 10  PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 10  ? 4.840   -0.551  16.794  1.00 61.43  ? 10  PRO A CD  1 
ATOM   8    N  N   . GLN A 1 11  ? 1.608   2.995   16.871  1.00 43.44  ? 11  GLN A N   1 
ATOM   9    C  CA  . GLN A 1 11  ? 0.453   3.659   16.272  1.00 42.11  ? 11  GLN A CA  1 
ATOM   10   C  C   . GLN A 1 11  ? 0.702   4.073   14.832  1.00 41.43  ? 11  GLN A C   1 
ATOM   11   O  O   . GLN A 1 11  ? -0.053  3.869   13.882  1.00 43.64  ? 11  GLN A O   1 
ATOM   12   C  CB  . GLN A 1 11  ? 0.091   4.853   17.166  1.00 48.76  ? 11  GLN A CB  1 
ATOM   13   C  CG  . GLN A 1 11  ? -0.888  5.870   16.617  1.00 61.68  ? 11  GLN A CG  1 
ATOM   14   C  CD  . GLN A 1 11  ? -1.176  6.960   17.649  1.00 70.58  ? 11  GLN A CD  1 
ATOM   15   O  OE1 . GLN A 1 11  ? -0.422  7.116   18.618  1.00 87.90  ? 11  GLN A OE1 1 
ATOM   16   N  NE2 . GLN A 1 11  ? -2.250  7.727   17.476  1.00 85.01  ? 11  GLN A NE2 1 
ATOM   17   N  N   . ASP A 1 12  ? 1.838   4.715   14.590  1.00 34.93  ? 12  ASP A N   1 
ATOM   18   C  CA  . ASP A 1 12  ? 2.075   5.271   13.267  1.00 33.35  ? 12  ASP A CA  1 
ATOM   19   C  C   . ASP A 1 12  ? 2.569   4.174   12.354  1.00 29.52  ? 12  ASP A C   1 
ATOM   20   O  O   . ASP A 1 12  ? 3.486   3.455   12.757  1.00 30.24  ? 12  ASP A O   1 
ATOM   21   C  CB  . ASP A 1 12  ? 3.136   6.375   13.338  1.00 34.55  ? 12  ASP A CB  1 
ATOM   22   C  CG  . ASP A 1 12  ? 2.655   7.602   14.079  1.00 44.02  ? 12  ASP A CG  1 
ATOM   23   O  OD1 . ASP A 1 12  ? 1.412   7.728   14.236  1.00 57.27  ? 12  ASP A OD1 1 
ATOM   24   O  OD2 . ASP A 1 12  ? 3.503   8.426   14.505  1.00 60.48  ? 12  ASP A OD2 1 
ATOM   25   N  N   . LEU A 1 13  ? 1.976   4.096   11.181  1.00 28.44  ? 13  LEU A N   1 
ATOM   26   C  CA  . LEU A 1 13  ? 2.387   3.129   10.190  1.00 29.10  ? 13  LEU A CA  1 
ATOM   27   C  C   . LEU A 1 13  ? 3.870   3.242   9.887   1.00 26.98  ? 13  LEU A C   1 
ATOM   28   O  O   . LEU A 1 13  ? 4.511   2.209   9.756   1.00 26.75  ? 13  LEU A O   1 
ATOM   29   C  CB  . LEU A 1 13  ? 1.583   3.329   8.895   1.00 29.74  ? 13  LEU A CB  1 
ATOM   30   C  CG  . LEU A 1 13  ? 1.926   2.380   7.741   1.00 28.77  ? 13  LEU A CG  1 
ATOM   31   C  CD1 . LEU A 1 13  ? 1.641   0.922   8.065   1.00 35.47  ? 13  LEU A CD1 1 
ATOM   32   C  CD2 . LEU A 1 13  ? 1.174   2.816   6.478   1.00 34.96  ? 13  LEU A CD2 1 
ATOM   33   N  N   . SER A 1 14  ? 4.394   4.458   9.777   1.00 28.79  ? 14  SER A N   1 
ATOM   34   C  CA  . SER A 1 14  ? 5.805   4.581   9.414   1.00 30.47  ? 14  SER A CA  1 
ATOM   35   C  C   . SER A 1 14  ? 6.699   3.908   10.458  1.00 28.82  ? 14  SER A C   1 
ATOM   36   O  O   . SER A 1 14  ? 7.680   3.282   10.042  1.00 33.24  ? 14  SER A O   1 
ATOM   37   C  CB  . SER A 1 14  ? 6.144   6.056   9.241   1.00 31.64  ? 14  SER A CB  1 
ATOM   38   O  OG  . SER A 1 14  ? 6.123   6.648   10.536  1.00 32.56  ? 14  SER A OG  1 
ATOM   39   N  N   . GLU A 1 15  ? 6.361   4.032   11.746  1.00 33.89  ? 15  GLU A N   1 
ATOM   40   C  CA  . GLU A 1 15  ? 7.068   3.350   12.819  1.00 32.84  ? 15  GLU A CA  1 
ATOM   41   C  C   . GLU A 1 15  ? 6.765   1.858   12.834  1.00 31.57  ? 15  GLU A C   1 
ATOM   42   O  O   . GLU A 1 15  ? 7.655   1.031   13.089  1.00 34.30  ? 15  GLU A O   1 
ATOM   43   C  CB  . GLU A 1 15  ? 6.716   3.939   14.194  1.00 37.12  ? 15  GLU A CB  1 
ATOM   44   C  CG  . GLU A 1 15  ? 7.063   5.398   14.406  1.00 50.02  ? 15  GLU A CG  1 
ATOM   45   C  CD  . GLU A 1 15  ? 7.307   5.741   15.855  1.00 56.18  ? 15  GLU A CD  1 
ATOM   46   O  OE1 . GLU A 1 15  ? 6.347   5.740   16.659  1.00 63.73  ? 15  GLU A OE1 1 
ATOM   47   O  OE2 . GLU A 1 15  ? 8.479   6.022   16.204  1.00 79.25  ? 15  GLU A OE2 1 
ATOM   48   N  N   . ALA A 1 16  ? 5.522   1.459   12.589  1.00 29.96  ? 16  ALA A N   1 
ATOM   49   C  CA  . ALA A 1 16  ? 5.195   0.034   12.507  1.00 31.32  ? 16  ALA A CA  1 
ATOM   50   C  C   . ALA A 1 16  ? 6.046   -0.675  11.455  1.00 27.75  ? 16  ALA A C   1 
ATOM   51   O  O   . ALA A 1 16  ? 6.587   -1.771  11.623  1.00 29.71  ? 16  ALA A O   1 
ATOM   52   C  CB  . ALA A 1 16  ? 3.712   -0.162  12.209  1.00 28.27  ? 16  ALA A CB  1 
ATOM   53   N  N   . LEU A 1 17  ? 6.172   -0.018  10.299  1.00 26.92  ? 17  LEU A N   1 
ATOM   54   C  CA  . LEU A 1 17  ? 6.935   -0.593  9.194   1.00 25.28  ? 17  LEU A CA  1 
ATOM   55   C  C   . LEU A 1 17  ? 8.404   -0.736  9.537   1.00 28.18  ? 17  LEU A C   1 
ATOM   56   O  O   . LEU A 1 17  ? 9.006   -1.768  9.286   1.00 28.12  ? 17  LEU A O   1 
ATOM   57   C  CB  . LEU A 1 17  ? 6.789   0.258   7.927   1.00 25.79  ? 17  LEU A CB  1 
ATOM   58   C  CG  . LEU A 1 17  ? 5.440   0.129   7.199   1.00 27.20  ? 17  LEU A CG  1 
ATOM   59   C  CD1 . LEU A 1 17  ? 5.203   1.250   6.204   1.00 24.70  ? 17  LEU A CD1 1 
ATOM   60   C  CD2 . LEU A 1 17  ? 5.323   -1.198  6.454   1.00 32.30  ? 17  LEU A CD2 1 
ATOM   61   N  N   . LYS A 1 18  ? 8.919   0.342   10.113  1.00 30.56  ? 18  LYS A N   1 
ATOM   62   C  CA  . LYS A 1 18  ? 10.343  0.342   10.492  1.00 31.61  ? 18  LYS A CA  1 
ATOM   63   C  C   . LYS A 1 18  ? 10.620  -0.788  11.475  1.00 31.61  ? 18  LYS A C   1 
ATOM   64   O  O   . LYS A 1 18  ? 11.583  -1.537  11.323  1.00 29.52  ? 18  LYS A O   1 
ATOM   65   C  CB  . LYS A 1 18  ? 10.721  1.711   11.053  1.00 33.72  ? 18  LYS A CB  1 
ATOM   66   C  CG  . LYS A 1 18  ? 12.048  1.793   11.782  1.00 39.47  ? 18  LYS A CG  1 
ATOM   67   C  CD  . LYS A 1 18  ? 12.862  3.015   11.440  1.00 44.24  ? 18  LYS A CD  1 
ATOM   68   C  CE  . LYS A 1 18  ? 13.855  3.412   12.516  1.00 49.83  ? 18  LYS A CE  1 
ATOM   69   N  NZ  . LYS A 1 18  ? 14.426  4.761   12.254  1.00 66.33  ? 18  LYS A NZ  1 
ATOM   70   N  N   . GLU A 1 19  ? 9.754   -0.902  12.484  1.00 33.79  ? 19  GLU A N   1 
ATOM   71   C  CA  . GLU A 1 19  ? 9.959   -1.918  13.502  1.00 31.59  ? 19  GLU A CA  1 
ATOM   72   C  C   . GLU A 1 19  ? 9.736   -3.313  12.923  1.00 32.16  ? 19  GLU A C   1 
ATOM   73   O  O   . GLU A 1 19  ? 10.534  -4.211  13.221  1.00 38.93  ? 19  GLU A O   1 
ATOM   74   C  CB  . GLU A 1 19  ? 9.013   -1.699  14.687  1.00 39.96  ? 19  GLU A CB  1 
ATOM   75   C  CG  . GLU A 1 19  ? 8.407   -3.012  15.156  1.00 52.75  ? 19  GLU A CG  1 
ATOM   76   C  CD  . GLU A 1 19  ? 7.937   -2.924  16.593  1.00 59.72  ? 19  GLU A CD  1 
ATOM   77   O  OE1 . GLU A 1 19  ? 7.993   -3.953  17.303  1.00 79.04  ? 19  GLU A OE1 1 
ATOM   78   O  OE2 . GLU A 1 19  ? 7.524   -1.825  17.021  1.00 67.46  ? 19  GLU A OE2 1 
ATOM   79   N  N   . ALA A 1 20  ? 8.690   -3.502  12.114  1.00 31.93  ? 20  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 20  ? 8.396   -4.848  11.612  1.00 30.61  ? 20  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 20  ? 9.483   -5.335  10.665  1.00 27.35  ? 20  ALA A C   1 
ATOM   82   O  O   . ALA A 1 20  ? 9.686   -6.551  10.502  1.00 30.87  ? 20  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 20  ? 7.084   -4.934  10.872  1.00 29.70  ? 20  ALA A CB  1 
ATOM   84   N  N   . THR A 1 21  ? 10.197  -4.416  10.021  1.00 27.28  ? 21  THR A N   1 
ATOM   85   C  CA  . THR A 1 21  ? 11.155  -4.912  8.999   1.00 28.14  ? 21  THR A CA  1 
ATOM   86   C  C   . THR A 1 21  ? 12.590  -4.875  9.490   1.00 28.26  ? 21  THR A C   1 
ATOM   87   O  O   . THR A 1 21  ? 13.513  -5.056  8.690   1.00 26.51  ? 21  THR A O   1 
ATOM   88   C  CB  . THR A 1 21  ? 11.050  -4.148  7.659   1.00 30.25  ? 21  THR A CB  1 
ATOM   89   O  OG1 . THR A 1 21  ? 11.240  -2.736  7.881   1.00 25.46  ? 21  THR A OG1 1 
ATOM   90   C  CG2 . THR A 1 21  ? 9.686   -4.398  7.045   1.00 27.23  ? 21  THR A CG2 1 
ATOM   91   N  N   . LYS A 1 22  ? 12.783  -4.655  10.786  1.00 28.99  ? 22  LYS A N   1 
ATOM   92   C  CA  . LYS A 1 22  ? 14.172  -4.588  11.267  1.00 29.89  ? 22  LYS A CA  1 
ATOM   93   C  C   . LYS A 1 22  ? 14.944  -5.861  10.966  1.00 29.29  ? 22  LYS A C   1 
ATOM   94   O  O   . LYS A 1 22  ? 16.090  -5.825  10.541  1.00 30.05  ? 22  LYS A O   1 
ATOM   95   C  CB  . LYS A 1 22  ? 14.238  -4.299  12.772  1.00 38.87  ? 22  LYS A CB  1 
ATOM   96   C  CG  . LYS A 1 22  ? 15.506  -3.553  13.154  1.00 54.79  ? 22  LYS A CG  1 
ATOM   97   C  CD  . LYS A 1 22  ? 15.585  -3.218  14.632  1.00 65.28  ? 22  LYS A CD  1 
ATOM   98   C  CE  . LYS A 1 22  ? 16.989  -3.465  15.179  1.00 73.19  ? 22  LYS A CE  1 
ATOM   99   N  NZ  . LYS A 1 22  ? 17.145  -3.255  16.649  1.00 76.77  ? 22  LYS A NZ  1 
ATOM   100  N  N   . GLU A 1 23  ? 14.285  -6.983  11.233  1.00 27.44  ? 23  GLU A N   1 
ATOM   101  C  CA  . GLU A 1 23  ? 15.024  -8.253  11.132  1.00 29.76  ? 23  GLU A CA  1 
ATOM   102  C  C   . GLU A 1 23  ? 15.242  -8.628  9.678   1.00 29.51  ? 23  GLU A C   1 
ATOM   103  O  O   . GLU A 1 23  ? 16.298  -9.140  9.304   1.00 28.38  ? 23  GLU A O   1 
ATOM   104  C  CB  . GLU A 1 23  ? 14.279  -9.273  11.984  1.00 37.38  ? 23  GLU A CB  1 
ATOM   105  C  CG  . GLU A 1 23  ? 14.140  -10.641 11.339  1.00 54.45  ? 23  GLU A CG  1 
ATOM   106  C  CD  . GLU A 1 23  ? 12.716  -10.757 10.802  1.00 69.06  ? 23  GLU A CD  1 
ATOM   107  O  OE1 . GLU A 1 23  ? 12.444  -11.578 9.901   1.00 93.59  ? 23  GLU A OE1 1 
ATOM   108  O  OE2 . GLU A 1 23  ? 11.878  -9.977  11.323  1.00 94.05  ? 23  GLU A OE2 1 
ATOM   109  N  N   . VAL A 1 24  ? 14.285  -8.355  8.787   1.00 26.64  ? 24  VAL A N   1 
ATOM   110  C  CA  . VAL A 1 24  ? 14.622  -8.667  7.395   1.00 25.30  ? 24  VAL A CA  1 
ATOM   111  C  C   . VAL A 1 24  ? 15.619  -7.634  6.851   1.00 24.82  ? 24  VAL A C   1 
ATOM   112  O  O   . VAL A 1 24  ? 16.356  -8.044  5.945   1.00 23.02  ? 24  VAL A O   1 
ATOM   113  C  CB  . VAL A 1 24  ? 13.459  -8.754  6.386   1.00 25.89  ? 24  VAL A CB  1 
ATOM   114  C  CG1 . VAL A 1 24  ? 12.599  -9.982  6.593   1.00 31.75  ? 24  VAL A CG1 1 
ATOM   115  C  CG2 . VAL A 1 24  ? 12.614  -7.483  6.433   1.00 27.66  ? 24  VAL A CG2 1 
ATOM   116  N  N   . HIS A 1 25  ? 15.671  -6.391  7.323   1.00 23.76  ? 25  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 25  ? 16.717  -5.481  6.830   1.00 24.32  ? 25  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 25  ? 18.092  -6.057  7.161   1.00 22.77  ? 25  HIS A C   1 
ATOM   119  O  O   . HIS A 1 25  ? 19.085  -6.056  6.427   1.00 23.11  ? 25  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 25  ? 16.528  -4.068  7.419   1.00 23.51  ? 25  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 25  ? 17.405  -3.001  6.819   1.00 27.76  ? 25  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 25  ? 18.753  -2.882  7.128   1.00 26.11  ? 25  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 25  ? 17.156  -2.027  5.922   1.00 24.63  ? 25  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 25  ? 19.266  -1.882  6.448   1.00 25.17  ? 25  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 25  ? 18.322  -1.340  5.710   1.00 23.11  ? 25  HIS A NE2 1 
ATOM   126  N  N   . THR A 1 26  ? 18.216  -6.618  8.371   1.00 27.43  ? 26  THR A N   1 
ATOM   127  C  CA  . THR A 1 26  ? 19.491  -7.212  8.771   1.00 27.96  ? 26  THR A CA  1 
ATOM   128  C  C   . THR A 1 26  ? 19.820  -8.411  7.881   1.00 25.42  ? 26  THR A C   1 
ATOM   129  O  O   . THR A 1 26  ? 20.967  -8.631  7.519   1.00 24.89  ? 26  THR A O   1 
ATOM   130  C  CB  . THR A 1 26  ? 19.469  -7.646  10.252  1.00 32.60  ? 26  THR A CB  1 
ATOM   131  O  OG1 . THR A 1 26  ? 19.168  -6.494  11.055  1.00 32.87  ? 26  THR A OG1 1 
ATOM   132  C  CG2 . THR A 1 26  ? 20.819  -8.168  10.727  1.00 42.27  ? 26  THR A CG2 1 
ATOM   133  N  N   . GLN A 1 27  ? 18.779  -9.178  7.540   1.00 24.59  ? 27  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 27  ? 18.996  -10.335 6.668   1.00 25.83  ? 27  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 27  ? 19.576  -9.862  5.349   1.00 25.70  ? 27  GLN A C   1 
ATOM   136  O  O   . GLN A 1 27  ? 20.452  -10.473 4.737   1.00 27.01  ? 27  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 27  ? 17.663  -11.064 6.564   1.00 31.32  ? 27  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 27  ? 17.616  -12.360 5.790   1.00 38.80  ? 27  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 27  ? 16.272  -13.079 5.772   1.00 42.63  ? 27  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 27  ? 15.422  -12.781 6.610   1.00 42.75  ? 27  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 27  ? 16.070  -14.016 4.839   1.00 45.41  ? 27  GLN A NE2 1 
ATOM   142  N  N   . ALA A 1 28  ? 19.110  -8.717  4.874   1.00 23.85  ? 28  ALA A N   1 
ATOM   143  C  CA  . ALA A 1 28  ? 19.612  -8.136  3.621   1.00 24.80  ? 28  ALA A CA  1 
ATOM   144  C  C   . ALA A 1 28  ? 21.062  -7.672  3.771   1.00 24.46  ? 28  ALA A C   1 
ATOM   145  O  O   . ALA A 1 28  ? 21.903  -7.889  2.900   1.00 29.35  ? 28  ALA A O   1 
ATOM   146  C  CB  . ALA A 1 28  ? 18.674  -7.015  3.148   1.00 23.73  ? 28  ALA A CB  1 
ATOM   147  N  N   . GLU A 1 29  ? 21.335  -7.030  4.920   1.00 25.54  ? 29  GLU A N   1 
ATOM   148  C  CA  . GLU A 1 29  ? 22.685  -6.599  5.223   1.00 26.83  ? 29  GLU A CA  1 
ATOM   149  C  C   . GLU A 1 29  ? 23.624  -7.806  5.330   1.00 27.54  ? 29  GLU A C   1 
ATOM   150  O  O   . GLU A 1 29  ? 24.834  -7.617  5.119   1.00 31.06  ? 29  GLU A O   1 
ATOM   151  C  CB  . GLU A 1 29  ? 22.822  -5.817  6.537   1.00 30.34  ? 29  GLU A CB  1 
ATOM   152  C  CG  . GLU A 1 29  ? 22.092  -4.492  6.578   1.00 33.26  ? 29  GLU A CG  1 
ATOM   153  C  CD  . GLU A 1 29  ? 22.032  -3.972  8.000   1.00 34.43  ? 29  GLU A CD  1 
ATOM   154  O  OE1 . GLU A 1 29  ? 23.113  -3.639  8.532   1.00 38.37  ? 29  GLU A OE1 1 
ATOM   155  O  OE2 . GLU A 1 29  ? 20.948  -3.905  8.596   1.00 34.06  ? 29  GLU A OE2 1 
ATOM   156  N  N   . ASN A 1 30  ? 23.075  -8.959  5.658   1.00 25.44  ? 30  ASN A N   1 
ATOM   157  C  CA  . ASN A 1 30  ? 23.900  -10.131 5.901   1.00 25.99  ? 30  ASN A CA  1 
ATOM   158  C  C   . ASN A 1 30  ? 24.061  -10.961 4.649   1.00 29.06  ? 30  ASN A C   1 
ATOM   159  O  O   . ASN A 1 30  ? 24.856  -11.914 4.608   1.00 31.33  ? 30  ASN A O   1 
ATOM   160  C  CB  . ASN A 1 30  ? 23.238  -10.988 6.981   1.00 25.58  ? 30  ASN A CB  1 
ATOM   161  C  CG  . ASN A 1 30  ? 23.523  -10.374 8.348   1.00 25.94  ? 30  ASN A CG  1 
ATOM   162  O  OD1 . ASN A 1 30  ? 24.361  -9.481  8.500   1.00 29.32  ? 30  ASN A OD1 1 
ATOM   163  N  ND2 . ASN A 1 30  ? 22.818  -10.847 9.372   1.00 26.73  ? 30  ASN A ND2 1 
ATOM   164  N  N   . ALA A 1 31  ? 23.280  -10.599 3.628   1.00 29.10  ? 31  ALA A N   1 
ATOM   165  C  CA  . ALA A 1 31  ? 23.341  -11.438 2.412   1.00 28.54  ? 31  ALA A CA  1 
ATOM   166  C  C   . ALA A 1 31  ? 24.743  -11.341 1.812   1.00 30.84  ? 31  ALA A C   1 
ATOM   167  O  O   . ALA A 1 31  ? 25.392  -10.304 1.830   1.00 31.61  ? 31  ALA A O   1 
ATOM   168  C  CB  . ALA A 1 31  ? 22.218  -11.071 1.461   1.00 37.68  ? 31  ALA A CB  1 
ATOM   169  N  N   . GLU A 1 32  ? 25.242  -12.456 1.284   1.00 34.02  ? 32  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 32  ? 26.642  -12.582 0.876   1.00 35.77  ? 32  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 32  ? 27.030  -11.486 -0.099  1.00 35.96  ? 32  GLU A C   1 
ATOM   172  O  O   . GLU A 1 32  ? 28.048  -10.790 -0.010  1.00 39.71  ? 32  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 32  ? 26.812  -14.014 0.342   1.00 36.94  ? 32  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 32  ? 28.197  -14.339 -0.160  1.00 38.95  ? 32  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 32  ? 28.260  -15.741 -0.730  1.00 44.92  ? 32  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 32  ? 27.240  -16.430 -0.925  1.00 45.54  ? 32  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 32  ? 29.405  -16.143 -0.993  1.00 56.32  ? 32  GLU A OE2 1 
ATOM   178  N  N   . PHE A 1 33  ? 26.158  -11.273 -1.100  1.00 32.77  ? 33  PHE A N   1 
ATOM   179  C  CA  . PHE A 1 33  ? 26.420  -10.228 -2.095  1.00 31.35  ? 33  PHE A CA  1 
ATOM   180  C  C   . PHE A 1 33  ? 26.540  -8.879  -1.408  1.00 31.25  ? 33  PHE A C   1 
ATOM   181  O  O   . PHE A 1 33  ? 27.423  -8.079  -1.689  1.00 33.45  ? 33  PHE A O   1 
ATOM   182  C  CB  . PHE A 1 33  ? 25.321  -10.217 -3.138  1.00 34.13  ? 33  PHE A CB  1 
ATOM   183  C  CG  . PHE A 1 33  ? 25.553  -9.270  -4.288  1.00 39.70  ? 33  PHE A CG  1 
ATOM   184  C  CD1 . PHE A 1 33  ? 26.324  -9.626  -5.370  1.00 42.70  ? 33  PHE A CD1 1 
ATOM   185  C  CD2 . PHE A 1 33  ? 24.955  -8.025  -4.251  1.00 42.51  ? 33  PHE A CD2 1 
ATOM   186  C  CE1 . PHE A 1 33  ? 26.474  -8.729  -6.407  1.00 44.79  ? 33  PHE A CE1 1 
ATOM   187  C  CE2 . PHE A 1 33  ? 25.115  -7.116  -5.273  1.00 44.28  ? 33  PHE A CE2 1 
ATOM   188  C  CZ  . PHE A 1 33  ? 25.903  -7.493  -6.353  1.00 43.95  ? 33  PHE A CZ  1 
ATOM   189  N  N   . MET A 1 34  ? 25.638  -8.607  -0.468  1.00 29.92  ? 34  MET A N   1 
ATOM   190  C  CA  . MET A 1 34  ? 25.769  -7.350  0.266   1.00 33.01  ? 34  MET A CA  1 
ATOM   191  C  C   . MET A 1 34  ? 26.912  -7.381  1.269   1.00 35.77  ? 34  MET A C   1 
ATOM   192  O  O   . MET A 1 34  ? 27.489  -6.323  1.491   1.00 36.71  ? 34  MET A O   1 
ATOM   193  C  CB  . MET A 1 34  ? 24.436  -7.061  0.956   1.00 36.04  ? 34  MET A CB  1 
ATOM   194  C  CG  . MET A 1 34  ? 23.349  -6.771  -0.068  1.00 37.26  ? 34  MET A CG  1 
ATOM   195  S  SD  . MET A 1 34  ? 23.548  -5.131  -0.752  1.00 44.35  ? 34  MET A SD  1 
ATOM   196  C  CE  . MET A 1 34  ? 24.166  -5.444  -2.381  1.00 58.77  ? 34  MET A CE  1 
ATOM   197  N  N   . ARG A 1 35  ? 27.261  -8.520  1.868   1.00 36.53  ? 35  ARG A N   1 
ATOM   198  C  CA  . ARG A 1 35  ? 28.434  -8.548  2.739   1.00 39.29  ? 35  ARG A CA  1 
ATOM   199  C  C   . ARG A 1 35  ? 29.604  -8.109  1.858   1.00 41.94  ? 35  ARG A C   1 
ATOM   200  O  O   . ARG A 1 35  ? 30.423  -7.278  2.227   1.00 41.26  ? 35  ARG A O   1 
ATOM   201  C  CB  . ARG A 1 35  ? 28.737  -9.893  3.410   1.00 40.87  ? 35  ARG A CB  1 
ATOM   202  C  CG  . ARG A 1 35  ? 27.698  -10.299 4.436   1.00 42.44  ? 35  ARG A CG  1 
ATOM   203  C  CD  . ARG A 1 35  ? 28.057  -11.446 5.339   1.00 46.41  ? 35  ARG A CD  1 
ATOM   204  N  NE  . ARG A 1 35  ? 28.592  -12.630 4.696   1.00 50.72  ? 35  ARG A NE  1 
ATOM   205  C  CZ  . ARG A 1 35  ? 27.941  -13.725 4.357   1.00 47.96  ? 35  ARG A CZ  1 
ATOM   206  N  NH1 . ARG A 1 35  ? 26.644  -13.889 4.566   1.00 46.95  ? 35  ARG A NH1 1 
ATOM   207  N  NH2 . ARG A 1 35  ? 28.579  -14.737 3.772   1.00 55.17  ? 35  ARG A NH2 1 
ATOM   208  N  N   . ASN A 1 36  ? 29.633  -8.689  0.665   1.00 39.20  ? 36  ASN A N   1 
ATOM   209  C  CA  . ASN A 1 36  ? 30.841  -8.382  -0.118  1.00 39.31  ? 36  ASN A CA  1 
ATOM   210  C  C   . ASN A 1 36  ? 30.855  -6.924  -0.530  1.00 42.70  ? 36  ASN A C   1 
ATOM   211  O  O   . ASN A 1 36  ? 31.902  -6.283  -0.472  1.00 42.19  ? 36  ASN A O   1 
ATOM   212  C  CB  . ASN A 1 36  ? 30.934  -9.348  -1.297  1.00 43.09  ? 36  ASN A CB  1 
ATOM   213  C  CG  . ASN A 1 36  ? 31.027  -10.812 -0.903  1.00 49.84  ? 36  ASN A CG  1 
ATOM   214  O  OD1 . ASN A 1 36  ? 30.672  -11.682 -1.719  1.00 54.44  ? 36  ASN A OD1 1 
ATOM   215  N  ND2 . ASN A 1 36  ? 31.482  -11.174 0.299   1.00 59.31  ? 36  ASN A ND2 1 
ATOM   216  N  N   . PHE A 1 37  ? 29.689  -6.411  -0.926  1.00 39.82  ? 37  PHE A N   1 
ATOM   217  C  CA  . PHE A 1 37  ? 29.602  -4.992  -1.312  1.00 38.85  ? 37  PHE A CA  1 
ATOM   218  C  C   . PHE A 1 37  ? 30.100  -4.145  -0.147  1.00 41.27  ? 37  PHE A C   1 
ATOM   219  O  O   . PHE A 1 37  ? 30.952  -3.260  -0.293  1.00 45.02  ? 37  PHE A O   1 
ATOM   220  C  CB  . PHE A 1 37  ? 28.180  -4.699  -1.715  1.00 36.64  ? 37  PHE A CB  1 
ATOM   221  C  CG  . PHE A 1 37  ? 27.722  -3.621  -2.646  1.00 44.88  ? 37  PHE A CG  1 
ATOM   222  C  CD1 . PHE A 1 37  ? 28.010  -2.291  -2.438  1.00 49.73  ? 37  PHE A CD1 1 
ATOM   223  C  CD2 . PHE A 1 37  ? 26.964  -3.929  -3.766  1.00 51.66  ? 37  PHE A CD2 1 
ATOM   224  C  CE1 . PHE A 1 37  ? 27.577  -1.303  -3.291  1.00 54.32  ? 37  PHE A CE1 1 
ATOM   225  C  CE2 . PHE A 1 37  ? 26.503  -2.955  -4.630  1.00 54.91  ? 37  PHE A CE2 1 
ATOM   226  C  CZ  . PHE A 1 37  ? 26.803  -1.625  -4.389  1.00 55.27  ? 37  PHE A CZ  1 
ATOM   227  N  N   . GLN A 1 38  ? 29.586  -4.413  1.054   1.00 38.66  ? 38  GLN A N   1 
ATOM   228  C  CA  . GLN A 1 38  ? 30.016  -3.672  2.240   1.00 37.79  ? 38  GLN A CA  1 
ATOM   229  C  C   . GLN A 1 38  ? 31.503  -3.844  2.539   1.00 37.05  ? 38  GLN A C   1 
ATOM   230  O  O   . GLN A 1 38  ? 32.202  -2.934  3.005   1.00 40.80  ? 38  GLN A O   1 
ATOM   231  C  CB  . GLN A 1 38  ? 29.177  -4.094  3.445   1.00 39.12  ? 38  GLN A CB  1 
ATOM   232  C  CG  . GLN A 1 38  ? 27.727  -3.661  3.480   1.00 41.34  ? 38  GLN A CG  1 
ATOM   233  C  CD  . GLN A 1 38  ? 26.979  -4.319  4.642   1.00 41.20  ? 38  GLN A CD  1 
ATOM   234  O  OE1 . GLN A 1 38  ? 26.937  -3.813  5.766   1.00 41.80  ? 38  GLN A OE1 1 
ATOM   235  N  NE2 . GLN A 1 38  ? 26.372  -5.477  4.382   1.00 44.45  ? 38  GLN A NE2 1 
ATOM   236  N  N   . LYS A 1 39  ? 32.123  -5.003  2.294   1.00 37.62  ? 39  LYS A N   1 
ATOM   237  C  CA  . LYS A 1 39  ? 33.555  -5.136  2.564   1.00 35.00  ? 39  LYS A CA  1 
ATOM   238  C  C   . LYS A 1 39  ? 34.387  -4.522  1.448   1.00 41.72  ? 39  LYS A C   1 
ATOM   239  O  O   . LYS A 1 39  ? 35.590  -4.772  1.385   1.00 46.52  ? 39  LYS A O   1 
ATOM   240  C  CB  . LYS A 1 39  ? 33.874  -6.625  2.727   1.00 38.10  ? 39  LYS A CB  1 
ATOM   241  C  CG  . LYS A 1 39  ? 33.206  -7.230  3.967   1.00 37.32  ? 39  LYS A CG  1 
ATOM   242  C  CD  . LYS A 1 39  ? 33.643  -8.686  4.140   1.00 41.34  ? 39  LYS A CD  1 
ATOM   243  C  CE  . LYS A 1 39  ? 33.321  -9.157  5.546   1.00 45.81  ? 39  LYS A CE  1 
ATOM   244  N  NZ  . LYS A 1 39  ? 31.934  -8.778  5.957   1.00 57.04  ? 39  LYS A NZ  1 
ATOM   245  N  N   . GLY A 1 40  ? 33.747  -3.763  0.568   1.00 42.15  ? 40  GLY A N   1 
ATOM   246  C  CA  . GLY A 1 40  ? 34.190  -3.166  -0.656  1.00 43.60  ? 40  GLY A CA  1 
ATOM   247  C  C   . GLY A 1 40  ? 34.632  -4.143  -1.726  1.00 43.90  ? 40  GLY A C   1 
ATOM   248  O  O   . GLY A 1 40  ? 35.454  -3.814  -2.585  1.00 47.76  ? 40  GLY A O   1 
ATOM   249  N  N   . GLN A 1 41  ? 34.135  -5.371  -1.739  1.00 43.85  ? 41  GLN A N   1 
ATOM   250  C  CA  . GLN A 1 41  ? 34.513  -6.311  -2.790  1.00 47.76  ? 41  GLN A CA  1 
ATOM   251  C  C   . GLN A 1 41  ? 33.440  -6.355  -3.864  1.00 49.94  ? 41  GLN A C   1 
ATOM   252  O  O   . GLN A 1 41  ? 32.945  -7.419  -4.245  1.00 66.02  ? 41  GLN A O   1 
ATOM   253  C  CB  . GLN A 1 41  ? 34.748  -7.692  -2.187  1.00 51.33  ? 41  GLN A CB  1 
ATOM   254  C  CG  . GLN A 1 41  ? 35.811  -7.669  -1.077  1.00 57.35  ? 41  GLN A CG  1 
ATOM   255  C  CD  . GLN A 1 41  ? 35.697  -8.945  -0.257  1.00 57.18  ? 41  GLN A CD  1 
ATOM   256  O  OE1 . GLN A 1 41  ? 35.238  -8.935  0.882   1.00 65.60  ? 41  GLN A OE1 1 
ATOM   257  N  NE2 . GLN A 1 41  ? 36.100  -10.063 -0.855  1.00 78.07  ? 41  GLN A NE2 1 
ATOM   258  N  N   . VAL A 1 42  ? 33.068  -5.167  -4.350  1.00 45.53  ? 42  VAL A N   1 
ATOM   259  C  CA  . VAL A 1 42  ? 32.144  -5.197  -5.481  1.00 37.09  ? 42  VAL A CA  1 
ATOM   260  C  C   . VAL A 1 42  ? 32.978  -5.135  -6.754  1.00 33.61  ? 42  VAL A C   1 
ATOM   261  O  O   . VAL A 1 42  ? 33.992  -4.436  -6.751  1.00 38.61  ? 42  VAL A O   1 
ATOM   262  C  CB  . VAL A 1 42  ? 31.130  -4.053  -5.503  1.00 38.34  ? 42  VAL A CB  1 
ATOM   263  C  CG1 . VAL A 1 42  ? 31.778  -2.737  -5.908  1.00 43.51  ? 42  VAL A CG1 1 
ATOM   264  C  CG2 . VAL A 1 42  ? 29.987  -4.384  -6.465  1.00 46.26  ? 42  VAL A CG2 1 
ATOM   265  N  N   . THR A 1 43  ? 32.570  -5.832  -7.794  1.00 32.07  ? 43  THR A N   1 
ATOM   266  C  CA  . THR A 1 43  ? 33.237  -5.686  -9.082  1.00 29.91  ? 43  THR A CA  1 
ATOM   267  C  C   . THR A 1 43  ? 32.337  -4.905  -10.035 1.00 26.06  ? 43  THR A C   1 
ATOM   268  O  O   . THR A 1 43  ? 31.141  -4.773  -9.780  1.00 22.61  ? 43  THR A O   1 
ATOM   269  C  CB  . THR A 1 43  ? 33.547  -7.041  -9.725  1.00 33.08  ? 43  THR A CB  1 
ATOM   270  O  OG1 . THR A 1 43  ? 32.338  -7.644  -10.230 1.00 37.18  ? 43  THR A OG1 1 
ATOM   271  C  CG2 . THR A 1 43  ? 34.092  -8.025  -8.705  1.00 36.76  ? 43  THR A CG2 1 
ATOM   272  N  N   . ARG A 1 44  ? 32.885  -4.402  -11.139 1.00 23.96  ? 44  ARG A N   1 
ATOM   273  C  CA  . ARG A 1 44  ? 32.051  -3.686  -12.105 1.00 23.16  ? 44  ARG A CA  1 
ATOM   274  C  C   . ARG A 1 44  ? 30.950  -4.563  -12.690 1.00 21.42  ? 44  ARG A C   1 
ATOM   275  O  O   . ARG A 1 44  ? 29.808  -4.147  -12.889 1.00 23.39  ? 44  ARG A O   1 
ATOM   276  C  CB  . ARG A 1 44  ? 32.901  -3.126  -13.253 1.00 28.60  ? 44  ARG A CB  1 
ATOM   277  C  CG  . ARG A 1 44  ? 33.689  -1.903  -12.808 1.00 31.03  ? 44  ARG A CG  1 
ATOM   278  C  CD  . ARG A 1 44  ? 34.151  -1.062  -13.977 1.00 38.16  ? 44  ARG A CD  1 
ATOM   279  N  NE  . ARG A 1 44  ? 35.153  -0.098  -13.584 1.00 43.01  ? 44  ARG A NE  1 
ATOM   280  C  CZ  . ARG A 1 44  ? 35.332  1.126   -14.058 1.00 54.03  ? 44  ARG A CZ  1 
ATOM   281  N  NH1 . ARG A 1 44  ? 34.560  1.649   -14.995 1.00 77.65  ? 44  ARG A NH1 1 
ATOM   282  N  NH2 . ARG A 1 44  ? 36.324  1.847   -13.564 1.00 69.67  ? 44  ARG A NH2 1 
ATOM   283  N  N   . ASP A 1 45  ? 31.319  -5.830  -12.924 1.00 22.71  ? 45  ASP A N   1 
ATOM   284  C  CA  . ASP A 1 45  ? 30.294  -6.756  -13.423 1.00 22.04  ? 45  ASP A CA  1 
ATOM   285  C  C   . ASP A 1 45  ? 29.169  -6.962  -12.420 1.00 18.90  ? 45  ASP A C   1 
ATOM   286  O  O   . ASP A 1 45  ? 27.996  -7.064  -12.796 1.00 21.77  ? 45  ASP A O   1 
ATOM   287  C  CB  . ASP A 1 45  ? 30.912  -8.113  -13.731 1.00 25.72  ? 45  ASP A CB  1 
ATOM   288  C  CG  . ASP A 1 45  ? 31.697  -8.164  -15.040 1.00 31.77  ? 45  ASP A CG  1 
ATOM   289  O  OD1 . ASP A 1 45  ? 31.572  -7.273  -15.920 1.00 34.78  ? 45  ASP A OD1 1 
ATOM   290  O  OD2 . ASP A 1 45  ? 32.480  -9.126  -15.207 1.00 38.50  ? 45  ASP A OD2 1 
ATOM   291  N  N   . GLY A 1 46  ? 29.483  -7.053  -11.142 1.00 21.83  ? 46  GLY A N   1 
ATOM   292  C  CA  . GLY A 1 46  ? 28.453  -7.197  -10.118 1.00 20.38  ? 46  GLY A CA  1 
ATOM   293  C  C   . GLY A 1 46  ? 27.637  -5.921  -10.003 1.00 19.50  ? 46  GLY A C   1 
ATOM   294  O  O   . GLY A 1 46  ? 26.396  -6.021  -9.900  1.00 21.95  ? 46  GLY A O   1 
ATOM   295  N  N   . PHE A 1 47  ? 28.310  -4.780  -10.042 1.00 18.64  ? 47  PHE A N   1 
ATOM   296  C  CA  . PHE A 1 47  ? 27.597  -3.497  -9.975  1.00 19.50  ? 47  PHE A CA  1 
ATOM   297  C  C   . PHE A 1 47  ? 26.634  -3.278  -11.119 1.00 17.59  ? 47  PHE A C   1 
ATOM   298  O  O   . PHE A 1 47  ? 25.495  -2.819  -10.911 1.00 18.55  ? 47  PHE A O   1 
ATOM   299  C  CB  . PHE A 1 47  ? 28.599  -2.322  -9.918  1.00 20.54  ? 47  PHE A CB  1 
ATOM   300  C  CG  . PHE A 1 47  ? 27.896  -1.024  -9.553  1.00 22.76  ? 47  PHE A CG  1 
ATOM   301  C  CD1 . PHE A 1 47  ? 27.443  -0.803  -8.260  1.00 27.76  ? 47  PHE A CD1 1 
ATOM   302  C  CD2 . PHE A 1 47  ? 27.694  -0.058  -10.541 1.00 24.06  ? 47  PHE A CD2 1 
ATOM   303  C  CE1 . PHE A 1 47  ? 26.804  0.390   -7.963  1.00 28.92  ? 47  PHE A CE1 1 
ATOM   304  C  CE2 . PHE A 1 47  ? 27.083  1.150   -10.238 1.00 26.95  ? 47  PHE A CE2 1 
ATOM   305  C  CZ  . PHE A 1 47  ? 26.641  1.356   -8.943  1.00 27.73  ? 47  PHE A CZ  1 
ATOM   306  N  N   . LYS A 1 48  ? 27.066  -3.589  -12.339 1.00 19.33  ? 48  LYS A N   1 
ATOM   307  C  CA  . LYS A 1 48  ? 26.240  -3.529  -13.532 1.00 20.13  ? 48  LYS A CA  1 
ATOM   308  C  C   . LYS A 1 48  ? 24.967  -4.338  -13.350 1.00 18.41  ? 48  LYS A C   1 
ATOM   309  O  O   . LYS A 1 48  ? 23.880  -3.892  -13.695 1.00 18.18  ? 48  LYS A O   1 
ATOM   310  C  CB  . LYS A 1 48  ? 26.971  -4.100  -14.757 1.00 24.74  ? 48  LYS A CB  1 
ATOM   311  C  CG  . LYS A 1 48  ? 27.967  -3.067  -15.221 1.00 31.27  ? 48  LYS A CG  1 
ATOM   312  C  CD  . LYS A 1 48  ? 28.964  -3.719  -16.193 1.00 36.21  ? 48  LYS A CD  1 
ATOM   313  C  CE  . LYS A 1 48  ? 28.265  -3.836  -17.530 1.00 37.03  ? 48  LYS A CE  1 
ATOM   314  N  NZ  . LYS A 1 48  ? 29.193  -4.391  -18.543 1.00 50.57  ? 48  LYS A NZ  1 
ATOM   315  N  N   . LEU A 1 49  ? 25.146  -5.528  -12.774 1.00 18.66  ? 49  LEU A N   1 
ATOM   316  C  CA  . LEU A 1 49  ? 23.972  -6.381  -12.586 1.00 17.63  ? 49  LEU A CA  1 
ATOM   317  C  C   . LEU A 1 49  ? 22.960  -5.786  -11.614 1.00 19.52  ? 49  LEU A C   1 
ATOM   318  O  O   . LEU A 1 49  ? 21.762  -5.903  -11.846 1.00 18.24  ? 49  LEU A O   1 
ATOM   319  C  CB  . LEU A 1 49  ? 24.346  -7.777  -12.079 1.00 21.80  ? 49  LEU A CB  1 
ATOM   320  C  CG  . LEU A 1 49  ? 24.509  -8.914  -13.033 1.00 27.55  ? 49  LEU A CG  1 
ATOM   321  C  CD1 . LEU A 1 49  ? 24.889  -10.157 -12.250 1.00 24.46  ? 49  LEU A CD1 1 
ATOM   322  C  CD2 . LEU A 1 49  ? 23.242  -9.112  -13.848 1.00 34.59  ? 49  LEU A CD2 1 
ATOM   323  N  N   . VAL A 1 50  ? 23.486  -5.173  -10.535 1.00 17.24  ? 50  VAL A N   1 
ATOM   324  C  CA  . VAL A 1 50  ? 22.500  -4.586  -9.619  1.00 17.42  ? 50  VAL A CA  1 
ATOM   325  C  C   . VAL A 1 50  ? 21.819  -3.382  -10.275 1.00 17.93  ? 50  VAL A C   1 
ATOM   326  O  O   . VAL A 1 50  ? 20.612  -3.203  -10.033 1.00 15.80  ? 50  VAL A O   1 
ATOM   327  C  CB  A VAL A 1 50  ? 23.101  -4.146  -8.285  0.50 20.87  ? 50  VAL A CB  1 
ATOM   328  C  CB  B VAL A 1 50  ? 23.017  -4.154  -8.246  0.50 21.43  ? 50  VAL A CB  1 
ATOM   329  C  CG1 A VAL A 1 50  ? 24.399  -3.389  -8.405  0.50 23.66  ? 50  VAL A CG1 1 
ATOM   330  C  CG1 B VAL A 1 50  ? 24.013  -5.164  -7.705  0.50 19.22  ? 50  VAL A CG1 1 
ATOM   331  C  CG2 A VAL A 1 50  ? 22.118  -3.225  -7.551  0.50 28.02  ? 50  VAL A CG2 1 
ATOM   332  C  CG2 B VAL A 1 50  ? 23.605  -2.756  -8.283  0.50 27.62  ? 50  VAL A CG2 1 
ATOM   333  N  N   . MET A 1 51  ? 22.530  -2.587  -11.069 1.00 15.75  ? 51  MET A N   1 
ATOM   334  C  CA  . MET A 1 51  ? 21.923  -1.453  -11.750 1.00 14.39  ? 51  MET A CA  1 
ATOM   335  C  C   . MET A 1 51  ? 20.890  -1.930  -12.765 1.00 14.06  ? 51  MET A C   1 
ATOM   336  O  O   . MET A 1 51  ? 19.807  -1.320  -12.834 1.00 15.31  ? 51  MET A O   1 
ATOM   337  C  CB  . MET A 1 51  ? 22.965  -0.541  -12.384 1.00 16.10  ? 51  MET A CB  1 
ATOM   338  C  CG  . MET A 1 51  ? 23.921  0.063   -11.370 1.00 19.03  ? 51  MET A CG  1 
ATOM   339  S  SD  . MET A 1 51  ? 23.185  1.266   -10.294 1.00 24.15  ? 51  MET A SD  1 
ATOM   340  C  CE  . MET A 1 51  ? 23.140  2.695   -11.364 1.00 27.74  ? 51  MET A CE  1 
ATOM   341  N  N   . ALA A 1 52  ? 21.166  -3.002  -13.496 1.00 15.63  ? 52  ALA A N   1 
ATOM   342  C  CA  . ALA A 1 52  ? 20.142  -3.554  -14.379 1.00 13.83  ? 52  ALA A CA  1 
ATOM   343  C  C   . ALA A 1 52  ? 18.916  -3.989  -13.581 1.00 15.64  ? 52  ALA A C   1 
ATOM   344  O  O   . ALA A 1 52  ? 17.783  -3.722  -14.012 1.00 15.92  ? 52  ALA A O   1 
ATOM   345  C  CB  . ALA A 1 52  ? 20.723  -4.708  -15.193 1.00 16.39  ? 52  ALA A CB  1 
ATOM   346  N  N   . SER A 1 53  ? 19.127  -4.636  -12.457 1.00 14.18  ? 53  SER A N   1 
ATOM   347  C  CA  . SER A 1 53  ? 18.019  -5.092  -11.608 1.00 15.20  ? 53  SER A CA  1 
ATOM   348  C  C   . SER A 1 53  ? 17.117  -3.899  -11.231 1.00 13.76  ? 53  SER A C   1 
ATOM   349  O  O   . SER A 1 53  ? 15.909  -3.984  -11.382 1.00 17.27  ? 53  SER A O   1 
ATOM   350  C  CB  . SER A 1 53  ? 18.472  -5.764  -10.322 1.00 16.28  ? 53  SER A CB  1 
ATOM   351  O  OG  . SER A 1 53  ? 19.281  -6.896  -10.573 1.00 16.81  ? 53  SER A OG  1 
ATOM   352  N  N   . LEU A 1 54  ? 17.773  -2.840  -10.726 1.00 15.97  ? 54  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 54  ? 17.069  -1.654  -10.254 1.00 14.90  ? 54  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 54  ? 16.248  -1.024  -11.375 1.00 13.55  ? 54  LEU A C   1 
ATOM   355  O  O   . LEU A 1 54  ? 15.090  -0.587  -11.158 1.00 15.66  ? 54  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 54  ? 18.033  -0.623  -9.607  1.00 16.68  ? 54  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 54  ? 18.641  -0.999  -8.273  1.00 15.55  ? 54  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 54  ? 19.783  -0.063  -7.905  1.00 23.29  ? 54  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 54  ? 17.624  -0.975  -7.133  1.00 25.54  ? 54  LEU A CD2 1 
ATOM   360  N  N   . TYR A 1 55  ? 16.796  -0.980  -12.585 1.00 15.43  ? 55  TYR A N   1 
ATOM   361  C  CA  . TYR A 1 55  ? 15.994  -0.457  -13.715 1.00 15.89  ? 55  TYR A CA  1 
ATOM   362  C  C   . TYR A 1 55  ? 14.694  -1.213  -13.849 1.00 15.32  ? 55  TYR A C   1 
ATOM   363  O  O   . TYR A 1 55  ? 13.601  -0.658  -13.886 1.00 15.43  ? 55  TYR A O   1 
ATOM   364  C  CB  . TYR A 1 55  ? 16.860  -0.516  -14.988 1.00 16.56  ? 55  TYR A CB  1 
ATOM   365  C  CG  . TYR A 1 55  ? 16.005  -0.275  -16.212 1.00 15.41  ? 55  TYR A CG  1 
ATOM   366  C  CD1 . TYR A 1 55  ? 15.618  1.020   -16.574 1.00 17.02  ? 55  TYR A CD1 1 
ATOM   367  C  CD2 . TYR A 1 55  ? 15.567  -1.339  -17.001 1.00 16.92  ? 55  TYR A CD2 1 
ATOM   368  C  CE1 . TYR A 1 55  ? 14.817  1.223   -17.711 1.00 19.50  ? 55  TYR A CE1 1 
ATOM   369  C  CE2 . TYR A 1 55  ? 14.783  -1.133  -18.094 1.00 17.50  ? 55  TYR A CE2 1 
ATOM   370  C  CZ  . TYR A 1 55  ? 14.409  0.131   -18.456 1.00 15.78  ? 55  TYR A CZ  1 
ATOM   371  O  OH  . TYR A 1 55  ? 13.613  0.260   -19.578 1.00 18.13  ? 55  TYR A OH  1 
ATOM   372  N  N   . HIS A 1 56  ? 14.739  -2.558  -13.962 1.00 15.36  ? 56  HIS A N   1 
ATOM   373  C  CA  . HIS A 1 56  ? 13.530  -3.344  -14.101 1.00 14.23  ? 56  HIS A CA  1 
ATOM   374  C  C   . HIS A 1 56  ? 12.539  -3.135  -12.963 1.00 16.25  ? 56  HIS A C   1 
ATOM   375  O  O   . HIS A 1 56  ? 11.330  -3.002  -13.218 1.00 17.67  ? 56  HIS A O   1 
ATOM   376  C  CB  . HIS A 1 56  ? 13.899  -4.829  -14.184 1.00 17.19  ? 56  HIS A CB  1 
ATOM   377  C  CG  . HIS A 1 56  ? 14.633  -5.163  -15.446 1.00 18.70  ? 56  HIS A CG  1 
ATOM   378  N  ND1 . HIS A 1 56  ? 15.896  -5.731  -15.554 1.00 20.49  ? 56  HIS A ND1 1 
ATOM   379  C  CD2 . HIS A 1 56  ? 14.199  -4.970  -16.705 1.00 16.96  ? 56  HIS A CD2 1 
ATOM   380  C  CE1 . HIS A 1 56  ? 16.205  -5.882  -16.850 1.00 19.18  ? 56  HIS A CE1 1 
ATOM   381  N  NE2 . HIS A 1 56  ? 15.169  -5.411  -17.546 1.00 21.21  ? 56  HIS A NE2 1 
ATOM   382  N  N   . ILE A 1 57  ? 13.043  -3.106  -11.735 1.00 15.95  ? 57  ILE A N   1 
ATOM   383  C  CA  . ILE A 1 57  ? 12.214  -2.929  -10.547 1.00 15.55  ? 57  ILE A CA  1 
ATOM   384  C  C   . ILE A 1 57  ? 11.490  -1.593  -10.591 1.00 13.96  ? 57  ILE A C   1 
ATOM   385  O  O   . ILE A 1 57  ? 10.274  -1.492  -10.424 1.00 17.59  ? 57  ILE A O   1 
ATOM   386  C  CB  . ILE A 1 57  ? 13.054  -3.105  -9.268  1.00 16.38  ? 57  ILE A CB  1 
ATOM   387  C  CG1 . ILE A 1 57  ? 13.579  -4.532  -9.105  1.00 18.60  ? 57  ILE A CG1 1 
ATOM   388  C  CG2 . ILE A 1 57  ? 12.298  -2.699  -8.008  1.00 18.99  ? 57  ILE A CG2 1 
ATOM   389  C  CD1 . ILE A 1 57  ? 14.805  -4.688  -8.213  1.00 24.07  ? 57  ILE A CD1 1 
ATOM   390  N  N   . TYR A 1 58  ? 12.254  -0.501  -10.782 1.00 16.07  ? 58  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 58  ? 11.654  0.825   -10.797 1.00 14.81  ? 58  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 58  ? 10.798  1.061   -12.023 1.00 15.05  ? 58  TYR A C   1 
ATOM   393  O  O   . TYR A 1 58  ? 9.783   1.777   -11.885 1.00 16.37  ? 58  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 58  ? 12.729  1.937   -10.708 1.00 15.53  ? 58  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 58  ? 13.174  2.172   -9.296  1.00 14.42  ? 58  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 58  ? 12.315  2.845   -8.453  1.00 19.52  ? 58  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 58  ? 14.391  1.727   -8.829  1.00 19.44  ? 58  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 58  ? 12.662  3.085   -7.163  1.00 22.83  ? 58  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 58  ? 14.757  1.971   -7.502  1.00 24.94  ? 58  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 58  ? 13.870  2.649   -6.689  1.00 23.58  ? 58  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 58  ? 14.157  2.935   -5.361  1.00 37.26  ? 58  TYR A OH  1 
ATOM   402  N  N   . VAL A 1 59  ? 11.092  0.488   -13.191 1.00 15.61  ? 59  VAL A N   1 
ATOM   403  C  CA  . VAL A 1 59  ? 10.095  0.602   -14.278 1.00 16.64  ? 59  VAL A CA  1 
ATOM   404  C  C   . VAL A 1 59  ? 8.738   0.058   -13.838 1.00 15.59  ? 59  VAL A C   1 
ATOM   405  O  O   . VAL A 1 59  ? 7.691   0.686   -14.061 1.00 18.33  ? 59  VAL A O   1 
ATOM   406  C  CB  . VAL A 1 59  ? 10.582  -0.142  -15.511 1.00 15.22  ? 59  VAL A CB  1 
ATOM   407  C  CG1 . VAL A 1 59  ? 9.455   -0.378  -16.513 1.00 19.06  ? 59  VAL A CG1 1 
ATOM   408  C  CG2 . VAL A 1 59  ? 11.768  0.565   -16.180 1.00 17.91  ? 59  VAL A CG2 1 
ATOM   409  N  N   . ALA A 1 60  ? 8.792   -1.113  -13.200 1.00 17.49  ? 60  ALA A N   1 
ATOM   410  C  CA  . ALA A 1 60  ? 7.532   -1.751  -12.793 1.00 16.74  ? 60  ALA A CA  1 
ATOM   411  C  C   . ALA A 1 60  ? 6.880   -0.966  -11.669 1.00 17.55  ? 60  ALA A C   1 
ATOM   412  O  O   . ALA A 1 60  ? 5.664   -0.683  -11.704 1.00 18.94  ? 60  ALA A O   1 
ATOM   413  C  CB  . ALA A 1 60  ? 7.754   -3.191  -12.410 1.00 18.43  ? 60  ALA A CB  1 
ATOM   414  N  N   . LEU A 1 61  ? 7.659   -0.597  -10.675 1.00 17.47  ? 61  LEU A N   1 
ATOM   415  C  CA  . LEU A 1 61  ? 7.061   0.167   -9.566  1.00 17.25  ? 61  LEU A CA  1 
ATOM   416  C  C   . LEU A 1 61  ? 6.458   1.495   -10.022 1.00 16.58  ? 61  LEU A C   1 
ATOM   417  O  O   . LEU A 1 61  ? 5.350   1.869   -9.601  1.00 16.49  ? 61  LEU A O   1 
ATOM   418  C  CB  . LEU A 1 61  ? 8.110   0.422   -8.481  1.00 16.99  ? 61  LEU A CB  1 
ATOM   419  C  CG  . LEU A 1 61  ? 7.701   1.349   -7.329  1.00 17.49  ? 61  LEU A CG  1 
ATOM   420  C  CD1 . LEU A 1 61  ? 6.585   0.761   -6.480  1.00 20.76  ? 61  LEU A CD1 1 
ATOM   421  C  CD2 . LEU A 1 61  ? 8.899   1.664   -6.451  1.00 20.46  ? 61  LEU A CD2 1 
ATOM   422  N  N   . GLU A 1 62  ? 7.184   2.208   -10.868 1.00 15.49  ? 62  GLU A N   1 
ATOM   423  C  CA  . GLU A 1 62  ? 6.709   3.537   -11.301 1.00 16.73  ? 62  GLU A CA  1 
ATOM   424  C  C   . GLU A 1 62  ? 5.537   3.444   -12.260 1.00 17.35  ? 62  GLU A C   1 
ATOM   425  O  O   . GLU A 1 62  ? 4.679   4.320   -12.332 1.00 20.31  ? 62  GLU A O   1 
ATOM   426  C  CB  . GLU A 1 62  ? 7.887   4.387   -11.822 1.00 16.40  ? 62  GLU A CB  1 
ATOM   427  C  CG  . GLU A 1 62  ? 8.785   4.691   -10.638 1.00 15.28  ? 62  GLU A CG  1 
ATOM   428  C  CD  . GLU A 1 62  ? 10.075  5.404   -10.788 1.00 16.62  ? 62  GLU A CD  1 
ATOM   429  O  OE1 . GLU A 1 62  ? 10.447  5.677   -11.946 1.00 16.11  ? 62  GLU A OE1 1 
ATOM   430  O  OE2 . GLU A 1 62  ? 10.740  5.682   -9.755  1.00 18.64  ? 62  GLU A OE2 1 
ATOM   431  N  N   . GLU A 1 63  ? 5.420   2.356   -13.017 1.00 17.20  ? 63  GLU A N   1 
ATOM   432  C  CA  . GLU A 1 63  ? 4.220   2.141   -13.828 1.00 19.10  ? 63  GLU A CA  1 
ATOM   433  C  C   . GLU A 1 63  ? 2.972   1.976   -12.962 1.00 18.43  ? 63  GLU A C   1 
ATOM   434  O  O   . GLU A 1 63  ? 1.892   2.513   -13.260 1.00 21.47  ? 63  GLU A O   1 
ATOM   435  C  CB  . GLU A 1 63  ? 4.383   0.938   -14.786 1.00 22.43  ? 63  GLU A CB  1 
ATOM   436  C  CG  . GLU A 1 63  ? 3.079   0.563   -15.507 1.00 31.57  ? 63  GLU A CG  1 
ATOM   437  C  CD  . GLU A 1 63  ? 3.361   -0.580  -16.464 1.00 44.34  ? 63  GLU A CD  1 
ATOM   438  O  OE1 . GLU A 1 63  ? 4.559   -0.946  -16.548 1.00 45.43  ? 63  GLU A OE1 1 
ATOM   439  O  OE2 . GLU A 1 63  ? 2.425   -1.087  -17.098 1.00 61.02  ? 63  GLU A OE2 1 
ATOM   440  N  N   . GLU A 1 64  ? 3.137   1.211   -11.898 1.00 17.07  ? 64  GLU A N   1 
ATOM   441  C  CA  . GLU A 1 64  ? 2.009   0.943   -11.023 1.00 18.32  ? 64  GLU A CA  1 
ATOM   442  C  C   . GLU A 1 64  ? 1.710   2.152   -10.154 1.00 18.11  ? 64  GLU A C   1 
ATOM   443  O  O   . GLU A 1 64  ? 0.550   2.345   -9.781  1.00 22.63  ? 64  GLU A O   1 
ATOM   444  C  CB  . GLU A 1 64  ? 2.304   -0.295  -10.173 1.00 19.08  ? 64  GLU A CB  1 
ATOM   445  C  CG  . GLU A 1 64  ? 2.431   -1.582  -10.975 1.00 19.52  ? 64  GLU A CG  1 
ATOM   446  C  CD  . GLU A 1 64  ? 1.171   -1.867  -11.798 1.00 22.06  ? 64  GLU A CD  1 
ATOM   447  O  OE1 . GLU A 1 64  ? 0.098   -1.337  -11.418 1.00 20.46  ? 64  GLU A OE1 1 
ATOM   448  O  OE2 . GLU A 1 64  ? 1.248   -2.610  -12.799 1.00 23.62  ? 64  GLU A OE2 1 
ATOM   449  N  N   . ILE A 1 65  ? 2.710   2.974   -9.822  1.00 18.24  ? 65  ILE A N   1 
ATOM   450  C  CA  . ILE A 1 65  ? 2.395   4.201   -9.079  1.00 19.46  ? 65  ILE A CA  1 
ATOM   451  C  C   . ILE A 1 65  ? 1.583   5.123   -9.975  1.00 20.92  ? 65  ILE A C   1 
ATOM   452  O  O   . ILE A 1 65  ? 0.564   5.718   -9.580  1.00 22.99  ? 65  ILE A O   1 
ATOM   453  C  CB  . ILE A 1 65  ? 3.668   4.856   -8.536  1.00 18.27  ? 65  ILE A CB  1 
ATOM   454  C  CG1 . ILE A 1 65  ? 4.257   4.010   -7.405  1.00 17.75  ? 65  ILE A CG1 1 
ATOM   455  C  CG2 . ILE A 1 65  ? 3.396   6.287   -8.115  1.00 24.46  ? 65  ILE A CG2 1 
ATOM   456  C  CD1 . ILE A 1 65  ? 5.594   4.514   -6.901  1.00 21.40  ? 65  ILE A CD1 1 
ATOM   457  N  N   . GLU A 1 66  ? 1.984   5.249   -11.238 1.00 21.85  ? 66  GLU A N   1 
ATOM   458  C  CA  . GLU A 1 66  ? 1.210   6.078   -12.154 1.00 24.40  ? 66  GLU A CA  1 
ATOM   459  C  C   . GLU A 1 66  ? -0.213  5.564   -12.310 1.00 23.35  ? 66  GLU A C   1 
ATOM   460  O  O   . GLU A 1 66  ? -1.162  6.349   -12.404 1.00 25.39  ? 66  GLU A O   1 
ATOM   461  C  CB  . GLU A 1 66  ? 1.912   6.103   -13.517 1.00 28.00  ? 66  GLU A CB  1 
ATOM   462  C  CG  . GLU A 1 66  ? 3.123   7.040   -13.492 1.00 29.79  ? 66  GLU A CG  1 
ATOM   463  C  CD  . GLU A 1 66  ? 2.753   8.463   -13.072 1.00 36.05  ? 66  GLU A CD  1 
ATOM   464  O  OE1 . GLU A 1 66  ? 1.920   9.070   -13.778 1.00 40.52  ? 66  GLU A OE1 1 
ATOM   465  O  OE2 . GLU A 1 66  ? 3.315   8.946   -12.065 1.00 34.44  ? 66  GLU A OE2 1 
ATOM   466  N  N   . ARG A 1 67  ? -0.388  4.252   -12.360 1.00 23.24  ? 67  ARG A N   1 
ATOM   467  C  CA  . ARG A 1 67  ? -1.731  3.685   -12.449 1.00 25.38  ? 67  ARG A CA  1 
ATOM   468  C  C   . ARG A 1 67  ? -2.615  4.084   -11.278 1.00 27.29  ? 67  ARG A C   1 
ATOM   469  O  O   . ARG A 1 67  ? -3.828  4.304   -11.452 1.00 27.28  ? 67  ARG A O   1 
ATOM   470  C  CB  . ARG A 1 67  ? -1.651  2.139   -12.490 1.00 27.68  ? 67  ARG A CB  1 
ATOM   471  C  CG  . ARG A 1 67  ? -2.951  1.387   -12.676 1.00 29.32  ? 67  ARG A CG  1 
ATOM   472  C  CD  . ARG A 1 67  ? -2.913  -0.123  -12.615 1.00 29.94  ? 67  ARG A CD  1 
ATOM   473  N  NE  . ARG A 1 67  ? -1.776  -0.773  -13.217 1.00 43.09  ? 67  ARG A NE  1 
ATOM   474  C  CZ  . ARG A 1 67  ? -1.509  -1.011  -14.492 1.00 45.83  ? 67  ARG A CZ  1 
ATOM   475  N  NH1 . ARG A 1 67  ? -2.369  -0.624  -15.432 1.00 42.93  ? 67  ARG A NH1 1 
ATOM   476  N  NH2 . ARG A 1 67  ? -0.397  -1.635  -14.892 1.00 56.48  ? 67  ARG A NH2 1 
ATOM   477  N  N   . ASN A 1 68  ? -2.034  4.135   -10.093 1.00 23.48  ? 68  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 68  ? -2.799  4.291   -8.857  1.00 25.11  ? 68  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 68  ? -2.668  5.650   -8.199  1.00 25.40  ? 68  ASN A C   1 
ATOM   480  O  O   . ASN A 1 68  ? -3.055  5.880   -7.043  1.00 29.14  ? 68  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 68  ? -2.294  3.203   -7.895  1.00 25.39  ? 68  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 68  ? -2.664  1.803   -8.334  1.00 25.33  ? 68  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 68  ? -1.807  1.005   -8.748  1.00 28.18  ? 68  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 68  ? -3.939  1.498   -8.234  1.00 25.78  ? 68  ASN A ND2 1 
ATOM   485  N  N   . LYS A 1 69  ? -2.116  6.610   -8.927  1.00 24.23  ? 69  LYS A N   1 
ATOM   486  C  CA  . LYS A 1 69  ? -1.775  7.896   -8.322  1.00 26.23  ? 69  LYS A CA  1 
ATOM   487  C  C   . LYS A 1 69  ? -2.966  8.670   -7.785  1.00 25.47  ? 69  LYS A C   1 
ATOM   488  O  O   . LYS A 1 69  ? -2.803  9.473   -6.849  1.00 30.66  ? 69  LYS A O   1 
ATOM   489  C  CB  . LYS A 1 69  ? -0.994  8.684   -9.375  1.00 25.22  ? 69  LYS A CB  1 
ATOM   490  C  CG  . LYS A 1 69  ? -1.798  9.213   -10.554 1.00 25.04  ? 69  LYS A CG  1 
ATOM   491  C  CD  . LYS A 1 69  ? -0.950  10.223  -11.310 1.00 33.99  ? 69  LYS A CD  1 
ATOM   492  C  CE  . LYS A 1 69  ? -1.273  10.246  -12.787 1.00 36.92  ? 69  LYS A CE  1 
ATOM   493  N  NZ  . LYS A 1 69  ? -0.178  10.870  -13.593 1.00 52.72  ? 69  LYS A NZ  1 
ATOM   494  N  N   . GLU A 1 70  ? -4.156  8.452   -8.339  1.00 25.98  ? 70  GLU A N   1 
ATOM   495  C  CA  . GLU A 1 70  ? -5.324  9.198   -7.885  1.00 27.05  ? 70  GLU A CA  1 
ATOM   496  C  C   . GLU A 1 70  ? -6.099  8.337   -6.900  1.00 28.00  ? 70  GLU A C   1 
ATOM   497  O  O   . GLU A 1 70  ? -7.111  8.762   -6.355  1.00 30.22  ? 70  GLU A O   1 
ATOM   498  C  CB  . GLU A 1 70  ? -6.187  9.683   -9.063  1.00 32.77  ? 70  GLU A CB  1 
ATOM   499  C  CG  . GLU A 1 70  ? -5.464  10.685  -9.938  1.00 42.06  ? 70  GLU A CG  1 
ATOM   500  C  CD  . GLU A 1 70  ? -6.055  11.193  -11.217 1.00 52.51  ? 70  GLU A CD  1 
ATOM   501  O  OE1 . GLU A 1 70  ? -6.291  12.422  -11.325 1.00 69.66  ? 70  GLU A OE1 1 
ATOM   502  O  OE2 . GLU A 1 70  ? -6.294  10.419  -12.176 1.00 70.91  ? 70  GLU A OE2 1 
ATOM   503  N  N   . SER A 1 71  ? -5.663  7.112   -6.586  1.00 28.20  ? 71  SER A N   1 
ATOM   504  C  CA  . SER A 1 71  ? -6.434  6.296   -5.634  1.00 29.37  ? 71  SER A CA  1 
ATOM   505  C  C   . SER A 1 71  ? -6.219  6.724   -4.195  1.00 25.03  ? 71  SER A C   1 
ATOM   506  O  O   . SER A 1 71  ? -5.081  7.075   -3.810  1.00 27.17  ? 71  SER A O   1 
ATOM   507  C  CB  . SER A 1 71  ? -6.003  4.846   -5.694  1.00 32.87  ? 71  SER A CB  1 
ATOM   508  O  OG  . SER A 1 71  ? -6.878  3.993   -4.965  1.00 37.51  ? 71  SER A OG  1 
ATOM   509  N  N   . PRO A 1 72  ? -7.243  6.677   -3.364  1.00 28.83  ? 72  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 72  ? -7.025  7.118   -1.983  1.00 31.63  ? 72  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 72  ? -6.070  6.237   -1.204  1.00 28.56  ? 72  PRO A C   1 
ATOM   512  O  O   . PRO A 1 72  ? -5.566  6.648   -0.161  1.00 34.73  ? 72  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 72  ? -8.417  7.023   -1.353  1.00 36.08  ? 72  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 72  ? -9.378  6.896   -2.486  1.00 37.79  ? 72  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 72  ? -8.625  6.245   -3.604  1.00 36.20  ? 72  PRO A CD  1 
ATOM   516  N  N   . VAL A 1 73  ? -5.784  5.040   -1.630  1.00 26.06  ? 73  VAL A N   1 
ATOM   517  C  CA  . VAL A 1 73  ? -4.863  4.096   -1.012  1.00 24.80  ? 73  VAL A CA  1 
ATOM   518  C  C   . VAL A 1 73  ? -3.404  4.405   -1.356  1.00 21.89  ? 73  VAL A C   1 
ATOM   519  O  O   . VAL A 1 73  ? -2.504  3.800   -0.776  1.00 25.25  ? 73  VAL A O   1 
ATOM   520  C  CB  . VAL A 1 73  ? -5.166  2.644   -1.397  1.00 29.06  ? 73  VAL A CB  1 
ATOM   521  C  CG1 . VAL A 1 73  ? -6.647  2.319   -1.189  1.00 32.82  ? 73  VAL A CG1 1 
ATOM   522  C  CG2 . VAL A 1 73  ? -4.771  2.318   -2.831  1.00 30.37  ? 73  VAL A CG2 1 
ATOM   523  N  N   . PHE A 1 74  ? -3.144  5.333   -2.271  1.00 24.03  ? 74  PHE A N   1 
ATOM   524  C  CA  . PHE A 1 74  ? -1.786  5.711   -2.647  1.00 22.15  ? 74  PHE A CA  1 
ATOM   525  C  C   . PHE A 1 74  ? -1.590  7.217   -2.814  1.00 23.03  ? 74  PHE A C   1 
ATOM   526  O  O   . PHE A 1 74  ? -0.468  7.660   -2.539  1.00 26.00  ? 74  PHE A O   1 
ATOM   527  C  CB  . PHE A 1 74  ? -1.327  5.006   -3.952  1.00 22.50  ? 74  PHE A CB  1 
ATOM   528  C  CG  . PHE A 1 74  ? 0.199   5.113   -4.086  1.00 19.34  ? 74  PHE A CG  1 
ATOM   529  C  CD1 . PHE A 1 74  ? 0.994   4.169   -3.482  1.00 18.44  ? 74  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A 1 74  ? 0.814   6.133   -4.788  1.00 22.46  ? 74  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A 1 74  ? 2.367   4.211   -3.570  1.00 19.08  ? 74  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A 1 74  ? 2.193   6.213   -4.846  1.00 21.34  ? 74  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A 1 74  ? 2.971   5.268   -4.205  1.00 18.42  ? 74  PHE A CZ  1 
ATOM   534  N  N   . ALA A 1 75  ? -2.546  8.026   -3.240  1.00 24.18  ? 75  ALA A N   1 
ATOM   535  C  CA  . ALA A 1 75  ? -2.315  9.457   -3.514  1.00 22.55  ? 75  ALA A CA  1 
ATOM   536  C  C   . ALA A 1 75  ? -1.549  10.221  -2.430  1.00 22.38  ? 75  ALA A C   1 
ATOM   537  O  O   . ALA A 1 75  ? -0.690  11.073  -2.755  1.00 24.90  ? 75  ALA A O   1 
ATOM   538  C  CB  . ALA A 1 75  ? -3.653  10.160  -3.837  1.00 25.75  ? 75  ALA A CB  1 
ATOM   539  N  N   . PRO A 1 76  ? -1.793  10.032  -1.136  1.00 22.93  ? 76  PRO A N   1 
ATOM   540  C  CA  . PRO A 1 76  ? -1.025  10.772  -0.138  1.00 24.86  ? 76  PRO A CA  1 
ATOM   541  C  C   . PRO A 1 76  ? 0.480   10.591  -0.217  1.00 23.50  ? 76  PRO A C   1 
ATOM   542  O  O   . PRO A 1 76  ? 1.212   11.477  0.245   1.00 25.68  ? 76  PRO A O   1 
ATOM   543  C  CB  . PRO A 1 76  ? -1.533  10.175  1.187   1.00 26.17  ? 76  PRO A CB  1 
ATOM   544  C  CG  . PRO A 1 76  ? -2.954  9.792   0.880   1.00 27.31  ? 76  PRO A CG  1 
ATOM   545  C  CD  . PRO A 1 76  ? -2.847  9.206   -0.512  1.00 24.84  ? 76  PRO A CD  1 
ATOM   546  N  N   . VAL A 1 77  ? 0.972   9.500   -0.770  1.00 23.23  ? 77  VAL A N   1 
ATOM   547  C  CA  . VAL A 1 77  ? 2.428   9.315   -0.865  1.00 22.84  ? 77  VAL A CA  1 
ATOM   548  C  C   . VAL A 1 77  ? 2.906   9.429   -2.313  1.00 21.03  ? 77  VAL A C   1 
ATOM   549  O  O   . VAL A 1 77  ? 4.009   8.970   -2.669  1.00 22.41  ? 77  VAL A O   1 
ATOM   550  C  CB  . VAL A 1 77  ? 2.923   7.974   -0.282  1.00 20.66  ? 77  VAL A CB  1 
ATOM   551  C  CG1 . VAL A 1 77  ? 2.778   7.998   1.223   1.00 26.05  ? 77  VAL A CG1 1 
ATOM   552  C  CG2 . VAL A 1 77  ? 2.188   6.782   -0.845  1.00 19.83  ? 77  VAL A CG2 1 
ATOM   553  N  N   . TYR A 1 78  ? 2.124   10.051  -3.191  1.00 22.34  ? 78  TYR A N   1 
ATOM   554  C  CA  . TYR A 1 78  ? 2.498   10.271  -4.582  1.00 20.81  ? 78  TYR A CA  1 
ATOM   555  C  C   . TYR A 1 78  ? 3.388   11.518  -4.691  1.00 19.62  ? 78  TYR A C   1 
ATOM   556  O  O   . TYR A 1 78  ? 2.937   12.661  -4.569  1.00 21.24  ? 78  TYR A O   1 
ATOM   557  C  CB  . TYR A 1 78  ? 1.255   10.358  -5.477  1.00 21.57  ? 78  TYR A CB  1 
ATOM   558  C  CG  . TYR A 1 78  ? 1.541   10.550  -6.954  1.00 23.48  ? 78  TYR A CG  1 
ATOM   559  C  CD1 . TYR A 1 78  ? 2.222   9.610   -7.724  1.00 24.60  ? 78  TYR A CD1 1 
ATOM   560  C  CD2 . TYR A 1 78  ? 1.121   11.697  -7.634  1.00 22.58  ? 78  TYR A CD2 1 
ATOM   561  C  CE1 . TYR A 1 78  ? 2.492   9.761   -9.085  1.00 23.41  ? 78  TYR A CE1 1 
ATOM   562  C  CE2 . TYR A 1 78  ? 1.385   11.875  -8.985  1.00 23.92  ? 78  TYR A CE2 1 
ATOM   563  C  CZ  . TYR A 1 78  ? 2.067   10.913  -9.713  1.00 24.08  ? 78  TYR A CZ  1 
ATOM   564  O  OH  . TYR A 1 78  ? 2.315   11.117  -11.049 1.00 23.86  ? 78  TYR A OH  1 
ATOM   565  N  N   . PHE A 1 79  ? 4.675   11.264  -4.929  1.00 19.59  ? 79  PHE A N   1 
ATOM   566  C  CA  . PHE A 1 79  ? 5.698   12.294  -5.082  1.00 19.36  ? 79  PHE A CA  1 
ATOM   567  C  C   . PHE A 1 79  ? 6.580   12.011  -6.291  1.00 18.83  ? 79  PHE A C   1 
ATOM   568  O  O   . PHE A 1 79  ? 7.764   11.636  -6.178  1.00 18.67  ? 79  PHE A O   1 
ATOM   569  C  CB  . PHE A 1 79  ? 6.528   12.341  -3.818  1.00 19.00  ? 79  PHE A CB  1 
ATOM   570  C  CG  . PHE A 1 79  ? 5.859   12.929  -2.599  1.00 21.60  ? 79  PHE A CG  1 
ATOM   571  C  CD1 . PHE A 1 79  ? 5.743   14.312  -2.456  1.00 21.88  ? 79  PHE A CD1 1 
ATOM   572  C  CD2 . PHE A 1 79  ? 5.335   12.133  -1.588  1.00 26.02  ? 79  PHE A CD2 1 
ATOM   573  C  CE1 . PHE A 1 79  ? 5.114   14.851  -1.334  1.00 22.02  ? 79  PHE A CE1 1 
ATOM   574  C  CE2 . PHE A 1 79  ? 4.709   12.653  -0.473  1.00 23.31  ? 79  PHE A CE2 1 
ATOM   575  C  CZ  . PHE A 1 79  ? 4.597   14.024  -0.351  1.00 23.58  ? 79  PHE A CZ  1 
ATOM   576  N  N   . PRO A 1 80  ? 6.011   12.150  -7.490  1.00 20.28  ? 80  PRO A N   1 
ATOM   577  C  CA  . PRO A 1 80  ? 6.751   11.752  -8.695  1.00 21.23  ? 80  PRO A CA  1 
ATOM   578  C  C   . PRO A 1 80  ? 8.032   12.521  -8.988  1.00 20.73  ? 80  PRO A C   1 
ATOM   579  O  O   . PRO A 1 80  ? 9.047   11.911  -9.361  1.00 19.23  ? 80  PRO A O   1 
ATOM   580  C  CB  . PRO A 1 80  ? 5.735   11.989  -9.841  1.00 25.95  ? 80  PRO A CB  1 
ATOM   581  C  CG  . PRO A 1 80  ? 4.722   12.923  -9.288  1.00 26.41  ? 80  PRO A CG  1 
ATOM   582  C  CD  . PRO A 1 80  ? 4.659   12.642  -7.815  1.00 22.31  ? 80  PRO A CD  1 
ATOM   583  N  N   . GLU A 1 81  ? 7.980   13.857  -8.855  1.00 19.86  ? 81  GLU A N   1 
ATOM   584  C  CA  . GLU A 1 81  ? 9.160   14.633  -9.219  1.00 17.91  ? 81  GLU A CA  1 
ATOM   585  C  C   . GLU A 1 81  ? 10.295  14.355  -8.244  1.00 17.69  ? 81  GLU A C   1 
ATOM   586  O  O   . GLU A 1 81  ? 11.474  14.318  -8.563  1.00 19.65  ? 81  GLU A O   1 
ATOM   587  C  CB  . GLU A 1 81  ? 8.819   16.112  -9.208  1.00 21.29  ? 81  GLU A CB  1 
ATOM   588  C  CG  . GLU A 1 81  ? 7.903   16.545  -10.343 1.00 25.68  ? 81  GLU A CG  1 
ATOM   589  C  CD  . GLU A 1 81  ? 8.523   16.182  -11.675 1.00 25.31  ? 81  GLU A CD  1 
ATOM   590  O  OE1 . GLU A 1 81  ? 9.723   16.531  -11.795 1.00 28.44  ? 81  GLU A OE1 1 
ATOM   591  O  OE2 . GLU A 1 81  ? 7.838   15.594  -12.529 1.00 31.23  ? 81  GLU A OE2 1 
ATOM   592  N  N   . GLU A 1 82  ? 9.915   14.171  -6.964  1.00 18.64  ? 82  GLU A N   1 
ATOM   593  C  CA  . GLU A 1 82  ? 10.914  14.039  -5.916  1.00 15.89  ? 82  GLU A CA  1 
ATOM   594  C  C   . GLU A 1 82  ? 11.622  12.686  -5.953  1.00 15.76  ? 82  GLU A C   1 
ATOM   595  O  O   . GLU A 1 82  ? 12.808  12.571  -5.636  1.00 15.93  ? 82  GLU A O   1 
ATOM   596  C  CB  . GLU A 1 82  ? 10.281  14.200  -4.538  1.00 19.01  ? 82  GLU A CB  1 
ATOM   597  C  CG  . GLU A 1 82  ? 9.763   15.564  -4.232  1.00 19.51  ? 82  GLU A CG  1 
ATOM   598  C  CD  . GLU A 1 82  ? 8.520   15.983  -4.985  1.00 23.21  ? 82  GLU A CD  1 
ATOM   599  O  OE1 . GLU A 1 82  ? 7.722   15.114  -5.405  1.00 24.02  ? 82  GLU A OE1 1 
ATOM   600  O  OE2 . GLU A 1 82  ? 8.351   17.230  -5.162  1.00 28.49  ? 82  GLU A OE2 1 
ATOM   601  N  N   . LEU A 1 83  ? 10.884  11.646  -6.339  1.00 16.38  ? 83  LEU A N   1 
ATOM   602  C  CA  . LEU A 1 83  ? 11.369  10.292  -6.127  1.00 16.97  ? 83  LEU A CA  1 
ATOM   603  C  C   . LEU A 1 83  ? 11.637  9.521   -7.408  1.00 17.10  ? 83  LEU A C   1 
ATOM   604  O  O   . LEU A 1 83  ? 12.401  8.540   -7.279  1.00 17.69  ? 83  LEU A O   1 
ATOM   605  C  CB  . LEU A 1 83  ? 10.370  9.495   -5.268  1.00 16.23  ? 83  LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 83  ? 10.366  9.894   -3.781  1.00 17.11  ? 83  LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 83  ? 9.247   9.170   -3.047  1.00 19.56  ? 83  LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 83  ? 11.696  9.652   -3.092  1.00 17.02  ? 83  LEU A CD2 1 
ATOM   609  N  N   . HIS A 1 84  ? 11.072  9.899   -8.559  1.00 17.82  ? 84  HIS A N   1 
ATOM   610  C  CA  . HIS A 1 84  ? 11.208  8.988   -9.703  1.00 16.46  ? 84  HIS A CA  1 
ATOM   611  C  C   . HIS A 1 84  ? 12.656  8.637   -10.028 1.00 15.06  ? 84  HIS A C   1 
ATOM   612  O  O   . HIS A 1 84  ? 13.529  9.527   -9.997  1.00 15.86  ? 84  HIS A O   1 
ATOM   613  C  CB  . HIS A 1 84  ? 10.502  9.609   -10.904 1.00 18.17  ? 84  HIS A CB  1 
ATOM   614  C  CG  . HIS A 1 84  ? 11.187  10.726  -11.664 1.00 18.37  ? 84  HIS A CG  1 
ATOM   615  N  ND1 . HIS A 1 84  ? 11.243  12.046  -11.366 1.00 22.87  ? 84  HIS A ND1 1 
ATOM   616  C  CD2 . HIS A 1 84  ? 11.878  10.629  -12.837 1.00 19.75  ? 84  HIS A CD2 1 
ATOM   617  C  CE1 . HIS A 1 84  ? 11.924  12.760  -12.269 1.00 19.03  ? 84  HIS A CE1 1 
ATOM   618  N  NE2 . HIS A 1 84  ? 12.334  11.891  -13.179 1.00 23.03  ? 84  HIS A NE2 1 
ATOM   619  N  N   . ARG A 1 85  ? 12.881  7.360   -10.290 1.00 15.48  ? 85  ARG A N   1 
ATOM   620  C  CA  . ARG A 1 85  ? 14.234  6.870   -10.548 1.00 14.56  ? 85  ARG A CA  1 
ATOM   621  C  C   . ARG A 1 85  ? 14.431  6.258   -11.928 1.00 14.12  ? 85  ARG A C   1 
ATOM   622  O  O   . ARG A 1 85  ? 15.579  6.035   -12.327 1.00 14.97  ? 85  ARG A O   1 
ATOM   623  C  CB  . ARG A 1 85  ? 14.624  5.848   -9.475  1.00 16.29  ? 85  ARG A CB  1 
ATOM   624  C  CG  . ARG A 1 85  ? 14.762  6.305   -8.027  1.00 17.64  ? 85  ARG A CG  1 
ATOM   625  C  CD  . ARG A 1 85  ? 16.000  7.133   -7.826  1.00 15.74  ? 85  ARG A CD  1 
ATOM   626  N  NE  . ARG A 1 85  ? 15.783  8.513   -8.296  1.00 15.95  ? 85  ARG A NE  1 
ATOM   627  C  CZ  . ARG A 1 85  ? 16.713  9.381   -8.639  1.00 14.28  ? 85  ARG A CZ  1 
ATOM   628  N  NH1 . ARG A 1 85  ? 17.987  9.012   -8.584  1.00 15.23  ? 85  ARG A NH1 1 
ATOM   629  N  NH2 . ARG A 1 85  ? 16.244  10.574  -9.018  1.00 16.61  ? 85  ARG A NH2 1 
ATOM   630  N  N   . LYS A 1 86  ? 13.399  5.944   -12.711 1.00 15.33  ? 86  LYS A N   1 
ATOM   631  C  CA  . LYS A 1 86  ? 13.581  5.281   -13.997 1.00 14.69  ? 86  LYS A CA  1 
ATOM   632  C  C   . LYS A 1 86  ? 14.511  6.084   -14.896 1.00 14.80  ? 86  LYS A C   1 
ATOM   633  O  O   . LYS A 1 86  ? 15.463  5.547   -15.478 1.00 14.03  ? 86  LYS A O   1 
ATOM   634  C  CB  . LYS A 1 86  ? 12.216  5.089   -14.680 1.00 16.96  ? 86  LYS A CB  1 
ATOM   635  C  CG  . LYS A 1 86  ? 12.310  4.514   -16.091 1.00 15.23  ? 86  LYS A CG  1 
ATOM   636  C  CD  . LYS A 1 86  ? 10.925  4.369   -16.679 1.00 23.20  ? 86  LYS A CD  1 
ATOM   637  C  CE  . LYS A 1 86  ? 10.896  4.064   -18.159 1.00 30.23  ? 86  LYS A CE  1 
ATOM   638  N  NZ  . LYS A 1 86  ? 10.770  5.374   -18.871 1.00 40.91  ? 86  LYS A NZ  1 
ATOM   639  N  N   . ALA A 1 87  ? 14.294  7.398   -15.012 1.00 15.14  ? 87  ALA A N   1 
ATOM   640  C  CA  . ALA A 1 87  ? 15.138  8.190   -15.911 1.00 15.43  ? 87  ALA A CA  1 
ATOM   641  C  C   . ALA A 1 87  ? 16.603  8.187   -15.495 1.00 14.04  ? 87  ALA A C   1 
ATOM   642  O  O   . ALA A 1 87  ? 17.525  8.137   -16.308 1.00 15.14  ? 87  ALA A O   1 
ATOM   643  C  CB  . ALA A 1 87  ? 14.578  9.615   -15.994 1.00 16.71  ? 87  ALA A CB  1 
ATOM   644  N  N   . ALA A 1 88  ? 16.844  8.242   -14.192 1.00 15.21  ? 88  ALA A N   1 
ATOM   645  C  CA  . ALA A 1 88  ? 18.226  8.233   -13.688 1.00 15.85  ? 88  ALA A CA  1 
ATOM   646  C  C   . ALA A 1 88  ? 18.910  6.929   -14.063 1.00 15.21  ? 88  ALA A C   1 
ATOM   647  O  O   . ALA A 1 88  ? 20.078  6.910   -14.465 1.00 14.85  ? 88  ALA A O   1 
ATOM   648  C  CB  . ALA A 1 88  ? 18.217  8.452   -12.182 1.00 14.81  ? 88  ALA A CB  1 
ATOM   649  N  N   . LEU A 1 89  ? 18.166  5.824   -13.954 1.00 14.41  ? 89  LEU A N   1 
ATOM   650  C  CA  . LEU A 1 89  ? 18.711  4.499   -14.251 1.00 14.35  ? 89  LEU A CA  1 
ATOM   651  C  C   . LEU A 1 89  ? 18.932  4.314   -15.736 1.00 14.63  ? 89  LEU A C   1 
ATOM   652  O  O   . LEU A 1 89  ? 19.894  3.646   -16.112 1.00 15.10  ? 89  LEU A O   1 
ATOM   653  C  CB  . LEU A 1 89  ? 17.783  3.444   -13.661 1.00 14.07  ? 89  LEU A CB  1 
ATOM   654  C  CG  . LEU A 1 89  ? 17.915  3.297   -12.137 1.00 13.46  ? 89  LEU A CG  1 
ATOM   655  C  CD1 . LEU A 1 89  ? 16.712  2.615   -11.499 1.00 17.50  ? 89  LEU A CD1 1 
ATOM   656  C  CD2 . LEU A 1 89  ? 19.134  2.482   -11.781 1.00 16.24  ? 89  LEU A CD2 1 
ATOM   657  N  N   . GLU A 1 90  ? 18.065  4.921   -16.578 1.00 14.71  ? 90  GLU A N   1 
ATOM   658  C  CA  . GLU A 1 90  ? 18.318  4.934   -18.007 1.00 14.35  ? 90  GLU A CA  1 
ATOM   659  C  C   . GLU A 1 90  ? 19.644  5.609   -18.305 1.00 14.58  ? 90  GLU A C   1 
ATOM   660  O  O   . GLU A 1 90  ? 20.451  5.051   -19.060 1.00 14.86  ? 90  GLU A O   1 
ATOM   661  C  CB  . GLU A 1 90  ? 17.185  5.632   -18.757 1.00 15.11  ? 90  GLU A CB  1 
ATOM   662  C  CG  . GLU A 1 90  ? 15.870  4.858   -18.748 1.00 15.30  ? 90  GLU A CG  1 
ATOM   663  C  CD  . GLU A 1 90  ? 14.653  5.676   -19.120 1.00 18.29  ? 90  GLU A CD  1 
ATOM   664  O  OE1 . GLU A 1 90  ? 13.613  4.974   -19.338 1.00 19.91  ? 90  GLU A OE1 1 
ATOM   665  O  OE2 . GLU A 1 90  ? 14.753  6.940   -19.196 1.00 17.01  ? 90  GLU A OE2 1 
ATOM   666  N  N   . GLN A 1 91  ? 19.871  6.782   -17.755 1.00 14.21  ? 91  GLN A N   1 
ATOM   667  C  CA  . GLN A 1 91  ? 21.174  7.455   -17.926 1.00 14.40  ? 91  GLN A CA  1 
ATOM   668  C  C   . GLN A 1 91  ? 22.341  6.550   -17.532 1.00 13.90  ? 91  GLN A C   1 
ATOM   669  O  O   . GLN A 1 91  ? 23.355  6.383   -18.196 1.00 14.98  ? 91  GLN A O   1 
ATOM   670  C  CB  . GLN A 1 91  ? 21.231  8.738   -17.076 1.00 15.81  ? 91  GLN A CB  1 
ATOM   671  C  CG  . GLN A 1 91  ? 20.213  9.788   -17.517 1.00 16.27  ? 91  GLN A CG  1 
ATOM   672  C  CD  . GLN A 1 91  ? 20.688  10.487  -18.769 1.00 15.13  ? 91  GLN A CD  1 
ATOM   673  O  OE1 . GLN A 1 91  ? 21.791  10.524  -19.315 1.00 19.21  ? 91  GLN A OE1 1 
ATOM   674  N  NE2 . GLN A 1 91  ? 19.670  11.130  -19.260 1.00 13.95  ? 91  GLN A NE2 1 
ATOM   675  N  N   . ASP A 1 92  ? 22.175  5.946   -16.344 1.00 14.34  ? 92  ASP A N   1 
ATOM   676  C  CA  . ASP A 1 92  ? 23.258  5.143   -15.791 1.00 15.60  ? 92  ASP A CA  1 
ATOM   677  C  C   . ASP A 1 92  ? 23.540  3.920   -16.647 1.00 15.95  ? 92  ASP A C   1 
ATOM   678  O  O   . ASP A 1 92  ? 24.698  3.558   -16.891 1.00 16.54  ? 92  ASP A O   1 
ATOM   679  C  CB  . ASP A 1 92  ? 22.941  4.755   -14.339 1.00 15.71  ? 92  ASP A CB  1 
ATOM   680  C  CG  . ASP A 1 92  ? 23.068  5.918   -13.371 1.00 18.12  ? 92  ASP A CG  1 
ATOM   681  O  OD1 . ASP A 1 92  ? 22.568  5.790   -12.227 1.00 16.67  ? 92  ASP A OD1 1 
ATOM   682  O  OD2 . ASP A 1 92  ? 23.679  6.962   -13.735 1.00 17.03  ? 92  ASP A OD2 1 
ATOM   683  N  N   . LEU A 1 93  ? 22.495  3.241   -17.140 1.00 14.67  ? 93  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 93  ? 22.719  2.017   -17.892 1.00 14.00  ? 93  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 93  ? 23.309  2.328   -19.242 1.00 14.82  ? 93  LEU A C   1 
ATOM   686  O  O   . LEU A 1 93  ? 24.080  1.521   -19.764 1.00 17.64  ? 93  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 93  ? 21.419  1.232   -18.012 1.00 15.58  ? 93  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 93  ? 20.943  0.530   -16.742 1.00 15.38  ? 93  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 93  ? 19.611  -0.165  -17.043 1.00 19.44  ? 93  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 93  ? 21.972  -0.460  -16.213 1.00 18.01  ? 93  LEU A CD2 1 
ATOM   691  N  N   . ALA A 1 94  ? 22.972  3.472   -19.810 1.00 15.80  ? 94  ALA A N   1 
ATOM   692  C  CA  . ALA A 1 94  ? 23.660  3.849   -21.050 1.00 16.25  ? 94  ALA A CA  1 
ATOM   693  C  C   . ALA A 1 94  ? 25.154  3.972   -20.831 1.00 16.89  ? 94  ALA A C   1 
ATOM   694  O  O   . ALA A 1 94  ? 25.916  3.676   -21.738 1.00 18.45  ? 94  ALA A O   1 
ATOM   695  C  CB  . ALA A 1 94  ? 23.067  5.135   -21.611 1.00 15.96  ? 94  ALA A CB  1 
ATOM   696  N  N   . PHE A 1 95  ? 25.576  4.413   -19.646 1.00 16.05  ? 95  PHE A N   1 
ATOM   697  C  CA  . PHE A 1 95  ? 27.011  4.453   -19.332 1.00 19.89  ? 95  PHE A CA  1 
ATOM   698  C  C   . PHE A 1 95  ? 27.591  3.060   -19.152 1.00 18.99  ? 95  PHE A C   1 
ATOM   699  O  O   . PHE A 1 95  ? 28.597  2.640   -19.747 1.00 22.09  ? 95  PHE A O   1 
ATOM   700  C  CB  . PHE A 1 95  ? 27.250  5.285   -18.070 1.00 20.53  ? 95  PHE A CB  1 
ATOM   701  C  CG  . PHE A 1 95  ? 28.669  5.172   -17.551 1.00 23.13  ? 95  PHE A CG  1 
ATOM   702  C  CD1 . PHE A 1 95  ? 29.695  5.824   -18.214 1.00 30.70  ? 95  PHE A CD1 1 
ATOM   703  C  CD2 . PHE A 1 95  ? 28.968  4.438   -16.405 1.00 23.67  ? 95  PHE A CD2 1 
ATOM   704  C  CE1 . PHE A 1 95  ? 31.010  5.749   -17.762 1.00 34.37  ? 95  PHE A CE1 1 
ATOM   705  C  CE2 . PHE A 1 95  ? 30.287  4.338   -15.974 1.00 27.96  ? 95  PHE A CE2 1 
ATOM   706  C  CZ  . PHE A 1 95  ? 31.312  4.995   -16.644 1.00 33.04  ? 95  PHE A CZ  1 
ATOM   707  N  N   . TRP A 1 96  ? 26.928  2.277   -18.297 1.00 19.64  ? 96  TRP A N   1 
ATOM   708  C  CA  . TRP A 1 96  ? 27.487  0.979   -17.931 1.00 19.29  ? 96  TRP A CA  1 
ATOM   709  C  C   . TRP A 1 96  ? 27.420  -0.091  -19.014 1.00 19.01  ? 96  TRP A C   1 
ATOM   710  O  O   . TRP A 1 96  ? 28.291  -0.985  -19.030 1.00 23.26  ? 96  TRP A O   1 
ATOM   711  C  CB  . TRP A 1 96  ? 26.791  0.440   -16.674 1.00 19.34  ? 96  TRP A CB  1 
ATOM   712  C  CG  . TRP A 1 96  ? 27.114  1.222   -15.430 1.00 21.39  ? 96  TRP A CG  1 
ATOM   713  C  CD1 . TRP A 1 96  ? 26.301  2.078   -14.739 1.00 20.14  ? 96  TRP A CD1 1 
ATOM   714  C  CD2 . TRP A 1 96  ? 28.364  1.176   -14.754 1.00 22.83  ? 96  TRP A CD2 1 
ATOM   715  N  NE1 . TRP A 1 96  ? 26.989  2.575   -13.674 1.00 19.92  ? 96  TRP A NE1 1 
ATOM   716  C  CE2 . TRP A 1 96  ? 28.257  2.036   -13.660 1.00 23.98  ? 96  TRP A CE2 1 
ATOM   717  C  CE3 . TRP A 1 96  ? 29.555  0.507   -14.971 1.00 27.77  ? 96  TRP A CE3 1 
ATOM   718  C  CZ2 . TRP A 1 96  ? 29.315  2.233   -12.781 1.00 28.46  ? 96  TRP A CZ2 1 
ATOM   719  C  CZ3 . TRP A 1 96  ? 30.615  0.698   -14.095 1.00 33.46  ? 96  TRP A CZ3 1 
ATOM   720  C  CH2 . TRP A 1 96  ? 30.486  1.559   -13.005 1.00 31.06  ? 96  TRP A CH2 1 
ATOM   721  N  N   . TYR A 1 97  ? 26.405  -0.035  -19.860 1.00 17.93  ? 97  TYR A N   1 
ATOM   722  C  CA  . TYR A 1 97  ? 26.219  -1.079  -20.856 1.00 18.84  ? 97  TYR A CA  1 
ATOM   723  C  C   . TYR A 1 97  ? 26.312  -0.504  -22.272 1.00 20.08  ? 97  TYR A C   1 
ATOM   724  O  O   . TYR A 1 97  ? 26.241  -1.296  -23.224 1.00 22.53  ? 97  TYR A O   1 
ATOM   725  C  CB  . TYR A 1 97  ? 24.883  -1.771  -20.668 1.00 18.39  ? 97  TYR A CB  1 
ATOM   726  C  CG  . TYR A 1 97  ? 24.760  -2.796  -19.572 1.00 18.58  ? 97  TYR A CG  1 
ATOM   727  C  CD1 . TYR A 1 97  ? 25.016  -4.147  -19.808 1.00 19.67  ? 97  TYR A CD1 1 
ATOM   728  C  CD2 . TYR A 1 97  ? 24.387  -2.431  -18.296 1.00 18.77  ? 97  TYR A CD2 1 
ATOM   729  C  CE1 . TYR A 1 97  ? 24.911  -5.088  -18.807 1.00 18.86  ? 97  TYR A CE1 1 
ATOM   730  C  CE2 . TYR A 1 97  ? 24.267  -3.354  -17.295 1.00 18.78  ? 97  TYR A CE2 1 
ATOM   731  C  CZ  . TYR A 1 97  ? 24.530  -4.683  -17.541 1.00 20.03  ? 97  TYR A CZ  1 
ATOM   732  O  OH  . TYR A 1 97  ? 24.388  -5.586  -16.513 1.00 20.43  ? 97  TYR A OH  1 
ATOM   733  N  N   . GLY A 1 98  ? 26.472  0.827   -22.389 1.00 20.04  ? 98  GLY A N   1 
ATOM   734  C  CA  . GLY A 1 98  ? 26.627  1.440   -23.697 1.00 21.46  ? 98  GLY A CA  1 
ATOM   735  C  C   . GLY A 1 98  ? 25.322  1.790   -24.370 1.00 19.94  ? 98  GLY A C   1 
ATOM   736  O  O   . GLY A 1 98  ? 24.222  1.573   -23.889 1.00 18.87  ? 98  GLY A O   1 
ATOM   737  N  N   . PRO A 1 99  ? 25.430  2.369   -25.560 1.00 21.83  ? 99  PRO A N   1 
ATOM   738  C  CA  . PRO A 1 99  ? 24.242  2.891   -26.238 1.00 25.17  ? 99  PRO A CA  1 
ATOM   739  C  C   . PRO A 1 99  ? 23.178  1.848   -26.536 1.00 23.94  ? 99  PRO A C   1 
ATOM   740  O  O   . PRO A 1 99  ? 22.002  2.183   -26.597 1.00 22.09  ? 99  PRO A O   1 
ATOM   741  C  CB  . PRO A 1 99  ? 24.763  3.472   -27.564 1.00 26.90  ? 99  PRO A CB  1 
ATOM   742  C  CG  . PRO A 1 99  ? 26.210  3.216   -27.591 1.00 30.33  ? 99  PRO A CG  1 
ATOM   743  C  CD  . PRO A 1 99  ? 26.655  2.589   -26.310 1.00 25.89  ? 99  PRO A CD  1 
ATOM   744  N  N   . ARG A 1 100 ? 23.569  0.597   -26.709 1.00 23.51  ? 100 ARG A N   1 
ATOM   745  C  CA  . ARG A 1 100 ? 22.574  -0.432  -26.970 1.00 23.06  ? 100 ARG A CA  1 
ATOM   746  C  C   . ARG A 1 100 ? 22.170  -1.199  -25.723 1.00 21.18  ? 100 ARG A C   1 
ATOM   747  O  O   . ARG A 1 100 ? 21.750  -2.370  -25.819 1.00 21.36  ? 100 ARG A O   1 
ATOM   748  C  CB  . ARG A 1 100 ? 23.141  -1.377  -28.034 1.00 28.96  ? 100 ARG A CB  1 
ATOM   749  C  CG  . ARG A 1 100 ? 23.158  -0.636  -29.385 1.00 36.02  ? 100 ARG A CG  1 
ATOM   750  C  CD  . ARG A 1 100 ? 23.844  -1.556  -30.402 1.00 41.36  ? 100 ARG A CD  1 
ATOM   751  N  NE  . ARG A 1 100 ? 22.904  -2.540  -30.918 1.00 49.20  ? 100 ARG A NE  1 
ATOM   752  C  CZ  . ARG A 1 100 ? 23.080  -3.278  -32.000 1.00 52.08  ? 100 ARG A CZ  1 
ATOM   753  N  NH1 . ARG A 1 100 ? 24.167  -3.199  -32.753 1.00 59.41  ? 100 ARG A NH1 1 
ATOM   754  N  NH2 . ARG A 1 100 ? 22.101  -4.124  -32.313 1.00 53.67  ? 100 ARG A NH2 1 
ATOM   755  N  N   . TRP A 1 101 ? 22.299  -0.558  -24.558 1.00 18.91  ? 101 TRP A N   1 
ATOM   756  C  CA  . TRP A 1 101 ? 21.989  -1.183  -23.275 1.00 17.82  ? 101 TRP A CA  1 
ATOM   757  C  C   . TRP A 1 101 ? 20.640  -1.900  -23.284 1.00 16.73  ? 101 TRP A C   1 
ATOM   758  O  O   . TRP A 1 101 ? 20.527  -2.974  -22.680 1.00 18.78  ? 101 TRP A O   1 
ATOM   759  C  CB  . TRP A 1 101 ? 22.059  -0.158  -22.162 1.00 17.29  ? 101 TRP A CB  1 
ATOM   760  C  CG  . TRP A 1 101 ? 21.048  0.945   -22.175 1.00 16.39  ? 101 TRP A CG  1 
ATOM   761  C  CD1 . TRP A 1 101 ? 21.179  2.139   -22.853 1.00 18.81  ? 101 TRP A CD1 1 
ATOM   762  C  CD2 . TRP A 1 101 ? 19.778  0.989   -21.499 1.00 15.27  ? 101 TRP A CD2 1 
ATOM   763  N  NE1 . TRP A 1 101 ? 20.065  2.925   -22.646 1.00 16.92  ? 101 TRP A NE1 1 
ATOM   764  C  CE2 . TRP A 1 101 ? 19.177  2.241   -21.812 1.00 16.02  ? 101 TRP A CE2 1 
ATOM   765  C  CE3 . TRP A 1 101 ? 19.046  0.134   -20.672 1.00 15.86  ? 101 TRP A CE3 1 
ATOM   766  C  CZ2 . TRP A 1 101 ? 17.913  2.586   -21.300 1.00 16.48  ? 101 TRP A CZ2 1 
ATOM   767  C  CZ3 . TRP A 1 101 ? 17.808  0.489   -20.176 1.00 16.05  ? 101 TRP A CZ3 1 
ATOM   768  C  CH2 . TRP A 1 101 ? 17.242  1.727   -20.493 1.00 17.19  ? 101 TRP A CH2 1 
ATOM   769  N  N   . GLN A 1 102 ? 19.585  -1.389  -23.938 1.00 19.99  ? 102 GLN A N   1 
ATOM   770  C  CA  . GLN A 1 102 ? 18.287  -2.074  -23.867 1.00 19.04  ? 102 GLN A CA  1 
ATOM   771  C  C   . GLN A 1 102 ? 18.297  -3.476  -24.418 1.00 19.36  ? 102 GLN A C   1 
ATOM   772  O  O   . GLN A 1 102 ? 17.542  -4.348  -23.967 1.00 25.23  ? 102 GLN A O   1 
ATOM   773  C  CB  . GLN A 1 102 ? 17.231  -1.246  -24.624 1.00 22.79  ? 102 GLN A CB  1 
ATOM   774  C  CG  . GLN A 1 102 ? 16.740  -0.090  -23.799 1.00 25.29  ? 102 GLN A CG  1 
ATOM   775  C  CD  . GLN A 1 102 ? 15.608  -0.495  -22.850 1.00 26.03  ? 102 GLN A CD  1 
ATOM   776  O  OE1 . GLN A 1 102 ? 15.443  -1.630  -22.375 1.00 33.57  ? 102 GLN A OE1 1 
ATOM   777  N  NE2 . GLN A 1 102 ? 14.760  0.497   -22.571 1.00 35.02  ? 102 GLN A NE2 1 
ATOM   778  N  N   . GLU A 1 103 ? 19.157  -3.651  -25.413 1.00 20.64  ? 103 GLU A N   1 
ATOM   779  C  CA  . GLU A 1 103 ? 19.267  -4.952  -26.040 1.00 24.79  ? 103 GLU A CA  1 
ATOM   780  C  C   . GLU A 1 103 ? 20.188  -5.927  -25.307 1.00 23.48  ? 103 GLU A C   1 
ATOM   781  O  O   . GLU A 1 103 ? 20.256  -7.087  -25.713 1.00 29.67  ? 103 GLU A O   1 
ATOM   782  C  CB  . GLU A 1 103 ? 19.843  -4.836  -27.450 1.00 28.39  ? 103 GLU A CB  1 
ATOM   783  C  CG  . GLU A 1 103 ? 19.013  -4.040  -28.409 1.00 30.46  ? 103 GLU A CG  1 
ATOM   784  C  CD  . GLU A 1 103 ? 19.735  -3.625  -29.674 1.00 36.29  ? 103 GLU A CD  1 
ATOM   785  O  OE1 . GLU A 1 103 ? 19.916  -4.475  -30.551 1.00 40.63  ? 103 GLU A OE1 1 
ATOM   786  O  OE2 . GLU A 1 103 ? 20.110  -2.435  -29.826 1.00 39.36  ? 103 GLU A OE2 1 
ATOM   787  N  N   . VAL A 1 104 ? 20.931  -5.444  -24.310 1.00 20.99  ? 104 VAL A N   1 
ATOM   788  C  CA  . VAL A 1 104 ? 21.905  -6.341  -23.722 1.00 21.98  ? 104 VAL A CA  1 
ATOM   789  C  C   . VAL A 1 104 ? 21.771  -6.508  -22.210 1.00 18.38  ? 104 VAL A C   1 
ATOM   790  O  O   . VAL A 1 104 ? 22.305  -7.503  -21.692 1.00 20.86  ? 104 VAL A O   1 
ATOM   791  C  CB  . VAL A 1 104 ? 23.361  -5.945  -24.045 1.00 23.02  ? 104 VAL A CB  1 
ATOM   792  C  CG1 . VAL A 1 104 ? 23.585  -6.024  -25.573 1.00 32.99  ? 104 VAL A CG1 1 
ATOM   793  C  CG2 . VAL A 1 104 ? 23.809  -4.589  -23.568 1.00 25.60  ? 104 VAL A CG2 1 
ATOM   794  N  N   . ILE A 1 105 ? 21.109  -5.591  -21.510 1.00 16.23  ? 105 ILE A N   1 
ATOM   795  C  CA  . ILE A 1 105 ? 20.947  -5.789  -20.065 1.00 16.88  ? 105 ILE A CA  1 
ATOM   796  C  C   . ILE A 1 105 ? 20.186  -7.087  -19.786 1.00 16.58  ? 105 ILE A C   1 
ATOM   797  O  O   . ILE A 1 105 ? 19.218  -7.494  -20.446 1.00 20.19  ? 105 ILE A O   1 
ATOM   798  C  CB  . ILE A 1 105 ? 20.197  -4.637  -19.360 1.00 17.51  ? 105 ILE A CB  1 
ATOM   799  C  CG1 . ILE A 1 105 ? 18.791  -4.356  -19.889 1.00 19.21  ? 105 ILE A CG1 1 
ATOM   800  C  CG2 . ILE A 1 105 ? 21.059  -3.372  -19.336 1.00 17.78  ? 105 ILE A CG2 1 
ATOM   801  C  CD1 . ILE A 1 105 ? 17.980  -3.414  -19.041 1.00 20.17  ? 105 ILE A CD1 1 
ATOM   802  N  N   . PRO A 1 106 ? 20.639  -7.770  -18.742 1.00 16.47  ? 106 PRO A N   1 
ATOM   803  C  CA  . PRO A 1 106 ? 19.933  -8.985  -18.377 1.00 17.04  ? 106 PRO A CA  1 
ATOM   804  C  C   . PRO A 1 106 ? 18.609  -8.709  -17.677 1.00 16.69  ? 106 PRO A C   1 
ATOM   805  O  O   . PRO A 1 106 ? 18.432  -7.686  -17.058 1.00 16.90  ? 106 PRO A O   1 
ATOM   806  C  CB  . PRO A 1 106 ? 20.899  -9.652  -17.381 1.00 19.60  ? 106 PRO A CB  1 
ATOM   807  C  CG  . PRO A 1 106 ? 21.689  -8.515  -16.819 1.00 21.99  ? 106 PRO A CG  1 
ATOM   808  C  CD  . PRO A 1 106 ? 21.810  -7.483  -17.905 1.00 16.79  ? 106 PRO A CD  1 
ATOM   809  N  N   . TYR A 1 107 ? 17.714  -9.677  -17.798 1.00 17.86  ? 107 TYR A N   1 
ATOM   810  C  CA  . TYR A 1 107 ? 16.432  -9.694  -17.118 1.00 17.93  ? 107 TYR A CA  1 
ATOM   811  C  C   . TYR A 1 107 ? 16.257  -11.118 -16.601 1.00 18.40  ? 107 TYR A C   1 
ATOM   812  O  O   . TYR A 1 107 ? 15.793  -12.017 -17.334 1.00 20.55  ? 107 TYR A O   1 
ATOM   813  C  CB  . TYR A 1 107 ? 15.268  -9.320  -18.034 1.00 17.69  ? 107 TYR A CB  1 
ATOM   814  C  CG  . TYR A 1 107 ? 13.920  -9.152  -17.374 1.00 19.75  ? 107 TYR A CG  1 
ATOM   815  C  CD1 . TYR A 1 107 ? 13.833  -8.612  -16.094 1.00 18.43  ? 107 TYR A CD1 1 
ATOM   816  C  CD2 . TYR A 1 107 ? 12.715  -9.505  -17.997 1.00 20.31  ? 107 TYR A CD2 1 
ATOM   817  C  CE1 . TYR A 1 107 ? 12.626  -8.432  -15.441 1.00 18.62  ? 107 TYR A CE1 1 
ATOM   818  C  CE2 . TYR A 1 107 ? 11.503  -9.326  -17.353 1.00 19.90  ? 107 TYR A CE2 1 
ATOM   819  C  CZ  . TYR A 1 107 ? 11.450  -8.790  -16.075 1.00 20.08  ? 107 TYR A CZ  1 
ATOM   820  O  OH  . TYR A 1 107 ? 10.234  -8.611  -15.436 1.00 22.50  ? 107 TYR A OH  1 
ATOM   821  N  N   . THR A 1 108 ? 16.668  -11.317 -15.366 1.00 17.26  ? 108 THR A N   1 
ATOM   822  C  CA  . THR A 1 108 ? 16.785  -12.685 -14.853 1.00 16.52  ? 108 THR A CA  1 
ATOM   823  C  C   . THR A 1 108 ? 15.510  -13.153 -14.146 1.00 16.79  ? 108 THR A C   1 
ATOM   824  O  O   . THR A 1 108 ? 14.640  -12.351 -13.781 1.00 17.70  ? 108 THR A O   1 
ATOM   825  C  CB  . THR A 1 108 ? 17.977  -12.768 -13.884 1.00 15.53  ? 108 THR A CB  1 
ATOM   826  O  OG1 . THR A 1 108 ? 17.686  -11.947 -12.754 1.00 18.56  ? 108 THR A OG1 1 
ATOM   827  C  CG2 . THR A 1 108 ? 19.293  -12.251 -14.431 1.00 18.60  ? 108 THR A CG2 1 
ATOM   828  N  N   . PRO A 1 109 ? 15.371  -14.463 -13.937 1.00 17.63  ? 109 PRO A N   1 
ATOM   829  C  CA  . PRO A 1 109 ? 14.221  -14.963 -13.173 1.00 17.94  ? 109 PRO A CA  1 
ATOM   830  C  C   . PRO A 1 109 ? 14.034  -14.272 -11.833 1.00 16.75  ? 109 PRO A C   1 
ATOM   831  O  O   . PRO A 1 109 ? 12.856  -13.999 -11.502 1.00 18.07  ? 109 PRO A O   1 
ATOM   832  C  CB  . PRO A 1 109 ? 14.533  -16.454 -13.038 1.00 19.50  ? 109 PRO A CB  1 
ATOM   833  C  CG  . PRO A 1 109 ? 15.334  -16.767 -14.286 1.00 19.39  ? 109 PRO A CG  1 
ATOM   834  C  CD  . PRO A 1 109 ? 16.188  -15.552 -14.473 1.00 17.72  ? 109 PRO A CD  1 
ATOM   835  N  N   . ALA A 1 110 ? 15.030  -13.944 -11.032 1.00 16.80  ? 110 ALA A N   1 
ATOM   836  C  CA  . ALA A 1 110 ? 14.777  -13.288 -9.744  1.00 17.08  ? 110 ALA A CA  1 
ATOM   837  C  C   . ALA A 1 110 ? 14.275  -11.860 -9.903  1.00 16.70  ? 110 ALA A C   1 
ATOM   838  O  O   . ALA A 1 110 ? 13.450  -11.348 -9.138  1.00 18.78  ? 110 ALA A O   1 
ATOM   839  C  CB  . ALA A 1 110 ? 16.047  -13.349 -8.893  1.00 19.13  ? 110 ALA A CB  1 
ATOM   840  N  N   . MET A 1 111 ? 14.754  -11.146 -10.910 1.00 15.60  ? 111 MET A N   1 
ATOM   841  C  CA  . MET A 1 111 ? 14.276  -9.855  -11.281 1.00 15.66  ? 111 MET A CA  1 
ATOM   842  C  C   . MET A 1 111 ? 12.795  -9.942  -11.714 1.00 16.70  ? 111 MET A C   1 
ATOM   843  O  O   . MET A 1 111 ? 12.014  -9.095  -11.284 1.00 16.92  ? 111 MET A O   1 
ATOM   844  C  CB  . MET A 1 111 ? 15.052  -9.194  -12.421 1.00 16.29  ? 111 MET A CB  1 
ATOM   845  C  CG  . MET A 1 111 ? 16.524  -8.932  -12.118 1.00 17.62  ? 111 MET A CG  1 
ATOM   846  S  SD  . MET A 1 111 ? 17.364  -8.444  -13.631 1.00 17.67  ? 111 MET A SD  1 
ATOM   847  C  CE  . MET A 1 111 ? 19.085  -8.692  -13.187 1.00 18.81  ? 111 MET A CE  1 
ATOM   848  N  N   . GLN A 1 112 ? 12.469  -10.919 -12.548 1.00 17.73  ? 112 GLN A N   1 
ATOM   849  C  CA  . GLN A 1 112 ? 11.100  -11.123 -13.006 1.00 19.10  ? 112 GLN A CA  1 
ATOM   850  C  C   . GLN A 1 112 ? 10.155  -11.392 -11.844 1.00 18.34  ? 112 GLN A C   1 
ATOM   851  O  O   . GLN A 1 112 ? 9.002   -10.926 -11.806 1.00 21.23  ? 112 GLN A O   1 
ATOM   852  C  CB  . GLN A 1 112 ? 11.067  -12.291 -13.990 1.00 18.11  ? 112 GLN A CB  1 
ATOM   853  C  CG  . GLN A 1 112 ? 11.819  -11.985 -15.285 1.00 21.14  ? 112 GLN A CG  1 
ATOM   854  C  CD  . GLN A 1 112 ? 12.202  -13.270 -15.999 1.00 21.48  ? 112 GLN A CD  1 
ATOM   855  O  OE1 . GLN A 1 112 ? 13.216  -13.372 -16.713 1.00 23.86  ? 112 GLN A OE1 1 
ATOM   856  N  NE2 . GLN A 1 112 ? 11.396  -14.305 -15.799 1.00 22.10  ? 112 GLN A NE2 1 
ATOM   857  N  N   . ARG A 1 113 ? 10.615  -12.163 -10.859 1.00 19.74  ? 113 ARG A N   1 
ATOM   858  C  CA  . ARG A 1 113 ? 9.748   -12.450 -9.712  1.00 18.66  ? 113 ARG A CA  1 
ATOM   859  C  C   . ARG A 1 113 ? 9.327   -11.174 -9.011  1.00 17.55  ? 113 ARG A C   1 
ATOM   860  O  O   . ARG A 1 113 ? 8.189   -10.980 -8.625  1.00 21.62  ? 113 ARG A O   1 
ATOM   861  C  CB  . ARG A 1 113 ? 10.488  -13.356 -8.734  1.00 21.32  ? 113 ARG A CB  1 
ATOM   862  C  CG  . ARG A 1 113 ? 9.589   -14.080 -7.797  1.00 34.99  ? 113 ARG A CG  1 
ATOM   863  C  CD  . ARG A 1 113 ? 10.021  -15.426 -7.278  1.00 41.47  ? 113 ARG A CD  1 
ATOM   864  N  NE  . ARG A 1 113 ? 11.137  -16.101 -7.886  1.00 46.18  ? 113 ARG A NE  1 
ATOM   865  C  CZ  . ARG A 1 113 ? 12.439  -15.999 -7.836  1.00 48.07  ? 113 ARG A CZ  1 
ATOM   866  N  NH1 . ARG A 1 113 ? 13.047  -15.083 -7.095  1.00 49.27  ? 113 ARG A NH1 1 
ATOM   867  N  NH2 . ARG A 1 113 ? 13.151  -16.856 -8.573  1.00 59.95  ? 113 ARG A NH2 1 
ATOM   868  N  N   . TYR A 1 114 ? 10.293  -10.269 -8.817  1.00 17.91  ? 114 TYR A N   1 
ATOM   869  C  CA  . TYR A 1 114 ? 10.035  -8.992  -8.163  1.00 16.73  ? 114 TYR A CA  1 
ATOM   870  C  C   . TYR A 1 114 ? 9.092   -8.119  -9.008  1.00 17.12  ? 114 TYR A C   1 
ATOM   871  O  O   . TYR A 1 114 ? 8.116   -7.561  -8.480  1.00 17.47  ? 114 TYR A O   1 
ATOM   872  C  CB  . TYR A 1 114 ? 11.365  -8.320  -7.867  1.00 17.29  ? 114 TYR A CB  1 
ATOM   873  C  CG  . TYR A 1 114 ? 11.448  -7.192  -6.885  1.00 15.75  ? 114 TYR A CG  1 
ATOM   874  C  CD1 . TYR A 1 114 ? 10.363  -6.447  -6.450  1.00 17.56  ? 114 TYR A CD1 1 
ATOM   875  C  CD2 . TYR A 1 114 ? 12.700  -6.817  -6.368  1.00 15.95  ? 114 TYR A CD2 1 
ATOM   876  C  CE1 . TYR A 1 114 ? 10.500  -5.409  -5.547  1.00 18.53  ? 114 TYR A CE1 1 
ATOM   877  C  CE2 . TYR A 1 114 ? 12.835  -5.784  -5.465  1.00 15.98  ? 114 TYR A CE2 1 
ATOM   878  C  CZ  . TYR A 1 114 ? 11.738  -5.069  -5.047  1.00 16.60  ? 114 TYR A CZ  1 
ATOM   879  O  OH  . TYR A 1 114 ? 11.909  -4.042  -4.147  1.00 19.33  ? 114 TYR A OH  1 
ATOM   880  N  N   . VAL A 1 115 ? 9.376   -7.981  -10.290 1.00 16.39  ? 115 VAL A N   1 
ATOM   881  C  CA  . VAL A 1 115 ? 8.514   -7.208  -11.200 1.00 18.55  ? 115 VAL A CA  1 
ATOM   882  C  C   . VAL A 1 115 ? 7.112   -7.779  -11.212 1.00 17.52  ? 115 VAL A C   1 
ATOM   883  O  O   . VAL A 1 115 ? 6.143   -7.030  -11.171 1.00 18.71  ? 115 VAL A O   1 
ATOM   884  C  CB  . VAL A 1 115 ? 9.117   -7.225  -12.613 1.00 16.60  ? 115 VAL A CB  1 
ATOM   885  C  CG1 . VAL A 1 115 ? 8.138   -6.757  -13.660 1.00 20.97  ? 115 VAL A CG1 1 
ATOM   886  C  CG2 . VAL A 1 115 ? 10.407  -6.390  -12.725 1.00 19.98  ? 115 VAL A CG2 1 
ATOM   887  N  N   . LYS A 1 116 ? 6.954   -9.104  -11.235 1.00 18.61  ? 116 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 116 ? 5.639   -9.756  -11.256 1.00 19.36  ? 116 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 116 ? 4.828   -9.362  -10.035 1.00 21.76  ? 116 LYS A C   1 
ATOM   890  O  O   . LYS A 1 116 ? 3.628   -9.044  -10.140 1.00 20.96  ? 116 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 116 ? 5.773   -11.292 -11.367 1.00 24.70  ? 116 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 116 ? 4.518   -12.078 -10.979 1.00 36.67  ? 116 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 116 ? 4.845   -13.569 -11.126 1.00 46.09  ? 116 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 116 ? 3.706   -14.439 -10.626 1.00 55.28  ? 116 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 116 ? 3.996   -15.915 -10.652 1.00 65.40  ? 116 LYS A NZ  1 
ATOM   896  N  N   . ARG A 1 117 ? 5.491   -9.386  -8.883  1.00 18.86  ? 117 ARG A N   1 
ATOM   897  C  CA  . ARG A 1 117 ? 4.742   -9.015  -7.672  1.00 19.32  ? 117 ARG A CA  1 
ATOM   898  C  C   . ARG A 1 117 ? 4.354   -7.544  -7.654  1.00 16.75  ? 117 ARG A C   1 
ATOM   899  O  O   . ARG A 1 117 ? 3.258   -7.207  -7.199  1.00 18.48  ? 117 ARG A O   1 
ATOM   900  C  CB  . ARG A 1 117 ? 5.560   -9.368  -6.430  1.00 20.21  ? 117 ARG A CB  1 
ATOM   901  C  CG  . ARG A 1 117 ? 4.879   -9.027  -5.118  1.00 20.92  ? 117 ARG A CG  1 
ATOM   902  C  CD  . ARG A 1 117 ? 3.572   -9.795  -4.952  1.00 23.05  ? 117 ARG A CD  1 
ATOM   903  N  NE  . ARG A 1 117 ? 2.795   -9.410  -3.783  1.00 20.41  ? 117 ARG A NE  1 
ATOM   904  C  CZ  . ARG A 1 117 ? 1.486   -9.592  -3.666  1.00 19.50  ? 117 ARG A CZ  1 
ATOM   905  N  NH1 . ARG A 1 117 ? 0.834   -9.209  -2.579  1.00 20.03  ? 117 ARG A NH1 1 
ATOM   906  N  NH2 . ARG A 1 117 ? 0.761   -10.184 -4.627  1.00 22.66  ? 117 ARG A NH2 1 
ATOM   907  N  N   . LEU A 1 118 ? 5.271   -6.681  -8.137  1.00 17.37  ? 118 LEU A N   1 
ATOM   908  C  CA  . LEU A 1 118 ? 4.909   -5.284  -8.196  1.00 17.33  ? 118 LEU A CA  1 
ATOM   909  C  C   . LEU A 1 118 ? 3.674   -5.063  -9.076  1.00 18.70  ? 118 LEU A C   1 
ATOM   910  O  O   . LEU A 1 118 ? 2.796   -4.290  -8.712  1.00 19.32  ? 118 LEU A O   1 
ATOM   911  C  CB  . LEU A 1 118 ? 6.092   -4.513  -8.740  1.00 15.80  ? 118 LEU A CB  1 
ATOM   912  C  CG  . LEU A 1 118 ? 7.241   -4.273  -7.776  1.00 15.87  ? 118 LEU A CG  1 
ATOM   913  C  CD1 . LEU A 1 118 ? 8.496   -3.851  -8.549  1.00 17.15  ? 118 LEU A CD1 1 
ATOM   914  C  CD2 . LEU A 1 118 ? 6.779   -3.272  -6.707  1.00 19.82  ? 118 LEU A CD2 1 
ATOM   915  N  N   . HIS A 1 119 ? 3.573   -5.767  -10.221 1.00 19.11  ? 119 HIS A N   1 
ATOM   916  C  CA  . HIS A 1 119 ? 2.398   -5.564  -11.078 1.00 22.54  ? 119 HIS A CA  1 
ATOM   917  C  C   . HIS A 1 119 ? 1.156   -6.196  -10.446 1.00 21.60  ? 119 HIS A C   1 
ATOM   918  O  O   . HIS A 1 119 ? 0.048   -5.637  -10.508 1.00 24.84  ? 119 HIS A O   1 
ATOM   919  C  CB  . HIS A 1 119 ? 2.684   -6.104  -12.480 1.00 20.76  ? 119 HIS A CB  1 
ATOM   920  C  CG  . HIS A 1 119 ? 3.586   -5.254  -13.334 1.00 19.63  ? 119 HIS A CG  1 
ATOM   921  N  ND1 . HIS A 1 119 ? 3.366   -3.931  -13.613 1.00 20.64  ? 119 HIS A ND1 1 
ATOM   922  C  CD2 . HIS A 1 119 ? 4.744   -5.557  -13.969 1.00 19.43  ? 119 HIS A CD2 1 
ATOM   923  C  CE1 . HIS A 1 119 ? 4.331   -3.449  -14.379 1.00 19.37  ? 119 HIS A CE1 1 
ATOM   924  N  NE2 . HIS A 1 119 ? 5.183   -4.429  -14.617 1.00 20.37  ? 119 HIS A NE2 1 
ATOM   925  N  N   . GLU A 1 120 ? 1.296   -7.364  -9.798  1.00 22.35  ? 120 GLU A N   1 
ATOM   926  C  CA  . GLU A 1 120 ? 0.108   -7.937  -9.160  1.00 25.02  ? 120 GLU A CA  1 
ATOM   927  C  C   . GLU A 1 120 ? -0.408  -6.974  -8.097  1.00 25.40  ? 120 GLU A C   1 
ATOM   928  O  O   . GLU A 1 120 ? -1.593  -6.782  -7.959  1.00 25.26  ? 120 GLU A O   1 
ATOM   929  C  CB  . GLU A 1 120 ? 0.372   -9.253  -8.438  1.00 27.77  ? 120 GLU A CB  1 
ATOM   930  C  CG  . GLU A 1 120 ? 0.752   -10.433 -9.279  1.00 35.10  ? 120 GLU A CG  1 
ATOM   931  C  CD  . GLU A 1 120 ? 1.262   -11.630 -8.494  1.00 42.70  ? 120 GLU A CD  1 
ATOM   932  O  OE1 . GLU A 1 120 ? 1.490   -11.553 -7.255  1.00 42.58  ? 120 GLU A OE1 1 
ATOM   933  O  OE2 . GLU A 1 120 ? 1.457   -12.683 -9.148  1.00 48.01  ? 120 GLU A OE2 1 
ATOM   934  N  N   . VAL A 1 121 ? 0.537   -6.406  -7.345  1.00 22.67  ? 121 VAL A N   1 
ATOM   935  C  CA  . VAL A 1 121 ? 0.085   -5.485  -6.307  1.00 21.56  ? 121 VAL A CA  1 
ATOM   936  C  C   . VAL A 1 121 ? -0.618  -4.282  -6.915  1.00 23.17  ? 121 VAL A C   1 
ATOM   937  O  O   . VAL A 1 121 ? -1.712  -3.836  -6.538  1.00 22.29  ? 121 VAL A O   1 
ATOM   938  C  CB  . VAL A 1 121 ? 1.273   -5.078  -5.407  1.00 20.40  ? 121 VAL A CB  1 
ATOM   939  C  CG1 . VAL A 1 121 ? 0.975   -3.836  -4.602  1.00 19.99  ? 121 VAL A CG1 1 
ATOM   940  C  CG2 . VAL A 1 121 ? 1.628   -6.231  -4.475  1.00 19.83  ? 121 VAL A CG2 1 
ATOM   941  N  N   . GLY A 1 122 ? -0.001  -3.670  -7.918  1.00 22.46  ? 122 GLY A N   1 
ATOM   942  C  CA  . GLY A 1 122 ? -0.577  -2.451  -8.465  1.00 23.11  ? 122 GLY A CA  1 
ATOM   943  C  C   . GLY A 1 122 ? -1.886  -2.641  -9.176  1.00 25.60  ? 122 GLY A C   1 
ATOM   944  O  O   . GLY A 1 122 ? -2.729  -1.754  -9.126  1.00 26.69  ? 122 GLY A O   1 
ATOM   945  N  N   . ARG A 1 123 ? -2.022  -3.806  -9.814  1.00 25.94  ? 123 ARG A N   1 
ATOM   946  C  CA  . ARG A 1 123 ? -3.255  -4.107  -10.534 1.00 28.95  ? 123 ARG A CA  1 
ATOM   947  C  C   . ARG A 1 123 ? -4.330  -4.701  -9.654  1.00 29.66  ? 123 ARG A C   1 
ATOM   948  O  O   . ARG A 1 123 ? -5.518  -4.415  -9.920  1.00 29.52  ? 123 ARG A O   1 
ATOM   949  C  CB  . ARG A 1 123 ? -2.896  -5.083  -11.655 1.00 34.61  ? 123 ARG A CB  1 
ATOM   950  C  CG  . ARG A 1 123 ? -1.914  -4.449  -12.633 1.00 46.59  ? 123 ARG A CG  1 
ATOM   951  C  CD  . ARG A 1 123 ? -2.373  -4.794  -14.038 1.00 61.45  ? 123 ARG A CD  1 
ATOM   952  N  NE  . ARG A 1 123 ? -1.404  -4.431  -15.066 1.00 74.60  ? 123 ARG A NE  1 
ATOM   953  C  CZ  . ARG A 1 123 ? -1.635  -4.710  -16.356 1.00 82.03  ? 123 ARG A CZ  1 
ATOM   954  N  NH1 . ARG A 1 123 ? -2.779  -5.326  -16.637 1.00 91.66  ? 123 ARG A NH1 1 
ATOM   955  N  NH2 . ARG A 1 123 ? -0.680  -4.334  -17.196 1.00 91.79  ? 123 ARG A NH2 1 
ATOM   956  N  N   . THR A 1 124 ? -3.990  -5.509  -8.651  1.00 26.76  ? 124 THR A N   1 
ATOM   957  C  CA  . THR A 1 124 ? -5.063  -6.180  -7.921  1.00 29.68  ? 124 THR A CA  1 
ATOM   958  C  C   . THR A 1 124 ? -5.040  -6.019  -6.410  1.00 27.02  ? 124 THR A C   1 
ATOM   959  O  O   . THR A 1 124 ? -6.023  -6.332  -5.719  1.00 28.72  ? 124 THR A O   1 
ATOM   960  C  CB  . THR A 1 124 ? -5.071  -7.691  -8.253  1.00 32.01  ? 124 THR A CB  1 
ATOM   961  O  OG1 . THR A 1 124 ? -3.865  -8.300  -7.801  1.00 39.30  ? 124 THR A OG1 1 
ATOM   962  C  CG2 . THR A 1 124 ? -5.143  -7.893  -9.759  1.00 39.80  ? 124 THR A CG2 1 
ATOM   963  N  N   . GLU A 1 125 ? -3.979  -5.528  -5.824  1.00 23.12  ? 125 GLU A N   1 
ATOM   964  C  CA  . GLU A 1 125 ? -3.969  -5.226  -4.409  1.00 24.33  ? 125 GLU A CA  1 
ATOM   965  C  C   . GLU A 1 125 ? -3.259  -3.881  -4.210  1.00 21.90  ? 125 GLU A C   1 
ATOM   966  O  O   . GLU A 1 125 ? -2.247  -3.786  -3.521  1.00 23.11  ? 125 GLU A O   1 
ATOM   967  C  CB  . GLU A 1 125 ? -3.279  -6.337  -3.615  1.00 30.64  ? 125 GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 125 ? -3.543  -7.770  -4.024  1.00 31.05  ? 125 GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 125 ? -2.716  -8.740  -3.186  1.00 32.47  ? 125 GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 125 ? -2.657  -8.582  -1.948  1.00 32.51  ? 125 GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 125 ? -2.112  -9.682  -3.772  1.00 31.66  ? 125 GLU A OE2 1 
ATOM   972  N  N   . PRO A 1 126 ? -3.764  -2.805  -4.806  1.00 22.01  ? 126 PRO A N   1 
ATOM   973  C  CA  . PRO A 1 126 ? -3.065  -1.518  -4.836  1.00 19.88  ? 126 PRO A CA  1 
ATOM   974  C  C   . PRO A 1 126 ? -2.897  -0.902  -3.466  1.00 20.81  ? 126 PRO A C   1 
ATOM   975  O  O   . PRO A 1 126 ? -2.011  -0.078  -3.218  1.00 22.00  ? 126 PRO A O   1 
ATOM   976  C  CB  . PRO A 1 126 ? -3.943  -0.682  -5.761  1.00 20.56  ? 126 PRO A CB  1 
ATOM   977  C  CG  . PRO A 1 126 ? -5.305  -1.270  -5.568  1.00 21.21  ? 126 PRO A CG  1 
ATOM   978  C  CD  . PRO A 1 126 ? -5.070  -2.754  -5.497  1.00 24.34  ? 126 PRO A CD  1 
ATOM   979  N  N   . GLU A 1 127 ? -3.700  -1.330  -2.494  1.00 21.21  ? 127 GLU A N   1 
ATOM   980  C  CA  . GLU A 1 127 ? -3.569  -0.870  -1.116  1.00 23.09  ? 127 GLU A CA  1 
ATOM   981  C  C   . GLU A 1 127 ? -2.219  -1.222  -0.512  1.00 22.94  ? 127 GLU A C   1 
ATOM   982  O  O   . GLU A 1 127 ? -1.884  -0.595  0.493   1.00 22.92  ? 127 GLU A O   1 
ATOM   983  C  CB  . GLU A 1 127 ? -4.690  -1.477  -0.286  1.00 27.22  ? 127 GLU A CB  1 
ATOM   984  C  CG  . GLU A 1 127 ? -4.638  -2.982  -0.093  1.00 33.18  ? 127 GLU A CG  1 
ATOM   985  C  CD  . GLU A 1 127 ? -5.409  -3.781  -1.126  1.00 36.11  ? 127 GLU A CD  1 
ATOM   986  O  OE1 . GLU A 1 127 ? -5.812  -3.149  -2.129  1.00 27.48  ? 127 GLU A OE1 1 
ATOM   987  O  OE2 . GLU A 1 127 ? -5.599  -5.009  -0.928  1.00 34.84  ? 127 GLU A OE2 1 
ATOM   988  N  N   . LEU A 1 128 ? -1.546  -2.190  -1.138  1.00 22.12  ? 128 LEU A N   1 
ATOM   989  C  CA  . LEU A 1 128 ? -0.257  -2.649  -0.667  1.00 19.55  ? 128 LEU A CA  1 
ATOM   990  C  C   . LEU A 1 128 ? 0.908   -1.965  -1.361  1.00 18.75  ? 128 LEU A C   1 
ATOM   991  O  O   . LEU A 1 128 ? 2.095   -2.204  -1.097  1.00 20.64  ? 128 LEU A O   1 
ATOM   992  C  CB  . LEU A 1 128 ? -0.129  -4.168  -0.840  1.00 20.48  ? 128 LEU A CB  1 
ATOM   993  C  CG  . LEU A 1 128 ? -1.248  -5.013  -0.238  1.00 21.90  ? 128 LEU A CG  1 
ATOM   994  C  CD1 . LEU A 1 128 ? -0.900  -6.484  -0.323  1.00 25.99  ? 128 LEU A CD1 1 
ATOM   995  C  CD2 . LEU A 1 128 ? -1.513  -4.645  1.221   1.00 24.56  ? 128 LEU A CD2 1 
ATOM   996  N  N   . LEU A 1 129 ? 0.583   -1.088  -2.290  1.00 20.26  ? 129 LEU A N   1 
ATOM   997  C  CA  . LEU A 1 129 ? 1.680   -0.494  -3.070  1.00 18.14  ? 129 LEU A CA  1 
ATOM   998  C  C   . LEU A 1 129 ? 2.570   0.390   -2.209  1.00 18.44  ? 129 LEU A C   1 
ATOM   999  O  O   . LEU A 1 129 ? 3.790   0.430   -2.443  1.00 18.74  ? 129 LEU A O   1 
ATOM   1000 C  CB  . LEU A 1 129 ? 1.107   0.239   -4.297  1.00 19.44  ? 129 LEU A CB  1 
ATOM   1001 C  CG  . LEU A 1 129 ? 2.075   0.791   -5.356  1.00 21.08  ? 129 LEU A CG  1 
ATOM   1002 C  CD1 . LEU A 1 129 ? 2.879   -0.278  -6.062  1.00 23.70  ? 129 LEU A CD1 1 
ATOM   1003 C  CD2 . LEU A 1 129 ? 1.328   1.595   -6.427  1.00 23.34  ? 129 LEU A CD2 1 
ATOM   1004 N  N   . VAL A 1 130 ? 1.979   1.036   -1.240  1.00 19.39  ? 130 VAL A N   1 
ATOM   1005 C  CA  . VAL A 1 130 ? 2.770   1.857   -0.308  1.00 18.24  ? 130 VAL A CA  1 
ATOM   1006 C  C   . VAL A 1 130 ? 3.867   1.041   0.331   1.00 18.28  ? 130 VAL A C   1 
ATOM   1007 O  O   . VAL A 1 130 ? 4.936   1.600   0.631   1.00 20.01  ? 130 VAL A O   1 
ATOM   1008 C  CB  . VAL A 1 130 ? 1.828   2.493   0.731   1.00 19.16  ? 130 VAL A CB  1 
ATOM   1009 C  CG1 . VAL A 1 130 ? 1.142   1.435   1.555   1.00 20.93  ? 130 VAL A CG1 1 
ATOM   1010 C  CG2 . VAL A 1 130 ? 2.609   3.476   1.589   1.00 21.61  ? 130 VAL A CG2 1 
ATOM   1011 N  N   . ALA A 1 131 ? 3.656   -0.248  0.543   1.00 19.87  ? 131 ALA A N   1 
ATOM   1012 C  CA  . ALA A 1 131 ? 4.723   -1.056  1.145   1.00 20.25  ? 131 ALA A CA  1 
ATOM   1013 C  C   . ALA A 1 131 ? 5.957   -1.129  0.259   1.00 19.79  ? 131 ALA A C   1 
ATOM   1014 O  O   . ALA A 1 131 ? 7.114   -1.129  0.704   1.00 20.13  ? 131 ALA A O   1 
ATOM   1015 C  CB  . ALA A 1 131 ? 4.219   -2.468  1.471   1.00 22.82  ? 131 ALA A CB  1 
ATOM   1016 N  N   . HIS A 1 132 ? 5.706   -1.233  -1.051  1.00 18.61  ? 132 HIS A N   1 
ATOM   1017 C  CA  . HIS A 1 132 ? 6.793   -1.355  -2.001  1.00 18.46  ? 132 HIS A CA  1 
ATOM   1018 C  C   . HIS A 1 132 ? 7.482   -0.029  -2.237  1.00 17.42  ? 132 HIS A C   1 
ATOM   1019 O  O   . HIS A 1 132 ? 8.719   0.015   -2.417  1.00 19.56  ? 132 HIS A O   1 
ATOM   1020 C  CB  . HIS A 1 132 ? 6.234   -1.907  -3.311  1.00 18.25  ? 132 HIS A CB  1 
ATOM   1021 C  CG  . HIS A 1 132 ? 6.048   -3.394  -3.215  1.00 17.63  ? 132 HIS A CG  1 
ATOM   1022 N  ND1 . HIS A 1 132 ? 7.123   -4.254  -3.393  1.00 18.85  ? 132 HIS A ND1 1 
ATOM   1023 C  CD2 . HIS A 1 132 ? 4.978   -4.161  -2.971  1.00 18.55  ? 132 HIS A CD2 1 
ATOM   1024 C  CE1 . HIS A 1 132 ? 6.706   -5.504  -3.260  1.00 19.78  ? 132 HIS A CE1 1 
ATOM   1025 N  NE2 . HIS A 1 132 ? 5.405   -5.474  -3.002  1.00 20.43  ? 132 HIS A NE2 1 
ATOM   1026 N  N   . ALA A 1 133 ? 6.709   1.034   -2.215  1.00 17.27  ? 133 ALA A N   1 
ATOM   1027 C  CA  . ALA A 1 133 ? 7.309   2.364   -2.378  1.00 17.01  ? 133 ALA A CA  1 
ATOM   1028 C  C   . ALA A 1 133 ? 8.136   2.741   -1.158  1.00 18.27  ? 133 ALA A C   1 
ATOM   1029 O  O   . ALA A 1 133 ? 9.228   3.283   -1.265  1.00 19.07  ? 133 ALA A O   1 
ATOM   1030 C  CB  . ALA A 1 133 ? 6.190   3.346   -2.701  1.00 21.64  ? 133 ALA A CB  1 
ATOM   1031 N  N   . TYR A 1 134 ? 7.655   2.443   0.039   1.00 18.44  ? 134 TYR A N   1 
ATOM   1032 C  CA  . TYR A 1 134 ? 8.435   2.576   1.266   1.00 20.70  ? 134 TYR A CA  1 
ATOM   1033 C  C   . TYR A 1 134 ? 9.748   1.817   1.158   1.00 19.50  ? 134 TYR A C   1 
ATOM   1034 O  O   . TYR A 1 134 ? 10.799  2.428   1.370   1.00 20.44  ? 134 TYR A O   1 
ATOM   1035 C  CB  . TYR A 1 134 ? 7.667   2.007   2.470   1.00 24.61  ? 134 TYR A CB  1 
ATOM   1036 C  CG  . TYR A 1 134 ? 8.440   1.719   3.728   1.00 23.54  ? 134 TYR A CG  1 
ATOM   1037 C  CD1 . TYR A 1 134 ? 8.777   2.773   4.577   1.00 22.67  ? 134 TYR A CD1 1 
ATOM   1038 C  CD2 . TYR A 1 134 ? 8.823   0.425   4.080   1.00 24.87  ? 134 TYR A CD2 1 
ATOM   1039 C  CE1 . TYR A 1 134 ? 9.484   2.564   5.748   1.00 24.17  ? 134 TYR A CE1 1 
ATOM   1040 C  CE2 . TYR A 1 134 ? 9.528   0.202   5.236   1.00 24.86  ? 134 TYR A CE2 1 
ATOM   1041 C  CZ  . TYR A 1 134 ? 9.847   1.266   6.053   1.00 24.45  ? 134 TYR A CZ  1 
ATOM   1042 O  OH  . TYR A 1 134 ? 10.549  1.034   7.194   1.00 29.81  ? 134 TYR A OH  1 
ATOM   1043 N  N   . THR A 1 135 ? 9.665   0.514   0.841   1.00 20.02  ? 135 THR A N   1 
ATOM   1044 C  CA  . THR A 1 135 ? 10.893  -0.323  0.896   1.00 20.65  ? 135 THR A CA  1 
ATOM   1045 C  C   . THR A 1 135 ? 11.963  0.187   -0.063  1.00 18.56  ? 135 THR A C   1 
ATOM   1046 O  O   . THR A 1 135 ? 13.157  0.280   0.241   1.00 22.66  ? 135 THR A O   1 
ATOM   1047 C  CB  . THR A 1 135 ? 10.476  -1.768  0.604   1.00 22.28  ? 135 THR A CB  1 
ATOM   1048 O  OG1 . THR A 1 135 ? 9.711   -2.215  1.738   1.00 29.46  ? 135 THR A OG1 1 
ATOM   1049 C  CG2 . THR A 1 135 ? 11.648  -2.721  0.497   1.00 22.25  ? 135 THR A CG2 1 
ATOM   1050 N  N   . ARG A 1 136 ? 11.564  0.550   -1.291  1.00 17.74  ? 136 ARG A N   1 
ATOM   1051 C  CA  . ARG A 1 136 ? 12.466  1.024   -2.336  1.00 17.06  ? 136 ARG A CA  1 
ATOM   1052 C  C   . ARG A 1 136 ? 12.844  2.476   -2.072  1.00 17.43  ? 136 ARG A C   1 
ATOM   1053 O  O   . ARG A 1 136 ? 14.036  2.755   -1.885  1.00 17.96  ? 136 ARG A O   1 
ATOM   1054 C  CB  . ARG A 1 136 ? 11.820  0.865   -3.717  1.00 19.89  ? 136 ARG A CB  1 
ATOM   1055 C  CG  . ARG A 1 136 ? 12.010  -0.516  -4.332  1.00 23.03  ? 136 ARG A CG  1 
ATOM   1056 C  CD  . ARG A 1 136 ? 13.223  -0.520  -5.218  1.00 24.37  ? 136 ARG A CD  1 
ATOM   1057 N  NE  . ARG A 1 136 ? 14.518  -0.400  -4.545  1.00 21.59  ? 136 ARG A NE  1 
ATOM   1058 C  CZ  . ARG A 1 136 ? 15.166  -1.434  -4.102  1.00 23.95  ? 136 ARG A CZ  1 
ATOM   1059 N  NH1 . ARG A 1 136 ? 14.712  -2.695  -4.158  1.00 28.63  ? 136 ARG A NH1 1 
ATOM   1060 N  NH2 . ARG A 1 136 ? 16.331  -1.234  -3.539  1.00 24.84  ? 136 ARG A NH2 1 
ATOM   1061 N  N   . TYR A 1 137 ? 11.874  3.400   -2.059  1.00 17.01  ? 137 TYR A N   1 
ATOM   1062 C  CA  . TYR A 1 137 ? 12.266  4.807   -2.010  1.00 17.56  ? 137 TYR A CA  1 
ATOM   1063 C  C   . TYR A 1 137 ? 12.850  5.225   -0.680  1.00 18.31  ? 137 TYR A C   1 
ATOM   1064 O  O   . TYR A 1 137 ? 13.845  5.958   -0.658  1.00 21.65  ? 137 TYR A O   1 
ATOM   1065 C  CB  . TYR A 1 137 ? 11.082  5.717   -2.344  1.00 17.85  ? 137 TYR A CB  1 
ATOM   1066 C  CG  . TYR A 1 137 ? 10.619  5.652   -3.783  1.00 17.71  ? 137 TYR A CG  1 
ATOM   1067 C  CD1 . TYR A 1 137 ? 11.467  5.908   -4.848  1.00 17.95  ? 137 TYR A CD1 1 
ATOM   1068 C  CD2 . TYR A 1 137 ? 9.314   5.324   -4.087  1.00 22.21  ? 137 TYR A CD2 1 
ATOM   1069 C  CE1 . TYR A 1 137 ? 11.011  5.842   -6.151  1.00 17.13  ? 137 TYR A CE1 1 
ATOM   1070 C  CE2 . TYR A 1 137 ? 8.848   5.255   -5.365  1.00 22.43  ? 137 TYR A CE2 1 
ATOM   1071 C  CZ  . TYR A 1 137 ? 9.704   5.519   -6.412  1.00 20.94  ? 137 TYR A CZ  1 
ATOM   1072 O  OH  . TYR A 1 137 ? 9.270   5.443   -7.728  1.00 26.35  ? 137 TYR A OH  1 
ATOM   1073 N  N   . LEU A 1 138 ? 12.273  4.809   0.439   1.00 19.77  ? 138 LEU A N   1 
ATOM   1074 C  CA  . LEU A 1 138 ? 12.806  5.342   1.709   1.00 20.38  ? 138 LEU A CA  1 
ATOM   1075 C  C   . LEU A 1 138 ? 14.118  4.621   1.985   1.00 20.81  ? 138 LEU A C   1 
ATOM   1076 O  O   . LEU A 1 138 ? 15.062  5.186   2.530   1.00 23.97  ? 138 LEU A O   1 
ATOM   1077 C  CB  . LEU A 1 138 ? 11.787  5.250   2.832   1.00 24.42  ? 138 LEU A CB  1 
ATOM   1078 C  CG  . LEU A 1 138 ? 11.899  6.226   3.993   1.00 33.76  ? 138 LEU A CG  1 
ATOM   1079 C  CD1 . LEU A 1 138 ? 11.873  7.675   3.506   1.00 50.84  ? 138 LEU A CD1 1 
ATOM   1080 C  CD2 . LEU A 1 138 ? 10.806  5.971   5.025   1.00 39.10  ? 138 LEU A CD2 1 
ATOM   1081 N  N   . GLY A 1 139 ? 14.209  3.356   1.571   1.00 21.25  ? 139 GLY A N   1 
ATOM   1082 C  CA  . GLY A 1 139 ? 15.489  2.693   1.674   1.00 22.40  ? 139 GLY A CA  1 
ATOM   1083 C  C   . GLY A 1 139 ? 16.535  3.311   0.784   1.00 23.75  ? 139 GLY A C   1 
ATOM   1084 O  O   . GLY A 1 139 ? 17.650  3.539   1.286   1.00 24.05  ? 139 GLY A O   1 
ATOM   1085 N  N   . ASP A 1 140 ? 16.261  3.593   -0.486  1.00 21.65  ? 140 ASP A N   1 
ATOM   1086 C  CA  . ASP A 1 140 ? 17.332  4.059   -1.383  1.00 24.17  ? 140 ASP A CA  1 
ATOM   1087 C  C   . ASP A 1 140 ? 17.745  5.461   -0.962  1.00 25.07  ? 140 ASP A C   1 
ATOM   1088 O  O   . ASP A 1 140 ? 18.885  5.935   -0.965  1.00 28.67  ? 140 ASP A O   1 
ATOM   1089 C  CB  . ASP A 1 140 ? 16.805  3.891   -2.818  1.00 26.37  ? 140 ASP A CB  1 
ATOM   1090 C  CG  . ASP A 1 140 ? 16.662  2.445   -3.229  1.00 27.46  ? 140 ASP A CG  1 
ATOM   1091 O  OD1 . ASP A 1 140 ? 17.076  1.483   -2.538  1.00 37.70  ? 140 ASP A OD1 1 
ATOM   1092 O  OD2 . ASP A 1 140 ? 16.058  2.185   -4.301  1.00 33.37  ? 140 ASP A OD2 1 
ATOM   1093 N  N   . LEU A 1 141 ? 16.753  6.238   -0.501  1.00 29.58  ? 141 LEU A N   1 
ATOM   1094 C  CA  . LEU A 1 141 ? 16.997  7.599   -0.039  1.00 32.68  ? 141 LEU A CA  1 
ATOM   1095 C  C   . LEU A 1 141 ? 17.803  7.556   1.250   1.00 37.85  ? 141 LEU A C   1 
ATOM   1096 O  O   . LEU A 1 141 ? 18.817  8.251   1.257   1.00 35.71  ? 141 LEU A O   1 
ATOM   1097 C  CB  . LEU A 1 141 ? 15.644  8.302   0.118   1.00 32.72  ? 141 LEU A CB  1 
ATOM   1098 C  CG  . LEU A 1 141 ? 15.612  9.758   0.495   1.00 29.77  ? 141 LEU A CG  1 
ATOM   1099 C  CD1 . LEU A 1 141 ? 16.335  10.614  -0.542  1.00 30.82  ? 141 LEU A CD1 1 
ATOM   1100 C  CD2 . LEU A 1 141 ? 14.178  10.235  0.669   1.00 34.72  ? 141 LEU A CD2 1 
ATOM   1101 N  N   . SER A 1 142 ? 17.431  6.794   2.258   1.00 38.09  ? 142 SER A N   1 
ATOM   1102 C  CA  . SER A 1 142 ? 17.993  6.713   3.593   1.00 38.81  ? 142 SER A CA  1 
ATOM   1103 C  C   . SER A 1 142 ? 19.369  6.059   3.592   1.00 42.86  ? 142 SER A C   1 
ATOM   1104 O  O   . SER A 1 142 ? 20.280  6.462   4.320   1.00 43.68  ? 142 SER A O   1 
ATOM   1105 C  CB  . SER A 1 142 ? 17.117  5.894   4.554   1.00 42.20  ? 142 SER A CB  1 
ATOM   1106 O  OG  . SER A 1 142 ? 16.810  6.626   5.705   1.00 55.42  ? 142 SER A OG  1 
ATOM   1107 N  N   . GLY A 1 143 ? 19.485  5.038   2.754   1.00 39.14  ? 143 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 143 ? 20.725  4.303   2.634   1.00 40.20  ? 143 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 143 ? 21.617  4.743   1.499   1.00 37.96  ? 143 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 143 ? 22.765  4.301   1.448   1.00 35.92  ? 143 GLY A O   1 
ATOM   1111 N  N   . GLY A 1 144 ? 21.177  5.586   0.575   1.00 36.40  ? 144 GLY A N   1 
ATOM   1112 C  CA  . GLY A 1 144 ? 21.940  5.977   -0.593  1.00 38.17  ? 144 GLY A CA  1 
ATOM   1113 C  C   . GLY A 1 144 ? 23.291  6.597   -0.316  1.00 39.29  ? 144 GLY A C   1 
ATOM   1114 O  O   . GLY A 1 144 ? 24.222  6.413   -1.093  1.00 43.36  ? 144 GLY A O   1 
ATOM   1115 N  N   . GLN A 1 145 ? 23.406  7.331   0.780   1.00 43.09  ? 145 GLN A N   1 
ATOM   1116 C  CA  . GLN A 1 145 ? 24.646  7.923   1.249   1.00 50.99  ? 145 GLN A CA  1 
ATOM   1117 C  C   . GLN A 1 145 ? 25.743  6.869   1.444   1.00 47.52  ? 145 GLN A C   1 
ATOM   1118 O  O   . GLN A 1 145 ? 26.838  6.989   0.893   1.00 48.84  ? 145 GLN A O   1 
ATOM   1119 C  CB  . GLN A 1 145 ? 24.519  8.682   2.582   1.00 63.14  ? 145 GLN A CB  1 
ATOM   1120 C  CG  . GLN A 1 145 ? 23.478  9.775   2.665   1.00 70.64  ? 145 GLN A CG  1 
ATOM   1121 C  CD  . GLN A 1 145 ? 22.034  9.358   2.485   1.00 82.29  ? 145 GLN A CD  1 
ATOM   1122 O  OE1 . GLN A 1 145 ? 21.219  10.116  1.944   1.00 88.91  ? 145 GLN A OE1 1 
ATOM   1123 N  NE2 . GLN A 1 145 ? 21.691  8.142   2.911   1.00 88.75  ? 145 GLN A NE2 1 
ATOM   1124 N  N   . VAL A 1 146 ? 25.452  5.852   2.252   1.00 47.04  ? 146 VAL A N   1 
ATOM   1125 C  CA  . VAL A 1 146 ? 26.540  4.893   2.504   1.00 46.25  ? 146 VAL A CA  1 
ATOM   1126 C  C   . VAL A 1 146 ? 26.712  4.000   1.269   1.00 44.12  ? 146 VAL A C   1 
ATOM   1127 O  O   . VAL A 1 146 ? 27.825  3.591   0.922   1.00 45.19  ? 146 VAL A O   1 
ATOM   1128 C  CB  . VAL A 1 146 ? 26.358  4.027   3.762   1.00 56.60  ? 146 VAL A CB  1 
ATOM   1129 C  CG1 . VAL A 1 146 ? 25.543  4.730   4.842   1.00 61.17  ? 146 VAL A CG1 1 
ATOM   1130 C  CG2 . VAL A 1 146 ? 25.697  2.693   3.423   1.00 56.28  ? 146 VAL A CG2 1 
ATOM   1131 N  N   . LEU A 1 147 ? 25.614  3.715   0.592   1.00 45.31  ? 147 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 147 ? 25.577  2.751   -0.517  1.00 45.23  ? 147 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 147 ? 26.389  3.282   -1.693  1.00 41.32  ? 147 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 147 ? 27.131  2.567   -2.364  1.00 45.87  ? 147 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 147 ? 24.130  2.423   -0.917  1.00 51.75  ? 147 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 147 ? 23.173  1.869   0.146   1.00 52.67  ? 147 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 147 ? 21.698  1.964   -0.277  1.00 58.22  ? 147 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 147 ? 23.463  0.423   0.521   1.00 56.71  ? 147 LEU A CD2 1 
ATOM   1139 N  N   . LYS A 1 148 ? 26.296  4.578   -2.012  1.00 35.82  ? 148 LYS A N   1 
ATOM   1140 C  CA  . LYS A 1 148 ? 27.077  5.105   -3.105  1.00 33.47  ? 148 LYS A CA  1 
ATOM   1141 C  C   . LYS A 1 148 ? 28.561  5.132   -2.751  1.00 38.71  ? 148 LYS A C   1 
ATOM   1142 O  O   . LYS A 1 148 ? 29.363  4.821   -3.636  1.00 52.28  ? 148 LYS A O   1 
ATOM   1143 C  CB  . LYS A 1 148 ? 26.621  6.530   -3.455  1.00 32.27  ? 148 LYS A CB  1 
ATOM   1144 C  CG  . LYS A 1 148 ? 27.425  7.134   -4.570  1.00 32.66  ? 148 LYS A CG  1 
ATOM   1145 C  CD  . LYS A 1 148 ? 27.063  8.600   -4.839  1.00 31.85  ? 148 LYS A CD  1 
ATOM   1146 C  CE  . LYS A 1 148 ? 27.864  9.034   -6.059  1.00 29.43  ? 148 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A 1 148 ? 27.612  10.432  -6.442  1.00 26.29  ? 148 LYS A NZ  1 
ATOM   1148 N  N   . LYS A 1 149 ? 28.882  5.494   -1.522  1.00 43.81  ? 149 LYS A N   1 
ATOM   1149 C  CA  . LYS A 1 149 ? 30.231  5.802   -1.073  1.00 54.91  ? 149 LYS A CA  1 
ATOM   1150 C  C   . LYS A 1 149 ? 31.191  4.706   -1.523  1.00 55.78  ? 149 LYS A C   1 
ATOM   1151 O  O   . LYS A 1 149 ? 32.265  4.925   -2.061  1.00 56.12  ? 149 LYS A O   1 
ATOM   1152 C  CB  . LYS A 1 149 ? 30.240  5.920   0.449   1.00 61.32  ? 149 LYS A CB  1 
ATOM   1153 C  CG  . LYS A 1 149 ? 31.462  5.307   1.130   1.00 71.72  ? 149 LYS A CG  1 
ATOM   1154 C  CD  . LYS A 1 149 ? 32.442  6.397   1.532   1.00 80.40  ? 149 LYS A CD  1 
ATOM   1155 C  CE  . LYS A 1 149 ? 33.899  6.032   1.283   1.00 85.78  ? 149 LYS A CE  1 
ATOM   1156 N  NZ  . LYS A 1 149 ? 34.667  7.226   0.831   1.00 96.29  ? 149 LYS A NZ  1 
ATOM   1157 N  N   . ILE A 1 150 ? 30.692  3.517   -1.250  1.00 56.22  ? 150 ILE A N   1 
ATOM   1158 C  CA  . ILE A 1 150 ? 31.321  2.227   -1.447  1.00 60.17  ? 150 ILE A CA  1 
ATOM   1159 C  C   . ILE A 1 150 ? 31.666  2.035   -2.910  1.00 61.41  ? 150 ILE A C   1 
ATOM   1160 O  O   . ILE A 1 150 ? 32.767  1.633   -3.308  1.00 56.90  ? 150 ILE A O   1 
ATOM   1161 C  CB  . ILE A 1 150 ? 30.364  1.154   -0.877  1.00 65.02  ? 150 ILE A CB  1 
ATOM   1162 C  CG1 . ILE A 1 150 ? 29.703  1.576   0.443   1.00 67.57  ? 150 ILE A CG1 1 
ATOM   1163 C  CG2 . ILE A 1 150 ? 31.037  -0.195  -0.705  1.00 72.70  ? 150 ILE A CG2 1 
ATOM   1164 C  CD1 . ILE A 1 150 ? 29.440  0.477   1.444   1.00 61.51  ? 150 ILE A CD1 1 
ATOM   1165 N  N   . ALA A 1 151 ? 30.714  2.344   -3.798  1.00 56.07  ? 151 ALA A N   1 
ATOM   1166 C  CA  . ALA A 1 151 ? 30.947  2.010   -5.200  1.00 53.49  ? 151 ALA A CA  1 
ATOM   1167 C  C   . ALA A 1 151 ? 32.089  2.805   -5.799  1.00 52.63  ? 151 ALA A C   1 
ATOM   1168 O  O   . ALA A 1 151 ? 32.995  2.252   -6.392  1.00 51.07  ? 151 ALA A O   1 
ATOM   1169 C  CB  . ALA A 1 151 ? 29.686  2.254   -6.002  1.00 47.79  ? 151 ALA A CB  1 
ATOM   1170 N  N   . GLN A 1 152 ? 31.993  4.112   -5.637  1.00 49.82  ? 152 GLN A N   1 
ATOM   1171 C  CA  . GLN A 1 152 ? 32.874  5.005   -6.370  1.00 55.17  ? 152 GLN A CA  1 
ATOM   1172 C  C   . GLN A 1 152 ? 34.313  4.685   -5.983  1.00 57.07  ? 152 GLN A C   1 
ATOM   1173 O  O   . GLN A 1 152 ? 35.252  4.766   -6.764  1.00 63.66  ? 152 GLN A O   1 
ATOM   1174 C  CB  . GLN A 1 152 ? 32.647  6.489   -6.118  1.00 53.70  ? 152 GLN A CB  1 
ATOM   1175 C  CG  . GLN A 1 152 ? 31.747  6.849   -4.960  1.00 54.72  ? 152 GLN A CG  1 
ATOM   1176 C  CD  . GLN A 1 152 ? 31.601  8.350   -4.807  1.00 58.58  ? 152 GLN A CD  1 
ATOM   1177 O  OE1 . GLN A 1 152 ? 32.038  9.097   -5.677  1.00 68.82  ? 152 GLN A OE1 1 
ATOM   1178 N  NE2 . GLN A 1 152 ? 30.998  8.753   -3.697  1.00 66.21  ? 152 GLN A NE2 1 
ATOM   1179 N  N   . LYS A 1 153 ? 34.441  4.311   -4.711  1.00 64.05  ? 153 LYS A N   1 
ATOM   1180 C  CA  . LYS A 1 153 ? 35.835  4.094   -4.292  1.00 66.19  ? 153 LYS A CA  1 
ATOM   1181 C  C   . LYS A 1 153 ? 36.229  2.687   -4.703  1.00 61.41  ? 153 LYS A C   1 
ATOM   1182 O  O   . LYS A 1 153 ? 37.421  2.399   -4.768  1.00 59.14  ? 153 LYS A O   1 
ATOM   1183 C  CB  . LYS A 1 153 ? 35.952  4.424   -2.808  1.00 68.39  ? 153 LYS A CB  1 
ATOM   1184 C  CG  . LYS A 1 153 ? 35.162  5.662   -2.384  1.00 77.12  ? 153 LYS A CG  1 
ATOM   1185 C  CD  . LYS A 1 153 ? 35.263  6.842   -3.341  1.00 81.57  ? 153 LYS A CD  1 
ATOM   1186 C  CE  . LYS A 1 153 ? 34.345  7.992   -2.939  1.00 83.63  ? 153 LYS A CE  1 
ATOM   1187 N  NZ  . LYS A 1 153 ? 34.733  9.279   -3.587  1.00 82.91  ? 153 LYS A NZ  1 
ATOM   1188 N  N   . ALA A 1 154 ? 35.222  1.849   -5.015  1.00 57.51  ? 154 ALA A N   1 
ATOM   1189 C  CA  . ALA A 1 154 ? 35.498  0.483   -5.448  1.00 48.59  ? 154 ALA A CA  1 
ATOM   1190 C  C   . ALA A 1 154 ? 35.561  0.353   -6.968  1.00 48.12  ? 154 ALA A C   1 
ATOM   1191 O  O   . ALA A 1 154 ? 36.394  -0.417  -7.444  1.00 51.16  ? 154 ALA A O   1 
ATOM   1192 C  CB  . ALA A 1 154 ? 34.482  -0.532  -4.959  1.00 49.51  ? 154 ALA A CB  1 
ATOM   1193 N  N   . LEU A 1 155 ? 34.726  1.044   -7.724  1.00 45.69  ? 155 LEU A N   1 
ATOM   1194 C  CA  . LEU A 1 155 ? 34.647  0.856   -9.176  1.00 42.26  ? 155 LEU A CA  1 
ATOM   1195 C  C   . LEU A 1 155 ? 35.706  1.598   -9.985  1.00 42.17  ? 155 LEU A C   1 
ATOM   1196 O  O   . LEU A 1 155 ? 35.863  1.308   -11.172 1.00 49.41  ? 155 LEU A O   1 
ATOM   1197 C  CB  . LEU A 1 155 ? 33.269  1.290   -9.671  1.00 40.99  ? 155 LEU A CB  1 
ATOM   1198 C  CG  . LEU A 1 155 ? 32.113  0.273   -9.563  1.00 39.40  ? 155 LEU A CG  1 
ATOM   1199 C  CD1 . LEU A 1 155 ? 32.303  -0.590  -8.352  1.00 49.91  ? 155 LEU A CD1 1 
ATOM   1200 C  CD2 . LEU A 1 155 ? 30.777  1.001   -9.542  1.00 55.17  ? 155 LEU A CD2 1 
ATOM   1201 N  N   . ASP A 1 156 ? 36.450  2.551   -9.442  1.00 43.68  ? 156 ASP A N   1 
ATOM   1202 C  CA  . ASP A 1 156 ? 37.507  3.257   -10.180 1.00 49.93  ? 156 ASP A CA  1 
ATOM   1203 C  C   . ASP A 1 156 ? 36.940  3.876   -11.446 1.00 48.43  ? 156 ASP A C   1 
ATOM   1204 O  O   . ASP A 1 156 ? 37.503  3.795   -12.541 1.00 50.68  ? 156 ASP A O   1 
ATOM   1205 C  CB  . ASP A 1 156 ? 38.669  2.322   -10.530 1.00 54.68  ? 156 ASP A CB  1 
ATOM   1206 C  CG  . ASP A 1 156 ? 39.821  3.055   -11.179 1.00 63.30  ? 156 ASP A CG  1 
ATOM   1207 O  OD1 . ASP A 1 156 ? 40.452  3.855   -10.464 1.00 77.10  ? 156 ASP A OD1 1 
ATOM   1208 O  OD2 . ASP A 1 156 ? 40.049  2.832   -12.384 1.00 74.03  ? 156 ASP A OD2 1 
ATOM   1209 N  N   . LEU A 1 157 ? 35.753  4.498   -11.294 1.00 45.98  ? 157 LEU A N   1 
ATOM   1210 C  CA  . LEU A 1 157 ? 35.207  4.993   -12.561 1.00 51.17  ? 157 LEU A CA  1 
ATOM   1211 C  C   . LEU A 1 157 ? 36.084  6.149   -13.045 1.00 50.63  ? 157 LEU A C   1 
ATOM   1212 O  O   . LEU A 1 157 ? 36.791  6.838   -12.300 1.00 43.21  ? 157 LEU A O   1 
ATOM   1213 C  CB  . LEU A 1 157 ? 33.726  5.350   -12.516 1.00 54.73  ? 157 LEU A CB  1 
ATOM   1214 C  CG  . LEU A 1 157 ? 32.803  5.602   -11.376 1.00 56.49  ? 157 LEU A CG  1 
ATOM   1215 C  CD1 . LEU A 1 157 ? 31.477  6.086   -11.972 1.00 55.48  ? 157 LEU A CD1 1 
ATOM   1216 C  CD2 . LEU A 1 157 ? 32.536  4.383   -10.511 1.00 61.96  ? 157 LEU A CD2 1 
ATOM   1217 N  N   . PRO A 1 158 ? 36.028  6.292   -14.367 1.00 46.79  ? 158 PRO A N   1 
ATOM   1218 C  CA  . PRO A 1 158 ? 36.710  7.434   -14.975 1.00 44.63  ? 158 PRO A CA  1 
ATOM   1219 C  C   . PRO A 1 158 ? 36.077  8.712   -14.447 1.00 42.48  ? 158 PRO A C   1 
ATOM   1220 O  O   . PRO A 1 158 ? 35.116  8.846   -13.684 1.00 49.56  ? 158 PRO A O   1 
ATOM   1221 C  CB  . PRO A 1 158 ? 36.428  7.250   -16.462 1.00 48.95  ? 158 PRO A CB  1 
ATOM   1222 C  CG  . PRO A 1 158 ? 35.193  6.396   -16.529 1.00 46.88  ? 158 PRO A CG  1 
ATOM   1223 C  CD  . PRO A 1 158 ? 35.339  5.446   -15.375 1.00 48.04  ? 158 PRO A CD  1 
ATOM   1224 N  N   . SER A 1 159 ? 36.641  9.831   -14.862 1.00 42.91  ? 159 SER A N   1 
ATOM   1225 C  CA  . SER A 1 159 ? 35.934  11.053  -14.430 1.00 41.90  ? 159 SER A CA  1 
ATOM   1226 C  C   . SER A 1 159 ? 34.991  11.447  -15.544 1.00 33.67  ? 159 SER A C   1 
ATOM   1227 O  O   . SER A 1 159 ? 35.122  12.481  -16.214 1.00 33.90  ? 159 SER A O   1 
ATOM   1228 C  CB  . SER A 1 159 ? 37.030  12.067  -14.094 1.00 48.30  ? 159 SER A CB  1 
ATOM   1229 O  OG  . SER A 1 159 ? 37.982  11.394  -13.272 1.00 59.89  ? 159 SER A OG  1 
ATOM   1230 N  N   . SER A 1 160 ? 33.998  10.582  -15.825 1.00 29.46  ? 160 SER A N   1 
ATOM   1231 C  CA  . SER A 1 160 ? 33.245  10.912  -17.031 1.00 29.37  ? 160 SER A CA  1 
ATOM   1232 C  C   . SER A 1 160 ? 31.868  11.473  -16.720 1.00 25.49  ? 160 SER A C   1 
ATOM   1233 O  O   . SER A 1 160 ? 31.182  11.529  -17.718 1.00 28.16  ? 160 SER A O   1 
ATOM   1234 C  CB  . SER A 1 160 ? 33.050  9.725   -17.968 1.00 32.92  ? 160 SER A CB  1 
ATOM   1235 O  OG  . SER A 1 160 ? 32.313  8.715   -17.358 1.00 38.21  ? 160 SER A OG  1 
ATOM   1236 N  N   . GLY A 1 161 ? 31.555  11.816  -15.478 1.00 21.90  ? 161 GLY A N   1 
ATOM   1237 C  CA  . GLY A 1 161 ? 30.344  12.532  -15.144 1.00 21.37  ? 161 GLY A CA  1 
ATOM   1238 C  C   . GLY A 1 161 ? 29.067  11.748  -15.330 1.00 18.51  ? 161 GLY A C   1 
ATOM   1239 O  O   . GLY A 1 161 ? 27.979  12.287  -15.431 1.00 18.78  ? 161 GLY A O   1 
ATOM   1240 N  N   . GLU A 1 162 ? 29.167  10.431  -15.371 1.00 18.30  ? 162 GLU A N   1 
ATOM   1241 C  CA  . GLU A 1 162 ? 27.947  9.633   -15.431 1.00 20.22  ? 162 GLU A CA  1 
ATOM   1242 C  C   . GLU A 1 162 ? 28.125  8.274   -14.773 1.00 17.87  ? 162 GLU A C   1 
ATOM   1243 O  O   . GLU A 1 162 ? 29.224  7.881   -14.435 1.00 20.19  ? 162 GLU A O   1 
ATOM   1244 C  CB  . GLU A 1 162 ? 27.471  9.403   -16.839 1.00 25.98  ? 162 GLU A CB  1 
ATOM   1245 C  CG  . GLU A 1 162 ? 28.399  9.478   -17.963 1.00 36.74  ? 162 GLU A CG  1 
ATOM   1246 C  CD  . GLU A 1 162 ? 27.830  9.539   -19.369 1.00 39.75  ? 162 GLU A CD  1 
ATOM   1247 O  OE1 . GLU A 1 162 ? 26.604  9.657   -19.637 1.00 41.39  ? 162 GLU A OE1 1 
ATOM   1248 O  OE2 . GLU A 1 162 ? 28.700  9.467   -20.265 1.00 35.04  ? 162 GLU A OE2 1 
ATOM   1249 N  N   . GLY A 1 163 ? 27.012  7.581   -14.629 1.00 18.46  ? 163 GLY A N   1 
ATOM   1250 C  CA  . GLY A 1 163 ? 27.045  6.203   -14.111 1.00 17.70  ? 163 GLY A CA  1 
ATOM   1251 C  C   . GLY A 1 163 ? 26.453  6.078   -12.720 1.00 18.18  ? 163 GLY A C   1 
ATOM   1252 O  O   . GLY A 1 163 ? 26.084  4.968   -12.313 1.00 18.08  ? 163 GLY A O   1 
ATOM   1253 N  N   . LEU A 1 164 ? 26.330  7.175   -11.968 1.00 17.17  ? 164 LEU A N   1 
ATOM   1254 C  CA  . LEU A 1 164 ? 25.785  7.085   -10.605 1.00 16.41  ? 164 LEU A CA  1 
ATOM   1255 C  C   . LEU A 1 164 ? 24.647  8.061   -10.298 1.00 15.93  ? 164 LEU A C   1 
ATOM   1256 O  O   . LEU A 1 164 ? 24.377  8.395   -9.147  1.00 16.42  ? 164 LEU A O   1 
ATOM   1257 C  CB  . LEU A 1 164 ? 26.906  7.254   -9.573  1.00 17.86  ? 164 LEU A CB  1 
ATOM   1258 C  CG  . LEU A 1 164 ? 28.029  6.219   -9.649  1.00 16.89  ? 164 LEU A CG  1 
ATOM   1259 C  CD1 . LEU A 1 164 ? 29.175  6.562   -8.686  1.00 19.46  ? 164 LEU A CD1 1 
ATOM   1260 C  CD2 . LEU A 1 164 ? 27.569  4.802   -9.338  1.00 19.74  ? 164 LEU A CD2 1 
ATOM   1261 N  N   . ALA A 1 165 ? 23.927  8.489   -11.317 1.00 15.41  ? 165 ALA A N   1 
ATOM   1262 C  CA  . ALA A 1 165 ? 22.772  9.374   -11.182 1.00 15.80  ? 165 ALA A CA  1 
ATOM   1263 C  C   . ALA A 1 165 ? 21.745  8.754   -10.240 1.00 15.40  ? 165 ALA A C   1 
ATOM   1264 O  O   . ALA A 1 165 ? 21.054  9.475   -9.513  1.00 15.15  ? 165 ALA A O   1 
ATOM   1265 C  CB  . ALA A 1 165 ? 22.194  9.712   -12.548 1.00 16.64  ? 165 ALA A CB  1 
ATOM   1266 N  N   . PHE A 1 166 ? 21.601  7.432   -10.243 1.00 14.83  ? 166 PHE A N   1 
ATOM   1267 C  CA  . PHE A 1 166 ? 20.631  6.799   -9.355  1.00 15.89  ? 166 PHE A CA  1 
ATOM   1268 C  C   . PHE A 1 166 ? 20.733  7.224   -7.892  1.00 14.07  ? 166 PHE A C   1 
ATOM   1269 O  O   . PHE A 1 166 ? 19.737  7.241   -7.158  1.00 15.78  ? 166 PHE A O   1 
ATOM   1270 C  CB  . PHE A 1 166 ? 20.818  5.270   -9.459  1.00 16.24  ? 166 PHE A CB  1 
ATOM   1271 C  CG  . PHE A 1 166 ? 19.934  4.524   -8.469  1.00 16.01  ? 166 PHE A CG  1 
ATOM   1272 C  CD1 . PHE A 1 166 ? 18.568  4.395   -8.648  1.00 16.01  ? 166 PHE A CD1 1 
ATOM   1273 C  CD2 . PHE A 1 166 ? 20.514  3.970   -7.349  1.00 16.63  ? 166 PHE A CD2 1 
ATOM   1274 C  CE1 . PHE A 1 166 ? 17.775  3.727   -7.726  1.00 15.14  ? 166 PHE A CE1 1 
ATOM   1275 C  CE2 . PHE A 1 166 ? 19.721  3.306   -6.422  1.00 18.63  ? 166 PHE A CE2 1 
ATOM   1276 C  CZ  . PHE A 1 166 ? 18.355  3.190   -6.587  1.00 16.53  ? 166 PHE A CZ  1 
ATOM   1277 N  N   . PHE A 1 167 ? 21.943  7.544   -7.462  1.00 15.41  ? 167 PHE A N   1 
ATOM   1278 C  CA  . PHE A 1 167 ? 22.210  7.815   -6.051  1.00 16.77  ? 167 PHE A CA  1 
ATOM   1279 C  C   . PHE A 1 167 ? 21.979  9.277   -5.674  1.00 16.63  ? 167 PHE A C   1 
ATOM   1280 O  O   . PHE A 1 167 ? 22.192  9.604   -4.488  1.00 19.90  ? 167 PHE A O   1 
ATOM   1281 C  CB  . PHE A 1 167 ? 23.639  7.353   -5.702  1.00 18.41  ? 167 PHE A CB  1 
ATOM   1282 C  CG  . PHE A 1 167 ? 23.779  5.842   -5.807  1.00 19.27  ? 167 PHE A CG  1 
ATOM   1283 C  CD1 . PHE A 1 167 ? 23.320  5.038   -4.779  1.00 22.20  ? 167 PHE A CD1 1 
ATOM   1284 C  CD2 . PHE A 1 167 ? 24.368  5.246   -6.898  1.00 24.58  ? 167 PHE A CD2 1 
ATOM   1285 C  CE1 . PHE A 1 167 ? 23.448  3.651   -4.820  1.00 24.32  ? 167 PHE A CE1 1 
ATOM   1286 C  CE2 . PHE A 1 167 ? 24.470  3.872   -6.983  1.00 28.25  ? 167 PHE A CE2 1 
ATOM   1287 C  CZ  . PHE A 1 167 ? 24.011  3.073   -5.951  1.00 29.63  ? 167 PHE A CZ  1 
ATOM   1288 N  N   . THR A 1 168 ? 21.563  10.088  -6.647  1.00 15.30  ? 168 THR A N   1 
ATOM   1289 C  CA  . THR A 1 168 ? 21.204  11.481  -6.395  1.00 16.02  ? 168 THR A CA  1 
ATOM   1290 C  C   . THR A 1 168 ? 19.735  11.711  -6.759  1.00 15.89  ? 168 THR A C   1 
ATOM   1291 O  O   . THR A 1 168 ? 19.330  11.453  -7.863  1.00 14.80  ? 168 THR A O   1 
ATOM   1292 C  CB  . THR A 1 168 ? 22.119  12.452  -7.161  1.00 16.10  ? 168 THR A CB  1 
ATOM   1293 O  OG1 . THR A 1 168 ? 23.474  12.357  -6.655  1.00 18.02  ? 168 THR A OG1 1 
ATOM   1294 C  CG2 . THR A 1 168 ? 21.626  13.897  -6.997  1.00 18.54  ? 168 THR A CG2 1 
ATOM   1295 N  N   . PHE A 1 169 ? 18.983  12.219  -5.800  1.00 17.15  ? 169 PHE A N   1 
ATOM   1296 C  CA  . PHE A 1 169 ? 17.594  12.619  -5.954  1.00 16.21  ? 169 PHE A CA  1 
ATOM   1297 C  C   . PHE A 1 169 ? 17.608  14.136  -6.114  1.00 14.61  ? 169 PHE A C   1 
ATOM   1298 O  O   . PHE A 1 169 ? 17.603  14.855  -5.130  1.00 16.82  ? 169 PHE A O   1 
ATOM   1299 C  CB  . PHE A 1 169 ? 16.737  12.232  -4.745  1.00 17.59  ? 169 PHE A CB  1 
ATOM   1300 C  CG  . PHE A 1 169 ? 16.496  10.742  -4.586  1.00 16.82  ? 169 PHE A CG  1 
ATOM   1301 C  CD1 . PHE A 1 169 ? 17.394  9.907   -3.969  1.00 21.18  ? 169 PHE A CD1 1 
ATOM   1302 C  CD2 . PHE A 1 169 ? 15.318  10.192  -5.041  1.00 15.57  ? 169 PHE A CD2 1 
ATOM   1303 C  CE1 . PHE A 1 169 ? 17.154  8.555   -3.811  1.00 22.59  ? 169 PHE A CE1 1 
ATOM   1304 C  CE2 . PHE A 1 169 ? 15.084  8.848   -4.933  1.00 16.98  ? 169 PHE A CE2 1 
ATOM   1305 C  CZ  . PHE A 1 169 ? 15.984  8.019   -4.295  1.00 19.16  ? 169 PHE A CZ  1 
ATOM   1306 N  N   . PRO A 1 170 ? 17.708  14.683  -7.315  1.00 15.50  ? 170 PRO A N   1 
ATOM   1307 C  CA  . PRO A 1 170 ? 17.962  16.120  -7.425  1.00 15.99  ? 170 PRO A CA  1 
ATOM   1308 C  C   . PRO A 1 170 ? 16.767  16.953  -6.994  1.00 16.21  ? 170 PRO A C   1 
ATOM   1309 O  O   . PRO A 1 170 ? 16.939  18.157  -6.762  1.00 20.03  ? 170 PRO A O   1 
ATOM   1310 C  CB  . PRO A 1 170 ? 18.176  16.313  -8.928  1.00 14.59  ? 170 PRO A CB  1 
ATOM   1311 C  CG  . PRO A 1 170 ? 17.397  15.191  -9.552  1.00 15.06  ? 170 PRO A CG  1 
ATOM   1312 C  CD  . PRO A 1 170 ? 17.609  14.023  -8.627  1.00 16.18  ? 170 PRO A CD  1 
ATOM   1313 N  N   . ASN A 1 171 ? 15.570  16.372  -6.886  1.00 16.68  ? 171 ASN A N   1 
ATOM   1314 C  CA  . ASN A 1 171 ? 14.416  17.212  -6.555  1.00 19.49  ? 171 ASN A CA  1 
ATOM   1315 C  C   . ASN A 1 171 ? 14.004  17.166  -5.102  1.00 18.41  ? 171 ASN A C   1 
ATOM   1316 O  O   . ASN A 1 171 ? 12.913  17.621  -4.773  1.00 22.26  ? 171 ASN A O   1 
ATOM   1317 C  CB  . ASN A 1 171 ? 13.250  16.820  -7.471  1.00 19.79  ? 171 ASN A CB  1 
ATOM   1318 C  CG  . ASN A 1 171 ? 13.554  16.962  -8.953  1.00 17.59  ? 171 ASN A CG  1 
ATOM   1319 O  OD1 . ASN A 1 171 ? 13.176  16.132  -9.841  1.00 22.87  ? 171 ASN A OD1 1 
ATOM   1320 N  ND2 . ASN A 1 171 ? 14.253  17.990  -9.348  1.00 18.37  ? 171 ASN A ND2 1 
ATOM   1321 N  N   . ILE A 1 172 ? 14.897  16.616  -4.308  1.00 18.98  ? 172 ILE A N   1 
ATOM   1322 C  CA  . ILE A 1 172 ? 14.839  16.619  -2.852  1.00 20.62  ? 172 ILE A CA  1 
ATOM   1323 C  C   . ILE A 1 172 ? 15.999  17.480  -2.342  1.00 21.43  ? 172 ILE A C   1 
ATOM   1324 O  O   . ILE A 1 172 ? 17.176  17.098  -2.497  1.00 26.05  ? 172 ILE A O   1 
ATOM   1325 C  CB  . ILE A 1 172 ? 14.859  15.200  -2.296  1.00 19.58  ? 172 ILE A CB  1 
ATOM   1326 C  CG1 . ILE A 1 172 ? 13.650  14.378  -2.754  1.00 18.39  ? 172 ILE A CG1 1 
ATOM   1327 C  CG2 . ILE A 1 172 ? 15.002  15.249  -0.758  1.00 24.68  ? 172 ILE A CG2 1 
ATOM   1328 C  CD1 . ILE A 1 172 ? 13.650  12.937  -2.315  1.00 19.80  ? 172 ILE A CD1 1 
ATOM   1329 N  N   . ALA A 1 173 ? 15.665  18.635  -1.754  1.00 23.55  ? 173 ALA A N   1 
ATOM   1330 C  CA  . ALA A 1 173 ? 16.764  19.518  -1.283  1.00 26.52  ? 173 ALA A CA  1 
ATOM   1331 C  C   . ALA A 1 173 ? 17.309  19.030  0.051   1.00 31.18  ? 173 ALA A C   1 
ATOM   1332 O  O   . ALA A 1 173 ? 18.489  19.236  0.348   1.00 32.08  ? 173 ALA A O   1 
ATOM   1333 C  CB  . ALA A 1 173 ? 16.351  20.955  -1.123  1.00 35.26  ? 173 ALA A CB  1 
ATOM   1334 N  N   . SER A 1 174 ? 16.431  18.400  0.829   1.00 32.81  ? 174 SER A N   1 
ATOM   1335 C  CA  . SER A 1 174 ? 16.789  17.814  2.101   1.00 34.79  ? 174 SER A CA  1 
ATOM   1336 C  C   . SER A 1 174 ? 16.211  16.424  2.336   1.00 30.29  ? 174 SER A C   1 
ATOM   1337 O  O   . SER A 1 174 ? 14.985  16.303  2.486   1.00 32.00  ? 174 SER A O   1 
ATOM   1338 C  CB  . SER A 1 174 ? 16.258  18.697  3.243   1.00 37.91  ? 174 SER A CB  1 
ATOM   1339 O  OG  . SER A 1 174 ? 16.762  18.127  4.436   1.00 38.56  ? 174 SER A OG  1 
ATOM   1340 N  N   . ALA A 1 175 ? 17.066  15.395  2.391   1.00 32.60  ? 175 ALA A N   1 
ATOM   1341 C  CA  . ALA A 1 175 ? 16.548  14.037  2.574   1.00 32.22  ? 175 ALA A CA  1 
ATOM   1342 C  C   . ALA A 1 175 ? 15.859  13.885  3.915   1.00 32.82  ? 175 ALA A C   1 
ATOM   1343 O  O   . ALA A 1 175 ? 14.921  13.149  4.130   1.00 31.67  ? 175 ALA A O   1 
ATOM   1344 C  CB  . ALA A 1 175 ? 17.653  12.991  2.446   1.00 30.17  ? 175 ALA A CB  1 
ATOM   1345 N  N   . THR A 1 176 ? 16.362  14.602  4.906   1.00 35.57  ? 176 THR A N   1 
ATOM   1346 C  CA  . THR A 1 176 ? 15.853  14.428  6.266   1.00 40.29  ? 176 THR A CA  1 
ATOM   1347 C  C   . THR A 1 176 ? 14.424  14.990  6.302   1.00 36.66  ? 176 THR A C   1 
ATOM   1348 O  O   . THR A 1 176 ? 13.500  14.307  6.778   1.00 39.06  ? 176 THR A O   1 
ATOM   1349 C  CB  . THR A 1 176 ? 16.704  14.989  7.403   1.00 44.76  ? 176 THR A CB  1 
ATOM   1350 O  OG1 . THR A 1 176 ? 17.692  16.005  7.176   1.00 53.62  ? 176 THR A OG1 1 
ATOM   1351 C  CG2 . THR A 1 176 ? 17.561  13.796  7.895   1.00 56.17  ? 176 THR A CG2 1 
ATOM   1352 N  N   . LYS A 1 177 ? 14.190  16.188  5.807   1.00 35.50  ? 177 LYS A N   1 
ATOM   1353 C  CA  . LYS A 1 177 ? 12.903  16.861  5.739   1.00 32.82  ? 177 LYS A CA  1 
ATOM   1354 C  C   . LYS A 1 177 ? 11.970  15.974  4.902   1.00 29.12  ? 177 LYS A C   1 
ATOM   1355 O  O   . LYS A 1 177 ? 10.829  15.755  5.314   1.00 30.01  ? 177 LYS A O   1 
ATOM   1356 C  CB  . LYS A 1 177 ? 12.962  18.283  5.210   1.00 40.70  ? 177 LYS A CB  1 
ATOM   1357 C  CG  . LYS A 1 177 ? 13.645  19.378  6.007   1.00 56.25  ? 177 LYS A CG  1 
ATOM   1358 C  CD  . LYS A 1 177 ? 14.303  19.002  7.301   1.00 64.24  ? 177 LYS A CD  1 
ATOM   1359 C  CE  . LYS A 1 177 ? 15.743  19.490  7.422   1.00 68.61  ? 177 LYS A CE  1 
ATOM   1360 N  NZ  . LYS A 1 177 ? 16.222  19.624  8.823   1.00 85.34  ? 177 LYS A NZ  1 
ATOM   1361 N  N   . PHE A 1 178 ? 12.505  15.494  3.757   1.00 28.93  ? 178 PHE A N   1 
ATOM   1362 C  CA  . PHE A 1 178 ? 11.641  14.704  2.890   1.00 25.54  ? 178 PHE A CA  1 
ATOM   1363 C  C   . PHE A 1 178 ? 11.193  13.417  3.593   1.00 25.68  ? 178 PHE A C   1 
ATOM   1364 O  O   . PHE A 1 178 ? 9.999   13.085  3.493   1.00 23.99  ? 178 PHE A O   1 
ATOM   1365 C  CB  . PHE A 1 178 ? 12.278  14.375  1.520   1.00 25.58  ? 178 PHE A CB  1 
ATOM   1366 C  CG  . PHE A 1 178 ? 11.220  13.730  0.620   1.00 22.69  ? 178 PHE A CG  1 
ATOM   1367 C  CD1 . PHE A 1 178 ? 10.279  14.450  -0.077  1.00 26.15  ? 178 PHE A CD1 1 
ATOM   1368 C  CD2 . PHE A 1 178 ? 11.199  12.341  0.500   1.00 27.13  ? 178 PHE A CD2 1 
ATOM   1369 C  CE1 . PHE A 1 178 ? 9.322   13.791  -0.838  1.00 22.49  ? 178 PHE A CE1 1 
ATOM   1370 C  CE2 . PHE A 1 178 ? 10.233  11.686  -0.220  1.00 23.99  ? 178 PHE A CE2 1 
ATOM   1371 C  CZ  . PHE A 1 178 ? 9.277   12.416  -0.906  1.00 22.72  ? 178 PHE A CZ  1 
ATOM   1372 N  N   . LYS A 1 179 ? 12.112  12.698  4.227   1.00 25.73  ? 179 LYS A N   1 
ATOM   1373 C  CA  . LYS A 1 179 ? 11.687  11.476  4.916   1.00 28.96  ? 179 LYS A CA  1 
ATOM   1374 C  C   . LYS A 1 179 ? 10.623  11.764  5.958   1.00 27.90  ? 179 LYS A C   1 
ATOM   1375 O  O   . LYS A 1 179 ? 9.691   11.024  6.247   1.00 29.36  ? 179 LYS A O   1 
ATOM   1376 C  CB  . LYS A 1 179 ? 12.912  10.821  5.566   1.00 32.13  ? 179 LYS A CB  1 
ATOM   1377 C  CG  . LYS A 1 179 ? 13.974  10.375  4.577   1.00 38.34  ? 179 LYS A CG  1 
ATOM   1378 C  CD  . LYS A 1 179 ? 15.295  10.034  5.283   1.00 42.19  ? 179 LYS A CD  1 
ATOM   1379 C  CE  . LYS A 1 179 ? 15.012  9.046   6.396   1.00 52.73  ? 179 LYS A CE  1 
ATOM   1380 N  NZ  . LYS A 1 179 ? 14.364  7.805   5.882   1.00 74.73  ? 179 LYS A NZ  1 
ATOM   1381 N  N   . GLN A 1 180 ? 10.743  12.918  6.598   1.00 28.39  ? 180 GLN A N   1 
ATOM   1382 C  CA  . GLN A 1 180 ? 9.781   13.275  7.636   1.00 31.22  ? 180 GLN A CA  1 
ATOM   1383 C  C   . GLN A 1 180 ? 8.433   13.476  6.969   1.00 28.49  ? 180 GLN A C   1 
ATOM   1384 O  O   . GLN A 1 180 ? 7.425   13.026  7.481   1.00 29.96  ? 180 GLN A O   1 
ATOM   1385 C  CB  . GLN A 1 180 ? 10.193  14.537  8.399   1.00 43.24  ? 180 GLN A CB  1 
ATOM   1386 C  CG  . GLN A 1 180 ? 11.568  14.449  9.049   1.00 55.44  ? 180 GLN A CG  1 
ATOM   1387 C  CD  . GLN A 1 180 ? 11.983  15.643  9.885   1.00 65.77  ? 180 GLN A CD  1 
ATOM   1388 O  OE1 . GLN A 1 180 ? 11.819  16.804  9.476   1.00 65.81  ? 180 GLN A OE1 1 
ATOM   1389 N  NE2 . GLN A 1 180 ? 12.542  15.389  11.082  1.00 78.84  ? 180 GLN A NE2 1 
ATOM   1390 N  N   . LEU A 1 181 ? 8.478   14.146  5.829   1.00 27.14  ? 181 LEU A N   1 
ATOM   1391 C  CA  . LEU A 1 181 ? 7.255   14.452  5.107   1.00 25.39  ? 181 LEU A CA  1 
ATOM   1392 C  C   . LEU A 1 181 ? 6.633   13.150  4.622   1.00 23.20  ? 181 LEU A C   1 
ATOM   1393 O  O   . LEU A 1 181 ? 5.430   12.944  4.788   1.00 27.54  ? 181 LEU A O   1 
ATOM   1394 C  CB  . LEU A 1 181 ? 7.527   15.404  3.940   1.00 27.09  ? 181 LEU A CB  1 
ATOM   1395 C  CG  . LEU A 1 181 ? 6.393   15.542  2.924   1.00 26.92  ? 181 LEU A CG  1 
ATOM   1396 C  CD1 . LEU A 1 181 ? 5.168   16.138  3.590   1.00 29.05  ? 181 LEU A CD1 1 
ATOM   1397 C  CD2 . LEU A 1 181 ? 6.839   16.376  1.735   1.00 30.62  ? 181 LEU A CD2 1 
ATOM   1398 N  N   . TYR A 1 182 ? 7.480   12.281  4.042   1.00 23.52  ? 182 TYR A N   1 
ATOM   1399 C  CA  . TYR A 1 182 ? 6.907   11.048  3.522   1.00 23.52  ? 182 TYR A CA  1 
ATOM   1400 C  C   . TYR A 1 182 ? 6.288   10.195  4.616   1.00 27.33  ? 182 TYR A C   1 
ATOM   1401 O  O   . TYR A 1 182 ? 5.251   9.533   4.491   1.00 25.51  ? 182 TYR A O   1 
ATOM   1402 C  CB  . TYR A 1 182 ? 7.997   10.238  2.840   1.00 25.98  ? 182 TYR A CB  1 
ATOM   1403 C  CG  . TYR A 1 182 ? 7.573   9.188   1.855   1.00 25.79  ? 182 TYR A CG  1 
ATOM   1404 C  CD1 . TYR A 1 182 ? 7.593   7.832   2.199   1.00 30.12  ? 182 TYR A CD1 1 
ATOM   1405 C  CD2 . TYR A 1 182 ? 7.170   9.500   0.567   1.00 26.51  ? 182 TYR A CD2 1 
ATOM   1406 C  CE1 . TYR A 1 182 ? 7.208   6.881   1.281   1.00 30.07  ? 182 TYR A CE1 1 
ATOM   1407 C  CE2 . TYR A 1 182 ? 6.785   8.535   -0.347  1.00 20.14  ? 182 TYR A CE2 1 
ATOM   1408 C  CZ  . TYR A 1 182 ? 6.807   7.217   0.011   1.00 26.60  ? 182 TYR A CZ  1 
ATOM   1409 O  OH  . TYR A 1 182 ? 6.440   6.217   -0.851  1.00 30.14  ? 182 TYR A OH  1 
ATOM   1410 N  N   . ARG A 1 183 ? 7.020   10.199  5.748   1.00 25.90  ? 183 ARG A N   1 
ATOM   1411 C  CA  . ARG A 1 183 ? 6.437   9.392   6.828   1.00 25.06  ? 183 ARG A CA  1 
ATOM   1412 C  C   . ARG A 1 183 ? 5.087   9.946   7.275   1.00 27.71  ? 183 ARG A C   1 
ATOM   1413 O  O   . ARG A 1 183 ? 4.129   9.239   7.594   1.00 33.13  ? 183 ARG A O   1 
ATOM   1414 C  CB  . ARG A 1 183 ? 7.469   9.305   7.946   1.00 24.85  ? 183 ARG A CB  1 
ATOM   1415 C  CG  . ARG A 1 183 ? 8.712   8.497   7.532   1.00 28.29  ? 183 ARG A CG  1 
ATOM   1416 C  CD  . ARG A 1 183 ? 9.541   8.430   8.798   1.00 33.14  ? 183 ARG A CD  1 
ATOM   1417 N  NE  . ARG A 1 183 ? 10.769  7.690   8.666   1.00 32.98  ? 183 ARG A NE  1 
ATOM   1418 C  CZ  . ARG A 1 183 ? 12.013  8.135   8.723   1.00 35.11  ? 183 ARG A CZ  1 
ATOM   1419 N  NH1 . ARG A 1 183 ? 12.335  9.419   8.918   1.00 46.14  ? 183 ARG A NH1 1 
ATOM   1420 N  NH2 . ARG A 1 183 ? 12.999  7.252   8.577   1.00 49.61  ? 183 ARG A NH2 1 
ATOM   1421 N  N   . SER A 1 184 ? 4.976   11.265  7.291   1.00 29.89  ? 184 SER A N   1 
ATOM   1422 C  CA  . SER A 1 184 ? 3.747   11.942  7.696   1.00 28.46  ? 184 SER A CA  1 
ATOM   1423 C  C   . SER A 1 184 ? 2.580   11.530  6.822   1.00 26.87  ? 184 SER A C   1 
ATOM   1424 O  O   . SER A 1 184 ? 1.459   11.284  7.243   1.00 28.80  ? 184 SER A O   1 
ATOM   1425 C  CB  . SER A 1 184 ? 3.945   13.458  7.566   1.00 36.77  ? 184 SER A CB  1 
ATOM   1426 O  OG  . SER A 1 184 ? 2.762   14.183  7.837   1.00 41.89  ? 184 SER A OG  1 
ATOM   1427 N  N   . ARG A 1 185 ? 2.931   11.500  5.532   1.00 27.46  ? 185 ARG A N   1 
ATOM   1428 C  CA  . ARG A 1 185 ? 1.944   11.167  4.533   1.00 24.08  ? 185 ARG A CA  1 
ATOM   1429 C  C   . ARG A 1 185 ? 1.540   9.698   4.671   1.00 24.32  ? 185 ARG A C   1 
ATOM   1430 O  O   . ARG A 1 185 ? 0.341   9.389   4.597   1.00 24.88  ? 185 ARG A O   1 
ATOM   1431 C  CB  . ARG A 1 185 ? 2.523   11.474  3.153   1.00 22.44  ? 185 ARG A CB  1 
ATOM   1432 C  CG  . ARG A 1 185 ? 2.671   12.945  2.817   1.00 22.43  ? 185 ARG A CG  1 
ATOM   1433 C  CD  . ARG A 1 185 ? 1.384   13.766  2.841   1.00 24.41  ? 185 ARG A CD  1 
ATOM   1434 N  NE  . ARG A 1 185 ? 1.556   15.070  2.187   1.00 22.04  ? 185 ARG A NE  1 
ATOM   1435 C  CZ  . ARG A 1 185 ? 1.420   15.273  0.880   1.00 21.78  ? 185 ARG A CZ  1 
ATOM   1436 N  NH1 . ARG A 1 185 ? 1.100   14.282  0.044   1.00 24.20  ? 185 ARG A NH1 1 
ATOM   1437 N  NH2 . ARG A 1 185 ? 1.592   16.471  0.347   1.00 24.13  ? 185 ARG A NH2 1 
ATOM   1438 N  N   . MET A 1 186 ? 2.516   8.810   4.870   1.00 23.76  ? 186 MET A N   1 
ATOM   1439 C  CA  . MET A 1 186 ? 2.210   7.410   5.115   1.00 24.90  ? 186 MET A CA  1 
ATOM   1440 C  C   . MET A 1 186 ? 1.262   7.291   6.291   1.00 25.01  ? 186 MET A C   1 
ATOM   1441 O  O   . MET A 1 186 ? 0.280   6.557   6.315   1.00 26.21  ? 186 MET A O   1 
ATOM   1442 C  CB  . MET A 1 186 ? 3.467   6.605   5.469   1.00 31.63  ? 186 MET A CB  1 
ATOM   1443 C  CG  . MET A 1 186 ? 3.829   5.565   4.427   1.00 41.19  ? 186 MET A CG  1 
ATOM   1444 S  SD  . MET A 1 186 ? 5.490   4.929   4.520   1.00 38.89  ? 186 MET A SD  1 
ATOM   1445 C  CE  . MET A 1 186 ? 6.420   6.147   5.390   1.00 60.72  ? 186 MET A CE  1 
ATOM   1446 N  N   . ASN A 1 187 ? 1.597   8.059   7.330   1.00 27.40  ? 187 ASN A N   1 
ATOM   1447 C  CA  . ASN A 1 187 ? 0.782   7.977   8.530   1.00 30.91  ? 187 ASN A CA  1 
ATOM   1448 C  C   . ASN A 1 187 ? -0.607  8.538   8.319   1.00 28.94  ? 187 ASN A C   1 
ATOM   1449 O  O   . ASN A 1 187 ? -1.466  8.211   9.158   1.00 36.45  ? 187 ASN A O   1 
ATOM   1450 C  CB  . ASN A 1 187 ? 1.461   8.721   9.690   1.00 32.61  ? 187 ASN A CB  1 
ATOM   1451 C  CG  . ASN A 1 187 ? 2.714   7.950   10.091  1.00 31.55  ? 187 ASN A CG  1 
ATOM   1452 O  OD1 . ASN A 1 187 ? 2.832   6.780   9.768   1.00 36.04  ? 187 ASN A OD1 1 
ATOM   1453 N  ND2 . ASN A 1 187 ? 3.566   8.679   10.784  1.00 36.97  ? 187 ASN A ND2 1 
ATOM   1454 N  N   . SER A 1 188 ? -0.864  9.337   7.293   1.00 31.10  ? 188 SER A N   1 
ATOM   1455 C  CA  . SER A 1 188 ? -2.203  9.894   7.099   1.00 38.07  ? 188 SER A CA  1 
ATOM   1456 C  C   . SER A 1 188 ? -3.078  8.932   6.314   1.00 35.27  ? 188 SER A C   1 
ATOM   1457 O  O   . SER A 1 188 ? -4.268  9.169   6.228   1.00 41.36  ? 188 SER A O   1 
ATOM   1458 C  CB  . SER A 1 188 ? -2.228  11.227  6.337   1.00 37.49  ? 188 SER A CB  1 
ATOM   1459 O  OG  . SER A 1 188 ? -2.023  10.907  4.968   1.00 39.60  ? 188 SER A OG  1 
ATOM   1460 N  N   . LEU A 1 189 ? -2.465  7.885   5.759   1.00 31.86  ? 189 LEU A N   1 
ATOM   1461 C  CA  . LEU A 1 189 ? -3.297  6.876   5.137   1.00 31.28  ? 189 LEU A CA  1 
ATOM   1462 C  C   . LEU A 1 189 ? -4.237  6.207   6.151   1.00 30.71  ? 189 LEU A C   1 
ATOM   1463 O  O   . LEU A 1 189 ? -3.915  5.769   7.236   1.00 39.35  ? 189 LEU A O   1 
ATOM   1464 C  CB  . LEU A 1 189 ? -2.493  5.763   4.468   1.00 29.84  ? 189 LEU A CB  1 
ATOM   1465 C  CG  . LEU A 1 189 ? -1.716  6.206   3.237   1.00 32.40  ? 189 LEU A CG  1 
ATOM   1466 C  CD1 . LEU A 1 189 ? -0.664  5.160   2.918   1.00 29.48  ? 189 LEU A CD1 1 
ATOM   1467 C  CD2 . LEU A 1 189 ? -2.660  6.452   2.074   1.00 42.06  ? 189 LEU A CD2 1 
ATOM   1468 N  N   . GLU A 1 190 ? -5.491  6.128   5.720   1.00 36.01  ? 190 GLU A N   1 
ATOM   1469 C  CA  . GLU A 1 190 ? -6.535  5.457   6.480   1.00 38.59  ? 190 GLU A CA  1 
ATOM   1470 C  C   . GLU A 1 190 ? -6.644  4.028   5.989   1.00 41.69  ? 190 GLU A C   1 
ATOM   1471 O  O   . GLU A 1 190 ? -6.814  3.815   4.789   1.00 48.89  ? 190 GLU A O   1 
ATOM   1472 C  CB  . GLU A 1 190 ? -7.870  6.197   6.343   1.00 46.50  ? 190 GLU A CB  1 
ATOM   1473 C  CG  . GLU A 1 190 ? -8.113  7.157   7.486   1.00 51.95  ? 190 GLU A CG  1 
ATOM   1474 C  CD  . GLU A 1 190 ? -9.005  8.330   7.153   1.00 59.54  ? 190 GLU A CD  1 
ATOM   1475 O  OE1 . GLU A 1 190 ? -10.080 8.143   6.535   1.00 68.20  ? 190 GLU A OE1 1 
ATOM   1476 O  OE2 . GLU A 1 190 ? -8.589  9.453   7.533   1.00 65.14  ? 190 GLU A OE2 1 
ATOM   1477 N  N   . MET A 1 191 ? -6.522  3.086   6.903   1.00 36.05  ? 191 MET A N   1 
ATOM   1478 C  CA  . MET A 1 191 ? -6.644  1.686   6.539   1.00 36.49  ? 191 MET A CA  1 
ATOM   1479 C  C   . MET A 1 191 ? -7.265  0.961   7.738   1.00 36.18  ? 191 MET A C   1 
ATOM   1480 O  O   . MET A 1 191 ? -7.073  1.392   8.866   1.00 36.30  ? 191 MET A O   1 
ATOM   1481 C  CB  . MET A 1 191 ? -5.336  0.987   6.141   1.00 39.20  ? 191 MET A CB  1 
ATOM   1482 C  CG  . MET A 1 191 ? -4.081  1.575   6.728   1.00 42.71  ? 191 MET A CG  1 
ATOM   1483 S  SD  . MET A 1 191 ? -2.557  0.826   6.121   1.00 33.34  ? 191 MET A SD  1 
ATOM   1484 C  CE  . MET A 1 191 ? -2.300  1.793   4.635   1.00 49.07  ? 191 MET A CE  1 
ATOM   1485 N  N   . THR A 1 192 ? -7.979  -0.114  7.446   1.00 29.65  ? 192 THR A N   1 
ATOM   1486 C  CA  . THR A 1 192 ? -8.423  -0.975  8.534   1.00 32.68  ? 192 THR A CA  1 
ATOM   1487 C  C   . THR A 1 192 ? -7.228  -1.721  9.105   1.00 33.21  ? 192 THR A C   1 
ATOM   1488 O  O   . THR A 1 192 ? -6.152  -1.759  8.504   1.00 27.95  ? 192 THR A O   1 
ATOM   1489 C  CB  . THR A 1 192 ? -9.485  -1.951  8.007   1.00 34.58  ? 192 THR A CB  1 
ATOM   1490 O  OG1 . THR A 1 192 ? -8.867  -2.736  6.986   1.00 35.01  ? 192 THR A OG1 1 
ATOM   1491 C  CG2 . THR A 1 192 ? -10.607 -1.188  7.337   1.00 49.80  ? 192 THR A CG2 1 
ATOM   1492 N  N   . PRO A 1 193 ? -7.426  -2.302  10.276  1.00 33.02  ? 193 PRO A N   1 
ATOM   1493 C  CA  . PRO A 1 193 ? -6.368  -3.153  10.847  1.00 29.16  ? 193 PRO A CA  1 
ATOM   1494 C  C   . PRO A 1 193 ? -5.985  -4.306  9.925   1.00 29.73  ? 193 PRO A C   1 
ATOM   1495 O  O   . PRO A 1 193 ? -4.805  -4.649  9.815   1.00 28.33  ? 193 PRO A O   1 
ATOM   1496 C  CB  . PRO A 1 193 ? -6.997  -3.642  12.140  1.00 29.96  ? 193 PRO A CB  1 
ATOM   1497 C  CG  . PRO A 1 193 ? -7.958  -2.557  12.486  1.00 29.57  ? 193 PRO A CG  1 
ATOM   1498 C  CD  . PRO A 1 193 ? -8.603  -2.201  11.167  1.00 30.41  ? 193 PRO A CD  1 
ATOM   1499 N  N   . ALA A 1 194 ? -6.900  -4.951  9.213   1.00 29.23  ? 194 ALA A N   1 
ATOM   1500 C  CA  . ALA A 1 194 ? -6.473  -6.007  8.285   1.00 27.52  ? 194 ALA A CA  1 
ATOM   1501 C  C   . ALA A 1 194 ? -5.519  -5.535  7.201   1.00 27.42  ? 194 ALA A C   1 
ATOM   1502 O  O   . ALA A 1 194 ? -4.505  -6.184  6.931   1.00 27.95  ? 194 ALA A O   1 
ATOM   1503 C  CB  . ALA A 1 194 ? -7.717  -6.603  7.642   1.00 29.37  ? 194 ALA A CB  1 
ATOM   1504 N  N   . VAL A 1 195 ? -5.763  -4.439  6.496   1.00 31.25  ? 195 VAL A N   1 
ATOM   1505 C  CA  . VAL A 1 195 ? -4.997  -3.832  5.444   1.00 28.39  ? 195 VAL A CA  1 
ATOM   1506 C  C   . VAL A 1 195 ? -3.654  -3.424  6.024   1.00 26.23  ? 195 VAL A C   1 
ATOM   1507 O  O   . VAL A 1 195 ? -2.620  -3.667  5.434   1.00 28.49  ? 195 VAL A O   1 
ATOM   1508 C  CB  . VAL A 1 195 ? -5.723  -2.612  4.841   1.00 27.91  ? 195 VAL A CB  1 
ATOM   1509 C  CG1 . VAL A 1 195 ? -4.826  -1.779  3.936   1.00 27.19  ? 195 VAL A CG1 1 
ATOM   1510 C  CG2 . VAL A 1 195 ? -6.958  -3.077  4.077   1.00 27.87  ? 195 VAL A CG2 1 
ATOM   1511 N  N   . ARG A 1 196 ? -3.719  -2.828  7.213   1.00 27.95  ? 196 ARG A N   1 
ATOM   1512 C  CA  . ARG A 1 196 ? -2.435  -2.447  7.819   1.00 24.38  ? 196 ARG A CA  1 
ATOM   1513 C  C   . ARG A 1 196 ? -1.570  -3.680  8.024   1.00 23.93  ? 196 ARG A C   1 
ATOM   1514 O  O   . ARG A 1 196 ? -0.371  -3.603  7.747   1.00 23.65  ? 196 ARG A O   1 
ATOM   1515 C  CB  . ARG A 1 196 ? -2.653  -1.661  9.105   1.00 25.96  ? 196 ARG A CB  1 
ATOM   1516 C  CG  . ARG A 1 196 ? -1.355  -1.090  9.677   1.00 35.91  ? 196 ARG A CG  1 
ATOM   1517 C  CD  . ARG A 1 196 ? -1.731  -0.337  10.940  1.00 47.68  ? 196 ARG A CD  1 
ATOM   1518 N  NE  . ARG A 1 196 ? -0.647  0.015   11.834  1.00 52.72  ? 196 ARG A NE  1 
ATOM   1519 C  CZ  . ARG A 1 196 ? -0.272  1.227   12.229  1.00 57.42  ? 196 ARG A CZ  1 
ATOM   1520 N  NH1 . ARG A 1 196 ? -0.849  2.371   11.847  1.00 57.53  ? 196 ARG A NH1 1 
ATOM   1521 N  NH2 . ARG A 1 196 ? 0.763   1.294   13.070  1.00 66.65  ? 196 ARG A NH2 1 
ATOM   1522 N  N   . GLN A 1 197 ? -2.181  -4.785  8.454   1.00 23.82  ? 197 GLN A N   1 
ATOM   1523 C  CA  . GLN A 1 197 ? -1.429  -6.035  8.649   1.00 22.31  ? 197 GLN A CA  1 
ATOM   1524 C  C   . GLN A 1 197 ? -0.815  -6.505  7.330   1.00 21.80  ? 197 GLN A C   1 
ATOM   1525 O  O   . GLN A 1 197 ? 0.336   -6.936  7.200   1.00 22.13  ? 197 GLN A O   1 
ATOM   1526 C  CB  . GLN A 1 197 ? -2.397  -7.069  9.286   1.00 28.46  ? 197 GLN A CB  1 
ATOM   1527 C  CG  . GLN A 1 197 ? -2.914  -6.677  10.657  1.00 41.62  ? 197 GLN A CG  1 
ATOM   1528 C  CD  . GLN A 1 197 ? -4.107  -7.398  11.240  1.00 49.25  ? 197 GLN A CD  1 
ATOM   1529 O  OE1 . GLN A 1 197 ? -4.855  -8.186  10.635  1.00 62.67  ? 197 GLN A OE1 1 
ATOM   1530 N  NE2 . GLN A 1 197 ? -4.406  -7.157  12.538  1.00 68.18  ? 197 GLN A NE2 1 
ATOM   1531 N  N   . ARG A 1 198 ? -1.622  -6.438  6.258   1.00 21.34  ? 198 ARG A N   1 
ATOM   1532 C  CA  . ARG A 1 198 ? -1.152  -6.850  4.933   1.00 22.04  ? 198 ARG A CA  1 
ATOM   1533 C  C   . ARG A 1 198 ? -0.064  -5.945  4.379   1.00 20.39  ? 198 ARG A C   1 
ATOM   1534 O  O   . ARG A 1 198 ? 0.842   -6.452  3.698   1.00 20.80  ? 198 ARG A O   1 
ATOM   1535 C  CB  . ARG A 1 198 ? -2.300  -6.939  3.905   1.00 22.14  ? 198 ARG A CB  1 
ATOM   1536 C  CG  . ARG A 1 198 ? -3.299  -8.018  4.305   1.00 28.47  ? 198 ARG A CG  1 
ATOM   1537 C  CD  . ARG A 1 198 ? -3.997  -8.562  3.059   1.00 31.94  ? 198 ARG A CD  1 
ATOM   1538 N  NE  . ARG A 1 198 ? -4.680  -7.468  2.368   1.00 35.25  ? 198 ARG A NE  1 
ATOM   1539 C  CZ  . ARG A 1 198 ? -5.835  -6.926  2.744   1.00 34.84  ? 198 ARG A CZ  1 
ATOM   1540 N  NH1 . ARG A 1 198 ? -6.480  -7.359  3.812   1.00 39.33  ? 198 ARG A NH1 1 
ATOM   1541 N  NH2 . ARG A 1 198 ? -6.342  -5.929  2.014   1.00 33.77  ? 198 ARG A NH2 1 
ATOM   1542 N  N   . VAL A 1 199 ? -0.171  -4.662  4.683   1.00 21.67  ? 199 VAL A N   1 
ATOM   1543 C  CA  . VAL A 1 199 ? 0.851   -3.694  4.259   1.00 19.66  ? 199 VAL A CA  1 
ATOM   1544 C  C   . VAL A 1 199 ? 2.174   -4.052  4.910   1.00 21.56  ? 199 VAL A C   1 
ATOM   1545 O  O   . VAL A 1 199 ? 3.242   -4.053  4.328   1.00 22.31  ? 199 VAL A O   1 
ATOM   1546 C  CB  . VAL A 1 199 ? 0.460   -2.250  4.625   1.00 21.00  ? 199 VAL A CB  1 
ATOM   1547 C  CG1 . VAL A 1 199 ? 1.643   -1.279  4.521   1.00 20.93  ? 199 VAL A CG1 1 
ATOM   1548 C  CG2 . VAL A 1 199 ? -0.703  -1.815  3.754   1.00 22.20  ? 199 VAL A CG2 1 
ATOM   1549 N  N   . ILE A 1 200 ? 2.086   -4.370  6.199   1.00 22.40  ? 200 ILE A N   1 
ATOM   1550 C  CA  . ILE A 1 200 ? 3.324   -4.675  6.928   1.00 22.29  ? 200 ILE A CA  1 
ATOM   1551 C  C   . ILE A 1 200 ? 3.931   -5.943  6.356   1.00 21.35  ? 200 ILE A C   1 
ATOM   1552 O  O   . ILE A 1 200 ? 5.148   -6.030  6.145   1.00 21.64  ? 200 ILE A O   1 
ATOM   1553 C  CB  . ILE A 1 200 ? 3.032   -4.751  8.448   1.00 23.67  ? 200 ILE A CB  1 
ATOM   1554 C  CG1 . ILE A 1 200 ? 2.660   -3.397  9.060   1.00 32.92  ? 200 ILE A CG1 1 
ATOM   1555 C  CG2 . ILE A 1 200 ? 4.172   -5.455  9.226   1.00 29.56  ? 200 ILE A CG2 1 
ATOM   1556 C  CD1 . ILE A 1 200 ? 3.708   -2.671  9.846   1.00 53.23  ? 200 ILE A CD1 1 
ATOM   1557 N  N   . GLU A 1 201 ? 3.078   -6.945  6.085   1.00 21.45  ? 201 GLU A N   1 
ATOM   1558 C  CA  . GLU A 1 201 ? 3.619   -8.194  5.578   1.00 23.56  ? 201 GLU A CA  1 
ATOM   1559 C  C   . GLU A 1 201 ? 4.216   -7.996  4.191   1.00 22.82  ? 201 GLU A C   1 
ATOM   1560 O  O   . GLU A 1 201 ? 5.205   -8.650  3.842   1.00 24.61  ? 201 GLU A O   1 
ATOM   1561 C  CB  . GLU A 1 201 ? 2.564   -9.306  5.535   1.00 28.73  ? 201 GLU A CB  1 
ATOM   1562 C  CG  . GLU A 1 201 ? 2.174   -9.735  6.943   1.00 34.76  ? 201 GLU A CG  1 
ATOM   1563 C  CD  . GLU A 1 201 ? 3.369   -10.173 7.787   1.00 40.85  ? 201 GLU A CD  1 
ATOM   1564 O  OE1 . GLU A 1 201 ? 4.161   -10.984 7.253   1.00 40.07  ? 201 GLU A OE1 1 
ATOM   1565 O  OE2 . GLU A 1 201 ? 3.518   -9.724  8.959   1.00 50.54  ? 201 GLU A OE2 1 
ATOM   1566 N  N   . GLU A 1 202 ? 3.576   -7.092  3.453   1.00 21.74  ? 202 GLU A N   1 
ATOM   1567 C  CA  . GLU A 1 202 ? 4.074   -6.830  2.084   1.00 20.12  ? 202 GLU A CA  1 
ATOM   1568 C  C   . GLU A 1 202 ? 5.435   -6.145  2.137   1.00 18.44  ? 202 GLU A C   1 
ATOM   1569 O  O   . GLU A 1 202 ? 6.239   -6.420  1.262   1.00 19.97  ? 202 GLU A O   1 
ATOM   1570 C  CB  . GLU A 1 202 ? 3.091   -6.049  1.230   1.00 19.85  ? 202 GLU A CB  1 
ATOM   1571 C  CG  . GLU A 1 202 ? 3.441   -5.987  -0.275  1.00 21.78  ? 202 GLU A CG  1 
ATOM   1572 C  CD  . GLU A 1 202 ? 3.254   -7.312  -0.990  1.00 21.14  ? 202 GLU A CD  1 
ATOM   1573 O  OE1 . GLU A 1 202 ? 2.479   -8.158  -0.497  1.00 21.61  ? 202 GLU A OE1 1 
ATOM   1574 O  OE2 . GLU A 1 202 ? 3.891   -7.538  -2.049  1.00 20.91  ? 202 GLU A OE2 1 
ATOM   1575 N  N   . ALA A 1 203 ? 5.663   -5.302  3.136   1.00 19.27  ? 203 ALA A N   1 
ATOM   1576 C  CA  . ALA A 1 203 ? 7.014   -4.735  3.272   1.00 19.25  ? 203 ALA A CA  1 
ATOM   1577 C  C   . ALA A 1 203 ? 8.005   -5.843  3.552   1.00 19.52  ? 203 ALA A C   1 
ATOM   1578 O  O   . ALA A 1 203 ? 9.113   -5.859  2.988   1.00 19.97  ? 203 ALA A O   1 
ATOM   1579 C  CB  . ALA A 1 203 ? 7.027   -3.647  4.325   1.00 23.47  ? 203 ALA A CB  1 
ATOM   1580 N  N   . LYS A 1 204 ? 7.689   -6.822  4.366   1.00 19.28  ? 204 LYS A N   1 
ATOM   1581 C  CA  . LYS A 1 204 ? 8.615   -7.934  4.548   1.00 20.79  ? 204 LYS A CA  1 
ATOM   1582 C  C   . LYS A 1 204 ? 8.843   -8.713  3.261   1.00 19.30  ? 204 LYS A C   1 
ATOM   1583 O  O   . LYS A 1 204 ? 9.963   -9.099  2.893   1.00 19.38  ? 204 LYS A O   1 
ATOM   1584 C  CB  . LYS A 1 204 ? 8.033   -8.881  5.602   1.00 21.80  ? 204 LYS A CB  1 
ATOM   1585 C  CG  . LYS A 1 204 ? 8.098   -8.266  6.993   1.00 25.52  ? 204 LYS A CG  1 
ATOM   1586 C  CD  . LYS A 1 204 ? 7.547   -9.204  8.054   1.00 35.24  ? 204 LYS A CD  1 
ATOM   1587 C  CE  . LYS A 1 204 ? 8.078   -8.779  9.408   1.00 45.86  ? 204 LYS A CE  1 
ATOM   1588 N  NZ  . LYS A 1 204 ? 7.520   -9.629  10.511  1.00 66.95  ? 204 LYS A NZ  1 
ATOM   1589 N  N   . THR A 1 205 ? 7.740   -8.942  2.547   1.00 19.48  ? 205 THR A N   1 
ATOM   1590 C  CA  . THR A 1 205 ? 7.842   -9.606  1.236   1.00 20.21  ? 205 THR A CA  1 
ATOM   1591 C  C   . THR A 1 205 ? 8.771   -8.858  0.285   1.00 20.02  ? 205 THR A C   1 
ATOM   1592 O  O   . THR A 1 205 ? 9.600   -9.451  -0.431  1.00 20.35  ? 205 THR A O   1 
ATOM   1593 C  CB  . THR A 1 205 ? 6.453   -9.817  0.606   1.00 19.88  ? 205 THR A CB  1 
ATOM   1594 O  OG1 . THR A 1 205 ? 5.712   -10.736 1.425   1.00 24.53  ? 205 THR A OG1 1 
ATOM   1595 C  CG2 . THR A 1 205 ? 6.598   -10.425 -0.793  1.00 26.64  ? 205 THR A CG2 1 
ATOM   1596 N  N   . ALA A 1 206 ? 8.675   -7.539  0.247   1.00 18.83  ? 206 ALA A N   1 
ATOM   1597 C  CA  . ALA A 1 206 ? 9.529   -6.728  -0.606  1.00 18.52  ? 206 ALA A CA  1 
ATOM   1598 C  C   . ALA A 1 206 ? 10.998  -6.973  -0.260  1.00 17.67  ? 206 ALA A C   1 
ATOM   1599 O  O   . ALA A 1 206 ? 11.872  -7.173  -1.112  1.00 19.47  ? 206 ALA A O   1 
ATOM   1600 C  CB  . ALA A 1 206 ? 9.164   -5.254  -0.499  1.00 18.72  ? 206 ALA A CB  1 
ATOM   1601 N  N   . PHE A 1 207 ? 11.328  -6.968  1.024   1.00 19.53  ? 207 PHE A N   1 
ATOM   1602 C  CA  . PHE A 1 207 ? 12.701  -7.254  1.428   1.00 18.73  ? 207 PHE A CA  1 
ATOM   1603 C  C   . PHE A 1 207 ? 13.109  -8.642  0.969   1.00 18.63  ? 207 PHE A C   1 
ATOM   1604 O  O   . PHE A 1 207 ? 14.209  -8.849  0.464   1.00 19.43  ? 207 PHE A O   1 
ATOM   1605 C  CB  . PHE A 1 207 ? 12.873  -7.157  2.943   1.00 18.25  ? 207 PHE A CB  1 
ATOM   1606 C  CG  . PHE A 1 207 ? 13.152  -5.757  3.463   1.00 19.49  ? 207 PHE A CG  1 
ATOM   1607 C  CD1 . PHE A 1 207 ? 12.133  -4.889  3.807   1.00 21.83  ? 207 PHE A CD1 1 
ATOM   1608 C  CD2 . PHE A 1 207 ? 14.449  -5.297  3.606   1.00 21.66  ? 207 PHE A CD2 1 
ATOM   1609 C  CE1 . PHE A 1 207 ? 12.416  -3.634  4.271   1.00 20.73  ? 207 PHE A CE1 1 
ATOM   1610 C  CE2 . PHE A 1 207 ? 14.733  -4.034  4.087   1.00 20.11  ? 207 PHE A CE2 1 
ATOM   1611 C  CZ  . PHE A 1 207 ? 13.705  -3.179  4.424   1.00 18.86  ? 207 PHE A CZ  1 
ATOM   1612 N  N   . LEU A 1 208 ? 12.225  -9.623  1.152   1.00 19.02  ? 208 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 208 ? 12.648  -10.965 0.759   1.00 19.86  ? 208 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 208 ? 12.885  -11.114 -0.739  1.00 17.29  ? 208 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 208 ? 13.749  -11.885 -1.142  1.00 19.27  ? 208 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 208 ? 11.589  -11.974 1.230   1.00 22.16  ? 208 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 208 ? 11.533  -12.161 2.745   1.00 23.61  ? 208 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 208 ? 10.282  -12.933 3.158   1.00 26.88  ? 208 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 208 ? 12.793  -12.858 3.239   1.00 28.69  ? 208 LEU A CD2 1 
ATOM   1620 N  N   . LEU A 1 209 ? 12.107  -10.381 -1.536  1.00 18.95  ? 209 LEU A N   1 
ATOM   1621 C  CA  . LEU A 1 209 ? 12.289  -10.343 -2.976  1.00 16.59  ? 209 LEU A CA  1 
ATOM   1622 C  C   . LEU A 1 209 ? 13.655  -9.771  -3.309  1.00 16.30  ? 209 LEU A C   1 
ATOM   1623 O  O   . LEU A 1 209 ? 14.356  -10.235 -4.208  1.00 18.22  ? 209 LEU A O   1 
ATOM   1624 C  CB  . LEU A 1 209 ? 11.158  -9.549  -3.661  1.00 17.64  ? 209 LEU A CB  1 
ATOM   1625 C  CG  . LEU A 1 209 ? 9.781   -10.237 -3.667  1.00 17.60  ? 209 LEU A CG  1 
ATOM   1626 C  CD1 . LEU A 1 209 ? 8.709   -9.217  -3.951  1.00 19.99  ? 209 LEU A CD1 1 
ATOM   1627 C  CD2 . LEU A 1 209 ? 9.816   -11.355 -4.697  1.00 19.05  ? 209 LEU A CD2 1 
ATOM   1628 N  N   . ASN A 1 210 ? 14.097  -8.756  -2.603  1.00 17.47  ? 210 ASN A N   1 
ATOM   1629 C  CA  . ASN A 1 210 ? 15.437  -8.224  -2.781  1.00 18.35  ? 210 ASN A CA  1 
ATOM   1630 C  C   . ASN A 1 210 ? 16.515  -9.241  -2.388  1.00 17.98  ? 210 ASN A C   1 
ATOM   1631 O  O   . ASN A 1 210 ? 17.510  -9.454  -3.096  1.00 20.26  ? 210 ASN A O   1 
ATOM   1632 C  CB  . ASN A 1 210 ? 15.583  -6.951  -1.943  1.00 18.85  ? 210 ASN A CB  1 
ATOM   1633 C  CG  . ASN A 1 210 ? 15.032  -5.721  -2.622  1.00 16.71  ? 210 ASN A CG  1 
ATOM   1634 O  OD1 . ASN A 1 210 ? 15.665  -5.023  -3.413  1.00 21.11  ? 210 ASN A OD1 1 
ATOM   1635 N  ND2 . ASN A 1 210 ? 13.775  -5.428  -2.300  1.00 19.18  ? 210 ASN A ND2 1 
ATOM   1636 N  N   . ILE A 1 211 ? 16.330  -9.886  -1.234  1.00 18.12  ? 211 ILE A N   1 
ATOM   1637 C  CA  . ILE A 1 211 ? 17.290  -10.885 -0.747  1.00 20.96  ? 211 ILE A CA  1 
ATOM   1638 C  C   . ILE A 1 211 ? 17.436  -12.040 -1.729  1.00 20.02  ? 211 ILE A C   1 
ATOM   1639 O  O   . ILE A 1 211 ? 18.546  -12.482 -2.059  1.00 22.15  ? 211 ILE A O   1 
ATOM   1640 C  CB  . ILE A 1 211 ? 16.882  -11.345 0.675   1.00 18.64  ? 211 ILE A CB  1 
ATOM   1641 C  CG1 . ILE A 1 211 ? 17.002  -10.245 1.730   1.00 24.23  ? 211 ILE A CG1 1 
ATOM   1642 C  CG2 . ILE A 1 211 ? 17.699  -12.546 1.101   1.00 23.07  ? 211 ILE A CG2 1 
ATOM   1643 C  CD1 . ILE A 1 211 ? 16.301  -10.450 3.046   1.00 27.05  ? 211 ILE A CD1 1 
ATOM   1644 N  N   . GLN A 1 212 ? 16.322  -12.544 -2.253  1.00 18.99  ? 212 GLN A N   1 
ATOM   1645 C  CA  . GLN A 1 212 ? 16.413  -13.630 -3.231  1.00 19.76  ? 212 GLN A CA  1 
ATOM   1646 C  C   . GLN A 1 212 ? 17.099  -13.144 -4.498  1.00 18.05  ? 212 GLN A C   1 
ATOM   1647 O  O   . GLN A 1 212 ? 17.848  -13.911 -5.123  1.00 19.78  ? 212 GLN A O   1 
ATOM   1648 C  CB  . GLN A 1 212 ? 15.050  -14.240 -3.564  1.00 22.25  ? 212 GLN A CB  1 
ATOM   1649 C  CG  . GLN A 1 212 ? 13.980  -13.277 -4.001  1.00 35.03  ? 212 GLN A CG  1 
ATOM   1650 C  CD  . GLN A 1 212 ? 12.638  -14.012 -4.091  1.00 47.92  ? 212 GLN A CD  1 
ATOM   1651 O  OE1 . GLN A 1 212 ? 12.351  -14.969 -3.375  1.00 61.30  ? 212 GLN A OE1 1 
ATOM   1652 N  NE2 . GLN A 1 212 ? 11.876  -13.500 -5.033  1.00 69.26  ? 212 GLN A NE2 1 
ATOM   1653 N  N   . LEU A 1 213 ? 16.864  -11.887 -4.874  1.00 17.71  ? 213 LEU A N   1 
ATOM   1654 C  CA  . LEU A 1 213 ? 17.605  -11.350 -6.019  1.00 17.59  ? 213 LEU A CA  1 
ATOM   1655 C  C   . LEU A 1 213 ? 19.105  -11.389 -5.744  1.00 18.09  ? 213 LEU A C   1 
ATOM   1656 O  O   . LEU A 1 213 ? 19.913  -11.802 -6.576  1.00 19.81  ? 213 LEU A O   1 
ATOM   1657 C  CB  . LEU A 1 213 ? 17.119  -9.928  -6.301  1.00 18.41  ? 213 LEU A CB  1 
ATOM   1658 C  CG  . LEU A 1 213 ? 17.932  -9.152  -7.354  1.00 20.98  ? 213 LEU A CG  1 
ATOM   1659 C  CD1 . LEU A 1 213 ? 17.865  -9.832  -8.713  1.00 23.88  ? 213 LEU A CD1 1 
ATOM   1660 C  CD2 . LEU A 1 213 ? 17.425  -7.719  -7.442  1.00 26.11  ? 213 LEU A CD2 1 
ATOM   1661 N  N   . PHE A 1 214 ? 19.520  -10.950 -4.546  1.00 21.04  ? 214 PHE A N   1 
ATOM   1662 C  CA  . PHE A 1 214 ? 20.925  -10.862 -4.191  1.00 19.36  ? 214 PHE A CA  1 
ATOM   1663 C  C   . PHE A 1 214 ? 21.553  -12.260 -4.245  1.00 18.08  ? 214 PHE A C   1 
ATOM   1664 O  O   . PHE A 1 214 ? 22.674  -12.379 -4.714  1.00 20.69  ? 214 PHE A O   1 
ATOM   1665 C  CB  . PHE A 1 214 ? 21.154  -10.282 -2.814  1.00 23.38  ? 214 PHE A CB  1 
ATOM   1666 C  CG  . PHE A 1 214 ? 20.691  -8.864  -2.534  1.00 24.67  ? 214 PHE A CG  1 
ATOM   1667 C  CD1 . PHE A 1 214 ? 20.508  -7.937  -3.542  1.00 28.55  ? 214 PHE A CD1 1 
ATOM   1668 C  CD2 . PHE A 1 214 ? 20.443  -8.478  -1.206  1.00 27.44  ? 214 PHE A CD2 1 
ATOM   1669 C  CE1 . PHE A 1 214 ? 20.080  -6.638  -3.250  1.00 30.11  ? 214 PHE A CE1 1 
ATOM   1670 C  CE2 . PHE A 1 214 ? 20.033  -7.200  -0.931  1.00 28.31  ? 214 PHE A CE2 1 
ATOM   1671 C  CZ  . PHE A 1 214 ? 19.853  -6.269  -1.938  1.00 30.22  ? 214 PHE A CZ  1 
ATOM   1672 N  N   . GLU A 1 215 ? 20.812  -13.243 -3.766  1.00 18.96  ? 215 GLU A N   1 
ATOM   1673 C  CA  . GLU A 1 215 ? 21.275  -14.634 -3.834  1.00 20.91  ? 215 GLU A CA  1 
ATOM   1674 C  C   . GLU A 1 215 ? 21.500  -15.097 -5.276  1.00 21.90  ? 215 GLU A C   1 
ATOM   1675 O  O   . GLU A 1 215 ? 22.529  -15.724 -5.576  1.00 21.46  ? 215 GLU A O   1 
ATOM   1676 C  CB  . GLU A 1 215 ? 20.285  -15.519 -3.060  1.00 24.12  ? 215 GLU A CB  1 
ATOM   1677 C  CG  . GLU A 1 215 ? 20.360  -15.226 -1.552  1.00 29.32  ? 215 GLU A CG  1 
ATOM   1678 C  CD  . GLU A 1 215 ? 19.254  -15.932 -0.787  1.00 31.56  ? 215 GLU A CD  1 
ATOM   1679 O  OE1 . GLU A 1 215 ? 18.316  -16.411 -1.458  1.00 37.67  ? 215 GLU A OE1 1 
ATOM   1680 O  OE2 . GLU A 1 215 ? 19.353  -15.984 0.467   1.00 32.73  ? 215 GLU A OE2 1 
ATOM   1681 N  N   . GLU A 1 216 ? 20.543  -14.770 -6.172  1.00 19.28  ? 216 GLU A N   1 
ATOM   1682 C  CA  . GLU A 1 216 ? 20.716  -15.076 -7.585  1.00 18.26  ? 216 GLU A CA  1 
ATOM   1683 C  C   . GLU A 1 216 ? 21.934  -14.371 -8.197  1.00 17.64  ? 216 GLU A C   1 
ATOM   1684 O  O   . GLU A 1 216 ? 22.746  -14.979 -8.900  1.00 18.47  ? 216 GLU A O   1 
ATOM   1685 C  CB  . GLU A 1 216 ? 19.461  -14.700 -8.398  1.00 17.97  ? 216 GLU A CB  1 
ATOM   1686 C  CG  . GLU A 1 216 ? 19.549  -15.177 -9.840  1.00 17.26  ? 216 GLU A CG  1 
ATOM   1687 C  CD  . GLU A 1 216 ? 18.542  -14.463 -10.726 1.00 18.18  ? 216 GLU A CD  1 
ATOM   1688 O  OE1 . GLU A 1 216 ? 18.665  -13.213 -10.732 1.00 19.03  ? 216 GLU A OE1 1 
ATOM   1689 O  OE2 . GLU A 1 216 ? 17.685  -15.089 -11.358 1.00 17.97  ? 216 GLU A OE2 1 
ATOM   1690 N  N   . LEU A 1 217 ? 22.075  -13.052 -7.961  1.00 18.44  ? 217 LEU A N   1 
ATOM   1691 C  CA  . LEU A 1 217 ? 23.175  -12.327 -8.574  1.00 17.75  ? 217 LEU A CA  1 
ATOM   1692 C  C   . LEU A 1 217 ? 24.494  -12.882 -8.085  1.00 18.24  ? 217 LEU A C   1 
ATOM   1693 O  O   . LEU A 1 217 ? 25.449  -13.053 -8.839  1.00 19.49  ? 217 LEU A O   1 
ATOM   1694 C  CB  . LEU A 1 217 ? 23.085  -10.835 -8.274  1.00 19.29  ? 217 LEU A CB  1 
ATOM   1695 C  CG  . LEU A 1 217 ? 21.808  -10.145 -8.757  1.00 18.70  ? 217 LEU A CG  1 
ATOM   1696 C  CD1 . LEU A 1 217 ? 21.892  -8.625  -8.603  1.00 23.52  ? 217 LEU A CD1 1 
ATOM   1697 C  CD2 . LEU A 1 217 ? 21.525  -10.488 -10.210 1.00 24.12  ? 217 LEU A CD2 1 
ATOM   1698 N  N   . GLN A 1 218 ? 24.607  -13.215 -6.812  1.00 19.60  ? 218 GLN A N   1 
ATOM   1699 C  CA  . GLN A 1 218 ? 25.902  -13.756 -6.390  1.00 19.93  ? 218 GLN A CA  1 
ATOM   1700 C  C   . GLN A 1 218 ? 26.200  -15.091 -7.053  1.00 18.91  ? 218 GLN A C   1 
ATOM   1701 O  O   . GLN A 1 218 ? 27.361  -15.346 -7.377  1.00 22.47  ? 218 GLN A O   1 
ATOM   1702 C  CB  . GLN A 1 218 ? 25.822  -13.901 -4.886  1.00 23.87  ? 218 GLN A CB  1 
ATOM   1703 C  CG  . GLN A 1 218 ? 27.026  -14.664 -4.336  1.00 27.58  ? 218 GLN A CG  1 
ATOM   1704 C  CD  . GLN A 1 218 ? 28.128  -13.648 -4.079  1.00 31.58  ? 218 GLN A CD  1 
ATOM   1705 O  OE1 . GLN A 1 218 ? 27.886  -12.442 -4.136  1.00 30.14  ? 218 GLN A OE1 1 
ATOM   1706 N  NE2 . GLN A 1 218 ? 29.310  -14.179 -3.806  1.00 38.43  ? 218 GLN A NE2 1 
ATOM   1707 N  N   . GLU A 1 219 ? 25.191  -15.927 -7.275  1.00 19.37  ? 219 GLU A N   1 
ATOM   1708 C  CA  . GLU A 1 219 ? 25.359  -17.170 -8.013  1.00 20.30  ? 219 GLU A CA  1 
ATOM   1709 C  C   . GLU A 1 219 ? 25.869  -16.910 -9.427  1.00 18.84  ? 219 GLU A C   1 
ATOM   1710 O  O   . GLU A 1 219 ? 26.802  -17.577 -9.845  1.00 21.76  ? 219 GLU A O   1 
ATOM   1711 C  CB  . GLU A 1 219 ? 24.068  -18.019 -8.148  1.00 29.38  ? 219 GLU A CB  1 
ATOM   1712 C  CG  . GLU A 1 219 ? 24.373  -19.327 -8.816  1.00 45.05  ? 219 GLU A CG  1 
ATOM   1713 C  CD  . GLU A 1 219 ? 24.059  -19.690 -10.228 1.00 55.34  ? 219 GLU A CD  1 
ATOM   1714 O  OE1 . GLU A 1 219 ? 23.493  -18.971 -11.073 1.00 61.32  ? 219 GLU A OE1 1 
ATOM   1715 O  OE2 . GLU A 1 219 ? 24.451  -20.861 -10.520 1.00 79.03  ? 219 GLU A OE2 1 
ATOM   1716 N  N   . LEU A 1 220 ? 25.229  -15.940 -10.098 1.00 19.36  ? 220 LEU A N   1 
ATOM   1717 C  CA  . LEU A 1 220 ? 25.533  -15.672 -11.504 1.00 20.76  ? 220 LEU A CA  1 
ATOM   1718 C  C   . LEU A 1 220 ? 26.974  -15.201 -11.684 1.00 20.73  ? 220 LEU A C   1 
ATOM   1719 O  O   . LEU A 1 220 ? 27.629  -15.465 -12.693 1.00 22.79  ? 220 LEU A O   1 
ATOM   1720 C  CB  . LEU A 1 220 ? 24.547  -14.638 -12.086 1.00 19.44  ? 220 LEU A CB  1 
ATOM   1721 C  CG  . LEU A 1 220 ? 23.149  -15.101 -12.456 1.00 19.91  ? 220 LEU A CG  1 
ATOM   1722 C  CD1 . LEU A 1 220 ? 22.250  -13.897 -12.647 1.00 22.89  ? 220 LEU A CD1 1 
ATOM   1723 C  CD2 . LEU A 1 220 ? 23.224  -16.007 -13.697 1.00 25.41  ? 220 LEU A CD2 1 
ATOM   1724 N  N   . LEU A 1 221 ? 27.450  -14.498 -10.658 1.00 19.53  ? 221 LEU A N   1 
ATOM   1725 C  CA  . LEU A 1 221 ? 28.775  -13.885 -10.722 1.00 21.40  ? 221 LEU A CA  1 
ATOM   1726 C  C   . LEU A 1 221 ? 29.919  -14.793 -10.339 1.00 23.10  ? 221 LEU A C   1 
ATOM   1727 O  O   . LEU A 1 221 ? 31.101  -14.471 -10.439 1.00 27.79  ? 221 LEU A O   1 
ATOM   1728 C  CB  . LEU A 1 221 ? 28.744  -12.657 -9.816  1.00 21.57  ? 221 LEU A CB  1 
ATOM   1729 C  CG  . LEU A 1 221 ? 27.930  -11.459 -10.331 1.00 23.84  ? 221 LEU A CG  1 
ATOM   1730 C  CD1 . LEU A 1 221 ? 27.640  -10.509 -9.170  1.00 28.42  ? 221 LEU A CD1 1 
ATOM   1731 C  CD2 . LEU A 1 221 ? 28.643  -10.715 -11.428 1.00 25.38  ? 221 LEU A CD2 1 
ATOM   1732 N  N   . THR A 1 222 ? 29.604  -15.992 -9.864  1.00 23.23  ? 222 THR A N   1 
ATOM   1733 C  CA  . THR A 1 222 ? 30.696  -16.767 -9.283  1.00 28.49  ? 222 THR A CA  1 
ATOM   1734 C  C   . THR A 1 222 ? 30.895  -18.081 -9.996  1.00 27.75  ? 222 THR A C   1 
ATOM   1735 O  O   . THR A 1 222 ? 31.418  -19.024 -9.415  1.00 42.31  ? 222 THR A O   1 
ATOM   1736 C  CB  . THR A 1 222 ? 30.383  -16.926 -7.785  1.00 28.87  ? 222 THR A CB  1 
ATOM   1737 O  OG1 . THR A 1 222 ? 29.031  -17.323 -7.546  1.00 41.96  ? 222 THR A OG1 1 
ATOM   1738 C  CG2 . THR A 1 222 ? 30.591  -15.566 -7.097  1.00 35.48  ? 222 THR A CG2 1 
ATOM   1739 N  N   . HIS A 1 223 ? 30.508  -18.165 -11.275 1.00 27.50  ? 223 HIS A N   1 
ATOM   1740 C  CA  . HIS A 1 223 ? 30.882  -19.322 -12.087 1.00 29.16  ? 223 HIS A CA  1 
ATOM   1741 C  C   . HIS A 1 223 ? 32.338  -19.333 -12.556 1.00 40.27  ? 223 HIS A C   1 
ATOM   1742 O  O   . HIS A 1 223 ? 33.026  -18.361 -12.875 1.00 48.02  ? 223 HIS A O   1 
ATOM   1743 C  CB  . HIS A 1 223 ? 29.928  -19.432 -13.294 1.00 27.95  ? 223 HIS A CB  1 
ATOM   1744 C  CG  . HIS A 1 223 ? 28.509  -19.709 -12.856 1.00 28.90  ? 223 HIS A CG  1 
ATOM   1745 N  ND1 . HIS A 1 223 ? 28.061  -20.939 -12.398 1.00 30.12  ? 223 HIS A ND1 1 
ATOM   1746 C  CD2 . HIS A 1 223 ? 27.432  -18.892 -12.823 1.00 28.56  ? 223 HIS A CD2 1 
ATOM   1747 C  CE1 . HIS A 1 223 ? 26.779  -20.868 -12.099 1.00 30.47  ? 223 HIS A CE1 1 
ATOM   1748 N  NE2 . HIS A 1 223 ? 26.371  -19.631 -12.352 1.00 29.10  ? 223 HIS A NE2 1 
ATOM   1749 N  N   . PRO B 1 10  ? 14.346  24.632  -50.009 1.00 63.67  ? 10  PRO B N   1 
ATOM   1750 C  CA  . PRO B 1 10  ? 13.971  23.385  -50.650 1.00 58.95  ? 10  PRO B CA  1 
ATOM   1751 C  C   . PRO B 1 10  ? 12.712  22.782  -50.022 1.00 58.40  ? 10  PRO B C   1 
ATOM   1752 O  O   . PRO B 1 10  ? 12.142  23.342  -49.104 1.00 63.96  ? 10  PRO B O   1 
ATOM   1753 C  CB  . PRO B 1 10  ? 15.140  22.431  -50.448 1.00 61.20  ? 10  PRO B CB  1 
ATOM   1754 C  CG  . PRO B 1 10  ? 15.918  23.068  -49.348 1.00 61.84  ? 10  PRO B CG  1 
ATOM   1755 C  CD  . PRO B 1 10  ? 15.754  24.553  -49.563 1.00 63.83  ? 10  PRO B CD  1 
ATOM   1756 N  N   . GLN B 1 11  ? 12.324  21.645  -50.576 1.00 57.84  ? 11  GLN B N   1 
ATOM   1757 C  CA  . GLN B 1 11  ? 11.010  21.056  -50.473 1.00 59.74  ? 11  GLN B CA  1 
ATOM   1758 C  C   . GLN B 1 11  ? 10.801  20.474  -49.081 1.00 50.15  ? 11  GLN B C   1 
ATOM   1759 O  O   . GLN B 1 11  ? 9.795   20.866  -48.486 1.00 47.25  ? 11  GLN B O   1 
ATOM   1760 C  CB  . GLN B 1 11  ? 10.762  20.016  -51.582 1.00 66.94  ? 11  GLN B CB  1 
ATOM   1761 C  CG  . GLN B 1 11  ? 9.385   20.148  -52.228 1.00 76.91  ? 11  GLN B CG  1 
ATOM   1762 C  CD  . GLN B 1 11  ? 9.255   21.340  -53.156 1.00 79.86  ? 11  GLN B CD  1 
ATOM   1763 O  OE1 . GLN B 1 11  ? 10.098  21.557  -54.031 1.00 92.32  ? 11  GLN B OE1 1 
ATOM   1764 N  NE2 . GLN B 1 11  ? 8.197   22.140  -53.003 1.00 92.23  ? 11  GLN B NE2 1 
ATOM   1765 N  N   . ASP B 1 12  ? 11.715  19.614  -48.623 1.00 39.49  ? 12  ASP B N   1 
ATOM   1766 C  CA  . ASP B 1 12  ? 11.488  19.010  -47.316 1.00 37.59  ? 12  ASP B CA  1 
ATOM   1767 C  C   . ASP B 1 12  ? 11.691  20.038  -46.212 1.00 34.55  ? 12  ASP B C   1 
ATOM   1768 O  O   . ASP B 1 12  ? 12.713  20.704  -46.239 1.00 33.09  ? 12  ASP B O   1 
ATOM   1769 C  CB  . ASP B 1 12  ? 12.416  17.813  -47.062 1.00 38.63  ? 12  ASP B CB  1 
ATOM   1770 C  CG  . ASP B 1 12  ? 11.988  16.578  -47.827 1.00 46.39  ? 12  ASP B CG  1 
ATOM   1771 O  OD1 . ASP B 1 12  ? 10.792  16.471  -48.191 1.00 52.15  ? 12  ASP B OD1 1 
ATOM   1772 O  OD2 . ASP B 1 12  ? 12.832  15.684  -48.098 1.00 57.05  ? 12  ASP B OD2 1 
ATOM   1773 N  N   . LEU B 1 13  ? 10.765  20.149  -45.268 1.00 32.69  ? 13  LEU B N   1 
ATOM   1774 C  CA  . LEU B 1 13  ? 10.920  21.061  -44.135 1.00 31.33  ? 13  LEU B CA  1 
ATOM   1775 C  C   . LEU B 1 13  ? 12.252  20.828  -43.421 1.00 30.20  ? 13  LEU B C   1 
ATOM   1776 O  O   . LEU B 1 13  ? 12.959  21.764  -43.058 1.00 31.97  ? 13  LEU B O   1 
ATOM   1777 C  CB  . LEU B 1 13  ? 9.787   20.891  -43.127 1.00 32.21  ? 13  LEU B CB  1 
ATOM   1778 C  CG  . LEU B 1 13  ? 9.900   21.772  -41.882 1.00 30.73  ? 13  LEU B CG  1 
ATOM   1779 C  CD1 . LEU B 1 13  ? 9.959   23.241  -42.281 1.00 30.70  ? 13  LEU B CD1 1 
ATOM   1780 C  CD2 . LEU B 1 13  ? 8.748   21.490  -40.921 1.00 29.51  ? 13  LEU B CD2 1 
ATOM   1781 N  N   . SER B 1 14  ? 12.565  19.542  -43.250 1.00 32.52  ? 14  SER B N   1 
ATOM   1782 C  CA  . SER B 1 14  ? 13.832  19.190  -42.603 1.00 38.08  ? 14  SER B CA  1 
ATOM   1783 C  C   . SER B 1 14  ? 14.981  19.848  -43.364 1.00 35.98  ? 14  SER B C   1 
ATOM   1784 O  O   . SER B 1 14  ? 15.882  20.438  -42.753 1.00 39.87  ? 14  SER B O   1 
ATOM   1785 C  CB  . SER B 1 14  ? 13.992  17.669  -42.510 1.00 41.41  ? 14  SER B CB  1 
ATOM   1786 O  OG  . SER B 1 14  ? 14.304  17.142  -43.801 1.00 41.26  ? 14  SER B OG  1 
ATOM   1787 N  N   . GLU B 1 15  ? 14.971  19.788  -44.698 1.00 36.45  ? 15  GLU B N   1 
ATOM   1788 C  CA  . GLU B 1 15  ? 16.077  20.413  -45.420 1.00 38.28  ? 15  GLU B CA  1 
ATOM   1789 C  C   . GLU B 1 15  ? 15.965  21.930  -45.467 1.00 36.58  ? 15  GLU B C   1 
ATOM   1790 O  O   . GLU B 1 15  ? 16.992  22.626  -45.517 1.00 35.79  ? 15  GLU B O   1 
ATOM   1791 C  CB  . GLU B 1 15  ? 16.189  19.876  -46.859 1.00 45.08  ? 15  GLU B CB  1 
ATOM   1792 C  CG  . GLU B 1 15  ? 17.013  18.588  -46.915 1.00 57.42  ? 15  GLU B CG  1 
ATOM   1793 C  CD  . GLU B 1 15  ? 18.468  18.725  -46.500 1.00 64.79  ? 15  GLU B CD  1 
ATOM   1794 O  OE1 . GLU B 1 15  ? 19.031  19.846  -46.596 1.00 75.23  ? 15  GLU B OE1 1 
ATOM   1795 O  OE2 . GLU B 1 15  ? 19.091  17.720  -46.076 1.00 83.41  ? 15  GLU B OE2 1 
ATOM   1796 N  N   . ALA B 1 16  ? 14.731  22.437  -45.468 1.00 32.12  ? 16  ALA B N   1 
ATOM   1797 C  CA  . ALA B 1 16  ? 14.600  23.892  -45.524 1.00 32.27  ? 16  ALA B CA  1 
ATOM   1798 C  C   . ALA B 1 16  ? 15.229  24.526  -44.292 1.00 31.20  ? 16  ALA B C   1 
ATOM   1799 O  O   . ALA B 1 16  ? 15.860  25.575  -44.326 1.00 36.10  ? 16  ALA B O   1 
ATOM   1800 C  CB  . ALA B 1 16  ? 13.133  24.283  -45.661 1.00 30.57  ? 16  ALA B CB  1 
ATOM   1801 N  N   . LEU B 1 17  ? 15.005  23.830  -43.177 1.00 30.01  ? 17  LEU B N   1 
ATOM   1802 C  CA  . LEU B 1 17  ? 15.392  24.335  -41.855 1.00 31.13  ? 17  LEU B CA  1 
ATOM   1803 C  C   . LEU B 1 17  ? 16.908  24.446  -41.815 1.00 31.56  ? 17  LEU B C   1 
ATOM   1804 O  O   . LEU B 1 17  ? 17.426  25.464  -41.403 1.00 35.52  ? 17  LEU B O   1 
ATOM   1805 C  CB  . LEU B 1 17  ? 14.883  23.433  -40.730 1.00 30.07  ? 17  LEU B CB  1 
ATOM   1806 C  CG  . LEU B 1 17  ? 13.420  23.660  -40.318 1.00 28.81  ? 17  LEU B CG  1 
ATOM   1807 C  CD1 . LEU B 1 17  ? 12.902  22.486  -39.485 1.00 32.12  ? 17  LEU B CD1 1 
ATOM   1808 C  CD2 . LEU B 1 17  ? 13.314  24.996  -39.609 1.00 40.29  ? 17  LEU B CD2 1 
ATOM   1809 N  N   . LYS B 1 18  ? 17.504  23.349  -42.276 1.00 34.10  ? 18  LYS B N   1 
ATOM   1810 C  CA  . LYS B 1 18  ? 18.956  23.194  -42.350 1.00 35.02  ? 18  LYS B CA  1 
ATOM   1811 C  C   . LYS B 1 18  ? 19.573  24.296  -43.200 1.00 32.94  ? 18  LYS B C   1 
ATOM   1812 O  O   . LYS B 1 18  ? 20.516  25.040  -42.888 1.00 37.73  ? 18  LYS B O   1 
ATOM   1813 C  CB  . LYS B 1 18  ? 19.260  21.773  -42.860 1.00 36.34  ? 18  LYS B CB  1 
ATOM   1814 C  CG  . LYS B 1 18  ? 20.738  21.449  -42.860 1.00 42.49  ? 18  LYS B CG  1 
ATOM   1815 C  CD  . LYS B 1 18  ? 21.056  20.004  -42.568 1.00 49.38  ? 18  LYS B CD  1 
ATOM   1816 C  CE  . LYS B 1 18  ? 22.525  19.782  -42.249 1.00 54.38  ? 18  LYS B CE  1 
ATOM   1817 N  NZ  . LYS B 1 18  ? 22.829  20.188  -40.840 1.00 70.01  ? 18  LYS B NZ  1 
ATOM   1818 N  N   . GLU B 1 19  ? 19.029  24.504  -44.403 1.00 37.74  ? 19  GLU B N   1 
ATOM   1819 C  CA  . GLU B 1 19  ? 19.650  25.525  -45.250 1.00 44.28  ? 19  GLU B CA  1 
ATOM   1820 C  C   . GLU B 1 19  ? 19.399  26.934  -44.743 1.00 39.40  ? 19  GLU B C   1 
ATOM   1821 O  O   . GLU B 1 19  ? 20.255  27.816  -44.820 1.00 41.83  ? 19  GLU B O   1 
ATOM   1822 C  CB  . GLU B 1 19  ? 19.097  25.389  -46.666 1.00 49.42  ? 19  GLU B CB  1 
ATOM   1823 C  CG  . GLU B 1 19  ? 19.819  26.271  -47.676 1.00 60.52  ? 19  GLU B CG  1 
ATOM   1824 C  CD  . GLU B 1 19  ? 18.812  27.104  -48.453 1.00 70.14  ? 19  GLU B CD  1 
ATOM   1825 O  OE1 . GLU B 1 19  ? 18.833  27.045  -49.705 1.00 84.80  ? 19  GLU B OE1 1 
ATOM   1826 O  OE2 . GLU B 1 19  ? 18.013  27.793  -47.777 1.00 80.52  ? 19  GLU B OE2 1 
ATOM   1827 N  N   . ALA B 1 20  ? 18.183  27.139  -44.226 1.00 34.57  ? 20  ALA B N   1 
ATOM   1828 C  CA  . ALA B 1 20  ? 17.875  28.478  -43.731 1.00 34.53  ? 20  ALA B CA  1 
ATOM   1829 C  C   . ALA B 1 20  ? 18.717  28.832  -42.510 1.00 36.02  ? 20  ALA B C   1 
ATOM   1830 O  O   . ALA B 1 20  ? 18.986  30.008  -42.263 1.00 35.59  ? 20  ALA B O   1 
ATOM   1831 C  CB  . ALA B 1 20  ? 16.392  28.620  -43.440 1.00 35.90  ? 20  ALA B CB  1 
ATOM   1832 N  N   . THR B 1 21  ? 19.191  27.887  -41.700 1.00 32.78  ? 21  THR B N   1 
ATOM   1833 C  CA  . THR B 1 21  ? 19.944  28.282  -40.520 1.00 30.05  ? 21  THR B CA  1 
ATOM   1834 C  C   . THR B 1 21  ? 21.450  28.092  -40.590 1.00 30.42  ? 21  THR B C   1 
ATOM   1835 O  O   . THR B 1 21  ? 22.117  28.358  -39.590 1.00 34.08  ? 21  THR B O   1 
ATOM   1836 C  CB  . THR B 1 21  ? 19.398  27.486  -39.305 1.00 31.93  ? 21  THR B CB  1 
ATOM   1837 O  OG1 . THR B 1 21  ? 19.400  26.082  -39.608 1.00 30.56  ? 21  THR B OG1 1 
ATOM   1838 C  CG2 . THR B 1 21  ? 17.962  27.879  -39.004 1.00 31.14  ? 21  THR B CG2 1 
ATOM   1839 N  N   . LYS B 1 22  ? 22.021  27.655  -41.704 1.00 32.08  ? 22  LYS B N   1 
ATOM   1840 C  CA  . LYS B 1 22  ? 23.447  27.414  -41.905 1.00 36.71  ? 22  LYS B CA  1 
ATOM   1841 C  C   . LYS B 1 22  ? 24.264  28.650  -41.536 1.00 34.41  ? 22  LYS B C   1 
ATOM   1842 O  O   . LYS B 1 22  ? 25.307  28.597  -40.876 1.00 36.91  ? 22  LYS B O   1 
ATOM   1843 C  CB  . LYS B 1 22  ? 23.704  26.964  -43.351 1.00 40.38  ? 22  LYS B CB  1 
ATOM   1844 C  CG  . LYS B 1 22  ? 24.765  25.904  -43.538 1.00 52.42  ? 22  LYS B CG  1 
ATOM   1845 C  CD  . LYS B 1 22  ? 24.926  25.456  -44.985 1.00 63.78  ? 22  LYS B CD  1 
ATOM   1846 C  CE  . LYS B 1 22  ? 26.360  25.642  -45.458 1.00 68.41  ? 22  LYS B CE  1 
ATOM   1847 N  NZ  . LYS B 1 22  ? 26.795  24.718  -46.545 1.00 75.55  ? 22  LYS B NZ  1 
ATOM   1848 N  N   . GLU B 1 23  ? 23.801  29.824  -41.944 1.00 37.20  ? 23  GLU B N   1 
ATOM   1849 C  CA  . GLU B 1 23  ? 24.486  31.079  -41.602 1.00 40.55  ? 23  GLU B CA  1 
ATOM   1850 C  C   . GLU B 1 23  ? 24.467  31.379  -40.108 1.00 38.10  ? 23  GLU B C   1 
ATOM   1851 O  O   . GLU B 1 23  ? 25.541  31.631  -39.529 1.00 35.47  ? 23  GLU B O   1 
ATOM   1852 C  CB  . GLU B 1 23  ? 23.910  32.205  -42.457 1.00 43.73  ? 23  GLU B CB  1 
ATOM   1853 C  CG  . GLU B 1 23  ? 22.688  33.008  -42.154 1.00 51.02  ? 23  GLU B CG  1 
ATOM   1854 C  CD  . GLU B 1 23  ? 21.451  32.508  -41.459 1.00 54.06  ? 23  GLU B CD  1 
ATOM   1855 O  OE1 . GLU B 1 23  ? 21.128  31.313  -41.359 1.00 59.37  ? 23  GLU B OE1 1 
ATOM   1856 O  OE2 . GLU B 1 23  ? 20.701  33.390  -40.931 1.00 70.43  ? 23  GLU B OE2 1 
ATOM   1857 N  N   . VAL B 1 24  ? 23.324  31.361  -39.427 1.00 35.81  ? 24  VAL B N   1 
ATOM   1858 C  CA  . VAL B 1 24  ? 23.307  31.643  -37.989 1.00 32.68  ? 24  VAL B CA  1 
ATOM   1859 C  C   . VAL B 1 24  ? 23.998  30.520  -37.210 1.00 30.03  ? 24  VAL B C   1 
ATOM   1860 O  O   . VAL B 1 24  ? 24.520  30.759  -36.119 1.00 33.47  ? 24  VAL B O   1 
ATOM   1861 C  CB  . VAL B 1 24  ? 21.907  31.841  -37.365 1.00 35.24  ? 24  VAL B CB  1 
ATOM   1862 C  CG1 . VAL B 1 24  ? 21.293  33.191  -37.679 1.00 37.42  ? 24  VAL B CG1 1 
ATOM   1863 C  CG2 . VAL B 1 24  ? 20.950  30.753  -37.834 1.00 37.71  ? 24  VAL B CG2 1 
ATOM   1864 N  N   . HIS B 1 25  ? 24.037  29.285  -37.699 1.00 33.40  ? 25  HIS B N   1 
ATOM   1865 C  CA  . HIS B 1 25  ? 24.757  28.224  -36.963 1.00 34.97  ? 25  HIS B CA  1 
ATOM   1866 C  C   . HIS B 1 25  ? 26.240  28.567  -36.938 1.00 35.95  ? 25  HIS B C   1 
ATOM   1867 O  O   . HIS B 1 25  ? 26.995  28.429  -35.975 1.00 35.01  ? 25  HIS B O   1 
ATOM   1868 C  CB  . HIS B 1 25  ? 24.499  26.848  -37.588 1.00 39.49  ? 25  HIS B CB  1 
ATOM   1869 C  CG  . HIS B 1 25  ? 25.036  25.659  -36.862 1.00 41.97  ? 25  HIS B CG  1 
ATOM   1870 N  ND1 . HIS B 1 25  ? 26.363  25.268  -36.892 1.00 45.17  ? 25  HIS B ND1 1 
ATOM   1871 C  CD2 . HIS B 1 25  ? 24.412  24.734  -36.089 1.00 43.21  ? 25  HIS B CD2 1 
ATOM   1872 C  CE1 . HIS B 1 25  ? 26.515  24.170  -36.156 1.00 45.09  ? 25  HIS B CE1 1 
ATOM   1873 N  NE2 . HIS B 1 25  ? 25.340  23.828  -35.655 1.00 43.75  ? 25  HIS B NE2 1 
ATOM   1874 N  N   . THR B 1 26  ? 26.641  29.073  -38.115 1.00 36.80  ? 26  THR B N   1 
ATOM   1875 C  CA  . THR B 1 26  ? 28.026  29.523  -38.227 1.00 40.29  ? 26  THR B CA  1 
ATOM   1876 C  C   . THR B 1 26  ? 28.297  30.637  -37.227 1.00 35.70  ? 26  THR B C   1 
ATOM   1877 O  O   . THR B 1 26  ? 29.327  30.737  -36.550 1.00 41.35  ? 26  THR B O   1 
ATOM   1878 C  CB  . THR B 1 26  ? 28.262  29.915  -39.697 1.00 43.86  ? 26  THR B CB  1 
ATOM   1879 O  OG1 . THR B 1 26  ? 28.272  28.728  -40.501 1.00 49.98  ? 26  THR B OG1 1 
ATOM   1880 C  CG2 . THR B 1 26  ? 29.622  30.561  -39.865 1.00 53.98  ? 26  THR B CG2 1 
ATOM   1881 N  N   . GLN B 1 27  ? 27.334  31.554  -37.038 1.00 38.66  ? 27  GLN B N   1 
ATOM   1882 C  CA  . GLN B 1 27  ? 27.603  32.643  -36.091 1.00 35.89  ? 27  GLN B CA  1 
ATOM   1883 C  C   . GLN B 1 27  ? 27.690  32.130  -34.660 1.00 35.55  ? 27  GLN B C   1 
ATOM   1884 O  O   . GLN B 1 27  ? 28.454  32.650  -33.842 1.00 35.70  ? 27  GLN B O   1 
ATOM   1885 C  CB  . GLN B 1 27  ? 26.546  33.753  -36.149 1.00 36.86  ? 27  GLN B CB  1 
ATOM   1886 C  CG  . GLN B 1 27  ? 26.522  34.422  -37.515 1.00 40.53  ? 27  GLN B CG  1 
ATOM   1887 C  CD  . GLN B 1 27  ? 25.374  35.394  -37.709 1.00 48.98  ? 27  GLN B CD  1 
ATOM   1888 O  OE1 . GLN B 1 27  ? 24.691  35.751  -36.744 1.00 56.42  ? 27  GLN B OE1 1 
ATOM   1889 N  NE2 . GLN B 1 27  ? 25.171  35.822  -38.958 1.00 60.79  ? 27  GLN B NE2 1 
ATOM   1890 N  N   . ALA B 1 28  ? 26.873  31.125  -34.392 1.00 33.87  ? 28  ALA B N   1 
ATOM   1891 C  CA  . ALA B 1 28  ? 26.820  30.551  -33.042 1.00 35.52  ? 28  ALA B CA  1 
ATOM   1892 C  C   . ALA B 1 28  ? 28.154  29.869  -32.779 1.00 34.56  ? 28  ALA B C   1 
ATOM   1893 O  O   . ALA B 1 28  ? 28.713  29.978  -31.688 1.00 39.66  ? 28  ALA B O   1 
ATOM   1894 C  CB  . ALA B 1 28  ? 25.631  29.625  -32.888 1.00 36.13  ? 28  ALA B CB  1 
ATOM   1895 N  N   . GLU B 1 29  ? 28.657  29.195  -33.817 1.00 37.62  ? 29  GLU B N   1 
ATOM   1896 C  CA  . GLU B 1 29  ? 29.948  28.527  -33.678 1.00 40.77  ? 29  GLU B CA  1 
ATOM   1897 C  C   . GLU B 1 29  ? 31.055  29.517  -33.348 1.00 42.51  ? 29  GLU B C   1 
ATOM   1898 O  O   . GLU B 1 29  ? 32.015  29.157  -32.660 1.00 42.10  ? 29  GLU B O   1 
ATOM   1899 C  CB  . GLU B 1 29  ? 30.293  27.776  -34.960 1.00 43.02  ? 29  GLU B CB  1 
ATOM   1900 C  CG  . GLU B 1 29  ? 29.476  26.525  -35.221 1.00 45.16  ? 29  GLU B CG  1 
ATOM   1901 C  CD  . GLU B 1 29  ? 29.980  25.837  -36.477 1.00 47.44  ? 29  GLU B CD  1 
ATOM   1902 O  OE1 . GLU B 1 29  ? 30.870  24.981  -36.347 1.00 61.19  ? 29  GLU B OE1 1 
ATOM   1903 O  OE2 . GLU B 1 29  ? 29.530  26.139  -37.592 1.00 49.26  ? 29  GLU B OE2 1 
ATOM   1904 N  N   . ASN B 1 30  ? 30.929  30.747  -33.850 1.00 37.53  ? 30  ASN B N   1 
ATOM   1905 C  CA  . ASN B 1 30  ? 32.044  31.689  -33.696 1.00 38.24  ? 30  ASN B CA  1 
ATOM   1906 C  C   . ASN B 1 30  ? 31.787  32.684  -32.592 1.00 35.41  ? 30  ASN B C   1 
ATOM   1907 O  O   . ASN B 1 30  ? 32.658  33.498  -32.317 1.00 44.46  ? 30  ASN B O   1 
ATOM   1908 C  CB  . ASN B 1 30  ? 32.337  32.346  -35.044 1.00 44.15  ? 30  ASN B CB  1 
ATOM   1909 C  CG  . ASN B 1 30  ? 32.659  31.347  -36.147 1.00 51.03  ? 30  ASN B CG  1 
ATOM   1910 O  OD1 . ASN B 1 30  ? 32.343  31.600  -37.319 1.00 65.34  ? 30  ASN B OD1 1 
ATOM   1911 N  ND2 . ASN B 1 30  ? 33.274  30.198  -35.866 1.00 63.09  ? 30  ASN B ND2 1 
ATOM   1912 N  N   . ALA B 1 31  ? 30.641  32.621  -31.933 1.00 35.53  ? 31  ALA B N   1 
ATOM   1913 C  CA  . ALA B 1 31  ? 30.503  33.331  -30.664 1.00 34.37  ? 31  ALA B CA  1 
ATOM   1914 C  C   . ALA B 1 31  ? 31.680  32.948  -29.762 1.00 33.26  ? 31  ALA B C   1 
ATOM   1915 O  O   . ALA B 1 31  ? 32.054  31.777  -29.656 1.00 38.95  ? 31  ALA B O   1 
ATOM   1916 C  CB  . ALA B 1 31  ? 29.170  33.005  -30.007 1.00 31.46  ? 31  ALA B CB  1 
ATOM   1917 N  N   . GLU B 1 32  ? 32.290  33.946  -29.134 1.00 32.72  ? 32  GLU B N   1 
ATOM   1918 C  CA  . GLU B 1 32  ? 33.523  33.740  -28.380 1.00 32.23  ? 32  GLU B CA  1 
ATOM   1919 C  C   . GLU B 1 32  ? 33.414  32.648  -27.319 1.00 31.71  ? 32  GLU B C   1 
ATOM   1920 O  O   . GLU B 1 32  ? 34.309  31.818  -27.124 1.00 32.84  ? 32  GLU B O   1 
ATOM   1921 C  CB  . GLU B 1 32  ? 33.979  35.043  -27.704 1.00 40.54  ? 32  GLU B CB  1 
ATOM   1922 C  CG  . GLU B 1 32  ? 35.349  34.955  -27.050 1.00 52.31  ? 32  GLU B CG  1 
ATOM   1923 C  CD  . GLU B 1 32  ? 35.824  36.276  -26.466 1.00 62.65  ? 32  GLU B CD  1 
ATOM   1924 O  OE1 . GLU B 1 32  ? 35.184  37.329  -26.722 1.00 66.27  ? 32  GLU B OE1 1 
ATOM   1925 O  OE2 . GLU B 1 32  ? 36.855  36.269  -25.741 1.00 83.30  ? 32  GLU B OE2 1 
ATOM   1926 N  N   . PHE B 1 33  ? 32.294  32.643  -26.595 1.00 30.89  ? 33  PHE B N   1 
ATOM   1927 C  CA  . PHE B 1 33  ? 32.103  31.644  -25.553 1.00 29.98  ? 33  PHE B CA  1 
ATOM   1928 C  C   . PHE B 1 33  ? 32.188  30.241  -26.137 1.00 29.42  ? 33  PHE B C   1 
ATOM   1929 O  O   . PHE B 1 33  ? 32.833  29.331  -25.614 1.00 34.76  ? 33  PHE B O   1 
ATOM   1930 C  CB  . PHE B 1 33  ? 30.746  31.884  -24.870 1.00 31.51  ? 33  PHE B CB  1 
ATOM   1931 C  CG  . PHE B 1 33  ? 30.454  30.856  -23.799 1.00 33.73  ? 33  PHE B CG  1 
ATOM   1932 C  CD1 . PHE B 1 33  ? 29.683  29.726  -24.078 1.00 37.43  ? 33  PHE B CD1 1 
ATOM   1933 C  CD2 . PHE B 1 33  ? 30.982  31.043  -22.537 1.00 33.88  ? 33  PHE B CD2 1 
ATOM   1934 C  CE1 . PHE B 1 33  ? 29.500  28.843  -23.041 1.00 40.93  ? 33  PHE B CE1 1 
ATOM   1935 C  CE2 . PHE B 1 33  ? 30.771  30.165  -21.483 1.00 38.13  ? 33  PHE B CE2 1 
ATOM   1936 C  CZ  . PHE B 1 33  ? 30.012  29.052  -21.760 1.00 39.88  ? 33  PHE B CZ  1 
ATOM   1937 N  N   . MET B 1 34  ? 31.458  30.051  -27.229 1.00 36.31  ? 34  MET B N   1 
ATOM   1938 C  CA  . MET B 1 34  ? 31.271  28.710  -27.795 1.00 38.20  ? 34  MET B CA  1 
ATOM   1939 C  C   . MET B 1 34  ? 32.560  28.312  -28.489 1.00 40.22  ? 34  MET B C   1 
ATOM   1940 O  O   . MET B 1 34  ? 33.048  27.188  -28.430 1.00 37.81  ? 34  MET B O   1 
ATOM   1941 C  CB  . MET B 1 34  ? 30.110  28.703  -28.767 1.00 40.85  ? 34  MET B CB  1 
ATOM   1942 C  CG  . MET B 1 34  ? 28.971  27.732  -28.628 1.00 48.67  ? 34  MET B CG  1 
ATOM   1943 S  SD  . MET B 1 34  ? 29.117  26.283  -27.589 1.00 57.69  ? 34  MET B SD  1 
ATOM   1944 C  CE  . MET B 1 34  ? 28.641  26.919  -25.985 1.00 83.90  ? 34  MET B CE  1 
ATOM   1945 N  N   . ARG B 1 35  ? 33.124  29.294  -29.190 1.00 39.13  ? 35  ARG B N   1 
ATOM   1946 C  CA  . ARG B 1 35  ? 34.397  28.997  -29.849 1.00 42.64  ? 35  ARG B CA  1 
ATOM   1947 C  C   . ARG B 1 35  ? 35.447  28.576  -28.830 1.00 41.36  ? 35  ARG B C   1 
ATOM   1948 O  O   . ARG B 1 35  ? 36.344  27.741  -29.014 1.00 48.48  ? 35  ARG B O   1 
ATOM   1949 C  CB  . ARG B 1 35  ? 34.785  30.245  -30.631 1.00 48.96  ? 35  ARG B CB  1 
ATOM   1950 C  CG  . ARG B 1 35  ? 35.868  30.075  -31.678 1.00 55.89  ? 35  ARG B CG  1 
ATOM   1951 C  CD  . ARG B 1 35  ? 36.636  31.382  -31.858 1.00 59.23  ? 35  ARG B CD  1 
ATOM   1952 N  NE  . ARG B 1 35  ? 35.929  32.342  -32.679 1.00 68.39  ? 35  ARG B NE  1 
ATOM   1953 C  CZ  . ARG B 1 35  ? 35.806  33.648  -32.508 1.00 68.43  ? 35  ARG B CZ  1 
ATOM   1954 N  NH1 . ARG B 1 35  ? 36.350  34.296  -31.491 1.00 71.28  ? 35  ARG B NH1 1 
ATOM   1955 N  NH2 . ARG B 1 35  ? 35.095  34.326  -33.408 1.00 71.36  ? 35  ARG B NH2 1 
ATOM   1956 N  N   . ASN B 1 36  ? 35.375  29.184  -27.640 1.00 36.61  ? 36  ASN B N   1 
ATOM   1957 C  CA  . ASN B 1 36  ? 36.366  28.814  -26.630 1.00 34.95  ? 36  ASN B CA  1 
ATOM   1958 C  C   . ASN B 1 36  ? 36.104  27.409  -26.095 1.00 34.65  ? 36  ASN B C   1 
ATOM   1959 O  O   . ASN B 1 36  ? 37.024  26.604  -26.005 1.00 39.28  ? 36  ASN B O   1 
ATOM   1960 C  CB  . ASN B 1 36  ? 36.386  29.872  -25.534 1.00 37.93  ? 36  ASN B CB  1 
ATOM   1961 C  CG  . ASN B 1 36  ? 37.055  31.192  -25.844 1.00 41.40  ? 36  ASN B CG  1 
ATOM   1962 O  OD1 . ASN B 1 36  ? 36.899  32.147  -25.053 1.00 45.78  ? 36  ASN B OD1 1 
ATOM   1963 N  ND2 . ASN B 1 36  ? 37.805  31.375  -26.930 1.00 47.20  ? 36  ASN B ND2 1 
ATOM   1964 N  N   . PHE B 1 37  ? 34.836  27.178  -25.783 1.00 34.84  ? 37  PHE B N   1 
ATOM   1965 C  CA  . PHE B 1 37  ? 34.412  25.861  -25.292 1.00 36.00  ? 37  PHE B CA  1 
ATOM   1966 C  C   . PHE B 1 37  ? 34.902  24.802  -26.279 1.00 41.10  ? 37  PHE B C   1 
ATOM   1967 O  O   . PHE B 1 37  ? 35.459  23.788  -25.829 1.00 41.49  ? 37  PHE B O   1 
ATOM   1968 C  CB  . PHE B 1 37  ? 32.916  25.846  -25.057 1.00 38.28  ? 37  PHE B CB  1 
ATOM   1969 C  CG  . PHE B 1 37  ? 32.272  24.634  -24.413 1.00 44.65  ? 37  PHE B CG  1 
ATOM   1970 C  CD1 . PHE B 1 37  ? 32.930  23.495  -24.005 1.00 41.64  ? 37  PHE B CD1 1 
ATOM   1971 C  CD2 . PHE B 1 37  ? 30.894  24.649  -24.210 1.00 46.14  ? 37  PHE B CD2 1 
ATOM   1972 C  CE1 . PHE B 1 37  ? 32.333  22.393  -23.450 1.00 42.80  ? 37  PHE B CE1 1 
ATOM   1973 C  CE2 . PHE B 1 37  ? 30.243  23.570  -23.656 1.00 48.50  ? 37  PHE B CE2 1 
ATOM   1974 C  CZ  . PHE B 1 37  ? 30.965  22.445  -23.269 1.00 45.92  ? 37  PHE B CZ  1 
ATOM   1975 N  N   . GLN B 1 38  ? 34.713  25.013  -27.562 1.00 43.14  ? 38  GLN B N   1 
ATOM   1976 C  CA  . GLN B 1 38  ? 35.139  24.069  -28.604 1.00 48.50  ? 38  GLN B CA  1 
ATOM   1977 C  C   . GLN B 1 38  ? 36.646  23.843  -28.577 1.00 51.97  ? 38  GLN B C   1 
ATOM   1978 O  O   . GLN B 1 38  ? 37.208  22.792  -28.886 1.00 61.34  ? 38  GLN B O   1 
ATOM   1979 C  CB  . GLN B 1 38  ? 34.674  24.596  -29.965 1.00 56.05  ? 38  GLN B CB  1 
ATOM   1980 C  CG  . GLN B 1 38  ? 34.559  23.573  -31.084 1.00 66.32  ? 38  GLN B CG  1 
ATOM   1981 C  CD  . GLN B 1 38  ? 34.499  24.295  -32.427 1.00 69.79  ? 38  GLN B CD  1 
ATOM   1982 O  OE1 . GLN B 1 38  ? 33.648  25.175  -32.586 1.00 90.05  ? 38  GLN B OE1 1 
ATOM   1983 N  NE2 . GLN B 1 38  ? 35.373  23.949  -33.362 1.00 74.01  ? 38  GLN B NE2 1 
ATOM   1984 N  N   . LYS B 1 39  ? 37.339  24.882  -28.173 1.00 55.42  ? 39  LYS B N   1 
ATOM   1985 C  CA  . LYS B 1 39  ? 38.794  25.001  -28.109 1.00 58.16  ? 39  LYS B CA  1 
ATOM   1986 C  C   . LYS B 1 39  ? 39.300  24.262  -26.883 1.00 56.08  ? 39  LYS B C   1 
ATOM   1987 O  O   . LYS B 1 39  ? 40.478  24.090  -26.584 1.00 64.54  ? 39  LYS B O   1 
ATOM   1988 C  CB  . LYS B 1 39  ? 39.092  26.490  -28.089 1.00 65.70  ? 39  LYS B CB  1 
ATOM   1989 C  CG  . LYS B 1 39  ? 40.327  27.121  -28.654 1.00 69.68  ? 39  LYS B CG  1 
ATOM   1990 C  CD  . LYS B 1 39  ? 40.171  28.631  -28.812 1.00 75.87  ? 39  LYS B CD  1 
ATOM   1991 C  CE  . LYS B 1 39  ? 41.223  29.456  -28.089 1.00 81.22  ? 39  LYS B CE  1 
ATOM   1992 N  NZ  . LYS B 1 39  ? 41.487  30.825  -28.624 1.00 86.88  ? 39  LYS B NZ  1 
ATOM   1993 N  N   . GLY B 1 40  ? 38.378  23.759  -26.056 1.00 48.76  ? 40  GLY B N   1 
ATOM   1994 C  CA  . GLY B 1 40  ? 38.766  23.207  -24.772 1.00 50.03  ? 40  GLY B CA  1 
ATOM   1995 C  C   . GLY B 1 40  ? 38.911  24.272  -23.695 1.00 47.15  ? 40  GLY B C   1 
ATOM   1996 O  O   . GLY B 1 40  ? 39.325  23.975  -22.571 1.00 42.45  ? 40  GLY B O   1 
ATOM   1997 N  N   . GLN B 1 41  ? 38.577  25.510  -24.035 1.00 43.65  ? 41  GLN B N   1 
ATOM   1998 C  CA  . GLN B 1 41  ? 38.669  26.645  -23.125 1.00 39.61  ? 41  GLN B CA  1 
ATOM   1999 C  C   . GLN B 1 41  ? 37.329  26.933  -22.461 1.00 39.72  ? 41  GLN B C   1 
ATOM   2000 O  O   . GLN B 1 41  ? 36.539  27.762  -22.886 1.00 46.45  ? 41  GLN B O   1 
ATOM   2001 C  CB  . GLN B 1 41  ? 39.219  27.823  -23.922 1.00 43.95  ? 41  GLN B CB  1 
ATOM   2002 C  CG  . GLN B 1 41  ? 40.506  27.413  -24.627 1.00 48.06  ? 41  GLN B CG  1 
ATOM   2003 C  CD  . GLN B 1 41  ? 41.545  28.513  -24.606 1.00 60.24  ? 41  GLN B CD  1 
ATOM   2004 O  OE1 . GLN B 1 41  ? 41.206  29.700  -24.740 1.00 65.93  ? 41  GLN B OE1 1 
ATOM   2005 N  NE2 . GLN B 1 41  ? 42.797  28.084  -24.448 1.00 78.68  ? 41  GLN B NE2 1 
ATOM   2006 N  N   . VAL B 1 42  ? 37.089  26.189  -21.380 1.00 35.51  ? 42  VAL B N   1 
ATOM   2007 C  CA  . VAL B 1 42  ? 35.872  26.329  -20.593 1.00 32.28  ? 42  VAL B CA  1 
ATOM   2008 C  C   . VAL B 1 42  ? 36.231  26.107  -19.127 1.00 33.02  ? 42  VAL B C   1 
ATOM   2009 O  O   . VAL B 1 42  ? 37.092  25.242  -18.812 1.00 31.51  ? 42  VAL B O   1 
ATOM   2010 C  CB  . VAL B 1 42  ? 34.801  25.338  -21.087 1.00 32.12  ? 42  VAL B CB  1 
ATOM   2011 C  CG1 . VAL B 1 42  ? 35.296  23.912  -20.930 1.00 37.10  ? 42  VAL B CG1 1 
ATOM   2012 C  CG2 . VAL B 1 42  ? 33.502  25.505  -20.327 1.00 37.12  ? 42  VAL B CG2 1 
ATOM   2013 N  N   . THR B 1 43  ? 35.621  26.882  -18.224 1.00 28.99  ? 43  THR B N   1 
ATOM   2014 C  CA  . THR B 1 43  ? 35.940  26.673  -16.816 1.00 30.63  ? 43  THR B CA  1 
ATOM   2015 C  C   . THR B 1 43  ? 34.716  26.149  -16.090 1.00 26.04  ? 43  THR B C   1 
ATOM   2016 O  O   . THR B 1 43  ? 33.630  26.142  -16.641 1.00 27.09  ? 43  THR B O   1 
ATOM   2017 C  CB  . THR B 1 43  ? 36.333  27.972  -16.120 1.00 28.36  ? 43  THR B CB  1 
ATOM   2018 O  OG1 . THR B 1 43  ? 35.268  28.863  -16.428 1.00 32.57  ? 43  THR B OG1 1 
ATOM   2019 C  CG2 . THR B 1 43  ? 37.553  28.663  -16.703 1.00 36.65  ? 43  THR B CG2 1 
ATOM   2020 N  N   . ARG B 1 44  ? 34.932  25.746  -14.841 1.00 25.02  ? 44  ARG B N   1 
ATOM   2021 C  CA  . ARG B 1 44  ? 33.769  25.215  -14.121 1.00 22.72  ? 44  ARG B CA  1 
ATOM   2022 C  C   . ARG B 1 44  ? 32.726  26.330  -13.979 1.00 22.15  ? 44  ARG B C   1 
ATOM   2023 O  O   . ARG B 1 44  ? 31.518  26.009  -14.082 1.00 22.78  ? 44  ARG B O   1 
ATOM   2024 C  CB  . ARG B 1 44  ? 34.175  24.556  -12.798 1.00 23.67  ? 44  ARG B CB  1 
ATOM   2025 C  CG  . ARG B 1 44  ? 34.937  23.253  -12.947 1.00 25.36  ? 44  ARG B CG  1 
ATOM   2026 C  CD  . ARG B 1 44  ? 35.332  22.670  -11.594 1.00 26.52  ? 44  ARG B CD  1 
ATOM   2027 N  NE  . ARG B 1 44  ? 35.955  21.349  -11.824 1.00 27.32  ? 44  ARG B NE  1 
ATOM   2028 C  CZ  . ARG B 1 44  ? 36.155  20.415  -10.901 1.00 27.73  ? 44  ARG B CZ  1 
ATOM   2029 N  NH1 . ARG B 1 44  ? 35.763  20.659  -9.648  1.00 29.87  ? 44  ARG B NH1 1 
ATOM   2030 N  NH2 . ARG B 1 44  ? 36.728  19.248  -11.187 1.00 27.58  ? 44  ARG B NH2 1 
ATOM   2031 N  N   . ASP B 1 45  ? 33.088  27.587  -13.769 1.00 24.08  ? 45  ASP B N   1 
ATOM   2032 C  CA  . ASP B 1 45  ? 32.081  28.655  -13.588 1.00 25.93  ? 45  ASP B CA  1 
ATOM   2033 C  C   . ASP B 1 45  ? 31.149  28.857  -14.788 1.00 23.55  ? 45  ASP B C   1 
ATOM   2034 O  O   . ASP B 1 45  ? 29.915  29.059  -14.824 1.00 26.97  ? 45  ASP B O   1 
ATOM   2035 C  CB  . ASP B 1 45  ? 32.745  29.990  -13.272 1.00 28.65  ? 45  ASP B CB  1 
ATOM   2036 C  CG  . ASP B 1 45  ? 33.538  30.151  -12.010 1.00 40.51  ? 45  ASP B CG  1 
ATOM   2037 O  OD1 . ASP B 1 45  ? 33.302  29.411  -11.024 1.00 56.54  ? 45  ASP B OD1 1 
ATOM   2038 O  OD2 . ASP B 1 45  ? 34.432  31.053  -11.936 1.00 58.50  ? 45  ASP B OD2 1 
ATOM   2039 N  N   . GLY B 1 46  ? 31.743  28.845  -15.953 1.00 24.43  ? 46  GLY B N   1 
ATOM   2040 C  CA  . GLY B 1 46  ? 31.339  29.003  -17.306 1.00 22.19  ? 46  GLY B CA  1 
ATOM   2041 C  C   . GLY B 1 46  ? 30.439  27.820  -17.616 1.00 21.15  ? 46  GLY B C   1 
ATOM   2042 O  O   . GLY B 1 46  ? 29.339  27.989  -18.149 1.00 22.08  ? 46  GLY B O   1 
ATOM   2043 N  N   . PHE B 1 47  ? 30.943  26.626  -17.244 1.00 20.00  ? 47  PHE B N   1 
ATOM   2044 C  CA  . PHE B 1 47  ? 30.117  25.455  -17.565 1.00 18.78  ? 47  PHE B CA  1 
ATOM   2045 C  C   . PHE B 1 47  ? 28.826  25.443  -16.760 1.00 17.87  ? 47  PHE B C   1 
ATOM   2046 O  O   . PHE B 1 47  ? 27.772  25.080  -17.275 1.00 17.91  ? 47  PHE B O   1 
ATOM   2047 C  CB  . PHE B 1 47  ? 30.936  24.198  -17.346 1.00 19.92  ? 47  PHE B CB  1 
ATOM   2048 C  CG  . PHE B 1 47  ? 30.262  22.946  -17.856 1.00 20.20  ? 47  PHE B CG  1 
ATOM   2049 C  CD1 . PHE B 1 47  ? 30.248  22.635  -19.202 1.00 21.97  ? 47  PHE B CD1 1 
ATOM   2050 C  CD2 . PHE B 1 47  ? 29.657  22.119  -16.934 1.00 20.12  ? 47  PHE B CD2 1 
ATOM   2051 C  CE1 . PHE B 1 47  ? 29.619  21.469  -19.636 1.00 23.05  ? 47  PHE B CE1 1 
ATOM   2052 C  CE2 . PHE B 1 47  ? 29.037  20.954  -17.373 1.00 21.42  ? 47  PHE B CE2 1 
ATOM   2053 C  CZ  . PHE B 1 47  ? 29.026  20.637  -18.705 1.00 21.52  ? 47  PHE B CZ  1 
ATOM   2054 N  N   . LYS B 1 48  ? 28.932  25.838  -15.495 1.00 19.43  ? 48  LYS B N   1 
ATOM   2055 C  CA  . LYS B 1 48  ? 27.768  25.914  -14.619 1.00 20.92  ? 48  LYS B CA  1 
ATOM   2056 C  C   . LYS B 1 48  ? 26.724  26.861  -15.182 1.00 18.78  ? 48  LYS B C   1 
ATOM   2057 O  O   . LYS B 1 48  ? 25.520  26.576  -15.162 1.00 18.99  ? 48  LYS B O   1 
ATOM   2058 C  CB  . LYS B 1 48  ? 28.186  26.394  -13.231 1.00 22.97  ? 48  LYS B CB  1 
ATOM   2059 C  CG  . LYS B 1 48  ? 28.786  25.287  -12.400 1.00 27.10  ? 48  LYS B CG  1 
ATOM   2060 C  CD  . LYS B 1 48  ? 29.421  25.731  -11.093 1.00 30.16  ? 48  LYS B CD  1 
ATOM   2061 C  CE  . LYS B 1 48  ? 28.437  26.297  -10.096 1.00 31.10  ? 48  LYS B CE  1 
ATOM   2062 N  NZ  . LYS B 1 48  ? 29.076  26.470  -8.756  1.00 47.92  ? 48  LYS B NZ  1 
ATOM   2063 N  N   . LEU B 1 49  ? 27.186  27.996  -15.702 1.00 20.22  ? 49  LEU B N   1 
ATOM   2064 C  CA  . LEU B 1 49  ? 26.260  28.963  -16.274 1.00 19.49  ? 49  LEU B CA  1 
ATOM   2065 C  C   . LEU B 1 49  ? 25.511  28.406  -17.474 1.00 18.46  ? 49  LEU B C   1 
ATOM   2066 O  O   . LEU B 1 49  ? 24.324  28.629  -17.661 1.00 17.96  ? 49  LEU B O   1 
ATOM   2067 C  CB  . LEU B 1 49  ? 27.031  30.220  -16.690 1.00 21.50  ? 49  LEU B CB  1 
ATOM   2068 C  CG  . LEU B 1 49  ? 27.156  31.314  -15.641 1.00 25.59  ? 49  LEU B CG  1 
ATOM   2069 C  CD1 . LEU B 1 49  ? 28.114  32.417  -16.111 1.00 26.77  ? 49  LEU B CD1 1 
ATOM   2070 C  CD2 . LEU B 1 49  ? 25.767  31.867  -15.289 1.00 25.42  ? 49  LEU B CD2 1 
ATOM   2071 N  N   . VAL B 1 50  ? 26.266  27.668  -18.282 1.00 17.39  ? 50  VAL B N   1 
ATOM   2072 C  CA  . VAL B 1 50  ? 25.686  27.002  -19.448 1.00 20.51  ? 50  VAL B CA  1 
ATOM   2073 C  C   . VAL B 1 50  ? 24.620  25.998  -19.041 1.00 18.14  ? 50  VAL B C   1 
ATOM   2074 O  O   . VAL B 1 50  ? 23.529  25.936  -19.588 1.00 18.15  ? 50  VAL B O   1 
ATOM   2075 C  CB  . VAL B 1 50  ? 26.758  26.232  -20.267 1.00 23.74  ? 50  VAL B CB  1 
ATOM   2076 C  CG1 . VAL B 1 50  ? 26.199  25.072  -21.043 1.00 39.30  ? 50  VAL B CG1 1 
ATOM   2077 C  CG2 . VAL B 1 50  ? 27.330  27.253  -21.184 1.00 33.96  ? 50  VAL B CG2 1 
ATOM   2078 N  N   . MET B 1 51  ? 24.980  25.178  -18.071 1.00 17.30  ? 51  MET B N   1 
ATOM   2079 C  CA  . MET B 1 51  ? 24.060  24.127  -17.632 1.00 17.48  ? 51  MET B CA  1 
ATOM   2080 C  C   . MET B 1 51  ? 22.834  24.778  -17.030 1.00 15.69  ? 51  MET B C   1 
ATOM   2081 O  O   . MET B 1 51  ? 21.698  24.334  -17.264 1.00 15.91  ? 51  MET B O   1 
ATOM   2082 C  CB  . MET B 1 51  ? 24.772  23.175  -16.655 1.00 17.53  ? 51  MET B CB  1 
ATOM   2083 C  CG  . MET B 1 51  ? 25.910  22.415  -17.310 1.00 20.68  ? 51  MET B CG  1 
ATOM   2084 S  SD  . MET B 1 51  ? 25.312  21.276  -18.593 1.00 24.11  ? 51  MET B SD  1 
ATOM   2085 C  CE  . MET B 1 51  ? 24.801  19.868  -17.589 1.00 32.80  ? 51  MET B CE  1 
ATOM   2086 N  N   . ALA B 1 52  ? 22.980  25.840  -16.247 1.00 16.17  ? 52  ALA B N   1 
ATOM   2087 C  CA  . ALA B 1 52  ? 21.849  26.549  -15.671 1.00 16.31  ? 52  ALA B CA  1 
ATOM   2088 C  C   . ALA B 1 52  ? 20.955  27.082  -16.788 1.00 16.01  ? 52  ALA B C   1 
ATOM   2089 O  O   . ALA B 1 52  ? 19.730  26.956  -16.689 1.00 16.59  ? 52  ALA B O   1 
ATOM   2090 C  CB  . ALA B 1 52  ? 22.312  27.678  -14.735 1.00 17.35  ? 52  ALA B CB  1 
ATOM   2091 N  N   . SER B 1 53  ? 21.560  27.653  -17.823 1.00 16.67  ? 53  SER B N   1 
ATOM   2092 C  CA  . SER B 1 53  ? 20.820  28.189  -18.959 1.00 15.65  ? 53  SER B CA  1 
ATOM   2093 C  C   . SER B 1 53  ? 19.956  27.106  -19.599 1.00 15.53  ? 53  SER B C   1 
ATOM   2094 O  O   . SER B 1 53  ? 18.765  27.298  -19.868 1.00 15.77  ? 53  SER B O   1 
ATOM   2095 C  CB  . SER B 1 53  ? 21.769  28.765  -20.016 1.00 16.78  ? 53  SER B CB  1 
ATOM   2096 O  OG  . SER B 1 53  ? 22.577  29.781  -19.471 1.00 17.60  ? 53  SER B OG  1 
ATOM   2097 N  N   . LEU B 1 54  ? 20.627  25.947  -19.827 1.00 15.70  ? 54  LEU B N   1 
ATOM   2098 C  CA  . LEU B 1 54  ? 19.947  24.834  -20.497 1.00 15.26  ? 54  LEU B CA  1 
ATOM   2099 C  C   . LEU B 1 54  ? 18.769  24.325  -19.676 1.00 15.40  ? 54  LEU B C   1 
ATOM   2100 O  O   . LEU B 1 54  ? 17.727  23.983  -20.232 1.00 15.52  ? 54  LEU B O   1 
ATOM   2101 C  CB  . LEU B 1 54  ? 20.923  23.709  -20.827 1.00 16.75  ? 54  LEU B CB  1 
ATOM   2102 C  CG  . LEU B 1 54  ? 21.899  23.929  -21.976 1.00 17.88  ? 54  LEU B CG  1 
ATOM   2103 C  CD1 . LEU B 1 54  ? 23.038  22.932  -21.845 1.00 21.52  ? 54  LEU B CD1 1 
ATOM   2104 C  CD2 . LEU B 1 54  ? 21.209  23.775  -23.330 1.00 22.85  ? 54  LEU B CD2 1 
ATOM   2105 N  N   . TYR B 1 55  ? 18.891  24.278  -18.364 1.00 13.90  ? 55  TYR B N   1 
ATOM   2106 C  CA  . TYR B 1 55  ? 17.745  23.867  -17.543 1.00 14.53  ? 55  TYR B CA  1 
ATOM   2107 C  C   . TYR B 1 55  ? 16.585  24.814  -17.746 1.00 12.92  ? 55  TYR B C   1 
ATOM   2108 O  O   . TYR B 1 55  ? 15.459  24.360  -18.008 1.00 15.52  ? 55  TYR B O   1 
ATOM   2109 C  CB  . TYR B 1 55  ? 18.228  23.812  -16.086 1.00 14.84  ? 55  TYR B CB  1 
ATOM   2110 C  CG  . TYR B 1 55  ? 17.082  23.727  -15.118 1.00 15.05  ? 55  TYR B CG  1 
ATOM   2111 C  CD1 . TYR B 1 55  ? 16.474  22.514  -14.852 1.00 14.03  ? 55  TYR B CD1 1 
ATOM   2112 C  CD2 . TYR B 1 55  ? 16.566  24.840  -14.460 1.00 16.64  ? 55  TYR B CD2 1 
ATOM   2113 C  CE1 . TYR B 1 55  ? 15.422  22.414  -13.977 1.00 16.63  ? 55  TYR B CE1 1 
ATOM   2114 C  CE2 . TYR B 1 55  ? 15.496  24.743  -13.589 1.00 16.16  ? 55  TYR B CE2 1 
ATOM   2115 C  CZ  . TYR B 1 55  ? 14.932  23.526  -13.352 1.00 15.81  ? 55  TYR B CZ  1 
ATOM   2116 O  OH  . TYR B 1 55  ? 13.877  23.425  -12.484 1.00 17.76  ? 55  TYR B OH  1 
ATOM   2117 N  N   . HIS B 1 56  ? 16.786  26.136  -17.640 1.00 14.24  ? 56  HIS B N   1 
ATOM   2118 C  CA  . HIS B 1 56  ? 15.655  27.022  -17.833 1.00 14.70  ? 56  HIS B CA  1 
ATOM   2119 C  C   . HIS B 1 56  ? 15.028  26.855  -19.202 1.00 14.11  ? 56  HIS B C   1 
ATOM   2120 O  O   . HIS B 1 56  ? 13.795  26.844  -19.326 1.00 16.31  ? 56  HIS B O   1 
ATOM   2121 C  CB  . HIS B 1 56  ? 16.084  28.480  -17.633 1.00 16.57  ? 56  HIS B CB  1 
ATOM   2122 C  CG  . HIS B 1 56  ? 16.451  28.788  -16.201 1.00 17.84  ? 56  HIS B CG  1 
ATOM   2123 N  ND1 . HIS B 1 56  ? 17.697  29.220  -15.823 1.00 19.51  ? 56  HIS B ND1 1 
ATOM   2124 C  CD2 . HIS B 1 56  ? 15.750  28.746  -15.073 1.00 16.25  ? 56  HIS B CD2 1 
ATOM   2125 C  CE1 . HIS B 1 56  ? 17.750  29.436  -14.517 1.00 19.02  ? 56  HIS B CE1 1 
ATOM   2126 N  NE2 . HIS B 1 56  ? 16.551  29.143  -14.026 1.00 21.37  ? 56  HIS B NE2 1 
ATOM   2127 N  N   . ILE B 1 57  ? 15.872  26.735  -20.194 1.00 14.60  ? 57  ILE B N   1 
ATOM   2128 C  CA  . ILE B 1 57  ? 15.365  26.634  -21.571 1.00 15.61  ? 57  ILE B CA  1 
ATOM   2129 C  C   . ILE B 1 57  ? 14.570  25.351  -21.752 1.00 15.33  ? 57  ILE B C   1 
ATOM   2130 O  O   . ILE B 1 57  ? 13.474  25.380  -22.296 1.00 16.05  ? 57  ILE B O   1 
ATOM   2131 C  CB  . ILE B 1 57  ? 16.547  26.686  -22.550 1.00 19.27  ? 57  ILE B CB  1 
ATOM   2132 C  CG1 . ILE B 1 57  ? 17.255  28.041  -22.521 1.00 18.86  ? 57  ILE B CG1 1 
ATOM   2133 C  CG2 . ILE B 1 57  ? 16.034  26.314  -23.927 1.00 19.68  ? 57  ILE B CG2 1 
ATOM   2134 C  CD1 . ILE B 1 57  ? 18.676  28.044  -23.054 1.00 20.20  ? 57  ILE B CD1 1 
ATOM   2135 N  N   . TYR B 1 58  ? 15.133  24.211  -21.282 1.00 14.65  ? 58  TYR B N   1 
ATOM   2136 C  CA  . TYR B 1 58  ? 14.414  22.956  -21.469 1.00 14.05  ? 58  TYR B CA  1 
ATOM   2137 C  C   . TYR B 1 58  ? 13.178  22.849  -20.598 1.00 16.06  ? 58  TYR B C   1 
ATOM   2138 O  O   . TYR B 1 58  ? 12.200  22.217  -21.051 1.00 16.18  ? 58  TYR B O   1 
ATOM   2139 C  CB  . TYR B 1 58  ? 15.380  21.799  -21.233 1.00 15.33  ? 58  TYR B CB  1 
ATOM   2140 C  CG  . TYR B 1 58  ? 16.111  21.394  -22.483 1.00 16.08  ? 58  TYR B CG  1 
ATOM   2141 C  CD1 . TYR B 1 58  ? 15.376  20.756  -23.489 1.00 19.27  ? 58  TYR B CD1 1 
ATOM   2142 C  CD2 . TYR B 1 58  ? 17.461  21.599  -22.697 1.00 19.63  ? 58  TYR B CD2 1 
ATOM   2143 C  CE1 . TYR B 1 58  ? 16.008  20.374  -24.645 1.00 18.71  ? 58  TYR B CE1 1 
ATOM   2144 C  CE2 . TYR B 1 58  ? 18.109  21.195  -23.873 1.00 21.04  ? 58  TYR B CE2 1 
ATOM   2145 C  CZ  . TYR B 1 58  ? 17.349  20.584  -24.838 1.00 21.41  ? 58  TYR B CZ  1 
ATOM   2146 O  OH  . TYR B 1 58  ? 17.907  20.142  -26.026 1.00 23.01  ? 58  TYR B OH  1 
ATOM   2147 N  N   . VAL B 1 59  ? 13.180  23.444  -19.401 1.00 15.81  ? 59  VAL B N   1 
ATOM   2148 C  CA  . VAL B 1 59  ? 11.952  23.479  -18.592 1.00 15.17  ? 59  VAL B CA  1 
ATOM   2149 C  C   . VAL B 1 59  ? 10.811  24.105  -19.405 1.00 14.21  ? 59  VAL B C   1 
ATOM   2150 O  O   . VAL B 1 59  ? 9.687   23.605  -19.555 1.00 16.66  ? 59  VAL B O   1 
ATOM   2151 C  CB  . VAL B 1 59  ? 12.158  24.187  -17.234 1.00 14.54  ? 59  VAL B CB  1 
ATOM   2152 C  CG1 . VAL B 1 59  ? 10.823  24.519  -16.583 1.00 16.20  ? 59  VAL B CG1 1 
ATOM   2153 C  CG2 . VAL B 1 59  ? 12.989  23.316  -16.311 1.00 15.58  ? 59  VAL B CG2 1 
ATOM   2154 N  N   . ALA B 1 60  ? 11.103  25.283  -19.974 1.00 16.45  ? 60  ALA B N   1 
ATOM   2155 C  CA  . ALA B 1 60  ? 10.112  26.013  -20.783 1.00 14.63  ? 60  ALA B CA  1 
ATOM   2156 C  C   . ALA B 1 60  ? 9.671   25.257  -22.033 1.00 15.25  ? 60  ALA B C   1 
ATOM   2157 O  O   . ALA B 1 60  ? 8.492   25.132  -22.348 1.00 16.40  ? 60  ALA B O   1 
ATOM   2158 C  CB  . ALA B 1 60  ? 10.685  27.384  -21.136 1.00 17.10  ? 60  ALA B CB  1 
ATOM   2159 N  N   . LEU B 1 61  ? 10.646  24.735  -22.787 1.00 14.98  ? 61  LEU B N   1 
ATOM   2160 C  CA  . LEU B 1 61  ? 10.322  24.026  -24.006 1.00 15.23  ? 61  LEU B CA  1 
ATOM   2161 C  C   . LEU B 1 61  ? 9.468   22.807  -23.700 1.00 16.12  ? 61  LEU B C   1 
ATOM   2162 O  O   . LEU B 1 61  ? 8.472   22.528  -24.375 1.00 17.40  ? 61  LEU B O   1 
ATOM   2163 C  CB  . LEU B 1 61  ? 11.617  23.617  -24.718 1.00 16.12  ? 61  LEU B CB  1 
ATOM   2164 C  CG  . LEU B 1 61  ? 11.519  22.716  -25.942 1.00 15.74  ? 61  LEU B CG  1 
ATOM   2165 C  CD1 . LEU B 1 61  ? 10.683  23.354  -27.051 1.00 19.00  ? 61  LEU B CD1 1 
ATOM   2166 C  CD2 . LEU B 1 61  ? 12.923  22.363  -26.441 1.00 19.19  ? 61  LEU B CD2 1 
ATOM   2167 N  N   . GLU B 1 62  ? 9.858   22.061  -22.662 1.00 17.52  ? 62  GLU B N   1 
ATOM   2168 C  CA  . GLU B 1 62  ? 9.155   20.813  -22.342 1.00 16.88  ? 62  GLU B CA  1 
ATOM   2169 C  C   . GLU B 1 62  ? 7.792   21.084  -21.754 1.00 17.87  ? 62  GLU B C   1 
ATOM   2170 O  O   . GLU B 1 62  ? 6.853   20.305  -21.997 1.00 18.10  ? 62  GLU B O   1 
ATOM   2171 C  CB  . GLU B 1 62  ? 10.090  19.925  -21.492 1.00 15.90  ? 62  GLU B CB  1 
ATOM   2172 C  CG  . GLU B 1 62  ? 11.226  19.474  -22.428 1.00 16.03  ? 62  GLU B CG  1 
ATOM   2173 C  CD  . GLU B 1 62  ? 12.305  18.555  -21.907 1.00 15.72  ? 62  GLU B CD  1 
ATOM   2174 O  OE1 . GLU B 1 62  ? 12.353  18.179  -20.716 1.00 18.08  ? 62  GLU B OE1 1 
ATOM   2175 O  OE2 . GLU B 1 62  ? 13.208  18.136  -22.696 1.00 17.61  ? 62  GLU B OE2 1 
ATOM   2176 N  N   . GLU B 1 63  ? 7.622   22.162  -21.014 1.00 17.52  ? 63  GLU B N   1 
ATOM   2177 C  CA  . GLU B 1 63  ? 6.282   22.545  -20.561 1.00 19.35  ? 63  GLU B CA  1 
ATOM   2178 C  C   . GLU B 1 63  ? 5.390   22.764  -21.780 1.00 18.46  ? 63  GLU B C   1 
ATOM   2179 O  O   . GLU B 1 63  ? 4.218   22.354  -21.854 1.00 21.26  ? 63  GLU B O   1 
ATOM   2180 C  CB  . GLU B 1 63  ? 6.301   23.815  -19.693 1.00 22.98  ? 63  GLU B CB  1 
ATOM   2181 C  CG  . GLU B 1 63  ? 6.765   23.644  -18.262 1.00 28.72  ? 63  GLU B CG  1 
ATOM   2182 C  CD  . GLU B 1 63  ? 6.847   24.939  -17.477 1.00 34.96  ? 63  GLU B CD  1 
ATOM   2183 O  OE1 . GLU B 1 63  ? 6.486   26.027  -17.993 1.00 39.36  ? 63  GLU B OE1 1 
ATOM   2184 O  OE2 . GLU B 1 63  ? 7.290   24.871  -16.293 1.00 30.00  ? 63  GLU B OE2 1 
ATOM   2185 N  N   . GLU B 1 64  ? 5.936   23.482  -22.770 1.00 19.08  ? 64  GLU B N   1 
ATOM   2186 C  CA  . GLU B 1 64  ? 5.092   23.878  -23.914 1.00 19.91  ? 64  GLU B CA  1 
ATOM   2187 C  C   . GLU B 1 64  ? 4.814   22.698  -24.829 1.00 20.69  ? 64  GLU B C   1 
ATOM   2188 O  O   . GLU B 1 64  ? 3.772   22.595  -25.489 1.00 20.19  ? 64  GLU B O   1 
ATOM   2189 C  CB  . GLU B 1 64  ? 5.764   25.053  -24.650 1.00 19.72  ? 64  GLU B CB  1 
ATOM   2190 C  CG  . GLU B 1 64  ? 5.726   26.354  -23.848 1.00 19.75  ? 64  GLU B CG  1 
ATOM   2191 C  CD  . GLU B 1 64  ? 4.335   26.768  -23.394 1.00 20.90  ? 64  GLU B CD  1 
ATOM   2192 O  OE1 . GLU B 1 64  ? 3.352   26.384  -24.057 1.00 21.28  ? 64  GLU B OE1 1 
ATOM   2193 O  OE2 . GLU B 1 64  ? 4.207   27.495  -22.383 1.00 22.18  ? 64  GLU B OE2 1 
ATOM   2194 N  N   . ILE B 1 65  ? 5.762   21.760  -24.867 1.00 18.76  ? 65  ILE B N   1 
ATOM   2195 C  CA  . ILE B 1 65  ? 5.567   20.514  -25.624 1.00 19.29  ? 65  ILE B CA  1 
ATOM   2196 C  C   . ILE B 1 65  ? 4.440   19.735  -24.969 1.00 20.26  ? 65  ILE B C   1 
ATOM   2197 O  O   . ILE B 1 65  ? 3.534   19.244  -25.646 1.00 19.66  ? 65  ILE B O   1 
ATOM   2198 C  CB  . ILE B 1 65  ? 6.867   19.706  -25.758 1.00 18.27  ? 65  ILE B CB  1 
ATOM   2199 C  CG1 . ILE B 1 65  ? 7.840   20.362  -26.763 1.00 19.09  ? 65  ILE B CG1 1 
ATOM   2200 C  CG2 . ILE B 1 65  ? 6.596   18.251  -26.143 1.00 21.17  ? 65  ILE B CG2 1 
ATOM   2201 C  CD1 . ILE B 1 65  ? 9.221   19.782  -26.845 1.00 18.74  ? 65  ILE B CD1 1 
ATOM   2202 N  N   . GLU B 1 66  ? 4.494   19.676  -23.642 1.00 20.06  ? 66  GLU B N   1 
ATOM   2203 C  CA  . GLU B 1 66  ? 3.436   18.933  -22.941 1.00 22.61  ? 66  GLU B CA  1 
ATOM   2204 C  C   . GLU B 1 66  ? 2.069   19.576  -23.117 1.00 23.73  ? 66  GLU B C   1 
ATOM   2205 O  O   . GLU B 1 66  ? 1.046   18.879  -23.252 1.00 25.98  ? 66  GLU B O   1 
ATOM   2206 C  CB  . GLU B 1 66  ? 3.806   18.765  -21.472 1.00 23.97  ? 66  GLU B CB  1 
ATOM   2207 C  CG  . GLU B 1 66  ? 4.921   17.734  -21.258 1.00 27.38  ? 66  GLU B CG  1 
ATOM   2208 C  CD  . GLU B 1 66  ? 4.538   16.374  -21.825 1.00 29.51  ? 66  GLU B CD  1 
ATOM   2209 O  OE1 . GLU B 1 66  ? 3.471   15.836  -21.412 1.00 33.17  ? 66  GLU B OE1 1 
ATOM   2210 O  OE2 . GLU B 1 66  ? 5.274   15.837  -22.679 1.00 28.55  ? 66  GLU B OE2 1 
ATOM   2211 N  N   . ARG B 1 67  ? 2.011   20.913  -23.151 1.00 23.36  ? 67  ARG B N   1 
ATOM   2212 C  CA  . ARG B 1 67  ? 0.749   21.609  -23.464 1.00 21.09  ? 67  ARG B CA  1 
ATOM   2213 C  C   . ARG B 1 67  ? 0.229   21.262  -24.858 1.00 21.17  ? 67  ARG B C   1 
ATOM   2214 O  O   . ARG B 1 67  ? -0.968  21.154  -25.097 1.00 26.00  ? 67  ARG B O   1 
ATOM   2215 C  CB  . ARG B 1 67  ? 0.954   23.127  -23.333 1.00 23.69  ? 67  ARG B CB  1 
ATOM   2216 C  CG  . ARG B 1 67  ? -0.311  23.916  -23.363 1.00 29.22  ? 67  ARG B CG  1 
ATOM   2217 C  CD  A ARG B 1 67  ? -0.159  25.430  -23.430 0.50 35.37  ? 67  ARG B CD  1 
ATOM   2218 C  CD  B ARG B 1 67  ? -0.195  25.387  -23.717 0.50 32.40  ? 67  ARG B CD  1 
ATOM   2219 N  NE  A ARG B 1 67  ? -1.113  26.173  -22.629 0.50 39.58  ? 67  ARG B NE  1 
ATOM   2220 N  NE  B ARG B 1 67  ? 0.860   26.094  -22.995 0.50 28.76  ? 67  ARG B NE  1 
ATOM   2221 C  CZ  A ARG B 1 67  ? -2.432  26.051  -22.580 0.50 46.33  ? 67  ARG B CZ  1 
ATOM   2222 C  CZ  B ARG B 1 67  ? 0.817   26.321  -21.692 0.50 30.15  ? 67  ARG B CZ  1 
ATOM   2223 N  NH1 A ARG B 1 67  ? -3.140  26.834  -21.767 0.50 62.65  ? 67  ARG B NH1 1 
ATOM   2224 N  NH1 B ARG B 1 67  ? 1.805   26.969  -21.092 0.50 32.85  ? 67  ARG B NH1 1 
ATOM   2225 N  NH2 A ARG B 1 67  ? -3.076  25.163  -23.327 0.50 53.44  ? 67  ARG B NH2 1 
ATOM   2226 N  NH2 B ARG B 1 67  ? -0.228  25.889  -21.011 0.50 32.36  ? 67  ARG B NH2 1 
ATOM   2227 N  N   . ASN B 1 68  ? 1.096   21.076  -25.842 1.00 21.27  ? 68  ASN B N   1 
ATOM   2228 C  CA  . ASN B 1 68  ? 0.632   20.969  -27.225 1.00 20.88  ? 68  ASN B CA  1 
ATOM   2229 C  C   . ASN B 1 68  ? 0.800   19.586  -27.839 1.00 20.19  ? 68  ASN B C   1 
ATOM   2230 O  O   . ASN B 1 68  ? 0.622   19.450  -29.050 1.00 23.76  ? 68  ASN B O   1 
ATOM   2231 C  CB  . ASN B 1 68  ? 1.407   22.022  -28.030 1.00 22.52  ? 68  ASN B CB  1 
ATOM   2232 C  CG  . ASN B 1 68  ? 1.127   23.444  -27.613 1.00 23.90  ? 68  ASN B CG  1 
ATOM   2233 O  OD1 . ASN B 1 68  ? 1.911   24.166  -26.975 1.00 28.09  ? 68  ASN B OD1 1 
ATOM   2234 N  ND2 . ASN B 1 68  ? -0.057  23.852  -28.011 1.00 22.01  ? 68  ASN B ND2 1 
ATOM   2235 N  N   . LYS B 1 69  ? 1.183   18.577  -27.073 1.00 21.40  ? 69  LYS B N   1 
ATOM   2236 C  CA  . LYS B 1 69  ? 1.567   17.281  -27.595 1.00 22.66  ? 69  LYS B CA  1 
ATOM   2237 C  C   . LYS B 1 69  ? 0.438   16.588  -28.369 1.00 22.11  ? 69  LYS B C   1 
ATOM   2238 O  O   . LYS B 1 69  ? 0.789   15.806  -29.254 1.00 25.96  ? 69  LYS B O   1 
ATOM   2239 C  CB  . LYS B 1 69  ? 2.027   16.334  -26.496 1.00 24.63  ? 69  LYS B CB  1 
ATOM   2240 C  CG  . LYS B 1 69  ? 1.022   16.028  -25.422 1.00 24.41  ? 69  LYS B CG  1 
ATOM   2241 C  CD  . LYS B 1 69  ? 1.623   15.201  -24.272 1.00 28.64  ? 69  LYS B CD  1 
ATOM   2242 C  CE  . LYS B 1 69  ? 0.644   15.178  -23.096 1.00 32.40  ? 69  LYS B CE  1 
ATOM   2243 N  NZ  . LYS B 1 69  ? 1.008   14.222  -22.054 1.00 44.65  ? 69  LYS B NZ  1 
ATOM   2244 N  N   . GLU B 1 70  ? -0.810  16.900  -28.062 1.00 22.21  ? 70  GLU B N   1 
ATOM   2245 C  CA  . GLU B 1 70  ? -1.878  16.229  -28.796 1.00 27.27  ? 70  GLU B CA  1 
ATOM   2246 C  C   . GLU B 1 70  ? -2.312  16.982  -30.039 1.00 25.35  ? 70  GLU B C   1 
ATOM   2247 O  O   . GLU B 1 70  ? -3.112  16.484  -30.848 1.00 30.56  ? 70  GLU B O   1 
ATOM   2248 C  CB  . GLU B 1 70  ? -3.078  16.027  -27.874 1.00 37.84  ? 70  GLU B CB  1 
ATOM   2249 C  CG  . GLU B 1 70  ? -2.671  15.330  -26.569 1.00 50.07  ? 70  GLU B CG  1 
ATOM   2250 C  CD  . GLU B 1 70  ? -3.204  13.913  -26.528 1.00 60.11  ? 70  GLU B CD  1 
ATOM   2251 O  OE1 . GLU B 1 70  ? -3.728  13.448  -27.570 1.00 71.39  ? 70  GLU B OE1 1 
ATOM   2252 O  OE2 . GLU B 1 70  ? -3.092  13.278  -25.457 1.00 61.96  ? 70  GLU B OE2 1 
ATOM   2253 N  N   . SER B 1 71  ? -1.772  18.181  -30.198 1.00 26.42  ? 71  SER B N   1 
ATOM   2254 C  CA  . SER B 1 71  ? -2.202  18.958  -31.356 1.00 27.59  ? 71  SER B CA  1 
ATOM   2255 C  C   . SER B 1 71  ? -1.614  18.472  -32.659 1.00 23.96  ? 71  SER B C   1 
ATOM   2256 O  O   . SER B 1 71  ? -0.446  18.084  -32.672 1.00 28.31  ? 71  SER B O   1 
ATOM   2257 C  CB  . SER B 1 71  ? -1.759  20.399  -31.060 1.00 30.21  ? 71  SER B CB  1 
ATOM   2258 O  OG  . SER B 1 71  ? -2.222  21.222  -32.076 1.00 37.07  ? 71  SER B OG  1 
ATOM   2259 N  N   . PRO B 1 72  ? -2.278  18.495  -33.802 1.00 27.79  ? 72  PRO B N   1 
ATOM   2260 C  CA  . PRO B 1 72  ? -1.580  18.024  -35.012 1.00 29.11  ? 72  PRO B CA  1 
ATOM   2261 C  C   . PRO B 1 72  ? -0.381  18.863  -35.412 1.00 27.84  ? 72  PRO B C   1 
ATOM   2262 O  O   . PRO B 1 72  ? 0.456   18.427  -36.214 1.00 28.70  ? 72  PRO B O   1 
ATOM   2263 C  CB  . PRO B 1 72  ? -2.685  18.066  -36.083 1.00 36.32  ? 72  PRO B CB  1 
ATOM   2264 C  CG  . PRO B 1 72  ? -3.696  19.024  -35.538 1.00 38.39  ? 72  PRO B CG  1 
ATOM   2265 C  CD  . PRO B 1 72  ? -3.656  18.928  -34.035 1.00 34.36  ? 72  PRO B CD  1 
ATOM   2266 N  N   . VAL B 1 73  ? -0.170  20.073  -34.927 1.00 26.60  ? 73  VAL B N   1 
ATOM   2267 C  CA  . VAL B 1 73  ? 0.962   20.918  -35.227 1.00 26.31  ? 73  VAL B CA  1 
ATOM   2268 C  C   . VAL B 1 73  ? 2.231   20.425  -34.532 1.00 23.12  ? 73  VAL B C   1 
ATOM   2269 O  O   . VAL B 1 73  ? 3.323   20.926  -34.864 1.00 27.31  ? 73  VAL B O   1 
ATOM   2270 C  CB  . VAL B 1 73  ? 0.738   22.404  -34.875 1.00 27.69  ? 73  VAL B CB  1 
ATOM   2271 C  CG1 . VAL B 1 73  ? -0.609  22.913  -35.384 1.00 34.47  ? 73  VAL B CG1 1 
ATOM   2272 C  CG2 . VAL B 1 73  ? 0.822   22.637  -33.377 1.00 28.32  ? 73  VAL B CG2 1 
ATOM   2273 N  N   . PHE B 1 74  ? 2.107   19.473  -33.604 1.00 24.37  ? 74  PHE B N   1 
ATOM   2274 C  CA  . PHE B 1 74  ? 3.283   18.931  -32.915 1.00 22.21  ? 74  PHE B CA  1 
ATOM   2275 C  C   . PHE B 1 74  ? 3.284   17.430  -32.679 1.00 22.09  ? 74  PHE B C   1 
ATOM   2276 O  O   . PHE B 1 74  ? 4.385   16.857  -32.557 1.00 22.54  ? 74  PHE B O   1 
ATOM   2277 C  CB  . PHE B 1 74  ? 3.473   19.638  -31.558 1.00 23.41  ? 74  PHE B CB  1 
ATOM   2278 C  CG  . PHE B 1 74  ? 4.913   19.469  -31.082 1.00 21.60  ? 74  PHE B CG  1 
ATOM   2279 C  CD1 . PHE B 1 74  ? 5.857   20.425  -31.442 1.00 19.60  ? 74  PHE B CD1 1 
ATOM   2280 C  CD2 . PHE B 1 74  ? 5.319   18.404  -30.291 1.00 23.22  ? 74  PHE B CD2 1 
ATOM   2281 C  CE1 . PHE B 1 74  ? 7.142   20.238  -30.978 1.00 23.40  ? 74  PHE B CE1 1 
ATOM   2282 C  CE2 . PHE B 1 74  ? 6.626   18.212  -29.865 1.00 22.04  ? 74  PHE B CE2 1 
ATOM   2283 C  CZ  . PHE B 1 74  ? 7.568   19.154  -30.224 1.00 21.36  ? 74  PHE B CZ  1 
ATOM   2284 N  N   . ALA B 1 75  ? 2.128   16.780  -32.578 1.00 23.61  ? 75  ALA B N   1 
ATOM   2285 C  CA  . ALA B 1 75  ? 2.071   15.350  -32.281 1.00 23.72  ? 75  ALA B CA  1 
ATOM   2286 C  C   . ALA B 1 75  ? 3.008   14.521  -33.148 1.00 20.89  ? 75  ALA B C   1 
ATOM   2287 O  O   . ALA B 1 75  ? 3.668   13.642  -32.553 1.00 21.97  ? 75  ALA B O   1 
ATOM   2288 C  CB  . ALA B 1 75  ? 0.630   14.839  -32.378 1.00 25.71  ? 75  ALA B CB  1 
ATOM   2289 N  N   . PRO B 1 76  ? 3.135   14.705  -34.441 1.00 23.81  ? 76  PRO B N   1 
ATOM   2290 C  CA  . PRO B 1 76  ? 4.053   13.839  -35.205 1.00 24.56  ? 76  PRO B CA  1 
ATOM   2291 C  C   . PRO B 1 76  ? 5.510   13.899  -34.791 1.00 21.21  ? 76  PRO B C   1 
ATOM   2292 O  O   . PRO B 1 76  ? 6.267   12.993  -35.152 1.00 24.69  ? 76  PRO B O   1 
ATOM   2293 C  CB  . PRO B 1 76  ? 3.918   14.399  -36.626 1.00 25.29  ? 76  PRO B CB  1 
ATOM   2294 C  CG  . PRO B 1 76  ? 2.534   14.982  -36.670 1.00 25.92  ? 76  PRO B CG  1 
ATOM   2295 C  CD  . PRO B 1 76  ? 2.408   15.640  -35.323 1.00 26.49  ? 76  PRO B CD  1 
ATOM   2296 N  N   . VAL B 1 77  ? 5.908   14.966  -34.076 1.00 21.18  ? 77  VAL B N   1 
ATOM   2297 C  CA  . VAL B 1 77  ? 7.278   15.096  -33.621 1.00 21.90  ? 77  VAL B CA  1 
ATOM   2298 C  C   . VAL B 1 77  ? 7.367   14.962  -32.115 1.00 18.06  ? 77  VAL B C   1 
ATOM   2299 O  O   . VAL B 1 77  ? 8.390   15.327  -31.513 1.00 20.05  ? 77  VAL B O   1 
ATOM   2300 C  CB  . VAL B 1 77  ? 7.943   16.415  -34.050 1.00 21.22  ? 77  VAL B CB  1 
ATOM   2301 C  CG1 . VAL B 1 77  ? 8.165   16.337  -35.553 1.00 26.98  ? 77  VAL B CG1 1 
ATOM   2302 C  CG2 . VAL B 1 77  ? 7.144   17.652  -33.670 1.00 22.55  ? 77  VAL B CG2 1 
ATOM   2303 N  N   . TYR B 1 78  ? 6.349   14.382  -31.496 1.00 20.76  ? 78  TYR B N   1 
ATOM   2304 C  CA  . TYR B 1 78  ? 6.406   14.156  -30.041 1.00 18.73  ? 78  TYR B CA  1 
ATOM   2305 C  C   . TYR B 1 78  ? 7.103   12.851  -29.645 1.00 18.69  ? 78  TYR B C   1 
ATOM   2306 O  O   . TYR B 1 78  ? 6.541   11.771  -29.870 1.00 22.90  ? 78  TYR B O   1 
ATOM   2307 C  CB  . TYR B 1 78  ? 4.996   14.175  -29.446 1.00 19.09  ? 78  TYR B CB  1 
ATOM   2308 C  CG  . TYR B 1 78  ? 4.919   14.076  -27.943 1.00 20.37  ? 78  TYR B CG  1 
ATOM   2309 C  CD1 . TYR B 1 78  ? 5.581   14.979  -27.107 1.00 19.16  ? 78  TYR B CD1 1 
ATOM   2310 C  CD2 . TYR B 1 78  ? 4.159   13.071  -27.357 1.00 22.37  ? 78  TYR B CD2 1 
ATOM   2311 C  CE1 . TYR B 1 78  ? 5.469   14.837  -25.724 1.00 18.80  ? 78  TYR B CE1 1 
ATOM   2312 C  CE2 . TYR B 1 78  ? 4.047   12.929  -25.983 1.00 21.57  ? 78  TYR B CE2 1 
ATOM   2313 C  CZ  . TYR B 1 78  ? 4.710   13.829  -25.161 1.00 21.02  ? 78  TYR B CZ  1 
ATOM   2314 O  OH  . TYR B 1 78  ? 4.596   13.686  -23.788 1.00 21.85  ? 78  TYR B OH  1 
ATOM   2315 N  N   . PHE B 1 79  ? 8.285   12.950  -29.068 1.00 17.09  ? 79  PHE B N   1 
ATOM   2316 C  CA  . PHE B 1 79  ? 9.121   11.808  -28.693 1.00 17.93  ? 79  PHE B CA  1 
ATOM   2317 C  C   . PHE B 1 79  ? 9.675   12.013  -27.292 1.00 16.70  ? 79  PHE B C   1 
ATOM   2318 O  O   . PHE B 1 79  ? 10.848  12.280  -27.072 1.00 16.87  ? 79  PHE B O   1 
ATOM   2319 C  CB  . PHE B 1 79  ? 10.263  11.627  -29.658 1.00 17.90  ? 79  PHE B CB  1 
ATOM   2320 C  CG  . PHE B 1 79  ? 9.861   11.105  -31.039 1.00 18.96  ? 79  PHE B CG  1 
ATOM   2321 C  CD1 . PHE B 1 79  ? 9.753   9.744   -31.246 1.00 22.26  ? 79  PHE B CD1 1 
ATOM   2322 C  CD2 . PHE B 1 79  ? 9.605   11.924  -32.130 1.00 20.37  ? 79  PHE B CD2 1 
ATOM   2323 C  CE1 . PHE B 1 79  ? 9.393   9.225   -32.483 1.00 23.15  ? 79  PHE B CE1 1 
ATOM   2324 C  CE2 . PHE B 1 79  ? 9.255   11.416  -33.379 1.00 21.46  ? 79  PHE B CE2 1 
ATOM   2325 C  CZ  . PHE B 1 79  ? 9.170   10.025  -33.579 1.00 22.30  ? 79  PHE B CZ  1 
ATOM   2326 N  N   . PRO B 1 80  ? 8.760   11.906  -26.332 1.00 17.97  ? 80  PRO B N   1 
ATOM   2327 C  CA  . PRO B 1 80  ? 9.101   12.278  -24.964 1.00 17.60  ? 80  PRO B CA  1 
ATOM   2328 C  C   . PRO B 1 80  ? 10.184  11.392  -24.365 1.00 17.66  ? 80  PRO B C   1 
ATOM   2329 O  O   . PRO B 1 80  ? 11.107  12.001  -23.779 1.00 17.82  ? 80  PRO B O   1 
ATOM   2330 C  CB  . PRO B 1 80  ? 7.781   12.112  -24.181 1.00 19.91  ? 80  PRO B CB  1 
ATOM   2331 C  CG  . PRO B 1 80  ? 7.001   11.147  -25.022 1.00 20.05  ? 80  PRO B CG  1 
ATOM   2332 C  CD  . PRO B 1 80  ? 7.370   11.465  -26.456 1.00 18.81  ? 80  PRO B CD  1 
ATOM   2333 N  N   . GLU B 1 81  ? 10.085  10.074  -24.472 1.00 17.71  ? 81  GLU B N   1 
ATOM   2334 C  CA  . GLU B 1 81  ? 11.111  9.264   -23.778 1.00 17.01  ? 81  GLU B CA  1 
ATOM   2335 C  C   . GLU B 1 81  ? 12.474  9.455   -24.415 1.00 16.42  ? 81  GLU B C   1 
ATOM   2336 O  O   . GLU B 1 81  ? 13.511  9.502   -23.750 1.00 17.33  ? 81  GLU B O   1 
ATOM   2337 C  CB  . GLU B 1 81  ? 10.629  7.814   -23.796 1.00 18.31  ? 81  GLU B CB  1 
ATOM   2338 C  CG  . GLU B 1 81  ? 9.366   7.586   -22.986 1.00 24.55  ? 81  GLU B CG  1 
ATOM   2339 C  CD  . GLU B 1 81  ? 9.449   8.031   -21.543 1.00 28.51  ? 81  GLU B CD  1 
ATOM   2340 O  OE1 . GLU B 1 81  ? 10.403  7.592   -20.866 1.00 30.15  ? 81  GLU B OE1 1 
ATOM   2341 O  OE2 . GLU B 1 81  ? 8.614   8.787   -20.971 1.00 42.36  ? 81  GLU B OE2 1 
ATOM   2342 N  N   . GLU B 1 82  ? 12.499  9.594   -25.747 1.00 17.08  ? 82  GLU B N   1 
ATOM   2343 C  CA  . GLU B 1 82  ? 13.763  9.700   -26.473 1.00 16.54  ? 82  GLU B CA  1 
ATOM   2344 C  C   . GLU B 1 82  ? 14.529  11.000  -26.210 1.00 16.17  ? 82  GLU B C   1 
ATOM   2345 O  O   . GLU B 1 82  ? 15.772  10.959  -26.159 1.00 16.88  ? 82  GLU B O   1 
ATOM   2346 C  CB  . GLU B 1 82  ? 13.557  9.536   -27.998 1.00 18.48  ? 82  GLU B CB  1 
ATOM   2347 C  CG  . GLU B 1 82  ? 13.129  8.127   -28.375 1.00 22.47  ? 82  GLU B CG  1 
ATOM   2348 C  CD  . GLU B 1 82  ? 11.657  7.826   -28.166 1.00 24.33  ? 82  GLU B CD  1 
ATOM   2349 O  OE1 . GLU B 1 82  ? 10.827  8.740   -27.912 1.00 20.81  ? 82  GLU B OE1 1 
ATOM   2350 O  OE2 . GLU B 1 82  ? 11.355  6.615   -28.247 1.00 28.48  ? 82  GLU B OE2 1 
ATOM   2351 N  N   . LEU B 1 83  ? 13.795  12.116  -26.108 1.00 15.58  ? 83  LEU B N   1 
ATOM   2352 C  CA  . LEU B 1 83  ? 14.428  13.442  -26.118 1.00 16.37  ? 83  LEU B CA  1 
ATOM   2353 C  C   . LEU B 1 83  ? 14.390  14.170  -24.793 1.00 16.55  ? 83  LEU B C   1 
ATOM   2354 O  O   . LEU B 1 83  ? 15.242  15.086  -24.677 1.00 17.44  ? 83  LEU B O   1 
ATOM   2355 C  CB  . LEU B 1 83  ? 13.764  14.319  -27.230 1.00 19.17  ? 83  LEU B CB  1 
ATOM   2356 C  CG  . LEU B 1 83  ? 14.063  13.840  -28.663 1.00 18.86  ? 83  LEU B CG  1 
ATOM   2357 C  CD1 . LEU B 1 83  ? 13.210  14.633  -29.654 1.00 19.38  ? 83  LEU B CD1 1 
ATOM   2358 C  CD2 . LEU B 1 83  ? 15.539  13.929  -28.984 1.00 18.93  ? 83  LEU B CD2 1 
ATOM   2359 N  N   . HIS B 1 84  ? 13.497  13.858  -23.854 1.00 15.34  ? 84  HIS B N   1 
ATOM   2360 C  CA  . HIS B 1 84  ? 13.369  14.760  -22.703 1.00 15.80  ? 84  HIS B CA  1 
ATOM   2361 C  C   . HIS B 1 84  ? 14.702  14.978  -21.971 1.00 15.48  ? 84  HIS B C   1 
ATOM   2362 O  O   . HIS B 1 84  ? 15.473  14.028  -21.801 1.00 15.27  ? 84  HIS B O   1 
ATOM   2363 C  CB  . HIS B 1 84  ? 12.302  14.249  -21.753 1.00 17.46  ? 84  HIS B CB  1 
ATOM   2364 C  CG  . HIS B 1 84  ? 12.631  13.090  -20.876 1.00 17.85  ? 84  HIS B CG  1 
ATOM   2365 N  ND1 . HIS B 1 84  ? 12.714  11.749  -21.191 1.00 25.72  ? 84  HIS B ND1 1 
ATOM   2366 C  CD2 . HIS B 1 84  ? 12.924  13.139  -19.533 1.00 14.37  ? 84  HIS B CD2 1 
ATOM   2367 C  CE1 . HIS B 1 84  ? 13.022  11.037  -20.121 1.00 19.05  ? 84  HIS B CE1 1 
ATOM   2368 N  NE2 . HIS B 1 84  ? 13.153  11.866  -19.103 1.00 20.03  ? 84  HIS B NE2 1 
ATOM   2369 N  N   . ARG B 1 85  ? 14.972  16.230  -21.636 1.00 13.64  ? 85  ARG B N   1 
ATOM   2370 C  CA  . ARG B 1 85  ? 16.220  16.639  -21.017 1.00 14.66  ? 85  ARG B CA  1 
ATOM   2371 C  C   . ARG B 1 85  ? 16.077  17.255  -19.638 1.00 13.05  ? 85  ARG B C   1 
ATOM   2372 O  O   . ARG B 1 85  ? 17.079  17.354  -18.929 1.00 15.43  ? 85  ARG B O   1 
ATOM   2373 C  CB  . ARG B 1 85  ? 16.984  17.657  -21.891 1.00 15.06  ? 85  ARG B CB  1 
ATOM   2374 C  CG  . ARG B 1 85  ? 17.528  17.105  -23.207 1.00 16.05  ? 85  ARG B CG  1 
ATOM   2375 C  CD  . ARG B 1 85  ? 18.681  16.141  -23.014 1.00 17.08  ? 85  ARG B CD  1 
ATOM   2376 N  NE  . ARG B 1 85  ? 18.206  14.787  -22.693 1.00 16.78  ? 85  ARG B NE  1 
ATOM   2377 C  CZ  . ARG B 1 85  ? 18.961  13.855  -22.123 1.00 18.43  ? 85  ARG B CZ  1 
ATOM   2378 N  NH1 . ARG B 1 85  ? 20.220  14.117  -21.809 1.00 17.25  ? 85  ARG B NH1 1 
ATOM   2379 N  NH2 . ARG B 1 85  ? 18.325  12.702  -21.932 1.00 18.96  ? 85  ARG B NH2 1 
ATOM   2380 N  N   . LYS B 1 86  ? 14.879  17.669  -19.217 1.00 15.68  ? 86  LYS B N   1 
ATOM   2381 C  CA  . LYS B 1 86  ? 14.796  18.279  -17.893 1.00 15.20  ? 86  LYS B CA  1 
ATOM   2382 C  C   . LYS B 1 86  ? 15.333  17.401  -16.772 1.00 15.37  ? 86  LYS B C   1 
ATOM   2383 O  O   . LYS B 1 86  ? 16.109  17.916  -15.956 1.00 16.23  ? 86  LYS B O   1 
ATOM   2384 C  CB  . LYS B 1 86  ? 13.333  18.642  -17.559 1.00 16.51  ? 86  LYS B CB  1 
ATOM   2385 C  CG  . LYS B 1 86  ? 13.168  19.364  -16.234 1.00 16.98  ? 86  LYS B CG  1 
ATOM   2386 C  CD  . LYS B 1 86  ? 11.674  19.579  -15.944 1.00 19.38  ? 86  LYS B CD  1 
ATOM   2387 C  CE  A LYS B 1 86  ? 11.041  18.303  -15.420 0.50 22.15  ? 86  LYS B CE  1 
ATOM   2388 C  CE  B LYS B 1 86  ? 10.950  18.276  -15.667 0.50 22.57  ? 86  LYS B CE  1 
ATOM   2389 N  NZ  A LYS B 1 86  ? 10.439  18.486  -14.067 0.50 26.61  ? 86  LYS B NZ  1 
ATOM   2390 N  NZ  B LYS B 1 86  ? 9.506   18.409  -15.312 0.50 20.95  ? 86  LYS B NZ  1 
ATOM   2391 N  N   . ALA B 1 87  ? 14.938  16.143  -16.722 1.00 14.21  ? 87  ALA B N   1 
ATOM   2392 C  CA  . ALA B 1 87  ? 15.421  15.294  -15.629 1.00 15.03  ? 87  ALA B CA  1 
ATOM   2393 C  C   . ALA B 1 87  ? 16.934  15.133  -15.653 1.00 14.23  ? 87  ALA B C   1 
ATOM   2394 O  O   . ALA B 1 87  ? 17.504  15.124  -14.563 1.00 14.29  ? 87  ALA B O   1 
ATOM   2395 C  CB  . ALA B 1 87  ? 14.785  13.919  -15.675 1.00 17.75  ? 87  ALA B CB  1 
ATOM   2396 N  N   . ALA B 1 88  ? 17.551  14.986  -16.823 1.00 13.81  ? 88  ALA B N   1 
ATOM   2397 C  CA  . ALA B 1 88  ? 19.019  14.910  -16.896 1.00 13.59  ? 88  ALA B CA  1 
ATOM   2398 C  C   . ALA B 1 88  ? 19.652  16.170  -16.312 1.00 13.48  ? 88  ALA B C   1 
ATOM   2399 O  O   . ALA B 1 88  ? 20.638  16.133  -15.603 1.00 14.22  ? 88  ALA B O   1 
ATOM   2400 C  CB  . ALA B 1 88  ? 19.424  14.707  -18.332 1.00 15.41  ? 88  ALA B CB  1 
ATOM   2401 N  N   . LEU B 1 89  ? 19.068  17.323  -16.670 1.00 13.15  ? 89  LEU B N   1 
ATOM   2402 C  CA  . LEU B 1 89  ? 19.614  18.586  -16.182 1.00 14.45  ? 89  LEU B CA  1 
ATOM   2403 C  C   . LEU B 1 89  ? 19.411  18.783  -14.692 1.00 13.25  ? 89  LEU B C   1 
ATOM   2404 O  O   . LEU B 1 89  ? 20.290  19.369  -14.013 1.00 14.74  ? 89  LEU B O   1 
ATOM   2405 C  CB  . LEU B 1 89  ? 19.033  19.716  -17.049 1.00 14.12  ? 89  LEU B CB  1 
ATOM   2406 C  CG  . LEU B 1 89  ? 19.635  19.819  -18.435 1.00 14.78  ? 89  LEU B CG  1 
ATOM   2407 C  CD1 . LEU B 1 89  ? 18.700  20.566  -19.394 1.00 19.33  ? 89  LEU B CD1 1 
ATOM   2408 C  CD2 . LEU B 1 89  ? 20.992  20.517  -18.431 1.00 16.53  ? 89  LEU B CD2 1 
ATOM   2409 N  N   . GLU B 1 90  ? 18.283  18.303  -14.150 1.00 14.87  ? 90  GLU B N   1 
ATOM   2410 C  CA  . GLU B 1 90  ? 18.106  18.323  -12.699 1.00 14.14  ? 90  GLU B CA  1 
ATOM   2411 C  C   . GLU B 1 90  ? 19.221  17.535  -12.009 1.00 16.28  ? 90  GLU B C   1 
ATOM   2412 O  O   . GLU B 1 90  ? 19.859  17.992  -11.054 1.00 15.71  ? 90  GLU B O   1 
ATOM   2413 C  CB  . GLU B 1 90  ? 16.747  17.745  -12.315 1.00 14.22  ? 90  GLU B CB  1 
ATOM   2414 C  CG  . GLU B 1 90  ? 15.580  18.628  -12.763 1.00 15.34  ? 90  GLU B CG  1 
ATOM   2415 C  CD  . GLU B 1 90  ? 14.230  17.956  -12.698 1.00 15.06  ? 90  GLU B CD  1 
ATOM   2416 O  OE1 . GLU B 1 90  ? 14.192  16.708  -12.633 1.00 16.46  ? 90  GLU B OE1 1 
ATOM   2417 O  OE2 . GLU B 1 90  ? 13.213  18.682  -12.766 1.00 17.91  ? 90  GLU B OE2 1 
ATOM   2418 N  N   . GLN B 1 91  ? 19.471  16.324  -12.524 1.00 13.82  ? 91  GLN B N   1 
ATOM   2419 C  CA  . GLN B 1 91  ? 20.580  15.520  -12.006 1.00 12.91  ? 91  GLN B CA  1 
ATOM   2420 C  C   . GLN B 1 91  ? 21.910  16.273  -12.026 1.00 12.98  ? 91  GLN B C   1 
ATOM   2421 O  O   . GLN B 1 91  ? 22.617  16.303  -11.043 1.00 13.85  ? 91  GLN B O   1 
ATOM   2422 C  CB  . GLN B 1 91  ? 20.730  14.209  -12.801 1.00 14.18  ? 91  GLN B CB  1 
ATOM   2423 C  CG  . GLN B 1 91  ? 19.563  13.253  -12.681 1.00 13.94  ? 91  GLN B CG  1 
ATOM   2424 C  CD  . GLN B 1 91  ? 19.621  12.562  -11.323 1.00 16.95  ? 91  GLN B CD  1 
ATOM   2425 O  OE1 . GLN B 1 91  ? 20.481  12.397  -10.462 1.00 18.40  ? 91  GLN B OE1 1 
ATOM   2426 N  NE2 . GLN B 1 91  ? 18.441  11.999  -11.190 1.00 13.56  ? 91  GLN B NE2 1 
ATOM   2427 N  N   . ASP B 1 92  ? 22.217  16.866  -13.175 1.00 14.63  ? 92  ASP B N   1 
ATOM   2428 C  CA  . ASP B 1 92  ? 23.507  17.531  -13.335 1.00 14.52  ? 92  ASP B CA  1 
ATOM   2429 C  C   . ASP B 1 92  ? 23.655  18.753  -12.431 1.00 14.11  ? 92  ASP B C   1 
ATOM   2430 O  O   . ASP B 1 92  ? 24.687  18.999  -11.816 1.00 15.79  ? 92  ASP B O   1 
ATOM   2431 C  CB  . ASP B 1 92  ? 23.724  17.918  -14.785 1.00 15.48  ? 92  ASP B CB  1 
ATOM   2432 C  CG  . ASP B 1 92  ? 23.993  16.704  -15.686 1.00 17.89  ? 92  ASP B CG  1 
ATOM   2433 O  OD1 . ASP B 1 92  ? 24.351  15.622  -15.156 1.00 16.63  ? 92  ASP B OD1 1 
ATOM   2434 O  OD2 . ASP B 1 92  ? 23.841  16.925  -16.918 1.00 17.06  ? 92  ASP B OD2 1 
ATOM   2435 N  N   . LEU B 1 93  ? 22.601  19.538  -12.341 1.00 15.26  ? 93  LEU B N   1 
ATOM   2436 C  CA  . LEU B 1 93  ? 22.673  20.740  -11.495 1.00 15.64  ? 93  LEU B CA  1 
ATOM   2437 C  C   . LEU B 1 93  ? 22.726  20.409  -10.013 1.00 14.66  ? 93  LEU B C   1 
ATOM   2438 O  O   . LEU B 1 93  ? 23.330  21.164  -9.233  1.00 16.57  ? 93  LEU B O   1 
ATOM   2439 C  CB  . LEU B 1 93  ? 21.500  21.653  -11.799 1.00 14.13  ? 93  LEU B CB  1 
ATOM   2440 C  CG  . LEU B 1 93  ? 21.500  22.333  -13.160 1.00 13.95  ? 93  LEU B CG  1 
ATOM   2441 C  CD1 . LEU B 1 93  ? 20.208  23.117  -13.336 1.00 20.47  ? 93  LEU B CD1 1 
ATOM   2442 C  CD2 . LEU B 1 93  ? 22.739  23.214  -13.317 1.00 17.18  ? 93  LEU B CD2 1 
ATOM   2443 N  N   . ALA B 1 94  ? 22.170  19.291  -9.557  1.00 15.32  ? 94  ALA B N   1 
ATOM   2444 C  CA  . ALA B 1 94  ? 22.381  18.906  -8.153  1.00 16.43  ? 94  ALA B CA  1 
ATOM   2445 C  C   . ALA B 1 94  ? 23.850  18.641  -7.876  1.00 16.21  ? 94  ALA B C   1 
ATOM   2446 O  O   . ALA B 1 94  ? 24.338  18.924  -6.785  1.00 19.45  ? 94  ALA B O   1 
ATOM   2447 C  CB  . ALA B 1 94  ? 21.506  17.693  -7.859  1.00 17.12  ? 94  ALA B CB  1 
ATOM   2448 N  N   . PHE B 1 95  ? 24.570  18.102  -8.861  1.00 15.86  ? 95  PHE B N   1 
ATOM   2449 C  CA  . PHE B 1 95  ? 26.020  17.937  -8.722  1.00 17.29  ? 95  PHE B CA  1 
ATOM   2450 C  C   . PHE B 1 95  ? 26.735  19.264  -8.752  1.00 17.04  ? 95  PHE B C   1 
ATOM   2451 O  O   . PHE B 1 95  ? 27.562  19.520  -7.885  1.00 20.51  ? 95  PHE B O   1 
ATOM   2452 C  CB  . PHE B 1 95  ? 26.538  17.034  -9.846  1.00 16.86  ? 95  PHE B CB  1 
ATOM   2453 C  CG  . PHE B 1 95  ? 28.034  17.009  -9.974  1.00 17.92  ? 95  PHE B CG  1 
ATOM   2454 C  CD1 . PHE B 1 95  ? 28.762  16.225  -9.110  1.00 19.33  ? 95  PHE B CD1 1 
ATOM   2455 C  CD2 . PHE B 1 95  ? 28.654  17.773  -10.956 1.00 18.87  ? 95  PHE B CD2 1 
ATOM   2456 C  CE1 . PHE B 1 95  ? 30.143  16.214  -9.195  1.00 22.07  ? 95  PHE B CE1 1 
ATOM   2457 C  CE2 . PHE B 1 95  ? 30.033  17.752  -11.031 1.00 19.49  ? 95  PHE B CE2 1 
ATOM   2458 C  CZ  . PHE B 1 95  ? 30.771  16.966  -10.161 1.00 21.74  ? 95  PHE B CZ  1 
ATOM   2459 N  N   . TRP B 1 96  ? 26.458  20.123  -9.740  1.00 18.83  ? 96  TRP B N   1 
ATOM   2460 C  CA  . TRP B 1 96  ? 27.230  21.352  -9.939  1.00 18.46  ? 96  TRP B CA  1 
ATOM   2461 C  C   . TRP B 1 96  ? 26.936  22.429  -8.888  1.00 19.61  ? 96  TRP B C   1 
ATOM   2462 O  O   . TRP B 1 96  ? 27.837  23.226  -8.553  1.00 22.75  ? 96  TRP B O   1 
ATOM   2463 C  CB  . TRP B 1 96  ? 27.012  21.921  -11.360 1.00 18.19  ? 96  TRP B CB  1 
ATOM   2464 C  CG  . TRP B 1 96  ? 27.692  21.097  -12.411 1.00 18.09  ? 96  TRP B CG  1 
ATOM   2465 C  CD1 . TRP B 1 96  ? 27.073  20.248  -13.304 1.00 17.76  ? 96  TRP B CD1 1 
ATOM   2466 C  CD2 . TRP B 1 96  ? 29.100  21.030  -12.679 1.00 19.33  ? 96  TRP B CD2 1 
ATOM   2467 N  NE1 . TRP B 1 96  ? 28.025  19.669  -14.104 1.00 19.27  ? 96  TRP B NE1 1 
ATOM   2468 C  CE2 . TRP B 1 96  ? 29.271  20.127  -13.748 1.00 20.01  ? 96  TRP B CE2 1 
ATOM   2469 C  CE3 . TRP B 1 96  ? 30.219  21.648  -12.126 1.00 19.90  ? 96  TRP B CE3 1 
ATOM   2470 C  CZ2 . TRP B 1 96  ? 30.535  19.833  -14.259 1.00 23.60  ? 96  TRP B CZ2 1 
ATOM   2471 C  CZ3 . TRP B 1 96  ? 31.463  21.344  -12.648 1.00 22.96  ? 96  TRP B CZ3 1 
ATOM   2472 C  CH2 . TRP B 1 96  ? 31.629  20.459  -13.692 1.00 23.41  ? 96  TRP B CH2 1 
ATOM   2473 N  N   . TYR B 1 97  ? 25.724  22.467  -8.342  1.00 18.85  ? 97  TYR B N   1 
ATOM   2474 C  CA  . TYR B 1 97  ? 25.385  23.517  -7.380  1.00 19.40  ? 97  TYR B CA  1 
ATOM   2475 C  C   . TYR B 1 97  ? 24.985  22.968  -6.019  1.00 19.34  ? 97  TYR B C   1 
ATOM   2476 O  O   . TYR B 1 97  ? 24.794  23.766  -5.089  1.00 23.87  ? 97  TYR B O   1 
ATOM   2477 C  CB  . TYR B 1 97  ? 24.260  24.350  -7.940  1.00 17.83  ? 97  TYR B CB  1 
ATOM   2478 C  CG  . TYR B 1 97  ? 24.566  25.264  -9.109  1.00 17.64  ? 97  TYR B CG  1 
ATOM   2479 C  CD1 . TYR B 1 97  ? 24.582  24.867  -10.434 1.00 18.12  ? 97  TYR B CD1 1 
ATOM   2480 C  CD2 . TYR B 1 97  ? 24.846  26.624  -8.890  1.00 22.99  ? 97  TYR B CD2 1 
ATOM   2481 C  CE1 . TYR B 1 97  ? 24.865  25.728  -11.483 1.00 19.20  ? 97  TYR B CE1 1 
ATOM   2482 C  CE2 . TYR B 1 97  ? 25.127  27.510  -9.933  1.00 22.07  ? 97  TYR B CE2 1 
ATOM   2483 C  CZ  . TYR B 1 97  ? 25.138  27.060  -11.248 1.00 21.30  ? 97  TYR B CZ  1 
ATOM   2484 O  OH  . TYR B 1 97  ? 25.403  27.912  -12.299 1.00 24.72  ? 97  TYR B OH  1 
ATOM   2485 N  N   . GLY B 1 98  ? 24.866  21.659  -5.911  1.00 17.57  ? 98  GLY B N   1 
ATOM   2486 C  CA  . GLY B 1 98  ? 24.464  21.081  -4.634  1.00 18.55  ? 98  GLY B CA  1 
ATOM   2487 C  C   . GLY B 1 98  ? 22.968  20.905  -4.487  1.00 18.02  ? 98  GLY B C   1 
ATOM   2488 O  O   . GLY B 1 98  ? 22.126  21.144  -5.368  1.00 18.05  ? 98  GLY B O   1 
ATOM   2489 N  N   . PRO B 1 99  ? 22.553  20.380  -3.331  1.00 19.49  ? 99  PRO B N   1 
ATOM   2490 C  CA  . PRO B 1 99  ? 21.155  19.975  -3.154  1.00 20.23  ? 99  PRO B CA  1 
ATOM   2491 C  C   . PRO B 1 99  ? 20.143  21.118  -3.213  1.00 21.15  ? 99  PRO B C   1 
ATOM   2492 O  O   . PRO B 1 99  ? 18.958  20.852  -3.476  1.00 24.17  ? 99  PRO B O   1 
ATOM   2493 C  CB  . PRO B 1 99  ? 21.127  19.319  -1.765  1.00 23.70  ? 99  PRO B CB  1 
ATOM   2494 C  CG  . PRO B 1 99  ? 22.360  19.783  -1.098  1.00 26.23  ? 99  PRO B CG  1 
ATOM   2495 C  CD  . PRO B 1 99  ? 23.375  20.063  -2.159  1.00 23.28  ? 99  PRO B CD  1 
ATOM   2496 N  N   . ARG B 1 100 ? 20.570  22.337  -2.954  1.00 20.50  ? 100 ARG B N   1 
ATOM   2497 C  CA  . ARG B 1 100 ? 19.637  23.469  -3.030  1.00 22.39  ? 100 ARG B CA  1 
ATOM   2498 C  C   . ARG B 1 100 ? 19.842  24.217  -4.343  1.00 20.93  ? 100 ARG B C   1 
ATOM   2499 O  O   . ARG B 1 100 ? 19.529  25.410  -4.446  1.00 22.30  ? 100 ARG B O   1 
ATOM   2500 C  CB  . ARG B 1 100 ? 19.798  24.374  -1.817  1.00 26.77  ? 100 ARG B CB  1 
ATOM   2501 C  CG  . ARG B 1 100 ? 19.495  23.683  -0.524  1.00 27.63  ? 100 ARG B CG  1 
ATOM   2502 C  CD  . ARG B 1 100 ? 19.193  24.646  0.610   1.00 40.86  ? 100 ARG B CD  1 
ATOM   2503 N  NE  . ARG B 1 100 ? 18.440  23.918  1.647   1.00 51.81  ? 100 ARG B NE  1 
ATOM   2504 C  CZ  . ARG B 1 100 ? 17.218  23.411  1.552   1.00 60.46  ? 100 ARG B CZ  1 
ATOM   2505 N  NH1 . ARG B 1 100 ? 16.479  23.503  0.448   1.00 77.44  ? 100 ARG B NH1 1 
ATOM   2506 N  NH2 . ARG B 1 100 ? 16.739  22.790  2.629   1.00 60.92  ? 100 ARG B NH2 1 
ATOM   2507 N  N   . TRP B 1 101 ? 20.304  23.509  -5.367  1.00 20.16  ? 101 TRP B N   1 
ATOM   2508 C  CA  . TRP B 1 101 ? 20.517  24.131  -6.677  1.00 17.47  ? 101 TRP B CA  1 
ATOM   2509 C  C   . TRP B 1 101 ? 19.336  24.931  -7.181  1.00 18.10  ? 101 TRP B C   1 
ATOM   2510 O  O   . TRP B 1 101 ? 19.530  26.019  -7.743  1.00 19.55  ? 101 TRP B O   1 
ATOM   2511 C  CB  . TRP B 1 101 ? 20.865  23.061  -7.710  1.00 17.49  ? 101 TRP B CB  1 
ATOM   2512 C  CG  . TRP B 1 101 ? 19.785  22.065  -7.984  1.00 16.18  ? 101 TRP B CG  1 
ATOM   2513 C  CD1 . TRP B 1 101 ? 19.577  20.895  -7.289  1.00 18.68  ? 101 TRP B CD1 1 
ATOM   2514 C  CD2 . TRP B 1 101 ? 18.768  22.114  -8.984  1.00 15.58  ? 101 TRP B CD2 1 
ATOM   2515 N  NE1 . TRP B 1 101 ? 18.501  20.231  -7.814  1.00 18.14  ? 101 TRP B NE1 1 
ATOM   2516 C  CE2 . TRP B 1 101 ? 17.981  20.953  -8.853  1.00 15.05  ? 101 TRP B CE2 1 
ATOM   2517 C  CE3 . TRP B 1 101 ? 18.457  23.042  -9.988  1.00 18.28  ? 101 TRP B CE3 1 
ATOM   2518 C  CZ2 . TRP B 1 101 ? 16.903  20.720  -9.699  1.00 17.32  ? 101 TRP B CZ2 1 
ATOM   2519 C  CZ3 . TRP B 1 101 ? 17.383  22.798  -10.821 1.00 18.80  ? 101 TRP B CZ3 1 
ATOM   2520 C  CH2 . TRP B 1 101 ? 16.614  21.639  -10.667 1.00 17.24  ? 101 TRP B CH2 1 
ATOM   2521 N  N   . GLN B 1 102 ? 18.118  24.440  -6.987  1.00 18.91  ? 102 GLN B N   1 
ATOM   2522 C  CA  . GLN B 1 102 ? 17.012  25.163  -7.622  1.00 23.29  ? 102 GLN B CA  1 
ATOM   2523 C  C   . GLN B 1 102 ? 16.873  26.563  -7.043  1.00 25.82  ? 102 GLN B C   1 
ATOM   2524 O  O   . GLN B 1 102 ? 16.411  27.455  -7.772  1.00 28.70  ? 102 GLN B O   1 
ATOM   2525 C  CB  . GLN B 1 102 ? 15.687  24.377  -7.498  1.00 25.20  ? 102 GLN B CB  1 
ATOM   2526 C  CG  . GLN B 1 102 ? 14.679  24.853  -8.553  1.00 30.22  ? 102 GLN B CG  1 
ATOM   2527 C  CD  . GLN B 1 102 ? 13.437  23.987  -8.615  1.00 32.05  ? 102 GLN B CD  1 
ATOM   2528 O  OE1 . GLN B 1 102 ? 12.614  24.135  -9.528  1.00 35.85  ? 102 GLN B OE1 1 
ATOM   2529 N  NE2 . GLN B 1 102 ? 13.293  23.089  -7.639  1.00 39.14  ? 102 GLN B NE2 1 
ATOM   2530 N  N   . GLU B 1 103 ? 17.261  26.766  -5.787  1.00 23.91  ? 103 GLU B N   1 
ATOM   2531 C  CA  . GLU B 1 103 ? 17.221  28.060  -5.095  1.00 25.24  ? 103 GLU B CA  1 
ATOM   2532 C  C   . GLU B 1 103 ? 18.348  29.007  -5.507  1.00 26.83  ? 103 GLU B C   1 
ATOM   2533 O  O   . GLU B 1 103 ? 18.311  30.236  -5.402  1.00 34.07  ? 103 GLU B O   1 
ATOM   2534 C  CB  . GLU B 1 103 ? 17.309  27.852  -3.575  1.00 29.51  ? 103 GLU B CB  1 
ATOM   2535 C  CG  . GLU B 1 103 ? 16.185  27.062  -2.946  1.00 38.39  ? 103 GLU B CG  1 
ATOM   2536 C  CD  . GLU B 1 103 ? 16.542  26.590  -1.536  1.00 44.34  ? 103 GLU B CD  1 
ATOM   2537 O  OE1 . GLU B 1 103 ? 17.042  27.485  -0.812  1.00 52.43  ? 103 GLU B OE1 1 
ATOM   2538 O  OE2 . GLU B 1 103 ? 16.334  25.396  -1.194  1.00 40.67  ? 103 GLU B OE2 1 
ATOM   2539 N  N   . VAL B 1 104 ? 19.471  28.455  -5.968  1.00 21.60  ? 104 VAL B N   1 
ATOM   2540 C  CA  . VAL B 1 104 ? 20.663  29.286  -6.140  1.00 22.14  ? 104 VAL B CA  1 
ATOM   2541 C  C   . VAL B 1 104 ? 21.073  29.436  -7.614  1.00 19.63  ? 104 VAL B C   1 
ATOM   2542 O  O   . VAL B 1 104 ? 21.887  30.344  -7.875  1.00 20.38  ? 104 VAL B O   1 
ATOM   2543 C  CB  . VAL B 1 104 ? 21.864  28.781  -5.309  1.00 23.35  ? 104 VAL B CB  1 
ATOM   2544 C  CG1 . VAL B 1 104 ? 21.556  28.733  -3.804  1.00 37.15  ? 104 VAL B CG1 1 
ATOM   2545 C  CG2 . VAL B 1 104 ? 22.338  27.395  -5.726  1.00 24.40  ? 104 VAL B CG2 1 
ATOM   2546 N  N   . ILE B 1 105 ? 20.566  28.612  -8.527  1.00 17.28  ? 105 ILE B N   1 
ATOM   2547 C  CA  . ILE B 1 105 ? 21.023  28.832  -9.900  1.00 17.91  ? 105 ILE B CA  1 
ATOM   2548 C  C   . ILE B 1 105 ? 20.637  30.228  -10.395 1.00 18.10  ? 105 ILE B C   1 
ATOM   2549 O  O   . ILE B 1 105 ? 19.590  30.761  -10.015 1.00 18.56  ? 105 ILE B O   1 
ATOM   2550 C  CB  . ILE B 1 105 ? 20.484  27.756  -10.879 1.00 17.59  ? 105 ILE B CB  1 
ATOM   2551 C  CG1 . ILE B 1 105 ? 18.977  27.642  -10.839 1.00 18.35  ? 105 ILE B CG1 1 
ATOM   2552 C  CG2 . ILE B 1 105 ? 21.221  26.434  -10.617 1.00 19.50  ? 105 ILE B CG2 1 
ATOM   2553 C  CD1 . ILE B 1 105 ? 18.429  26.765  -11.942 1.00 19.13  ? 105 ILE B CD1 1 
ATOM   2554 N  N   . PRO B 1 106 ? 21.520  30.780  -11.240 1.00 17.11  ? 106 PRO B N   1 
ATOM   2555 C  CA  . PRO B 1 106 ? 21.243  32.084  -11.857 1.00 18.38  ? 106 PRO B CA  1 
ATOM   2556 C  C   . PRO B 1 106 ? 20.093  31.995  -12.865 1.00 17.89  ? 106 PRO B C   1 
ATOM   2557 O  O   . PRO B 1 106 ? 19.842  30.946  -13.456 1.00 19.69  ? 106 PRO B O   1 
ATOM   2558 C  CB  . PRO B 1 106 ? 22.566  32.456  -12.549 1.00 20.54  ? 106 PRO B CB  1 
ATOM   2559 C  CG  . PRO B 1 106 ? 23.142  31.115  -12.887 1.00 21.81  ? 106 PRO B CG  1 
ATOM   2560 C  CD  . PRO B 1 106 ? 22.812  30.243  -11.692 1.00 18.22  ? 106 PRO B CD  1 
ATOM   2561 N  N   . TYR B 1 107 ? 19.397  33.108  -13.086 1.00 19.01  ? 107 TYR B N   1 
ATOM   2562 C  CA  . TYR B 1 107 ? 18.351  33.309  -14.075 1.00 16.02  ? 107 TYR B CA  1 
ATOM   2563 C  C   . TYR B 1 107 ? 18.539  34.715  -14.643 1.00 16.46  ? 107 TYR B C   1 
ATOM   2564 O  O   . TYR B 1 107 ? 18.061  35.694  -14.066 1.00 20.90  ? 107 TYR B O   1 
ATOM   2565 C  CB  . TYR B 1 107 ? 16.945  33.158  -13.483 1.00 17.60  ? 107 TYR B CB  1 
ATOM   2566 C  CG  . TYR B 1 107 ? 15.841  33.169  -14.521 1.00 17.11  ? 107 TYR B CG  1 
ATOM   2567 C  CD1 . TYR B 1 107 ? 15.916  32.400  -15.673 1.00 19.15  ? 107 TYR B CD1 1 
ATOM   2568 C  CD2 . TYR B 1 107 ? 14.716  33.976  -14.348 1.00 18.61  ? 107 TYR B CD2 1 
ATOM   2569 C  CE1 . TYR B 1 107 ? 14.933  32.413  -16.623 1.00 20.23  ? 107 TYR B CE1 1 
ATOM   2570 C  CE2 . TYR B 1 107 ? 13.725  33.976  -15.303 1.00 19.26  ? 107 TYR B CE2 1 
ATOM   2571 C  CZ  . TYR B 1 107 ? 13.813  33.196  -16.457 1.00 18.57  ? 107 TYR B CZ  1 
ATOM   2572 O  OH  . TYR B 1 107 ? 12.839  33.141  -17.450 1.00 19.57  ? 107 TYR B OH  1 
ATOM   2573 N  N   . THR B 1 108 ? 19.269  34.836  -15.727 1.00 18.36  ? 108 THR B N   1 
ATOM   2574 C  CA  . THR B 1 108 ? 19.723  36.102  -16.288 1.00 17.88  ? 108 THR B CA  1 
ATOM   2575 C  C   . THR B 1 108 ? 18.805  36.611  -17.389 1.00 16.18  ? 108 THR B C   1 
ATOM   2576 O  O   . THR B 1 108 ? 17.993  35.843  -17.882 1.00 17.64  ? 108 THR B O   1 
ATOM   2577 C  CB  . THR B 1 108 ? 21.147  35.950  -16.873 1.00 20.06  ? 108 THR B CB  1 
ATOM   2578 O  OG1 . THR B 1 108 ? 21.126  35.054  -18.002 1.00 21.67  ? 108 THR B OG1 1 
ATOM   2579 C  CG2 . THR B 1 108 ? 22.118  35.330  -15.858 1.00 21.48  ? 108 THR B CG2 1 
ATOM   2580 N  N   . PRO B 1 109 ? 18.907  37.871  -17.773 1.00 17.61  ? 109 PRO B N   1 
ATOM   2581 C  CA  . PRO B 1 109 ? 18.075  38.434  -18.827 1.00 18.32  ? 109 PRO B CA  1 
ATOM   2582 C  C   . PRO B 1 109 ? 18.082  37.617  -20.114 1.00 17.39  ? 109 PRO B C   1 
ATOM   2583 O  O   . PRO B 1 109 ? 17.014  37.442  -20.715 1.00 18.03  ? 109 PRO B O   1 
ATOM   2584 C  CB  . PRO B 1 109 ? 18.716  39.803  -19.107 1.00 20.40  ? 109 PRO B CB  1 
ATOM   2585 C  CG  . PRO B 1 109 ? 19.221  40.217  -17.765 1.00 19.12  ? 109 PRO B CG  1 
ATOM   2586 C  CD  . PRO B 1 109 ? 19.791  38.928  -17.164 1.00 18.92  ? 109 PRO B CD  1 
ATOM   2587 N  N   . ALA B 1 110 ? 19.250  37.132  -20.548 1.00 18.09  ? 110 ALA B N   1 
ATOM   2588 C  CA  . ALA B 1 110 ? 19.249  36.387  -21.808 1.00 17.65  ? 110 ALA B CA  1 
ATOM   2589 C  C   . ALA B 1 110 ? 18.615  35.008  -21.709 1.00 18.13  ? 110 ALA B C   1 
ATOM   2590 O  O   . ALA B 1 110 ? 18.048  34.464  -22.661 1.00 18.33  ? 110 ALA B O   1 
ATOM   2591 C  CB  . ALA B 1 110 ? 20.662  36.234  -22.378 1.00 19.01  ? 110 ALA B CB  1 
ATOM   2592 N  N   . MET B 1 111 ? 18.708  34.364  -20.550 1.00 18.02  ? 111 MET B N   1 
ATOM   2593 C  CA  . MET B 1 111 ? 18.031  33.113  -20.266 1.00 16.03  ? 111 MET B CA  1 
ATOM   2594 C  C   . MET B 1 111 ? 16.527  33.374  -20.303 1.00 15.89  ? 111 MET B C   1 
ATOM   2595 O  O   . MET B 1 111 ? 15.755  32.634  -20.918 1.00 17.29  ? 111 MET B O   1 
ATOM   2596 C  CB  . MET B 1 111 ? 18.412  32.537  -18.903 1.00 18.12  ? 111 MET B CB  1 
ATOM   2597 C  CG  . MET B 1 111 ? 19.882  32.148  -18.778 1.00 18.28  ? 111 MET B CG  1 
ATOM   2598 S  SD  . MET B 1 111 ? 20.151  31.640  -17.050 1.00 17.73  ? 111 MET B SD  1 
ATOM   2599 C  CE  . MET B 1 111 ? 21.946  31.665  -16.933 1.00 21.18  ? 111 MET B CE  1 
ATOM   2600 N  N   . GLN B 1 112 ? 16.164  34.479  -19.659 1.00 17.60  ? 112 GLN B N   1 
ATOM   2601 C  CA  . GLN B 1 112 ? 14.745  34.821  -19.641 1.00 16.70  ? 112 GLN B CA  1 
ATOM   2602 C  C   . GLN B 1 112 ? 14.165  35.173  -20.998 1.00 17.35  ? 112 GLN B C   1 
ATOM   2603 O  O   . GLN B 1 112 ? 13.017  34.803  -21.274 1.00 19.28  ? 112 GLN B O   1 
ATOM   2604 C  CB  . GLN B 1 112 ? 14.581  35.985  -18.642 1.00 18.06  ? 112 GLN B CB  1 
ATOM   2605 C  CG  . GLN B 1 112 ? 13.132  36.415  -18.486 1.00 20.65  ? 112 GLN B CG  1 
ATOM   2606 C  CD  . GLN B 1 112 ? 12.879  37.601  -17.601 1.00 20.05  ? 112 GLN B CD  1 
ATOM   2607 O  OE1 . GLN B 1 112 ? 11.971  37.645  -16.755 1.00 28.34  ? 112 GLN B OE1 1 
ATOM   2608 N  NE2 . GLN B 1 112 ? 13.678  38.630  -17.778 1.00 22.82  ? 112 GLN B NE2 1 
ATOM   2609 N  N   . ARG B 1 113 ? 14.890  35.892  -21.851 1.00 18.87  ? 113 ARG B N   1 
ATOM   2610 C  CA  . ARG B 1 113 ? 14.332  36.213  -23.168 1.00 18.08  ? 113 ARG B CA  1 
ATOM   2611 C  C   . ARG B 1 113 ? 13.982  34.923  -23.912 1.00 16.75  ? 113 ARG B C   1 
ATOM   2612 O  O   . ARG B 1 113 ? 13.003  34.847  -24.627 1.00 18.26  ? 113 ARG B O   1 
ATOM   2613 C  CB  . ARG B 1 113 ? 15.293  37.047  -24.021 1.00 26.27  ? 113 ARG B CB  1 
ATOM   2614 C  CG  . ARG B 1 113 ? 15.329  38.541  -23.791 1.00 41.76  ? 113 ARG B CG  1 
ATOM   2615 C  CD  . ARG B 1 113 ? 16.267  39.279  -24.745 1.00 52.00  ? 113 ARG B CD  1 
ATOM   2616 N  NE  . ARG B 1 113 ? 17.007  40.342  -24.102 1.00 63.32  ? 113 ARG B NE  1 
ATOM   2617 C  CZ  . ARG B 1 113 ? 18.249  40.413  -23.662 1.00 67.07  ? 113 ARG B CZ  1 
ATOM   2618 N  NH1 . ARG B 1 113 ? 18.627  41.564  -23.107 1.00 77.37  ? 113 ARG B NH1 1 
ATOM   2619 N  NH2 . ARG B 1 113 ? 19.133  39.422  -23.734 1.00 72.40  ? 113 ARG B NH2 1 
ATOM   2620 N  N   . TYR B 1 114 ? 14.830  33.932  -23.767 1.00 16.69  ? 114 TYR B N   1 
ATOM   2621 C  CA  . TYR B 1 114 ? 14.676  32.632  -24.448 1.00 15.76  ? 114 TYR B CA  1 
ATOM   2622 C  C   . TYR B 1 114 ? 13.440  31.921  -23.901 1.00 16.18  ? 114 TYR B C   1 
ATOM   2623 O  O   . TYR B 1 114 ? 12.565  31.486  -24.653 1.00 15.62  ? 114 TYR B O   1 
ATOM   2624 C  CB  . TYR B 1 114 ? 15.960  31.830  -24.348 1.00 18.20  ? 114 TYR B CB  1 
ATOM   2625 C  CG  . TYR B 1 114 ? 16.216  30.680  -25.292 1.00 16.84  ? 114 TYR B CG  1 
ATOM   2626 C  CD1 . TYR B 1 114 ? 15.217  30.024  -26.017 1.00 18.63  ? 114 TYR B CD1 1 
ATOM   2627 C  CD2 . TYR B 1 114 ? 17.531  30.204  -25.470 1.00 17.87  ? 114 TYR B CD2 1 
ATOM   2628 C  CE1 . TYR B 1 114 ? 15.485  28.956  -26.885 1.00 17.62  ? 114 TYR B CE1 1 
ATOM   2629 C  CE2 . TYR B 1 114 ? 17.793  29.142  -26.322 1.00 18.00  ? 114 TYR B CE2 1 
ATOM   2630 C  CZ  . TYR B 1 114 ? 16.794  28.515  -27.027 1.00 18.07  ? 114 TYR B CZ  1 
ATOM   2631 O  OH  . TYR B 1 114 ? 17.131  27.465  -27.850 1.00 17.96  ? 114 TYR B OH  1 
ATOM   2632 N  N   . VAL B 1 115 ? 13.346  31.814  -22.585 1.00 16.40  ? 115 VAL B N   1 
ATOM   2633 C  CA  . VAL B 1 115 ? 12.185  31.244  -21.934 1.00 16.16  ? 115 VAL B CA  1 
ATOM   2634 C  C   . VAL B 1 115 ? 10.883  31.954  -22.302 1.00 18.15  ? 115 VAL B C   1 
ATOM   2635 O  O   . VAL B 1 115 ? 9.830   31.350  -22.599 1.00 17.03  ? 115 VAL B O   1 
ATOM   2636 C  CB  . VAL B 1 115 ? 12.402  31.292  -20.398 1.00 14.97  ? 115 VAL B CB  1 
ATOM   2637 C  CG1 . VAL B 1 115 ? 11.107  31.018  -19.649 1.00 17.98  ? 115 VAL B CG1 1 
ATOM   2638 C  CG2 . VAL B 1 115 ? 13.545  30.348  -19.988 1.00 18.23  ? 115 VAL B CG2 1 
ATOM   2639 N  N   . LYS B 1 116 ? 10.906  33.294  -22.333 1.00 18.02  ? 116 LYS B N   1 
ATOM   2640 C  CA  . LYS B 1 116 ? 9.715   34.047  -22.677 1.00 17.82  ? 116 LYS B CA  1 
ATOM   2641 C  C   . LYS B 1 116 ? 9.267   33.721  -24.082 1.00 20.11  ? 116 LYS B C   1 
ATOM   2642 O  O   . LYS B 1 116 ? 8.065   33.566  -24.308 1.00 20.86  ? 116 LYS B O   1 
ATOM   2643 C  CB  . LYS B 1 116 ? 10.011  35.550  -22.560 1.00 25.09  ? 116 LYS B CB  1 
ATOM   2644 C  CG  . LYS B 1 116 ? 8.853   36.478  -22.887 1.00 36.88  ? 116 LYS B CG  1 
ATOM   2645 C  CD  . LYS B 1 116 ? 9.247   37.948  -22.855 1.00 47.44  ? 116 LYS B CD  1 
ATOM   2646 C  CE  . LYS B 1 116 ? 8.136   38.806  -23.450 1.00 55.26  ? 116 LYS B CE  1 
ATOM   2647 N  NZ  . LYS B 1 116 ? 7.218   39.261  -22.362 1.00 71.86  ? 116 LYS B NZ  1 
ATOM   2648 N  N   . ARG B 1 117 ? 10.207  33.662  -25.027 1.00 17.95  ? 117 ARG B N   1 
ATOM   2649 C  CA  . ARG B 1 117 ? 9.776   33.357  -26.402 1.00 18.27  ? 117 ARG B CA  1 
ATOM   2650 C  C   . ARG B 1 117 ? 9.201   31.957  -26.506 1.00 18.62  ? 117 ARG B C   1 
ATOM   2651 O  O   . ARG B 1 117 ? 8.218   31.732  -27.214 1.00 18.49  ? 117 ARG B O   1 
ATOM   2652 C  CB  . ARG B 1 117 ? 10.922  33.549  -27.408 1.00 17.76  ? 117 ARG B CB  1 
ATOM   2653 C  CG  . ARG B 1 117 ? 10.550  33.283  -28.858 1.00 18.94  ? 117 ARG B CG  1 
ATOM   2654 C  CD  . ARG B 1 117 ? 9.453   34.210  -29.335 1.00 19.34  ? 117 ARG B CD  1 
ATOM   2655 N  NE  . ARG B 1 117 ? 8.954   33.788  -30.658 1.00 20.33  ? 117 ARG B NE  1 
ATOM   2656 C  CZ  . ARG B 1 117 ? 7.743   34.035  -31.151 1.00 19.01  ? 117 ARG B CZ  1 
ATOM   2657 N  NH1 . ARG B 1 117 ? 7.382   33.601  -32.368 1.00 23.99  ? 117 ARG B NH1 1 
ATOM   2658 N  NH2 . ARG B 1 117 ? 6.852   34.726  -30.441 1.00 22.75  ? 117 ARG B NH2 1 
ATOM   2659 N  N   . LEU B 1 118 ? 9.828   30.987  -25.832 1.00 17.60  ? 118 LEU B N   1 
ATOM   2660 C  CA  . LEU B 1 118 ? 9.311   29.616  -25.857 1.00 16.91  ? 118 LEU B CA  1 
ATOM   2661 C  C   . LEU B 1 118 ? 7.867   29.589  -25.360 1.00 19.35  ? 118 LEU B C   1 
ATOM   2662 O  O   . LEU B 1 118 ? 7.010   28.953  -25.993 1.00 19.22  ? 118 LEU B O   1 
ATOM   2663 C  CB  . LEU B 1 118 ? 10.194  28.708  -25.020 1.00 15.54  ? 118 LEU B CB  1 
ATOM   2664 C  CG  . LEU B 1 118 ? 11.512  28.318  -25.692 1.00 15.47  ? 118 LEU B CG  1 
ATOM   2665 C  CD1 . LEU B 1 118 ? 12.480  27.793  -24.635 1.00 17.23  ? 118 LEU B CD1 1 
ATOM   2666 C  CD2 . LEU B 1 118 ? 11.248  27.314  -26.797 1.00 20.02  ? 118 LEU B CD2 1 
ATOM   2667 N  N   . HIS B 1 119 ? 7.569   30.292  -24.264 1.00 18.60  ? 119 HIS B N   1 
ATOM   2668 C  CA  . HIS B 1 119 ? 6.178   30.282  -23.777 1.00 19.07  ? 119 HIS B CA  1 
ATOM   2669 C  C   . HIS B 1 119 ? 5.267   31.052  -24.717 1.00 21.29  ? 119 HIS B C   1 
ATOM   2670 O  O   . HIS B 1 119 ? 4.119   30.645  -24.918 1.00 20.40  ? 119 HIS B O   1 
ATOM   2671 C  CB  . HIS B 1 119 ? 6.073   30.853  -22.365 1.00 18.85  ? 119 HIS B CB  1 
ATOM   2672 C  CG  . HIS B 1 119 ? 6.681   29.983  -21.300 1.00 20.31  ? 119 HIS B CG  1 
ATOM   2673 N  ND1 . HIS B 1 119 ? 6.264   28.683  -21.133 1.00 21.06  ? 119 HIS B ND1 1 
ATOM   2674 C  CD2 . HIS B 1 119 ? 7.644   30.157  -20.385 1.00 19.26  ? 119 HIS B CD2 1 
ATOM   2675 C  CE1 . HIS B 1 119 ? 6.931   28.097  -20.150 1.00 18.41  ? 119 HIS B CE1 1 
ATOM   2676 N  NE2 . HIS B 1 119 ? 7.786   28.989  -19.673 1.00 18.60  ? 119 HIS B NE2 1 
ATOM   2677 N  N   . GLU B 1 120 ? 5.717   32.171  -25.313 1.00 20.28  ? 120 GLU B N   1 
ATOM   2678 C  CA  . GLU B 1 120 ? 4.843   32.857  -26.293 1.00 20.16  ? 120 GLU B CA  1 
ATOM   2679 C  C   . GLU B 1 120 ? 4.486   31.922  -27.442 1.00 20.61  ? 120 GLU B C   1 
ATOM   2680 O  O   . GLU B 1 120 ? 3.351   31.835  -27.901 1.00 20.90  ? 120 GLU B O   1 
ATOM   2681 C  CB  . GLU B 1 120 ? 5.515   34.107  -26.869 1.00 23.33  ? 120 GLU B CB  1 
ATOM   2682 C  CG  . GLU B 1 120 ? 5.810   35.312  -26.019 1.00 29.41  ? 120 GLU B CG  1 
ATOM   2683 C  CD  . GLU B 1 120 ? 6.770   36.336  -26.610 1.00 31.44  ? 120 GLU B CD  1 
ATOM   2684 O  OE1 . GLU B 1 120 ? 7.373   36.209  -27.706 1.00 33.26  ? 120 GLU B OE1 1 
ATOM   2685 O  OE2 . GLU B 1 120 ? 6.955   37.379  -25.946 1.00 39.35  ? 120 GLU B OE2 1 
ATOM   2686 N  N   . VAL B 1 121 ? 5.493   31.178  -27.908 1.00 19.66  ? 121 VAL B N   1 
ATOM   2687 C  CA  . VAL B 1 121 ? 5.188   30.279  -29.015 1.00 20.91  ? 121 VAL B CA  1 
ATOM   2688 C  C   . VAL B 1 121 ? 4.205   29.213  -28.573 1.00 20.32  ? 121 VAL B C   1 
ATOM   2689 O  O   . VAL B 1 121 ? 3.209   28.947  -29.251 1.00 23.28  ? 121 VAL B O   1 
ATOM   2690 C  CB  . VAL B 1 121 ? 6.493   29.640  -29.551 1.00 19.70  ? 121 VAL B CB  1 
ATOM   2691 C  CG1 . VAL B 1 121 ? 6.217   28.449  -30.478 1.00 21.31  ? 121 VAL B CG1 1 
ATOM   2692 C  CG2 . VAL B 1 121 ? 7.322   30.702  -30.252 1.00 21.23  ? 121 VAL B CG2 1 
ATOM   2693 N  N   . GLY B 1 122 ? 4.448   28.550  -27.436 1.00 18.76  ? 122 GLY B N   1 
ATOM   2694 C  CA  . GLY B 1 122 ? 3.609   27.464  -26.969 1.00 19.79  ? 122 GLY B CA  1 
ATOM   2695 C  C   . GLY B 1 122 ? 2.183   27.869  -26.702 1.00 21.35  ? 122 GLY B C   1 
ATOM   2696 O  O   . GLY B 1 122 ? 1.222   27.101  -26.931 1.00 20.55  ? 122 GLY B O   1 
ATOM   2697 N  N   . ARG B 1 123 ? 2.034   29.104  -26.232 1.00 23.55  ? 123 ARG B N   1 
ATOM   2698 C  CA  . ARG B 1 123 ? 0.724   29.595  -25.832 1.00 24.10  ? 123 ARG B CA  1 
ATOM   2699 C  C   . ARG B 1 123 ? -0.046  30.254  -26.972 1.00 23.43  ? 123 ARG B C   1 
ATOM   2700 O  O   . ARG B 1 123 ? -1.266  30.096  -26.999 1.00 27.62  ? 123 ARG B O   1 
ATOM   2701 C  CB  . ARG B 1 123 ? 0.841   30.597  -24.660 1.00 27.47  ? 123 ARG B CB  1 
ATOM   2702 C  CG  . ARG B 1 123 ? 1.389   29.934  -23.381 1.00 36.00  ? 123 ARG B CG  1 
ATOM   2703 C  CD  . ARG B 1 123 ? 1.476   30.801  -22.151 1.00 42.42  ? 123 ARG B CD  1 
ATOM   2704 N  NE  . ARG B 1 123 ? 2.016   30.196  -20.927 1.00 49.57  ? 123 ARG B NE  1 
ATOM   2705 C  CZ  . ARG B 1 123 ? 2.799   30.705  -19.995 1.00 44.13  ? 123 ARG B CZ  1 
ATOM   2706 N  NH1 . ARG B 1 123 ? 3.231   31.969  -20.073 1.00 52.88  ? 123 ARG B NH1 1 
ATOM   2707 N  NH2 . ARG B 1 123 ? 3.217   30.024  -18.925 1.00 52.34  ? 123 ARG B NH2 1 
ATOM   2708 N  N   . THR B 1 124 ? 0.644   30.951  -27.870 1.00 24.75  ? 124 THR B N   1 
ATOM   2709 C  CA  . THR B 1 124 ? -0.063  31.727  -28.889 1.00 26.52  ? 124 THR B CA  1 
ATOM   2710 C  C   . THR B 1 124 ? 0.209   31.299  -30.330 1.00 25.73  ? 124 THR B C   1 
ATOM   2711 O  O   . THR B 1 124 ? -0.584  31.680  -31.209 1.00 26.95  ? 124 THR B O   1 
ATOM   2712 C  CB  . THR B 1 124 ? 0.248   33.235  -28.788 1.00 29.21  ? 124 THR B CB  1 
ATOM   2713 O  OG1 . THR B 1 124 ? 1.612   33.496  -29.134 1.00 26.05  ? 124 THR B OG1 1 
ATOM   2714 C  CG2 . THR B 1 124 ? 0.066   33.739  -27.364 1.00 31.58  ? 124 THR B CG2 1 
ATOM   2715 N  N   . GLU B 1 125 ? 1.274   30.556  -30.619 1.00 23.54  ? 125 GLU B N   1 
ATOM   2716 C  CA  . GLU B 1 125 ? 1.562   30.081  -31.970 1.00 22.25  ? 125 GLU B CA  1 
ATOM   2717 C  C   . GLU B 1 125 ? 2.332   28.767  -31.941 1.00 22.72  ? 125 GLU B C   1 
ATOM   2718 O  O   . GLU B 1 125 ? 3.462   28.687  -32.403 1.00 21.15  ? 125 GLU B O   1 
ATOM   2719 C  CB  . GLU B 1 125 ? 2.337   31.067  -32.843 1.00 26.69  ? 125 GLU B CB  1 
ATOM   2720 C  CG  . GLU B 1 125 ? 3.437   31.871  -32.206 1.00 27.48  ? 125 GLU B CG  1 
ATOM   2721 C  CD  . GLU B 1 125 ? 3.885   33.095  -32.977 1.00 23.24  ? 125 GLU B CD  1 
ATOM   2722 O  OE1 . GLU B 1 125 ? 3.639   33.199  -34.211 1.00 28.35  ? 125 GLU B OE1 1 
ATOM   2723 O  OE2 . GLU B 1 125 ? 4.491   33.984  -32.342 1.00 30.27  ? 125 GLU B OE2 1 
ATOM   2724 N  N   . PRO B 1 126 ? 1.698   27.750  -31.372 1.00 22.26  ? 126 PRO B N   1 
ATOM   2725 C  CA  . PRO B 1 126 ? 2.398   26.466  -31.150 1.00 22.57  ? 126 PRO B CA  1 
ATOM   2726 C  C   . PRO B 1 126 ? 2.757   25.747  -32.440 1.00 22.99  ? 126 PRO B C   1 
ATOM   2727 O  O   . PRO B 1 126 ? 3.592   24.849  -32.433 1.00 21.32  ? 126 PRO B O   1 
ATOM   2728 C  CB  . PRO B 1 126 ? 1.382   25.673  -30.330 1.00 23.96  ? 126 PRO B CB  1 
ATOM   2729 C  CG  . PRO B 1 126 ? 0.054   26.236  -30.722 1.00 24.34  ? 126 PRO B CG  1 
ATOM   2730 C  CD  . PRO B 1 126 ? 0.324   27.726  -30.833 1.00 23.02  ? 126 PRO B CD  1 
ATOM   2731 N  N   . GLU B 1 127 ? 2.168   26.172  -33.560 1.00 22.89  ? 127 GLU B N   1 
ATOM   2732 C  CA  . GLU B 1 127 ? 2.579   25.703  -34.884 1.00 24.68  ? 127 GLU B CA  1 
ATOM   2733 C  C   . GLU B 1 127 ? 4.074   25.965  -35.098 1.00 22.90  ? 127 GLU B C   1 
ATOM   2734 O  O   . GLU B 1 127 ? 4.694   25.308  -35.941 1.00 24.32  ? 127 GLU B O   1 
ATOM   2735 C  CB  . GLU B 1 127 ? 1.684   26.332  -35.954 1.00 26.81  ? 127 GLU B CB  1 
ATOM   2736 C  CG  . GLU B 1 127 ? 1.706   27.839  -36.158 1.00 28.76  ? 127 GLU B CG  1 
ATOM   2737 C  CD  . GLU B 1 127 ? 0.733   28.621  -35.279 1.00 31.49  ? 127 GLU B CD  1 
ATOM   2738 O  OE1 . GLU B 1 127 ? 0.486   29.823  -35.543 1.00 28.10  ? 127 GLU B OE1 1 
ATOM   2739 O  OE2 . GLU B 1 127 ? 0.234   28.011  -34.306 1.00 26.00  ? 127 GLU B OE2 1 
ATOM   2740 N  N   . LEU B 1 128 ? 4.711   26.895  -34.370 1.00 21.28  ? 128 LEU B N   1 
ATOM   2741 C  CA  . LEU B 1 128 ? 6.125   27.192  -34.493 1.00 20.09  ? 128 LEU B CA  1 
ATOM   2742 C  C   . LEU B 1 128 ? 6.973   26.407  -33.519 1.00 20.10  ? 128 LEU B C   1 
ATOM   2743 O  O   . LEU B 1 128 ? 8.198   26.526  -33.560 1.00 21.75  ? 128 LEU B O   1 
ATOM   2744 C  CB  . LEU B 1 128 ? 6.374   28.699  -34.268 1.00 20.61  ? 128 LEU B CB  1 
ATOM   2745 C  CG  . LEU B 1 128 ? 5.555   29.663  -35.153 1.00 21.89  ? 128 LEU B CG  1 
ATOM   2746 C  CD1 . LEU B 1 128 ? 6.081   31.078  -34.932 1.00 21.26  ? 128 LEU B CD1 1 
ATOM   2747 C  CD2 . LEU B 1 128 ? 5.562   29.249  -36.624 1.00 23.06  ? 128 LEU B CD2 1 
ATOM   2748 N  N   . LEU B 1 129 ? 6.392   25.599  -32.658 1.00 18.78  ? 129 LEU B N   1 
ATOM   2749 C  CA  . LEU B 1 129 ? 7.215   24.985  -31.612 1.00 20.19  ? 129 LEU B CA  1 
ATOM   2750 C  C   . LEU B 1 129 ? 8.220   24.008  -32.208 1.00 19.13  ? 129 LEU B C   1 
ATOM   2751 O  O   . LEU B 1 129 ? 9.323   23.841  -31.671 1.00 18.84  ? 129 LEU B O   1 
ATOM   2752 C  CB  . LEU B 1 129 ? 6.317   24.347  -30.575 1.00 21.78  ? 129 LEU B CB  1 
ATOM   2753 C  CG  . LEU B 1 129 ? 6.690   23.980  -29.175 1.00 24.24  ? 129 LEU B CG  1 
ATOM   2754 C  CD1 . LEU B 1 129 ? 7.257   25.170  -28.395 1.00 24.82  ? 129 LEU B CD1 1 
ATOM   2755 C  CD2 . LEU B 1 129 ? 5.502   23.384  -28.403 1.00 29.04  ? 129 LEU B CD2 1 
ATOM   2756 N  N   . VAL B 1 130 ? 7.825   23.385  -33.326 1.00 20.94  ? 130 VAL B N   1 
ATOM   2757 C  CA  . VAL B 1 130 ? 8.731   22.458  -34.010 1.00 19.90  ? 130 VAL B CA  1 
ATOM   2758 C  C   . VAL B 1 130 ? 10.075  23.107  -34.347 1.00 20.00  ? 130 VAL B C   1 
ATOM   2759 O  O   . VAL B 1 130 ? 11.144  22.484  -34.365 1.00 21.30  ? 130 VAL B O   1 
ATOM   2760 C  CB  . VAL B 1 130 ? 8.032   21.847  -35.259 1.00 18.23  ? 130 VAL B CB  1 
ATOM   2761 C  CG1 . VAL B 1 130 ? 7.699   22.879  -36.329 1.00 21.88  ? 130 VAL B CG1 1 
ATOM   2762 C  CG2 . VAL B 1 130 ? 8.887   20.754  -35.865 1.00 24.82  ? 130 VAL B CG2 1 
ATOM   2763 N  N   . ALA B 1 131 ? 10.091  24.421  -34.624 1.00 18.31  ? 131 ALA B N   1 
ATOM   2764 C  CA  . ALA B 1 131 ? 11.349  25.103  -34.881 1.00 18.78  ? 131 ALA B CA  1 
ATOM   2765 C  C   . ALA B 1 131 ? 12.278  25.090  -33.662 1.00 19.60  ? 131 ALA B C   1 
ATOM   2766 O  O   . ALA B 1 131 ? 13.479  24.938  -33.843 1.00 19.60  ? 131 ALA B O   1 
ATOM   2767 C  CB  . ALA B 1 131 ? 11.085  26.521  -35.340 1.00 23.49  ? 131 ALA B CB  1 
ATOM   2768 N  N   . HIS B 1 132 ? 11.695  25.245  -32.474 1.00 18.50  ? 132 HIS B N   1 
ATOM   2769 C  CA  . HIS B 1 132 ? 12.464  25.264  -31.238 1.00 16.35  ? 132 HIS B CA  1 
ATOM   2770 C  C   . HIS B 1 132 ? 12.932  23.866  -30.857 1.00 16.50  ? 132 HIS B C   1 
ATOM   2771 O  O   . HIS B 1 132 ? 14.046  23.683  -30.358 1.00 21.43  ? 132 HIS B O   1 
ATOM   2772 C  CB  . HIS B 1 132 ? 11.636  25.932  -30.141 1.00 20.01  ? 132 HIS B CB  1 
ATOM   2773 C  CG  . HIS B 1 132 ? 11.667  27.426  -30.290 1.00 17.81  ? 132 HIS B CG  1 
ATOM   2774 N  ND1 . HIS B 1 132 ? 12.761  28.181  -29.896 1.00 18.48  ? 132 HIS B ND1 1 
ATOM   2775 C  CD2 . HIS B 1 132 ? 10.782  28.312  -30.792 1.00 21.29  ? 132 HIS B CD2 1 
ATOM   2776 C  CE1 . HIS B 1 132 ? 12.516  29.471  -30.147 1.00 21.00  ? 132 HIS B CE1 1 
ATOM   2777 N  NE2 . HIS B 1 132 ? 11.317  29.569  -30.688 1.00 19.47  ? 132 HIS B NE2 1 
ATOM   2778 N  N   . ALA B 1 133 ? 12.082  22.865  -31.092 1.00 17.45  ? 133 ALA B N   1 
ATOM   2779 C  CA  . ALA B 1 133 ? 12.441  21.484  -30.793 1.00 18.37  ? 133 ALA B CA  1 
ATOM   2780 C  C   . ALA B 1 133 ? 13.540  21.022  -31.739 1.00 19.17  ? 133 ALA B C   1 
ATOM   2781 O  O   . ALA B 1 133 ? 14.458  20.376  -31.238 1.00 20.35  ? 133 ALA B O   1 
ATOM   2782 C  CB  . ALA B 1 133 ? 11.184  20.613  -30.884 1.00 21.25  ? 133 ALA B CB  1 
ATOM   2783 N  N   . TYR B 1 134 ? 13.493  21.349  -33.022 1.00 21.73  ? 134 TYR B N   1 
ATOM   2784 C  CA  . TYR B 1 134 ? 14.521  21.037  -34.011 1.00 23.99  ? 134 TYR B CA  1 
ATOM   2785 C  C   . TYR B 1 134 ? 15.875  21.582  -33.564 1.00 22.62  ? 134 TYR B C   1 
ATOM   2786 O  O   . TYR B 1 134 ? 16.884  20.889  -33.478 1.00 25.61  ? 134 TYR B O   1 
ATOM   2787 C  CB  . TYR B 1 134 ? 14.168  21.653  -35.382 1.00 26.81  ? 134 TYR B CB  1 
ATOM   2788 C  CG  . TYR B 1 134 ? 15.332  21.805  -36.342 1.00 28.72  ? 134 TYR B CG  1 
ATOM   2789 C  CD1 . TYR B 1 134 ? 15.782  20.725  -37.097 1.00 28.82  ? 134 TYR B CD1 1 
ATOM   2790 C  CD2 . TYR B 1 134 ? 16.008  23.008  -36.529 1.00 27.38  ? 134 TYR B CD2 1 
ATOM   2791 C  CE1 . TYR B 1 134 ? 16.849  20.832  -37.995 1.00 31.01  ? 134 TYR B CE1 1 
ATOM   2792 C  CE2 . TYR B 1 134 ? 17.075  23.141  -37.405 1.00 31.51  ? 134 TYR B CE2 1 
ATOM   2793 C  CZ  . TYR B 1 134 ? 17.509  22.050  -38.146 1.00 33.23  ? 134 TYR B CZ  1 
ATOM   2794 O  OH  . TYR B 1 134 ? 18.579  22.207  -39.018 1.00 31.53  ? 134 TYR B OH  1 
ATOM   2795 N  N   . THR B 1 135 ? 15.871  22.887  -33.301 1.00 24.04  ? 135 THR B N   1 
ATOM   2796 C  CA  . THR B 1 135 ? 17.060  23.642  -32.963 1.00 24.07  ? 135 THR B CA  1 
ATOM   2797 C  C   . THR B 1 135 ? 17.715  23.055  -31.719 1.00 23.25  ? 135 THR B C   1 
ATOM   2798 O  O   . THR B 1 135 ? 18.893  22.748  -31.697 1.00 25.07  ? 135 THR B O   1 
ATOM   2799 C  CB  . THR B 1 135 ? 16.773  25.144  -32.728 1.00 26.43  ? 135 THR B CB  1 
ATOM   2800 O  OG1 . THR B 1 135 ? 16.247  25.738  -33.911 1.00 31.66  ? 135 THR B OG1 1 
ATOM   2801 C  CG2 . THR B 1 135 ? 18.049  25.919  -32.388 1.00 31.29  ? 135 THR B CG2 1 
ATOM   2802 N  N   . ARG B 1 136 ? 16.935  22.880  -30.663 1.00 21.38  ? 136 ARG B N   1 
ATOM   2803 C  CA  . ARG B 1 136 ? 17.504  22.373  -29.429 1.00 18.62  ? 136 ARG B CA  1 
ATOM   2804 C  C   . ARG B 1 136 ? 17.841  20.889  -29.500 1.00 18.47  ? 136 ARG B C   1 
ATOM   2805 O  O   . ARG B 1 136 ? 19.012  20.517  -29.313 1.00 21.23  ? 136 ARG B O   1 
ATOM   2806 C  CB  . ARG B 1 136 ? 16.558  22.593  -28.222 1.00 20.04  ? 136 ARG B CB  1 
ATOM   2807 C  CG  . ARG B 1 136 ? 16.707  23.966  -27.577 1.00 25.08  ? 136 ARG B CG  1 
ATOM   2808 C  CD  . ARG B 1 136 ? 17.581  23.812  -26.370 1.00 24.68  ? 136 ARG B CD  1 
ATOM   2809 N  NE  . ARG B 1 136 ? 18.985  23.583  -26.688 1.00 21.52  ? 136 ARG B NE  1 
ATOM   2810 C  CZ  . ARG B 1 136 ? 19.869  24.529  -26.919 1.00 22.56  ? 136 ARG B CZ  1 
ATOM   2811 N  NH1 . ARG B 1 136 ? 19.514  25.817  -26.909 1.00 22.81  ? 136 ARG B NH1 1 
ATOM   2812 N  NH2 . ARG B 1 136 ? 21.121  24.195  -27.172 1.00 23.88  ? 136 ARG B NH2 1 
ATOM   2813 N  N   . TYR B 1 137 ? 16.809  20.070  -29.723 1.00 18.21  ? 137 TYR B N   1 
ATOM   2814 C  CA  . TYR B 1 137 ? 17.024  18.616  -29.617 1.00 20.55  ? 137 TYR B CA  1 
ATOM   2815 C  C   . TYR B 1 137 ? 17.951  18.099  -30.701 1.00 21.13  ? 137 TYR B C   1 
ATOM   2816 O  O   . TYR B 1 137 ? 18.870  17.330  -30.384 1.00 23.08  ? 137 TYR B O   1 
ATOM   2817 C  CB  . TYR B 1 137 ? 15.715  17.845  -29.712 1.00 19.74  ? 137 TYR B CB  1 
ATOM   2818 C  CG  . TYR B 1 137 ? 14.809  18.006  -28.531 1.00 17.61  ? 137 TYR B CG  1 
ATOM   2819 C  CD1 . TYR B 1 137 ? 15.258  17.701  -27.262 1.00 19.08  ? 137 TYR B CD1 1 
ATOM   2820 C  CD2 . TYR B 1 137 ? 13.504  18.454  -28.698 1.00 20.84  ? 137 TYR B CD2 1 
ATOM   2821 C  CE1 . TYR B 1 137 ? 14.434  17.839  -26.155 1.00 18.94  ? 137 TYR B CE1 1 
ATOM   2822 C  CE2 . TYR B 1 137 ? 12.684  18.599  -27.597 1.00 21.67  ? 137 TYR B CE2 1 
ATOM   2823 C  CZ  . TYR B 1 137 ? 13.140  18.297  -26.334 1.00 21.57  ? 137 TYR B CZ  1 
ATOM   2824 O  OH  . TYR B 1 137 ? 12.333  18.426  -25.220 1.00 27.84  ? 137 TYR B OH  1 
ATOM   2825 N  N   . LEU B 1 138 ? 17.739  18.472  -31.970 1.00 22.70  ? 138 LEU B N   1 
ATOM   2826 C  CA  . LEU B 1 138 ? 18.654  17.844  -32.947 1.00 25.19  ? 138 LEU B CA  1 
ATOM   2827 C  C   . LEU B 1 138 ? 20.060  18.427  -32.881 1.00 24.55  ? 138 LEU B C   1 
ATOM   2828 O  O   . LEU B 1 138 ? 21.042  17.722  -33.157 1.00 28.58  ? 138 LEU B O   1 
ATOM   2829 C  CB  . LEU B 1 138 ? 18.051  17.906  -34.337 1.00 33.78  ? 138 LEU B CB  1 
ATOM   2830 C  CG  . LEU B 1 138 ? 16.799  17.064  -34.618 1.00 41.75  ? 138 LEU B CG  1 
ATOM   2831 C  CD1 . LEU B 1 138 ? 16.841  16.572  -36.064 1.00 57.46  ? 138 LEU B CD1 1 
ATOM   2832 C  CD2 . LEU B 1 138 ? 16.635  15.915  -33.636 1.00 49.43  ? 138 LEU B CD2 1 
ATOM   2833 N  N   . GLY B 1 139 ? 20.191  19.705  -32.480 1.00 24.52  ? 139 GLY B N   1 
ATOM   2834 C  CA  . GLY B 1 139 ? 21.535  20.206  -32.296 1.00 25.07  ? 139 GLY B CA  1 
ATOM   2835 C  C   . GLY B 1 139 ? 22.247  19.550  -31.124 1.00 24.73  ? 139 GLY B C   1 
ATOM   2836 O  O   . GLY B 1 139 ? 23.437  19.222  -31.221 1.00 24.69  ? 139 GLY B O   1 
ATOM   2837 N  N   . ASP B 1 140 ? 21.533  19.386  -30.011 1.00 21.64  ? 140 ASP B N   1 
ATOM   2838 C  CA  . ASP B 1 140 ? 22.170  18.890  -28.769 1.00 23.79  ? 140 ASP B CA  1 
ATOM   2839 C  C   . ASP B 1 140 ? 22.535  17.430  -28.971 1.00 23.04  ? 140 ASP B C   1 
ATOM   2840 O  O   . ASP B 1 140 ? 23.610  16.945  -28.607 1.00 24.48  ? 140 ASP B O   1 
ATOM   2841 C  CB  . ASP B 1 140 ? 21.305  19.184  -27.533 1.00 25.55  ? 140 ASP B CB  1 
ATOM   2842 C  CG  . ASP B 1 140 ? 21.233  20.648  -27.156 1.00 26.90  ? 140 ASP B CG  1 
ATOM   2843 O  OD1 . ASP B 1 140 ? 22.025  21.482  -27.634 1.00 41.23  ? 140 ASP B OD1 1 
ATOM   2844 O  OD2 . ASP B 1 140 ? 20.332  20.991  -26.324 1.00 27.33  ? 140 ASP B OD2 1 
ATOM   2845 N  N   . LEU B 1 141 ? 21.655  16.683  -29.629 1.00 24.74  ? 141 LEU B N   1 
ATOM   2846 C  CA  . LEU B 1 141 ? 21.902  15.274  -29.919 1.00 28.23  ? 141 LEU B CA  1 
ATOM   2847 C  C   . LEU B 1 141 ? 23.090  15.133  -30.856 1.00 32.56  ? 141 LEU B C   1 
ATOM   2848 O  O   . LEU B 1 141 ? 23.941  14.309  -30.621 1.00 32.51  ? 141 LEU B O   1 
ATOM   2849 C  CB  . LEU B 1 141 ? 20.656  14.704  -30.580 1.00 29.32  ? 141 LEU B CB  1 
ATOM   2850 C  CG  . LEU B 1 141 ? 20.602  13.243  -30.945 1.00 30.41  ? 141 LEU B CG  1 
ATOM   2851 C  CD1 . LEU B 1 141 ? 20.813  12.424  -29.695 1.00 24.73  ? 141 LEU B CD1 1 
ATOM   2852 C  CD2 . LEU B 1 141 ? 19.287  12.933  -31.671 1.00 28.52  ? 141 LEU B CD2 1 
ATOM   2853 N  N   . SER B 1 142 ? 23.105  15.957  -31.903 1.00 34.38  ? 142 SER B N   1 
ATOM   2854 C  CA  . SER B 1 142 ? 24.152  15.835  -32.911 1.00 39.74  ? 142 SER B CA  1 
ATOM   2855 C  C   . SER B 1 142 ? 25.524  16.170  -32.340 1.00 40.64  ? 142 SER B C   1 
ATOM   2856 O  O   . SER B 1 142 ? 26.583  15.608  -32.647 1.00 37.64  ? 142 SER B O   1 
ATOM   2857 C  CB  . SER B 1 142 ? 23.908  16.731  -34.120 1.00 40.14  ? 142 SER B CB  1 
ATOM   2858 O  OG  . SER B 1 142 ? 22.682  16.534  -34.795 1.00 51.20  ? 142 SER B OG  1 
ATOM   2859 N  N   . GLY B 1 143 ? 25.643  17.153  -31.447 1.00 43.62  ? 143 GLY B N   1 
ATOM   2860 C  CA  . GLY B 1 143 ? 27.018  17.489  -31.060 1.00 47.24  ? 143 GLY B CA  1 
ATOM   2861 C  C   . GLY B 1 143 ? 27.431  17.036  -29.683 1.00 44.02  ? 143 GLY B C   1 
ATOM   2862 O  O   . GLY B 1 143 ? 28.577  17.227  -29.264 1.00 49.00  ? 143 GLY B O   1 
ATOM   2863 N  N   . GLY B 1 144 ? 26.510  16.430  -28.941 1.00 38.67  ? 144 GLY B N   1 
ATOM   2864 C  CA  . GLY B 1 144 ? 26.738  16.087  -27.562 1.00 38.89  ? 144 GLY B CA  1 
ATOM   2865 C  C   . GLY B 1 144 ? 27.868  15.168  -27.222 1.00 37.57  ? 144 GLY B C   1 
ATOM   2866 O  O   . GLY B 1 144 ? 28.442  15.260  -26.124 1.00 40.23  ? 144 GLY B O   1 
ATOM   2867 N  N   . GLN B 1 145 ? 28.222  14.239  -28.107 1.00 37.74  ? 145 GLN B N   1 
ATOM   2868 C  CA  . GLN B 1 145 ? 29.264  13.307  -27.658 1.00 40.71  ? 145 GLN B CA  1 
ATOM   2869 C  C   . GLN B 1 145 ? 30.637  13.964  -27.752 1.00 40.92  ? 145 GLN B C   1 
ATOM   2870 O  O   . GLN B 1 145 ? 31.510  13.752  -26.881 1.00 37.41  ? 145 GLN B O   1 
ATOM   2871 C  CB  . GLN B 1 145 ? 29.120  11.984  -28.412 1.00 41.52  ? 145 GLN B CB  1 
ATOM   2872 C  CG  . GLN B 1 145 ? 27.772  11.337  -28.037 1.00 50.48  ? 145 GLN B CG  1 
ATOM   2873 C  CD  . GLN B 1 145 ? 27.661  11.083  -26.540 1.00 55.77  ? 145 GLN B CD  1 
ATOM   2874 O  OE1 . GLN B 1 145 ? 26.823  11.582  -25.788 1.00 73.48  ? 145 GLN B OE1 1 
ATOM   2875 N  NE2 . GLN B 1 145 ? 28.574  10.238  -26.047 1.00 75.92  ? 145 GLN B NE2 1 
ATOM   2876 N  N   . VAL B 1 146 ? 30.771  14.775  -28.797 1.00 40.14  ? 146 VAL B N   1 
ATOM   2877 C  CA  . VAL B 1 146 ? 31.953  15.640  -28.933 1.00 44.63  ? 146 VAL B CA  1 
ATOM   2878 C  C   . VAL B 1 146 ? 32.055  16.639  -27.787 1.00 38.96  ? 146 VAL B C   1 
ATOM   2879 O  O   . VAL B 1 146 ? 33.107  16.848  -27.161 1.00 45.88  ? 146 VAL B O   1 
ATOM   2880 C  CB  . VAL B 1 146 ? 31.912  16.321  -30.317 1.00 47.32  ? 146 VAL B CB  1 
ATOM   2881 C  CG1 . VAL B 1 146 ? 32.898  17.470  -30.452 1.00 56.62  ? 146 VAL B CG1 1 
ATOM   2882 C  CG2 . VAL B 1 146 ? 32.175  15.261  -31.388 1.00 48.19  ? 146 VAL B CG2 1 
ATOM   2883 N  N   . LEU B 1 147 ? 30.974  17.329  -27.398 1.00 35.64  ? 147 LEU B N   1 
ATOM   2884 C  CA  . LEU B 1 147 ? 31.168  18.272  -26.293 1.00 35.82  ? 147 LEU B CA  1 
ATOM   2885 C  C   . LEU B 1 147 ? 31.377  17.590  -24.947 1.00 33.22  ? 147 LEU B C   1 
ATOM   2886 O  O   . LEU B 1 147 ? 32.081  18.126  -24.084 1.00 32.93  ? 147 LEU B O   1 
ATOM   2887 C  CB  . LEU B 1 147 ? 29.985  19.251  -26.239 1.00 37.18  ? 147 LEU B CB  1 
ATOM   2888 C  CG  . LEU B 1 147 ? 30.193  20.380  -27.265 1.00 45.35  ? 147 LEU B CG  1 
ATOM   2889 C  CD1 . LEU B 1 147 ? 28.881  21.082  -27.533 1.00 55.32  ? 147 LEU B CD1 1 
ATOM   2890 C  CD2 . LEU B 1 147 ? 31.278  21.352  -26.807 1.00 48.70  ? 147 LEU B CD2 1 
ATOM   2891 N  N   . LYS B 1 148 ? 30.772  16.400  -24.788 1.00 31.43  ? 148 LYS B N   1 
ATOM   2892 C  CA  . LYS B 1 148 ? 31.015  15.667  -23.561 1.00 28.69  ? 148 LYS B CA  1 
ATOM   2893 C  C   . LYS B 1 148 ? 32.515  15.441  -23.367 1.00 27.87  ? 148 LYS B C   1 
ATOM   2894 O  O   . LYS B 1 148 ? 33.071  15.666  -22.282 1.00 29.60  ? 148 LYS B O   1 
ATOM   2895 C  CB  . LYS B 1 148 ? 30.231  14.354  -23.555 1.00 29.16  ? 148 LYS B CB  1 
ATOM   2896 C  CG  . LYS B 1 148 ? 30.406  13.603  -22.248 1.00 30.60  ? 148 LYS B CG  1 
ATOM   2897 C  CD  . LYS B 1 148 ? 29.799  12.234  -22.215 1.00 39.24  ? 148 LYS B CD  1 
ATOM   2898 C  CE  . LYS B 1 148 ? 28.288  12.204  -22.189 1.00 48.83  ? 148 LYS B CE  1 
ATOM   2899 N  NZ  . LYS B 1 148 ? 27.694  12.599  -20.872 1.00 69.11  ? 148 LYS B NZ  1 
ATOM   2900 N  N   . LYS B 1 149 ? 33.190  14.985  -24.413 1.00 29.24  ? 149 LYS B N   1 
ATOM   2901 C  CA  . LYS B 1 149 ? 34.599  14.638  -24.307 1.00 32.88  ? 149 LYS B CA  1 
ATOM   2902 C  C   . LYS B 1 149 ? 35.462  15.870  -24.003 1.00 31.17  ? 149 LYS B C   1 
ATOM   2903 O  O   . LYS B 1 149 ? 36.416  15.835  -23.224 1.00 32.60  ? 149 LYS B O   1 
ATOM   2904 C  CB  . LYS B 1 149 ? 35.112  13.987  -25.598 1.00 38.61  ? 149 LYS B CB  1 
ATOM   2905 C  CG  . LYS B 1 149 ? 36.647  13.951  -25.583 1.00 53.99  ? 149 LYS B CG  1 
ATOM   2906 C  CD  . LYS B 1 149 ? 37.310  13.544  -26.885 1.00 65.33  ? 149 LYS B CD  1 
ATOM   2907 C  CE  . LYS B 1 149 ? 38.422  12.520  -26.733 1.00 71.92  ? 149 LYS B CE  1 
ATOM   2908 N  NZ  . LYS B 1 149 ? 38.709  11.789  -28.013 1.00 82.29  ? 149 LYS B NZ  1 
ATOM   2909 N  N   . ILE B 1 150 ? 35.120  16.975  -24.650 1.00 29.23  ? 150 ILE B N   1 
ATOM   2910 C  CA  . ILE B 1 150 ? 35.823  18.232  -24.390 1.00 30.76  ? 150 ILE B CA  1 
ATOM   2911 C  C   . ILE B 1 150 ? 35.616  18.652  -22.942 1.00 27.13  ? 150 ILE B C   1 
ATOM   2912 O  O   . ILE B 1 150 ? 36.579  19.051  -22.288 1.00 29.05  ? 150 ILE B O   1 
ATOM   2913 C  CB  . ILE B 1 150 ? 35.359  19.342  -25.354 1.00 37.29  ? 150 ILE B CB  1 
ATOM   2914 C  CG1 . ILE B 1 150 ? 35.850  19.185  -26.805 1.00 39.82  ? 150 ILE B CG1 1 
ATOM   2915 C  CG2 . ILE B 1 150 ? 35.736  20.733  -24.853 1.00 37.52  ? 150 ILE B CG2 1 
ATOM   2916 C  CD1 . ILE B 1 150 ? 34.994  19.929  -27.818 1.00 51.99  ? 150 ILE B CD1 1 
ATOM   2917 N  N   . ALA B 1 151 ? 34.363  18.546  -22.468 1.00 27.36  ? 151 ALA B N   1 
ATOM   2918 C  CA  . ALA B 1 151 ? 34.100  18.935  -21.081 1.00 27.55  ? 151 ALA B CA  1 
ATOM   2919 C  C   . ALA B 1 151 ? 34.827  18.037  -20.080 1.00 29.10  ? 151 ALA B C   1 
ATOM   2920 O  O   . ALA B 1 151 ? 35.388  18.563  -19.107 1.00 29.98  ? 151 ALA B O   1 
ATOM   2921 C  CB  . ALA B 1 151 ? 32.616  18.944  -20.748 1.00 25.90  ? 151 ALA B CB  1 
ATOM   2922 N  N   . GLN B 1 152 ? 34.802  16.720  -20.303 1.00 27.24  ? 152 GLN B N   1 
ATOM   2923 C  CA  . GLN B 1 152 ? 35.506  15.831  -19.385 1.00 28.97  ? 152 GLN B CA  1 
ATOM   2924 C  C   . GLN B 1 152 ? 36.989  16.190  -19.278 1.00 29.50  ? 152 GLN B C   1 
ATOM   2925 O  O   . GLN B 1 152 ? 37.598  16.199  -18.202 1.00 29.87  ? 152 GLN B O   1 
ATOM   2926 C  CB  . GLN B 1 152 ? 35.365  14.373  -19.819 1.00 29.82  ? 152 GLN B CB  1 
ATOM   2927 C  CG  . GLN B 1 152 ? 33.969  13.816  -19.703 1.00 33.66  ? 152 GLN B CG  1 
ATOM   2928 C  CD  . GLN B 1 152 ? 33.661  12.467  -20.307 1.00 32.11  ? 152 GLN B CD  1 
ATOM   2929 O  OE1 . GLN B 1 152 ? 32.705  11.774  -19.889 1.00 35.52  ? 152 GLN B OE1 1 
ATOM   2930 N  NE2 . GLN B 1 152 ? 34.416  12.020  -21.296 1.00 39.77  ? 152 GLN B NE2 1 
ATOM   2931 N  N   . LYS B 1 153 ? 37.606  16.510  -20.413 1.00 32.07  ? 153 LYS B N   1 
ATOM   2932 C  CA  . LYS B 1 153 ? 39.043  16.842  -20.412 1.00 29.84  ? 153 LYS B CA  1 
ATOM   2933 C  C   . LYS B 1 153 ? 39.291  18.175  -19.725 1.00 28.85  ? 153 LYS B C   1 
ATOM   2934 O  O   . LYS B 1 153 ? 40.213  18.346  -18.936 1.00 33.07  ? 153 LYS B O   1 
ATOM   2935 C  CB  . LYS B 1 153 ? 39.518  16.813  -21.853 1.00 36.11  ? 153 LYS B CB  1 
ATOM   2936 C  CG  . LYS B 1 153 ? 40.939  17.183  -22.211 1.00 45.43  ? 153 LYS B CG  1 
ATOM   2937 C  CD  . LYS B 1 153 ? 41.098  16.889  -23.715 1.00 53.69  ? 153 LYS B CD  1 
ATOM   2938 C  CE  . LYS B 1 153 ? 42.523  16.891  -24.213 1.00 57.90  ? 153 LYS B CE  1 
ATOM   2939 N  NZ  . LYS B 1 153 ? 42.644  16.791  -25.707 1.00 67.63  ? 153 LYS B NZ  1 
ATOM   2940 N  N   . ALA B 1 154 ? 38.419  19.125  -20.035 1.00 26.43  ? 154 ALA B N   1 
ATOM   2941 C  CA  . ALA B 1 154 ? 38.562  20.456  -19.491 1.00 26.09  ? 154 ALA B CA  1 
ATOM   2942 C  C   . ALA B 1 154 ? 38.259  20.558  -18.000 1.00 26.32  ? 154 ALA B C   1 
ATOM   2943 O  O   . ALA B 1 154 ? 38.891  21.338  -17.246 1.00 29.03  ? 154 ALA B O   1 
ATOM   2944 C  CB  . ALA B 1 154 ? 37.636  21.364  -20.302 1.00 30.81  ? 154 ALA B CB  1 
ATOM   2945 N  N   . LEU B 1 155 ? 37.265  19.840  -17.491 1.00 25.27  ? 155 LEU B N   1 
ATOM   2946 C  CA  . LEU B 1 155 ? 36.752  20.128  -16.150 1.00 24.82  ? 155 LEU B CA  1 
ATOM   2947 C  C   . LEU B 1 155 ? 37.301  19.222  -15.060 1.00 23.63  ? 155 LEU B C   1 
ATOM   2948 O  O   . LEU B 1 155 ? 37.134  19.522  -13.880 1.00 26.47  ? 155 LEU B O   1 
ATOM   2949 C  CB  . LEU B 1 155 ? 35.221  20.050  -16.156 1.00 25.83  ? 155 LEU B CB  1 
ATOM   2950 C  CG  . LEU B 1 155 ? 34.508  20.955  -17.182 1.00 28.27  ? 155 LEU B CG  1 
ATOM   2951 C  CD1 . LEU B 1 155 ? 33.062  20.511  -17.320 1.00 35.56  ? 155 LEU B CD1 1 
ATOM   2952 C  CD2 . LEU B 1 155 ? 34.650  22.401  -16.772 1.00 39.24  ? 155 LEU B CD2 1 
ATOM   2953 N  N   . ASP B 1 156 ? 37.960  18.143  -15.451 1.00 24.91  ? 156 ASP B N   1 
ATOM   2954 C  CA  . ASP B 1 156 ? 38.624  17.262  -14.512 1.00 24.66  ? 156 ASP B CA  1 
ATOM   2955 C  C   . ASP B 1 156 ? 37.769  16.875  -13.317 1.00 23.47  ? 156 ASP B C   1 
ATOM   2956 O  O   . ASP B 1 156 ? 38.133  17.190  -12.193 1.00 24.26  ? 156 ASP B O   1 
ATOM   2957 C  CB  . ASP B 1 156 ? 39.882  17.960  -13.958 1.00 34.90  ? 156 ASP B CB  1 
ATOM   2958 C  CG  . ASP B 1 156 ? 40.779  18.115  -15.160 1.00 43.09  ? 156 ASP B CG  1 
ATOM   2959 O  OD1 . ASP B 1 156 ? 41.862  18.710  -15.079 1.00 66.59  ? 156 ASP B OD1 1 
ATOM   2960 O  OD2 . ASP B 1 156 ? 40.309  17.573  -16.190 1.00 62.39  ? 156 ASP B OD2 1 
ATOM   2961 N  N   . LEU B 1 157 ? 36.680  16.233  -13.656 1.00 23.92  ? 157 LEU B N   1 
ATOM   2962 C  CA  . LEU B 1 157 ? 35.661  15.943  -12.664 1.00 23.48  ? 157 LEU B CA  1 
ATOM   2963 C  C   . LEU B 1 157 ? 36.135  14.924  -11.636 1.00 25.15  ? 157 LEU B C   1 
ATOM   2964 O  O   . LEU B 1 157 ? 36.996  14.110  -11.878 1.00 24.91  ? 157 LEU B O   1 
ATOM   2965 C  CB  . LEU B 1 157 ? 34.386  15.398  -13.305 1.00 24.84  ? 157 LEU B CB  1 
ATOM   2966 C  CG  . LEU B 1 157 ? 33.673  16.327  -14.298 1.00 31.74  ? 157 LEU B CG  1 
ATOM   2967 C  CD1 . LEU B 1 157 ? 32.483  15.606  -14.951 1.00 39.82  ? 157 LEU B CD1 1 
ATOM   2968 C  CD2 . LEU B 1 157 ? 33.293  17.608  -13.582 1.00 40.57  ? 157 LEU B CD2 1 
ATOM   2969 N  N   . PRO B 1 158 ? 35.511  14.964  -10.480 1.00 22.31  ? 158 PRO B N   1 
ATOM   2970 C  CA  . PRO B 1 158 ? 35.725  13.894  -9.522  1.00 22.56  ? 158 PRO B CA  1 
ATOM   2971 C  C   . PRO B 1 158 ? 35.141  12.617  -10.140 1.00 22.56  ? 158 PRO B C   1 
ATOM   2972 O  O   . PRO B 1 158 ? 34.384  12.582  -11.074 1.00 27.37  ? 158 PRO B O   1 
ATOM   2973 C  CB  . PRO B 1 158 ? 34.934  14.347  -8.302  1.00 23.82  ? 158 PRO B CB  1 
ATOM   2974 C  CG  . PRO B 1 158 ? 33.912  15.280  -8.862  1.00 23.66  ? 158 PRO B CG  1 
ATOM   2975 C  CD  . PRO B 1 158 ? 34.559  15.975  -10.016 1.00 23.28  ? 158 PRO B CD  1 
ATOM   2976 N  N   . SER B 1 159 ? 35.597  11.510  -9.565  1.00 27.07  ? 159 SER B N   1 
ATOM   2977 C  CA  . SER B 1 159 ? 35.118  10.244  -10.124 1.00 31.04  ? 159 SER B CA  1 
ATOM   2978 C  C   . SER B 1 159 ? 33.835  9.846   -9.406  1.00 28.44  ? 159 SER B C   1 
ATOM   2979 O  O   . SER B 1 159 ? 33.713  8.751   -8.855  1.00 37.53  ? 159 SER B O   1 
ATOM   2980 C  CB  . SER B 1 159 ? 36.209  9.189   -9.991  1.00 41.56  ? 159 SER B CB  1 
ATOM   2981 O  OG  . SER B 1 159 ? 36.409  8.933   -8.598  1.00 59.30  ? 159 SER B OG  1 
ATOM   2982 N  N   . SER B 1 160 ? 32.864  10.757  -9.400  1.00 25.13  ? 160 SER B N   1 
ATOM   2983 C  CA  . SER B 1 160 ? 31.663  10.432  -8.630  1.00 23.63  ? 160 SER B CA  1 
ATOM   2984 C  C   . SER B 1 160 ? 30.431  10.181  -9.480  1.00 21.77  ? 160 SER B C   1 
ATOM   2985 O  O   . SER B 1 160 ? 29.300  10.155  -8.975  1.00 22.09  ? 160 SER B O   1 
ATOM   2986 C  CB  . SER B 1 160 ? 31.405  11.549  -7.628  1.00 25.06  ? 160 SER B CB  1 
ATOM   2987 O  OG  . SER B 1 160 ? 31.279  12.808  -8.224  1.00 28.36  ? 160 SER B OG  1 
ATOM   2988 N  N   . GLY B 1 161 ? 30.623  9.978   -10.777 1.00 19.90  ? 161 GLY B N   1 
ATOM   2989 C  CA  . GLY B 1 161 ? 29.562  9.425   -11.594 1.00 20.81  ? 161 GLY B CA  1 
ATOM   2990 C  C   . GLY B 1 161 ? 28.414  10.346  -11.950 1.00 19.87  ? 161 GLY B C   1 
ATOM   2991 O  O   . GLY B 1 161 ? 27.333  9.837   -12.276 1.00 19.22  ? 161 GLY B O   1 
ATOM   2992 N  N   . GLU B 1 162 ? 28.631  11.652  -11.927 1.00 18.66  ? 162 GLU B N   1 
ATOM   2993 C  CA  . GLU B 1 162 ? 27.588  12.638  -12.096 1.00 18.57  ? 162 GLU B CA  1 
ATOM   2994 C  C   . GLU B 1 162 ? 28.060  13.964  -12.734 1.00 20.80  ? 162 GLU B C   1 
ATOM   2995 O  O   . GLU B 1 162 ? 29.256  14.276  -12.658 1.00 20.70  ? 162 GLU B O   1 
ATOM   2996 C  CB  . GLU B 1 162 ? 26.982  13.038  -10.750 1.00 28.00  ? 162 GLU B CB  1 
ATOM   2997 C  CG  . GLU B 1 162 ? 26.571  12.157  -9.636  1.00 30.44  ? 162 GLU B CG  1 
ATOM   2998 C  CD  . GLU B 1 162 ? 26.143  12.983  -8.428  1.00 26.08  ? 162 GLU B CD  1 
ATOM   2999 O  OE1 . GLU B 1 162 ? 24.967  13.388  -8.548  1.00 22.49  ? 162 GLU B OE1 1 
ATOM   3000 O  OE2 . GLU B 1 162 ? 26.904  13.194  -7.485  1.00 25.96  ? 162 GLU B OE2 1 
ATOM   3001 N  N   . GLY B 1 163 ? 27.114  14.729  -13.301 1.00 18.01  ? 163 GLY B N   1 
ATOM   3002 C  CA  . GLY B 1 163 ? 27.406  16.077  -13.782 1.00 18.12  ? 163 GLY B CA  1 
ATOM   3003 C  C   . GLY B 1 163 ? 27.324  16.246  -15.285 1.00 18.08  ? 163 GLY B C   1 
ATOM   3004 O  O   . GLY B 1 163 ? 27.279  17.405  -15.741 1.00 20.12  ? 163 GLY B O   1 
ATOM   3005 N  N   . LEU B 1 164 ? 27.302  15.133  -16.038 1.00 18.05  ? 164 LEU B N   1 
ATOM   3006 C  CA  . LEU B 1 164 ? 27.261  15.253  -17.494 1.00 17.18  ? 164 LEU B CA  1 
ATOM   3007 C  C   . LEU B 1 164 ? 26.151  14.430  -18.139 1.00 15.28  ? 164 LEU B C   1 
ATOM   3008 O  O   . LEU B 1 164 ? 26.200  14.085  -19.327 1.00 16.83  ? 164 LEU B O   1 
ATOM   3009 C  CB  . LEU B 1 164 ? 28.614  14.868  -18.102 1.00 17.98  ? 164 LEU B CB  1 
ATOM   3010 C  CG  . LEU B 1 164 ? 29.798  15.772  -17.701 1.00 19.78  ? 164 LEU B CG  1 
ATOM   3011 C  CD1 . LEU B 1 164 ? 31.121  15.185  -18.221 1.00 22.70  ? 164 LEU B CD1 1 
ATOM   3012 C  CD2 . LEU B 1 164 ? 29.575  17.197  -18.169 1.00 21.31  ? 164 LEU B CD2 1 
ATOM   3013 N  N   . ALA B 1 165 ? 25.115  14.095  -17.363 1.00 15.70  ? 165 ALA B N   1 
ATOM   3014 C  CA  . ALA B 1 165 ? 24.031  13.300  -17.902 1.00 15.03  ? 165 ALA B CA  1 
ATOM   3015 C  C   . ALA B 1 165 ? 23.375  13.974  -19.115 1.00 14.68  ? 165 ALA B C   1 
ATOM   3016 O  O   . ALA B 1 165 ? 22.885  13.300  -20.042 1.00 15.35  ? 165 ALA B O   1 
ATOM   3017 C  CB  . ALA B 1 165 ? 23.006  13.032  -16.821 1.00 15.75  ? 165 ALA B CB  1 
ATOM   3018 N  N   . PHE B 1 166 ? 23.361  15.320  -19.108 1.00 16.45  ? 166 PHE B N   1 
ATOM   3019 C  CA  . PHE B 1 166 ? 22.737  16.049  -20.196 1.00 15.65  ? 166 PHE B CA  1 
ATOM   3020 C  C   . PHE B 1 166 ? 23.251  15.614  -21.570 1.00 16.28  ? 166 PHE B C   1 
ATOM   3021 O  O   . PHE B 1 166 ? 22.558  15.631  -22.600 1.00 16.16  ? 166 PHE B O   1 
ATOM   3022 C  CB  . PHE B 1 166 ? 22.992  17.561  -19.991 1.00 15.90  ? 166 PHE B CB  1 
ATOM   3023 C  CG  . PHE B 1 166 ? 22.531  18.336  -21.234 1.00 16.52  ? 166 PHE B CG  1 
ATOM   3024 C  CD1 . PHE B 1 166 ? 21.172  18.529  -21.457 1.00 18.43  ? 166 PHE B CD1 1 
ATOM   3025 C  CD2 . PHE B 1 166 ? 23.449  18.854  -22.138 1.00 16.92  ? 166 PHE B CD2 1 
ATOM   3026 C  CE1 . PHE B 1 166 ? 20.746  19.211  -22.576 1.00 18.98  ? 166 PHE B CE1 1 
ATOM   3027 C  CE2 . PHE B 1 166 ? 23.018  19.529  -23.267 1.00 19.63  ? 166 PHE B CE2 1 
ATOM   3028 C  CZ  . PHE B 1 166 ? 21.666  19.712  -23.474 1.00 20.56  ? 166 PHE B CZ  1 
ATOM   3029 N  N   . PHE B 1 167 ? 24.524  15.204  -21.617 1.00 16.40  ? 167 PHE B N   1 
ATOM   3030 C  CA  . PHE B 1 167 ? 25.117  14.888  -22.917 1.00 17.91  ? 167 PHE B CA  1 
ATOM   3031 C  C   . PHE B 1 167 ? 24.854  13.482  -23.408 1.00 19.99  ? 167 PHE B C   1 
ATOM   3032 O  O   . PHE B 1 167 ? 25.334  13.128  -24.490 1.00 22.47  ? 167 PHE B O   1 
ATOM   3033 C  CB  . PHE B 1 167 ? 26.637  15.133  -22.904 1.00 18.50  ? 167 PHE B CB  1 
ATOM   3034 C  CG  . PHE B 1 167 ? 26.905  16.624  -22.701 1.00 19.32  ? 167 PHE B CG  1 
ATOM   3035 C  CD1 . PHE B 1 167 ? 26.904  17.481  -23.765 1.00 23.34  ? 167 PHE B CD1 1 
ATOM   3036 C  CD2 . PHE B 1 167 ? 27.134  17.111  -21.428 1.00 26.02  ? 167 PHE B CD2 1 
ATOM   3037 C  CE1 . PHE B 1 167 ? 27.113  18.846  -23.596 1.00 29.24  ? 167 PHE B CE1 1 
ATOM   3038 C  CE2 . PHE B 1 167 ? 27.336  18.474  -21.244 1.00 30.82  ? 167 PHE B CE2 1 
ATOM   3039 C  CZ  . PHE B 1 167 ? 27.325  19.341  -22.321 1.00 32.62  ? 167 PHE B CZ  1 
ATOM   3040 N  N   . THR B 1 168 ? 24.103  12.708  -22.657 1.00 15.66  ? 168 THR B N   1 
ATOM   3041 C  CA  . THR B 1 168 ? 23.693  11.402  -23.145 1.00 16.46  ? 168 THR B CA  1 
ATOM   3042 C  C   . THR B 1 168 ? 22.185  11.283  -23.164 1.00 16.41  ? 168 THR B C   1 
ATOM   3043 O  O   . THR B 1 168 ? 21.521  11.539  -22.150 1.00 16.08  ? 168 THR B O   1 
ATOM   3044 C  CB  . THR B 1 168 ? 24.227  10.301  -22.198 1.00 17.90  ? 168 THR B CB  1 
ATOM   3045 O  OG1 . THR B 1 168 ? 25.644  10.297  -22.248 1.00 17.50  ? 168 THR B OG1 1 
ATOM   3046 C  CG2 . THR B 1 168 ? 23.690  8.945   -22.623 1.00 18.81  ? 168 THR B CG2 1 
ATOM   3047 N  N   . PHE B 1 169 ? 21.675  10.884  -24.313 1.00 17.31  ? 169 PHE B N   1 
ATOM   3048 C  CA  . PHE B 1 169 ? 20.244  10.579  -24.500 1.00 17.36  ? 169 PHE B CA  1 
ATOM   3049 C  C   . PHE B 1 169 ? 20.087  9.073   -24.404 1.00 16.74  ? 169 PHE B C   1 
ATOM   3050 O  O   . PHE B 1 169 ? 20.262  8.381   -25.407 1.00 17.23  ? 169 PHE B O   1 
ATOM   3051 C  CB  . PHE B 1 169 ? 19.740  11.089  -25.834 1.00 18.18  ? 169 PHE B CB  1 
ATOM   3052 C  CG  . PHE B 1 169 ? 19.644  12.593  -26.044 1.00 17.44  ? 169 PHE B CG  1 
ATOM   3053 C  CD1 . PHE B 1 169 ? 20.740  13.408  -26.313 1.00 19.97  ? 169 PHE B CD1 1 
ATOM   3054 C  CD2 . PHE B 1 169 ? 18.411  13.210  -25.985 1.00 18.34  ? 169 PHE B CD2 1 
ATOM   3055 C  CE1 . PHE B 1 169 ? 20.631  14.778  -26.518 1.00 20.00  ? 169 PHE B CE1 1 
ATOM   3056 C  CE2 . PHE B 1 169 ? 18.291  14.584  -26.190 1.00 19.03  ? 169 PHE B CE2 1 
ATOM   3057 C  CZ  . PHE B 1 169 ? 19.388  15.390  -26.455 1.00 18.66  ? 169 PHE B CZ  1 
ATOM   3058 N  N   . PRO B 1 170 ? 19.837  8.528   -23.231 1.00 16.11  ? 170 PRO B N   1 
ATOM   3059 C  CA  . PRO B 1 170 ? 19.948  7.067   -23.080 1.00 16.83  ? 170 PRO B CA  1 
ATOM   3060 C  C   . PRO B 1 170 ? 18.866  6.303   -23.844 1.00 16.91  ? 170 PRO B C   1 
ATOM   3061 O  O   . PRO B 1 170 ? 19.087  5.128   -24.077 1.00 18.56  ? 170 PRO B O   1 
ATOM   3062 C  CB  . PRO B 1 170 ? 19.736  6.863   -21.580 1.00 15.79  ? 170 PRO B CB  1 
ATOM   3063 C  CG  . PRO B 1 170 ? 18.878  8.020   -21.181 1.00 14.18  ? 170 PRO B CG  1 
ATOM   3064 C  CD  . PRO B 1 170 ? 19.428  9.189   -21.986 1.00 15.15  ? 170 PRO B CD  1 
ATOM   3065 N  N   . ASN B 1 171 ? 17.742  6.940   -24.208 1.00 16.22  ? 171 ASN B N   1 
ATOM   3066 C  CA  . ASN B 1 171 ? 16.676  6.218   -24.901 1.00 17.08  ? 171 ASN B CA  1 
ATOM   3067 C  C   . ASN B 1 171 ? 16.768  6.343   -26.418 1.00 16.73  ? 171 ASN B C   1 
ATOM   3068 O  O   . ASN B 1 171 ? 15.836  5.984   -27.136 1.00 19.71  ? 171 ASN B O   1 
ATOM   3069 C  CB  . ASN B 1 171 ? 15.315  6.677   -24.373 1.00 17.71  ? 171 ASN B CB  1 
ATOM   3070 C  CG  . ASN B 1 171 ? 15.137  6.525   -22.863 1.00 16.54  ? 171 ASN B CG  1 
ATOM   3071 O  OD1 . ASN B 1 171 ? 14.625  7.427   -22.152 1.00 19.14  ? 171 ASN B OD1 1 
ATOM   3072 N  ND2 . ASN B 1 171 ? 15.543  5.381   -22.363 1.00 14.60  ? 171 ASN B ND2 1 
ATOM   3073 N  N   . ILE B 1 172 ? 17.916  6.838   -26.872 1.00 18.30  ? 172 ILE B N   1 
ATOM   3074 C  CA  . ILE B 1 172 ? 18.285  6.797   -28.283 1.00 19.15  ? 172 ILE B CA  1 
ATOM   3075 C  C   . ILE B 1 172 ? 19.524  5.930   -28.450 1.00 20.00  ? 172 ILE B C   1 
ATOM   3076 O  O   . ILE B 1 172 ? 20.603  6.275   -27.960 1.00 25.29  ? 172 ILE B O   1 
ATOM   3077 C  CB  . ILE B 1 172 ? 18.502  8.212   -28.839 1.00 18.57  ? 172 ILE B CB  1 
ATOM   3078 C  CG1 . ILE B 1 172 ? 17.190  9.014   -28.801 1.00 18.28  ? 172 ILE B CG1 1 
ATOM   3079 C  CG2 . ILE B 1 172 ? 19.126  8.185   -30.226 1.00 20.47  ? 172 ILE B CG2 1 
ATOM   3080 C  CD1 . ILE B 1 172 ? 17.355  10.454  -29.181 1.00 22.49  ? 172 ILE B CD1 1 
ATOM   3081 N  N   . ALA B 1 173 ? 19.365  4.790   -29.106 1.00 21.86  ? 173 ALA B N   1 
ATOM   3082 C  CA  . ALA B 1 173 ? 20.528  3.910   -29.302 1.00 23.67  ? 173 ALA B CA  1 
ATOM   3083 C  C   . ALA B 1 173 ? 21.439  4.407   -30.415 1.00 27.56  ? 173 ALA B C   1 
ATOM   3084 O  O   . ALA B 1 173 ? 22.644  4.200   -30.380 1.00 29.00  ? 173 ALA B O   1 
ATOM   3085 C  CB  . ALA B 1 173 ? 20.117  2.501   -29.631 1.00 25.81  ? 173 ALA B CB  1 
ATOM   3086 N  N   . SER B 1 174 ? 20.816  5.042   -31.382 1.00 30.31  ? 174 SER B N   1 
ATOM   3087 C  CA  . SER B 1 174 ? 21.479  5.543   -32.556 1.00 30.14  ? 174 SER B CA  1 
ATOM   3088 C  C   . SER B 1 174 ? 21.007  6.953   -32.901 1.00 27.62  ? 174 SER B C   1 
ATOM   3089 O  O   . SER B 1 174 ? 19.863  7.146   -33.312 1.00 29.83  ? 174 SER B O   1 
ATOM   3090 C  CB  . SER B 1 174 ? 21.174  4.664   -33.775 1.00 39.96  ? 174 SER B CB  1 
ATOM   3091 O  OG  . SER B 1 174 ? 21.886  5.152   -34.929 1.00 48.37  ? 174 SER B OG  1 
ATOM   3092 N  N   . ALA B 1 175 ? 21.925  7.906   -32.728 1.00 32.15  ? 175 ALA B N   1 
ATOM   3093 C  CA  . ALA B 1 175 ? 21.574  9.282   -33.087 1.00 31.71  ? 175 ALA B CA  1 
ATOM   3094 C  C   . ALA B 1 175 ? 21.197  9.372   -34.560 1.00 31.28  ? 175 ALA B C   1 
ATOM   3095 O  O   . ALA B 1 175 ? 20.243  10.025  -34.986 1.00 34.23  ? 175 ALA B O   1 
ATOM   3096 C  CB  . ALA B 1 175 ? 22.745  10.197  -32.732 1.00 33.24  ? 175 ALA B CB  1 
ATOM   3097 N  N   . THR B 1 176 ? 22.004  8.692   -35.377 1.00 34.50  ? 176 THR B N   1 
ATOM   3098 C  CA  . THR B 1 176 ? 21.759  8.771   -36.814 1.00 37.61  ? 176 THR B CA  1 
ATOM   3099 C  C   . THR B 1 176 ? 20.351  8.340   -37.198 1.00 34.24  ? 176 THR B C   1 
ATOM   3100 O  O   . THR B 1 176 ? 19.586  9.002   -37.901 1.00 32.98  ? 176 THR B O   1 
ATOM   3101 C  CB  . THR B 1 176 ? 22.761  7.874   -37.574 1.00 42.72  ? 176 THR B CB  1 
ATOM   3102 O  OG1 . THR B 1 176 ? 24.050  8.487   -37.470 1.00 51.14  ? 176 THR B OG1 1 
ATOM   3103 C  CG2 . THR B 1 176 ? 22.415  7.796   -39.047 1.00 49.47  ? 176 THR B CG2 1 
ATOM   3104 N  N   . LYS B 1 177 ? 20.036  7.153   -36.677 1.00 34.24  ? 177 LYS B N   1 
ATOM   3105 C  CA  . LYS B 1 177 ? 18.735  6.585   -37.015 1.00 35.21  ? 177 LYS B CA  1 
ATOM   3106 C  C   . LYS B 1 177 ? 17.617  7.392   -36.380 1.00 31.59  ? 177 LYS B C   1 
ATOM   3107 O  O   . LYS B 1 177 ? 16.573  7.534   -37.032 1.00 34.44  ? 177 LYS B O   1 
ATOM   3108 C  CB  . LYS B 1 177 ? 18.679  5.099   -36.640 1.00 41.29  ? 177 LYS B CB  1 
ATOM   3109 C  CG  . LYS B 1 177 ? 19.794  4.377   -37.418 1.00 54.07  ? 177 LYS B CG  1 
ATOM   3110 C  CD  . LYS B 1 177 ? 20.192  3.079   -36.755 1.00 60.83  ? 177 LYS B CD  1 
ATOM   3111 C  CE  . LYS B 1 177 ? 20.908  2.144   -37.719 1.00 69.62  ? 177 LYS B CE  1 
ATOM   3112 N  NZ  . LYS B 1 177 ? 21.630  1.075   -36.964 1.00 86.82  ? 177 LYS B NZ  1 
ATOM   3113 N  N   . PHE B 1 178 ? 17.787  7.936   -35.178 1.00 28.55  ? 178 PHE B N   1 
ATOM   3114 C  CA  . PHE B 1 178 ? 16.706  8.753   -34.626 1.00 26.21  ? 178 PHE B CA  1 
ATOM   3115 C  C   . PHE B 1 178 ? 16.479  9.997   -35.469 1.00 24.49  ? 178 PHE B C   1 
ATOM   3116 O  O   . PHE B 1 178 ? 15.345  10.419  -35.695 1.00 26.94  ? 178 PHE B O   1 
ATOM   3117 C  CB  . PHE B 1 178 ? 17.030  9.170   -33.185 1.00 24.71  ? 178 PHE B CB  1 
ATOM   3118 C  CG  . PHE B 1 178 ? 15.866  9.993   -32.648 1.00 21.59  ? 178 PHE B CG  1 
ATOM   3119 C  CD1 . PHE B 1 178 ? 14.736  9.317   -32.237 1.00 24.07  ? 178 PHE B CD1 1 
ATOM   3120 C  CD2 . PHE B 1 178 ? 15.895  11.377  -32.561 1.00 22.37  ? 178 PHE B CD2 1 
ATOM   3121 C  CE1 . PHE B 1 178 ? 13.642  10.045  -31.781 1.00 20.77  ? 178 PHE B CE1 1 
ATOM   3122 C  CE2 . PHE B 1 178 ? 14.803  12.092  -32.131 1.00 19.52  ? 178 PHE B CE2 1 
ATOM   3123 C  CZ  . PHE B 1 178 ? 13.656  11.417  -31.731 1.00 21.19  ? 178 PHE B CZ  1 
ATOM   3124 N  N   . LYS B 1 179 ? 17.589  10.635  -35.852 1.00 26.54  ? 179 LYS B N   1 
ATOM   3125 C  CA  . LYS B 1 179 ? 17.514  11.856  -36.639 1.00 29.15  ? 179 LYS B CA  1 
ATOM   3126 C  C   . LYS B 1 179 ? 16.795  11.555  -37.942 1.00 29.67  ? 179 LYS B C   1 
ATOM   3127 O  O   . LYS B 1 179 ? 16.019  12.399  -38.407 1.00 32.23  ? 179 LYS B O   1 
ATOM   3128 C  CB  . LYS B 1 179 ? 18.887  12.470  -36.920 1.00 31.53  ? 179 LYS B CB  1 
ATOM   3129 C  CG  . LYS B 1 179 ? 19.494  13.136  -35.691 1.00 35.10  ? 179 LYS B CG  1 
ATOM   3130 C  CD  . LYS B 1 179 ? 20.772  13.889  -36.004 1.00 45.49  ? 179 LYS B CD  1 
ATOM   3131 C  CE  . LYS B 1 179 ? 21.904  12.910  -36.261 1.00 46.36  ? 179 LYS B CE  1 
ATOM   3132 N  NZ  . LYS B 1 179 ? 23.227  13.591  -36.217 1.00 56.85  ? 179 LYS B NZ  1 
ATOM   3133 N  N   . GLN B 1 180 ? 17.013  10.377  -38.508 1.00 29.20  ? 180 GLN B N   1 
ATOM   3134 C  CA  . GLN B 1 180 ? 16.255  10.085  -39.729 1.00 29.94  ? 180 GLN B CA  1 
ATOM   3135 C  C   . GLN B 1 180 ? 14.741  10.043  -39.532 1.00 29.70  ? 180 GLN B C   1 
ATOM   3136 O  O   . GLN B 1 180 ? 13.975  10.573  -40.337 1.00 31.15  ? 180 GLN B O   1 
ATOM   3137 C  CB  . GLN B 1 180 ? 16.713  8.753   -40.320 1.00 35.92  ? 180 GLN B CB  1 
ATOM   3138 C  CG  . GLN B 1 180 ? 18.183  8.716   -40.699 1.00 44.66  ? 180 GLN B CG  1 
ATOM   3139 C  CD  . GLN B 1 180 ? 18.731  7.316   -40.905 1.00 53.08  ? 180 GLN B CD  1 
ATOM   3140 O  OE1 . GLN B 1 180 ? 19.946  7.147   -41.081 1.00 68.62  ? 180 GLN B OE1 1 
ATOM   3141 N  NE2 . GLN B 1 180 ? 17.924  6.258   -40.900 1.00 60.06  ? 180 GLN B NE2 1 
ATOM   3142 N  N   . LEU B 1 181 ? 14.339  9.362   -38.479 1.00 26.54  ? 181 LEU B N   1 
ATOM   3143 C  CA  . LEU B 1 181 ? 12.929  9.247   -38.144 1.00 26.45  ? 181 LEU B CA  1 
ATOM   3144 C  C   . LEU B 1 181 ? 12.360  10.635  -37.877 1.00 24.46  ? 181 LEU B C   1 
ATOM   3145 O  O   . LEU B 1 181 ? 11.307  11.043  -38.338 1.00 25.92  ? 181 LEU B O   1 
ATOM   3146 C  CB  . LEU B 1 181 ? 12.726  8.372   -36.906 1.00 26.40  ? 181 LEU B CB  1 
ATOM   3147 C  CG  . LEU B 1 181 ? 11.333  8.266   -36.277 1.00 25.93  ? 181 LEU B CG  1 
ATOM   3148 C  CD1 . LEU B 1 181 ? 10.284  7.872   -37.321 1.00 32.92  ? 181 LEU B CD1 1 
ATOM   3149 C  CD2 . LEU B 1 181 ? 11.276  7.276   -35.109 1.00 30.57  ? 181 LEU B CD2 1 
ATOM   3150 N  N   . TYR B 1 182 ? 13.084  11.403  -37.060 1.00 25.39  ? 182 TYR B N   1 
ATOM   3151 C  CA  . TYR B 1 182 ? 12.591  12.715  -36.654 1.00 25.00  ? 182 TYR B CA  1 
ATOM   3152 C  C   . TYR B 1 182 ? 12.398  13.611  -37.888 1.00 24.36  ? 182 TYR B C   1 
ATOM   3153 O  O   . TYR B 1 182 ? 11.423  14.339  -38.009 1.00 25.15  ? 182 TYR B O   1 
ATOM   3154 C  CB  . TYR B 1 182 ? 13.521  13.384  -35.671 1.00 23.30  ? 182 TYR B CB  1 
ATOM   3155 C  CG  . TYR B 1 182 ? 12.947  14.560  -34.899 1.00 21.95  ? 182 TYR B CG  1 
ATOM   3156 C  CD1 . TYR B 1 182 ? 12.212  14.334  -33.756 1.00 20.91  ? 182 TYR B CD1 1 
ATOM   3157 C  CD2 . TYR B 1 182 ? 13.118  15.885  -35.280 1.00 26.08  ? 182 TYR B CD2 1 
ATOM   3158 C  CE1 . TYR B 1 182 ? 11.671  15.383  -33.025 1.00 23.64  ? 182 TYR B CE1 1 
ATOM   3159 C  CE2 . TYR B 1 182 ? 12.597  16.938  -34.567 1.00 27.23  ? 182 TYR B CE2 1 
ATOM   3160 C  CZ  . TYR B 1 182 ? 11.870  16.682  -33.437 1.00 24.62  ? 182 TYR B CZ  1 
ATOM   3161 O  OH  . TYR B 1 182 ? 11.350  17.727  -32.710 1.00 30.23  ? 182 TYR B OH  1 
ATOM   3162 N  N   . ARG B 1 183 ? 13.354  13.540  -38.816 1.00 26.09  ? 183 ARG B N   1 
ATOM   3163 C  CA  . ARG B 1 183 ? 13.148  14.353  -40.004 1.00 26.47  ? 183 ARG B CA  1 
ATOM   3164 C  C   . ARG B 1 183 ? 11.976  13.884  -40.858 1.00 27.59  ? 183 ARG B C   1 
ATOM   3165 O  O   . ARG B 1 183 ? 11.277  14.717  -41.445 1.00 25.74  ? 183 ARG B O   1 
ATOM   3166 C  CB  . ARG B 1 183 ? 14.448  14.337  -40.815 1.00 28.30  ? 183 ARG B CB  1 
ATOM   3167 C  CG  . ARG B 1 183 ? 15.583  15.144  -40.225 1.00 31.46  ? 183 ARG B CG  1 
ATOM   3168 C  CD  . ARG B 1 183 ? 16.761  15.145  -41.176 1.00 36.72  ? 183 ARG B CD  1 
ATOM   3169 N  NE  . ARG B 1 183 ? 18.005  15.590  -40.544 1.00 38.61  ? 183 ARG B NE  1 
ATOM   3170 C  CZ  . ARG B 1 183 ? 19.084  14.916  -40.217 1.00 43.63  ? 183 ARG B CZ  1 
ATOM   3171 N  NH1 . ARG B 1 183 ? 19.179  13.605  -40.446 1.00 44.73  ? 183 ARG B NH1 1 
ATOM   3172 N  NH2 . ARG B 1 183 ? 20.124  15.534  -39.639 1.00 45.11  ? 183 ARG B NH2 1 
ATOM   3173 N  N   . SER B 1 184 ? 11.730  12.567  -40.960 1.00 26.35  ? 184 SER B N   1 
ATOM   3174 C  CA  . SER B 1 184 ? 10.551  12.062  -41.630 1.00 27.81  ? 184 SER B CA  1 
ATOM   3175 C  C   . SER B 1 184 ? 9.271   12.611  -41.001 1.00 26.32  ? 184 SER B C   1 
ATOM   3176 O  O   . SER B 1 184 ? 8.345   13.015  -41.697 1.00 28.61  ? 184 SER B O   1 
ATOM   3177 C  CB  A SER B 1 184 ? 10.624  10.530  -41.592 0.50 32.40  ? 184 SER B CB  1 
ATOM   3178 C  CB  B SER B 1 184 ? 10.415  10.535  -41.598 0.50 31.33  ? 184 SER B CB  1 
ATOM   3179 O  OG  A SER B 1 184 ? 11.812  10.043  -42.235 0.50 27.98  ? 184 SER B OG  1 
ATOM   3180 O  OG  B SER B 1 184 ? 9.332   10.129  -42.442 0.50 28.20  ? 184 SER B OG  1 
ATOM   3181 N  N   . ARG B 1 185 ? 9.258   12.587  -39.659 1.00 25.31  ? 185 ARG B N   1 
ATOM   3182 C  CA  . ARG B 1 185 ? 8.077   13.085  -38.948 1.00 24.79  ? 185 ARG B CA  1 
ATOM   3183 C  C   . ARG B 1 185 ? 7.956   14.578  -39.208 1.00 25.14  ? 185 ARG B C   1 
ATOM   3184 O  O   . ARG B 1 185 ? 6.830   15.015  -39.475 1.00 25.64  ? 185 ARG B O   1 
ATOM   3185 C  CB  . ARG B 1 185 ? 8.141   12.754  -37.460 1.00 23.50  ? 185 ARG B CB  1 
ATOM   3186 C  CG  . ARG B 1 185 ? 8.047   11.282  -37.073 1.00 23.75  ? 185 ARG B CG  1 
ATOM   3187 C  CD  . ARG B 1 185 ? 6.734   10.651  -37.457 1.00 25.59  ? 185 ARG B CD  1 
ATOM   3188 N  NE  . ARG B 1 185 ? 6.560   9.370   -36.750 1.00 22.66  ? 185 ARG B NE  1 
ATOM   3189 C  CZ  . ARG B 1 185 ? 6.050   9.269   -35.516 1.00 21.57  ? 185 ARG B CZ  1 
ATOM   3190 N  NH1 . ARG B 1 185 ? 5.649   10.333  -34.816 1.00 23.06  ? 185 ARG B NH1 1 
ATOM   3191 N  NH2 . ARG B 1 185 ? 5.930   8.076   -34.953 1.00 25.95  ? 185 ARG B NH2 1 
ATOM   3192 N  N   . MET B 1 186 ? 9.044   15.332  -39.151 1.00 23.34  ? 186 MET B N   1 
ATOM   3193 C  CA  . MET B 1 186 ? 9.013   16.764  -39.412 1.00 25.40  ? 186 MET B CA  1 
ATOM   3194 C  C   . MET B 1 186 ? 8.397   17.026  -40.781 1.00 26.90  ? 186 MET B C   1 
ATOM   3195 O  O   . MET B 1 186 ? 7.583   17.930  -40.994 1.00 26.23  ? 186 MET B O   1 
ATOM   3196 C  CB  . MET B 1 186 ? 10.402  17.401  -39.405 1.00 28.29  ? 186 MET B CB  1 
ATOM   3197 C  CG  . MET B 1 186 ? 11.002  17.714  -38.054 1.00 32.90  ? 186 MET B CG  1 
ATOM   3198 S  SD  . MET B 1 186 ? 12.339  18.914  -38.043 1.00 39.05  ? 186 MET B SD  1 
ATOM   3199 C  CE  . MET B 1 186 ? 13.398  18.356  -39.341 1.00 46.20  ? 186 MET B CE  1 
ATOM   3200 N  N   . ASN B 1 187 ? 8.823   16.190  -41.728 1.00 27.16  ? 187 ASN B N   1 
ATOM   3201 C  CA  . ASN B 1 187 ? 8.371   16.377  -43.099 1.00 29.56  ? 187 ASN B CA  1 
ATOM   3202 C  C   . ASN B 1 187 ? 6.940   15.925  -43.316 1.00 29.88  ? 187 ASN B C   1 
ATOM   3203 O  O   . ASN B 1 187 ? 6.371   16.278  -44.368 1.00 33.54  ? 187 ASN B O   1 
ATOM   3204 C  CB  . ASN B 1 187 ? 9.290   15.615  -44.042 1.00 30.60  ? 187 ASN B CB  1 
ATOM   3205 C  CG  . ASN B 1 187 ? 10.682  16.238  -44.014 1.00 30.88  ? 187 ASN B CG  1 
ATOM   3206 O  OD1 . ASN B 1 187 ? 10.859  17.415  -43.712 1.00 32.89  ? 187 ASN B OD1 1 
ATOM   3207 N  ND2 . ASN B 1 187 ? 11.611  15.350  -44.341 1.00 33.35  ? 187 ASN B ND2 1 
ATOM   3208 N  N   . SER B 1 188 ? 6.403   15.197  -42.342 1.00 32.10  ? 188 SER B N   1 
ATOM   3209 C  CA  . SER B 1 188 ? 4.999   14.814  -42.388 1.00 33.75  ? 188 SER B CA  1 
ATOM   3210 C  C   . SER B 1 188 ? 4.067   15.921  -41.887 1.00 32.63  ? 188 SER B C   1 
ATOM   3211 O  O   . SER B 1 188 ? 2.855   15.875  -42.130 1.00 34.91  ? 188 SER B O   1 
ATOM   3212 C  CB  . SER B 1 188 ? 4.745   13.545  -41.559 1.00 33.42  ? 188 SER B CB  1 
ATOM   3213 O  OG  . SER B 1 188 ? 4.619   13.834  -40.175 1.00 35.92  ? 188 SER B OG  1 
ATOM   3214 N  N   . LEU B 1 189 ? 4.590   16.907  -41.182 1.00 32.25  ? 189 LEU B N   1 
ATOM   3215 C  CA  . LEU B 1 189 ? 3.781   17.974  -40.629 1.00 31.60  ? 189 LEU B CA  1 
ATOM   3216 C  C   . LEU B 1 189 ? 3.134   18.747  -41.782 1.00 34.74  ? 189 LEU B C   1 
ATOM   3217 O  O   . LEU B 1 189 ? 3.729   19.073  -42.804 1.00 38.13  ? 189 LEU B O   1 
ATOM   3218 C  CB  . LEU B 1 189 ? 4.610   18.954  -39.840 1.00 36.36  ? 189 LEU B CB  1 
ATOM   3219 C  CG  . LEU B 1 189 ? 4.689   19.174  -38.338 1.00 40.57  ? 189 LEU B CG  1 
ATOM   3220 C  CD1 . LEU B 1 189 ? 4.035   18.126  -37.499 1.00 36.24  ? 189 LEU B CD1 1 
ATOM   3221 C  CD2 . LEU B 1 189 ? 6.166   19.329  -37.947 1.00 34.12  ? 189 LEU B CD2 1 
ATOM   3222 N  N   . GLU B 1 190 ? 1.862   19.073  -41.567 1.00 36.78  ? 190 GLU B N   1 
ATOM   3223 C  CA  . GLU B 1 190 ? 1.180   19.812  -42.611 1.00 43.30  ? 190 GLU B CA  1 
ATOM   3224 C  C   . GLU B 1 190 ? 0.964   21.241  -42.129 1.00 37.79  ? 190 GLU B C   1 
ATOM   3225 O  O   . GLU B 1 190 ? 0.657   21.515  -40.958 1.00 37.79  ? 190 GLU B O   1 
ATOM   3226 C  CB  . GLU B 1 190 ? -0.081  19.038  -42.975 1.00 46.91  ? 190 GLU B CB  1 
ATOM   3227 C  CG  . GLU B 1 190 ? 0.383   17.673  -43.519 1.00 53.68  ? 190 GLU B CG  1 
ATOM   3228 C  CD  . GLU B 1 190 ? -0.760  16.683  -43.535 1.00 59.71  ? 190 GLU B CD  1 
ATOM   3229 O  OE1 . GLU B 1 190 ? -1.415  16.591  -44.593 1.00 69.70  ? 190 GLU B OE1 1 
ATOM   3230 O  OE2 . GLU B 1 190 ? -0.977  16.001  -42.509 1.00 73.12  ? 190 GLU B OE2 1 
ATOM   3231 N  N   . MET B 1 191 ? 1.205   22.137  -43.075 1.00 32.84  ? 191 MET B N   1 
ATOM   3232 C  CA  . MET B 1 191 ? 1.137   23.557  -42.753 1.00 29.11  ? 191 MET B CA  1 
ATOM   3233 C  C   . MET B 1 191 ? 1.035   24.358  -44.048 1.00 29.86  ? 191 MET B C   1 
ATOM   3234 O  O   . MET B 1 191 ? 1.445   23.933  -45.131 1.00 31.51  ? 191 MET B O   1 
ATOM   3235 C  CB  . MET B 1 191 ? 2.332   24.026  -41.920 1.00 31.84  ? 191 MET B CB  1 
ATOM   3236 C  CG  . MET B 1 191 ? 3.651   23.785  -42.597 1.00 32.82  ? 191 MET B CG  1 
ATOM   3237 S  SD  . MET B 1 191 ? 5.086   24.029  -41.538 1.00 31.58  ? 191 MET B SD  1 
ATOM   3238 C  CE  . MET B 1 191 ? 4.963   22.645  -40.440 1.00 32.90  ? 191 MET B CE  1 
ATOM   3239 N  N   . THR B 1 192 ? 0.452   25.525  -43.920 1.00 31.03  ? 192 THR B N   1 
ATOM   3240 C  CA  . THR B 1 192 ? 0.246   26.414  -45.070 1.00 29.71  ? 192 THR B CA  1 
ATOM   3241 C  C   . THR B 1 192 ? 1.598   27.034  -45.398 1.00 27.16  ? 192 THR B C   1 
ATOM   3242 O  O   . THR B 1 192 ? 2.510   27.022  -44.577 1.00 28.34  ? 192 THR B O   1 
ATOM   3243 C  CB  . THR B 1 192 ? -0.757  27.533  -44.792 1.00 32.41  ? 192 THR B CB  1 
ATOM   3244 O  OG1 . THR B 1 192 ? -0.307  28.286  -43.641 1.00 30.54  ? 192 THR B OG1 1 
ATOM   3245 C  CG2 . THR B 1 192 ? -2.129  26.947  -44.529 1.00 38.33  ? 192 THR B CG2 1 
ATOM   3246 N  N   . PRO B 1 193 ? 1.713   27.543  -46.603 1.00 30.61  ? 193 PRO B N   1 
ATOM   3247 C  CA  . PRO B 1 193 ? 2.952   28.255  -46.937 1.00 29.58  ? 193 PRO B CA  1 
ATOM   3248 C  C   . PRO B 1 193 ? 3.229   29.368  -45.950 1.00 30.12  ? 193 PRO B C   1 
ATOM   3249 O  O   . PRO B 1 193 ? 4.390   29.612  -45.660 1.00 29.42  ? 193 PRO B O   1 
ATOM   3250 C  CB  . PRO B 1 193 ? 2.626   28.833  -48.300 1.00 34.65  ? 193 PRO B CB  1 
ATOM   3251 C  CG  . PRO B 1 193 ? 1.622   27.874  -48.878 1.00 32.56  ? 193 PRO B CG  1 
ATOM   3252 C  CD  . PRO B 1 193 ? 0.753   27.472  -47.714 1.00 29.97  ? 193 PRO B CD  1 
ATOM   3253 N  N   . ALA B 1 194 ? 2.200   30.063  -45.457 1.00 29.63  ? 194 ALA B N   1 
ATOM   3254 C  CA  . ALA B 1 194 ? 2.510   31.177  -44.536 1.00 30.51  ? 194 ALA B CA  1 
ATOM   3255 C  C   . ALA B 1 194 ? 3.154   30.686  -43.260 1.00 31.23  ? 194 ALA B C   1 
ATOM   3256 O  O   . ALA B 1 194 ? 4.077   31.280  -42.677 1.00 27.83  ? 194 ALA B O   1 
ATOM   3257 C  CB  . ALA B 1 194 ? 1.232   31.939  -44.236 1.00 34.71  ? 194 ALA B CB  1 
ATOM   3258 N  N   . VAL B 1 195 ? 2.666   29.549  -42.755 1.00 26.50  ? 195 VAL B N   1 
ATOM   3259 C  CA  . VAL B 1 195 ? 3.168   29.040  -41.474 1.00 25.35  ? 195 VAL B CA  1 
ATOM   3260 C  C   . VAL B 1 195 ? 4.552   28.455  -41.693 1.00 24.25  ? 195 VAL B C   1 
ATOM   3261 O  O   . VAL B 1 195 ? 5.433   28.659  -40.844 1.00 24.20  ? 195 VAL B O   1 
ATOM   3262 C  CB  . VAL B 1 195 ? 2.209   28.017  -40.849 1.00 26.32  ? 195 VAL B CB  1 
ATOM   3263 C  CG1 . VAL B 1 195 ? 2.899   27.161  -39.766 1.00 29.87  ? 195 VAL B CG1 1 
ATOM   3264 C  CG2 . VAL B 1 195 ? 0.989   28.700  -40.229 1.00 31.38  ? 195 VAL B CG2 1 
ATOM   3265 N  N   . ARG B 1 196 ? 4.699   27.767  -42.838 1.00 25.40  ? 196 ARG B N   1 
ATOM   3266 C  CA  . ARG B 1 196 ? 6.019   27.206  -43.144 1.00 25.67  ? 196 ARG B CA  1 
ATOM   3267 C  C   . ARG B 1 196 ? 7.109   28.277  -43.141 1.00 24.80  ? 196 ARG B C   1 
ATOM   3268 O  O   . ARG B 1 196 ? 8.214   28.055  -42.590 1.00 25.43  ? 196 ARG B O   1 
ATOM   3269 C  CB  . ARG B 1 196 ? 6.026   26.452  -44.481 1.00 25.10  ? 196 ARG B CB  1 
ATOM   3270 C  CG  . ARG B 1 196 ? 7.357   25.743  -44.770 1.00 35.04  ? 196 ARG B CG  1 
ATOM   3271 C  CD  . ARG B 1 196 ? 7.307   25.215  -46.186 1.00 43.07  ? 196 ARG B CD  1 
ATOM   3272 N  NE  . ARG B 1 196 ? 8.518   24.562  -46.629 1.00 46.42  ? 196 ARG B NE  1 
ATOM   3273 C  CZ  . ARG B 1 196 ? 8.790   23.267  -46.599 1.00 48.53  ? 196 ARG B CZ  1 
ATOM   3274 N  NH1 . ARG B 1 196 ? 7.930   22.369  -46.119 1.00 58.34  ? 196 ARG B NH1 1 
ATOM   3275 N  NH2 . ARG B 1 196 ? 9.972   22.907  -47.071 1.00 55.19  ? 196 ARG B NH2 1 
ATOM   3276 N  N   . GLN B 1 197 ? 6.772   29.427  -43.718 1.00 23.33  ? 197 GLN B N   1 
ATOM   3277 C  CA  . GLN B 1 197 ? 7.734   30.539  -43.699 1.00 25.70  ? 197 GLN B CA  1 
ATOM   3278 C  C   . GLN B 1 197 ? 8.009   31.003  -42.275 1.00 24.89  ? 197 GLN B C   1 
ATOM   3279 O  O   . GLN B 1 197 ? 9.156   31.285  -41.892 1.00 24.12  ? 197 GLN B O   1 
ATOM   3280 C  CB  . GLN B 1 197 ? 7.266   31.711  -44.574 1.00 29.61  ? 197 GLN B CB  1 
ATOM   3281 C  CG  . GLN B 1 197 ? 8.243   32.881  -44.552 1.00 32.06  ? 197 GLN B CG  1 
ATOM   3282 C  CD  . GLN B 1 197 ? 9.641   32.636  -45.064 1.00 39.25  ? 197 GLN B CD  1 
ATOM   3283 O  OE1 . GLN B 1 197 ? 9.864   31.873  -46.028 1.00 43.35  ? 197 GLN B OE1 1 
ATOM   3284 N  NE2 . GLN B 1 197 ? 10.632  33.285  -44.458 1.00 47.88  ? 197 GLN B NE2 1 
ATOM   3285 N  N   . ARG B 1 198 ? 6.991   31.088  -41.445 1.00 23.64  ? 198 ARG B N   1 
ATOM   3286 C  CA  . ARG B 1 198 ? 7.233   31.473  -40.055 1.00 22.40  ? 198 ARG B CA  1 
ATOM   3287 C  C   . ARG B 1 198 ? 7.963   30.421  -39.249 1.00 20.94  ? 198 ARG B C   1 
ATOM   3288 O  O   . ARG B 1 198 ? 8.705   30.764  -38.309 1.00 20.09  ? 198 ARG B O   1 
ATOM   3289 C  CB  . ARG B 1 198 ? 5.914   31.825  -39.362 1.00 23.66  ? 198 ARG B CB  1 
ATOM   3290 C  CG  . ARG B 1 198 ? 5.407   33.228  -39.653 1.00 27.23  ? 198 ARG B CG  1 
ATOM   3291 C  CD  . ARG B 1 198 ? 4.378   33.706  -38.642 1.00 27.64  ? 198 ARG B CD  1 
ATOM   3292 N  NE  . ARG B 1 198 ? 3.118   32.969  -38.736 1.00 27.44  ? 198 ARG B NE  1 
ATOM   3293 C  CZ  . ARG B 1 198 ? 2.224   33.183  -39.698 1.00 28.16  ? 198 ARG B CZ  1 
ATOM   3294 N  NH1 . ARG B 1 198 ? 2.431   34.113  -40.640 1.00 28.55  ? 198 ARG B NH1 1 
ATOM   3295 N  NH2 . ARG B 1 198 ? 1.107   32.462  -39.711 1.00 32.61  ? 198 ARG B NH2 1 
ATOM   3296 N  N   . VAL B 1 199 ? 7.790   29.139  -39.562 1.00 20.60  ? 199 VAL B N   1 
ATOM   3297 C  CA  . VAL B 1 199 ? 8.565   28.095  -38.864 1.00 20.67  ? 199 VAL B CA  1 
ATOM   3298 C  C   . VAL B 1 199 ? 10.052  28.244  -39.148 1.00 22.87  ? 199 VAL B C   1 
ATOM   3299 O  O   . VAL B 1 199 ? 10.928  28.137  -38.269 1.00 22.03  ? 199 VAL B O   1 
ATOM   3300 C  CB  . VAL B 1 199 ? 8.062   26.688  -39.263 1.00 23.52  ? 199 VAL B CB  1 
ATOM   3301 C  CG1 . VAL B 1 199 ? 9.055   25.586  -38.835 1.00 25.69  ? 199 VAL B CG1 1 
ATOM   3302 C  CG2 . VAL B 1 199 ? 6.676   26.458  -38.686 1.00 27.96  ? 199 VAL B CG2 1 
ATOM   3303 N  N   . ILE B 1 200 ? 10.339  28.497  -40.430 1.00 22.09  ? 200 ILE B N   1 
ATOM   3304 C  CA  . ILE B 1 200 ? 11.713  28.717  -40.861 1.00 23.27  ? 200 ILE B CA  1 
ATOM   3305 C  C   . ILE B 1 200 ? 12.361  29.925  -40.190 1.00 25.12  ? 200 ILE B C   1 
ATOM   3306 O  O   . ILE B 1 200 ? 13.503  29.888  -39.677 1.00 23.58  ? 200 ILE B O   1 
ATOM   3307 C  CB  . ILE B 1 200 ? 11.713  28.856  -42.393 1.00 27.47  ? 200 ILE B CB  1 
ATOM   3308 C  CG1 . ILE B 1 200 ? 11.240  27.626  -43.154 1.00 34.73  ? 200 ILE B CG1 1 
ATOM   3309 C  CG2 . ILE B 1 200 ? 13.099  29.340  -42.787 1.00 31.35  ? 200 ILE B CG2 1 
ATOM   3310 C  CD1 . ILE B 1 200 ? 12.089  26.394  -43.090 1.00 46.76  ? 200 ILE B CD1 1 
ATOM   3311 N  N   . GLU B 1 201 ? 11.604  31.015  -40.172 1.00 23.83  ? 201 GLU B N   1 
ATOM   3312 C  CA  . GLU B 1 201 ? 12.056  32.217  -39.492 1.00 22.28  ? 201 GLU B CA  1 
ATOM   3313 C  C   . GLU B 1 201 ? 12.245  31.944  -38.002 1.00 22.19  ? 201 GLU B C   1 
ATOM   3314 O  O   . GLU B 1 201 ? 13.169  32.499  -37.434 1.00 22.83  ? 201 GLU B O   1 
ATOM   3315 C  CB  . GLU B 1 201 ? 11.121  33.412  -39.738 1.00 24.80  ? 201 GLU B CB  1 
ATOM   3316 C  CG  . GLU B 1 201 ? 11.149  33.857  -41.206 1.00 35.13  ? 201 GLU B CG  1 
ATOM   3317 C  CD  . GLU B 1 201 ? 9.935   34.654  -41.664 1.00 38.15  ? 201 GLU B CD  1 
ATOM   3318 O  OE1 . GLU B 1 201 ? 8.859   34.606  -41.011 1.00 42.15  ? 201 GLU B OE1 1 
ATOM   3319 O  OE2 . GLU B 1 201 ? 10.027  35.358  -42.715 1.00 47.07  ? 201 GLU B OE2 1 
ATOM   3320 N  N   . GLU B 1 202 ? 11.391  31.127  -37.398 1.00 22.03  ? 202 GLU B N   1 
ATOM   3321 C  CA  . GLU B 1 202 ? 11.518  30.916  -35.950 1.00 20.64  ? 202 GLU B CA  1 
ATOM   3322 C  C   . GLU B 1 202 ? 12.766  30.091  -35.669 1.00 19.97  ? 202 GLU B C   1 
ATOM   3323 O  O   . GLU B 1 202 ? 13.351  30.233  -34.604 1.00 20.93  ? 202 GLU B O   1 
ATOM   3324 C  CB  . GLU B 1 202 ? 10.251  30.271  -35.406 1.00 21.68  ? 202 GLU B CB  1 
ATOM   3325 C  CG  . GLU B 1 202 ? 10.166  30.175  -33.886 1.00 21.44  ? 202 GLU B CG  1 
ATOM   3326 C  CD  . GLU B 1 202 ? 9.928   31.534  -33.246 1.00 21.80  ? 202 GLU B CD  1 
ATOM   3327 O  OE1 . GLU B 1 202 ? 9.391   32.430  -33.957 1.00 22.31  ? 202 GLU B OE1 1 
ATOM   3328 O  OE2 . GLU B 1 202 ? 10.267  31.692  -32.053 1.00 21.53  ? 202 GLU B OE2 1 
ATOM   3329 N  N   . ALA B 1 203 ? 13.168  29.209  -36.626 1.00 20.10  ? 203 ALA B N   1 
ATOM   3330 C  CA  . ALA B 1 203 ? 14.406  28.455  -36.385 1.00 20.30  ? 203 ALA B CA  1 
ATOM   3331 C  C   . ALA B 1 203 ? 15.548  29.454  -36.305 1.00 20.38  ? 203 ALA B C   1 
ATOM   3332 O  O   . ALA B 1 203 ? 16.423  29.335  -35.446 1.00 22.35  ? 203 ALA B O   1 
ATOM   3333 C  CB  . ALA B 1 203 ? 14.548  27.397  -37.457 1.00 23.24  ? 203 ALA B CB  1 
ATOM   3334 N  N   . LYS B 1 204 ? 15.538  30.468  -37.157 1.00 21.22  ? 204 LYS B N   1 
ATOM   3335 C  CA  . LYS B 1 204 ? 16.585  31.488  -37.113 1.00 21.58  ? 204 LYS B CA  1 
ATOM   3336 C  C   . LYS B 1 204 ? 16.538  32.252  -35.791 1.00 22.28  ? 204 LYS B C   1 
ATOM   3337 O  O   . LYS B 1 204 ? 17.564  32.524  -35.140 1.00 23.36  ? 204 LYS B O   1 
ATOM   3338 C  CB  . LYS B 1 204 ? 16.504  32.441  -38.317 1.00 25.47  ? 204 LYS B CB  1 
ATOM   3339 C  CG  . LYS B 1 204 ? 16.633  31.764  -39.666 1.00 31.68  ? 204 LYS B CG  1 
ATOM   3340 C  CD  . LYS B 1 204 ? 16.572  32.809  -40.790 1.00 44.75  ? 204 LYS B CD  1 
ATOM   3341 C  CE  . LYS B 1 204 ? 15.471  32.535  -41.798 1.00 55.15  ? 204 LYS B CE  1 
ATOM   3342 N  NZ  . LYS B 1 204 ? 15.723  33.120  -43.148 1.00 71.25  ? 204 LYS B NZ  1 
ATOM   3343 N  N   . THR B 1 205 ? 15.340  32.621  -35.349 1.00 21.22  ? 205 THR B N   1 
ATOM   3344 C  CA  . THR B 1 205 ? 15.171  33.270  -34.058 1.00 19.49  ? 205 THR B CA  1 
ATOM   3345 C  C   . THR B 1 205 ? 15.759  32.430  -32.934 1.00 20.05  ? 205 THR B C   1 
ATOM   3346 O  O   . THR B 1 205 ? 16.445  32.948  -32.047 1.00 20.18  ? 205 THR B O   1 
ATOM   3347 C  CB  . THR B 1 205 ? 13.670  33.516  -33.807 1.00 21.07  ? 205 THR B CB  1 
ATOM   3348 O  OG1 . THR B 1 205 ? 13.235  34.505  -34.747 1.00 23.87  ? 205 THR B OG1 1 
ATOM   3349 C  CG2 . THR B 1 205 ? 13.408  34.082  -32.431 1.00 23.35  ? 205 THR B CG2 1 
ATOM   3350 N  N   . ALA B 1 206 ? 15.489  31.133  -32.975 1.00 19.62  ? 206 ALA B N   1 
ATOM   3351 C  CA  . ALA B 1 206 ? 16.051  30.215  -31.971 1.00 18.94  ? 206 ALA B CA  1 
ATOM   3352 C  C   . ALA B 1 206 ? 17.560  30.317  -31.932 1.00 17.85  ? 206 ALA B C   1 
ATOM   3353 O  O   . ALA B 1 206 ? 18.225  30.415  -30.897 1.00 17.18  ? 206 ALA B O   1 
ATOM   3354 C  CB  . ALA B 1 206 ? 15.573  28.788  -32.239 1.00 19.05  ? 206 ALA B CB  1 
ATOM   3355 N  N   . PHE B 1 207 ? 18.215  30.283  -33.095 1.00 18.99  ? 207 PHE B N   1 
ATOM   3356 C  CA  . PHE B 1 207 ? 19.669  30.420  -33.110 1.00 19.62  ? 207 PHE B CA  1 
ATOM   3357 C  C   . PHE B 1 207 ? 20.100  31.778  -32.554 1.00 18.74  ? 207 PHE B C   1 
ATOM   3358 O  O   . PHE B 1 207 ? 21.045  31.839  -31.756 1.00 20.96  ? 207 PHE B O   1 
ATOM   3359 C  CB  . PHE B 1 207 ? 20.233  30.220  -34.512 1.00 21.35  ? 207 PHE B CB  1 
ATOM   3360 C  CG  . PHE B 1 207 ? 20.496  28.770  -34.888 1.00 20.38  ? 207 PHE B CG  1 
ATOM   3361 C  CD1 . PHE B 1 207 ? 21.717  28.161  -34.625 1.00 25.35  ? 207 PHE B CD1 1 
ATOM   3362 C  CD2 . PHE B 1 207 ? 19.551  27.988  -35.500 1.00 22.82  ? 207 PHE B CD2 1 
ATOM   3363 C  CE1 . PHE B 1 207 ? 21.983  26.848  -34.960 1.00 24.80  ? 207 PHE B CE1 1 
ATOM   3364 C  CE2 . PHE B 1 207 ? 19.799  26.670  -35.828 1.00 24.55  ? 207 PHE B CE2 1 
ATOM   3365 C  CZ  . PHE B 1 207 ? 21.024  26.065  -35.561 1.00 25.68  ? 207 PHE B CZ  1 
ATOM   3366 N  N   . LEU B 1 208 ? 19.393  32.851  -32.958 1.00 19.38  ? 208 LEU B N   1 
ATOM   3367 C  CA  . LEU B 1 208 ? 19.744  34.162  -32.414 1.00 18.82  ? 208 LEU B CA  1 
ATOM   3368 C  C   . LEU B 1 208 ? 19.626  34.214  -30.899 1.00 17.64  ? 208 LEU B C   1 
ATOM   3369 O  O   . LEU B 1 208 ? 20.438  34.898  -30.252 1.00 21.40  ? 208 LEU B O   1 
ATOM   3370 C  CB  . LEU B 1 208 ? 18.856  35.223  -33.099 1.00 22.71  ? 208 LEU B CB  1 
ATOM   3371 C  CG  . LEU B 1 208 ? 19.203  35.471  -34.565 1.00 28.63  ? 208 LEU B CG  1 
ATOM   3372 C  CD1 . LEU B 1 208 ? 18.170  36.367  -35.259 1.00 43.73  ? 208 LEU B CD1 1 
ATOM   3373 C  CD2 . LEU B 1 208 ? 20.608  36.066  -34.733 1.00 38.68  ? 208 LEU B CD2 1 
ATOM   3374 N  N   . LEU B 1 209 ? 18.641  33.544  -30.320 1.00 19.42  ? 209 LEU B N   1 
ATOM   3375 C  CA  . LEU B 1 209 ? 18.485  33.561  -28.855 1.00 17.70  ? 209 LEU B CA  1 
ATOM   3376 C  C   . LEU B 1 209 ? 19.651  32.848  -28.189 1.00 17.62  ? 209 LEU B C   1 
ATOM   3377 O  O   . LEU B 1 209 ? 20.122  33.259  -27.135 1.00 18.50  ? 209 LEU B O   1 
ATOM   3378 C  CB  . LEU B 1 209 ? 17.155  32.927  -28.438 1.00 18.42  ? 209 LEU B CB  1 
ATOM   3379 C  CG  . LEU B 1 209 ? 15.909  33.777  -28.743 1.00 17.23  ? 209 LEU B CG  1 
ATOM   3380 C  CD1 . LEU B 1 209 ? 14.647  32.918  -28.810 1.00 18.63  ? 209 LEU B CD1 1 
ATOM   3381 C  CD2 . LEU B 1 209 ? 15.755  34.910  -27.712 1.00 19.35  ? 209 LEU B CD2 1 
ATOM   3382 N  N   . ASN B 1 210 ? 20.150  31.806  -28.822 1.00 19.22  ? 210 ASN B N   1 
ATOM   3383 C  CA  . ASN B 1 210 ? 21.368  31.147  -28.342 1.00 19.01  ? 210 ASN B CA  1 
ATOM   3384 C  C   . ASN B 1 210 ? 22.598  32.042  -28.459 1.00 18.51  ? 210 ASN B C   1 
ATOM   3385 O  O   . ASN B 1 210 ? 23.405  32.124  -27.538 1.00 19.95  ? 210 ASN B O   1 
ATOM   3386 C  CB  . ASN B 1 210 ? 21.605  29.823  -29.095 1.00 18.64  ? 210 ASN B CB  1 
ATOM   3387 C  CG  . ASN B 1 210 ? 20.687  28.736  -28.561 1.00 17.19  ? 210 ASN B CG  1 
ATOM   3388 O  OD1 . ASN B 1 210 ? 20.974  28.049  -27.560 1.00 19.57  ? 210 ASN B OD1 1 
ATOM   3389 N  ND2 . ASN B 1 210 ? 19.538  28.576  -29.211 1.00 20.17  ? 210 ASN B ND2 1 
ATOM   3390 N  N   . ILE B 1 211 ? 22.766  32.709  -29.600 1.00 19.35  ? 211 ILE B N   1 
ATOM   3391 C  CA  . ILE B 1 211 ? 23.913  33.613  -29.772 1.00 22.08  ? 211 ILE B CA  1 
ATOM   3392 C  C   . ILE B 1 211 ? 23.898  34.702  -28.707 1.00 20.88  ? 211 ILE B C   1 
ATOM   3393 O  O   . ILE B 1 211 ? 24.898  35.005  -28.091 1.00 22.99  ? 211 ILE B O   1 
ATOM   3394 C  CB  . ILE B 1 211 ? 23.910  34.197  -31.194 1.00 24.19  ? 211 ILE B CB  1 
ATOM   3395 C  CG1 . ILE B 1 211 ? 24.151  33.121  -32.251 1.00 26.15  ? 211 ILE B CG1 1 
ATOM   3396 C  CG2 . ILE B 1 211 ? 24.917  35.329  -31.347 1.00 27.33  ? 211 ILE B CG2 1 
ATOM   3397 C  CD1 . ILE B 1 211 ? 23.760  33.441  -33.697 1.00 26.31  ? 211 ILE B CD1 1 
ATOM   3398 N  N   . GLN B 1 212 ? 22.714  35.298  -28.463 1.00 19.95  ? 212 GLN B N   1 
ATOM   3399 C  CA  . GLN B 1 212 ? 22.583  36.357  -27.462 1.00 19.92  ? 212 GLN B CA  1 
ATOM   3400 C  C   . GLN B 1 212 ? 22.930  35.797  -26.095 1.00 18.28  ? 212 GLN B C   1 
ATOM   3401 O  O   . GLN B 1 212 ? 23.591  36.466  -25.313 1.00 20.11  ? 212 GLN B O   1 
ATOM   3402 C  CB  A GLN B 1 212 ? 21.177  36.929  -27.582 0.50 23.01  ? 212 GLN B CB  1 
ATOM   3403 C  CB  B GLN B 1 212 ? 21.163  36.919  -27.417 0.50 23.29  ? 212 GLN B CB  1 
ATOM   3404 C  CG  A GLN B 1 212 ? 20.662  37.672  -26.372 0.50 25.34  ? 212 GLN B CG  1 
ATOM   3405 C  CG  B GLN B 1 212 ? 20.867  37.787  -28.618 0.50 23.62  ? 212 GLN B CG  1 
ATOM   3406 C  CD  A GLN B 1 212 ? 19.143  37.653  -26.356 0.50 26.75  ? 212 GLN B CD  1 
ATOM   3407 C  CD  B GLN B 1 212 ? 19.488  38.402  -28.568 0.50 30.89  ? 212 GLN B CD  1 
ATOM   3408 O  OE1 A GLN B 1 212 ? 18.541  37.517  -25.320 0.50 34.66  ? 212 GLN B OE1 1 
ATOM   3409 O  OE1 B GLN B 1 212 ? 19.023  38.882  -27.530 0.50 36.74  ? 212 GLN B OE1 1 
ATOM   3410 N  NE2 A GLN B 1 212 ? 18.555  37.785  -27.536 0.50 32.33  ? 212 GLN B NE2 1 
ATOM   3411 N  NE2 B GLN B 1 212 ? 18.871  38.394  -29.740 0.50 46.71  ? 212 GLN B NE2 1 
ATOM   3412 N  N   . LEU B 1 213 ? 22.475  34.581  -25.841 1.00 16.63  ? 213 LEU B N   1 
ATOM   3413 C  CA  . LEU B 1 213 ? 22.830  33.953  -24.564 1.00 17.88  ? 213 LEU B CA  1 
ATOM   3414 C  C   . LEU B 1 213 ? 24.335  33.810  -24.416 1.00 18.35  ? 213 LEU B C   1 
ATOM   3415 O  O   . LEU B 1 213 ? 24.910  34.180  -23.377 1.00 18.85  ? 213 LEU B O   1 
ATOM   3416 C  CB  . LEU B 1 213 ? 22.095  32.607  -24.397 1.00 18.84  ? 213 LEU B CB  1 
ATOM   3417 C  CG  . LEU B 1 213 ? 22.505  31.766  -23.170 1.00 20.11  ? 213 LEU B CG  1 
ATOM   3418 C  CD1 . LEU B 1 213 ? 22.012  32.395  -21.871 1.00 19.52  ? 213 LEU B CD1 1 
ATOM   3419 C  CD2 . LEU B 1 213 ? 21.986  30.356  -23.329 1.00 22.66  ? 213 LEU B CD2 1 
ATOM   3420 N  N   . PHE B 1 214 ? 25.048  33.293  -25.427 1.00 19.03  ? 214 PHE B N   1 
ATOM   3421 C  CA  . PHE B 1 214 ? 26.494  33.152  -25.273 1.00 20.18  ? 214 PHE B CA  1 
ATOM   3422 C  C   . PHE B 1 214 ? 27.204  34.483  -25.116 1.00 18.17  ? 214 PHE B C   1 
ATOM   3423 O  O   . PHE B 1 214 ? 28.207  34.534  -24.404 1.00 23.64  ? 214 PHE B O   1 
ATOM   3424 C  CB  . PHE B 1 214 ? 27.089  32.444  -26.486 1.00 24.73  ? 214 PHE B CB  1 
ATOM   3425 C  CG  . PHE B 1 214 ? 26.572  31.048  -26.750 1.00 25.75  ? 214 PHE B CG  1 
ATOM   3426 C  CD1 . PHE B 1 214 ? 26.313  30.179  -25.711 1.00 29.16  ? 214 PHE B CD1 1 
ATOM   3427 C  CD2 . PHE B 1 214 ? 26.351  30.630  -28.056 1.00 29.70  ? 214 PHE B CD2 1 
ATOM   3428 C  CE1 . PHE B 1 214 ? 25.835  28.913  -26.001 1.00 33.04  ? 214 PHE B CE1 1 
ATOM   3429 C  CE2 . PHE B 1 214 ? 25.875  29.361  -28.358 1.00 34.35  ? 214 PHE B CE2 1 
ATOM   3430 C  CZ  . PHE B 1 214 ? 25.612  28.485  -27.313 1.00 36.43  ? 214 PHE B CZ  1 
ATOM   3431 N  N   . GLU B 1 215 ? 26.699  35.522  -25.776 1.00 19.11  ? 215 GLU B N   1 
ATOM   3432 C  CA  . GLU B 1 215 ? 27.285  36.845  -25.617 1.00 21.64  ? 215 GLU B CA  1 
ATOM   3433 C  C   . GLU B 1 215 ? 27.153  37.340  -24.195 1.00 21.47  ? 215 GLU B C   1 
ATOM   3434 O  O   . GLU B 1 215 ? 28.055  37.963  -23.658 1.00 21.69  ? 215 GLU B O   1 
ATOM   3435 C  CB  . GLU B 1 215 ? 26.613  37.842  -26.600 1.00 21.08  ? 215 GLU B CB  1 
ATOM   3436 C  CG  . GLU B 1 215 ? 27.008  37.538  -28.025 1.00 26.89  ? 215 GLU B CG  1 
ATOM   3437 C  CD  . GLU B 1 215 ? 26.368  38.372  -29.110 1.00 31.83  ? 215 GLU B CD  1 
ATOM   3438 O  OE1 . GLU B 1 215 ? 25.417  39.114  -28.783 1.00 41.33  ? 215 GLU B OE1 1 
ATOM   3439 O  OE2 . GLU B 1 215 ? 26.812  38.287  -30.292 1.00 31.09  ? 215 GLU B OE2 1 
ATOM   3440 N  N   . GLU B 1 216 ? 25.998  37.052  -23.577 1.00 19.84  ? 216 GLU B N   1 
ATOM   3441 C  CA  . GLU B 1 216 ? 25.807  37.453  -22.184 1.00 20.46  ? 216 GLU B CA  1 
ATOM   3442 C  C   . GLU B 1 216 ? 26.729  36.671  -21.251 1.00 16.91  ? 216 GLU B C   1 
ATOM   3443 O  O   . GLU B 1 216 ? 27.373  37.262  -20.396 1.00 20.25  ? 216 GLU B O   1 
ATOM   3444 C  CB  . GLU B 1 216 ? 24.352  37.276  -21.743 1.00 19.48  ? 216 GLU B CB  1 
ATOM   3445 C  CG  . GLU B 1 216 ? 24.112  37.704  -20.297 1.00 20.35  ? 216 GLU B CG  1 
ATOM   3446 C  CD  . GLU B 1 216 ? 22.774  37.173  -19.793 1.00 20.09  ? 216 GLU B CD  1 
ATOM   3447 O  OE1 . GLU B 1 216 ? 22.705  35.945  -19.540 1.00 24.49  ? 216 GLU B OE1 1 
ATOM   3448 O  OE2 . GLU B 1 216 ? 21.829  37.971  -19.622 1.00 23.49  ? 216 GLU B OE2 1 
ATOM   3449 N  N   . LEU B 1 217 ? 26.757  35.362  -21.480 1.00 18.67  ? 217 LEU B N   1 
ATOM   3450 C  CA  . LEU B 1 217 ? 27.559  34.558  -20.578 1.00 18.20  ? 217 LEU B CA  1 
ATOM   3451 C  C   . LEU B 1 217 ? 29.006  35.020  -20.603 1.00 19.90  ? 217 LEU B C   1 
ATOM   3452 O  O   . LEU B 1 217 ? 29.667  35.137  -19.593 1.00 21.56  ? 217 LEU B O   1 
ATOM   3453 C  CB  . LEU B 1 217 ? 27.455  33.080  -20.953 1.00 21.51  ? 217 LEU B CB  1 
ATOM   3454 C  CG  . LEU B 1 217 ? 26.052  32.490  -20.895 1.00 22.64  ? 217 LEU B CG  1 
ATOM   3455 C  CD1 . LEU B 1 217 ? 26.088  30.969  -21.028 1.00 24.50  ? 217 LEU B CD1 1 
ATOM   3456 C  CD2 . LEU B 1 217 ? 25.339  32.922  -19.606 1.00 25.18  ? 217 LEU B CD2 1 
ATOM   3457 N  N   . GLN B 1 218 ? 29.533  35.308  -21.785 1.00 20.05  ? 218 GLN B N   1 
ATOM   3458 C  CA  . GLN B 1 218 ? 30.900  35.770  -21.924 1.00 24.44  ? 218 GLN B CA  1 
ATOM   3459 C  C   . GLN B 1 218 ? 31.093  37.069  -21.159 1.00 24.45  ? 218 GLN B C   1 
ATOM   3460 O  O   . GLN B 1 218 ? 32.130  37.277  -20.516 1.00 27.24  ? 218 GLN B O   1 
ATOM   3461 C  CB  . GLN B 1 218 ? 31.213  35.925  -23.414 1.00 27.49  ? 218 GLN B CB  1 
ATOM   3462 C  CG  . GLN B 1 218 ? 32.662  36.384  -23.686 1.00 29.27  ? 218 GLN B CG  1 
ATOM   3463 C  CD  . GLN B 1 218 ? 33.644  35.259  -23.473 1.00 31.99  ? 218 GLN B CD  1 
ATOM   3464 O  OE1 . GLN B 1 218 ? 33.219  34.124  -23.260 1.00 31.28  ? 218 GLN B OE1 1 
ATOM   3465 N  NE2 . GLN B 1 218 ? 34.933  35.559  -23.536 1.00 36.38  ? 218 GLN B NE2 1 
ATOM   3466 N  N   . GLU B 1 219 ? 30.089  37.969  -21.222 1.00 24.07  ? 219 GLU B N   1 
ATOM   3467 C  CA  . GLU B 1 219 ? 30.241  39.232  -20.500 1.00 24.40  ? 219 GLU B CA  1 
ATOM   3468 C  C   . GLU B 1 219 ? 30.271  38.981  -19.003 1.00 22.53  ? 219 GLU B C   1 
ATOM   3469 O  O   . GLU B 1 219 ? 31.019  39.600  -18.256 1.00 24.41  ? 219 GLU B O   1 
ATOM   3470 C  CB  . GLU B 1 219 ? 29.102  40.190  -20.857 1.00 29.27  ? 219 GLU B CB  1 
ATOM   3471 C  CG  . GLU B 1 219 ? 29.249  41.570  -20.272 1.00 37.02  ? 219 GLU B CG  1 
ATOM   3472 C  CD  . GLU B 1 219 ? 30.537  42.338  -20.445 1.00 46.01  ? 219 GLU B CD  1 
ATOM   3473 O  OE1 . GLU B 1 219 ? 31.438  41.942  -21.221 1.00 61.41  ? 219 GLU B OE1 1 
ATOM   3474 O  OE2 . GLU B 1 219 ? 30.723  43.393  -19.780 1.00 62.69  ? 219 GLU B OE2 1 
ATOM   3475 N  N   . LEU B 1 220 ? 29.422  38.046  -18.595 1.00 20.91  ? 220 LEU B N   1 
ATOM   3476 C  CA  . LEU B 1 220 ? 29.344  37.735  -17.160 1.00 19.82  ? 220 LEU B CA  1 
ATOM   3477 C  C   . LEU B 1 220 ? 30.685  37.213  -16.704 1.00 21.98  ? 220 LEU B C   1 
ATOM   3478 O  O   . LEU B 1 220 ? 31.084  37.493  -15.579 1.00 22.37  ? 220 LEU B O   1 
ATOM   3479 C  CB  . LEU B 1 220 ? 28.246  36.719  -16.757 1.00 21.37  ? 220 LEU B CB  1 
ATOM   3480 C  CG  . LEU B 1 220 ? 26.818  37.263  -16.951 1.00 20.10  ? 220 LEU B CG  1 
ATOM   3481 C  CD1 . LEU B 1 220 ? 25.710  36.230  -16.822 1.00 23.37  ? 220 LEU B CD1 1 
ATOM   3482 C  CD2 . LEU B 1 220 ? 26.541  38.403  -15.961 1.00 25.41  ? 220 LEU B CD2 1 
ATOM   3483 N  N   . LEU B 1 221 ? 31.381  36.492  -17.559 1.00 21.83  ? 221 LEU B N   1 
ATOM   3484 C  CA  . LEU B 1 221 ? 32.584  35.785  -17.137 1.00 22.42  ? 221 LEU B CA  1 
ATOM   3485 C  C   . LEU B 1 221 ? 33.835  36.624  -17.262 1.00 24.47  ? 221 LEU B C   1 
ATOM   3486 O  O   . LEU B 1 221 ? 34.832  36.267  -16.625 1.00 29.91  ? 221 LEU B O   1 
ATOM   3487 C  CB  . LEU B 1 221 ? 32.730  34.502  -17.973 1.00 23.12  ? 221 LEU B CB  1 
ATOM   3488 C  CG  . LEU B 1 221 ? 31.696  33.417  -17.652 1.00 29.18  ? 221 LEU B CG  1 
ATOM   3489 C  CD1 . LEU B 1 221 ? 31.611  32.369  -18.751 1.00 26.56  ? 221 LEU B CD1 1 
ATOM   3490 C  CD2 . LEU B 1 221 ? 31.994  32.692  -16.354 1.00 26.31  ? 221 LEU B CD2 1 
ATOM   3491 N  N   . THR B 1 222 ? 33.767  37.695  -18.052 1.00 26.08  ? 222 THR B N   1 
ATOM   3492 C  CA  . THR B 1 222 ? 34.951  38.504  -18.319 1.00 34.03  ? 222 THR B CA  1 
ATOM   3493 C  C   . THR B 1 222 ? 34.767  39.979  -18.002 1.00 37.84  ? 222 THR B C   1 
ATOM   3494 O  O   . THR B 1 222 ? 35.750  40.724  -18.018 1.00 43.11  ? 222 THR B O   1 
ATOM   3495 C  CB  . THR B 1 222 ? 35.382  38.438  -19.807 1.00 34.13  ? 222 THR B CB  1 
ATOM   3496 O  OG1 . THR B 1 222 ? 34.327  38.999  -20.616 1.00 35.09  ? 222 THR B OG1 1 
ATOM   3497 C  CG2 . THR B 1 222 ? 35.622  37.010  -20.280 1.00 34.85  ? 222 THR B CG2 1 
ATOM   3498 N  N   . HIS B 1 223 ? 33.576  40.460  -17.749 1.00 41.41  ? 223 HIS B N   1 
ATOM   3499 C  CA  . HIS B 1 223 ? 33.327  41.889  -17.672 1.00 47.73  ? 223 HIS B CA  1 
ATOM   3500 C  C   . HIS B 1 223 ? 33.926  42.679  -18.832 1.00 51.74  ? 223 HIS B C   1 
ATOM   3501 O  O   . HIS B 1 223 ? 34.005  42.210  -19.979 1.00 61.00  ? 223 HIS B O   1 
ATOM   3502 C  CB  . HIS B 1 223 ? 33.874  42.446  -16.338 1.00 52.56  ? 223 HIS B CB  1 
ATOM   3503 C  CG  . HIS B 1 223 ? 32.887  42.020  -15.266 1.00 50.55  ? 223 HIS B CG  1 
ATOM   3504 N  ND1 . HIS B 1 223 ? 32.416  42.835  -14.261 1.00 48.74  ? 223 HIS B ND1 1 
ATOM   3505 C  CD2 . HIS B 1 223 ? 32.279  40.819  -15.074 1.00 48.92  ? 223 HIS B CD2 1 
ATOM   3506 C  CE1 . HIS B 1 223 ? 31.576  42.173  -13.489 1.00 47.67  ? 223 HIS B CE1 1 
ATOM   3507 N  NE2 . HIS B 1 223 ? 31.479  40.942  -13.963 1.00 46.88  ? 223 HIS B NE2 1 
HETATM 3508 S  S   . SO4 C 2 .   ? 29.353  12.623  -3.538  1.00 74.93  ? 234 SO4 A S   1 
HETATM 3509 O  O1  . SO4 C 2 .   ? 29.110  13.963  -3.283  1.00 77.98  ? 234 SO4 A O1  1 
HETATM 3510 O  O2  . SO4 C 2 .   ? 30.027  12.074  -2.466  1.00 69.45  ? 234 SO4 A O2  1 
HETATM 3511 O  O3  . SO4 C 2 .   ? 28.159  11.973  -3.732  1.00 81.74  ? 234 SO4 A O3  1 
HETATM 3512 O  O4  . SO4 C 2 .   ? 30.127  12.513  -4.678  1.00 68.26  ? 234 SO4 A O4  1 
HETATM 3513 C  CHA . HEM D 3 .   ? 17.333  2.416   6.037   1.00 28.75  ? 300 HEM A CHA 1 
HETATM 3514 C  CHB . HEM D 3 .   ? 21.724  0.930   4.802   1.00 37.84  ? 300 HEM A CHB 1 
HETATM 3515 C  CHC . HEM D 3 .   ? 19.875  -2.836  2.535   1.00 32.32  ? 300 HEM A CHC 1 
HETATM 3516 C  CHD . HEM D 3 .   ? 15.521  -0.712  2.859   1.00 22.27  ? 300 HEM A CHD 1 
HETATM 3517 C  C1A . HEM D 3 .   ? 18.700  2.163   6.179   1.00 34.86  ? 300 HEM A C1A 1 
HETATM 3518 C  C2A . HEM D 3 .   ? 19.599  3.215   6.561   1.00 43.12  ? 300 HEM A C2A 1 
HETATM 3519 C  C3A . HEM D 3 .   ? 20.803  2.934   6.015   1.00 40.56  ? 300 HEM A C3A 1 
HETATM 3520 C  C4A . HEM D 3 .   ? 20.658  1.675   5.326   1.00 38.31  ? 300 HEM A C4A 1 
HETATM 3521 C  CMA . HEM D 3 .   ? 22.177  3.564   6.283   1.00 43.21  ? 300 HEM A CMA 1 
HETATM 3522 C  CAA . HEM D 3 .   ? 19.341  4.267   7.624   1.00 53.86  ? 300 HEM A CAA 1 
HETATM 3523 C  CBA . HEM D 3 .   ? 18.381  3.953   8.752   1.00 62.07  ? 300 HEM A CBA 1 
HETATM 3524 C  CGA . HEM D 3 .   ? 17.358  5.043   9.045   1.00 61.28  ? 300 HEM A CGA 1 
HETATM 3525 O  O1A . HEM D 3 .   ? 17.591  5.777   10.034  1.00 72.05  ? 300 HEM A O1A 1 
HETATM 3526 O  O2A . HEM D 3 .   ? 16.312  5.186   8.347   1.00 65.35  ? 300 HEM A O2A 1 
HETATM 3527 C  C1B . HEM D 3 .   ? 21.581  -0.435  4.513   1.00 40.10  ? 300 HEM A C1B 1 
HETATM 3528 C  C2B . HEM D 3 .   ? 22.721  -1.211  4.104   1.00 39.56  ? 300 HEM A C2B 1 
HETATM 3529 C  C3B . HEM D 3 .   ? 22.216  -2.239  3.380   1.00 36.83  ? 300 HEM A C3B 1 
HETATM 3530 C  C4B . HEM D 3 .   ? 20.787  -2.033  3.245   1.00 34.73  ? 300 HEM A C4B 1 
HETATM 3531 C  CMB . HEM D 3 .   ? 24.188  -0.941  4.473   1.00 46.40  ? 300 HEM A CMB 1 
HETATM 3532 C  CAB . HEM D 3 .   ? 22.881  -3.362  2.921   1.00 40.86  ? 300 HEM A CAB 1 
HETATM 3533 C  CBB . HEM D 3 .   ? 24.163  -3.821  2.892   1.00 50.09  ? 300 HEM A CBB 1 
HETATM 3534 C  C1C . HEM D 3 .   ? 18.560  -2.436  2.227   1.00 26.22  ? 300 HEM A C1C 1 
HETATM 3535 C  C2C . HEM D 3 .   ? 17.674  -3.175  1.367   1.00 26.92  ? 300 HEM A C2C 1 
HETATM 3536 C  C3C . HEM D 3 .   ? 16.465  -2.586  1.481   1.00 25.06  ? 300 HEM A C3C 1 
HETATM 3537 C  C4C . HEM D 3 .   ? 16.595  -1.496  2.409   1.00 22.81  ? 300 HEM A C4C 1 
HETATM 3538 C  CMC . HEM D 3 .   ? 18.090  -4.384  0.528   1.00 33.72  ? 300 HEM A CMC 1 
HETATM 3539 C  CAC . HEM D 3 .   ? 15.308  -2.804  0.709   1.00 29.42  ? 300 HEM A CAC 1 
HETATM 3540 C  CBC . HEM D 3 .   ? 15.268  -3.109  -0.620  1.00 50.53  ? 300 HEM A CBC 1 
HETATM 3541 C  C1D . HEM D 3 .   ? 15.611  0.190   3.918   1.00 20.14  ? 300 HEM A C1D 1 
HETATM 3542 C  C2D . HEM D 3 .   ? 14.497  0.957   4.428   1.00 22.49  ? 300 HEM A C2D 1 
HETATM 3543 C  C3D . HEM D 3 .   ? 15.003  1.851   5.307   1.00 22.93  ? 300 HEM A C3D 1 
HETATM 3544 C  C4D . HEM D 3 .   ? 16.429  1.638   5.333   1.00 24.73  ? 300 HEM A C4D 1 
HETATM 3545 C  CMD . HEM D 3 .   ? 13.069  0.802   3.882   1.00 23.40  ? 300 HEM A CMD 1 
HETATM 3546 C  CAD . HEM D 3 .   ? 14.273  2.971   6.029   1.00 27.42  ? 300 HEM A CAD 1 
HETATM 3547 C  CBD . HEM D 3 .   ? 13.743  2.599   7.397   1.00 29.24  ? 300 HEM A CBD 1 
HETATM 3548 C  CGD . HEM D 3 .   ? 12.700  3.538   7.965   1.00 33.24  ? 300 HEM A CGD 1 
HETATM 3549 O  O1D . HEM D 3 .   ? 11.549  3.122   8.154   1.00 30.87  ? 300 HEM A O1D 1 
HETATM 3550 O  O2D . HEM D 3 .   ? 13.024  4.717   8.229   1.00 44.83  ? 300 HEM A O2D 1 
HETATM 3551 N  NA  . HEM D 3 .   ? 19.357  1.212   5.410   1.00 37.61  ? 300 HEM A NA  1 
HETATM 3552 N  NB  . HEM D 3 .   ? 20.393  -0.908  3.949   1.00 38.13  ? 300 HEM A NB  1 
HETATM 3553 N  NC  . HEM D 3 .   ? 17.871  -1.456  2.918   1.00 23.92  ? 300 HEM A NC  1 
HETATM 3554 N  ND  . HEM D 3 .   ? 16.812  0.693   4.375   1.00 22.31  ? 300 HEM A ND  1 
HETATM 3555 FE FE  . HEM D 3 .   ? 18.585  -0.110  4.173   1.00 27.83  ? 300 HEM A FE  1 
HETATM 3556 C  CHA . HEM E 3 .   ? 24.345  20.281  -36.663 1.00 39.90  ? 300 HEM B CHA 1 
HETATM 3557 C  CHB . HEM E 3 .   ? 28.640  21.227  -34.810 1.00 57.46  ? 300 HEM B CHB 1 
HETATM 3558 C  CHC . HEM E 3 .   ? 26.798  24.781  -32.132 1.00 38.48  ? 300 HEM B CHC 1 
HETATM 3559 C  CHD . HEM E 3 .   ? 22.426  23.573  -33.723 1.00 28.61  ? 300 HEM B CHD 1 
HETATM 3560 C  C1A . HEM E 3 .   ? 25.704  20.242  -36.362 1.00 46.48  ? 300 HEM B C1A 1 
HETATM 3561 C  C2A . HEM E 3 .   ? 26.603  19.197  -36.803 1.00 57.97  ? 300 HEM B C2A 1 
HETATM 3562 C  C3A . HEM E 3 .   ? 27.734  19.295  -36.070 1.00 61.60  ? 300 HEM B C3A 1 
HETATM 3563 C  C4A . HEM E 3 .   ? 27.554  20.435  -35.203 1.00 56.69  ? 300 HEM B C4A 1 
HETATM 3564 C  CMA . HEM E 3 .   ? 28.681  18.124  -35.790 1.00 72.48  ? 300 HEM B CMA 1 
HETATM 3565 C  CAA . HEM E 3 .   ? 26.368  18.232  -37.965 1.00 65.33  ? 300 HEM B CAA 1 
HETATM 3566 C  CBA . HEM E 3 .   ? 25.866  18.891  -39.242 1.00 77.86  ? 300 HEM B CBA 1 
HETATM 3567 C  CGA . HEM E 3 .   ? 24.831  18.112  -40.026 1.00 82.41  ? 300 HEM B CGA 1 
HETATM 3568 O  O1A . HEM E 3 .   ? 25.204  17.551  -41.088 1.00 93.36  ? 300 HEM B O1A 1 
HETATM 3569 O  O2A . HEM E 3 .   ? 23.646  18.080  -39.598 1.00 87.37  ? 300 HEM B O2A 1 
HETATM 3570 C  C1B . HEM E 3 .   ? 28.499  22.447  -34.162 1.00 49.40  ? 300 HEM B C1B 1 
HETATM 3571 C  C2B . HEM E 3 .   ? 29.642  23.124  -33.603 1.00 47.16  ? 300 HEM B C2B 1 
HETATM 3572 C  C3B . HEM E 3 .   ? 29.152  24.072  -32.751 1.00 44.35  ? 300 HEM B C3B 1 
HETATM 3573 C  C4B . HEM E 3 .   ? 27.700  23.989  -32.836 1.00 42.22  ? 300 HEM B C4B 1 
HETATM 3574 C  CMB . HEM E 3 .   ? 31.077  22.705  -33.896 1.00 51.36  ? 300 HEM B CMB 1 
HETATM 3575 C  CAB . HEM E 3 .   ? 29.830  24.667  -31.697 1.00 46.80  ? 300 HEM B CAB 1 
HETATM 3576 C  CBB . HEM E 3 .   ? 31.043  24.447  -31.114 1.00 51.34  ? 300 HEM B CBB 1 
HETATM 3577 C  C1C . HEM E 3 .   ? 25.413  24.666  -32.237 1.00 36.99  ? 300 HEM B C1C 1 
HETATM 3578 C  C2C . HEM E 3 .   ? 24.489  25.524  -31.536 1.00 38.65  ? 300 HEM B C2C 1 
HETATM 3579 C  C3C . HEM E 3 .   ? 23.251  25.141  -31.933 1.00 35.55  ? 300 HEM B C3C 1 
HETATM 3580 C  C4C . HEM E 3 .   ? 23.414  24.041  -32.861 1.00 33.28  ? 300 HEM B C4C 1 
HETATM 3581 C  CMC . HEM E 3 .   ? 24.780  26.552  -30.438 1.00 42.07  ? 300 HEM B CMC 1 
HETATM 3582 C  CAC . HEM E 3 .   ? 22.099  25.898  -31.805 1.00 35.12  ? 300 HEM B CAC 1 
HETATM 3583 C  CBC . HEM E 3 .   ? 21.033  25.846  -30.984 1.00 43.31  ? 300 HEM B CBC 1 
HETATM 3584 C  C1D . HEM E 3 .   ? 22.533  22.485  -34.575 1.00 26.33  ? 300 HEM B C1D 1 
HETATM 3585 C  C2D . HEM E 3 .   ? 21.440  21.869  -35.294 1.00 26.08  ? 300 HEM B C2D 1 
HETATM 3586 C  C3D . HEM E 3 .   ? 21.994  20.911  -36.074 1.00 26.99  ? 300 HEM B C3D 1 
HETATM 3587 C  C4D . HEM E 3 .   ? 23.415  20.930  -35.859 1.00 27.90  ? 300 HEM B C4D 1 
HETATM 3588 C  CMD . HEM E 3 .   ? 19.979  22.303  -35.187 1.00 28.44  ? 300 HEM B CMD 1 
HETATM 3589 C  CAD . HEM E 3 .   ? 21.241  19.879  -36.908 1.00 30.12  ? 300 HEM B CAD 1 
HETATM 3590 C  CBD . HEM E 3 .   ? 21.123  20.385  -38.345 1.00 35.68  ? 300 HEM B CBD 1 
HETATM 3591 C  CGD . HEM E 3 .   ? 20.381  19.436  -39.258 1.00 38.09  ? 300 HEM B CGD 1 
HETATM 3592 O  O1D . HEM E 3 .   ? 19.405  19.891  -39.900 1.00 39.12  ? 300 HEM B O1D 1 
HETATM 3593 O  O2D . HEM E 3 .   ? 20.786  18.245  -39.340 1.00 50.76  ? 300 HEM B O2D 1 
HETATM 3594 N  NA  . HEM E 3 .   ? 26.292  20.999  -35.367 1.00 46.91  ? 300 HEM B NA  1 
HETATM 3595 N  NB  . HEM E 3 .   ? 27.308  22.946  -33.655 1.00 44.38  ? 300 HEM B NB  1 
HETATM 3596 N  NC  . HEM E 3 .   ? 24.755  23.792  -33.093 1.00 34.02  ? 300 HEM B NC  1 
HETATM 3597 N  ND  . HEM E 3 .   ? 23.743  21.940  -34.966 1.00 29.04  ? 300 HEM B ND  1 
HETATM 3598 FE FE  . HEM E 3 .   ? 25.521  22.475  -34.333 1.00 33.65  ? 300 HEM B FE  1 
HETATM 3599 O  O   . HOH F 4 .   ? 18.814  1.187   2.610   1.00 40.20  ? 301 HOH A O   1 
HETATM 3600 O  O   . HOH F 4 .   ? 14.242  12.501  -9.731  1.00 19.26  ? 302 HOH A O   1 
HETATM 3601 O  O   . HOH F 4 .   ? 9.984   -3.994  -15.396 1.00 20.09  ? 303 HOH A O   1 
HETATM 3602 O  O   . HOH F 4 .   ? 24.524  8.868   -15.513 1.00 16.76  ? 304 HOH A O   1 
HETATM 3603 O  O   . HOH F 4 .   ? 25.339  -8.034  -16.888 1.00 22.68  ? 305 HOH A O   1 
HETATM 3604 O  O   . HOH F 4 .   ? 17.214  11.486  -18.133 1.00 15.19  ? 306 HOH A O   1 
HETATM 3605 O  O   . HOH F 4 .   ? 12.510  8.403   -19.378 1.00 17.56  ? 307 HOH A O   1 
HETATM 3606 O  O   . HOH F 4 .   ? -0.849  1.774   -1.581  1.00 21.78  ? 308 HOH A O   1 
HETATM 3607 O  O   . HOH F 4 .   ? 9.598   -2.918  -3.275  1.00 19.60  ? 309 HOH A O   1 
HETATM 3608 O  O   . HOH F 4 .   ? 14.701  13.720  -7.189  1.00 16.21  ? 310 HOH A O   1 
HETATM 3609 O  O   . HOH F 4 .   ? 14.719  9.564   -12.505 1.00 15.96  ? 311 HOH A O   1 
HETATM 3610 O  O   . HOH F 4 .   ? 11.451  8.547   -14.637 1.00 20.22  ? 312 HOH A O   1 
HETATM 3611 O  O   . HOH F 4 .   ? 19.567  0.859   -25.892 1.00 21.66  ? 313 HOH A O   1 
HETATM 3612 O  O   . HOH F 4 .   ? 15.727  0.379   -0.847  1.00 27.00  ? 314 HOH A O   1 
HETATM 3613 O  O   . HOH F 4 .   ? 6.018   15.420  -7.178  1.00 27.47  ? 315 HOH A O   1 
HETATM 3614 O  O   . HOH F 4 .   ? 7.183   7.907   -8.279  1.00 29.30  ? 316 HOH A O   1 
HETATM 3615 O  O   . HOH F 4 .   ? 15.384  -12.584 -19.980 1.00 27.74  ? 317 HOH A O   1 
HETATM 3616 O  O   . HOH F 4 .   ? 5.848   7.091   -3.448  1.00 22.96  ? 318 HOH A O   1 
HETATM 3617 O  O   . HOH F 4 .   ? 9.268   7.147   -13.901 1.00 18.82  ? 319 HOH A O   1 
HETATM 3618 O  O   . HOH F 4 .   ? 6.318   8.792   -5.594  1.00 28.17  ? 320 HOH A O   1 
HETATM 3619 O  O   . HOH F 4 .   ? -2.765  1.848   1.380   1.00 26.34  ? 321 HOH A O   1 
HETATM 3620 O  O   . HOH F 4 .   ? 25.774  -0.989  -25.954 1.00 23.82  ? 322 HOH A O   1 
HETATM 3621 O  O   . HOH F 4 .   ? 12.799  -2.621  -22.092 1.00 30.73  ? 323 HOH A O   1 
HETATM 3622 O  O   . HOH F 4 .   ? 13.291  -11.944 -6.382  1.00 23.00  ? 324 HOH A O   1 
HETATM 3623 O  O   . HOH F 4 .   ? 7.474   -3.959  -16.210 1.00 27.02  ? 325 HOH A O   1 
HETATM 3624 O  O   . HOH F 4 .   ? 2.939   -10.667 0.495   1.00 40.66  ? 326 HOH A O   1 
HETATM 3625 O  O   . HOH F 4 .   ? 16.206  -6.742  -20.348 1.00 36.52  ? 327 HOH A O   1 
HETATM 3626 O  O   . HOH F 4 .   ? 11.057  9.372   -17.102 1.00 22.65  ? 328 HOH A O   1 
HETATM 3627 O  O   . HOH F 4 .   ? 11.756  -3.962  -17.588 1.00 24.97  ? 329 HOH A O   1 
HETATM 3628 O  O   . HOH F 4 .   ? 11.015  14.567  -15.613 1.00 22.53  ? 330 HOH A O   1 
HETATM 3629 O  O   . HOH F 4 .   ? 7.628   5.667   -15.428 1.00 29.39  ? 331 HOH A O   1 
HETATM 3630 O  O   . HOH F 4 .   ? -5.054  6.627   -10.226 1.00 31.08  ? 332 HOH A O   1 
HETATM 3631 O  O   . HOH F 4 .   ? 18.890  -0.652  -27.895 1.00 28.97  ? 333 HOH A O   1 
HETATM 3632 O  O   . HOH F 4 .   ? 19.589  1.747   -2.529  1.00 35.50  ? 334 HOH A O   1 
HETATM 3633 O  O   . HOH F 4 .   ? 21.257  -1.965  -3.953  1.00 48.93  ? 335 HOH A O   1 
HETATM 3634 O  O   . HOH F 4 .   ? 24.028  11.591  -3.575  1.00 42.94  ? 336 HOH A O   1 
HETATM 3635 O  O   . HOH F 4 .   ? 20.133  12.773  -2.978  1.00 31.67  ? 337 HOH A O   1 
HETATM 3636 O  O   . HOH F 4 .   ? 20.246  -19.061 -11.376 1.00 40.89  ? 338 HOH A O   1 
HETATM 3637 O  O   . HOH F 4 .   ? 18.804  14.183  -1.637  1.00 39.07  ? 339 HOH A O   1 
HETATM 3638 O  O   . HOH F 4 .   ? 36.094  3.709   4.010   0.50 36.25  ? 340 HOH A O   1 
HETATM 3639 O  O   . HOH F 4 .   ? 23.788  -12.866 -1.638  1.00 33.33  ? 341 HOH A O   1 
HETATM 3640 O  O   . HOH F 4 .   ? 27.549  -8.379  -15.276 1.00 25.69  ? 342 HOH A O   1 
HETATM 3641 O  O   . HOH F 4 .   ? 25.104  10.138  -7.108  1.00 19.71  ? 343 HOH A O   1 
HETATM 3642 O  O   . HOH F 4 .   ? 6.948   -2.634  -18.363 1.00 39.58  ? 344 HOH A O   1 
HETATM 3643 O  O   . HOH F 4 .   ? 11.503  -8.374  9.720   1.00 28.14  ? 345 HOH A O   1 
HETATM 3644 O  O   . HOH F 4 .   ? 24.237  9.467   -18.237 1.00 22.13  ? 346 HOH A O   1 
HETATM 3645 O  O   . HOH F 4 .   ? 25.401  -9.080  -19.264 1.00 41.90  ? 347 HOH A O   1 
HETATM 3646 O  O   . HOH F 4 .   ? -1.107  -13.033 3.223   1.00 45.39  ? 348 HOH A O   1 
HETATM 3647 O  O   . HOH F 4 .   ? 31.711  8.583   -15.147 1.00 27.17  ? 349 HOH A O   1 
HETATM 3648 O  O   . HOH F 4 .   ? 13.546  18.602  0.972   1.00 35.36  ? 350 HOH A O   1 
HETATM 3649 O  O   . HOH F 4 .   ? -10.064 14.705  19.168  1.00 57.65  ? 351 HOH A O   1 
HETATM 3650 O  O   . HOH F 4 .   ? 25.909  -3.901  8.175   1.00 35.10  ? 352 HOH A O   1 
HETATM 3651 O  O   . HOH F 4 .   ? 8.070   -9.305  -16.848 1.00 38.30  ? 353 HOH A O   1 
HETATM 3652 O  O   . HOH F 4 .   ? 20.788  -12.152 -20.280 1.00 46.33  ? 354 HOH A O   1 
HETATM 3653 O  O   . HOH F 4 .   ? -2.701  12.108  -6.821  1.00 36.99  ? 355 HOH A O   1 
HETATM 3654 O  O   . HOH F 4 .   ? 19.389  6.066   -4.523  1.00 31.82  ? 356 HOH A O   1 
HETATM 3655 O  O   . HOH F 4 .   ? 20.018  20.188  2.019   1.00 49.11  ? 357 HOH A O   1 
HETATM 3656 O  O   . HOH F 4 .   ? -0.563  5.455   10.913  1.00 33.10  ? 358 HOH A O   1 
HETATM 3657 O  O   . HOH F 4 .   ? -13.198 0.589   5.234   1.00 56.06  ? 359 HOH A O   1 
HETATM 3658 O  O   . HOH F 4 .   ? -7.912  -4.849  15.423  1.00 27.90  ? 360 HOH A O   1 
HETATM 3659 O  O   . HOH F 4 .   ? 24.235  -15.868 -1.588  1.00 32.36  ? 361 HOH A O   1 
HETATM 3660 O  O   . HOH F 4 .   ? 28.556  -11.339 -15.405 1.00 42.22  ? 362 HOH A O   1 
HETATM 3661 O  O   . HOH F 4 .   ? 35.790  -26.423 -12.447 1.00 32.12  ? 363 HOH A O   1 
HETATM 3662 O  O   . HOH F 4 .   ? 37.454  11.155  -18.909 0.50 42.16  ? 364 HOH A O   1 
HETATM 3663 O  O   . HOH F 4 .   ? 12.971  2.693   -20.346 1.00 24.94  ? 365 HOH A O   1 
HETATM 3664 O  O   . HOH F 4 .   ? -2.124  13.288  -9.752  1.00 49.67  ? 366 HOH A O   1 
HETATM 3665 O  O   . HOH F 4 .   ? 31.092  -0.856  -18.329 1.00 41.43  ? 367 HOH A O   1 
HETATM 3666 O  O   . HOH F 4 .   ? 20.719  8.167   -2.680  1.00 31.62  ? 368 HOH A O   1 
HETATM 3667 O  O   . HOH F 4 .   ? 8.690   15.783  -15.017 1.00 35.98  ? 369 HOH A O   1 
HETATM 3668 O  O   . HOH F 4 .   ? 23.962  -17.175 -3.698  1.00 36.09  ? 370 HOH A O   1 
HETATM 3669 O  O   . HOH F 4 .   ? 13.381  20.433  -9.130  1.00 33.68  ? 371 HOH A O   1 
HETATM 3670 O  O   . HOH F 4 .   ? 15.642  10.719  9.317   0.50 42.54  ? 372 HOH A O   1 
HETATM 3671 O  O   . HOH F 4 .   ? 35.838  -5.217  -16.234 0.50 51.79  ? 373 HOH A O   1 
HETATM 3672 O  O   . HOH F 4 .   ? 15.716  -4.250  -21.790 1.00 33.78  ? 374 HOH A O   1 
HETATM 3673 O  O   . HOH F 4 .   ? -2.976  -10.774 -6.578  1.00 41.89  ? 375 HOH A O   1 
HETATM 3674 O  O   . HOH F 4 .   ? -1.503  5.079   8.005   1.00 29.33  ? 376 HOH A O   1 
HETATM 3675 O  O   . HOH F 4 .   ? 13.817  -1.052  9.618   1.00 37.25  ? 377 HOH A O   1 
HETATM 3676 O  O   . HOH F 4 .   ? 11.645  -1.986  -19.596 1.00 24.50  ? 378 HOH A O   1 
HETATM 3677 O  O   . HOH F 4 .   ? 7.831   2.927   -15.765 1.00 23.02  ? 379 HOH A O   1 
HETATM 3678 O  O   . HOH F 4 .   ? 2.935   -13.136 -2.803  1.00 48.99  ? 380 HOH A O   1 
HETATM 3679 O  O   . HOH F 4 .   ? 17.901  11.635  -15.425 1.00 18.26  ? 381 HOH A O   1 
HETATM 3680 O  O   . HOH F 4 .   ? 27.221  -3.798  -22.884 1.00 39.02  ? 382 HOH A O   1 
HETATM 3681 O  O   . HOH F 4 .   ? 15.455  -16.796 -7.630  1.00 42.93  ? 383 HOH A O   1 
HETATM 3682 O  O   . HOH F 4 .   ? 15.741  9.560   -19.536 1.00 15.57  ? 384 HOH A O   1 
HETATM 3683 O  O   . HOH F 4 .   ? 18.270  -11.470 -20.044 1.00 33.58  ? 385 HOH A O   1 
HETATM 3684 O  O   . HOH F 4 .   ? 0.919   -8.928  2.356   1.00 29.50  ? 386 HOH A O   1 
HETATM 3685 O  O   . HOH F 4 .   ? 38.303  -3.591  2.955   1.00 26.59  ? 387 HOH A O   1 
HETATM 3686 O  O   . HOH F 4 .   ? -1.099  -10.489 2.387   1.00 37.62  ? 388 HOH A O   1 
HETATM 3687 O  O   . HOH F 4 .   ? -5.274  -0.910  -9.421  1.00 37.11  ? 389 HOH A O   1 
HETATM 3688 O  O   . HOH F 4 .   ? 11.788  -7.112  12.873  1.00 39.89  ? 390 HOH A O   1 
HETATM 3689 O  O   . HOH F 4 .   ? 30.215  -7.643  -7.057  1.00 36.20  ? 391 HOH A O   1 
HETATM 3690 O  O   . HOH F 4 .   ? 9.886   4.926   8.997   1.00 32.16  ? 392 HOH A O   1 
HETATM 3691 O  O   . HOH F 4 .   ? 33.952  -6.787  -13.180 1.00 33.59  ? 393 HOH A O   1 
HETATM 3692 O  O   . HOH F 4 .   ? -7.563  0.494   2.109   1.00 40.75  ? 394 HOH A O   1 
HETATM 3693 O  O   . HOH F 4 .   ? 17.435  -16.572 -5.533  1.00 29.58  ? 395 HOH A O   1 
HETATM 3694 O  O   . HOH F 4 .   ? 26.587  -8.435  7.314   1.00 44.42  ? 396 HOH A O   1 
HETATM 3695 O  O   . HOH F 4 .   ? 18.059  -3.408  -3.404  1.00 37.74  ? 397 HOH A O   1 
HETATM 3696 O  O   . HOH F 4 .   ? 32.497  -10.145 -11.064 1.00 36.27  ? 398 HOH A O   1 
HETATM 3697 O  O   . HOH F 4 .   ? 3.228   -9.963  -14.855 1.00 57.89  ? 399 HOH A O   1 
HETATM 3698 O  O   . HOH F 4 .   ? 35.571  -18.086 -12.250 1.00 59.50  ? 400 HOH A O   1 
HETATM 3699 O  O   . HOH F 4 .   ? 32.386  1.942   -18.491 0.50 50.10  ? 401 HOH A O   1 
HETATM 3700 O  O   . HOH F 4 .   ? 15.394  2.939   -23.816 1.00 30.44  ? 402 HOH A O   1 
HETATM 3701 O  O   . HOH F 4 .   ? 20.886  -13.228 4.456   1.00 38.18  ? 403 HOH A O   1 
HETATM 3702 O  O   . HOH F 4 .   ? 20.966  -14.477 1.749   1.00 39.06  ? 404 HOH A O   1 
HETATM 3703 O  O   . HOH F 4 .   ? 7.527   2.381   -18.287 1.00 31.95  ? 405 HOH A O   1 
HETATM 3704 O  O   . HOH F 4 .   ? -1.398  13.287  -4.455  1.00 39.24  ? 406 HOH A O   1 
HETATM 3705 O  O   . HOH F 4 .   ? 5.449   8.169   -12.425 1.00 50.88  ? 407 HOH A O   1 
HETATM 3706 O  O   . HOH F 4 .   ? 11.419  11.889  -16.254 1.00 32.03  ? 408 HOH A O   1 
HETATM 3707 O  O   . HOH F 4 .   ? 35.881  -4.494  -11.473 1.00 38.56  ? 409 HOH A O   1 
HETATM 3708 O  O   . HOH F 4 .   ? 36.493  -20.634 -14.837 0.50 78.73  ? 410 HOH A O   1 
HETATM 3709 O  O   . HOH F 4 .   ? 18.496  -7.225  13.570  1.00 41.98  ? 411 HOH A O   1 
HETATM 3710 O  O   . HOH F 4 .   ? -0.834  13.064  -11.633 0.50 39.05  ? 412 HOH A O   1 
HETATM 3711 O  O   . HOH F 4 .   ? -7.631  10.424  -3.572  1.00 44.20  ? 413 HOH A O   1 
HETATM 3712 O  O   . HOH F 4 .   ? 26.530  5.556   -23.910 1.00 35.76  ? 414 HOH A O   1 
HETATM 3713 O  O   . HOH F 4 .   ? 6.279   -12.981 -7.491  1.00 37.92  ? 415 HOH A O   1 
HETATM 3714 O  O   . HOH F 4 .   ? 2.149   -9.792  -12.471 1.00 32.28  ? 416 HOH A O   1 
HETATM 3715 O  O   . HOH F 4 .   ? 20.458  4.007   -2.768  1.00 37.64  ? 417 HOH A O   1 
HETATM 3716 O  O   . HOH F 4 .   ? 23.320  6.471   3.805   1.00 45.87  ? 418 HOH A O   1 
HETATM 3717 O  O   . HOH F 4 .   ? 23.783  7.307   6.918   1.00 54.43  ? 419 HOH A O   1 
HETATM 3718 O  O   . HOH F 4 .   ? 13.619  20.822  2.272   1.00 49.09  ? 420 HOH A O   1 
HETATM 3719 O  O   . HOH F 4 .   ? 19.473  15.785  5.167   1.00 42.96  ? 421 HOH A O   1 
HETATM 3720 O  O   . HOH F 4 .   ? -8.524  0.298   4.826   1.00 41.32  ? 422 HOH A O   1 
HETATM 3721 O  O   . HOH F 4 .   ? -9.974  -4.949  9.422   1.00 30.44  ? 423 HOH A O   1 
HETATM 3722 O  O   . HOH F 4 .   ? -5.976  -9.257  5.898   1.00 41.92  ? 424 HOH A O   1 
HETATM 3723 O  O   . HOH F 4 .   ? 29.978  -6.415  7.095   0.50 56.30  ? 425 HOH A O   1 
HETATM 3724 O  O   . HOH F 4 .   ? 12.691  19.294  -1.925  1.00 47.29  ? 426 HOH A O   1 
HETATM 3725 O  O   . HOH F 4 .   ? 10.933  20.010  -8.545  1.00 34.78  ? 427 HOH A O   1 
HETATM 3726 O  O   . HOH F 4 .   ? 9.276   21.025  -4.799  1.00 40.70  ? 428 HOH A O   1 
HETATM 3727 O  O   . HOH F 4 .   ? 6.665   8.001   -10.511 1.00 42.84  ? 429 HOH A O   1 
HETATM 3728 O  O   . HOH F 4 .   ? -2.167  2.871   8.979   1.00 41.27  ? 430 HOH A O   1 
HETATM 3729 O  O   . HOH F 4 .   ? 30.667  -3.602  8.416   1.00 56.21  ? 431 HOH A O   1 
HETATM 3730 O  O   . HOH F 4 .   ? -6.787  -7.647  11.984  1.00 38.55  ? 432 HOH A O   1 
HETATM 3731 O  O   . HOH F 4 .   ? 29.049  -24.191 -12.705 1.00 38.92  ? 433 HOH A O   1 
HETATM 3732 O  O   . HOH F 4 .   ? -5.382  -6.270  14.983  1.00 54.85  ? 434 HOH A O   1 
HETATM 3733 O  O   . HOH F 4 .   ? 13.330  20.646  -4.247  1.00 55.49  ? 435 HOH A O   1 
HETATM 3734 O  O   . HOH F 4 .   ? 1.406   -0.389  18.328  0.50 44.12  ? 436 HOH A O   1 
HETATM 3735 O  O   . HOH F 4 .   ? 12.696  -1.058  7.291   1.00 46.51  ? 437 HOH A O   1 
HETATM 3736 O  O   . HOH F 4 .   ? 10.692  18.854  -5.745  1.00 29.09  ? 438 HOH A O   1 
HETATM 3737 O  O   . HOH F 4 .   ? 30.015  3.866   -21.730 1.00 45.10  ? 439 HOH A O   1 
HETATM 3738 O  O   . HOH F 4 .   ? 28.639  -0.384  -26.777 1.00 53.47  ? 440 HOH A O   1 
HETATM 3739 O  O   . HOH F 4 .   ? 1.434   -12.324 -12.652 1.00 52.99  ? 441 HOH A O   1 
HETATM 3740 O  O   . HOH F 4 .   ? -0.268  -14.963 -9.388  1.00 37.65  ? 442 HOH A O   1 
HETATM 3741 O  O   . HOH F 4 .   ? -0.070  -8.567  -13.271 1.00 44.35  ? 443 HOH A O   1 
HETATM 3742 O  O   . HOH F 4 .   ? 18.274  -0.035  -0.462  1.00 40.35  ? 444 HOH A O   1 
HETATM 3743 O  O   . HOH F 4 .   ? 15.289  20.646  -6.132  1.00 37.42  ? 445 HOH A O   1 
HETATM 3744 O  O   . HOH F 4 .   ? 10.355  18.517  -0.907  1.00 51.94  ? 446 HOH A O   1 
HETATM 3745 O  O   . HOH F 4 .   ? 10.858  18.582  -10.847 1.00 37.50  ? 447 HOH A O   1 
HETATM 3746 O  O   . HOH F 4 .   ? -5.364  2.236   2.495   1.00 41.37  ? 448 HOH A O   1 
HETATM 3747 O  O   . HOH F 4 .   ? -3.382  -4.115  12.247  1.00 49.58  ? 449 HOH A O   1 
HETATM 3748 O  O   . HOH F 4 .   ? 19.439  -16.701 -13.126 1.00 30.57  ? 450 HOH A O   1 
HETATM 3749 O  O   . HOH F 4 .   ? 34.468  -16.537 -13.538 0.50 42.03  ? 451 HOH A O   1 
HETATM 3750 O  O   . HOH F 4 .   ? 34.540  -21.734 -13.473 1.00 53.87  ? 452 HOH A O   1 
HETATM 3751 O  O   . HOH F 4 .   ? 12.443  -4.758  -23.814 1.00 56.34  ? 453 HOH A O   1 
HETATM 3752 O  O   . HOH F 4 .   ? -5.170  8.466   -12.629 0.50 42.75  ? 454 HOH A O   1 
HETATM 3753 O  O   . HOH F 4 .   ? 14.404  -4.378  -26.247 1.00 55.65  ? 455 HOH A O   1 
HETATM 3754 O  O   . HOH F 4 .   ? 16.756  -17.249 -10.127 1.00 33.64  ? 456 HOH A O   1 
HETATM 3755 O  O   . HOH F 4 .   ? 21.088  16.291  -4.220  1.00 33.25  ? 457 HOH A O   1 
HETATM 3756 O  O   . HOH F 4 .   ? 20.329  15.845  0.650   1.00 55.19  ? 458 HOH A O   1 
HETATM 3757 O  O   . HOH F 4 .   ? -10.220 -4.277  5.868   1.00 47.40  ? 459 HOH A O   1 
HETATM 3758 O  O   . HOH F 4 .   ? 19.135  17.526  -4.414  1.00 39.50  ? 460 HOH A O   1 
HETATM 3759 O  O   . HOH F 4 .   ? 23.715  -15.226 1.782   1.00 44.42  ? 461 HOH A O   1 
HETATM 3760 O  O   . HOH F 4 .   ? 26.389  -12.333 -15.665 1.00 48.47  ? 462 HOH A O   1 
HETATM 3761 O  O   . HOH F 4 .   ? 6.240   -0.193  -18.131 1.00 40.09  ? 463 HOH A O   1 
HETATM 3762 O  O   . HOH F 4 .   ? 8.761   6.468   -17.908 1.00 47.83  ? 464 HOH A O   1 
HETATM 3763 O  O   . HOH F 4 .   ? 34.318  -16.096 -11.097 1.00 48.82  ? 465 HOH A O   1 
HETATM 3764 O  O   . HOH F 4 .   ? 7.197   -10.852 -14.514 1.00 60.83  ? 466 HOH A O   1 
HETATM 3765 O  O   . HOH F 4 .   ? 28.496  -2.513  9.345   1.00 54.30  ? 467 HOH A O   1 
HETATM 3766 O  O   . HOH F 4 .   ? 6.482   -6.380  -17.311 1.00 53.86  ? 468 HOH A O   1 
HETATM 3767 O  O   . HOH F 4 .   ? 21.891  -14.274 -20.812 1.00 41.44  ? 469 HOH A O   1 
HETATM 3768 O  O   . HOH F 4 .   ? 29.367  -7.140  -4.141  1.00 47.55  ? 470 HOH A O   1 
HETATM 3769 O  O   . HOH F 4 .   ? -4.427  -7.223  -0.504  1.00 37.70  ? 471 HOH A O   1 
HETATM 3770 O  O   . HOH F 4 .   ? -4.360  7.488   9.735   1.00 55.58  ? 472 HOH A O   1 
HETATM 3771 O  O   . HOH F 4 .   ? -5.266  0.840   11.632  1.00 57.50  ? 473 HOH A O   1 
HETATM 3772 O  O   . HOH F 4 .   ? 27.908  -19.697 -9.128  1.00 45.58  ? 474 HOH A O   1 
HETATM 3773 O  O   . HOH F 4 .   ? 11.003  -5.922  -18.518 1.00 48.23  ? 475 HOH A O   1 
HETATM 3774 O  O   . HOH F 4 .   ? 20.573  0.228   -3.947  1.00 53.75  ? 476 HOH A O   1 
HETATM 3775 O  O   . HOH F 4 .   ? 15.197  -3.324  -28.377 1.00 57.09  ? 477 HOH A O   1 
HETATM 3776 O  O   . HOH F 4 .   ? 1.070   3.343   -15.549 1.00 36.45  ? 478 HOH A O   1 
HETATM 3777 O  O   . HOH F 4 .   ? -6.615  8.755   1.196   1.00 43.81  ? 479 HOH A O   1 
HETATM 3778 O  O   . HOH F 4 .   ? 17.592  -17.679 -3.228  1.00 46.98  ? 480 HOH A O   1 
HETATM 3779 O  O   . HOH F 4 .   ? 2.669   -12.751 -0.433  1.00 52.35  ? 481 HOH A O   1 
HETATM 3780 O  O   . HOH F 4 .   ? 20.460  9.659   -0.724  1.00 51.43  ? 482 HOH A O   1 
HETATM 3781 O  O   . HOH F 4 .   ? 3.929   16.094  -6.087  1.00 58.50  ? 483 HOH A O   1 
HETATM 3782 O  O   . HOH F 4 .   ? 10.549  -16.131 -12.555 1.00 47.36  ? 484 HOH A O   1 
HETATM 3783 O  O   . HOH F 4 .   ? 8.351   -14.942 -11.880 1.00 52.29  ? 485 HOH A O   1 
HETATM 3784 O  O   . HOH F 4 .   ? 30.021  0.324   -22.873 1.00 56.25  ? 486 HOH A O   1 
HETATM 3785 O  O   . HOH F 4 .   ? -10.495 -2.074  3.459   1.00 50.17  ? 487 HOH A O   1 
HETATM 3786 O  O   . HOH F 4 .   ? 30.983  -14.512 -0.028  1.00 58.78  ? 488 HOH A O   1 
HETATM 3787 O  O   . HOH F 4 .   ? -9.581  2.645   -4.034  0.50 51.44  ? 489 HOH A O   1 
HETATM 3788 O  O   . HOH F 4 .   ? 39.930  2.621   -5.973  0.50 57.72  ? 490 HOH A O   1 
HETATM 3789 O  O   . HOH F 4 .   ? 39.283  -0.284  -13.251 0.50 45.98  ? 491 HOH A O   1 
HETATM 3790 O  O   . HOH F 4 .   ? 9.846   5.774   11.949  1.00 51.43  ? 492 HOH A O   1 
HETATM 3791 O  O   . HOH F 4 .   ? 3.317   4.936   -16.854 1.00 54.88  ? 493 HOH A O   1 
HETATM 3792 O  O   . HOH F 4 .   ? -7.372  2.690   -11.836 0.50 46.36  ? 494 HOH A O   1 
HETATM 3793 O  O   . HOH F 4 .   ? 38.338  3.230   -16.760 0.50 50.70  ? 495 HOH A O   1 
HETATM 3794 O  O   . HOH F 4 .   ? -9.171  -4.229  1.484   1.00 60.17  ? 496 HOH A O   1 
HETATM 3795 O  O   . HOH F 4 .   ? 6.097   -16.500 -8.728  0.50 47.13  ? 497 HOH A O   1 
HETATM 3796 O  O   . HOH F 4 .   ? 29.603  15.756  -5.743  1.00 54.59  ? 498 HOH A O   1 
HETATM 3797 O  O   . HOH F 4 .   ? -3.594  7.171   -13.685 1.00 45.89  ? 499 HOH A O   1 
HETATM 3798 O  O   . HOH F 4 .   ? 21.839  21.395  1.422   1.00 118.45 ? 500 HOH A O   1 
HETATM 3799 O  O   . HOH F 4 .   ? 0.860   -6.749  11.684  1.00 71.34  ? 501 HOH A O   1 
HETATM 3800 O  O   . HOH F 4 .   ? 5.640   -3.081  13.489  1.00 73.93  ? 502 HOH A O   1 
HETATM 3801 O  O   . HOH F 4 .   ? 39.359  -25.380 -13.870 1.00 76.47  ? 503 HOH A O   1 
HETATM 3802 O  O   . HOH F 4 .   ? -3.692  14.030  -3.302  1.00 55.14  ? 504 HOH A O   1 
HETATM 3803 O  O   . HOH F 4 .   ? 12.493  -14.198 6.848   1.00 76.55  ? 505 HOH A O   1 
HETATM 3804 O  O   . HOH F 4 .   ? 12.205  -6.868  -20.956 1.00 64.72  ? 506 HOH A O   1 
HETATM 3805 O  O   . HOH F 4 .   ? 18.261  -11.141 10.729  1.00 71.34  ? 507 HOH A O   1 
HETATM 3806 O  O   . HOH F 4 .   ? -9.558  -5.491  -0.502  1.00 123.83 ? 508 HOH A O   1 
HETATM 3807 O  O   . HOH F 4 .   ? 39.166  -1.599  -3.841  1.00 140.34 ? 509 HOH A O   1 
HETATM 3808 O  O   . HOH F 4 .   ? 16.454  7.960   8.530   1.00 85.62  ? 510 HOH A O   1 
HETATM 3809 O  O   . HOH F 4 .   ? 10.063  -10.685 9.838   1.00 73.93  ? 511 HOH A O   1 
HETATM 3810 O  O   . HOH F 4 .   ? 7.400   11.104  -13.390 1.00 66.75  ? 512 HOH A O   1 
HETATM 3811 O  O   . HOH F 4 .   ? 25.045  7.877   -19.678 1.00 59.42  ? 513 HOH A O   1 
HETATM 3812 O  O   . HOH F 4 .   ? 3.556   5.458   16.880  1.00 63.13  ? 514 HOH A O   1 
HETATM 3813 O  O   . HOH F 4 .   ? 0.069   14.090  6.272   1.00 55.35  ? 515 HOH A O   1 
HETATM 3814 O  O   . HOH F 4 .   ? 18.323  -7.077  -23.102 1.00 61.29  ? 516 HOH A O   1 
HETATM 3815 O  O   . HOH F 4 .   ? 5.318   6.435   -15.635 1.00 64.14  ? 517 HOH A O   1 
HETATM 3816 O  O   . HOH F 4 .   ? 26.215  -18.586 -5.226  1.00 57.14  ? 518 HOH A O   1 
HETATM 3817 O  O   . HOH F 4 .   ? 23.676  22.919  -0.792  1.00 117.57 ? 519 HOH A O   1 
HETATM 3818 O  O   . HOH G 4 .   ? 25.327  21.142  -32.759 1.00 42.92  ? 301 HOH B O   1 
HETATM 3819 O  O   . HOH G 4 .   ? 16.320  11.868  -12.962 1.00 13.96  ? 302 HOH B O   1 
HETATM 3820 O  O   . HOH G 4 .   ? 4.939   22.834  -33.700 1.00 19.74  ? 303 HOH B O   1 
HETATM 3821 O  O   . HOH G 4 .   ? 14.934  26.497  -29.216 1.00 19.19  ? 304 HOH B O   1 
HETATM 3822 O  O   . HOH G 4 .   ? 6.274   19.461  -43.083 1.00 29.43  ? 305 HOH B O   1 
HETATM 3823 O  O   . HOH G 4 .   ? 24.357  13.683  -13.273 1.00 16.73  ? 306 HOH B O   1 
HETATM 3824 O  O   . HOH G 4 .   ? 16.996  9.700   -24.094 1.00 15.35  ? 307 HOH B O   1 
HETATM 3825 O  O   . HOH G 4 .   ? 9.414   28.351  -17.630 1.00 22.48  ? 308 HOH B O   1 
HETATM 3826 O  O   . HOH G 4 .   ? 12.980  21.049  -11.786 1.00 21.84  ? 309 HOH B O   1 
HETATM 3827 O  O   . HOH G 4 .   ? 11.983  27.988  -17.529 1.00 18.46  ? 310 HOH B O   1 
HETATM 3828 O  O   . HOH G 4 .   ? 23.426  10.392  -26.548 1.00 31.65  ? 311 HOH B O   1 
HETATM 3829 O  O   . HOH G 4 .   ? 9.603   15.362  -27.905 1.00 33.40  ? 312 HOH B O   1 
HETATM 3830 O  O   . HOH G 4 .   ? 8.815   33.082  -36.594 1.00 27.81  ? 313 HOH B O   1 
HETATM 3831 O  O   . HOH G 4 .   ? 10.179  16.955  -30.180 1.00 24.06  ? 314 HOH B O   1 
HETATM 3832 O  O   . HOH G 4 .   ? 23.243  13.547  -10.631 1.00 20.31  ? 315 HOH B O   1 
HETATM 3833 O  O   . HOH G 4 .   ? 14.926  39.218  -20.269 1.00 21.70  ? 316 HOH B O   1 
HETATM 3834 O  O   . HOH G 4 .   ? 11.865  15.481  -13.068 1.00 18.59  ? 317 HOH B O   1 
HETATM 3835 O  O   . HOH G 4 .   ? 15.992  11.052  -21.864 1.00 17.71  ? 318 HOH B O   1 
HETATM 3836 O  O   . HOH G 4 .   ? 9.106   21.339  -17.808 1.00 21.04  ? 319 HOH B O   1 
HETATM 3837 O  O   . HOH G 4 .   ? 6.701   35.566  -42.335 1.00 30.27  ? 320 HOH B O   1 
HETATM 3838 O  O   . HOH G 4 .   ? 10.584  17.016  -19.185 1.00 19.29  ? 321 HOH B O   1 
HETATM 3839 O  O   . HOH G 4 .   ? 3.483   35.109  -30.137 1.00 35.15  ? 322 HOH B O   1 
HETATM 3840 O  O   . HOH G 4 .   ? 18.737  34.940  -25.344 1.00 21.46  ? 323 HOH B O   1 
HETATM 3841 O  O   . HOH G 4 .   ? 12.291  15.298  -17.898 1.00 18.29  ? 324 HOH B O   1 
HETATM 3842 O  O   . HOH G 4 .   ? 8.635   8.504   -26.385 1.00 24.14  ? 325 HOH B O   1 
HETATM 3843 O  O   . HOH G 4 .   ? 16.767  30.525  -10.953 1.00 38.29  ? 326 HOH B O   1 
HETATM 3844 O  O   . HOH G 4 .   ? 18.241  4.812   -32.339 1.00 37.55  ? 327 HOH B O   1 
HETATM 3845 O  O   . HOH G 4 .   ? 29.300  13.748  -6.814  1.00 30.83  ? 328 HOH B O   1 
HETATM 3846 O  O   . HOH G 4 .   ? 23.150  26.436  -26.749 1.00 39.79  ? 329 HOH B O   1 
HETATM 3847 O  O   . HOH G 4 .   ? 3.819   22.810  -37.029 1.00 29.29  ? 330 HOH B O   1 
HETATM 3848 O  O   . HOH G 4 .   ? 36.566  14.899  -16.102 1.00 30.27  ? 331 HOH B O   1 
HETATM 3849 O  O   . HOH G 4 .   ? 17.976  3.088   -25.792 1.00 31.07  ? 332 HOH B O   1 
HETATM 3850 O  O   . HOH G 4 .   ? 29.837  39.227  -24.908 1.00 27.01  ? 333 HOH B O   1 
HETATM 3851 O  O   . HOH G 4 .   ? 31.186  13.215  -11.072 1.00 24.28  ? 334 HOH B O   1 
HETATM 3852 O  O   . HOH G 4 .   ? 4.923   10.535  -31.968 1.00 28.46  ? 335 HOH B O   1 
HETATM 3853 O  O   . HOH G 4 .   ? 38.920  19.845  -23.452 1.00 35.29  ? 336 HOH B O   1 
HETATM 3854 O  O   . HOH G 4 .   ? 24.973  11.203  -14.122 1.00 26.14  ? 337 HOH B O   1 
HETATM 3855 O  O   . HOH G 4 .   ? 0.699   12.958  -29.039 1.00 31.16  ? 338 HOH B O   1 
HETATM 3856 O  O   . HOH G 4 .   ? 30.127  34.554  -26.682 1.00 28.74  ? 339 HOH B O   1 
HETATM 3857 O  O   . HOH G 4 .   ? 10.438  34.917  -16.422 1.00 29.95  ? 340 HOH B O   1 
HETATM 3858 O  O   . HOH G 4 .   ? 2.573   10.225  -37.335 1.00 57.05  ? 341 HOH B O   1 
HETATM 3859 O  O   . HOH G 4 .   ? 3.867   8.049   -32.701 1.00 31.20  ? 342 HOH B O   1 
HETATM 3860 O  O   . HOH G 4 .   ? 6.762   8.990   -29.185 1.00 27.95  ? 343 HOH B O   1 
HETATM 3861 O  O   . HOH G 4 .   ? 6.250   28.908  -47.500 1.00 35.17  ? 344 HOH B O   1 
HETATM 3862 O  O   . HOH G 4 .   ? 13.000  28.321  -15.009 1.00 29.83  ? 345 HOH B O   1 
HETATM 3863 O  O   . HOH G 4 .   ? 14.818  13.993  -12.011 1.00 16.57  ? 346 HOH B O   1 
HETATM 3864 O  O   . HOH G 4 .   ? 4.630   34.002  -43.550 1.00 26.12  ? 347 HOH B O   1 
HETATM 3865 O  O   . HOH G 4 .   ? 0.578   11.958  -26.369 1.00 37.96  ? 348 HOH B O   1 
HETATM 3866 O  O   . HOH G 4 .   ? -1.712  30.732  -45.138 1.00 32.39  ? 349 HOH B O   1 
HETATM 3867 O  O   . HOH G 4 .   ? -0.749  25.872  -41.282 1.00 36.15  ? 350 HOH B O   1 
HETATM 3868 O  O   . HOH G 4 .   ? 26.066  26.364  -5.212  1.00 39.51  ? 351 HOH B O   1 
HETATM 3869 O  O   . HOH G 4 .   ? 11.518  27.074  -13.415 1.00 42.07  ? 352 HOH B O   1 
HETATM 3870 O  O   . HOH G 4 .   ? 11.749  3.689   -32.257 1.00 33.85  ? 353 HOH B O   1 
HETATM 3871 O  O   . HOH G 4 .   ? 21.661  5.047   -25.509 1.00 30.32  ? 354 HOH B O   1 
HETATM 3872 O  O   . HOH G 4 .   ? 22.615  23.852  -40.130 1.00 45.19  ? 355 HOH B O   1 
HETATM 3873 O  O   . HOH G 4 .   ? 38.730  22.606  -13.385 1.00 46.54  ? 356 HOH B O   1 
HETATM 3874 O  O   . HOH G 4 .   ? 9.753   37.562  -27.646 1.00 54.92  ? 357 HOH B O   1 
HETATM 3875 O  O   . HOH G 4 .   ? 24.897  18.627  -26.547 1.00 29.66  ? 358 HOH B O   1 
HETATM 3876 O  O   . HOH G 4 .   ? 7.537   11.856  -43.948 1.00 50.94  ? 359 HOH B O   1 
HETATM 3877 O  O   . HOH G 4 .   ? 28.799  35.415  -33.325 1.00 41.33  ? 360 HOH B O   1 
HETATM 3878 O  O   . HOH G 4 .   ? -2.130  18.977  -26.541 1.00 31.61  ? 361 HOH B O   1 
HETATM 3879 O  O   . HOH G 4 .   ? 2.621   31.704  -36.211 1.00 29.71  ? 362 HOH B O   1 
HETATM 3880 O  O   . HOH G 4 .   ? 16.924  3.608   -28.956 1.00 47.70  ? 363 HOH B O   1 
HETATM 3881 O  O   . HOH G 4 .   ? 37.672  25.737  -13.664 1.00 41.49  ? 364 HOH B O   1 
HETATM 3882 O  O   . HOH G 4 .   ? 8.912   12.348  -19.769 1.00 48.03  ? 365 HOH B O   1 
HETATM 3883 O  O   . HOH G 4 .   ? 21.125  22.749  -30.126 1.00 31.51  ? 366 HOH B O   1 
HETATM 3884 O  O   . HOH G 4 .   ? 12.446  3.868   -36.118 1.00 34.15  ? 367 HOH B O   1 
HETATM 3885 O  O   . HOH G 4 .   ? 8.364   18.746  -18.139 1.00 34.89  ? 368 HOH B O   1 
HETATM 3886 O  O   . HOH G 4 .   ? 21.556  29.923  -44.375 1.00 41.46  ? 369 HOH B O   1 
HETATM 3887 O  O   . HOH G 4 .   ? 22.682  12.757  -39.832 1.00 50.06  ? 370 HOH B O   1 
HETATM 3888 O  O   . HOH G 4 .   ? 6.174   22.053  -44.078 1.00 34.29  ? 371 HOH B O   1 
HETATM 3889 O  O   . HOH G 4 .   ? 2.613   9.505   -26.189 1.00 37.84  ? 372 HOH B O   1 
HETATM 3890 O  O   . HOH G 4 .   ? 5.993   6.951   -23.618 1.00 41.34  ? 373 HOH B O   1 
HETATM 3891 O  O   . HOH G 4 .   ? 23.209  16.701  -25.248 1.00 34.99  ? 374 HOH B O   1 
HETATM 3892 O  O   . HOH G 4 .   ? 15.392  28.146  -10.480 1.00 38.87  ? 375 HOH B O   1 
HETATM 3893 O  O   . HOH G 4 .   ? 22.439  8.668   -28.408 1.00 43.34  ? 376 HOH B O   1 
HETATM 3894 O  O   . HOH G 4 .   ? 1.479   23.085  -38.506 1.00 33.99  ? 377 HOH B O   1 
HETATM 3895 O  O   . HOH G 4 .   ? 15.928  37.707  -30.687 1.00 55.83  ? 378 HOH B O   1 
HETATM 3896 O  O   . HOH G 4 .   ? 23.000  39.178  -25.028 1.00 39.58  ? 379 HOH B O   1 
HETATM 3897 O  O   . HOH G 4 .   ? 30.137  38.553  -13.139 1.00 23.94  ? 380 HOH B O   1 
HETATM 3898 O  O   . HOH G 4 .   ? 23.410  41.540  -17.382 1.00 51.42  ? 381 HOH B O   1 
HETATM 3899 O  O   . HOH G 4 .   ? 8.467   27.078  -15.301 1.00 34.35  ? 382 HOH B O   1 
HETATM 3900 O  O   . HOH G 4 .   ? 5.697   28.127  -16.672 1.00 36.86  ? 383 HOH B O   1 
HETATM 3901 O  O   . HOH G 4 .   ? 17.094  22.277  -5.164  1.00 23.82  ? 384 HOH B O   1 
HETATM 3902 O  O   . HOH G 4 .   ? 24.043  40.592  -27.126 1.00 40.88  ? 385 HOH B O   1 
HETATM 3903 O  O   . HOH G 4 .   ? 8.377   16.385  -23.014 1.00 43.97  ? 386 HOH B O   1 
HETATM 3904 O  O   . HOH G 4 .   ? 34.966  32.231  -22.701 1.00 41.27  ? 387 HOH B O   1 
HETATM 3905 O  O   . HOH G 4 .   ? 26.506  30.181  -11.609 1.00 25.86  ? 388 HOH B O   1 
HETATM 3906 O  O   . HOH G 4 .   ? 4.482   37.367  -29.063 1.00 34.40  ? 389 HOH B O   1 
HETATM 3907 O  O   . HOH G 4 .   ? 15.883  27.893  -51.293 0.50 39.06  ? 390 HOH B O   1 
HETATM 3908 O  O   . HOH G 4 .   ? 6.197   34.516  -22.453 1.00 32.15  ? 391 HOH B O   1 
HETATM 3909 O  O   . HOH G 4 .   ? 29.594  44.113  -17.901 1.00 45.18  ? 392 HOH B O   1 
HETATM 3910 O  O   . HOH G 4 .   ? 12.987  31.063  -12.089 0.50 38.33  ? 393 HOH B O   1 
HETATM 3911 O  O   . HOH G 4 .   ? 28.865  14.442  -31.048 1.00 48.73  ? 394 HOH B O   1 
HETATM 3912 O  O   . HOH G 4 .   ? -2.322  23.206  -29.328 1.00 39.43  ? 395 HOH B O   1 
HETATM 3913 O  O   . HOH G 4 .   ? 9.194   31.276  -16.164 1.00 55.12  ? 396 HOH B O   1 
HETATM 3914 O  O   . HOH G 4 .   ? 26.006  15.244  -5.904  1.00 36.43  ? 397 HOH B O   1 
HETATM 3915 O  O   . HOH G 4 .   ? 7.673   33.447  -19.540 1.00 47.83  ? 398 HOH B O   1 
HETATM 3916 O  O   . HOH G 4 .   ? 14.432  10.974  -43.035 1.00 39.43  ? 399 HOH B O   1 
HETATM 3917 O  O   . HOH G 4 .   ? 17.705  30.083  -8.896  1.00 46.10  ? 400 HOH B O   1 
HETATM 3918 O  O   . HOH G 4 .   ? 3.463   24.738  -47.472 1.00 42.64  ? 401 HOH B O   1 
HETATM 3919 O  O   . HOH G 4 .   ? 8.114   18.987  -45.575 1.00 32.49  ? 402 HOH B O   1 
HETATM 3920 O  O   . HOH G 4 .   ? 6.143   9.111   -22.198 1.00 35.41  ? 403 HOH B O   1 
HETATM 3921 O  O   . HOH G 4 .   ? -2.821  33.184  -30.579 1.00 35.01  ? 404 HOH B O   1 
HETATM 3922 O  O   . HOH G 4 .   ? 13.259  4.919   -27.101 1.00 32.29  ? 405 HOH B O   1 
HETATM 3923 O  O   . HOH G 4 .   ? 23.802  17.000  -4.764  1.00 39.69  ? 406 HOH B O   1 
HETATM 3924 O  O   . HOH G 4 .   ? 14.202  5.413   -32.902 1.00 49.95  ? 407 HOH B O   1 
HETATM 3925 O  O   . HOH G 4 .   ? 13.526  25.715  -52.101 1.00 57.50  ? 408 HOH B O   1 
HETATM 3926 O  O   . HOH G 4 .   ? 17.676  18.531  -41.033 1.00 40.64  ? 409 HOH B O   1 
HETATM 3927 O  O   . HOH G 4 .   ? 20.757  23.987  -38.506 1.00 44.74  ? 410 HOH B O   1 
HETATM 3928 O  O   . HOH G 4 .   ? -1.315  14.483  -35.365 1.00 47.08  ? 411 HOH B O   1 
HETATM 3929 O  O   . HOH G 4 .   ? 16.115  24.226  -3.586  1.00 36.88  ? 412 HOH B O   1 
HETATM 3930 O  O   . HOH G 4 .   ? 14.867  35.156  -10.672 1.00 42.17  ? 413 HOH B O   1 
HETATM 3931 O  O   . HOH G 4 .   ? 11.830  37.026  -25.854 1.00 36.65  ? 414 HOH B O   1 
HETATM 3932 O  O   . HOH G 4 .   ? 25.798  23.071  -25.247 1.00 49.17  ? 415 HOH B O   1 
HETATM 3933 O  O   . HOH G 4 .   ? 37.852  13.767  -22.810 1.00 46.83  ? 416 HOH B O   1 
HETATM 3934 O  O   . HOH G 4 .   ? 26.114  10.186  -31.245 0.50 46.26  ? 417 HOH B O   1 
HETATM 3935 O  O   . HOH G 4 .   ? 25.109  7.297   -34.250 1.00 42.79  ? 418 HOH B O   1 
HETATM 3936 O  O   . HOH G 4 .   ? 11.018  12.449  -45.361 1.00 44.51  ? 419 HOH B O   1 
HETATM 3937 O  O   . HOH G 4 .   ? -0.031  14.236  -19.738 0.50 44.27  ? 420 HOH B O   1 
HETATM 3938 O  O   . HOH G 4 .   ? 16.356  16.106  -44.775 1.00 45.63  ? 421 HOH B O   1 
HETATM 3939 O  O   . HOH G 4 .   ? 2.867   21.858  -19.451 1.00 49.44  ? 422 HOH B O   1 
HETATM 3940 O  O   . HOH G 4 .   ? 34.042  28.963  -19.479 1.00 35.36  ? 423 HOH B O   1 
HETATM 3941 O  O   . HOH G 4 .   ? 4.963   20.073  -18.207 1.00 53.46  ? 424 HOH B O   1 
HETATM 3942 O  O   . HOH G 4 .   ? 10.010  16.264  -25.239 1.00 31.06  ? 425 HOH B O   1 
HETATM 3943 O  O   . HOH G 4 .   ? -5.278  21.774  -31.304 0.50 41.48  ? 426 HOH B O   1 
HETATM 3944 O  O   . HOH G 4 .   ? 32.720  9.542   -12.410 1.00 42.45  ? 427 HOH B O   1 
HETATM 3945 O  O   . HOH G 4 .   ? 10.927  5.334   -21.594 1.00 42.77  ? 428 HOH B O   1 
HETATM 3946 O  O   . HOH G 4 .   ? 2.422   11.579  -31.085 1.00 32.02  ? 429 HOH B O   1 
HETATM 3947 O  O   . HOH G 4 .   ? 24.059  6.424   -25.284 1.00 36.24  ? 430 HOH B O   1 
HETATM 3948 O  O   . HOH G 4 .   ? 32.672  11.790  -12.873 1.00 37.44  ? 431 HOH B O   1 
HETATM 3949 O  O   . HOH G 4 .   ? 7.542   17.050  -47.359 1.00 50.56  ? 432 HOH B O   1 
HETATM 3950 O  O   . HOH G 4 .   ? 17.957  17.460  -43.837 1.00 44.40  ? 433 HOH B O   1 
HETATM 3951 O  O   . HOH G 4 .   ? 11.510  30.914  -13.839 1.00 54.98  ? 434 HOH B O   1 
HETATM 3952 O  O   . HOH G 4 .   ? 2.330   34.282  -24.102 1.00 53.59  ? 435 HOH B O   1 
HETATM 3953 O  O   . HOH G 4 .   ? -2.434  26.620  -33.567 1.00 62.05  ? 436 HOH B O   1 
HETATM 3954 O  O   . HOH G 4 .   ? 37.712  11.915  -6.809  1.00 58.14  ? 437 HOH B O   1 
HETATM 3955 O  O   . HOH G 4 .   ? 24.324  7.404   -31.766 1.00 43.45  ? 438 HOH B O   1 
HETATM 3956 O  O   . HOH G 4 .   ? 14.753  5.012   -35.462 1.00 43.54  ? 439 HOH B O   1 
HETATM 3957 O  O   . HOH G 4 .   ? 3.503   21.586  -45.632 1.00 55.85  ? 440 HOH B O   1 
HETATM 3958 O  O   . HOH G 4 .   ? 3.676   33.866  -22.049 1.00 45.14  ? 441 HOH B O   1 
HETATM 3959 O  O   . HOH G 4 .   ? 25.885  21.045  -30.192 1.00 47.82  ? 442 HOH B O   1 
HETATM 3960 O  O   . HOH G 4 .   ? 11.489  3.404   -23.116 1.00 30.76  ? 443 HOH B O   1 
HETATM 3961 O  O   . HOH G 4 .   ? 8.844   9.240   -44.500 1.00 53.43  ? 444 HOH B O   1 
HETATM 3962 O  O   . HOH G 4 .   ? -0.268  24.789  -38.796 1.00 41.70  ? 445 HOH B O   1 
HETATM 3963 O  O   . HOH G 4 .   ? 7.685   36.929  -39.645 1.00 45.42  ? 446 HOH B O   1 
HETATM 3964 O  O   . HOH G 4 .   ? 25.113  25.231  -25.596 1.00 49.00  ? 447 HOH B O   1 
HETATM 3965 O  O   . HOH G 4 .   ? 16.062  13.887  -19.060 1.00 15.54  ? 448 HOH B O   1 
HETATM 3966 O  O   . HOH G 4 .   ? 24.270  14.434  -26.928 1.00 39.66  ? 449 HOH B O   1 
HETATM 3967 O  O   . HOH G 4 .   ? 33.459  27.417  -32.999 0.50 76.18  ? 450 HOH B O   1 
HETATM 3968 O  O   . HOH G 4 .   ? 30.870  36.672  -29.633 1.00 45.83  ? 451 HOH B O   1 
HETATM 3969 O  O   . HOH G 4 .   ? 29.060  36.485  -31.038 1.00 46.32  ? 452 HOH B O   1 
HETATM 3970 O  O   . HOH G 4 .   ? 10.854  21.995  -12.201 1.00 53.11  ? 453 HOH B O   1 
HETATM 3971 O  O   . HOH G 4 .   ? 32.201  39.826  -23.260 1.00 47.31  ? 454 HOH B O   1 
HETATM 3972 O  O   . HOH G 4 .   ? 6.953   5.073   -21.902 1.00 48.13  ? 455 HOH B O   1 
HETATM 3973 O  O   . HOH G 4 .   ? 8.795   8.704   -18.428 1.00 42.02  ? 456 HOH B O   1 
HETATM 3974 O  O   . HOH G 4 .   ? 8.042   25.155  -49.846 0.50 39.46  ? 457 HOH B O   1 
HETATM 3975 O  O   . HOH G 4 .   ? 22.277  36.726  -40.057 0.50 60.30  ? 458 HOH B O   1 
HETATM 3976 O  O   . HOH G 4 .   ? 25.857  31.432  -9.266  1.00 47.25  ? 459 HOH B O   1 
HETATM 3977 O  O   . HOH G 4 .   ? 30.172  18.693  -33.506 0.50 44.82  ? 460 HOH B O   1 
HETATM 3978 O  O   . HOH G 4 .   ? 26.081  38.927  -32.714 1.00 51.74  ? 461 HOH B O   1 
HETATM 3979 O  O   . HOH G 4 .   ? 30.881  37.434  -26.915 1.00 34.80  ? 462 HOH B O   1 
HETATM 3980 O  O   . HOH G 4 .   ? 32.376  37.536  -31.657 0.50 56.47  ? 463 HOH B O   1 
HETATM 3981 O  O   . HOH G 4 .   ? 1.335   11.562  -24.024 1.00 43.82  ? 464 HOH B O   1 
HETATM 3982 O  O   . HOH G 4 .   ? 12.488  26.866  -10.705 1.00 45.29  ? 465 HOH B O   1 
HETATM 3983 O  O   . HOH G 4 .   ? 10.817  34.811  -34.595 1.00 48.13  ? 466 HOH B O   1 
HETATM 3984 O  O   . HOH G 4 .   ? 7.630   37.979  -30.111 1.00 58.67  ? 467 HOH B O   1 
HETATM 3985 O  O   . HOH G 4 .   ? 26.658  36.490  -34.515 1.00 52.87  ? 468 HOH B O   1 
HETATM 3986 O  O   . HOH G 4 .   ? 37.727  35.165  -22.816 1.00 59.96  ? 469 HOH B O   1 
HETATM 3987 O  O   . HOH G 4 .   ? 8.828   28.843  -47.001 1.00 56.12  ? 470 HOH B O   1 
HETATM 3988 O  O   . HOH G 4 .   ? -0.560  15.736  -39.376 1.00 53.41  ? 471 HOH B O   1 
HETATM 3989 O  O   . HOH G 4 .   ? 17.847  11.774  -42.481 1.00 54.85  ? 472 HOH B O   1 
HETATM 3990 O  O   . HOH G 4 .   ? 10.730  28.312  -10.397 0.50 43.84  ? 473 HOH B O   1 
HETATM 3991 O  O   . HOH G 4 .   ? 5.523   6.940   -21.368 0.50 46.65  ? 474 HOH B O   1 
HETATM 3992 O  O   . HOH G 4 .   ? -1.889  29.582  -42.333 1.00 46.48  ? 475 HOH B O   1 
HETATM 3993 O  O   . HOH G 4 .   ? 3.261   9.471   -23.687 0.50 36.75  ? 476 HOH B O   1 
HETATM 3994 O  O   . HOH G 4 .   ? 22.281  38.452  -36.124 0.50 46.84  ? 477 HOH B O   1 
HETATM 3995 O  O   . HOH G 4 .   ? 24.593  5.235   -35.127 1.00 55.29  ? 478 HOH B O   1 
HETATM 3996 O  O   . HOH G 4 .   ? 7.885   28.781  -13.428 0.50 48.32  ? 479 HOH B O   1 
HETATM 3997 O  O   . HOH G 4 .   ? 28.346  21.221  -30.819 1.00 65.86  ? 480 HOH B O   1 
HETATM 3998 O  O   . HOH G 4 .   ? 16.274  5.955   -32.075 0.50 44.82  ? 481 HOH B O   1 
HETATM 3999 O  O   . HOH G 4 .   ? 21.311  41.081  -27.485 0.50 43.57  ? 482 HOH B O   1 
HETATM 4000 O  O   . HOH G 4 .   ? 5.454   26.664  -48.922 1.00 58.73  ? 483 HOH B O   1 
HETATM 4001 O  O   . HOH G 4 .   ? 3.792   41.136  -22.338 1.00 112.29 ? 484 HOH B O   1 
HETATM 4002 O  O   . HOH G 4 .   ? 26.649  14.446  -30.440 1.00 95.68  ? 485 HOH B O   1 
HETATM 4003 O  O   . HOH G 4 .   ? 1.203   14.272  -39.566 1.00 73.80  ? 486 HOH B O   1 
HETATM 4004 O  O   . HOH G 4 .   ? -1.827  20.746  -38.794 1.00 65.34  ? 487 HOH B O   1 
HETATM 4005 O  O   . HOH G 4 .   ? 0.334   9.700   -38.927 1.00 54.40  ? 488 HOH B O   1 
HETATM 4006 O  O   . HOH G 4 .   ? 23.269  4.312   -38.582 1.00 70.87  ? 489 HOH B O   1 
HETATM 4007 O  O   . HOH G 4 .   ? 8.392   38.173  -19.870 1.00 69.81  ? 490 HOH B O   1 
HETATM 4008 O  O   . HOH G 4 .   ? 12.387  36.041  -43.778 1.00 63.51  ? 491 HOH B O   1 
HETATM 4009 O  O   . HOH G 4 .   ? 37.894  42.091  -16.623 1.00 112.02 ? 492 HOH B O   1 
HETATM 4010 O  O   . HOH G 4 .   ? -2.540  27.184  -40.717 1.00 69.94  ? 493 HOH B O   1 
HETATM 4011 O  O   . HOH G 4 .   ? 40.322  28.618  -18.620 1.00 65.34  ? 494 HOH B O   1 
HETATM 4012 O  O   . HOH G 4 .   ? 35.538  31.513  -15.075 1.00 54.18  ? 495 HOH B O   1 
HETATM 4013 O  O   . HOH G 4 .   ? 19.329  31.496  -1.697  1.00 54.84  ? 496 HOH B O   1 
HETATM 4014 O  O   . HOH G 4 .   ? 5.815   13.443  -46.044 1.00 50.97  ? 497 HOH B O   1 
HETATM 4015 O  O   . HOH G 4 .   ? 33.803  28.684  -22.753 1.00 50.54  ? 498 HOH B O   1 
HETATM 4016 O  O   . HOH G 4 .   ? 5.684   37.031  -22.509 1.00 59.06  ? 499 HOH B O   1 
HETATM 4017 O  O   . HOH G 4 .   ? 3.097   39.192  -23.368 1.00 113.38 ? 500 HOH B O   1 
HETATM 4018 O  O   . HOH G 4 .   ? 0.034   17.905  -38.744 1.00 48.13  ? 501 HOH B O   1 
HETATM 4019 O  O   . HOH G 4 .   ? -0.779  28.980  -20.216 1.00 67.93  ? 502 HOH B O   1 
HETATM 4020 O  O   . HOH G 4 .   ? 27.022  12.192  -30.594 1.00 95.42  ? 503 HOH B O   1 
HETATM 4021 O  O   . HOH G 4 .   ? 8.743   14.768  -20.841 1.00 60.90  ? 504 HOH B O   1 
HETATM 4022 O  O   . HOH G 4 .   ? 14.252  7.743   -41.633 1.00 79.43  ? 505 HOH B O   1 
HETATM 4023 O  O   . HOH G 4 .   ? 8.612   20.179  -13.251 1.00 63.02  ? 506 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . PRO A 10  ? 0.7944 0.5046 0.9532 0.1428  -0.1471 -0.1865 10  PRO A N   
2    C  CA  . PRO A 10  ? 0.7561 0.4896 0.8666 0.1179  -0.0857 -0.1443 10  PRO A CA  
3    C  C   . PRO A 10  ? 0.7486 0.4251 0.6446 0.0488  -0.0224 -0.0642 10  PRO A C   
4    O  O   . PRO A 10  ? 0.8502 0.4867 0.5416 -0.1023 0.0306  0.0013  10  PRO A O   
5    C  CB  . PRO A 10  ? 0.7533 0.5818 0.8944 0.1076  -0.0654 -0.1564 10  PRO A CB  
6    C  CG  . PRO A 10  ? 0.7909 0.5877 0.9414 0.1417  -0.0191 -0.2145 10  PRO A CG  
7    C  CD  . PRO A 10  ? 0.8142 0.5754 0.9443 0.1459  -0.0330 -0.2883 10  PRO A CD  
8    N  N   . GLN A 11  ? 0.6306 0.4810 0.5390 0.0643  0.1833  0.0129  11  GLN A N   
9    C  CA  . GLN A 11  ? 0.5879 0.5191 0.4929 0.0548  0.1769  -0.0663 11  GLN A CA  
10   C  C   . GLN A 11  ? 0.6504 0.4422 0.4813 0.0202  0.1257  -0.0739 11  GLN A C   
11   O  O   . GLN A 11  ? 0.6988 0.4580 0.5013 -0.0508 0.1169  -0.1127 11  GLN A O   
12   C  CB  . GLN A 11  ? 0.7036 0.5969 0.5520 0.1377  0.2172  -0.1050 11  GLN A CB  
13   C  CG  . GLN A 11  ? 0.9119 0.6949 0.7368 0.2888  0.1094  -0.1608 11  GLN A CG  
14   C  CD  . GLN A 11  ? 1.0270 0.8072 0.8477 0.3994  0.0775  -0.2519 11  GLN A CD  
15   O  OE1 . GLN A 11  ? 1.2985 1.0596 0.9817 0.2945  -0.0631 -0.4243 11  GLN A OE1 
16   N  NE2 . GLN A 11  ? 1.2275 0.9217 1.0807 0.5976  0.2438  -0.0720 11  GLN A NE2 
17   N  N   . ASP A 12  ? 0.5791 0.3444 0.4037 0.1135  0.0961  -0.0381 12  ASP A N   
18   C  CA  . ASP A 12  ? 0.5831 0.3154 0.3686 0.1225  0.0506  -0.0553 12  ASP A CA  
19   C  C   . ASP A 12  ? 0.5130 0.2560 0.3525 0.0813  0.0106  -0.0362 12  ASP A C   
20   O  O   . ASP A 12  ? 0.5663 0.2692 0.3135 0.1111  0.0380  0.0122  12  ASP A O   
21   C  CB  . ASP A 12  ? 0.7413 0.2825 0.2888 0.0672  0.0466  -0.0677 12  ASP A CB  
22   C  CG  . ASP A 12  ? 0.9582 0.3135 0.4010 0.1781  -0.0305 -0.1094 12  ASP A CG  
23   O  OD1 . ASP A 12  ? 1.0076 0.5098 0.6584 0.2579  0.1162  -0.2336 12  ASP A OD1 
24   O  OD2 . ASP A 12  ? 1.1686 0.3477 0.7817 0.1538  -0.1656 -0.2670 12  ASP A OD2 
25   N  N   . LEU A 13  ? 0.4150 0.3014 0.3642 0.0382  0.0262  -0.0450 13  LEU A N   
26   C  CA  . LEU A 13  ? 0.4218 0.3187 0.3652 0.0430  0.0145  -0.0589 13  LEU A CA  
27   C  C   . LEU A 13  ? 0.4398 0.2808 0.3044 0.0353  0.0426  -0.0071 13  LEU A C   
28   O  O   . LEU A 13  ? 0.4336 0.2640 0.3188 0.0026  0.0939  -0.0720 13  LEU A O   
29   C  CB  . LEU A 13  ? 0.4164 0.4011 0.3125 0.0300  0.0682  -0.0123 13  LEU A CB  
30   C  CG  . LEU A 13  ? 0.4197 0.3786 0.2948 -0.0261 0.1128  0.0064  13  LEU A CG  
31   C  CD1 . LEU A 13  ? 0.5460 0.3372 0.4644 0.1328  0.2203  0.0685  13  LEU A CD1 
32   C  CD2 . LEU A 13  ? 0.6684 0.3627 0.2974 0.0591  0.0638  0.0025  13  LEU A CD2 
33   N  N   . SER A 14  ? 0.4613 0.2669 0.3657 0.0489  0.0261  0.0054  14  SER A N   
34   C  CA  . SER A 14  ? 0.4627 0.3047 0.3905 -0.0031 0.0092  0.0068  14  SER A CA  
35   C  C   . SER A 14  ? 0.4301 0.3042 0.3608 0.0665  0.0926  0.0150  14  SER A C   
36   O  O   . SER A 14  ? 0.4150 0.2963 0.5517 0.0422  0.1289  -0.0287 14  SER A O   
37   C  CB  . SER A 14  ? 0.4873 0.3000 0.4149 0.0127  -0.0067 0.0282  14  SER A CB  
38   O  OG  . SER A 14  ? 0.4939 0.2998 0.4434 -0.0166 -0.0051 0.0019  14  SER A OG  
39   N  N   . GLU A 15  ? 0.5902 0.3524 0.3450 0.0593  0.0662  -0.0298 15  GLU A N   
40   C  CA  . GLU A 15  ? 0.5013 0.4177 0.3289 0.0271  0.0526  -0.0461 15  GLU A CA  
41   C  C   . GLU A 15  ? 0.4718 0.4058 0.3219 0.0673  -0.0350 -0.0087 15  GLU A C   
42   O  O   . GLU A 15  ? 0.4750 0.4719 0.3564 0.0951  -0.0397 0.0046  15  GLU A O   
43   C  CB  . GLU A 15  ? 0.6872 0.3976 0.3255 0.0160  0.1432  0.0008  15  GLU A CB  
44   C  CG  . GLU A 15  ? 0.8333 0.4943 0.5730 -0.0735 0.0663  -0.1885 15  GLU A CG  
45   C  CD  . GLU A 15  ? 0.8548 0.6868 0.5928 -0.1077 -0.0237 -0.1895 15  GLU A CD  
46   O  OE1 . GLU A 15  ? 1.0053 0.8773 0.5387 0.2018  0.0475  -0.1049 15  GLU A OE1 
47   O  OE2 . GLU A 15  ? 0.9756 1.1330 0.9025 -0.2031 -0.2587 -0.0709 15  GLU A OE2 
48   N  N   . ALA A 16  ? 0.4333 0.3631 0.3417 0.0865  0.0449  -0.0345 16  ALA A N   
49   C  CA  . ALA A 16  ? 0.4421 0.3612 0.3866 0.0733  0.1003  0.0233  16  ALA A CA  
50   C  C   . ALA A 16  ? 0.3800 0.2912 0.3833 0.0384  0.0654  0.0083  16  ALA A C   
51   O  O   . ALA A 16  ? 0.3796 0.3150 0.4343 0.0537  0.0724  0.0474  16  ALA A O   
52   C  CB  . ALA A 16  ? 0.4350 0.2992 0.3398 0.0836  0.1187  0.0246  16  ALA A CB  
53   N  N   . LEU A 17  ? 0.3944 0.2891 0.3392 0.0786  0.0351  -0.0214 17  LEU A N   
54   C  CA  . LEU A 17  ? 0.3905 0.2271 0.3430 0.0761  0.0207  -0.0321 17  LEU A CA  
55   C  C   . LEU A 17  ? 0.3881 0.3205 0.3622 0.0841  0.0246  -0.0476 17  LEU A C   
56   O  O   . LEU A 17  ? 0.4226 0.3276 0.3184 0.1307  -0.0129 0.0047  17  LEU A O   
57   C  CB  . LEU A 17  ? 0.4215 0.2170 0.3413 0.0688  0.0388  -0.0305 17  LEU A CB  
58   C  CG  . LEU A 17  ? 0.4715 0.1903 0.3718 0.0548  -0.0182 -0.0050 17  LEU A CG  
59   C  CD1 . LEU A 17  ? 0.2962 0.2075 0.4349 -0.0071 0.0589  0.0594  17  LEU A CD1 
60   C  CD2 . LEU A 17  ? 0.5901 0.1939 0.4434 -0.0072 -0.0166 -0.0227 17  LEU A CD2 
61   N  N   . LYS A 18  ? 0.3937 0.3041 0.4633 0.0444  -0.0077 -0.0045 18  LYS A N   
62   C  CA  . LYS A 18  ? 0.4037 0.3264 0.4710 0.0338  -0.0217 0.0577  18  LYS A CA  
63   C  C   . LYS A 18  ? 0.4508 0.3238 0.4266 0.0720  0.0123  0.0336  18  LYS A C   
64   O  O   . LYS A 18  ? 0.4571 0.3350 0.3297 0.0789  -0.0231 -0.0029 18  LYS A O   
65   C  CB  . LYS A 18  ? 0.4356 0.3343 0.5112 0.0108  -0.0745 0.0614  18  LYS A CB  
66   C  CG  . LYS A 18  ? 0.5256 0.3547 0.6192 0.0328  -0.1909 0.0868  18  LYS A CG  
67   C  CD  . LYS A 18  ? 0.4861 0.4626 0.7321 -0.0455 -0.1697 0.0583  18  LYS A CD  
68   C  CE  . LYS A 18  ? 0.5431 0.4911 0.8594 -0.0055 -0.2784 0.0524  18  LYS A CE  
69   N  NZ  . LYS A 18  ? 0.7297 0.6422 1.1484 -0.2399 -0.3089 0.0601  18  LYS A NZ  
70   N  N   . GLU A 19  ? 0.4969 0.3551 0.4318 0.0971  0.0426  0.0309  19  GLU A N   
71   C  CA  . GLU A 19  ? 0.4934 0.3590 0.3480 0.1443  0.0470  -0.0215 19  GLU A CA  
72   C  C   . GLU A 19  ? 0.4263 0.3391 0.4566 0.1272  0.0184  -0.0070 19  GLU A C   
73   O  O   . GLU A 19  ? 0.6862 0.3795 0.4134 0.2218  -0.1329 -0.0316 19  GLU A O   
74   C  CB  . GLU A 19  ? 0.6082 0.4564 0.4536 0.1612  0.1654  0.0043  19  GLU A CB  
75   C  CG  . GLU A 19  ? 0.7726 0.6017 0.6299 0.0604  0.2201  0.1301  19  GLU A CG  
76   C  CD  . GLU A 19  ? 0.9825 0.7315 0.5550 0.1546  0.1538  0.2723  19  GLU A CD  
77   O  OE1 . GLU A 19  ? 1.4219 0.8633 0.7181 -0.0410 -0.1148 0.4247  19  GLU A OE1 
78   O  OE2 . GLU A 19  ? 1.0329 1.0017 0.5285 0.3853  0.1800  0.1636  19  GLU A OE2 
79   N  N   . ALA A 20  ? 0.4409 0.3556 0.4167 0.1059  0.0213  0.0253  20  ALA A N   
80   C  CA  . ALA A 20  ? 0.4222 0.3279 0.4131 0.1485  -0.0432 0.0509  20  ALA A CA  
81   C  C   . ALA A 20  ? 0.3586 0.2810 0.3995 0.0798  -0.0594 0.0402  20  ALA A C   
82   O  O   . ALA A 20  ? 0.4759 0.2715 0.4254 0.0829  0.0691  0.0840  20  ALA A O   
83   C  CB  . ALA A 20  ? 0.3789 0.3371 0.4125 0.1281  -0.0032 0.0816  20  ALA A CB  
84   N  N   . THR A 21  ? 0.4310 0.2446 0.3609 0.0271  -0.0825 -0.0073 21  THR A N   
85   C  CA  . THR A 21  ? 0.4380 0.2878 0.3433 0.0549  -0.0613 0.0661  21  THR A CA  
86   C  C   . THR A 21  ? 0.4393 0.3115 0.3230 0.0393  -0.0594 0.0164  21  THR A C   
87   O  O   . THR A 21  ? 0.4418 0.2715 0.2938 0.0631  -0.0677 0.0485  21  THR A O   
88   C  CB  . THR A 21  ? 0.4071 0.3212 0.4212 0.0143  -0.0517 0.1491  21  THR A CB  
89   O  OG1 . THR A 21  ? 0.2877 0.3298 0.3501 0.0310  -0.0199 0.1057  21  THR A OG1 
90   C  CG2 . THR A 21  ? 0.4407 0.3259 0.2680 0.0288  -0.0405 0.0172  21  THR A CG2 
91   N  N   . LYS A 22  ? 0.4444 0.3489 0.3081 0.1188  -0.0537 0.0441  22  LYS A N   
92   C  CA  . LYS A 22  ? 0.4732 0.3504 0.3121 0.1112  -0.0874 0.0467  22  LYS A CA  
93   C  C   . LYS A 22  ? 0.4178 0.3589 0.3363 0.0970  -0.0639 0.0462  22  LYS A C   
94   O  O   . LYS A 22  ? 0.4359 0.3629 0.3429 0.0585  -0.0410 0.0290  22  LYS A O   
95   C  CB  . LYS A 22  ? 0.6738 0.4482 0.3549 0.0375  -0.1288 -0.0757 22  LYS A CB  
96   C  CG  . LYS A 22  ? 0.8141 0.7648 0.5030 -0.1429 -0.2541 -0.0020 22  LYS A CG  
97   C  CD  . LYS A 22  ? 1.0051 0.9489 0.5265 -0.2031 -0.3733 -0.0411 22  LYS A CD  
98   C  CE  . LYS A 22  ? 1.0470 1.0418 0.6919 -0.1916 -0.4645 -0.0786 22  LYS A CE  
99   N  NZ  . LYS A 22  ? 1.0891 1.0871 0.7407 -0.2217 -0.5500 -0.1833 22  LYS A NZ  
100  N  N   . GLU A 23  ? 0.3430 0.3512 0.3485 0.1080  -0.0832 0.0192  23  GLU A N   
101  C  CA  . GLU A 23  ? 0.4046 0.3707 0.3556 0.1502  -0.0420 0.1068  23  GLU A CA  
102  C  C   . GLU A 23  ? 0.4282 0.3034 0.3895 0.1362  -0.0759 0.0316  23  GLU A C   
103  O  O   . GLU A 23  ? 0.4184 0.2942 0.3659 0.1239  -0.0739 0.0425  23  GLU A O   
104  C  CB  . GLU A 23  ? 0.4999 0.4169 0.5034 0.0713  -0.0117 0.1430  23  GLU A CB  
105  C  CG  . GLU A 23  ? 0.7242 0.5531 0.7916 -0.1789 -0.0242 -0.0132 23  GLU A CG  
106  C  CD  . GLU A 23  ? 0.7631 0.8434 1.0175 -0.1010 -0.1172 -0.1713 23  GLU A CD  
107  O  OE1 . GLU A 23  ? 1.1403 1.3510 1.0648 -0.2630 -0.2991 -0.3241 23  GLU A OE1 
108  O  OE2 . GLU A 23  ? 0.9035 1.1373 1.5326 0.2030  -0.0666 -0.1607 23  GLU A OE2 
109  N  N   . VAL A 24  ? 0.3688 0.2949 0.3484 0.0753  -0.0225 0.1064  24  VAL A N   
110  C  CA  . VAL A 24  ? 0.3422 0.2575 0.3615 0.0978  -0.0200 0.0998  24  VAL A CA  
111  C  C   . VAL A 24  ? 0.3608 0.2420 0.3404 0.0728  0.0053  0.0267  24  VAL A C   
112  O  O   . VAL A 24  ? 0.3331 0.2460 0.2957 0.0863  -0.0352 0.0351  24  VAL A O   
113  C  CB  . VAL A 24  ? 0.3044 0.3293 0.3500 0.1013  0.0045  0.0644  24  VAL A CB  
114  C  CG1 . VAL A 24  ? 0.4846 0.3556 0.3662 0.0065  -0.0643 0.0382  24  VAL A CG1 
115  C  CG2 . VAL A 24  ? 0.4330 0.3560 0.2619 0.1668  -0.0767 0.0348  24  VAL A CG2 
116  N  N   . HIS A 25  ? 0.3219 0.2560 0.3251 0.0927  -0.0691 0.0093  25  HIS A N   
117  C  CA  . HIS A 25  ? 0.3276 0.2456 0.3508 0.0769  -0.0797 -0.0033 25  HIS A CA  
118  C  C   . HIS A 25  ? 0.3324 0.2158 0.3169 0.0822  -0.0513 0.0176  25  HIS A C   
119  O  O   . HIS A 25  ? 0.3070 0.2166 0.3544 0.0300  -0.0579 0.0118  25  HIS A O   
120  C  CB  . HIS A 25  ? 0.3401 0.2423 0.3108 0.1037  -0.0437 0.0283  25  HIS A CB  
121  C  CG  . HIS A 25  ? 0.3880 0.2823 0.3845 -0.0045 -0.1478 0.0424  25  HIS A CG  
122  N  ND1 . HIS A 25  ? 0.3730 0.2340 0.3850 0.0477  -0.1220 -0.0015 25  HIS A ND1 
123  C  CD2 . HIS A 25  ? 0.3200 0.2201 0.3957 -0.0151 -0.1246 0.0184  25  HIS A CD2 
124  C  CE1 . HIS A 25  ? 0.3375 0.2139 0.4051 0.0397  -0.1751 0.0073  25  HIS A CE1 
125  N  NE2 . HIS A 25  ? 0.2740 0.2891 0.3149 -0.0080 -0.1564 0.0007  25  HIS A NE2 
126  N  N   . THR A 26  ? 0.4102 0.2730 0.3590 0.1077  -0.0492 0.0785  26  THR A N   
127  C  CA  . THR A 26  ? 0.4475 0.2905 0.3245 0.1406  -0.1113 -0.0222 26  THR A CA  
128  C  C   . THR A 26  ? 0.3716 0.2769 0.3172 0.0654  -0.0720 -0.0215 26  THR A C   
129  O  O   . THR A 26  ? 0.3592 0.1862 0.4002 0.0444  -0.0755 -0.0260 26  THR A O   
130  C  CB  . THR A 26  ? 0.4879 0.4515 0.2991 0.1713  -0.1366 -0.0415 26  THR A CB  
131  O  OG1 . THR A 26  ? 0.4858 0.4448 0.3184 0.1929  -0.0828 -0.0183 26  THR A OG1 
132  C  CG2 . THR A 26  ? 0.6145 0.5501 0.4414 0.3417  -0.1251 0.0808  26  THR A CG2 
133  N  N   . GLN A 27  ? 0.3532 0.2385 0.3425 0.0579  -0.0720 0.0531  27  GLN A N   
134  C  CA  . GLN A 27  ? 0.3724 0.2436 0.3654 0.0617  -0.1413 0.0295  27  GLN A CA  
135  C  C   . GLN A 27  ? 0.4152 0.2253 0.3361 0.0552  -0.1337 -0.0175 27  GLN A C   
136  O  O   . GLN A 27  ? 0.3457 0.1943 0.4865 0.0028  -0.0693 0.0114  27  GLN A O   
137  C  CB  . GLN A 27  ? 0.4287 0.3045 0.4569 -0.0072 -0.1788 0.0654  27  GLN A CB  
138  C  CG  . GLN A 27  ? 0.5106 0.3698 0.5938 -0.0647 -0.1508 -0.0231 27  GLN A CG  
139  C  CD  . GLN A 27  ? 0.5562 0.3876 0.6758 -0.1131 -0.1999 0.0357  27  GLN A CD  
140  O  OE1 . GLN A 27  ? 0.5074 0.3204 0.7966 -0.1058 -0.1577 0.0762  27  GLN A OE1 
141  N  NE2 . GLN A 27  ? 0.7598 0.2549 0.7107 -0.1903 -0.1802 0.0923  27  GLN A NE2 
142  N  N   . ALA A 28  ? 0.3055 0.2472 0.3536 0.0272  -0.1328 0.0210  28  ALA A N   
143  C  CA  . ALA A 28  ? 0.3459 0.2370 0.3595 -0.0153 -0.1169 -0.0016 28  ALA A CA  
144  C  C   . ALA A 28  ? 0.3266 0.2410 0.3617 0.0193  -0.0970 -0.0194 28  ALA A C   
145  O  O   . ALA A 28  ? 0.3613 0.3665 0.3872 0.0335  -0.0634 -0.0107 28  ALA A O   
146  C  CB  . ALA A 28  ? 0.2942 0.2394 0.3680 -0.0497 -0.0864 0.0549  28  ALA A CB  
147  N  N   . GLU A 29  ? 0.3448 0.2596 0.3659 -0.0035 -0.1344 -0.0134 29  GLU A N   
148  C  CA  . GLU A 29  ? 0.3407 0.2508 0.4280 -0.0145 -0.1076 -0.0222 29  GLU A CA  
149  C  C   . GLU A 29  ? 0.2857 0.2656 0.4952 -0.0159 -0.0040 -0.0057 29  GLU A C   
150  O  O   . GLU A 29  ? 0.2914 0.3271 0.5615 -0.0593 -0.0168 -0.0181 29  GLU A O   
151  C  CB  . GLU A 29  ? 0.4020 0.2539 0.4967 0.0206  -0.2014 -0.0705 29  GLU A CB  
152  C  CG  . GLU A 29  ? 0.5135 0.2864 0.4639 0.0827  -0.2202 -0.0605 29  GLU A CG  
153  C  CD  . GLU A 29  ? 0.5197 0.2946 0.4940 0.0419  -0.2187 -0.1053 29  GLU A CD  
154  O  OE1 . GLU A 29  ? 0.4942 0.3931 0.5705 0.0955  -0.2174 -0.2109 29  GLU A OE1 
155  O  OE2 . GLU A 29  ? 0.5026 0.3715 0.4199 0.0615  -0.2537 -0.0697 29  GLU A OE2 
156  N  N   . ASN A 30  ? 0.2687 0.2615 0.4363 0.0139  0.0446  0.0043  30  ASN A N   
157  C  CA  . ASN A 30  ? 0.2923 0.2442 0.4509 -0.0042 -0.1291 -0.0740 30  ASN A CA  
158  C  C   . ASN A 30  ? 0.4097 0.2563 0.4382 0.0661  -0.1342 -0.0620 30  ASN A C   
159  O  O   . ASN A 30  ? 0.3715 0.2869 0.5321 0.0642  -0.1656 -0.1180 30  ASN A O   
160  C  CB  . ASN A 30  ? 0.2842 0.1973 0.4903 0.0985  -0.0834 -0.0446 30  ASN A CB  
161  C  CG  . ASN A 30  ? 0.3111 0.1988 0.4758 0.0539  -0.0748 -0.0216 30  ASN A CG  
162  O  OD1 . ASN A 30  ? 0.3440 0.2764 0.4937 -0.0032 -0.0563 -0.0463 30  ASN A OD1 
163  N  ND2 . ASN A 30  ? 0.2488 0.2978 0.4692 0.0439  -0.1218 0.0264  30  ASN A ND2 
164  N  N   . ALA A 31  ? 0.3889 0.3004 0.4165 0.0437  -0.1133 -0.0398 31  ALA A N   
165  C  CA  . ALA A 31  ? 0.3119 0.3140 0.4585 0.0237  -0.1407 -0.0747 31  ALA A CA  
166  C  C   . ALA A 31  ? 0.3371 0.3661 0.4685 0.0674  -0.1048 -0.0414 31  ALA A C   
167  O  O   . ALA A 31  ? 0.3415 0.4894 0.3701 -0.0303 -0.0819 -0.1173 31  ALA A O   
168  C  CB  . ALA A 31  ? 0.3433 0.4951 0.5935 -0.0786 -0.2607 -0.0433 31  ALA A CB  
169  N  N   . GLU A 32  ? 0.3815 0.4459 0.4650 0.1401  -0.1584 -0.0856 32  GLU A N   
170  C  CA  . GLU A 32  ? 0.4099 0.5497 0.3995 0.1586  -0.1261 -0.0972 32  GLU A CA  
171  C  C   . GLU A 32  ? 0.4231 0.5734 0.3697 0.1614  -0.1224 -0.0994 32  GLU A C   
172  O  O   . GLU A 32  ? 0.4268 0.7523 0.3298 0.0954  -0.1836 0.0465  32  GLU A O   
173  C  CB  . GLU A 32  ? 0.4156 0.5580 0.4298 0.2158  -0.1953 -0.1053 32  GLU A CB  
174  C  CG  . GLU A 32  ? 0.4502 0.6224 0.4074 0.2807  -0.1816 -0.0509 32  GLU A CG  
175  C  CD  . GLU A 32  ? 0.5817 0.6314 0.4935 0.3806  -0.2048 -0.0666 32  GLU A CD  
176  O  OE1 . GLU A 32  ? 0.6854 0.6000 0.4451 0.3178  -0.1490 -0.1598 32  GLU A OE1 
177  O  OE2 . GLU A 32  ? 0.6374 0.8067 0.6958 0.4785  -0.1832 -0.1156 32  GLU A OE2 
178  N  N   . PHE A 33  ? 0.4060 0.4798 0.3592 0.1203  -0.1234 -0.1373 33  PHE A N   
179  C  CA  . PHE A 33  ? 0.2874 0.5255 0.3784 0.0562  -0.1707 -0.1138 33  PHE A CA  
180  C  C   . PHE A 33  ? 0.3072 0.5270 0.3532 0.0022  -0.1064 -0.1043 33  PHE A C   
181  O  O   . PHE A 33  ? 0.3222 0.5872 0.3616 -0.0276 -0.0488 -0.1469 33  PHE A O   
182  C  CB  . PHE A 33  ? 0.3151 0.6382 0.3433 0.0633  -0.1693 -0.1317 33  PHE A CB  
183  C  CG  . PHE A 33  ? 0.3367 0.7995 0.3723 0.1163  -0.1300 -0.0450 33  PHE A CG  
184  C  CD1 . PHE A 33  ? 0.4090 0.8408 0.3727 0.1425  -0.1173 -0.0639 33  PHE A CD1 
185  C  CD2 . PHE A 33  ? 0.4060 0.8195 0.3896 0.1559  -0.0014 0.0602  33  PHE A CD2 
186  C  CE1 . PHE A 33  ? 0.4854 0.8860 0.3305 0.2098  -0.1092 -0.0582 33  PHE A CE1 
187  C  CE2 . PHE A 33  ? 0.4330 0.9038 0.3458 0.1922  0.0569  0.0703  33  PHE A CE2 
188  C  CZ  . PHE A 33  ? 0.4815 0.9386 0.2499 0.2678  -0.0566 -0.0233 33  PHE A CZ  
189  N  N   . MET A 34  ? 0.3170 0.5050 0.3148 -0.0615 -0.1029 -0.0999 34  MET A N   
190  C  CA  . MET A 34  ? 0.4160 0.4926 0.3455 -0.0590 -0.0770 -0.1063 34  MET A CA  
191  C  C   . MET A 34  ? 0.4490 0.4646 0.4456 -0.1276 -0.1455 -0.1377 34  MET A C   
192  O  O   . MET A 34  ? 0.4955 0.4993 0.4002 -0.1656 0.0177  -0.2385 34  MET A O   
193  C  CB  . MET A 34  ? 0.4255 0.5029 0.4409 -0.1039 -0.0457 -0.1866 34  MET A CB  
194  C  CG  . MET A 34  ? 0.3636 0.5592 0.4930 -0.1215 -0.0427 -0.1776 34  MET A CG  
195  S  SD  . MET A 34  ? 0.4244 0.6627 0.5982 -0.1311 -0.0847 -0.0306 34  MET A SD  
196  C  CE  . MET A 34  ? 0.8489 1.0079 0.3761 -0.3442 -0.2493 -0.0496 34  MET A CE  
197  N  N   . ARG A 35  ? 0.4323 0.5070 0.4488 -0.0868 -0.1866 -0.1373 35  ARG A N   
198  C  CA  . ARG A 35  ? 0.3828 0.6380 0.4719 -0.1077 -0.1542 -0.1237 35  ARG A CA  
199  C  C   . ARG A 35  ? 0.4131 0.6611 0.5194 -0.0587 -0.1117 -0.0752 35  ARG A C   
200  O  O   . ARG A 35  ? 0.5029 0.7004 0.3643 -0.1638 -0.1434 0.0792  35  ARG A O   
201  C  CB  . ARG A 35  ? 0.3735 0.7314 0.4479 -0.0573 -0.1491 -0.0548 35  ARG A CB  
202  C  CG  . ARG A 35  ? 0.3878 0.7740 0.4507 0.0383  -0.1167 -0.0134 35  ARG A CG  
203  C  CD  . ARG A 35  ? 0.4307 0.8465 0.4862 0.1189  -0.0545 0.0386  35  ARG A CD  
204  N  NE  . ARG A 35  ? 0.5371 0.9069 0.4833 0.2297  -0.0542 0.0556  35  ARG A NE  
205  C  CZ  . ARG A 35  ? 0.5283 0.7966 0.4975 0.3075  -0.0332 0.0723  35  ARG A CZ  
206  N  NH1 . ARG A 35  ? 0.5631 0.7413 0.4796 0.2501  0.0183  0.1619  35  ARG A NH1 
207  N  NH2 . ARG A 35  ? 0.7211 0.7521 0.6229 0.4081  0.0893  0.1974  35  ARG A NH2 
208  N  N   . ASN A 36  ? 0.3579 0.6916 0.4397 0.0047  -0.1773 -0.0051 36  ASN A N   
209  C  CA  . ASN A 36  ? 0.3609 0.6932 0.4395 -0.0671 -0.1889 -0.0492 36  ASN A CA  
210  C  C   . ASN A 36  ? 0.4201 0.7089 0.4934 -0.0793 -0.2114 -0.0160 36  ASN A C   
211  O  O   . ASN A 36  ? 0.4139 0.6306 0.5586 -0.0464 -0.1797 -0.1177 36  ASN A O   
212  C  CB  . ASN A 36  ? 0.3802 0.7710 0.4859 0.0249  -0.1829 -0.0996 36  ASN A CB  
213  C  CG  . ASN A 36  ? 0.5468 0.7440 0.6027 0.0212  -0.2086 -0.1356 36  ASN A CG  
214  O  OD1 . ASN A 36  ? 0.6133 0.7953 0.6598 0.1944  -0.1606 -0.2912 36  ASN A OD1 
215  N  ND2 . ASN A 36  ? 0.7520 0.6761 0.8254 0.1639  -0.4846 -0.1239 36  ASN A ND2 
216  N  N   . PHE A 37  ? 0.4099 0.6464 0.4566 -0.0301 -0.1559 -0.1173 37  PHE A N   
217  C  CA  . PHE A 37  ? 0.3639 0.6155 0.4966 -0.0193 -0.0531 -0.1585 37  PHE A CA  
218  C  C   . PHE A 37  ? 0.5080 0.6313 0.4290 -0.1357 -0.1107 -0.0507 37  PHE A C   
219  O  O   . PHE A 37  ? 0.5532 0.7238 0.4334 -0.1998 -0.0019 -0.1276 37  PHE A O   
220  C  CB  . PHE A 37  ? 0.3416 0.5040 0.5464 -0.0584 -0.0470 -0.1624 37  PHE A CB  
221  C  CG  . PHE A 37  ? 0.3543 0.6222 0.7288 -0.0811 -0.0917 -0.0225 37  PHE A CG  
222  C  CD1 . PHE A 37  ? 0.4481 0.6039 0.8377 -0.0917 -0.1530 0.0524  37  PHE A CD1 
223  C  CD2 . PHE A 37  ? 0.5740 0.6907 0.6982 -0.0939 -0.1605 0.0310  37  PHE A CD2 
224  C  CE1 . PHE A 37  ? 0.6148 0.6771 0.7722 -0.1182 -0.1896 0.0837  37  PHE A CE1 
225  C  CE2 . PHE A 37  ? 0.7057 0.6936 0.6871 -0.1966 -0.1341 0.1117  37  PHE A CE2 
226  C  CZ  . PHE A 37  ? 0.6975 0.7019 0.7006 -0.1854 -0.1472 0.0744  37  PHE A CZ  
227  N  N   . GLN A 38  ? 0.5666 0.4605 0.4419 -0.1251 -0.1036 -0.0279 38  GLN A N   
228  C  CA  . GLN A 38  ? 0.5301 0.4594 0.4465 0.0440  -0.1211 -0.0752 38  GLN A CA  
229  C  C   . GLN A 38  ? 0.5112 0.4178 0.4785 -0.0166 -0.1133 -0.0537 38  GLN A C   
230  O  O   . GLN A 38  ? 0.6255 0.4375 0.4871 -0.0835 -0.1535 -0.0080 38  GLN A O   
231  C  CB  . GLN A 38  ? 0.5203 0.4870 0.4792 -0.0560 -0.0984 -0.1481 38  GLN A CB  
232  C  CG  . GLN A 38  ? 0.5673 0.5070 0.4965 0.0281  -0.0727 -0.0948 38  GLN A CG  
233  C  CD  . GLN A 38  ? 0.5766 0.4866 0.5020 0.0025  -0.0307 -0.1570 38  GLN A CD  
234  O  OE1 . GLN A 38  ? 0.7305 0.4197 0.4382 0.0939  -0.1280 -0.0795 38  GLN A OE1 
235  N  NE2 . GLN A 38  ? 0.5018 0.5478 0.6393 -0.0308 0.0510  -0.2348 38  GLN A NE2 
236  N  N   . LYS A 39  ? 0.5006 0.4424 0.4863 0.0161  -0.1321 -0.0272 39  LYS A N   
237  C  CA  . LYS A 39  ? 0.5175 0.4255 0.3869 -0.0096 -0.1762 0.0951  39  LYS A CA  
238  C  C   . LYS A 39  ? 0.5571 0.5446 0.4834 -0.0354 -0.1149 0.1319  39  LYS A C   
239  O  O   . LYS A 39  ? 0.6706 0.4656 0.6315 0.1863  0.0650  0.2319  39  LYS A O   
240  C  CB  . LYS A 39  ? 0.5519 0.4153 0.4805 -0.0284 -0.2723 0.0697  39  LYS A CB  
241  C  CG  . LYS A 39  ? 0.5760 0.3274 0.5145 0.0033  -0.2480 0.0792  39  LYS A CG  
242  C  CD  . LYS A 39  ? 0.5711 0.4015 0.5983 0.1154  -0.1798 0.1155  39  LYS A CD  
243  C  CE  . LYS A 39  ? 0.6700 0.4348 0.6357 0.1135  -0.1835 0.1879  39  LYS A CE  
244  N  NZ  . LYS A 39  ? 0.8307 0.6543 0.6823 0.2060  -0.0044 0.0551  39  LYS A NZ  
245  N  N   . GLY A 40  ? 0.5032 0.6760 0.4222 -0.0088 -0.0324 0.1875  40  GLY A N   
246  C  CA  . GLY A 40  ? 0.4960 0.7569 0.4038 -0.1398 -0.0501 0.1564  40  GLY A CA  
247  C  C   . GLY A 40  ? 0.4162 0.8520 0.4000 -0.1337 -0.0867 0.1068  40  GLY A C   
248  O  O   . GLY A 40  ? 0.4238 1.0182 0.3726 -0.1771 -0.0963 0.0895  40  GLY A O   
249  N  N   . GLN A 41  ? 0.3530 0.8310 0.4821 -0.0900 -0.1249 0.0617  41  GLN A N   
250  C  CA  . GLN A 41  ? 0.3927 0.9253 0.4966 -0.0278 -0.2066 0.0007  41  GLN A CA  
251  C  C   . GLN A 41  ? 0.5058 0.8325 0.5591 -0.1469 -0.2935 0.0958  41  GLN A C   
252  O  O   . GLN A 41  ? 0.7085 0.8334 0.9664 -0.2291 -0.5443 0.1846  41  GLN A O   
253  C  CB  . GLN A 41  ? 0.4469 0.9115 0.5919 0.0428  -0.3090 -0.0406 41  GLN A CB  
254  C  CG  . GLN A 41  ? 0.6043 0.9839 0.5909 0.0857  -0.3841 -0.0941 41  GLN A CG  
255  C  CD  . GLN A 41  ? 0.6787 0.9524 0.5415 0.1108  -0.4039 -0.1298 41  GLN A CD  
256  O  OE1 . GLN A 41  ? 0.8007 1.1551 0.5365 -0.1204 -0.3798 -0.1291 41  GLN A OE1 
257  N  NE2 . GLN A 41  ? 0.9403 1.0209 1.0051 0.3226  -0.2573 -0.1464 41  GLN A NE2 
258  N  N   . VAL A 42  ? 0.4657 0.8118 0.4526 -0.1360 -0.2132 0.0589  42  VAL A N   
259  C  CA  . VAL A 42  ? 0.3497 0.6246 0.4349 -0.0982 -0.1505 -0.0091 42  VAL A CA  
260  C  C   . VAL A 42  ? 0.2969 0.5353 0.4447 -0.0555 -0.1578 0.0047  42  VAL A C   
261  O  O   . VAL A 42  ? 0.3423 0.6133 0.5115 -0.1129 -0.1524 0.0215  42  VAL A O   
262  C  CB  . VAL A 42  ? 0.3718 0.6329 0.4518 -0.0806 -0.0686 -0.0165 42  VAL A CB  
263  C  CG1 . VAL A 42  ? 0.4984 0.6302 0.5247 -0.0444 0.1029  0.0153  42  VAL A CG1 
264  C  CG2 . VAL A 42  ? 0.6051 0.5911 0.5614 0.0386  -0.3109 0.0628  42  VAL A CG2 
265  N  N   . THR A 43  ? 0.3511 0.4338 0.4338 -0.0083 -0.1648 0.0297  43  THR A N   
266  C  CA  . THR A 43  ? 0.3317 0.3512 0.4534 0.0601  -0.1444 0.0162  43  THR A CA  
267  C  C   . THR A 43  ? 0.2840 0.2422 0.4641 0.0350  -0.0910 0.0392  43  THR A C   
268  O  O   . THR A 43  ? 0.2908 0.2292 0.3393 0.0252  -0.0924 -0.0292 43  THR A O   
269  C  CB  . THR A 43  ? 0.4116 0.3546 0.4907 0.1522  -0.2359 0.0219  43  THR A CB  
270  O  OG1 . THR A 43  ? 0.4902 0.2161 0.7065 0.0817  -0.2750 0.0671  43  THR A OG1 
271  C  CG2 . THR A 43  ? 0.5157 0.3482 0.5327 0.0293  -0.2172 0.1255  43  THR A CG2 
272  N  N   . ARG A 44  ? 0.2461 0.2196 0.4447 0.0004  -0.0921 -0.0117 44  ARG A N   
273  C  CA  . ARG A 44  ? 0.2582 0.2010 0.4209 -0.0297 -0.0874 0.0005  44  ARG A CA  
274  C  C   . ARG A 44  ? 0.2401 0.1778 0.3960 -0.0131 -0.0654 -0.0216 44  ARG A C   
275  O  O   . ARG A 44  ? 0.2455 0.1722 0.4710 -0.0171 -0.0868 0.0174  44  ARG A O   
276  C  CB  . ARG A 44  ? 0.3393 0.2870 0.4605 -0.1141 -0.0642 0.0174  44  ARG A CB  
277  C  CG  . ARG A 44  ? 0.4119 0.3189 0.4482 -0.1515 -0.0590 0.0017  44  ARG A CG  
278  C  CD  . ARG A 44  ? 0.4197 0.4267 0.6035 -0.1923 0.0804  0.0575  44  ARG A CD  
279  N  NE  . ARG A 44  ? 0.5401 0.4123 0.6819 -0.2341 0.1068  -0.0324 44  ARG A NE  
280  C  CZ  . ARG A 44  ? 0.6554 0.5673 0.8302 -0.3766 0.0425  0.1593  44  ARG A CZ  
281  N  NH1 . ARG A 44  ? 0.9198 0.9517 1.0789 -0.3264 -0.0411 0.4840  44  ARG A NH1 
282  N  NH2 . ARG A 44  ? 0.9001 0.7458 1.0014 -0.6184 0.0824  0.0653  44  ARG A NH2 
283  N  N   . ASP A 45  ? 0.2502 0.1985 0.4141 -0.0017 -0.0063 -0.0462 45  ASP A N   
284  C  CA  . ASP A 45  ? 0.2940 0.1652 0.3782 -0.0055 -0.0300 -0.0274 45  ASP A CA  
285  C  C   . ASP A 45  ? 0.2580 0.1368 0.3233 -0.0152 -0.0783 -0.0211 45  ASP A C   
286  O  O   . ASP A 45  ? 0.2636 0.2064 0.3570 -0.0148 -0.0917 -0.0217 45  ASP A O   
287  C  CB  . ASP A 45  ? 0.3520 0.2133 0.4119 0.0370  -0.0474 -0.0817 45  ASP A CB  
288  C  CG  . ASP A 45  ? 0.4153 0.3375 0.4543 0.0581  0.0055  -0.1037 45  ASP A CG  
289  O  OD1 . ASP A 45  ? 0.4678 0.4078 0.4460 0.0190  0.0331  -0.0598 45  ASP A OD1 
290  O  OD2 . ASP A 45  ? 0.4652 0.3116 0.6860 0.0398  0.1449  -0.1065 45  ASP A OD2 
291  N  N   . GLY A 46  ? 0.3023 0.1985 0.3286 0.0094  -0.0943 -0.0249 46  GLY A N   
292  C  CA  . GLY A 46  ? 0.3288 0.1371 0.3084 0.0120  -0.1011 0.0245  46  GLY A CA  
293  C  C   . GLY A 46  ? 0.2717 0.1523 0.3167 0.0052  -0.1175 -0.0041 46  GLY A C   
294  O  O   . GLY A 46  ? 0.2736 0.2143 0.3462 -0.0113 -0.1099 0.0730  46  GLY A O   
295  N  N   . PHE A 47  ? 0.2550 0.1399 0.3134 0.0230  -0.0552 -0.0017 47  PHE A N   
296  C  CA  . PHE A 47  ? 0.2540 0.1482 0.3386 0.0241  -0.0938 -0.0373 47  PHE A CA  
297  C  C   . PHE A 47  ? 0.2056 0.1454 0.3174 -0.0004 -0.0567 -0.0080 47  PHE A C   
298  O  O   . PHE A 47  ? 0.2201 0.1544 0.3305 0.0175  -0.0422 0.0192  47  PHE A O   
299  C  CB  . PHE A 47  ? 0.2991 0.1508 0.3306 0.0045  -0.1272 -0.0414 47  PHE A CB  
300  C  CG  . PHE A 47  ? 0.3495 0.1517 0.3636 0.0091  -0.1023 -0.0429 47  PHE A CG  
301  C  CD1 . PHE A 47  ? 0.4126 0.2670 0.3752 0.0644  -0.0980 -0.0856 47  PHE A CD1 
302  C  CD2 . PHE A 47  ? 0.3333 0.1447 0.4363 -0.0068 -0.1315 -0.0109 47  PHE A CD2 
303  C  CE1 . PHE A 47  ? 0.3790 0.3032 0.4166 0.0898  -0.0782 -0.0756 47  PHE A CE1 
304  C  CE2 . PHE A 47  ? 0.3478 0.2074 0.4689 0.0568  -0.1162 -0.0046 47  PHE A CE2 
305  C  CZ  . PHE A 47  ? 0.2979 0.2653 0.4903 0.0220  -0.1133 -0.0565 47  PHE A CZ  
306  N  N   . LYS A 48  ? 0.2212 0.1964 0.3170 -0.0012 -0.0462 -0.0077 48  LYS A N   
307  C  CA  . LYS A 48  ? 0.2543 0.1805 0.3302 -0.0174 -0.0747 -0.0423 48  LYS A CA  
308  C  C   . LYS A 48  ? 0.2331 0.1035 0.3629 0.0239  -0.0662 -0.0489 48  LYS A C   
309  O  O   . LYS A 48  ? 0.2369 0.1783 0.2756 0.0351  -0.0399 0.0089  48  LYS A O   
310  C  CB  . LYS A 48  ? 0.2476 0.3875 0.3050 0.0720  -0.0725 0.0010  48  LYS A CB  
311  C  CG  . LYS A 48  ? 0.3569 0.4444 0.3867 0.0443  0.0089  0.0497  48  LYS A CG  
312  C  CD  . LYS A 48  ? 0.3801 0.5393 0.4563 0.0194  0.0609  -0.0038 48  LYS A CD  
313  C  CE  . LYS A 48  ? 0.3855 0.5556 0.4660 0.0840  0.0526  -0.0679 48  LYS A CE  
314  N  NZ  . LYS A 48  ? 0.4580 1.0528 0.4108 0.3685  0.0420  0.0318  48  LYS A NZ  
315  N  N   . LEU A 49  ? 0.2350 0.1613 0.3125 0.0201  -0.0869 -0.0116 49  LEU A N   
316  C  CA  . LEU A 49  ? 0.2351 0.1244 0.3106 0.0280  -0.1035 -0.0026 49  LEU A CA  
317  C  C   . LEU A 49  ? 0.2450 0.1594 0.3373 -0.0053 -0.0734 -0.0279 49  LEU A C   
318  O  O   . LEU A 49  ? 0.2412 0.1304 0.3212 0.0199  -0.0765 -0.0098 49  LEU A O   
319  C  CB  . LEU A 49  ? 0.3389 0.1244 0.3651 0.0368  -0.1793 0.0012  49  LEU A CB  
320  C  CG  . LEU A 49  ? 0.5247 0.1135 0.4083 0.0382  -0.1858 -0.0112 49  LEU A CG  
321  C  CD1 . LEU A 49  ? 0.3872 0.1389 0.4034 0.0847  -0.0280 0.0249  49  LEU A CD1 
322  C  CD2 . LEU A 49  ? 0.6772 0.2087 0.4283 0.0035  -0.2995 -0.0433 49  LEU A CD2 
323  N  N   . VAL A 50  ? 0.2552 0.1216 0.2783 0.0176  -0.0859 0.0314  50  VAL A N   
324  C  CA  . VAL A 50  ? 0.2335 0.1452 0.2832 0.0069  -0.0809 0.0247  50  VAL A CA  
325  C  C   . VAL A 50  ? 0.2024 0.1414 0.3376 -0.0003 -0.0771 0.0385  50  VAL A C   
326  O  O   . VAL A 50  ? 0.2216 0.1390 0.2396 0.0096  -0.0566 0.0008  50  VAL A O   
327  C  CB  A VAL A 50  ? 0.2039 0.2692 0.3199 0.0786  -0.0975 -0.0436 50  VAL A CB  
328  C  CB  B VAL A 50  ? 0.2554 0.2398 0.3190 0.0758  -0.1110 -0.0379 50  VAL A CB  
329  C  CG1 A VAL A 50  ? 0.1689 0.2350 0.4953 0.1041  -0.1989 -0.0034 50  VAL A CG1 
330  C  CG1 B VAL A 50  ? 0.1921 0.2846 0.2534 0.0690  -0.0404 0.0158  50  VAL A CG1 
331  C  CG2 A VAL A 50  ? 0.2761 0.4246 0.3638 0.1594  -0.0994 -0.1068 50  VAL A CG2 
332  C  CG2 B VAL A 50  ? 0.2719 0.2311 0.5466 0.0716  -0.2454 -0.0943 50  VAL A CG2 
333  N  N   . MET A 51  ? 0.1910 0.1153 0.2920 0.0193  -0.0624 0.0015  51  MET A N   
334  C  CA  . MET A 51  ? 0.2039 0.1216 0.2211 0.0341  -0.0330 -0.0132 51  MET A CA  
335  C  C   . MET A 51  ? 0.2121 0.1027 0.2193 0.0188  -0.0345 0.0044  51  MET A C   
336  O  O   . MET A 51  ? 0.2225 0.0913 0.2680 0.0253  -0.0648 -0.0075 51  MET A O   
337  C  CB  . MET A 51  ? 0.1697 0.1465 0.2955 0.0307  -0.0485 0.0242  51  MET A CB  
338  C  CG  . MET A 51  ? 0.2199 0.1497 0.3534 0.0253  -0.1092 0.0382  51  MET A CG  
339  S  SD  . MET A 51  ? 0.3899 0.1538 0.3739 0.0072  -0.0941 -0.0124 51  MET A SD  
340  C  CE  . MET A 51  ? 0.3437 0.1918 0.5187 0.1169  -0.0872 0.0643  51  MET A CE  
341  N  N   . ALA A 52  ? 0.2435 0.0699 0.2806 0.0377  -0.0888 -0.0038 52  ALA A N   
342  C  CA  . ALA A 52  ? 0.2503 0.0685 0.2068 0.0306  -0.0708 0.0339  52  ALA A CA  
343  C  C   . ALA A 52  ? 0.2465 0.1254 0.2224 0.0111  -0.0670 0.0238  52  ALA A C   
344  O  O   . ALA A 52  ? 0.2488 0.0840 0.2719 0.0229  -0.0844 -0.0151 52  ALA A O   
345  C  CB  . ALA A 52  ? 0.2565 0.0757 0.2907 0.0117  -0.0540 -0.0165 52  ALA A CB  
346  N  N   . SER A 53  ? 0.2175 0.0937 0.2277 0.0042  -0.0497 0.0165  53  SER A N   
347  C  CA  . SER A 53  ? 0.2442 0.0743 0.2589 0.0114  -0.0159 0.0088  53  SER A CA  
348  C  C   . SER A 53  ? 0.2046 0.0657 0.2528 0.0024  -0.0559 0.0138  53  SER A C   
349  O  O   . SER A 53  ? 0.2013 0.1145 0.3405 -0.0055 -0.0608 0.0321  53  SER A O   
350  C  CB  . SER A 53  ? 0.2072 0.0967 0.3147 0.0226  0.0027  0.0743  53  SER A CB  
351  O  OG  . SER A 53  ? 0.2643 0.1010 0.2735 0.0227  -0.0563 -0.0080 53  SER A OG  
352  N  N   . LEU A 54  ? 0.2524 0.0798 0.2745 0.0042  -0.0886 -0.0124 54  LEU A N   
353  C  CA  . LEU A 54  ? 0.2359 0.0960 0.2342 0.0059  -0.0795 -0.0141 54  LEU A CA  
354  C  C   . LEU A 54  ? 0.1980 0.0877 0.2290 -0.0130 -0.0715 -0.0103 54  LEU A C   
355  O  O   . LEU A 54  ? 0.1934 0.1376 0.2639 -0.0085 -0.0453 0.0315  54  LEU A O   
356  C  CB  . LEU A 54  ? 0.2516 0.1379 0.2441 0.0235  -0.1070 -0.0633 54  LEU A CB  
357  C  CG  . LEU A 54  ? 0.2025 0.1513 0.2370 0.0261  -0.0684 -0.0378 54  LEU A CG  
358  C  CD1 . LEU A 54  ? 0.2214 0.2696 0.3938 0.0092  -0.1603 -0.0883 54  LEU A CD1 
359  C  CD2 . LEU A 54  ? 0.2667 0.4194 0.2845 0.0975  -0.0079 -0.0076 54  LEU A CD2 
360  N  N   . TYR A 55  ? 0.2250 0.1252 0.2362 0.0379  -0.0566 -0.0007 55  TYR A N   
361  C  CA  . TYR A 55  ? 0.2472 0.1072 0.2493 -0.0391 -0.0755 0.0423  55  TYR A CA  
362  C  C   . TYR A 55  ? 0.2301 0.0647 0.2872 -0.0098 -0.0728 0.0388  55  TYR A C   
363  O  O   . TYR A 55  ? 0.2345 0.0927 0.2589 0.0038  -0.0367 0.0268  55  TYR A O   
364  C  CB  . TYR A 55  ? 0.2649 0.1024 0.2619 -0.0239 -0.0600 0.0594  55  TYR A CB  
365  C  CG  . TYR A 55  ? 0.2381 0.1010 0.2465 0.0386  -0.0421 0.0044  55  TYR A CG  
366  C  CD1 . TYR A 55  ? 0.2723 0.1032 0.2711 0.0009  -0.0729 0.0401  55  TYR A CD1 
367  C  CD2 . TYR A 55  ? 0.2610 0.1036 0.2782 0.0039  -0.0565 0.0160  55  TYR A CD2 
368  C  CE1 . TYR A 55  ? 0.3374 0.1137 0.2899 -0.0046 -0.1196 0.0350  55  TYR A CE1 
369  C  CE2 . TYR A 55  ? 0.3107 0.1178 0.2364 -0.0018 -0.0489 0.0155  55  TYR A CE2 
370  C  CZ  . TYR A 55  ? 0.2696 0.1193 0.2108 0.0064  -0.0198 0.0192  55  TYR A CZ  
371  O  OH  . TYR A 55  ? 0.3196 0.1199 0.2495 0.0281  -0.0667 -0.0101 55  TYR A OH  
372  N  N   . HIS A 56  ? 0.2231 0.0752 0.2853 -0.0121 -0.0537 0.0263  56  HIS A N   
373  C  CA  . HIS A 56  ? 0.2297 0.0688 0.2420 -0.0160 -0.0583 0.0342  56  HIS A CA  
374  C  C   . HIS A 56  ? 0.2411 0.1160 0.2604 0.0067  -0.0382 0.0670  56  HIS A C   
375  O  O   . HIS A 56  ? 0.2342 0.1052 0.3322 -0.0029 -0.0454 -0.0130 56  HIS A O   
376  C  CB  . HIS A 56  ? 0.2564 0.0703 0.3262 -0.0122 -0.0831 0.0123  56  HIS A CB  
377  C  CG  . HIS A 56  ? 0.2475 0.1076 0.3555 0.0108  -0.0936 -0.0377 56  HIS A CG  
378  N  ND1 . HIS A 56  ? 0.2315 0.1343 0.4127 -0.0049 -0.0732 -0.0043 56  HIS A ND1 
379  C  CD2 . HIS A 56  ? 0.2426 0.0668 0.3351 -0.0092 -0.0545 -0.0013 56  HIS A CD2 
380  C  CE1 . HIS A 56  ? 0.2140 0.0938 0.4208 -0.0349 -0.0561 -0.0223 56  HIS A CE1 
381  N  NE2 . HIS A 56  ? 0.2580 0.1674 0.3804 0.0138  -0.0560 -0.0504 56  HIS A NE2 
382  N  N   . ILE A 57  ? 0.2599 0.0874 0.2586 0.0290  -0.0299 0.0280  57  ILE A N   
383  C  CA  . ILE A 57  ? 0.2363 0.0994 0.2553 0.0276  -0.0389 0.0674  57  ILE A CA  
384  C  C   . ILE A 57  ? 0.2187 0.0869 0.2249 0.0146  -0.0313 0.0505  57  ILE A C   
385  O  O   . ILE A 57  ? 0.2114 0.1146 0.3424 0.0077  -0.0505 -0.0118 57  ILE A O   
386  C  CB  . ILE A 57  ? 0.2572 0.1063 0.2587 0.0157  -0.0540 0.0712  57  ILE A CB  
387  C  CG1 . ILE A 57  ? 0.2980 0.1176 0.2909 0.0260  -0.0776 0.0921  57  ILE A CG1 
388  C  CG2 . ILE A 57  ? 0.2545 0.2083 0.2588 0.0263  -0.0601 0.0551  57  ILE A CG2 
389  C  CD1 . ILE A 57  ? 0.3005 0.2395 0.3746 0.0256  -0.1002 0.1875  57  ILE A CD1 
390  N  N   . TYR A 58  ? 0.2346 0.0892 0.2868 0.0144  -0.0163 0.0364  58  TYR A N   
391  C  CA  . TYR A 58  ? 0.2287 0.0748 0.2594 0.0028  -0.0570 0.0034  58  TYR A CA  
392  C  C   . TYR A 58  ? 0.1949 0.1189 0.2580 0.0123  -0.0445 -0.0003 58  TYR A C   
393  O  O   . TYR A 58  ? 0.2129 0.0971 0.3120 0.0200  -0.0556 -0.0064 58  TYR A O   
394  C  CB  . TYR A 58  ? 0.1952 0.1074 0.2873 -0.0014 -0.0266 -0.0318 58  TYR A CB  
395  C  CG  . TYR A 58  ? 0.1759 0.1004 0.2717 -0.0302 0.0081  -0.0232 58  TYR A CG  
396  C  CD1 . TYR A 58  ? 0.3008 0.1324 0.3085 0.0287  0.0507  -0.0299 58  TYR A CD1 
397  C  CD2 . TYR A 58  ? 0.1876 0.2804 0.2707 -0.0127 -0.0153 -0.0201 58  TYR A CD2 
398  C  CE1 . TYR A 58  ? 0.4313 0.1249 0.3113 -0.0552 0.0725  -0.0610 58  TYR A CE1 
399  C  CE2 . TYR A 58  ? 0.3211 0.3504 0.2760 -0.0514 -0.0571 0.0022  58  TYR A CE2 
400  C  CZ  . TYR A 58  ? 0.3598 0.2966 0.2397 -0.1963 0.0375  -0.0149 58  TYR A CZ  
401  O  OH  . TYR A 58  ? 0.5597 0.5803 0.2758 -0.3414 0.0143  -0.1032 58  TYR A OH  
402  N  N   . VAL A 59  ? 0.2011 0.1434 0.2488 0.0154  -0.0357 0.0125  59  VAL A N   
403  C  CA  . VAL A 59  ? 0.2321 0.1293 0.2707 0.0012  -0.0667 -0.0114 59  VAL A CA  
404  C  C   . VAL A 59  ? 0.2231 0.0861 0.2831 0.0133  -0.0771 -0.0111 59  VAL A C   
405  O  O   . VAL A 59  ? 0.2281 0.1229 0.3454 0.0153  -0.0923 0.0513  59  VAL A O   
406  C  CB  . VAL A 59  ? 0.2757 0.0479 0.2545 -0.0042 -0.0532 0.0277  59  VAL A CB  
407  C  CG1 . VAL A 59  ? 0.2848 0.1848 0.2544 -0.0238 -0.0403 -0.0236 59  VAL A CG1 
408  C  CG2 . VAL A 59  ? 0.2738 0.0950 0.3117 -0.0020 -0.0262 0.0352  59  VAL A CG2 
409  N  N   . ALA A 60  ? 0.2087 0.0925 0.3634 0.0336  -0.0627 0.0122  60  ALA A N   
410  C  CA  . ALA A 60  ? 0.2303 0.1021 0.3034 0.0009  -0.0759 -0.0009 60  ALA A CA  
411  C  C   . ALA A 60  ? 0.2410 0.1452 0.2807 0.0220  -0.0739 0.0184  60  ALA A C   
412  O  O   . ALA A 60  ? 0.2459 0.1380 0.3355 0.0298  -0.0705 0.0030  60  ALA A O   
413  C  CB  . ALA A 60  ? 0.2601 0.1308 0.3095 0.0188  -0.0506 0.0401  60  ALA A CB  
414  N  N   . LEU A 61  ? 0.2603 0.1131 0.2906 0.0109  -0.0798 0.0081  61  LEU A N   
415  C  CA  . LEU A 61  ? 0.2355 0.1455 0.2744 0.0183  -0.0706 0.0257  61  LEU A CA  
416  C  C   . LEU A 61  ? 0.2097 0.1252 0.2952 0.0038  -0.0523 0.0097  61  LEU A C   
417  O  O   . LEU A 61  ? 0.2417 0.1106 0.2742 0.0106  -0.0193 0.0075  61  LEU A O   
418  C  CB  . LEU A 61  ? 0.2131 0.1403 0.2923 0.0135  -0.0575 -0.0053 61  LEU A CB  
419  C  CG  . LEU A 61  ? 0.2644 0.1229 0.2770 0.0094  -0.0447 0.0127  61  LEU A CG  
420  C  CD1 . LEU A 61  ? 0.2760 0.1600 0.3527 0.0315  0.0093  0.0241  61  LEU A CD1 
421  C  CD2 . LEU A 61  ? 0.2848 0.1887 0.3040 0.0198  -0.0635 -0.0342 61  LEU A CD2 
422  N  N   . GLU A 62  ? 0.2070 0.1183 0.2634 0.0382  -0.0347 0.0029  62  GLU A N   
423  C  CA  . GLU A 62  ? 0.2179 0.1411 0.2765 0.0530  -0.0301 0.0232  62  GLU A CA  
424  C  C   . GLU A 62  ? 0.2443 0.1140 0.3009 0.0354  -0.0496 0.0424  62  GLU A C   
425  O  O   . GLU A 62  ? 0.2149 0.1592 0.3974 0.0484  -0.0698 0.0128  62  GLU A O   
426  C  CB  . GLU A 62  ? 0.2396 0.1347 0.2490 0.0407  -0.0517 0.0365  62  GLU A CB  
427  C  CG  . GLU A 62  ? 0.2394 0.1208 0.2204 0.0404  -0.0266 0.0228  62  GLU A CG  
428  C  CD  . GLU A 62  ? 0.2328 0.1536 0.2450 0.0353  0.0061  -0.0664 62  GLU A CD  
429  O  OE1 . GLU A 62  ? 0.2096 0.1473 0.2554 0.0022  -0.0304 -0.0190 62  GLU A OE1 
430  O  OE2 . GLU A 62  ? 0.3571 0.1041 0.2469 -0.0561 -0.0287 -0.0203 62  GLU A OE2 
431  N  N   . GLU A 63  ? 0.2171 0.1402 0.2962 -0.0028 -0.0058 0.0258  63  GLU A N   
432  C  CA  . GLU A 63  ? 0.2670 0.1746 0.2842 0.0457  -0.0533 0.0180  63  GLU A CA  
433  C  C   . GLU A 63  ? 0.2098 0.1951 0.2953 0.0040  -0.0989 0.0245  63  GLU A C   
434  O  O   . GLU A 63  ? 0.2328 0.2085 0.3744 0.0370  -0.1061 0.0290  63  GLU A O   
435  C  CB  . GLU A 63  ? 0.2934 0.1867 0.3719 0.1065  -0.1232 -0.0298 63  GLU A CB  
436  C  CG  . GLU A 63  ? 0.4588 0.3324 0.4082 0.0586  -0.2622 -0.0235 63  GLU A CG  
437  C  CD  . GLU A 63  ? 0.7321 0.4856 0.4669 0.0380  -0.2725 -0.1606 63  GLU A CD  
438  O  OE1 . GLU A 63  ? 0.8169 0.4865 0.4228 0.1490  -0.1474 -0.1469 63  GLU A OE1 
439  O  OE2 . GLU A 63  ? 0.9188 0.6814 0.7184 -0.1692 -0.2950 -0.2813 63  GLU A OE2 
440  N  N   . GLU A 64  ? 0.1787 0.1530 0.3169 0.0146  -0.0709 0.0224  64  GLU A N   
441  C  CA  . GLU A 64  ? 0.1917 0.1587 0.3458 -0.0059 -0.0592 0.0240  64  GLU A CA  
442  C  C   . GLU A 64  ? 0.2441 0.1432 0.3008 0.0067  -0.0260 0.0631  64  GLU A C   
443  O  O   . GLU A 64  ? 0.2398 0.1987 0.4214 0.0486  -0.0461 0.0158  64  GLU A O   
444  C  CB  . GLU A 64  ? 0.2047 0.1560 0.3640 0.0247  -0.0213 0.0300  64  GLU A CB  
445  C  CG  . GLU A 64  ? 0.2502 0.1801 0.3114 0.0511  -0.0456 0.0284  64  GLU A CG  
446  C  CD  . GLU A 64  ? 0.2809 0.2069 0.3503 0.0883  -0.0879 -0.0064 64  GLU A CD  
447  O  OE1 . GLU A 64  ? 0.2347 0.2099 0.3329 0.0084  -0.0337 0.0174  64  GLU A OE1 
448  O  OE2 . GLU A 64  ? 0.3193 0.2732 0.3051 0.0763  -0.0665 -0.0057 64  GLU A OE2 
449  N  N   . ILE A 65  ? 0.2587 0.1374 0.2969 0.0221  -0.0439 0.0268  65  ILE A N   
450  C  CA  . ILE A 65  ? 0.2554 0.1349 0.3489 0.0495  -0.0472 0.0319  65  ILE A CA  
451  C  C   . ILE A 65  ? 0.2351 0.1770 0.3827 0.0536  -0.0393 0.0616  65  ILE A C   
452  O  O   . ILE A 65  ? 0.2452 0.2027 0.4255 0.0745  -0.0560 0.0187  65  ILE A O   
453  C  CB  . ILE A 65  ? 0.2487 0.1509 0.2946 0.0678  -0.0266 -0.0226 65  ILE A CB  
454  C  CG1 . ILE A 65  ? 0.2762 0.1350 0.2631 0.0523  -0.0293 -0.0357 65  ILE A CG1 
455  C  CG2 . ILE A 65  ? 0.3511 0.1489 0.4293 0.0918  -0.1123 -0.0429 65  ILE A CG2 
456  C  CD1 . ILE A 65  ? 0.3125 0.1381 0.3624 0.0492  -0.0973 -0.0365 65  ILE A CD1 
457  N  N   . GLU A 66  ? 0.2248 0.2294 0.3762 0.0304  -0.0568 0.0803  66  GLU A N   
458  C  CA  . GLU A 66  ? 0.2922 0.2111 0.4237 0.0195  -0.1230 0.0868  66  GLU A CA  
459  C  C   . GLU A 66  ? 0.2764 0.1880 0.4226 0.0526  -0.1162 0.0556  66  GLU A C   
460  O  O   . GLU A 66  ? 0.2934 0.2167 0.4546 0.0763  -0.0789 0.0628  66  GLU A O   
461  C  CB  . GLU A 66  ? 0.3304 0.2968 0.4368 0.0094  -0.1059 0.1698  66  GLU A CB  
462  C  CG  . GLU A 66  ? 0.3024 0.2803 0.5490 0.0391  -0.0176 0.0243  66  GLU A CG  
463  C  CD  . GLU A 66  ? 0.4503 0.2522 0.6671 0.0783  -0.0248 0.0693  66  GLU A CD  
464  O  OE1 . GLU A 66  ? 0.3916 0.3673 0.7805 0.1158  0.0374  0.1814  66  GLU A OE1 
465  O  OE2 . GLU A 66  ? 0.5310 0.2005 0.5771 0.0201  0.0844  0.0549  66  GLU A OE2 
466  N  N   . ARG A 67  ? 0.2956 0.1912 0.3961 0.0344  -0.1198 0.0204  67  ARG A N   
467  C  CA  . ARG A 67  ? 0.2909 0.2366 0.4366 0.0273  -0.1253 0.0040  67  ARG A CA  
468  C  C   . ARG A 67  ? 0.2940 0.2953 0.4476 0.0529  -0.1054 0.0391  67  ARG A C   
469  O  O   . ARG A 67  ? 0.2977 0.2816 0.4572 0.0496  -0.1156 0.0307  67  ARG A O   
470  C  CB  . ARG A 67  ? 0.2749 0.2356 0.5413 0.0059  -0.1391 0.0113  67  ARG A CB  
471  C  CG  . ARG A 67  ? 0.2827 0.3071 0.5240 -0.0425 -0.0431 -0.0004 67  ARG A CG  
472  C  CD  . ARG A 67  ? 0.2683 0.3094 0.5599 -0.0601 -0.0499 0.0249  67  ARG A CD  
473  N  NE  . ARG A 67  ? 0.4566 0.5310 0.6498 0.2006  -0.1309 -0.0901 67  ARG A NE  
474  C  CZ  . ARG A 67  ? 0.4541 0.6208 0.6666 0.2793  -0.0953 -0.0861 67  ARG A CZ  
475  N  NH1 . ARG A 67  ? 0.5482 0.4610 0.6222 0.2377  -0.0434 0.0726  67  ARG A NH1 
476  N  NH2 . ARG A 67  ? 0.4767 0.8348 0.8344 0.3362  0.0161  -0.0115 67  ARG A NH2 
477  N  N   . ASN A 68  ? 0.2342 0.2208 0.4372 0.0244  -0.0722 0.0351  68  ASN A N   
478  C  CA  . ASN A 68  ? 0.2524 0.2511 0.4506 0.0287  -0.0531 0.0517  68  ASN A CA  
479  C  C   . ASN A 68  ? 0.2602 0.2628 0.4421 0.0508  -0.0380 0.0347  68  ASN A C   
480  O  O   . ASN A 68  ? 0.3026 0.3397 0.4650 0.1504  -0.0078 0.0295  68  ASN A O   
481  C  CB  . ASN A 68  ? 0.2400 0.2699 0.4548 0.0644  -0.0231 0.0571  68  ASN A CB  
482  C  CG  . ASN A 68  ? 0.1998 0.2614 0.5012 0.0822  -0.0516 0.0533  68  ASN A CG  
483  O  OD1 . ASN A 68  ? 0.2416 0.2866 0.5424 0.0945  -0.0086 0.0406  68  ASN A OD1 
484  N  ND2 . ASN A 68  ? 0.2230 0.2396 0.5171 0.0634  0.0162  0.1433  68  ASN A ND2 
485  N  N   . LYS A 69  ? 0.1949 0.2454 0.4804 0.0443  -0.0715 0.0335  69  LYS A N   
486  C  CA  . LYS A 69  ? 0.2354 0.2686 0.4926 0.0357  -0.0325 0.0034  69  LYS A CA  
487  C  C   . LYS A 69  ? 0.2586 0.2816 0.4275 0.0428  -0.0212 0.0211  69  LYS A C   
488  O  O   . LYS A 69  ? 0.3315 0.3866 0.4471 0.0500  -0.0206 -0.0408 69  LYS A O   
489  C  CB  . LYS A 69  ? 0.2317 0.2627 0.4639 -0.0008 -0.0251 -0.0482 69  LYS A CB  
490  C  CG  . LYS A 69  ? 0.2349 0.3243 0.3922 0.0067  0.0063  -0.0675 69  LYS A CG  
491  C  CD  . LYS A 69  ? 0.3922 0.4095 0.4898 -0.0535 0.0083  0.0252  69  LYS A CD  
492  C  CE  . LYS A 69  ? 0.4852 0.4370 0.4807 -0.1627 0.0218  0.0225  69  LYS A CE  
493  N  NZ  . LYS A 69  ? 0.7750 0.6236 0.6047 -0.4252 -0.0292 0.2548  69  LYS A NZ  
494  N  N   . GLU A 70  ? 0.2581 0.2818 0.4471 0.0907  -0.0446 0.0336  70  GLU A N   
495  C  CA  . GLU A 70  ? 0.2781 0.2780 0.4718 0.0885  -0.0107 0.0216  70  GLU A CA  
496  C  C   . GLU A 70  ? 0.2442 0.2644 0.5553 0.0593  -0.0202 0.0336  70  GLU A C   
497  O  O   . GLU A 70  ? 0.2569 0.3076 0.5839 0.0833  0.0083  0.0982  70  GLU A O   
498  C  CB  . GLU A 70  ? 0.3166 0.3753 0.5532 0.1764  -0.0343 0.0580  70  GLU A CB  
499  C  CG  . GLU A 70  ? 0.4364 0.5129 0.6489 0.1532  -0.0719 0.2175  70  GLU A CG  
500  C  CD  . GLU A 70  ? 0.8345 0.5190 0.6415 0.1995  -0.1641 0.1856  70  GLU A CD  
501  O  OE1 . GLU A 70  ? 1.1940 0.5960 0.8568 0.3974  -0.1867 0.2543  70  GLU A OE1 
502  O  OE2 . GLU A 70  ? 1.1149 0.8214 0.7581 0.2398  -0.2908 0.0075  70  GLU A OE2 
503  N  N   . SER A 71  ? 0.2922 0.2680 0.5113 0.0696  -0.0391 0.0267  71  SER A N   
504  C  CA  . SER A 71  ? 0.2495 0.2880 0.5784 0.0086  -0.0894 0.0577  71  SER A CA  
505  C  C   . SER A 71  ? 0.2169 0.1866 0.5473 -0.0135 -0.0431 0.1128  71  SER A C   
506  O  O   . SER A 71  ? 0.2193 0.2344 0.5787 -0.0035 -0.0451 0.0195  71  SER A O   
507  C  CB  . SER A 71  ? 0.3540 0.2533 0.6416 -0.0417 -0.1642 0.0121  71  SER A CB  
508  O  OG  . SER A 71  ? 0.4300 0.2759 0.7192 0.0155  -0.0524 0.0612  71  SER A OG  
509  N  N   . PRO A 72  ? 0.2447 0.2205 0.6303 -0.0082 0.0061  0.1023  72  PRO A N   
510  C  CA  . PRO A 72  ? 0.2694 0.3004 0.6322 0.0484  0.0495  0.0581  72  PRO A CA  
511  C  C   . PRO A 72  ? 0.2544 0.3004 0.5303 0.0428  0.0775  0.0414  72  PRO A C   
512  O  O   . PRO A 72  ? 0.4853 0.2557 0.5784 0.0467  -0.0114 0.0239  72  PRO A O   
513  C  CB  . PRO A 72  ? 0.2753 0.3536 0.7420 0.0860  0.0816  0.0378  72  PRO A CB  
514  C  CG  . PRO A 72  ? 0.2670 0.3425 0.8263 0.0264  0.0487  -0.0357 72  PRO A CG  
515  C  CD  . PRO A 72  ? 0.2126 0.3931 0.7699 0.0148  0.0417  0.0053  72  PRO A CD  
516  N  N   . VAL A 73  ? 0.2235 0.2860 0.4808 0.0195  0.0324  0.0506  73  VAL A N   
517  C  CA  . VAL A 73  ? 0.2549 0.2472 0.4401 -0.0126 0.0149  0.0614  73  VAL A CA  
518  C  C   . VAL A 73  ? 0.2372 0.2185 0.3758 0.0233  0.0048  0.0297  73  VAL A C   
519  O  O   . VAL A 73  ? 0.2813 0.3064 0.3718 0.0498  -0.0481 0.0099  73  VAL A O   
520  C  CB  . VAL A 73  ? 0.3312 0.2594 0.5134 -0.0428 -0.1094 0.0813  73  VAL A CB  
521  C  CG1 . VAL A 73  ? 0.3126 0.3115 0.6230 -0.0578 -0.1833 0.0776  73  VAL A CG1 
522  C  CG2 . VAL A 73  ? 0.3763 0.2762 0.5015 0.0269  -0.2001 0.0055  73  VAL A CG2 
523  N  N   . PHE A 74  ? 0.2493 0.2574 0.4065 -0.0008 0.0236  0.0518  74  PHE A N   
524  C  CA  . PHE A 74  ? 0.2210 0.1963 0.4242 0.0688  0.0433  0.0393  74  PHE A CA  
525  C  C   . PHE A 74  ? 0.2050 0.2000 0.4700 0.0543  0.0410  0.0531  74  PHE A C   
526  O  O   . PHE A 74  ? 0.2224 0.2196 0.5461 0.0541  0.0037  0.0301  74  PHE A O   
527  C  CB  . PHE A 74  ? 0.2393 0.2407 0.3749 0.0790  -0.0124 0.0401  74  PHE A CB  
528  C  CG  . PHE A 74  ? 0.2497 0.1708 0.3142 0.0554  0.0127  -0.0155 74  PHE A CG  
529  C  CD1 . PHE A 74  ? 0.1999 0.1687 0.3318 0.0357  0.0158  -0.0092 74  PHE A CD1 
530  C  CD2 . PHE A 74  ? 0.2969 0.1992 0.3573 0.0306  -0.0069 0.0216  74  PHE A CD2 
531  C  CE1 . PHE A 74  ? 0.2029 0.2074 0.3145 0.0050  0.0385  0.0403  74  PHE A CE1 
532  C  CE2 . PHE A 74  ? 0.2975 0.1665 0.3467 0.0120  -0.0021 0.0145  74  PHE A CE2 
533  C  CZ  . PHE A 74  ? 0.2639 0.1762 0.2599 0.0054  0.0362  0.0159  74  PHE A CZ  
534  N  N   . ALA A 75  ? 0.2286 0.1611 0.5292 0.0581  0.0021  -0.0073 75  ALA A N   
535  C  CA  . ALA A 75  ? 0.2449 0.1514 0.4606 0.0737  0.0268  -0.0332 75  ALA A CA  
536  C  C   . ALA A 75  ? 0.2113 0.1958 0.4434 0.0279  0.0539  -0.0193 75  ALA A C   
537  O  O   . ALA A 75  ? 0.2744 0.1747 0.4969 0.0122  0.0427  0.0189  75  ALA A O   
538  C  CB  . ALA A 75  ? 0.2896 0.1712 0.5175 0.1099  -0.0306 -0.0749 75  ALA A CB  
539  N  N   . PRO A 76  ? 0.2533 0.1816 0.4364 0.0493  0.0296  0.0083  76  PRO A N   
540  C  CA  . PRO A 76  ? 0.3069 0.1875 0.4501 0.0490  0.0099  -0.0050 76  PRO A CA  
541  C  C   . PRO A 76  ? 0.3053 0.1777 0.4100 0.0449  -0.0199 -0.0137 76  PRO A C   
542  O  O   . PRO A 76  ? 0.3276 0.1843 0.4638 0.0358  -0.0302 -0.0255 76  PRO A O   
543  C  CB  . PRO A 76  ? 0.3632 0.1933 0.4379 0.0568  0.0369  -0.0278 76  PRO A CB  
544  C  CG  . PRO A 76  ? 0.3257 0.2558 0.4563 0.0786  0.0825  -0.0276 76  PRO A CG  
545  C  CD  . PRO A 76  ? 0.3184 0.1983 0.4271 0.0248  0.0536  0.0090  76  PRO A CD  
546  N  N   . VAL A 77  ? 0.3070 0.1624 0.4133 0.0386  0.0176  0.0066  77  VAL A N   
547  C  CA  . VAL A 77  ? 0.2926 0.1723 0.4028 0.0218  -0.0100 -0.0173 77  VAL A CA  
548  C  C   . VAL A 77  ? 0.2692 0.1138 0.4160 0.0200  -0.0051 0.0160  77  VAL A C   
549  O  O   . VAL A 77  ? 0.2805 0.1963 0.3747 0.0568  -0.0427 -0.0320 77  VAL A O   
550  C  CB  . VAL A 77  ? 0.2495 0.1859 0.3494 0.0136  0.0263  -0.0026 77  VAL A CB  
551  C  CG1 . VAL A 77  ? 0.4561 0.1886 0.3449 0.0075  0.0037  -0.0470 77  VAL A CG1 
552  C  CG2 . VAL A 77  ? 0.3018 0.1834 0.2682 -0.0047 -0.0201 0.0467  77  VAL A CG2 
553  N  N   . TYR A 78  ? 0.2650 0.1473 0.4364 0.0390  -0.0008 0.0300  78  TYR A N   
554  C  CA  . TYR A 78  ? 0.2101 0.1415 0.4392 0.0511  -0.0092 0.0421  78  TYR A CA  
555  C  C   . TYR A 78  ? 0.2392 0.1522 0.3542 0.0251  -0.0014 -0.0297 78  TYR A C   
556  O  O   . TYR A 78  ? 0.2488 0.1507 0.4075 0.0196  0.0017  -0.0303 78  TYR A O   
557  C  CB  . TYR A 78  ? 0.1861 0.1965 0.4370 0.0415  0.0028  0.0065  78  TYR A CB  
558  C  CG  . TYR A 78  ? 0.2371 0.2268 0.4282 0.0714  -0.0026 0.0118  78  TYR A CG  
559  C  CD1 . TYR A 78  ? 0.2891 0.1972 0.4484 0.0692  0.0573  0.0454  78  TYR A CD1 
560  C  CD2 . TYR A 78  ? 0.2431 0.2030 0.4117 0.0621  -0.0072 -0.0133 78  TYR A CD2 
561  C  CE1 . TYR A 78  ? 0.3315 0.1478 0.4102 0.0061  -0.0101 -0.0110 78  TYR A CE1 
562  C  CE2 . TYR A 78  ? 0.3068 0.2046 0.3976 0.0520  -0.0340 -0.0209 78  TYR A CE2 
563  C  CZ  . TYR A 78  ? 0.3428 0.2030 0.3692 0.0608  -0.0372 -0.0200 78  TYR A CZ  
564  O  OH  . TYR A 78  ? 0.3499 0.1748 0.3818 -0.0371 -0.0146 -0.0213 78  TYR A OH  
565  N  N   . PHE A 79  ? 0.2348 0.1621 0.3473 0.0245  -0.0024 0.0183  79  PHE A N   
566  C  CA  . PHE A 79  ? 0.2295 0.1600 0.3460 0.0363  -0.0206 0.0516  79  PHE A CA  
567  C  C   . PHE A 79  ? 0.2164 0.1603 0.3387 -0.0179 -0.0352 -0.0044 79  PHE A C   
568  O  O   . PHE A 79  ? 0.2211 0.1360 0.3523 -0.0129 -0.0207 -0.0041 79  PHE A O   
569  C  CB  . PHE A 79  ? 0.2383 0.1471 0.3367 0.0419  -0.0136 0.0143  79  PHE A CB  
570  C  CG  . PHE A 79  ? 0.2682 0.1907 0.3618 0.0171  0.0313  0.0060  79  PHE A CG  
571  C  CD1 . PHE A 79  ? 0.2939 0.1969 0.3407 -0.0004 0.0139  -0.0420 79  PHE A CD1 
572  C  CD2 . PHE A 79  ? 0.3725 0.2549 0.3613 0.0073  0.0378  0.0372  79  PHE A CD2 
573  C  CE1 . PHE A 79  ? 0.3094 0.1955 0.3318 0.0385  0.0546  0.0295  79  PHE A CE1 
574  C  CE2 . PHE A 79  ? 0.3067 0.2163 0.3628 0.0092  0.0310  0.0524  79  PHE A CE2 
575  C  CZ  . PHE A 79  ? 0.3320 0.2118 0.3522 -0.0274 0.0103  0.0467  79  PHE A CZ  
576  N  N   . PRO A 80  ? 0.2817 0.1457 0.3432 0.0010  -0.0471 0.0149  80  PRO A N   
577  C  CA  . PRO A 80  ? 0.3279 0.1420 0.3368 -0.0250 -0.0439 -0.0081 80  PRO A CA  
578  C  C   . PRO A 80  ? 0.3273 0.1257 0.3345 -0.0176 -0.0248 0.0094  80  PRO A C   
579  O  O   . PRO A 80  ? 0.3369 0.1123 0.2815 -0.0162 -0.0411 -0.0065 80  PRO A O   
580  C  CB  . PRO A 80  ? 0.3712 0.2553 0.3594 -0.0159 -0.0860 -0.0432 80  PRO A CB  
581  C  CG  . PRO A 80  ? 0.3518 0.3110 0.3405 0.0192  -0.1007 -0.0146 80  PRO A CG  
582  C  CD  . PRO A 80  ? 0.2733 0.2172 0.3570 -0.0228 -0.0797 0.0170  80  PRO A CD  
583  N  N   . GLU A 81  ? 0.2724 0.1328 0.3493 0.0045  -0.0280 0.0172  81  GLU A N   
584  C  CA  . GLU A 81  ? 0.2888 0.1072 0.2843 -0.0024 -0.0089 -0.0295 81  GLU A CA  
585  C  C   . GLU A 81  ? 0.2650 0.0832 0.3240 -0.0268 0.0066  0.0622  81  GLU A C   
586  O  O   . GLU A 81  ? 0.2706 0.1651 0.3111 -0.0238 0.0122  -0.0017 81  GLU A O   
587  C  CB  . GLU A 81  ? 0.2502 0.1218 0.4368 0.0173  -0.0419 0.0128  81  GLU A CB  
588  C  CG  . GLU A 81  ? 0.3017 0.2307 0.4433 0.0283  -0.0519 0.0602  81  GLU A CG  
589  C  CD  . GLU A 81  ? 0.3021 0.2154 0.4442 0.0416  -0.0524 0.0623  81  GLU A CD  
590  O  OE1 . GLU A 81  ? 0.2867 0.3532 0.4406 0.0497  -0.0645 0.0923  81  GLU A OE1 
591  O  OE2 . GLU A 81  ? 0.3676 0.2889 0.5303 -0.0171 -0.0147 -0.0521 81  GLU A OE2 
592  N  N   . GLU A 82  ? 0.2517 0.1390 0.3174 0.0274  0.0025  0.0557  82  GLU A N   
593  C  CA  . GLU A 82  ? 0.1887 0.1132 0.3016 -0.0041 0.0275  -0.0044 82  GLU A CA  
594  C  C   . GLU A 82  ? 0.2077 0.1155 0.2755 0.0102  -0.0126 -0.0087 82  GLU A C   
595  O  O   . GLU A 82  ? 0.2042 0.1328 0.2682 0.0029  0.0034  0.0221  82  GLU A O   
596  C  CB  . GLU A 82  ? 0.2961 0.1228 0.3035 -0.0091 0.0520  -0.0259 82  GLU A CB  
597  C  CG  . GLU A 82  ? 0.3466 0.1070 0.2878 -0.0200 0.0494  -0.0313 82  GLU A CG  
598  C  CD  . GLU A 82  ? 0.3491 0.1576 0.3753 0.0402  0.0357  -0.0674 82  GLU A CD  
599  O  OE1 . GLU A 82  ? 0.3647 0.1815 0.3665 0.0121  -0.0045 -0.0174 82  GLU A OE1 
600  O  OE2 . GLU A 82  ? 0.4313 0.1644 0.4869 0.0482  -0.0399 -0.0522 82  GLU A OE2 
601  N  N   . LEU A 83  ? 0.2239 0.1126 0.2858 -0.0030 -0.0054 0.0007  83  LEU A N   
602  C  CA  . LEU A 83  ? 0.2601 0.1152 0.2695 -0.0011 -0.0124 0.0055  83  LEU A CA  
603  C  C   . LEU A 83  ? 0.2621 0.1078 0.2800 -0.0301 -0.0174 -0.0166 83  LEU A C   
604  O  O   . LEU A 83  ? 0.2793 0.1311 0.2617 -0.0096 -0.0086 -0.0090 83  LEU A O   
605  C  CB  . LEU A 83  ? 0.2442 0.1053 0.2670 -0.0121 -0.0308 -0.0065 83  LEU A CB  
606  C  CG  . LEU A 83  ? 0.2545 0.1328 0.2629 -0.0094 -0.0206 -0.0029 83  LEU A CG  
607  C  CD1 . LEU A 83  ? 0.2532 0.1758 0.3141 -0.0066 0.0258  -0.0229 83  LEU A CD1 
608  C  CD2 . LEU A 83  ? 0.2527 0.1557 0.2383 -0.0041 -0.0132 -0.0097 83  LEU A CD2 
609  N  N   . HIS A 84  ? 0.2849 0.1260 0.2661 0.0035  0.0141  0.0020  84  HIS A N   
610  C  CA  . HIS A 84  ? 0.2561 0.1056 0.2636 0.0110  -0.0224 0.0062  84  HIS A CA  
611  C  C   . HIS A 84  ? 0.2340 0.1234 0.2147 0.0024  -0.0718 -0.0361 84  HIS A C   
612  O  O   . HIS A 84  ? 0.2476 0.1081 0.2470 0.0065  -0.0609 -0.0217 84  HIS A O   
613  C  CB  . HIS A 84  ? 0.2362 0.1366 0.3176 -0.0012 -0.0809 0.0100  84  HIS A CB  
614  C  CG  . HIS A 84  ? 0.3034 0.0986 0.2961 0.0357  -0.0467 0.0156  84  HIS A CG  
615  N  ND1 . HIS A 84  ? 0.3590 0.1301 0.3800 -0.0311 0.0129  -0.0619 84  HIS A ND1 
616  C  CD2 . HIS A 84  ? 0.3080 0.1409 0.3017 -0.0183 -0.0397 -0.0418 84  HIS A CD2 
617  C  CE1 . HIS A 84  ? 0.2939 0.1051 0.3242 -0.0065 -0.1122 0.0094  84  HIS A CE1 
618  N  NE2 . HIS A 84  ? 0.3274 0.1785 0.3691 -0.0172 0.0039  0.0109  84  HIS A NE2 
619  N  N   . ARG A 85  ? 0.2037 0.1240 0.2605 -0.0202 -0.0196 -0.0303 85  ARG A N   
620  C  CA  . ARG A 85  ? 0.2070 0.1038 0.2426 -0.0120 -0.0197 0.0244  85  ARG A CA  
621  C  C   . ARG A 85  ? 0.2051 0.0894 0.2420 0.0305  -0.0378 0.0257  85  ARG A C   
622  O  O   . ARG A 85  ? 0.2062 0.1220 0.2405 0.0259  -0.0493 0.0007  85  ARG A O   
623  C  CB  . ARG A 85  ? 0.2810 0.1019 0.2361 -0.0317 -0.0585 0.0166  85  ARG A CB  
624  C  CG  . ARG A 85  ? 0.3025 0.1208 0.2470 -0.0385 -0.0703 -0.0038 85  ARG A CG  
625  C  CD  . ARG A 85  ? 0.2485 0.1103 0.2394 0.0077  -0.0807 0.0152  85  ARG A CD  
626  N  NE  . ARG A 85  ? 0.2288 0.1030 0.2741 0.0081  -0.0462 0.0117  85  ARG A NE  
627  C  CZ  . ARG A 85  ? 0.2398 0.0872 0.2157 0.0353  0.0305  -0.0295 85  ARG A CZ  
628  N  NH1 . ARG A 85  ? 0.2401 0.0844 0.2543 0.0208  0.0272  0.0018  85  ARG A NH1 
629  N  NH2 . ARG A 85  ? 0.2464 0.0884 0.2962 -0.0134 -0.1111 -0.0030 85  ARG A NH2 
630  N  N   . LYS A 86  ? 0.1984 0.1298 0.2544 0.0097  -0.0225 0.0022  86  LYS A N   
631  C  CA  . LYS A 86  ? 0.2028 0.1088 0.2464 0.0202  -0.0229 0.0140  86  LYS A CA  
632  C  C   . LYS A 86  ? 0.2225 0.0957 0.2442 -0.0002 -0.0282 0.0014  86  LYS A C   
633  O  O   . LYS A 86  ? 0.2376 0.0940 0.2015 -0.0220 -0.0246 -0.0173 86  LYS A O   
634  C  CB  . LYS A 86  ? 0.2185 0.1480 0.2781 -0.0075 -0.0344 -0.0122 86  LYS A CB  
635  C  CG  . LYS A 86  ? 0.1831 0.1376 0.2581 -0.0052 -0.0057 0.0170  86  LYS A CG  
636  C  CD  . LYS A 86  ? 0.2643 0.2392 0.3779 -0.0223 -0.1224 -0.0406 86  LYS A CD  
637  C  CE  . LYS A 86  ? 0.4630 0.3486 0.3370 -0.0352 -0.1629 0.0718  86  LYS A CE  
638  N  NZ  . LYS A 86  ? 0.4446 0.5012 0.6087 0.1808  -0.0045 0.2683  86  LYS A NZ  
639  N  N   . ALA A 87  ? 0.2081 0.0992 0.2678 -0.0008 -0.0684 0.0155  87  ALA A N   
640  C  CA  . ALA A 87  ? 0.2202 0.0719 0.2942 0.0144  -0.0538 0.0123  87  ALA A CA  
641  C  C   . ALA A 87  ? 0.2222 0.0741 0.2371 -0.0045 -0.0382 -0.0063 87  ALA A C   
642  O  O   . ALA A 87  ? 0.2270 0.1112 0.2371 0.0109  -0.0320 0.0067  87  ALA A O   
643  C  CB  . ALA A 87  ? 0.2789 0.0537 0.3022 0.0036  -0.1221 -0.0214 87  ALA A CB  
644  N  N   . ALA A 88  ? 0.2475 0.0970 0.2333 -0.0293 -0.0395 -0.0029 88  ALA A N   
645  C  CA  . ALA A 88  ? 0.2512 0.1049 0.2460 0.0052  -0.0533 -0.0339 88  ALA A CA  
646  C  C   . ALA A 88  ? 0.2676 0.0876 0.2226 -0.0092 -0.0254 -0.0059 88  ALA A C   
647  O  O   . ALA A 88  ? 0.2423 0.0878 0.2339 0.0079  -0.0510 0.0064  88  ALA A O   
648  C  CB  . ALA A 88  ? 0.2143 0.1046 0.2439 -0.0223 -0.0313 -0.0247 88  ALA A CB  
649  N  N   . LEU A 89  ? 0.2356 0.0901 0.2219 0.0075  -0.0508 0.0206  89  LEU A N   
650  C  CA  . LEU A 89  ? 0.2322 0.0849 0.2281 -0.0044 -0.0560 0.0017  89  LEU A CA  
651  C  C   . LEU A 89  ? 0.2380 0.0862 0.2319 0.0067  -0.0571 0.0090  89  LEU A C   
652  O  O   . LEU A 89  ? 0.2508 0.0936 0.2293 0.0207  -0.0588 0.0003  89  LEU A O   
653  C  CB  . LEU A 89  ? 0.2138 0.0900 0.2309 0.0055  -0.0670 0.0133  89  LEU A CB  
654  C  CG  . LEU A 89  ? 0.1992 0.0942 0.2182 0.0108  -0.0493 -0.0085 89  LEU A CG  
655  C  CD1 . LEU A 89  ? 0.2435 0.1504 0.2710 -0.0079 0.0149  -0.0278 89  LEU A CD1 
656  C  CD2 . LEU A 89  ? 0.2292 0.1384 0.2493 0.0237  -0.0565 0.0617  89  LEU A CD2 
657  N  N   . GLU A 90  ? 0.2588 0.0809 0.2192 0.0237  -0.0502 -0.0006 90  GLU A N   
658  C  CA  . GLU A 90  ? 0.2742 0.0559 0.2149 0.0160  -0.0505 -0.0203 90  GLU A CA  
659  C  C   . GLU A 90  ? 0.2778 0.0904 0.1858 0.0003  -0.0593 -0.0229 90  GLU A C   
660  O  O   . GLU A 90  ? 0.2872 0.0922 0.1851 -0.0089 -0.0458 -0.0159 90  GLU A O   
661  C  CB  . GLU A 90  ? 0.2744 0.0860 0.2138 0.0097  -0.0468 0.0085  90  GLU A CB  
662  C  CG  . GLU A 90  ? 0.2648 0.0770 0.2394 0.0175  -0.0365 0.0216  90  GLU A CG  
663  C  CD  . GLU A 90  ? 0.2921 0.1039 0.2991 0.0266  -0.1072 -0.0053 90  GLU A CD  
664  O  OE1 . GLU A 90  ? 0.2959 0.1228 0.3377 0.0027  -0.1092 0.0601  90  GLU A OE1 
665  O  OE2 . GLU A 90  ? 0.2736 0.0979 0.2748 0.0384  -0.0845 -0.0176 90  GLU A OE2 
666  N  N   . GLN A 91  ? 0.2194 0.0777 0.2426 0.0277  -0.0833 -0.0232 91  GLN A N   
667  C  CA  . GLN A 91  ? 0.2223 0.1153 0.2097 0.0122  -0.0721 -0.0249 91  GLN A CA  
668  C  C   . GLN A 91  ? 0.2069 0.0997 0.2216 -0.0046 -0.0404 0.0036  91  GLN A C   
669  O  O   . GLN A 91  ? 0.2360 0.1050 0.2281 0.0200  -0.0192 0.0120  91  GLN A O   
670  C  CB  . GLN A 91  ? 0.2810 0.0753 0.2444 -0.0128 -0.0487 -0.0009 91  GLN A CB  
671  C  CG  . GLN A 91  ? 0.2861 0.0758 0.2564 -0.0073 0.0079  0.0339  91  GLN A CG  
672  C  CD  . GLN A 91  ? 0.3186 0.0348 0.2214 0.0495  0.0568  -0.0178 91  GLN A CD  
673  O  OE1 . GLN A 91  ? 0.3218 0.1601 0.2479 0.0272  0.0697  -0.0289 91  GLN A OE1 
674  N  NE2 . GLN A 91  ? 0.3075 0.0536 0.1691 0.0036  0.0195  -0.0221 91  GLN A NE2 
675  N  N   . ASP A 92  ? 0.2163 0.1064 0.2221 -0.0030 -0.0390 0.0085  92  ASP A N   
676  C  CA  . ASP A 92  ? 0.2462 0.0965 0.2501 0.0024  -0.0643 0.0052  92  ASP A CA  
677  C  C   . ASP A 92  ? 0.2517 0.1070 0.2472 0.0071  -0.0544 -0.0021 92  ASP A C   
678  O  O   . ASP A 92  ? 0.2541 0.1064 0.2678 0.0084  -0.0543 0.0073  92  ASP A O   
679  C  CB  . ASP A 92  ? 0.2299 0.1208 0.2461 0.0428  -0.0576 0.0037  92  ASP A CB  
680  C  CG  . ASP A 92  ? 0.2822 0.1467 0.2596 0.0080  -0.0543 -0.0118 92  ASP A CG  
681  O  OD1 . ASP A 92  ? 0.2844 0.0973 0.2517 -0.0036 -0.0648 -0.0122 92  ASP A OD1 
682  O  OD2 . ASP A 92  ? 0.2847 0.1316 0.2307 0.0230  -0.0390 -0.0201 92  ASP A OD2 
683  N  N   . LEU A 93  ? 0.2488 0.0605 0.2480 0.0434  -0.0785 0.0077  93  LEU A N   
684  C  CA  . LEU A 93  ? 0.1944 0.0804 0.2572 0.0477  -0.0526 -0.0065 93  LEU A CA  
685  C  C   . LEU A 93  ? 0.1955 0.1140 0.2537 0.0181  -0.0622 -0.0019 93  LEU A C   
686  O  O   . LEU A 93  ? 0.2765 0.1269 0.2670 0.0382  -0.0107 0.0029  93  LEU A O   
687  C  CB  . LEU A 93  ? 0.2399 0.1022 0.2499 0.0035  -0.0497 0.0048  93  LEU A CB  
688  C  CG  . LEU A 93  ? 0.2397 0.0873 0.2573 0.0373  -0.0533 0.0239  93  LEU A CG  
689  C  CD1 . LEU A 93  ? 0.1992 0.1664 0.3732 0.0338  -0.0461 0.0910  93  LEU A CD1 
690  C  CD2 . LEU A 93  ? 0.2429 0.1279 0.3136 0.0418  -0.1007 0.0204  93  LEU A CD2 
691  N  N   . ALA A 94  ? 0.2725 0.0969 0.2307 0.0171  -0.0513 -0.0225 94  ALA A N   
692  C  CA  . ALA A 94  ? 0.2700 0.1089 0.2387 0.0414  -0.0464 -0.0072 94  ALA A CA  
693  C  C   . ALA A 94  ? 0.2638 0.1307 0.2473 0.0538  -0.0400 -0.0017 94  ALA A C   
694  O  O   . ALA A 94  ? 0.2854 0.1426 0.2731 0.0184  -0.0082 -0.0132 94  ALA A O   
695  C  CB  . ALA A 94  ? 0.2278 0.0915 0.2871 0.0215  -0.0308 0.0019  94  ALA A CB  
696  N  N   . PHE A 95  ? 0.2448 0.1002 0.2649 0.0016  -0.0216 -0.0033 95  PHE A N   
697  C  CA  . PHE A 95  ? 0.2677 0.1403 0.3476 0.0115  -0.0611 -0.0673 95  PHE A CA  
698  C  C   . PHE A 95  ? 0.2463 0.1779 0.2974 0.0458  -0.0241 -0.0508 95  PHE A C   
699  O  O   . PHE A 95  ? 0.2362 0.2668 0.3363 0.0613  -0.0231 -0.0658 95  PHE A O   
700  C  CB  . PHE A 95  ? 0.2649 0.1768 0.3382 -0.0013 -0.0312 -0.0797 95  PHE A CB  
701  C  CG  . PHE A 95  ? 0.2579 0.2874 0.3334 -0.0682 -0.0346 -0.0547 95  PHE A CG  
702  C  CD1 . PHE A 95  ? 0.3111 0.4406 0.4146 -0.1218 0.0037  -0.0199 95  PHE A CD1 
703  C  CD2 . PHE A 95  ? 0.2835 0.3178 0.2981 -0.0495 -0.0625 -0.0838 95  PHE A CD2 
704  C  CE1 . PHE A 95  ? 0.2822 0.5540 0.4699 -0.1268 0.0296  -0.0458 95  PHE A CE1 
705  C  CE2 . PHE A 95  ? 0.2828 0.4858 0.2936 -0.0221 -0.0518 -0.1012 95  PHE A CE2 
706  C  CZ  . PHE A 95  ? 0.2998 0.5820 0.3734 -0.1195 -0.0506 -0.1405 95  PHE A CZ  
707  N  N   . TRP A 96  ? 0.3047 0.1870 0.2546 0.0601  -0.0300 -0.0311 96  TRP A N   
708  C  CA  . TRP A 96  ? 0.2319 0.1824 0.3188 0.0589  -0.0341 -0.0432 96  TRP A CA  
709  C  C   . TRP A 96  ? 0.2130 0.1872 0.3220 0.0469  -0.0299 -0.0452 96  TRP A C   
710  O  O   . TRP A 96  ? 0.2801 0.2454 0.3584 0.1100  -0.0856 -0.1015 96  TRP A O   
711  C  CB  . TRP A 96  ? 0.2870 0.1474 0.3003 0.0502  -0.0536 -0.0305 96  TRP A CB  
712  C  CG  . TRP A 96  ? 0.3032 0.2032 0.3062 0.0978  -0.0883 -0.0465 96  TRP A CG  
713  C  CD1 . TRP A 96  ? 0.3350 0.1756 0.2545 0.1073  -0.0910 -0.0165 96  TRP A CD1 
714  C  CD2 . TRP A 96  ? 0.3115 0.2540 0.3020 0.0990  -0.0921 -0.0411 96  TRP A CD2 
715  N  NE1 . TRP A 96  ? 0.3098 0.1550 0.2919 0.0557  -0.0797 -0.0160 96  TRP A NE1 
716  C  CE2 . TRP A 96  ? 0.3278 0.2541 0.3292 0.0955  -0.1096 -0.0577 96  TRP A CE2 
717  C  CE3 . TRP A 96  ? 0.3438 0.3921 0.3194 0.1703  -0.1498 -0.1019 96  TRP A CE3 
718  C  CZ2 . TRP A 96  ? 0.3760 0.2804 0.4249 0.1305  -0.1780 -0.1128 96  TRP A CZ2 
719  C  CZ3 . TRP A 96  ? 0.3850 0.4313 0.4549 0.1914  -0.2199 -0.1939 96  TRP A CZ3 
720  C  CH2 . TRP A 96  ? 0.3566 0.4138 0.4099 0.1427  -0.1730 -0.1575 96  TRP A CH2 
721  N  N   . TYR A 97  ? 0.2226 0.1467 0.3119 0.0369  -0.0285 -0.0219 97  TYR A N   
722  C  CA  . TYR A 97  ? 0.2831 0.1217 0.3108 0.0466  -0.0595 -0.0069 97  TYR A CA  
723  C  C   . TYR A 97  ? 0.3424 0.1102 0.3103 0.0298  -0.0812 -0.0122 97  TYR A C   
724  O  O   . TYR A 97  ? 0.4118 0.1270 0.3171 -0.0255 0.0018  -0.0308 97  TYR A O   
725  C  CB  . TYR A 97  ? 0.2674 0.1099 0.3216 0.0572  -0.0981 -0.0013 97  TYR A CB  
726  C  CG  . TYR A 97  ? 0.2553 0.1281 0.3225 0.0772  -0.0309 -0.0018 97  TYR A CG  
727  C  CD1 . TYR A 97  ? 0.3353 0.1207 0.2915 0.0734  -0.0280 0.0087  97  TYR A CD1 
728  C  CD2 . TYR A 97  ? 0.2596 0.1430 0.3106 0.0521  -0.0718 -0.0347 97  TYR A CD2 
729  C  CE1 . TYR A 97  ? 0.3177 0.1331 0.2656 0.0395  -0.0425 0.0012  97  TYR A CE1 
730  C  CE2 . TYR A 97  ? 0.2288 0.1712 0.3135 0.0556  -0.0310 -0.0244 97  TYR A CE2 
731  C  CZ  . TYR A 97  ? 0.3322 0.1644 0.2645 0.0561  -0.0603 -0.0118 97  TYR A CZ  
732  O  OH  . TYR A 97  ? 0.3079 0.2061 0.2621 0.0644  -0.0498 0.0104  97  TYR A OH  
733  N  N   . GLY A 98  ? 0.3479 0.1099 0.3037 0.0197  0.0158  -0.0275 98  GLY A N   
734  C  CA  . GLY A 98  ? 0.3452 0.1468 0.3232 0.0506  0.0645  -0.0045 98  GLY A CA  
735  C  C   . GLY A 98  ? 0.3709 0.1011 0.2855 0.0053  0.0320  -0.0092 98  GLY A C   
736  O  O   . GLY A 98  ? 0.3506 0.1070 0.2593 0.0332  0.0101  0.0056  98  GLY A O   
737  N  N   . PRO A 99  ? 0.4215 0.1572 0.2509 0.0000  0.0410  -0.0343 99  PRO A N   
738  C  CA  . PRO A 99  ? 0.4423 0.2136 0.3004 0.0043  0.0500  0.0707  99  PRO A CA  
739  C  C   . PRO A 99  ? 0.4072 0.2153 0.2870 0.0455  0.0142  0.0022  99  PRO A C   
740  O  O   . PRO A 99  ? 0.4320 0.1713 0.2358 0.0743  -0.0162 0.0199  99  PRO A O   
741  C  CB  . PRO A 99  ? 0.4633 0.2553 0.3034 0.1058  0.1261  0.0642  99  PRO A CB  
742  C  CG  . PRO A 99  ? 0.4441 0.3774 0.3309 0.0591  0.0764  0.0979  99  PRO A CG  
743  C  CD  . PRO A 99  ? 0.4445 0.2646 0.2746 0.0170  0.0638  0.0171  99  PRO A CD  
744  N  N   . ARG A 100 ? 0.3329 0.2319 0.3283 0.0499  0.0303  -0.0101 100 ARG A N   
745  C  CA  . ARG A 100 ? 0.3965 0.2419 0.2379 0.0200  0.0394  -0.0393 100 ARG A CA  
746  C  C   . ARG A 100 ? 0.4042 0.1643 0.2364 0.0520  -0.0210 -0.0195 100 ARG A C   
747  O  O   . ARG A 100 ? 0.4152 0.1525 0.2441 0.0744  -0.0370 -0.0356 100 ARG A O   
748  C  CB  . ARG A 100 ? 0.4607 0.3554 0.2841 0.0808  0.0341  -0.0988 100 ARG A CB  
749  C  CG  . ARG A 100 ? 0.6228 0.4756 0.2704 0.0157  0.1230  -0.0847 100 ARG A CG  
750  C  CD  . ARG A 100 ? 0.7045 0.5150 0.3519 -0.0505 0.1780  -0.1703 100 ARG A CD  
751  N  NE  . ARG A 100 ? 0.8848 0.5392 0.4455 -0.1159 0.0795  -0.1693 100 ARG A NE  
752  C  CZ  . ARG A 100 ? 0.9014 0.5325 0.5448 -0.1149 0.1216  -0.2325 100 ARG A CZ  
753  N  NH1 . ARG A 100 ? 0.9910 0.6108 0.6553 -0.1687 0.2251  -0.3000 100 ARG A NH1 
754  N  NH2 . ARG A 100 ? 0.9139 0.6125 0.5130 -0.1346 0.0704  -0.2314 100 ARG A NH2 
755  N  N   . TRP A 101 ? 0.3409 0.1402 0.2374 0.0162  0.0015  -0.0095 101 TRP A N   
756  C  CA  . TRP A 101 ? 0.3082 0.1354 0.2334 0.0254  -0.0317 0.0049  101 TRP A CA  
757  C  C   . TRP A 101 ? 0.2884 0.1362 0.2111 0.0429  -0.0245 -0.0011 101 TRP A C   
758  O  O   . TRP A 101 ? 0.3006 0.1565 0.2563 0.0065  -0.0808 0.0305  101 TRP A O   
759  C  CB  . TRP A 101 ? 0.3008 0.1308 0.2255 0.0366  -0.0400 0.0109  101 TRP A CB  
760  C  CG  . TRP A 101 ? 0.2819 0.1062 0.2347 0.0154  -0.0579 0.0146  101 TRP A CG  
761  C  CD1 . TRP A 101 ? 0.3208 0.1020 0.2919 0.0033  -0.0266 0.0206  101 TRP A CD1 
762  C  CD2 . TRP A 101 ? 0.2652 0.1146 0.2005 0.0163  -0.0839 0.0174  101 TRP A CD2 
763  N  NE1 . TRP A 101 ? 0.2985 0.0874 0.2572 -0.0029 -0.0916 0.0058  101 TRP A NE1 
764  C  CE2 . TRP A 101 ? 0.2902 0.0819 0.2366 0.0107  -0.0775 -0.0286 101 TRP A CE2 
765  C  CE3 . TRP A 101 ? 0.2621 0.1223 0.2184 0.0000  -0.0731 0.0005  101 TRP A CE3 
766  C  CZ2 . TRP A 101 ? 0.3056 0.1034 0.2174 0.0279  -0.0763 -0.0322 101 TRP A CZ2 
767  C  CZ3 . TRP A 101 ? 0.2389 0.1420 0.2291 0.0078  -0.0956 0.0060  101 TRP A CZ3 
768  C  CH2 . TRP A 101 ? 0.2689 0.1391 0.2454 0.0169  -0.0949 0.0005  101 TRP A CH2 
769  N  N   . GLN A 102 ? 0.3406 0.1458 0.2732 0.0323  -0.0954 0.0016  102 GLN A N   
770  C  CA  . GLN A 102 ? 0.3142 0.1674 0.2418 0.0491  -0.0837 0.0113  102 GLN A CA  
771  C  C   . GLN A 102 ? 0.3316 0.1537 0.2503 0.0254  -0.1170 0.0283  102 GLN A C   
772  O  O   . GLN A 102 ? 0.3954 0.2154 0.3477 -0.0422 -0.0816 0.0146  102 GLN A O   
773  C  CB  . GLN A 102 ? 0.3601 0.1883 0.3175 0.0674  -0.1207 0.0237  102 GLN A CB  
774  C  CG  . GLN A 102 ? 0.4309 0.2218 0.3081 0.1264  -0.0636 0.0518  102 GLN A CG  
775  C  CD  . GLN A 102 ? 0.4132 0.1556 0.4204 0.0683  -0.0457 0.0264  102 GLN A CD  
776  O  OE1 . GLN A 102 ? 0.7439 0.2201 0.3115 -0.0773 -0.1422 0.0551  102 GLN A OE1 
777  N  NE2 . GLN A 102 ? 0.2718 0.2611 0.7976 0.0127  -0.0756 -0.2454 102 GLN A NE2 
778  N  N   . GLU A 103 ? 0.3802 0.1447 0.2594 0.0048  -0.0986 -0.0257 103 GLU A N   
779  C  CA  . GLU A 103 ? 0.4407 0.1621 0.3390 0.0020  -0.1274 -0.0680 103 GLU A CA  
780  C  C   . GLU A 103 ? 0.4098 0.1578 0.3244 0.0256  -0.0685 -0.0676 103 GLU A C   
781  O  O   . GLU A 103 ? 0.5784 0.1556 0.3934 0.0273  -0.1619 -0.0689 103 GLU A O   
782  C  CB  . GLU A 103 ? 0.5385 0.2402 0.3001 0.0760  -0.1415 -0.1006 103 GLU A CB  
783  C  CG  . GLU A 103 ? 0.5442 0.2714 0.3417 0.0608  -0.1574 -0.0578 103 GLU A CG  
784  C  CD  . GLU A 103 ? 0.6766 0.3100 0.3921 0.0469  -0.1074 0.0030  103 GLU A CD  
785  O  OE1 . GLU A 103 ? 0.8086 0.2663 0.4689 0.0985  0.0863  0.0355  103 GLU A OE1 
786  O  OE2 . GLU A 103 ? 0.7342 0.3468 0.4144 -0.0316 -0.1562 -0.0100 103 GLU A OE2 
787  N  N   . VAL A 104 ? 0.3962 0.1545 0.2469 0.0541  -0.0383 -0.0505 104 VAL A N   
788  C  CA  . VAL A 104 ? 0.4014 0.1544 0.2793 0.0779  -0.0244 -0.0523 104 VAL A CA  
789  C  C   . VAL A 104 ? 0.3327 0.0876 0.2782 0.0188  -0.0410 -0.0379 104 VAL A C   
790  O  O   . VAL A 104 ? 0.3000 0.1381 0.3544 0.0477  -0.0137 0.0112  104 VAL A O   
791  C  CB  . VAL A 104 ? 0.4105 0.1625 0.3018 0.1019  0.0126  0.0278  104 VAL A CB  
792  C  CG1 . VAL A 104 ? 0.5244 0.4207 0.3081 0.0866  0.0370  0.0160  104 VAL A CG1 
793  C  CG2 . VAL A 104 ? 0.3978 0.1641 0.4107 0.0703  -0.0432 0.0506  104 VAL A CG2 
794  N  N   . ILE A 105 ? 0.2745 0.0838 0.2585 -0.0011 -0.0160 -0.0035 105 ILE A N   
795  C  CA  . ILE A 105 ? 0.2611 0.1200 0.2604 -0.0164 -0.0146 0.0070  105 ILE A CA  
796  C  C   . ILE A 105 ? 0.2747 0.1195 0.2358 -0.0208 -0.0555 0.0116  105 ILE A C   
797  O  O   . ILE A 105 ? 0.3115 0.1315 0.3242 -0.0174 -0.1147 -0.0118 105 ILE A O   
798  C  CB  . ILE A 105 ? 0.2981 0.1302 0.2369 0.0019  -0.0311 -0.0029 105 ILE A CB  
799  C  CG1 . ILE A 105 ? 0.2937 0.1283 0.3079 0.0119  -0.0415 -0.0279 105 ILE A CG1 
800  C  CG2 . ILE A 105 ? 0.2928 0.1270 0.2559 0.0116  -0.0430 -0.0056 105 ILE A CG2 
801  C  CD1 . ILE A 105 ? 0.3334 0.0857 0.3474 0.0137  0.0025  0.0050  105 ILE A CD1 
802  N  N   . PRO A 106 ? 0.3028 0.0785 0.2444 0.0163  -0.0610 -0.0096 106 PRO A N   
803  C  CA  . PRO A 106 ? 0.2883 0.0563 0.3030 0.0440  -0.0636 0.0090  106 PRO A CA  
804  C  C   . PRO A 106 ? 0.2836 0.0828 0.2676 0.0227  -0.0709 0.0148  106 PRO A C   
805  O  O   . PRO A 106 ? 0.2274 0.1060 0.3086 0.0166  -0.0608 -0.0111 106 PRO A O   
806  C  CB  . PRO A 106 ? 0.2921 0.1558 0.2967 0.0466  -0.0434 0.0635  106 PRO A CB  
807  C  CG  . PRO A 106 ? 0.2889 0.2413 0.3054 -0.0161 -0.0789 0.0918  106 PRO A CG  
808  C  CD  . PRO A 106 ? 0.2183 0.1553 0.2643 0.0403  -0.0290 0.0273  106 PRO A CD  
809  N  N   . TYR A 107 ? 0.2847 0.0879 0.3062 0.0201  -0.0882 0.0131  107 TYR A N   
810  C  CA  . TYR A 107 ? 0.2893 0.1002 0.2917 -0.0005 -0.0904 0.0266  107 TYR A CA  
811  C  C   . TYR A 107 ? 0.3091 0.0984 0.2915 -0.0094 -0.1251 0.0304  107 TYR A C   
812  O  O   . TYR A 107 ? 0.3695 0.1083 0.3030 -0.0054 -0.1223 -0.0010 107 TYR A O   
813  C  CB  . TYR A 107 ? 0.2888 0.0758 0.3074 0.0462  -0.0795 0.0101  107 TYR A CB  
814  C  CG  . TYR A 107 ? 0.2838 0.1876 0.2792 -0.0010 -0.0752 0.0149  107 TYR A CG  
815  C  CD1 . TYR A 107 ? 0.2777 0.1043 0.3184 -0.0075 -0.0690 -0.0185 107 TYR A CD1 
816  C  CD2 . TYR A 107 ? 0.2985 0.2037 0.2696 -0.0310 -0.0664 0.0100  107 TYR A CD2 
817  C  CE1 . TYR A 107 ? 0.2848 0.1267 0.2960 -0.0057 -0.0610 0.0288  107 TYR A CE1 
818  C  CE2 . TYR A 107 ? 0.2865 0.1728 0.2968 -0.0091 -0.0731 0.0278  107 TYR A CE2 
819  C  CZ  . TYR A 107 ? 0.2783 0.1515 0.3332 -0.0037 -0.0547 -0.0113 107 TYR A CZ  
820  O  OH  . TYR A 107 ? 0.2801 0.2180 0.3568 0.0224  -0.0533 -0.0033 107 TYR A OH  
821  N  N   . THR A 108 ? 0.2903 0.0937 0.2720 0.0312  -0.0924 0.0109  108 THR A N   
822  C  CA  . THR A 108 ? 0.2640 0.1058 0.2581 0.0106  -0.0835 0.0253  108 THR A CA  
823  C  C   . THR A 108 ? 0.2491 0.0829 0.3060 -0.0135 -0.0826 -0.0389 108 THR A C   
824  O  O   . THR A 108 ? 0.2757 0.0824 0.3144 0.0088  -0.0612 -0.0040 108 THR A O   
825  C  CB  . THR A 108 ? 0.2579 0.0451 0.2870 -0.0196 -0.0952 0.0145  108 THR A CB  
826  O  OG1 . THR A 108 ? 0.3189 0.0929 0.2933 -0.0435 -0.0779 -0.0127 108 THR A OG1 
827  C  CG2 . THR A 108 ? 0.2802 0.1040 0.3224 -0.0562 -0.0772 -0.0096 108 THR A CG2 
828  N  N   . PRO A 109 ? 0.2452 0.0863 0.3383 -0.0024 -0.0608 -0.0282 109 PRO A N   
829  C  CA  . PRO A 109 ? 0.2654 0.0819 0.3343 -0.0085 -0.0590 -0.0237 109 PRO A CA  
830  C  C   . PRO A 109 ? 0.2382 0.0801 0.3182 -0.0086 -0.0696 -0.0025 109 PRO A C   
831  O  O   . PRO A 109 ? 0.2345 0.1219 0.3302 -0.0258 -0.0513 -0.0084 109 PRO A O   
832  C  CB  . PRO A 109 ? 0.3046 0.1002 0.3360 0.0287  -0.0173 0.0037  109 PRO A CB  
833  C  CG  . PRO A 109 ? 0.3146 0.0894 0.3329 -0.0233 -0.0193 -0.0387 109 PRO A CG  
834  C  CD  . PRO A 109 ? 0.2792 0.0790 0.3151 -0.0071 -0.0518 -0.0259 109 PRO A CD  
835  N  N   . ALA A 110 ? 0.2441 0.0871 0.3072 0.0054  -0.0760 0.0040  110 ALA A N   
836  C  CA  . ALA A 110 ? 0.2810 0.0842 0.2838 -0.0190 -0.0630 0.0254  110 ALA A CA  
837  C  C   . ALA A 110 ? 0.2868 0.0842 0.2636 -0.0096 -0.0649 0.0050  110 ALA A C   
838  O  O   . ALA A 110 ? 0.3043 0.1314 0.2777 0.0031  -0.0389 0.0064  110 ALA A O   
839  C  CB  . ALA A 110 ? 0.2817 0.1721 0.2730 0.0473  -0.0564 -0.0309 110 ALA A CB  
840  N  N   . MET A 111 ? 0.2574 0.0713 0.2639 0.0171  -0.0625 -0.0015 111 MET A N   
841  C  CA  . MET A 111 ? 0.2493 0.0812 0.2645 0.0258  -0.0612 0.0101  111 MET A CA  
842  C  C   . MET A 111 ? 0.2499 0.1057 0.2789 0.0252  -0.0667 -0.0218 111 MET A C   
843  O  O   . MET A 111 ? 0.2257 0.1110 0.3061 -0.0021 -0.0230 -0.0270 111 MET A O   
844  C  CB  . MET A 111 ? 0.2886 0.0763 0.2540 -0.0159 -0.0580 -0.0158 111 MET A CB  
845  C  CG  . MET A 111 ? 0.2918 0.1114 0.2662 -0.0331 -0.0736 0.0220  111 MET A CG  
846  S  SD  . MET A 111 ? 0.2964 0.0946 0.2803 -0.0060 -0.0471 -0.0043 111 MET A SD  
847  C  CE  . MET A 111 ? 0.2987 0.1741 0.2418 -0.0248 -0.0665 -0.0004 111 MET A CE  
848  N  N   . GLN A 112 ? 0.2823 0.1128 0.2786 0.0094  -0.0597 -0.0245 112 GLN A N   
849  C  CA  . GLN A 112 ? 0.2971 0.1353 0.2935 -0.0053 -0.0740 -0.0442 112 GLN A CA  
850  C  C   . GLN A 112 ? 0.2707 0.1154 0.3107 0.0126  -0.0693 -0.0400 112 GLN A C   
851  O  O   . GLN A 112 ? 0.2683 0.1387 0.3995 0.0126  -0.0747 -0.0387 112 GLN A O   
852  C  CB  . GLN A 112 ? 0.2629 0.0925 0.3328 0.0028  -0.0426 -0.0398 112 GLN A CB  
853  C  CG  . GLN A 112 ? 0.3886 0.1169 0.2978 0.0084  -0.0420 -0.0244 112 GLN A CG  
854  C  CD  . GLN A 112 ? 0.3338 0.1436 0.3386 -0.0145 -0.0050 -0.0527 112 GLN A CD  
855  O  OE1 . GLN A 112 ? 0.3990 0.1880 0.3195 0.0033  0.0417  0.0069  112 GLN A OE1 
856  N  NE2 . GLN A 112 ? 0.2457 0.1507 0.4433 -0.0034 -0.0320 -0.1079 112 GLN A NE2 
857  N  N   . ARG A 113 ? 0.2901 0.0982 0.3616 0.0080  -0.0435 0.0035  113 ARG A N   
858  C  CA  . ARG A 113 ? 0.2463 0.0941 0.3687 -0.0125 -0.0637 0.0086  113 ARG A CA  
859  C  C   . ARG A 113 ? 0.2405 0.0953 0.3312 -0.0139 -0.0457 0.0321  113 ARG A C   
860  O  O   . ARG A 113 ? 0.2409 0.1604 0.4202 -0.0085 -0.0378 -0.0189 113 ARG A O   
861  C  CB  . ARG A 113 ? 0.3370 0.1161 0.3569 0.0343  -0.0621 0.0085  113 ARG A CB  
862  C  CG  . ARG A 113 ? 0.4956 0.2900 0.5438 -0.0441 -0.0452 0.1882  113 ARG A CG  
863  C  CD  . ARG A 113 ? 0.5899 0.2844 0.7013 -0.0161 0.0156  0.2222  113 ARG A CD  
864  N  NE  . ARG A 113 ? 0.6140 0.3474 0.7934 0.0356  -0.0014 0.1726  113 ARG A NE  
865  C  CZ  . ARG A 113 ? 0.6131 0.4189 0.7947 0.0918  -0.0417 0.1008  113 ARG A CZ  
866  N  NH1 . ARG A 113 ? 0.7661 0.4861 0.6197 -0.0792 -0.1019 0.2711  113 ARG A NH1 
867  N  NH2 . ARG A 113 ? 0.7822 0.4221 1.0735 0.4067  -0.1059 0.1553  113 ARG A NH2 
868  N  N   . TYR A 114 ? 0.2801 0.1060 0.2943 -0.0417 -0.0076 0.0070  114 TYR A N   
869  C  CA  . TYR A 114 ? 0.2371 0.1229 0.2756 -0.0171 -0.0396 0.0063  114 TYR A CA  
870  C  C   . TYR A 114 ? 0.2090 0.1664 0.2751 -0.0067 -0.0424 0.0019  114 TYR A C   
871  O  O   . TYR A 114 ? 0.2088 0.1682 0.2866 -0.0171 -0.0298 -0.0073 114 TYR A O   
872  C  CB  . TYR A 114 ? 0.2346 0.1279 0.2944 -0.0041 -0.0722 -0.0031 114 TYR A CB  
873  C  CG  . TYR A 114 ? 0.2295 0.1225 0.2463 -0.0095 -0.0502 0.0165  114 TYR A CG  
874  C  CD1 . TYR A 114 ? 0.2506 0.1238 0.2928 0.0399  -0.1057 0.0128  114 TYR A CD1 
875  C  CD2 . TYR A 114 ? 0.2367 0.1209 0.2483 -0.0009 -0.0518 0.0049  114 TYR A CD2 
876  C  CE1 . TYR A 114 ? 0.2318 0.1041 0.3681 0.0074  -0.0501 -0.0059 114 TYR A CE1 
877  C  CE2 . TYR A 114 ? 0.2244 0.0810 0.3019 -0.0171 -0.0412 0.0069  114 TYR A CE2 
878  C  CZ  . TYR A 114 ? 0.2345 0.1016 0.2948 -0.0182 -0.0223 0.0002  114 TYR A CZ  
879  O  OH  . TYR A 114 ? 0.2970 0.1151 0.3222 0.0021  -0.0402 -0.0248 114 TYR A OH  
880  N  N   . VAL A 115 ? 0.2287 0.1179 0.2764 0.0160  -0.0333 0.0001  115 VAL A N   
881  C  CA  . VAL A 115 ? 0.2490 0.1418 0.3140 -0.0170 -0.0826 0.0244  115 VAL A CA  
882  C  C   . VAL A 115 ? 0.2538 0.1105 0.3013 -0.0096 -0.0801 -0.0042 115 VAL A C   
883  O  O   . VAL A 115 ? 0.2510 0.1161 0.3439 -0.0077 -0.0506 -0.0263 115 VAL A O   
884  C  CB  . VAL A 115 ? 0.2505 0.0790 0.3015 -0.0293 -0.0996 0.0109  115 VAL A CB  
885  C  CG1 . VAL A 115 ? 0.3282 0.1356 0.3328 -0.0069 -0.1369 0.0314  115 VAL A CG1 
886  C  CG2 . VAL A 115 ? 0.2838 0.0907 0.3847 -0.0514 -0.0762 0.0585  115 VAL A CG2 
887  N  N   . LYS A 116 ? 0.2533 0.1159 0.3380 -0.0062 -0.0493 -0.0128 116 LYS A N   
888  C  CA  . LYS A 116 ? 0.2699 0.1053 0.3604 -0.0168 -0.0444 -0.0462 116 LYS A CA  
889  C  C   . LYS A 116 ? 0.2710 0.1904 0.3655 -0.0140 -0.0241 -0.0208 116 LYS A C   
890  O  O   . LYS A 116 ? 0.2582 0.1786 0.3595 -0.0342 -0.0231 -0.0055 116 LYS A O   
891  C  CB  . LYS A 116 ? 0.3252 0.1037 0.5097 -0.0118 -0.0819 -0.0390 116 LYS A CB  
892  C  CG  . LYS A 116 ? 0.4838 0.2208 0.6886 -0.2067 -0.1193 -0.0479 116 LYS A CG  
893  C  CD  . LYS A 116 ? 0.6228 0.2145 0.9138 -0.2226 -0.1201 -0.0831 116 LYS A CD  
894  C  CE  . LYS A 116 ? 0.7795 0.2448 1.0759 -0.3327 -0.0405 -0.1295 116 LYS A CE  
895  N  NZ  . LYS A 116 ? 0.7073 0.2747 1.5027 -0.2684 0.2251  -0.0634 116 LYS A NZ  
896  N  N   . ARG A 117 ? 0.2436 0.1167 0.3562 -0.0114 -0.0076 -0.0201 117 ARG A N   
897  C  CA  . ARG A 117 ? 0.2524 0.1277 0.3539 0.0022  0.0043  0.0185  117 ARG A CA  
898  C  C   . ARG A 117 ? 0.2069 0.1320 0.2974 -0.0104 0.0226  0.0136  117 ARG A C   
899  O  O   . ARG A 117 ? 0.1861 0.1770 0.3390 -0.0025 0.0096  0.0032  117 ARG A O   
900  C  CB  . ARG A 117 ? 0.2656 0.1475 0.3548 -0.0274 0.0064  0.0636  117 ARG A CB  
901  C  CG  . ARG A 117 ? 0.2400 0.1975 0.3572 -0.0083 -0.0134 0.0348  117 ARG A CG  
902  C  CD  . ARG A 117 ? 0.2292 0.2097 0.4370 0.0047  0.0300  0.0269  117 ARG A CD  
903  N  NE  . ARG A 117 ? 0.1970 0.1616 0.4168 0.0041  -0.0174 -0.0023 117 ARG A NE  
904  C  CZ  . ARG A 117 ? 0.2241 0.1860 0.3307 -0.0669 0.0066  0.0144  117 ARG A CZ  
905  N  NH1 . ARG A 117 ? 0.2707 0.1859 0.3045 -0.0260 0.0163  0.0614  117 ARG A NH1 
906  N  NH2 . ARG A 117 ? 0.2675 0.2424 0.3511 -0.0994 -0.0126 0.0079  117 ARG A NH2 
907  N  N   . LEU A 118 ? 0.2017 0.1433 0.3149 0.0004  0.0112  0.0505  118 LEU A N   
908  C  CA  . LEU A 118 ? 0.2363 0.1387 0.2834 -0.0028 -0.0277 0.0517  118 LEU A CA  
909  C  C   . LEU A 118 ? 0.2344 0.1315 0.3448 0.0085  -0.0578 -0.0084 118 LEU A C   
910  O  O   . LEU A 118 ? 0.2448 0.1278 0.3615 0.0186  -0.0258 0.0246  118 LEU A O   
911  C  CB  . LEU A 118 ? 0.2136 0.1072 0.2795 0.0208  -0.0075 0.0184  118 LEU A CB  
912  C  CG  . LEU A 118 ? 0.2406 0.0861 0.2763 0.0091  -0.0223 0.0363  118 LEU A CG  
913  C  CD1 . LEU A 118 ? 0.2442 0.1305 0.2767 -0.0292 -0.0342 0.0298  118 LEU A CD1 
914  C  CD2 . LEU A 118 ? 0.2656 0.1739 0.3136 0.0457  -0.0449 -0.0208 118 LEU A CD2 
915  N  N   . HIS A 119 ? 0.2503 0.1650 0.3107 -0.0142 -0.0326 0.0091  119 HIS A N   
916  C  CA  . HIS A 119 ? 0.2909 0.2341 0.3315 -0.0285 -0.0703 0.0041  119 HIS A CA  
917  C  C   . HIS A 119 ? 0.2604 0.2235 0.3366 -0.0185 -0.0839 -0.0029 119 HIS A C   
918  O  O   . HIS A 119 ? 0.2670 0.2958 0.3811 0.0056  -0.1124 0.0050  119 HIS A O   
919  C  CB  . HIS A 119 ? 0.2835 0.1648 0.3403 -0.0043 -0.0721 0.0070  119 HIS A CB  
920  C  CG  . HIS A 119 ? 0.2562 0.1630 0.3265 -0.0116 -0.0846 -0.0065 119 HIS A CG  
921  N  ND1 . HIS A 119 ? 0.2603 0.1713 0.3528 0.0005  -0.0679 0.0137  119 HIS A ND1 
922  C  CD2 . HIS A 119 ? 0.2605 0.1633 0.3146 -0.0059 -0.0910 -0.0169 119 HIS A CD2 
923  C  CE1 . HIS A 119 ? 0.2449 0.1763 0.3149 -0.0013 -0.0914 0.0122  119 HIS A CE1 
924  N  NE2 . HIS A 119 ? 0.2491 0.1883 0.3367 0.0007  -0.0832 0.0098  119 HIS A NE2 
925  N  N   . GLU A 120 ? 0.2903 0.2403 0.3184 -0.0144 -0.0614 0.0107  120 GLU A N   
926  C  CA  . GLU A 120 ? 0.3043 0.2802 0.3660 -0.0401 -0.0544 0.0227  120 GLU A CA  
927  C  C   . GLU A 120 ? 0.2622 0.3097 0.3933 -0.0347 -0.0287 0.0183  120 GLU A C   
928  O  O   . GLU A 120 ? 0.2587 0.3149 0.3862 -0.0254 -0.0587 0.0505  120 GLU A O   
929  C  CB  . GLU A 120 ? 0.3170 0.2679 0.4700 -0.0659 -0.0557 0.0504  120 GLU A CB  
930  C  CG  . GLU A 120 ? 0.3789 0.2916 0.6631 -0.0200 -0.1308 -0.0429 120 GLU A CG  
931  C  CD  . GLU A 120 ? 0.6325 0.2786 0.7114 0.0022  -0.1581 -0.0267 120 GLU A CD  
932  O  OE1 . GLU A 120 ? 0.6774 0.1923 0.7482 -0.0879 -0.2617 -0.0238 120 GLU A OE1 
933  O  OE2 . GLU A 120 ? 0.9440 0.1941 0.6861 -0.0967 -0.0939 0.0232  120 GLU A OE2 
934  N  N   . VAL A 121 ? 0.2283 0.2474 0.3857 -0.0341 0.0117  0.0062  121 VAL A N   
935  C  CA  . VAL A 121 ? 0.2098 0.2750 0.3343 0.0190  0.0012  0.0482  121 VAL A CA  
936  C  C   . VAL A 121 ? 0.2095 0.2919 0.3789 0.0248  -0.0257 0.0584  121 VAL A C   
937  O  O   . VAL A 121 ? 0.2056 0.2419 0.3993 0.0011  -0.0368 0.0057  121 VAL A O   
938  C  CB  . VAL A 121 ? 0.1975 0.2001 0.3773 0.0573  -0.0104 0.0086  121 VAL A CB  
939  C  CG1 . VAL A 121 ? 0.2505 0.2000 0.3091 0.0606  0.0492  0.0467  121 VAL A CG1 
940  C  CG2 . VAL A 121 ? 0.1715 0.1822 0.3996 0.0123  -0.0337 0.0128  121 VAL A CG2 
941  N  N   . GLY A 122 ? 0.2242 0.2427 0.3867 0.0158  -0.0320 0.0554  122 GLY A N   
942  C  CA  . GLY A 122 ? 0.2287 0.2006 0.4489 -0.0097 -0.0588 0.0328  122 GLY A CA  
943  C  C   . GLY A 122 ? 0.2674 0.2340 0.4714 0.0220  -0.1063 0.0221  122 GLY A C   
944  O  O   . GLY A 122 ? 0.2608 0.2228 0.5306 0.0198  -0.0593 0.1212  122 GLY A O   
945  N  N   . ARG A 123 ? 0.2785 0.2951 0.4120 -0.0131 -0.0737 -0.0098 123 ARG A N   
946  C  CA  . ARG A 123 ? 0.2723 0.4096 0.4182 -0.0109 -0.0620 -0.0606 123 ARG A CA  
947  C  C   . ARG A 123 ? 0.2470 0.4212 0.4588 -0.0038 -0.0769 -0.0240 123 ARG A C   
948  O  O   . ARG A 123 ? 0.2596 0.4127 0.4493 0.0070  -0.0818 0.0094  123 ARG A O   
949  C  CB  . ARG A 123 ? 0.2960 0.5583 0.4609 0.0343  -0.0950 -0.1480 123 ARG A CB  
950  C  CG  . ARG A 123 ? 0.4509 0.7781 0.5413 0.1053  0.0743  -0.0853 123 ARG A CG  
951  C  CD  . ARG A 123 ? 0.7517 1.0747 0.5084 0.1457  0.0648  -0.1070 123 ARG A CD  
952  N  NE  . ARG A 123 ? 0.9280 1.3268 0.5796 0.2187  0.2210  -0.0843 123 ARG A NE  
953  C  CZ  . ARG A 123 ? 1.0434 1.5221 0.5511 0.2115  0.1643  0.0058  123 ARG A CZ  
954  N  NH1 . ARG A 123 ? 1.0957 1.8449 0.5421 0.1261  -0.0269 0.1636  123 ARG A NH1 
955  N  NH2 . ARG A 123 ? 1.1855 1.7165 0.5855 0.1827  0.2613  0.0132  123 ARG A NH2 
956  N  N   . THR A 124 ? 0.1761 0.3762 0.4645 -0.0115 -0.0779 -0.0401 124 THR A N   
957  C  CA  . THR A 124 ? 0.2385 0.3718 0.5173 -0.0408 -0.0405 -0.0451 124 THR A CA  
958  C  C   . THR A 124 ? 0.2451 0.2754 0.5062 -0.0222 -0.0541 0.0282  124 THR A C   
959  O  O   . THR A 124 ? 0.2434 0.3311 0.5167 -0.0372 -0.0465 0.0054  124 THR A O   
960  C  CB  . THR A 124 ? 0.3055 0.3660 0.5448 -0.0290 -0.0535 -0.0338 124 THR A CB  
961  O  OG1 . THR A 124 ? 0.3686 0.4744 0.6504 0.0771  -0.0250 0.0250  124 THR A OG1 
962  C  CG2 . THR A 124 ? 0.5427 0.4080 0.5616 -0.2160 -0.1041 -0.0750 124 THR A CG2 
963  N  N   . GLU A 125 ? 0.2152 0.1992 0.4643 0.0234  -0.0468 0.0472  125 GLU A N   
964  C  CA  . GLU A 125 ? 0.2810 0.1875 0.4561 -0.0111 -0.0371 0.0679  125 GLU A CA  
965  C  C   . GLU A 125 ? 0.2200 0.1934 0.4187 -0.0061 -0.0130 0.0703  125 GLU A C   
966  O  O   . GLU A 125 ? 0.2079 0.2264 0.4437 0.0154  -0.0186 0.0516  125 GLU A O   
967  C  CB  . GLU A 125 ? 0.4684 0.1940 0.5017 -0.0020 -0.1072 0.0853  125 GLU A CB  
968  C  CG  . GLU A 125 ? 0.4405 0.1838 0.5553 -0.0334 -0.0520 0.1063  125 GLU A CG  
969  C  CD  . GLU A 125 ? 0.4603 0.1896 0.5840 -0.0160 -0.0521 0.1101  125 GLU A CD  
970  O  OE1 . GLU A 125 ? 0.4628 0.1894 0.5831 -0.0422 -0.0818 0.1194  125 GLU A OE1 
971  O  OE2 . GLU A 125 ? 0.2986 0.2980 0.6063 -0.0019 0.1102  0.1885  125 GLU A OE2 
972  N  N   . PRO A 126 ? 0.2496 0.1952 0.3915 -0.0152 -0.0352 0.0665  126 PRO A N   
973  C  CA  . PRO A 126 ? 0.1941 0.1661 0.3952 0.0244  0.0274  0.0273  126 PRO A CA  
974  C  C   . PRO A 126 ? 0.2416 0.1614 0.3877 0.0251  0.0221  0.0403  126 PRO A C   
975  O  O   . PRO A 126 ? 0.2567 0.2130 0.3663 -0.0070 0.0219  0.0325  126 PRO A O   
976  C  CB  . PRO A 126 ? 0.2287 0.1626 0.3900 0.0422  0.0167  0.0150  126 PRO A CB  
977  C  CG  . PRO A 126 ? 0.2418 0.1980 0.3662 -0.0027 -0.0475 0.0290  126 PRO A CG  
978  C  CD  . PRO A 126 ? 0.2745 0.2004 0.4500 -0.0051 -0.0773 0.0391  126 PRO A CD  
979  N  N   . GLU A 127 ? 0.2455 0.1706 0.3898 0.0087  0.0203  0.0282  127 GLU A N   
980  C  CA  . GLU A 127 ? 0.2694 0.2312 0.3769 0.0509  0.0117  0.0396  127 GLU A CA  
981  C  C   . GLU A 127 ? 0.3047 0.1813 0.3856 0.0796  -0.0080 0.0553  127 GLU A C   
982  O  O   . GLU A 127 ? 0.2341 0.2519 0.3848 0.0407  0.0319  0.0252  127 GLU A O   
983  C  CB  . GLU A 127 ? 0.3181 0.3251 0.3910 0.0540  0.0271  0.1151  127 GLU A CB  
984  C  CG  . GLU A 127 ? 0.4228 0.3336 0.5044 -0.0122 -0.0550 0.1831  127 GLU A CG  
985  C  CD  . GLU A 127 ? 0.4150 0.3639 0.5931 -0.0710 -0.0348 0.1386  127 GLU A CD  
986  O  OE1 . GLU A 127 ? 0.3003 0.2395 0.5044 -0.0919 0.0067  0.0469  127 GLU A OE1 
987  O  OE2 . GLU A 127 ? 0.4530 0.3713 0.4996 -0.0685 0.0462  0.1499  127 GLU A OE2 
988  N  N   . LEU A 128 ? 0.2366 0.1979 0.4058 0.0131  0.0326  0.0303  128 LEU A N   
989  C  CA  . LEU A 128 ? 0.2339 0.1558 0.3530 0.0187  0.0465  -0.0048 128 LEU A CA  
990  C  C   . LEU A 128 ? 0.2385 0.1287 0.3451 -0.0034 0.0229  -0.0099 128 LEU A C   
991  O  O   . LEU A 128 ? 0.2340 0.1727 0.3774 -0.0132 0.0197  0.0109  128 LEU A O   
992  C  CB  . LEU A 128 ? 0.2846 0.1415 0.3520 -0.0156 -0.0034 0.0268  128 LEU A CB  
993  C  CG  . LEU A 128 ? 0.3055 0.1839 0.3426 -0.0095 0.0342  0.0457  128 LEU A CG  
994  C  CD1 . LEU A 128 ? 0.3212 0.1731 0.4934 -0.0153 0.0908  0.0783  128 LEU A CD1 
995  C  CD2 . LEU A 128 ? 0.3262 0.2922 0.3148 -0.0223 -0.0193 0.0423  128 LEU A CD2 
996  N  N   . LEU A 129 ? 0.2633 0.1741 0.3324 -0.0004 0.0235  0.0015  129 LEU A N   
997  C  CA  . LEU A 129 ? 0.2092 0.2085 0.2714 0.0066  -0.0329 0.0137  129 LEU A CA  
998  C  C   . LEU A 129 ? 0.2228 0.2108 0.2671 0.0144  -0.0372 0.0034  129 LEU A C   
999  O  O   . LEU A 129 ? 0.2238 0.1558 0.3323 -0.0138 -0.0251 0.0189  129 LEU A O   
1000 C  CB  . LEU A 129 ? 0.2525 0.1720 0.3141 -0.0026 -0.0802 0.0219  129 LEU A CB  
1001 C  CG  . LEU A 129 ? 0.3262 0.1859 0.2888 0.0189  -0.0542 0.0351  129 LEU A CG  
1002 C  CD1 . LEU A 129 ? 0.3047 0.2360 0.3597 0.0332  -0.0426 0.0087  129 LEU A CD1 
1003 C  CD2 . LEU A 129 ? 0.3299 0.1871 0.3700 -0.0100 -0.0987 0.0689  129 LEU A CD2 
1004 N  N   . VAL A 130 ? 0.2694 0.1597 0.3075 0.0174  -0.0111 0.0021  130 VAL A N   
1005 C  CA  . VAL A 130 ? 0.2632 0.1278 0.3020 0.0342  -0.0007 0.0068  130 VAL A CA  
1006 C  C   . VAL A 130 ? 0.2416 0.1414 0.3117 0.0076  0.0046  0.0483  130 VAL A C   
1007 O  O   . VAL A 130 ? 0.2395 0.1737 0.3470 0.0049  0.0113  0.0124  130 VAL A O   
1008 C  CB  . VAL A 130 ? 0.2925 0.1685 0.2670 0.0475  0.0029  0.0240  130 VAL A CB  
1009 C  CG1 . VAL A 130 ? 0.2452 0.2460 0.3038 0.0276  -0.0211 0.0723  130 VAL A CG1 
1010 C  CG2 . VAL A 130 ? 0.3403 0.1923 0.2885 0.0355  0.0044  -0.0100 130 VAL A CG2 
1011 N  N   . ALA A 131 ? 0.2737 0.1296 0.3518 0.0225  0.0111  0.0400  131 ALA A N   
1012 C  CA  . ALA A 131 ? 0.3067 0.1383 0.3244 0.0373  0.0161  0.0393  131 ALA A CA  
1013 C  C   . ALA A 131 ? 0.2754 0.1758 0.3007 0.0462  -0.0107 0.0866  131 ALA A C   
1014 O  O   . ALA A 131 ? 0.2904 0.1540 0.3206 0.0348  -0.0334 0.0348  131 ALA A O   
1015 C  CB  . ALA A 131 ? 0.3168 0.1385 0.4117 0.0518  0.0624  0.0667  131 ALA A CB  
1016 N  N   . HIS A 132 ? 0.2457 0.1440 0.3176 0.0242  -0.0106 0.0125  132 HIS A N   
1017 C  CA  . HIS A 132 ? 0.2613 0.1101 0.3299 0.0222  -0.0007 -0.0424 132 HIS A CA  
1018 C  C   . HIS A 132 ? 0.2594 0.1103 0.2921 0.0298  0.0235  -0.0388 132 HIS A C   
1019 O  O   . HIS A 132 ? 0.2469 0.1828 0.3137 0.0220  -0.0069 0.0124  132 HIS A O   
1020 C  CB  . HIS A 132 ? 0.2468 0.1166 0.3299 0.0246  -0.0271 -0.0118 132 HIS A CB  
1021 C  CG  . HIS A 132 ? 0.2313 0.1143 0.3244 0.0243  -0.0301 -0.0264 132 HIS A CG  
1022 N  ND1 . HIS A 132 ? 0.2554 0.1274 0.3333 0.0371  0.0028  -0.0197 132 HIS A ND1 
1023 C  CD2 . HIS A 132 ? 0.2522 0.1252 0.3273 0.0150  0.0043  -0.0253 132 HIS A CD2 
1024 C  CE1 . HIS A 132 ? 0.2898 0.1199 0.3418 0.0430  0.0005  -0.0057 132 HIS A CE1 
1025 N  NE2 . HIS A 132 ? 0.2893 0.1238 0.3631 0.0207  0.0114  0.0012  132 HIS A NE2 
1026 N  N   . ALA A 133 ? 0.2820 0.1145 0.2597 0.0388  0.0343  -0.0076 133 ALA A N   
1027 C  CA  . ALA A 133 ? 0.2458 0.1198 0.2809 0.0415  -0.0278 0.0187  133 ALA A CA  
1028 C  C   . ALA A 133 ? 0.2357 0.1816 0.2771 0.0250  -0.0183 0.0188  133 ALA A C   
1029 O  O   . ALA A 133 ? 0.2563 0.1692 0.2989 0.0061  -0.0200 0.0209  133 ALA A O   
1030 C  CB  . ALA A 133 ? 0.2695 0.1516 0.4010 0.0417  -0.0607 0.0739  133 ALA A CB  
1031 N  N   . TYR A 134 ? 0.2594 0.1686 0.2727 0.0272  -0.0012 -0.0079 134 TYR A N   
1032 C  CA  . TYR A 134 ? 0.3218 0.1893 0.2755 0.0374  -0.0217 -0.0028 134 TYR A CA  
1033 C  C   . TYR A 134 ? 0.2887 0.1748 0.2774 0.0063  -0.0311 0.0298  134 TYR A C   
1034 O  O   . TYR A 134 ? 0.3139 0.2114 0.2515 -0.0225 -0.0132 0.0074  134 TYR A O   
1035 C  CB  . TYR A 134 ? 0.3755 0.3006 0.2589 0.0338  0.0225  -0.0359 134 TYR A CB  
1036 C  CG  . TYR A 134 ? 0.3441 0.2848 0.2655 0.0029  0.0297  -0.0031 134 TYR A CG  
1037 C  CD1 . TYR A 134 ? 0.3318 0.2654 0.2642 0.0309  0.0074  0.0069  134 TYR A CD1 
1038 C  CD2 . TYR A 134 ? 0.4271 0.2617 0.2560 -0.0472 0.0061  0.0055  134 TYR A CD2 
1039 C  CE1 . TYR A 134 ? 0.3879 0.2774 0.2529 0.0064  0.0045  0.0279  134 TYR A CE1 
1040 C  CE2 . TYR A 134 ? 0.3641 0.2821 0.2985 -0.0201 -0.0052 0.0086  134 TYR A CE2 
1041 C  CZ  . TYR A 134 ? 0.3860 0.2624 0.2807 -0.0432 -0.0428 0.0481  134 TYR A CZ  
1042 O  OH  . TYR A 134 ? 0.4833 0.3348 0.3146 0.0071  -0.0988 0.0369  134 TYR A OH  
1043 N  N   . THR A 135 ? 0.2683 0.1708 0.3214 0.0099  0.0225  0.0234  135 THR A N   
1044 C  CA  . THR A 135 ? 0.2773 0.2204 0.2867 0.0331  0.0083  0.0082  135 THR A CA  
1045 C  C   . THR A 135 ? 0.2477 0.1824 0.2751 0.0053  -0.0175 -0.0175 135 THR A C   
1046 O  O   . THR A 135 ? 0.2664 0.2298 0.3648 -0.0220 -0.0632 0.0425  135 THR A O   
1047 C  CB  . THR A 135 ? 0.2992 0.1710 0.3762 0.0467  0.0190  0.0988  135 THR A CB  
1048 O  OG1 . THR A 135 ? 0.3418 0.2729 0.5048 0.0687  0.1318  0.1156  135 THR A OG1 
1049 C  CG2 . THR A 135 ? 0.2233 0.1817 0.4404 0.0008  0.0383  0.1039  135 THR A CG2 
1050 N  N   . ARG A 136 ? 0.2618 0.1144 0.2977 -0.0229 -0.0323 0.0094  136 ARG A N   
1051 C  CA  . ARG A 136 ? 0.2499 0.1074 0.2909 0.0153  -0.0200 -0.0036 136 ARG A CA  
1052 C  C   . ARG A 136 ? 0.2412 0.0913 0.3296 0.0083  -0.0459 0.0429  136 ARG A C   
1053 O  O   . ARG A 136 ? 0.2288 0.1523 0.3012 -0.0104 0.0068  0.0213  136 ARG A O   
1054 C  CB  . ARG A 136 ? 0.3115 0.1530 0.2911 0.0339  -0.0320 -0.0077 136 ARG A CB  
1055 C  CG  . ARG A 136 ? 0.3072 0.1994 0.3684 -0.0223 -0.0112 -0.0854 136 ARG A CG  
1056 C  CD  . ARG A 136 ? 0.2672 0.2167 0.4420 0.0206  -0.0154 -0.0925 136 ARG A CD  
1057 N  NE  . ARG A 136 ? 0.3036 0.2015 0.3153 -0.0046 -0.0125 -0.0459 136 ARG A NE  
1058 C  CZ  . ARG A 136 ? 0.4055 0.2228 0.2817 -0.0871 -0.1177 0.0644  136 ARG A CZ  
1059 N  NH1 . ARG A 136 ? 0.4866 0.2083 0.3928 -0.0848 -0.0189 0.0204  136 ARG A NH1 
1060 N  NH2 . ARG A 136 ? 0.2573 0.3769 0.3097 0.0124  -0.0030 -0.0959 136 ARG A NH2 
1061 N  N   . TYR A 137 ? 0.2543 0.0979 0.2940 0.0129  -0.0424 0.0455  137 TYR A N   
1062 C  CA  . TYR A 137 ? 0.2806 0.0937 0.2928 0.0226  0.0155  0.0078  137 TYR A CA  
1063 C  C   . TYR A 137 ? 0.2796 0.1095 0.3067 -0.0043 -0.0023 0.0199  137 TYR A C   
1064 O  O   . TYR A 137 ? 0.2950 0.1591 0.3687 -0.0320 -0.0209 0.0388  137 TYR A O   
1065 C  CB  . TYR A 137 ? 0.3155 0.1036 0.2592 0.0420  0.0145  0.0153  137 TYR A CB  
1066 C  CG  . TYR A 137 ? 0.2866 0.1198 0.2666 -0.0272 0.0093  0.0275  137 TYR A CG  
1067 C  CD1 . TYR A 137 ? 0.2751 0.1540 0.2531 -0.0280 0.0104  -0.0228 137 TYR A CD1 
1068 C  CD2 . TYR A 137 ? 0.2922 0.2381 0.3135 -0.0636 0.0214  0.0036  137 TYR A CD2 
1069 C  CE1 . TYR A 137 ? 0.2675 0.1241 0.2593 -0.0525 0.0013  -0.0162 137 TYR A CE1 
1070 C  CE2 . TYR A 137 ? 0.2794 0.2488 0.3240 -0.0946 0.0131  -0.0299 137 TYR A CE2 
1071 C  CZ  . TYR A 137 ? 0.2616 0.2277 0.3064 -0.0584 -0.0101 0.0158  137 TYR A CZ  
1072 O  OH  . TYR A 137 ? 0.2379 0.4424 0.3207 -0.0343 -0.0371 0.0476  137 TYR A OH  
1073 N  N   . LEU A 138 ? 0.2748 0.1779 0.2985 -0.0091 -0.0166 0.0275  138 LEU A N   
1074 C  CA  . LEU A 138 ? 0.2956 0.1747 0.3042 -0.0041 -0.0045 0.0072  138 LEU A CA  
1075 C  C   . LEU A 138 ? 0.2885 0.1754 0.3267 -0.0257 -0.0441 -0.0092 138 LEU A C   
1076 O  O   . LEU A 138 ? 0.2802 0.2682 0.3624 -0.0697 -0.0088 -0.0442 138 LEU A O   
1077 C  CB  . LEU A 138 ? 0.3707 0.2235 0.3336 0.0133  0.0511  0.0090  138 LEU A CB  
1078 C  CG  . LEU A 138 ? 0.4909 0.2964 0.4954 -0.0271 0.1786  -0.1247 138 LEU A CG  
1079 C  CD1 . LEU A 138 ? 0.8593 0.2602 0.8123 -0.0561 0.2796  -0.1194 138 LEU A CD1 
1080 C  CD2 . LEU A 138 ? 0.5108 0.4089 0.5658 -0.1771 0.2212  -0.2695 138 LEU A CD2 
1081 N  N   . GLY A 139 ? 0.3556 0.1661 0.2856 0.0189  -0.0707 0.0190  139 GLY A N   
1082 C  CA  . GLY A 139 ? 0.3598 0.2296 0.2618 0.0452  -0.0360 0.0384  139 GLY A CA  
1083 C  C   . GLY A 139 ? 0.3657 0.2401 0.2965 0.0128  -0.0508 0.0660  139 GLY A C   
1084 O  O   . GLY A 139 ? 0.3456 0.2850 0.2832 0.0540  -0.0410 0.0453  139 GLY A O   
1085 N  N   . ASP A 140 ? 0.3235 0.2005 0.2986 -0.0113 -0.0479 0.0608  140 ASP A N   
1086 C  CA  . ASP A 140 ? 0.3035 0.2893 0.3257 -0.0109 -0.0631 0.1148  140 ASP A CA  
1087 C  C   . ASP A 140 ? 0.3101 0.2747 0.3678 -0.0294 -0.0312 0.1305  140 ASP A C   
1088 O  O   . ASP A 140 ? 0.3301 0.2908 0.4685 -0.0544 0.0290  0.1454  140 ASP A O   
1089 C  CB  . ASP A 140 ? 0.2796 0.4068 0.3154 -0.0503 -0.0372 0.1130  140 ASP A CB  
1090 C  CG  . ASP A 140 ? 0.3180 0.4379 0.2873 -0.0586 0.0575  0.0453  140 ASP A CG  
1091 O  OD1 . ASP A 140 ? 0.6463 0.3817 0.4044 0.0844  -0.1786 -0.0918 140 ASP A OD1 
1092 O  OD2 . ASP A 140 ? 0.4990 0.4158 0.3534 0.0299  -0.0462 0.0193  140 ASP A OD2 
1093 N  N   . LEU A 141 ? 0.3203 0.2716 0.5320 -0.0378 -0.0076 0.0905  141 LEU A N   
1094 C  CA  . LEU A 141 ? 0.2946 0.3426 0.6045 -0.0616 0.0153  -0.0105 141 LEU A CA  
1095 C  C   . LEU A 141 ? 0.3555 0.4629 0.6196 -0.1114 -0.0137 -0.0027 141 LEU A C   
1096 O  O   . LEU A 141 ? 0.3952 0.2838 0.6779 -0.0751 -0.0658 -0.0192 141 LEU A O   
1097 C  CB  . LEU A 141 ? 0.3535 0.3539 0.5359 -0.0185 0.0939  0.0295  141 LEU A CB  
1098 C  CG  . LEU A 141 ? 0.2939 0.3955 0.4416 -0.0470 0.0561  -0.0378 141 LEU A CG  
1099 C  CD1 . LEU A 141 ? 0.4244 0.3480 0.3986 -0.0240 -0.0177 0.0371  141 LEU A CD1 
1100 C  CD2 . LEU A 141 ? 0.3894 0.5796 0.3504 0.1580  -0.0014 0.0269  141 LEU A CD2 
1101 N  N   . SER A 142 ? 0.3992 0.5432 0.5047 -0.1496 0.0397  -0.0840 142 SER A N   
1102 C  CA  . SER A 142 ? 0.5275 0.3886 0.5586 -0.2566 -0.0599 -0.1003 142 SER A CA  
1103 C  C   . SER A 142 ? 0.5891 0.4022 0.6372 -0.1899 -0.1233 -0.0120 142 SER A C   
1104 O  O   . SER A 142 ? 0.6492 0.3360 0.6745 -0.1431 -0.2126 0.0365  142 SER A O   
1105 C  CB  . SER A 142 ? 0.6407 0.4645 0.4983 -0.3493 -0.1180 -0.0735 142 SER A CB  
1106 O  OG  . SER A 142 ? 0.7979 0.7059 0.6022 -0.0601 0.0616  -0.0692 142 SER A OG  
1107 N  N   . GLY A 143 ? 0.5146 0.4453 0.5271 -0.1648 -0.0619 0.0176  143 GLY A N   
1108 C  CA  . GLY A 143 ? 0.5300 0.4185 0.5789 -0.1384 -0.1090 0.1084  143 GLY A CA  
1109 C  C   . GLY A 143 ? 0.4970 0.4281 0.5171 -0.0042 -0.1037 0.0982  143 GLY A C   
1110 O  O   . GLY A 143 ? 0.4963 0.4496 0.4191 0.0064  -0.1851 0.0048  143 GLY A O   
1111 N  N   . GLY A 144 ? 0.4771 0.3980 0.5077 0.0162  -0.0934 0.0704  144 GLY A N   
1112 C  CA  . GLY A 144 ? 0.4993 0.4139 0.5372 -0.0695 -0.1098 0.1048  144 GLY A CA  
1113 C  C   . GLY A 144 ? 0.4959 0.4246 0.5724 -0.0526 -0.1469 0.1108  144 GLY A C   
1114 O  O   . GLY A 144 ? 0.4115 0.5539 0.6820 0.0488  -0.1746 0.0951  144 GLY A O   
1115 N  N   . GLN A 145 ? 0.6334 0.3405 0.6635 -0.0757 -0.1715 0.0767  145 GLN A N   
1116 C  CA  . GLN A 145 ? 0.6628 0.4627 0.8120 -0.0649 -0.2320 -0.0250 145 GLN A CA  
1117 C  C   . GLN A 145 ? 0.6129 0.4681 0.7245 -0.0951 -0.1601 0.0946  145 GLN A C   
1118 O  O   . GLN A 145 ? 0.6304 0.4257 0.7997 -0.1310 -0.1288 0.0861  145 GLN A O   
1119 C  CB  . GLN A 145 ? 0.7304 0.6812 0.9873 -0.1144 -0.1960 -0.2435 145 GLN A CB  
1120 C  CG  . GLN A 145 ? 0.6360 0.8579 1.1900 -0.0887 0.0145  -0.2815 145 GLN A CG  
1121 C  CD  . GLN A 145 ? 0.6493 1.1215 1.3557 -0.1710 0.0501  -0.2672 145 GLN A CD  
1122 O  OE1 . GLN A 145 ? 0.5168 1.3574 1.5039 -0.1821 0.1296  -0.0559 145 GLN A OE1 
1123 N  NE2 . GLN A 145 ? 0.7237 1.0703 1.5780 -0.2618 -0.0864 -0.3327 145 GLN A NE2 
1124 N  N   . VAL A 146 ? 0.6808 0.4631 0.6433 -0.1586 -0.1537 0.0415  146 VAL A N   
1125 C  CA  . VAL A 146 ? 0.7670 0.4868 0.5035 -0.1237 -0.1888 0.0874  146 VAL A CA  
1126 C  C   . VAL A 146 ? 0.7215 0.4394 0.5155 -0.1158 -0.2113 0.0937  146 VAL A C   
1127 O  O   . VAL A 146 ? 0.7386 0.4010 0.5774 -0.0513 -0.2690 0.0677  146 VAL A O   
1128 C  CB  . VAL A 146 ? 0.9606 0.6811 0.5088 -0.1974 -0.2110 0.1552  146 VAL A CB  
1129 C  CG1 . VAL A 146 ? 0.9846 0.7793 0.5603 -0.2786 -0.0925 0.1485  146 VAL A CG1 
1130 C  CG2 . VAL A 146 ? 0.9059 0.8023 0.4301 -0.3630 0.0092  0.1781  146 VAL A CG2 
1131 N  N   . LEU A 147 ? 0.7281 0.5000 0.4934 -0.0779 -0.2382 0.1116  147 LEU A N   
1132 C  CA  . LEU A 147 ? 0.7330 0.4168 0.5687 -0.1374 -0.2431 0.1072  147 LEU A CA  
1133 C  C   . LEU A 147 ? 0.6674 0.2870 0.6156 0.0679  -0.1312 0.0672  147 LEU A C   
1134 O  O   . LEU A 147 ? 0.7537 0.4348 0.5545 0.2203  -0.3018 -0.0447 147 LEU A O   
1135 C  CB  . LEU A 147 ? 0.7458 0.5050 0.7154 -0.1890 -0.2484 0.0860  147 LEU A CB  
1136 C  CG  . LEU A 147 ? 0.6830 0.6001 0.7181 -0.1138 -0.2328 0.1013  147 LEU A CG  
1137 C  CD1 . LEU A 147 ? 0.6846 0.9370 0.5906 -0.0411 -0.2208 -0.1012 147 LEU A CD1 
1138 C  CD2 . LEU A 147 ? 0.7979 0.5695 0.7871 -0.1783 -0.1384 0.1295  147 LEU A CD2 
1139 N  N   . LYS A 148 ? 0.5814 0.2434 0.5363 -0.0485 -0.1884 -0.0026 148 LYS A N   
1140 C  CA  . LYS A 148 ? 0.4516 0.2775 0.5428 -0.0537 -0.2232 -0.0055 148 LYS A CA  
1141 C  C   . LYS A 148 ? 0.4536 0.4071 0.6101 0.0764  -0.2382 -0.1135 148 LYS A C   
1142 O  O   . LYS A 148 ? 0.5251 0.8051 0.6564 0.2746  -0.2238 -0.1107 148 LYS A O   
1143 C  CB  . LYS A 148 ? 0.3873 0.3152 0.5235 -0.0345 -0.1738 0.0390  148 LYS A CB  
1144 C  CG  . LYS A 148 ? 0.4339 0.3188 0.4883 -0.0125 -0.1455 0.0068  148 LYS A CG  
1145 C  CD  . LYS A 148 ? 0.4589 0.2832 0.4680 -0.0495 -0.1026 -0.0206 148 LYS A CD  
1146 C  CE  . LYS A 148 ? 0.3874 0.2094 0.5216 0.0198  -0.0492 -0.0592 148 LYS A CE  
1147 N  NZ  . LYS A 148 ? 0.3477 0.2372 0.4140 0.0312  -0.1284 -0.0381 148 LYS A NZ  
1148 N  N   . LYS A 149 ? 0.4887 0.5199 0.6558 0.0450  -0.2901 -0.1600 149 LYS A N   
1149 C  CA  . LYS A 149 ? 0.5137 0.7028 0.8699 0.0788  -0.3954 -0.1805 149 LYS A CA  
1150 C  C   . LYS A 149 ? 0.5080 0.7248 0.8865 0.1048  -0.3921 -0.1420 149 LYS A C   
1151 O  O   . LYS A 149 ? 0.6127 0.7908 0.7289 0.0267  -0.3240 -0.3182 149 LYS A O   
1152 C  CB  . LYS A 149 ? 0.5361 0.9095 0.8843 0.0919  -0.4646 -0.2646 149 LYS A CB  
1153 C  CG  . LYS A 149 ? 0.6425 1.0456 1.0368 0.0995  -0.5902 -0.1924 149 LYS A CG  
1154 C  CD  . LYS A 149 ? 0.6575 1.1629 1.2345 0.0435  -0.6808 -0.1872 149 LYS A CD  
1155 C  CE  . LYS A 149 ? 0.6598 1.2557 1.3435 0.0475  -0.6658 -0.2268 149 LYS A CE  
1156 N  NZ  . LYS A 149 ? 0.7208 1.3666 1.5710 0.0019  -0.5275 -0.1644 149 LYS A NZ  
1157 N  N   . ILE A 150 ? 0.6019 0.7081 0.8262 0.1256  -0.3902 -0.1101 150 ILE A N   
1158 C  CA  . ILE A 150 ? 0.6718 0.7332 0.8810 0.1631  -0.3398 -0.1033 150 ILE A CA  
1159 C  C   . ILE A 150 ? 0.6801 0.7564 0.8967 0.1914  -0.3012 -0.0892 150 ILE A C   
1160 O  O   . ILE A 150 ? 0.7059 0.5328 0.9231 0.2206  -0.3554 -0.1607 150 ILE A O   
1161 C  CB  . ILE A 150 ? 0.8016 0.7130 0.9557 0.1858  -0.2588 -0.0427 150 ILE A CB  
1162 C  CG1 . ILE A 150 ? 0.8354 0.7603 0.9717 0.2116  -0.2279 -0.0262 150 ILE A CG1 
1163 C  CG2 . ILE A 150 ? 1.0182 0.7529 0.9913 0.2815  -0.2231 -0.0213 150 ILE A CG2 
1164 C  CD1 . ILE A 150 ? 0.9323 0.6371 0.7676 0.5396  -0.3511 -0.0559 150 ILE A CD1 
1165 N  N   . ALA A 151 ? 0.5951 0.7111 0.8240 0.1482  -0.2031 0.0016  151 ALA A N   
1166 C  CA  . ALA A 151 ? 0.5943 0.6096 0.8285 0.1217  -0.1860 0.0126  151 ALA A CA  
1167 C  C   . ALA A 151 ? 0.5576 0.6218 0.8203 0.1173  -0.2271 0.0073  151 ALA A C   
1168 O  O   . ALA A 151 ? 0.5445 0.5499 0.8459 0.0583  -0.2292 -0.0508 151 ALA A O   
1169 C  CB  . ALA A 151 ? 0.5879 0.4636 0.7642 0.0268  -0.1483 0.2103  151 ALA A CB  
1170 N  N   . GLN A 152 ? 0.5160 0.6371 0.7399 0.0888  -0.1789 -0.0571 152 GLN A N   
1171 C  CA  . GLN A 152 ? 0.5442 0.6516 0.9003 -0.0214 -0.1115 -0.1633 152 GLN A CA  
1172 C  C   . GLN A 152 ? 0.5584 0.6700 0.9401 0.0113  -0.1133 -0.1580 152 GLN A C   
1173 O  O   . GLN A 152 ? 0.6323 0.6694 1.1170 0.1611  0.0382  -0.3408 152 GLN A O   
1174 C  CB  . GLN A 152 ? 0.4603 0.6586 0.9213 -0.0374 -0.1038 -0.1946 152 GLN A CB  
1175 C  CG  . GLN A 152 ? 0.5187 0.6835 0.8771 -0.1456 -0.1034 -0.2629 152 GLN A CG  
1176 C  CD  . GLN A 152 ? 0.6224 0.7034 0.8998 -0.0542 -0.1252 -0.2821 152 GLN A CD  
1177 O  OE1 . GLN A 152 ? 1.0611 0.6732 0.8804 -0.0109 -0.1491 -0.2083 152 GLN A OE1 
1178 N  NE2 . GLN A 152 ? 0.4653 0.8840 1.1665 0.0771  0.0336  -0.3163 152 GLN A NE2 
1179 N  N   . LYS A 153 ? 0.7752 0.6542 1.0041 -0.0731 -0.2658 -0.0943 153 LYS A N   
1180 C  CA  . LYS A 153 ? 0.8038 0.5762 1.1349 -0.1251 -0.3591 -0.1188 153 LYS A CA  
1181 C  C   . LYS A 153 ? 0.7311 0.5568 1.0454 -0.1437 -0.3385 -0.0789 153 LYS A C   
1182 O  O   . LYS A 153 ? 0.6987 0.4923 1.0560 -0.2503 -0.1531 -0.0188 153 LYS A O   
1183 C  CB  . LYS A 153 ? 0.8650 0.5834 1.1502 -0.0497 -0.3892 -0.1442 153 LYS A CB  
1184 C  CG  . LYS A 153 ? 1.0430 0.5894 1.2980 -0.0014 -0.4366 -0.2312 153 LYS A CG  
1185 C  CD  . LYS A 153 ? 1.1159 0.5920 1.3912 0.0242  -0.5218 -0.1812 153 LYS A CD  
1186 C  CE  . LYS A 153 ? 1.1212 0.6427 1.4135 0.0622  -0.5886 -0.2272 153 LYS A CE  
1187 N  NZ  . LYS A 153 ? 1.1095 0.6506 1.3901 0.1574  -0.5517 -0.1848 153 LYS A NZ  
1188 N  N   . ALA A 154 ? 0.6741 0.5927 0.9182 -0.1233 -0.2936 -0.1117 154 ALA A N   
1189 C  CA  . ALA A 154 ? 0.5424 0.5134 0.7902 -0.1692 -0.1937 0.0351  154 ALA A CA  
1190 C  C   . ALA A 154 ? 0.5417 0.4943 0.7922 -0.0973 -0.1622 0.0446  154 ALA A C   
1191 O  O   . ALA A 154 ? 0.6484 0.4483 0.8473 -0.0518 -0.0997 0.1074  154 ALA A O   
1192 C  CB  . ALA A 154 ? 0.3952 0.6376 0.8484 -0.1336 -0.1632 0.0779  154 ALA A CB  
1193 N  N   . LEU A 155 ? 0.4958 0.4652 0.7750 -0.1324 -0.1214 0.0789  155 LEU A N   
1194 C  CA  . LEU A 155 ? 0.3748 0.4469 0.7838 -0.0709 -0.1132 0.0346  155 LEU A CA  
1195 C  C   . LEU A 155 ? 0.3769 0.4409 0.7843 -0.0494 -0.0724 0.0033  155 LEU A C   
1196 O  O   . LEU A 155 ? 0.5361 0.5328 0.8083 -0.1338 -0.0230 -0.0462 155 LEU A O   
1197 C  CB  . LEU A 155 ? 0.3822 0.3754 0.8000 -0.0584 -0.0795 0.1258  155 LEU A CB  
1198 C  CG  . LEU A 155 ? 0.2983 0.4329 0.7657 -0.0190 0.0270  0.1923  155 LEU A CG  
1199 C  CD1 . LEU A 155 ? 0.6210 0.6200 0.6554 -0.1133 0.0248  0.2019  155 LEU A CD1 
1200 C  CD2 . LEU A 155 ? 0.3662 0.6906 1.0395 0.1031  0.1450  0.0684  155 LEU A CD2 
1201 N  N   . ASP A 156 ? 0.4129 0.4640 0.7829 -0.0937 -0.0414 0.0037  156 ASP A N   
1202 C  CA  . ASP A 156 ? 0.4930 0.5318 0.8725 -0.1415 0.0095  0.0273  156 ASP A CA  
1203 C  C   . ASP A 156 ? 0.5542 0.5169 0.7689 -0.0720 0.0892  -0.0256 156 ASP A C   
1204 O  O   . ASP A 156 ? 0.6470 0.4311 0.8475 -0.1436 0.1943  -0.0351 156 ASP A O   
1205 C  CB  . ASP A 156 ? 0.4070 0.6303 1.0403 -0.1443 0.0347  0.0664  156 ASP A CB  
1206 C  CG  . ASP A 156 ? 0.4776 0.8356 1.0920 -0.2637 0.0675  0.0375  156 ASP A CG  
1207 O  OD1 . ASP A 156 ? 0.4112 1.1770 1.3411 -0.3757 -0.0357 -0.0642 156 ASP A OD1 
1208 O  OD2 . ASP A 156 ? 0.6244 1.1014 1.0868 -0.2277 0.1355  0.0940  156 ASP A OD2 
1209 N  N   . LEU A 157 ? 0.5901 0.4721 0.6848 -0.0430 -0.0099 -0.1670 157 LEU A N   
1210 C  CA  . LEU A 157 ? 0.6646 0.5343 0.7452 -0.1105 -0.1043 -0.1337 157 LEU A CA  
1211 C  C   . LEU A 157 ? 0.7008 0.4332 0.7896 -0.0502 -0.1201 -0.1078 157 LEU A C   
1212 O  O   . LEU A 157 ? 0.5578 0.3151 0.7689 0.0476  -0.1703 -0.0113 157 LEU A O   
1213 C  CB  . LEU A 157 ? 0.6867 0.6356 0.7571 -0.0478 -0.1072 -0.0904 157 LEU A CB  
1214 C  CG  . LEU A 157 ? 0.6738 0.6548 0.8179 -0.1069 -0.0430 -0.0228 157 LEU A CG  
1215 C  CD1 . LEU A 157 ? 0.4660 0.8081 0.8337 -0.3680 -0.0377 0.0210  157 LEU A CD1 
1216 C  CD2 . LEU A 157 ? 0.5888 0.6348 1.1304 -0.2677 -0.0126 0.0147  157 LEU A CD2 
1217 N  N   . PRO A 158 ? 0.6711 0.3192 0.7873 -0.0063 -0.1134 -0.1272 158 PRO A N   
1218 C  CA  . PRO A 158 ? 0.5668 0.3048 0.8241 0.0385  -0.1181 -0.1102 158 PRO A CA  
1219 C  C   . PRO A 158 ? 0.4446 0.3211 0.8485 0.0495  -0.0429 -0.0503 158 PRO A C   
1220 O  O   . PRO A 158 ? 0.3001 0.4871 1.0960 0.0968  -0.0318 0.0235  158 PRO A O   
1221 C  CB  . PRO A 158 ? 0.6436 0.4059 0.8104 0.0301  -0.0997 -0.0782 158 PRO A CB  
1222 C  CG  . PRO A 158 ? 0.6472 0.3289 0.8051 0.0639  -0.1303 -0.1747 158 PRO A CG  
1223 C  CD  . PRO A 158 ? 0.6488 0.3613 0.8152 -0.0156 -0.1181 -0.1460 158 PRO A CD  
1224 N  N   . SER A 159 ? 0.4191 0.2991 0.9122 0.0488  -0.0563 -0.0694 159 SER A N   
1225 C  CA  . SER A 159 ? 0.4089 0.3227 0.8606 0.0478  -0.1668 -0.1613 159 SER A CA  
1226 C  C   . SER A 159 ? 0.3569 0.2269 0.6956 -0.0013 -0.0534 -0.1488 159 SER A C   
1227 O  O   . SER A 159 ? 0.3020 0.2750 0.7111 -0.0665 0.0266  -0.1271 159 SER A O   
1228 C  CB  . SER A 159 ? 0.4805 0.3785 0.9763 0.0037  -0.2579 -0.1463 159 SER A CB  
1229 O  OG  . SER A 159 ? 0.6514 0.6776 0.9464 0.0845  -0.4160 -0.2233 159 SER A OG  
1230 N  N   . SER A 160 ? 0.3066 0.2054 0.6072 0.0056  -0.0139 -0.0583 160 SER A N   
1231 C  CA  . SER A 160 ? 0.2978 0.3020 0.5161 -0.0358 0.0439  -0.0727 160 SER A CA  
1232 C  C   . SER A 160 ? 0.2666 0.2183 0.4838 -0.0550 -0.0213 -0.0925 160 SER A C   
1233 O  O   . SER A 160 ? 0.3944 0.2416 0.4340 0.0053  -0.0184 -0.0148 160 SER A O   
1234 C  CB  . SER A 160 ? 0.3035 0.3880 0.5592 -0.0397 0.1048  -0.1511 160 SER A CB  
1235 O  OG  . SER A 160 ? 0.5596 0.2942 0.5982 -0.0866 -0.1107 -0.0039 160 SER A OG  
1236 N  N   . GLY A 161 ? 0.2060 0.1690 0.4572 -0.0300 -0.0405 -0.0387 161 GLY A N   
1237 C  CA  . GLY A 161 ? 0.2185 0.1874 0.4062 -0.0087 0.0209  0.1075  161 GLY A CA  
1238 C  C   . GLY A 161 ? 0.2086 0.1941 0.3007 0.0121  0.0163  0.0465  161 GLY A C   
1239 O  O   . GLY A 161 ? 0.2150 0.2070 0.2917 0.0295  0.0130  -0.0080 161 GLY A O   
1240 N  N   . GLU A 162 ? 0.2055 0.1921 0.2977 0.0115  -0.0320 0.0519  162 GLU A N   
1241 C  CA  . GLU A 162 ? 0.2303 0.2296 0.3084 -0.0255 -0.0243 0.0470  162 GLU A CA  
1242 C  C   . GLU A 162 ? 0.2366 0.1531 0.2895 -0.0067 -0.0288 -0.0438 162 GLU A C   
1243 O  O   . GLU A 162 ? 0.2422 0.1888 0.3362 -0.0240 -0.0542 0.0025  162 GLU A O   
1244 C  CB  . GLU A 162 ? 0.2798 0.3994 0.3079 -0.1178 -0.0361 0.0712  162 GLU A CB  
1245 C  CG  . GLU A 162 ? 0.3716 0.7108 0.3136 -0.2827 0.0040  0.0015  162 GLU A CG  
1246 C  CD  . GLU A 162 ? 0.3585 0.8347 0.3171 -0.2333 0.0021  0.0294  162 GLU A CD  
1247 O  OE1 . GLU A 162 ? 0.3651 0.8754 0.3320 -0.1677 0.0113  -0.0213 162 GLU A OE1 
1248 O  OE2 . GLU A 162 ? 0.3588 0.6647 0.3080 -0.1288 -0.0111 0.0043  162 GLU A OE2 
1249 N  N   . GLY A 163 ? 0.2439 0.1536 0.3038 -0.0141 -0.0975 0.0061  163 GLY A N   
1250 C  CA  . GLY A 163 ? 0.2345 0.1384 0.2996 0.0111  -0.0541 -0.0195 163 GLY A CA  
1251 C  C   . GLY A 163 ? 0.2444 0.1557 0.2906 -0.0045 -0.0642 -0.0138 163 GLY A C   
1252 O  O   . GLY A 163 ? 0.2747 0.1377 0.2745 0.0019  -0.0359 -0.0485 163 GLY A O   
1253 N  N   . LEU A 164 ? 0.2372 0.1251 0.2901 -0.0070 -0.0238 0.0081  164 LEU A N   
1254 C  CA  . LEU A 164 ? 0.2228 0.1283 0.2726 -0.0007 -0.0528 0.0256  164 LEU A CA  
1255 C  C   . LEU A 164 ? 0.2346 0.1405 0.2300 0.0085  -0.0610 0.0059  164 LEU A C   
1256 O  O   . LEU A 164 ? 0.2497 0.1454 0.2289 -0.0300 -0.0639 -0.0123 164 LEU A O   
1257 C  CB  . LEU A 164 ? 0.2226 0.1435 0.3127 -0.0201 -0.0758 0.0310  164 LEU A CB  
1258 C  CG  . LEU A 164 ? 0.2095 0.1641 0.2680 -0.0226 -0.0699 0.0072  164 LEU A CG  
1259 C  CD1 . LEU A 164 ? 0.2442 0.2099 0.2851 0.0048  -0.1048 -0.0153 164 LEU A CD1 
1260 C  CD2 . LEU A 164 ? 0.2845 0.1465 0.3190 -0.0054 -0.0777 0.0236  164 LEU A CD2 
1261 N  N   . ALA A 165 ? 0.2311 0.1254 0.2288 0.0033  -0.0606 0.0010  165 ALA A N   
1262 C  CA  . ALA A 165 ? 0.2202 0.1405 0.2396 0.0007  -0.0693 -0.0047 165 ALA A CA  
1263 C  C   . ALA A 165 ? 0.2401 0.1095 0.2355 0.0174  -0.0527 -0.0138 165 ALA A C   
1264 O  O   . ALA A 165 ? 0.2355 0.1244 0.2158 0.0372  -0.0771 -0.0124 165 ALA A O   
1265 C  CB  . ALA A 165 ? 0.2686 0.1438 0.2200 0.0514  -0.0593 -0.0151 165 ALA A CB  
1266 N  N   . PHE A 166 ? 0.2262 0.1089 0.2285 0.0212  -0.0648 -0.0039 166 PHE A N   
1267 C  CA  . PHE A 166 ? 0.2477 0.1133 0.2427 0.0058  -0.0444 -0.0314 166 PHE A CA  
1268 C  C   . PHE A 166 ? 0.2245 0.0767 0.2332 0.0007  -0.0549 -0.0183 166 PHE A C   
1269 O  O   . PHE A 166 ? 0.2303 0.1347 0.2344 -0.0150 -0.0462 -0.0087 166 PHE A O   
1270 C  CB  . PHE A 166 ? 0.2527 0.1076 0.2566 -0.0164 -0.0120 -0.0454 166 PHE A CB  
1271 C  CG  . PHE A 166 ? 0.2424 0.1259 0.2400 0.0110  -0.0049 -0.0285 166 PHE A CG  
1272 C  CD1 . PHE A 166 ? 0.2536 0.1395 0.2154 -0.0051 -0.0191 0.0030  166 PHE A CD1 
1273 C  CD2 . PHE A 166 ? 0.2578 0.1305 0.2434 -0.0147 -0.0460 -0.0432 166 PHE A CD2 
1274 C  CE1 . PHE A 166 ? 0.2555 0.1051 0.2145 -0.0168 -0.0302 -0.0018 166 PHE A CE1 
1275 C  CE2 . PHE A 166 ? 0.2748 0.1730 0.2601 -0.0064 -0.0559 0.0081  166 PHE A CE2 
1276 C  CZ  . PHE A 166 ? 0.2694 0.1121 0.2465 -0.0004 -0.0409 0.0239  166 PHE A CZ  
1277 N  N   . PHE A 167 ? 0.2153 0.1212 0.2489 0.0178  -0.0595 0.0014  167 PHE A N   
1278 C  CA  . PHE A 167 ? 0.2732 0.1025 0.2614 0.0032  -0.1095 0.0160  167 PHE A CA  
1279 C  C   . PHE A 167 ? 0.3005 0.1041 0.2271 -0.0004 -0.0835 0.0209  167 PHE A C   
1280 O  O   . PHE A 167 ? 0.3602 0.1631 0.2328 0.0530  -0.1080 -0.0054 167 PHE A O   
1281 C  CB  . PHE A 167 ? 0.2762 0.1291 0.2940 0.0054  -0.1168 -0.0080 167 PHE A CB  
1282 C  CG  . PHE A 167 ? 0.2612 0.1265 0.3444 0.0197  -0.0661 0.0244  167 PHE A CG  
1283 C  CD1 . PHE A 167 ? 0.3372 0.1698 0.3365 -0.0192 -0.0902 0.0387  167 PHE A CD1 
1284 C  CD2 . PHE A 167 ? 0.3055 0.1310 0.4976 0.0451  0.0761  0.0242  167 PHE A CD2 
1285 C  CE1 . PHE A 167 ? 0.3307 0.1662 0.4271 -0.0336 -0.0484 0.0662  167 PHE A CE1 
1286 C  CE2 . PHE A 167 ? 0.3488 0.1359 0.5887 0.0795  0.1447  0.0445  167 PHE A CE2 
1287 C  CZ  . PHE A 167 ? 0.4181 0.1539 0.5540 0.0412  0.0593  0.0665  167 PHE A CZ  
1288 N  N   . THR A 168 ? 0.2680 0.1056 0.2077 0.0231  -0.0405 0.0155  168 THR A N   
1289 C  CA  . THR A 168 ? 0.2679 0.1055 0.2354 0.0159  -0.0857 0.0136  168 THR A CA  
1290 C  C   . THR A 168 ? 0.2595 0.1232 0.2210 0.0227  -0.0632 -0.0069 168 THR A C   
1291 O  O   . THR A 168 ? 0.2309 0.1100 0.2215 -0.0008 -0.0619 0.0030  168 THR A O   
1292 C  CB  . THR A 168 ? 0.2709 0.1028 0.2379 -0.0049 -0.0978 0.0030  168 THR A CB  
1293 O  OG1 . THR A 168 ? 0.2786 0.1383 0.2679 -0.0104 -0.1091 -0.0037 168 THR A OG1 
1294 C  CG2 . THR A 168 ? 0.2742 0.1100 0.3204 -0.0031 0.0077  0.0030  168 THR A CG2 
1295 N  N   . PHE A 169 ? 0.2871 0.1331 0.2315 0.0105  -0.0372 -0.0090 169 PHE A N   
1296 C  CA  . PHE A 169 ? 0.2799 0.1158 0.2204 0.0054  -0.0206 0.0007  169 PHE A CA  
1297 C  C   . PHE A 169 ? 0.2267 0.1169 0.2114 -0.0268 -0.0686 -0.0134 169 PHE A C   
1298 O  O   . PHE A 169 ? 0.2730 0.1363 0.2299 -0.0322 -0.0291 -0.0321 169 PHE A O   
1299 C  CB  . PHE A 169 ? 0.3106 0.1333 0.2244 -0.0088 -0.0150 0.0001  169 PHE A CB  
1300 C  CG  . PHE A 169 ? 0.3020 0.1372 0.1999 0.0002  -0.0433 0.0297  169 PHE A CG  
1301 C  CD1 . PHE A 169 ? 0.3227 0.1988 0.2833 -0.0300 -0.0894 0.1092  169 PHE A CD1 
1302 C  CD2 . PHE A 169 ? 0.2590 0.0898 0.2427 0.0399  -0.0134 0.0018  169 PHE A CD2 
1303 C  CE1 . PHE A 169 ? 0.3679 0.1602 0.3304 0.0196  -0.1270 0.0457  169 PHE A CE1 
1304 C  CE2 . PHE A 169 ? 0.2662 0.0899 0.2890 0.0454  -0.0206 0.0010  169 PHE A CE2 
1305 C  CZ  . PHE A 169 ? 0.3147 0.1294 0.2837 0.0202  -0.0508 0.0729  169 PHE A CZ  
1306 N  N   . PRO A 170 ? 0.2447 0.1229 0.2212 -0.0068 -0.0729 0.0034  170 PRO A N   
1307 C  CA  . PRO A 170 ? 0.2621 0.1289 0.2165 -0.0285 -0.0153 -0.0118 170 PRO A CA  
1308 C  C   . PRO A 170 ? 0.2939 0.1037 0.2185 -0.0343 0.0312  0.0104  170 PRO A C   
1309 O  O   . PRO A 170 ? 0.3327 0.1132 0.3150 -0.0464 0.0350  -0.0242 170 PRO A O   
1310 C  CB  . PRO A 170 ? 0.2340 0.1022 0.2183 -0.0268 -0.0135 -0.0346 170 PRO A CB  
1311 C  CG  . PRO A 170 ? 0.2711 0.0814 0.2198 -0.0499 -0.0377 0.0114  170 PRO A CG  
1312 C  CD  . PRO A 170 ? 0.2938 0.1142 0.2070 -0.0472 -0.0707 0.0188  170 PRO A CD  
1313 N  N   . ASN A 171 ? 0.2747 0.1063 0.2526 -0.0225 0.0122  0.0072  171 ASN A N   
1314 C  CA  . ASN A 171 ? 0.3006 0.1580 0.2822 0.0108  0.0374  0.0345  171 ASN A CA  
1315 C  C   . ASN A 171 ? 0.2887 0.1147 0.2961 0.0306  0.0578  0.0760  171 ASN A C   
1316 O  O   . ASN A 171 ? 0.2729 0.2149 0.3579 0.0228  0.0533  -0.0241 171 ASN A O   
1317 C  CB  . ASN A 171 ? 0.2744 0.1515 0.3261 0.0156  0.0314  0.0398  171 ASN A CB  
1318 C  CG  . ASN A 171 ? 0.2124 0.1389 0.3170 -0.0095 0.0064  0.0220  171 ASN A CG  
1319 O  OD1 . ASN A 171 ? 0.2977 0.2092 0.3622 -0.0397 -0.0370 -0.0143 171 ASN A OD1 
1320 N  ND2 . ASN A 171 ? 0.2671 0.1190 0.3120 0.0018  -0.0253 0.0624  171 ASN A ND2 
1321 N  N   . ILE A 172 ? 0.3233 0.1112 0.2866 0.0116  -0.0181 -0.0111 172 ILE A N   
1322 C  CA  . ILE A 172 ? 0.3191 0.1798 0.2846 -0.0583 -0.0185 0.0013  172 ILE A CA  
1323 C  C   . ILE A 172 ? 0.2946 0.2008 0.3189 -0.0619 0.0222  -0.0571 172 ILE A C   
1324 O  O   . ILE A 172 ? 0.2964 0.2994 0.3941 -0.0643 0.0838  -0.1397 172 ILE A O   
1325 C  CB  . ILE A 172 ? 0.3265 0.1736 0.2438 -0.0468 -0.0120 -0.0186 172 ILE A CB  
1326 C  CG1 . ILE A 172 ? 0.3129 0.1180 0.2680 0.0041  -0.0525 -0.0190 172 ILE A CG1 
1327 C  CG2 . ILE A 172 ? 0.4325 0.2589 0.2463 -0.1031 -0.0541 -0.0007 172 ILE A CG2 
1328 C  CD1 . ILE A 172 ? 0.3574 0.1120 0.2828 -0.0045 -0.0112 -0.0277 172 ILE A CD1 
1329 N  N   . ALA A 173 ? 0.3107 0.1958 0.3882 -0.0400 0.0148  -0.0614 173 ALA A N   
1330 C  CA  . ALA A 173 ? 0.3438 0.2315 0.4325 -0.0595 0.0241  -0.1312 173 ALA A CA  
1331 C  C   . ALA A 173 ? 0.4281 0.3384 0.4183 -0.1498 -0.0182 -0.1274 173 ALA A C   
1332 O  O   . ALA A 173 ? 0.3806 0.4463 0.3919 -0.0563 0.0193  -0.1391 173 ALA A O   
1333 C  CB  . ALA A 173 ? 0.5359 0.2577 0.5463 -0.0194 -0.0114 -0.2346 173 ALA A CB  
1334 N  N   . SER A 174 ? 0.4729 0.3527 0.4211 -0.1583 -0.0008 -0.1170 174 SER A N   
1335 C  CA  . SER A 174 ? 0.4212 0.4812 0.4194 -0.1730 -0.0087 -0.0951 174 SER A CA  
1336 C  C   . SER A 174 ? 0.3844 0.4504 0.3160 -0.1222 -0.0019 -0.0891 174 SER A C   
1337 O  O   . SER A 174 ? 0.3943 0.4604 0.3611 -0.1305 0.0475  -0.0938 174 SER A O   
1338 C  CB  . SER A 174 ? 0.4901 0.5269 0.4233 -0.2053 -0.1137 -0.2003 174 SER A CB  
1339 O  OG  . SER A 174 ? 0.4382 0.5783 0.4485 -0.0881 -0.1085 -0.2152 174 SER A OG  
1340 N  N   . ALA A 175 ? 0.4251 0.5008 0.3128 -0.0756 -0.0445 -0.1222 175 ALA A N   
1341 C  CA  . ALA A 175 ? 0.3740 0.4955 0.3547 -0.0285 -0.1021 -0.0116 175 ALA A CA  
1342 C  C   . ALA A 175 ? 0.3764 0.5213 0.3495 -0.0289 -0.1000 -0.0297 175 ALA A C   
1343 O  O   . ALA A 175 ? 0.3765 0.4407 0.3860 0.0131  -0.0386 -0.0671 175 ALA A O   
1344 C  CB  . ALA A 175 ? 0.2659 0.5229 0.3576 -0.0674 -0.1190 0.0141  175 ALA A CB  
1345 N  N   . THR A 176 ? 0.3666 0.6014 0.3834 -0.0197 -0.1055 -0.0777 176 THR A N   
1346 C  CA  . THR A 176 ? 0.4850 0.6878 0.3581 0.0151  -0.1095 -0.0745 176 THR A CA  
1347 C  C   . THR A 176 ? 0.5072 0.5702 0.3157 0.0152  -0.0494 -0.1009 176 THR A C   
1348 O  O   . THR A 176 ? 0.5062 0.5850 0.3928 0.0373  -0.0580 -0.0095 176 THR A O   
1349 C  CB  . THR A 176 ? 0.5908 0.7178 0.3920 -0.0520 -0.1536 -0.0597 176 THR A CB  
1350 O  OG1 . THR A 176 ? 0.7770 0.6564 0.6038 -0.1266 -0.2246 -0.0350 176 THR A OG1 
1351 C  CG2 . THR A 176 ? 0.8090 0.7215 0.6037 -0.1302 -0.4016 0.0725  176 THR A CG2 
1352 N  N   . LYS A 177 ? 0.5141 0.5245 0.3102 -0.0309 -0.0549 -0.1349 177 LYS A N   
1353 C  CA  . LYS A 177 ? 0.5131 0.4514 0.2824 -0.0561 -0.0632 -0.1109 177 LYS A CA  
1354 C  C   . LYS A 177 ? 0.4739 0.3789 0.2536 -0.0839 0.0141  -0.0854 177 LYS A C   
1355 O  O   . LYS A 177 ? 0.4476 0.3236 0.3692 -0.0122 0.0348  -0.0590 177 LYS A O   
1356 C  CB  . LYS A 177 ? 0.6256 0.3959 0.5249 -0.1066 -0.1125 -0.1441 177 LYS A CB  
1357 C  CG  . LYS A 177 ? 0.8240 0.5238 0.7893 -0.1658 -0.2270 -0.2545 177 LYS A CG  
1358 C  CD  . LYS A 177 ? 0.9727 0.5354 0.9329 -0.2068 -0.4386 -0.3017 177 LYS A CD  
1359 C  CE  . LYS A 177 ? 0.9795 0.5389 1.0885 -0.2111 -0.4320 -0.3856 177 LYS A CE  
1360 N  NZ  . LYS A 177 ? 1.2176 0.7549 1.2701 -0.1286 -0.7251 -0.4502 177 LYS A NZ  
1361 N  N   . PHE A 178 ? 0.4434 0.3546 0.3012 -0.0094 -0.0076 -0.1162 178 PHE A N   
1362 C  CA  . PHE A 178 ? 0.4264 0.2851 0.2590 -0.0059 0.0080  -0.0701 178 PHE A CA  
1363 C  C   . PHE A 178 ? 0.3786 0.3116 0.2854 0.0303  -0.0053 -0.0181 178 PHE A C   
1364 O  O   . PHE A 178 ? 0.3744 0.2447 0.2925 0.0424  -0.0108 -0.0384 178 PHE A O   
1365 C  CB  . PHE A 178 ? 0.3333 0.3371 0.3017 -0.0933 0.0328  -0.1155 178 PHE A CB  
1366 C  CG  . PHE A 178 ? 0.3113 0.2556 0.2952 -0.0601 0.0233  -0.0942 178 PHE A CG  
1367 C  CD1 . PHE A 178 ? 0.4054 0.2821 0.3059 -0.0302 -0.0091 -0.0785 178 PHE A CD1 
1368 C  CD2 . PHE A 178 ? 0.3860 0.2686 0.3760 0.0105  -0.0164 -0.1679 178 PHE A CD2 
1369 C  CE1 . PHE A 178 ? 0.3033 0.2285 0.3228 -0.0293 0.0204  -0.0134 178 PHE A CE1 
1370 C  CE2 . PHE A 178 ? 0.3470 0.1888 0.3758 -0.0054 -0.0009 -0.1001 178 PHE A CE2 
1371 C  CZ  . PHE A 178 ? 0.2929 0.2302 0.3402 -0.0108 0.0630  -0.0473 178 PHE A CZ  
1372 N  N   . LYS A 179 ? 0.3741 0.3066 0.2967 0.0495  -0.0189 -0.0638 179 LYS A N   
1373 C  CA  . LYS A 179 ? 0.4184 0.3840 0.2978 0.0635  -0.0260 0.0218  179 LYS A CA  
1374 C  C   . LYS A 179 ? 0.3775 0.3716 0.3110 0.0287  -0.0397 -0.0111 179 LYS A C   
1375 O  O   . LYS A 179 ? 0.4290 0.3471 0.3396 0.0068  -0.0151 -0.0261 179 LYS A O   
1376 C  CB  . LYS A 179 ? 0.4008 0.4747 0.3455 0.0761  -0.0050 0.0674  179 LYS A CB  
1377 C  CG  . LYS A 179 ? 0.4169 0.5364 0.5033 0.0780  0.0871  0.0839  179 LYS A CG  
1378 C  CD  . LYS A 179 ? 0.4782 0.5610 0.5637 0.1854  0.0822  0.1507  179 LYS A CD  
1379 C  CE  . LYS A 179 ? 0.7758 0.5714 0.6563 0.0718  -0.0026 0.2126  179 LYS A CE  
1380 N  NZ  . LYS A 179 ? 1.1023 0.7510 0.9861 -0.2139 0.0539  0.1499  179 LYS A NZ  
1381 N  N   . GLN A 180 ? 0.3785 0.3690 0.3313 -0.0110 0.0017  -0.0064 180 GLN A N   
1382 C  CA  . GLN A 180 ? 0.4326 0.4312 0.3223 -0.0423 0.0162  -0.0600 180 GLN A CA  
1383 C  C   . GLN A 180 ? 0.3832 0.3377 0.3616 -0.0436 0.0603  -0.0238 180 GLN A C   
1384 O  O   . GLN A 180 ? 0.4342 0.3064 0.3977 -0.0877 0.0985  -0.0789 180 GLN A O   
1385 C  CB  . GLN A 180 ? 0.6575 0.6331 0.3523 -0.1739 0.0266  -0.1896 180 GLN A CB  
1386 C  CG  . GLN A 180 ? 0.7579 0.9128 0.4357 -0.2763 -0.1105 -0.1472 180 GLN A CG  
1387 C  CD  . GLN A 180 ? 0.9483 1.0282 0.5225 -0.3482 -0.1612 -0.2216 180 GLN A CD  
1388 O  OE1 . GLN A 180 ? 1.1093 0.9772 0.4141 -0.4820 0.0239  -0.2257 180 GLN A OE1 
1389 N  NE2 . GLN A 180 ? 1.2292 1.2033 0.5630 -0.1153 -0.2928 -0.3597 180 GLN A NE2 
1390 N  N   . LEU A 181 ? 0.3856 0.2671 0.3786 -0.0275 0.0466  -0.0323 181 LEU A N   
1391 C  CA  . LEU A 181 ? 0.3468 0.2618 0.3560 0.0036  0.1009  -0.0377 181 LEU A CA  
1392 C  C   . LEU A 181 ? 0.3077 0.2431 0.3308 0.0168  0.0744  -0.0029 181 LEU A C   
1393 O  O   . LEU A 181 ? 0.3087 0.3142 0.4235 0.0064  0.0855  -0.0139 181 LEU A O   
1394 C  CB  . LEU A 181 ? 0.3200 0.2883 0.4210 -0.0437 0.0642  0.0131  181 LEU A CB  
1395 C  CG  . LEU A 181 ? 0.3096 0.2517 0.4614 -0.0009 0.0610  0.0314  181 LEU A CG  
1396 C  CD1 . LEU A 181 ? 0.3421 0.2502 0.5116 -0.0029 0.0680  -0.0387 181 LEU A CD1 
1397 C  CD2 . LEU A 181 ? 0.3198 0.3146 0.5290 0.0126  0.0479  0.1109  181 LEU A CD2 
1398 N  N   . TYR A 182 ? 0.3133 0.2609 0.3195 0.0273  0.0430  -0.0286 182 TYR A N   
1399 C  CA  . TYR A 182 ? 0.3416 0.2370 0.3152 0.0487  -0.0112 -0.0014 182 TYR A CA  
1400 C  C   . TYR A 182 ? 0.4644 0.2835 0.2904 -0.0453 -0.0014 -0.0312 182 TYR A C   
1401 O  O   . TYR A 182 ? 0.3833 0.2039 0.3821 0.0393  0.0078  -0.0057 182 TYR A O   
1402 C  CB  . TYR A 182 ? 0.3387 0.2899 0.3586 0.0408  -0.0229 -0.0763 182 TYR A CB  
1403 C  CG  . TYR A 182 ? 0.3542 0.2470 0.3786 0.0453  -0.0566 -0.0522 182 TYR A CG  
1404 C  CD1 . TYR A 182 ? 0.4537 0.2614 0.4292 0.0105  -0.0598 -0.0168 182 TYR A CD1 
1405 C  CD2 . TYR A 182 ? 0.3459 0.2526 0.4087 0.0124  -0.1057 -0.0453 182 TYR A CD2 
1406 C  CE1 . TYR A 182 ? 0.4680 0.2237 0.4509 0.0524  -0.0994 -0.0110 182 TYR A CE1 
1407 C  CE2 . TYR A 182 ? 0.1947 0.2195 0.3510 -0.0321 0.0112  -0.0201 182 TYR A CE2 
1408 C  CZ  . TYR A 182 ? 0.3426 0.2267 0.4412 -0.0022 -0.0700 0.0059  182 TYR A CZ  
1409 O  OH  . TYR A 182 ? 0.5572 0.1790 0.4089 0.0539  -0.0591 -0.0008 182 TYR A OH  
1410 N  N   . ARG A 183 ? 0.4347 0.2841 0.2652 0.0335  0.0288  -0.0534 183 ARG A N   
1411 C  CA  . ARG A 183 ? 0.3550 0.2945 0.3026 0.0788  0.0264  -0.0160 183 ARG A CA  
1412 C  C   . ARG A 183 ? 0.3524 0.2969 0.4034 0.0820  0.0338  -0.0226 183 ARG A C   
1413 O  O   . ARG A 183 ? 0.3359 0.3551 0.5678 0.0364  0.0410  -0.0983 183 ARG A O   
1414 C  CB  . ARG A 183 ? 0.3324 0.3139 0.2978 0.0274  0.0308  -0.0141 183 ARG A CB  
1415 C  CG  . ARG A 183 ? 0.3434 0.3253 0.4064 0.0573  -0.0250 -0.0736 183 ARG A CG  
1416 C  CD  . ARG A 183 ? 0.4119 0.3798 0.4674 0.0883  -0.0897 -0.0933 183 ARG A CD  
1417 N  NE  . ARG A 183 ? 0.3619 0.3615 0.5296 0.0449  -0.0788 -0.0456 183 ARG A NE  
1418 C  CZ  . ARG A 183 ? 0.3917 0.3430 0.5993 0.0113  -0.0821 -0.0420 183 ARG A CZ  
1419 N  NH1 . ARG A 183 ? 0.6627 0.3926 0.6978 -0.0937 -0.1763 -0.0723 183 ARG A NH1 
1420 N  NH2 . ARG A 183 ? 0.3759 0.6228 0.8865 0.0852  -0.0471 -0.3507 183 ARG A NH2 
1421 N  N   . SER A 184 ? 0.3858 0.2976 0.4521 0.0934  -0.0353 -0.0801 184 SER A N   
1422 C  CA  . SER A 184 ? 0.3806 0.2473 0.4534 0.0243  0.0386  -0.1143 184 SER A CA  
1423 C  C   . SER A 184 ? 0.3460 0.2474 0.4274 0.0501  0.0479  -0.0780 184 SER A C   
1424 O  O   . SER A 184 ? 0.3267 0.3303 0.4374 0.0869  0.0378  -0.0206 184 SER A O   
1425 C  CB  . SER A 184 ? 0.4905 0.2366 0.6702 0.0281  0.0321  -0.1501 184 SER A CB  
1426 O  OG  . SER A 184 ? 0.6124 0.3142 0.6650 0.1461  0.0641  -0.1172 184 SER A OG  
1427 N  N   . ARG A 185 ? 0.3728 0.2537 0.4170 0.0302  0.0374  -0.0268 185 ARG A N   
1428 C  CA  . ARG A 185 ? 0.3193 0.2021 0.3934 0.0198  0.0632  0.0212  185 ARG A CA  
1429 C  C   . ARG A 185 ? 0.3060 0.2050 0.4132 0.0292  0.0629  0.0533  185 ARG A C   
1430 O  O   . ARG A 185 ? 0.3126 0.2027 0.4301 0.0219  0.0539  0.0514  185 ARG A O   
1431 C  CB  . ARG A 185 ? 0.2872 0.1596 0.4057 0.0281  0.0779  0.0119  185 ARG A CB  
1432 C  CG  . ARG A 185 ? 0.2424 0.1631 0.4469 0.0008  0.0410  0.0180  185 ARG A CG  
1433 C  CD  . ARG A 185 ? 0.2994 0.1988 0.4294 0.0572  0.0814  0.0511  185 ARG A CD  
1434 N  NE  . ARG A 185 ? 0.2644 0.1928 0.3801 0.0134  0.0172  0.0304  185 ARG A NE  
1435 C  CZ  . ARG A 185 ? 0.2705 0.1671 0.3898 0.0252  -0.0399 0.0172  185 ARG A CZ  
1436 N  NH1 . ARG A 185 ? 0.3150 0.1940 0.4106 -0.0286 0.0064  -0.0031 185 ARG A NH1 
1437 N  NH2 . ARG A 185 ? 0.3814 0.1872 0.3481 -0.0330 0.0150  0.0071  185 ARG A NH2 
1438 N  N   . MET A 186 ? 0.3343 0.2298 0.3389 0.0568  0.0388  0.0477  186 MET A N   
1439 C  CA  . MET A 186 ? 0.3517 0.2209 0.3734 0.0607  0.0494  0.0394  186 MET A CA  
1440 C  C   . MET A 186 ? 0.3473 0.2377 0.3653 -0.0062 0.0357  0.0139  186 MET A C   
1441 O  O   . MET A 186 ? 0.3726 0.2305 0.3926 -0.0172 0.0264  0.0214  186 MET A O   
1442 C  CB  . MET A 186 ? 0.4384 0.2730 0.4903 0.1525  0.0650  0.0487  186 MET A CB  
1443 C  CG  . MET A 186 ? 0.5339 0.4621 0.5688 0.2563  0.0117  -0.0718 186 MET A CG  
1444 S  SD  . MET A 186 ? 0.5546 0.4272 0.4958 0.2768  0.0861  0.0493  186 MET A SD  
1445 C  CE  . MET A 186 ? 0.5416 1.1047 0.6608 0.4248  -0.0601 -0.5265 186 MET A CE  
1446 N  N   . ASN A 187 ? 0.3978 0.2285 0.4149 -0.0256 0.0800  -0.0352 187 ASN A N   
1447 C  CA  . ASN A 187 ? 0.4999 0.2639 0.4107 0.0192  0.1087  -0.0171 187 ASN A CA  
1448 C  C   . ASN A 187 ? 0.4538 0.2196 0.4263 -0.0306 0.1617  0.0262  187 ASN A C   
1449 O  O   . ASN A 187 ? 0.5688 0.3641 0.4520 -0.0407 0.2538  -0.0062 187 ASN A O   
1450 C  CB  . ASN A 187 ? 0.5430 0.2868 0.4091 0.0357  0.0963  -0.0294 187 ASN A CB  
1451 C  CG  . ASN A 187 ? 0.4976 0.2701 0.4311 0.0058  0.0981  -0.0660 187 ASN A CG  
1452 O  OD1 . ASN A 187 ? 0.6677 0.2389 0.4626 0.0434  0.0327  -0.0109 187 ASN A OD1 
1453 N  ND2 . ASN A 187 ? 0.5262 0.3352 0.5434 -0.1107 0.0749  -0.0056 187 ASN A ND2 
1454 N  N   . SER A 188 ? 0.5094 0.1859 0.4864 0.0151  0.1534  0.0375  188 SER A N   
1455 C  CA  . SER A 188 ? 0.5531 0.2760 0.6175 0.0781  0.1484  0.0694  188 SER A CA  
1456 C  C   . SER A 188 ? 0.4782 0.2204 0.6418 0.1312  0.0836  0.1311  188 SER A C   
1457 O  O   . SER A 188 ? 0.4572 0.2597 0.8548 0.1196  0.1703  0.1112  188 SER A O   
1458 C  CB  . SER A 188 ? 0.5467 0.2968 0.5810 0.0208  0.0129  0.0804  188 SER A CB  
1459 O  OG  . SER A 188 ? 0.4979 0.4532 0.5536 0.1433  -0.0874 0.0860  188 SER A OG  
1460 N  N   . LEU A 189 ? 0.4101 0.2960 0.5046 0.1141  0.0735  0.0983  189 LEU A N   
1461 C  CA  . LEU A 189 ? 0.3609 0.3721 0.4556 0.1540  0.0429  0.0501  189 LEU A CA  
1462 C  C   . LEU A 189 ? 0.3336 0.3262 0.5070 0.1172  0.0376  0.0294  189 LEU A C   
1463 O  O   . LEU A 189 ? 0.3603 0.5092 0.6255 0.0129  0.0083  0.2274  189 LEU A O   
1464 C  CB  . LEU A 189 ? 0.2928 0.3711 0.4697 0.1655  -0.0074 0.0495  189 LEU A CB  
1465 C  CG  . LEU A 189 ? 0.4081 0.4104 0.4124 0.2031  0.0129  0.0256  189 LEU A CG  
1466 C  CD1 . LEU A 189 ? 0.4949 0.2990 0.3262 0.1751  0.0223  -0.0093 189 LEU A CD1 
1467 C  CD2 . LEU A 189 ? 0.6698 0.4515 0.4768 0.2724  -0.1153 0.0431  189 LEU A CD2 
1468 N  N   . GLU A 190 ? 0.3375 0.3806 0.6503 0.1372  0.0041  0.0539  190 GLU A N   
1469 C  CA  . GLU A 190 ? 0.3146 0.4261 0.7256 0.1324  0.0546  0.0080  190 GLU A CA  
1470 C  C   . GLU A 190 ? 0.4721 0.4124 0.6996 0.0617  -0.0465 0.0519  190 GLU A C   
1471 O  O   . GLU A 190 ? 0.8359 0.2844 0.7372 0.0095  -0.2907 0.1426  190 GLU A O   
1472 C  CB  . GLU A 190 ? 0.3188 0.6609 0.7870 0.1987  -0.0276 -0.0902 190 GLU A CB  
1473 C  CG  . GLU A 190 ? 0.3777 0.7513 0.8447 0.3458  -0.0971 -0.1521 190 GLU A CG  
1474 C  CD  . GLU A 190 ? 0.5906 0.7025 0.9692 0.3644  -0.2260 -0.1579 190 GLU A CD  
1475 O  OE1 . GLU A 190 ? 0.7544 0.7348 1.1020 0.4781  -0.4330 -0.2065 190 GLU A OE1 
1476 O  OE2 . GLU A 190 ? 0.7994 0.7897 0.8859 0.4529  -0.2058 -0.4169 190 GLU A OE2 
1477 N  N   . MET A 191 ? 0.4097 0.4293 0.5306 -0.0299 0.0753  0.0058  191 MET A N   
1478 C  CA  . MET A 191 ? 0.4327 0.4132 0.5407 -0.0278 0.0694  0.0358  191 MET A CA  
1479 C  C   . MET A 191 ? 0.4157 0.4324 0.5267 0.0243  0.0486  0.0705  191 MET A C   
1480 O  O   . MET A 191 ? 0.3732 0.4533 0.5527 -0.0307 0.1125  0.0163  191 MET A O   
1481 C  CB  . MET A 191 ? 0.4677 0.4212 0.6006 -0.0135 0.1077  0.0234  191 MET A CB  
1482 C  CG  . MET A 191 ? 0.4703 0.3791 0.7735 0.2045  -0.0763 -0.1231 191 MET A CG  
1483 S  SD  . MET A 191 ? 0.4878 0.2872 0.4918 0.1245  0.0643  0.0860  191 MET A SD  
1484 C  CE  . MET A 191 ? 0.9979 0.2236 0.6429 0.2122  0.0299  0.2204  191 MET A CE  
1485 N  N   . THR A 192 ? 0.2951 0.4083 0.4232 0.0795  0.1093  0.0505  192 THR A N   
1486 C  CA  . THR A 192 ? 0.3843 0.4144 0.4430 0.0798  0.1174  0.0652  192 THR A CA  
1487 C  C   . THR A 192 ? 0.3829 0.4210 0.4579 0.0766  0.1304  0.1001  192 THR A C   
1488 O  O   . THR A 192 ? 0.3640 0.2666 0.4314 0.0272  0.1022  0.0617  192 THR A O   
1489 C  CB  . THR A 192 ? 0.4258 0.3880 0.5001 0.0546  0.0803  0.1161  192 THR A CB  
1490 O  OG1 . THR A 192 ? 0.4098 0.4697 0.4508 -0.0003 0.0557  0.0666  192 THR A OG1 
1491 C  CG2 . THR A 192 ? 0.4664 0.7022 0.7237 0.1650  -0.0523 0.0642  192 THR A CG2 
1492 N  N   . PRO A 193 ? 0.3828 0.4308 0.4408 0.0650  0.1244  0.0816  193 PRO A N   
1493 C  CA  . PRO A 193 ? 0.3570 0.3583 0.3928 0.0077  0.0911  0.0447  193 PRO A CA  
1494 C  C   . PRO A 193 ? 0.3722 0.3936 0.3640 0.0345  0.0410  0.0272  193 PRO A C   
1495 O  O   . PRO A 193 ? 0.3581 0.3486 0.3696 -0.0011 0.0586  0.0174  193 PRO A O   
1496 C  CB  . PRO A 193 ? 0.3730 0.3081 0.4572 0.0430  0.1572  0.0627  193 PRO A CB  
1497 C  CG  . PRO A 193 ? 0.4385 0.2582 0.4266 0.0337  0.1221  0.0150  193 PRO A CG  
1498 C  CD  . PRO A 193 ? 0.4003 0.3110 0.4440 0.0404  0.1330  0.0590  193 PRO A CD  
1499 N  N   . ALA A 194 ? 0.3598 0.4138 0.3370 0.0331  0.0367  0.0468  194 ALA A N   
1500 C  CA  . ALA A 194 ? 0.3412 0.3475 0.3569 -0.0300 0.0751  0.0659  194 ALA A CA  
1501 C  C   . ALA A 194 ? 0.3207 0.2999 0.4211 0.0468  0.1071  0.1197  194 ALA A C   
1502 O  O   . ALA A 194 ? 0.2741 0.3721 0.4156 0.0350  0.0294  -0.0252 194 ALA A O   
1503 C  CB  . ALA A 194 ? 0.3582 0.2134 0.5442 -0.0185 0.0145  0.0915  194 ALA A CB  
1504 N  N   . VAL A 195 ? 0.3996 0.3559 0.4319 0.0088  0.0257  0.1544  195 VAL A N   
1505 C  CA  . VAL A 195 ? 0.4026 0.2782 0.3979 0.0066  0.0089  0.1245  195 VAL A CA  
1506 C  C   . VAL A 195 ? 0.3944 0.2787 0.3235 0.0264  0.0189  0.1274  195 VAL A C   
1507 O  O   . VAL A 195 ? 0.3983 0.2572 0.4270 0.0246  0.0152  -0.0352 195 VAL A O   
1508 C  CB  . VAL A 195 ? 0.3144 0.3208 0.4254 0.0507  0.0727  0.1302  195 VAL A CB  
1509 C  CG1 . VAL A 195 ? 0.3394 0.2941 0.3994 0.0178  0.0290  0.1349  195 VAL A CG1 
1510 C  CG2 . VAL A 195 ? 0.2971 0.3594 0.4025 0.0392  0.0967  0.1289  195 VAL A CG2 
1511 N  N   . ARG A 196 ? 0.3639 0.2997 0.3985 0.0243  0.0603  0.0566  196 ARG A N   
1512 C  CA  . ARG A 196 ? 0.3699 0.1891 0.3673 0.0471  0.0690  0.0424  196 ARG A CA  
1513 C  C   . ARG A 196 ? 0.3424 0.1626 0.4043 0.0306  0.1094  0.0308  196 ARG A C   
1514 O  O   . ARG A 196 ? 0.3393 0.1994 0.3599 0.0201  0.0975  0.0437  196 ARG A O   
1515 C  CB  . ARG A 196 ? 0.3823 0.1912 0.4130 0.0416  0.1177  0.0104  196 ARG A CB  
1516 C  CG  . ARG A 196 ? 0.4859 0.3428 0.5357 -0.0782 0.1198  -0.1202 196 ARG A CG  
1517 C  CD  . ARG A 196 ? 0.6003 0.5874 0.6240 -0.0947 0.1393  -0.2682 196 ARG A CD  
1518 N  NE  . ARG A 196 ? 0.5411 0.8235 0.6384 -0.1754 0.2185  -0.3762 196 ARG A NE  
1519 C  CZ  . ARG A 196 ? 0.5994 0.8453 0.7371 -0.1814 0.1802  -0.4153 196 ARG A CZ  
1520 N  NH1 . ARG A 196 ? 0.5784 0.8047 0.8028 -0.2904 0.2625  -0.2709 196 ARG A NH1 
1521 N  NH2 . ARG A 196 ? 0.8265 0.9512 0.7548 -0.2187 0.0368  -0.4251 196 ARG A NH2 
1522 N  N   . GLN A 197 ? 0.3090 0.1903 0.4057 0.0174  0.0454  0.0628  197 GLN A N   
1523 C  CA  . GLN A 197 ? 0.3363 0.1587 0.3525 0.0017  0.0041  0.0209  197 GLN A CA  
1524 C  C   . GLN A 197 ? 0.2855 0.1913 0.3513 0.0026  0.0058  0.0431  197 GLN A C   
1525 O  O   . GLN A 197 ? 0.2707 0.1896 0.3807 -0.0174 0.0026  0.0356  197 GLN A O   
1526 C  CB  . GLN A 197 ? 0.4039 0.2426 0.4347 0.0258  0.0807  0.1318  197 GLN A CB  
1527 C  CG  . GLN A 197 ? 0.5254 0.5214 0.5346 0.0343  0.2096  0.0708  197 GLN A CG  
1528 C  CD  . GLN A 197 ? 0.6013 0.7022 0.5679 -0.0616 0.2444  0.0723  197 GLN A CD  
1529 O  OE1 . GLN A 197 ? 0.8022 0.7612 0.8179 -0.2338 -0.1434 0.3863  197 GLN A OE1 
1530 N  NE2 . GLN A 197 ? 0.9200 1.0723 0.5984 0.1365  0.4206  0.1749  197 GLN A NE2 
1531 N  N   . ARG A 198 ? 0.2686 0.2048 0.3373 -0.0376 0.0141  0.0557  198 ARG A N   
1532 C  CA  . ARG A 198 ? 0.3163 0.1730 0.3483 -0.0276 0.0265  0.0471  198 ARG A CA  
1533 C  C   . ARG A 198 ? 0.2998 0.1457 0.3293 0.0070  0.0287  0.0674  198 ARG A C   
1534 O  O   . ARG A 198 ? 0.2914 0.2011 0.2977 -0.0057 0.0045  0.0145  198 ARG A O   
1535 C  CB  . ARG A 198 ? 0.2902 0.2307 0.3205 -0.0058 0.0507  0.0339  198 ARG A CB  
1536 C  CG  . ARG A 198 ? 0.3901 0.2800 0.4117 -0.1041 -0.0138 0.0402  198 ARG A CG  
1537 C  CD  . ARG A 198 ? 0.4934 0.3298 0.3902 -0.1450 -0.0559 0.0969  198 ARG A CD  
1538 N  NE  . ARG A 198 ? 0.4909 0.3805 0.4679 -0.1002 -0.0637 0.1103  198 ARG A NE  
1539 C  CZ  . ARG A 198 ? 0.5361 0.3261 0.4614 -0.1102 -0.0109 0.0839  198 ARG A CZ  
1540 N  NH1 . ARG A 198 ? 0.4520 0.5284 0.5141 -0.1401 -0.0577 0.2085  198 ARG A NH1 
1541 N  NH2 . ARG A 198 ? 0.5395 0.3221 0.4215 -0.0665 0.0476  0.0649  198 ARG A NH2 
1542 N  N   . VAL A 199 ? 0.3132 0.1432 0.3668 0.0083  0.0481  0.0742  199 VAL A N   
1543 C  CA  . VAL A 199 ? 0.2962 0.1641 0.2869 -0.0180 0.0079  0.0375  199 VAL A CA  
1544 C  C   . VAL A 199 ? 0.3078 0.2081 0.3033 0.0256  0.0140  0.0363  199 VAL A C   
1545 O  O   . VAL A 199 ? 0.3095 0.1772 0.3610 0.0330  0.0338  0.0481  199 VAL A O   
1546 C  CB  . VAL A 199 ? 0.3086 0.1515 0.3376 -0.0116 -0.0003 0.0670  199 VAL A CB  
1547 C  CG1 . VAL A 199 ? 0.3361 0.1588 0.3003 -0.0312 0.0029  0.0637  199 VAL A CG1 
1548 C  CG2 . VAL A 199 ? 0.3516 0.1669 0.3251 0.0180  -0.0395 -0.0177 199 VAL A CG2 
1549 N  N   . ILE A 200 ? 0.3203 0.2168 0.3141 0.0083  -0.0068 0.0579  200 ILE A N   
1550 C  CA  . ILE A 200 ? 0.3089 0.2164 0.3215 0.0409  0.0115  0.0591  200 ILE A CA  
1551 C  C   . ILE A 200 ? 0.2715 0.2183 0.3213 -0.0113 0.0591  0.0337  200 ILE A C   
1552 O  O   . ILE A 200 ? 0.2622 0.2150 0.3453 0.0113  0.0216  0.0627  200 ILE A O   
1553 C  CB  . ILE A 200 ? 0.3399 0.2497 0.3097 0.1062  0.0029  0.0334  200 ILE A CB  
1554 C  CG1 . ILE A 200 ? 0.4771 0.3100 0.4637 0.1239  0.0530  -0.0509 200 ILE A CG1 
1555 C  CG2 . ILE A 200 ? 0.3845 0.3548 0.3839 0.0960  -0.0471 0.1064  200 ILE A CG2 
1556 C  CD1 . ILE A 200 ? 0.9269 0.4160 0.6795 -0.0647 -0.1253 -0.1358 200 ILE A CD1 
1557 N  N   . GLU A 201 ? 0.2890 0.2235 0.3023 -0.0171 -0.0014 0.0749  201 GLU A N   
1558 C  CA  . GLU A 201 ? 0.3391 0.2363 0.3197 -0.0296 -0.0219 0.0226  201 GLU A CA  
1559 C  C   . GLU A 201 ? 0.3076 0.2162 0.3431 0.0201  -0.0010 0.0594  201 GLU A C   
1560 O  O   . GLU A 201 ? 0.3566 0.1986 0.3800 0.0588  0.0089  0.0779  201 GLU A O   
1561 C  CB  . GLU A 201 ? 0.3888 0.2166 0.4862 -0.0508 0.0059  0.1006  201 GLU A CB  
1562 C  CG  . GLU A 201 ? 0.4875 0.3151 0.5182 -0.0460 -0.0124 0.1971  201 GLU A CG  
1563 C  CD  . GLU A 201 ? 0.5907 0.3819 0.5793 0.0859  -0.0565 0.1754  201 GLU A CD  
1564 O  OE1 . GLU A 201 ? 0.6218 0.1908 0.7099 0.0215  -0.0506 0.1621  201 GLU A OE1 
1565 O  OE2 . GLU A 201 ? 0.7066 0.6777 0.5361 0.2752  -0.1005 0.1621  201 GLU A OE2 
1566 N  N   . GLU A 202 ? 0.2721 0.1697 0.3843 0.0133  0.0359  0.0672  202 GLU A N   
1567 C  CA  . GLU A 202 ? 0.2561 0.1506 0.3576 -0.0047 -0.0079 0.0578  202 GLU A CA  
1568 C  C   . GLU A 202 ? 0.2328 0.1663 0.3014 0.0162  -0.0038 0.0453  202 GLU A C   
1569 O  O   . GLU A 202 ? 0.2449 0.1552 0.3587 0.0472  0.0135  0.0105  202 GLU A O   
1570 C  CB  . GLU A 202 ? 0.2303 0.1257 0.3982 -0.0070 -0.0146 0.0512  202 GLU A CB  
1571 C  CG  . GLU A 202 ? 0.3070 0.1383 0.3821 0.0056  -0.0355 0.0648  202 GLU A CG  
1572 C  CD  . GLU A 202 ? 0.2723 0.1472 0.3839 -0.0147 -0.0211 0.0565  202 GLU A CD  
1573 O  OE1 . GLU A 202 ? 0.2531 0.1772 0.3907 -0.0267 -0.0116 0.0402  202 GLU A OE1 
1574 O  OE2 . GLU A 202 ? 0.2515 0.1554 0.3876 -0.0245 -0.0231 0.0537  202 GLU A OE2 
1575 N  N   . ALA A 203 ? 0.2371 0.1408 0.3542 0.0093  0.0317  0.0192  203 ALA A N   
1576 C  CA  . ALA A 203 ? 0.2512 0.1361 0.3442 -0.0030 0.0164  0.0305  203 ALA A CA  
1577 C  C   . ALA A 203 ? 0.2558 0.1789 0.3068 0.0159  -0.0135 0.0294  203 ALA A C   
1578 O  O   . ALA A 203 ? 0.2619 0.1942 0.3028 0.0289  -0.0137 0.0434  203 ALA A O   
1579 C  CB  . ALA A 203 ? 0.4237 0.1032 0.3647 -0.0009 -0.0536 0.0377  203 ALA A CB  
1580 N  N   . LYS A 204 ? 0.2764 0.1964 0.2598 0.0439  -0.0040 0.0315  204 LYS A N   
1581 C  CA  . LYS A 204 ? 0.2916 0.1905 0.3079 0.0468  -0.0158 0.0288  204 LYS A CA  
1582 C  C   . LYS A 204 ? 0.2541 0.1571 0.3221 0.0282  -0.0126 0.0319  204 LYS A C   
1583 O  O   . LYS A 204 ? 0.2493 0.1804 0.3067 0.0252  -0.0044 0.0527  204 LYS A O   
1584 C  CB  . LYS A 204 ? 0.3017 0.1624 0.3642 0.0926  0.0629  0.0278  204 LYS A CB  
1585 C  CG  . LYS A 204 ? 0.3832 0.2359 0.3505 0.1099  0.1049  0.0258  204 LYS A CG  
1586 C  CD  . LYS A 204 ? 0.5701 0.3649 0.4039 0.0217  0.1587  0.0669  204 LYS A CD  
1587 C  CE  . LYS A 204 ? 0.8347 0.5301 0.3778 -0.0798 0.1107  0.1210  204 LYS A CE  
1588 N  NZ  . LYS A 204 ? 1.1090 0.9567 0.4782 0.0112  0.3078  0.3105  204 LYS A NZ  
1589 N  N   . THR A 205 ? 0.2466 0.1432 0.3504 -0.0027 -0.0101 0.0243  205 THR A N   
1590 C  CA  . THR A 205 ? 0.2739 0.1693 0.3245 0.0174  -0.0241 0.0417  205 THR A CA  
1591 C  C   . THR A 205 ? 0.2470 0.1615 0.3522 0.0526  -0.0091 0.0610  205 THR A C   
1592 O  O   . THR A 205 ? 0.2298 0.1261 0.4174 0.0268  -0.0038 0.0308  205 THR A O   
1593 C  CB  . THR A 205 ? 0.2779 0.1680 0.3094 0.0109  -0.0186 0.0504  205 THR A CB  
1594 O  OG1 . THR A 205 ? 0.3454 0.2036 0.3832 -0.0573 -0.0076 0.0597  205 THR A OG1 
1595 C  CG2 . THR A 205 ? 0.3834 0.2828 0.3460 -0.0596 -0.0175 -0.0254 205 THR A CG2 
1596 N  N   . ALA A 206 ? 0.2189 0.1583 0.3383 0.0332  0.0263  0.0126  206 ALA A N   
1597 C  CA  . ALA A 206 ? 0.2391 0.1576 0.3069 0.0070  -0.0075 0.0121  206 ALA A CA  
1598 C  C   . ALA A 206 ? 0.2316 0.1626 0.2770 -0.0089 -0.0054 0.0129  206 ALA A C   
1599 O  O   . ALA A 206 ? 0.2515 0.1874 0.3009 0.0077  0.0167  0.0343  206 ALA A O   
1600 C  CB  . ALA A 206 ? 0.2732 0.1565 0.2816 0.0103  -0.0272 -0.0002 206 ALA A CB  
1601 N  N   . PHE A 207 ? 0.2810 0.1774 0.2839 0.0196  -0.0232 -0.0018 207 PHE A N   
1602 C  CA  . PHE A 207 ? 0.2760 0.1820 0.2535 0.0170  -0.0115 0.0152  207 PHE A CA  
1603 C  C   . PHE A 207 ? 0.2688 0.1823 0.2566 0.0163  0.0030  0.0217  207 PHE A C   
1604 O  O   . PHE A 207 ? 0.2719 0.2148 0.2517 0.0386  0.0001  0.0370  207 PHE A O   
1605 C  CB  . PHE A 207 ? 0.2610 0.1817 0.2508 -0.0344 0.0007  0.0196  207 PHE A CB  
1606 C  CG  . PHE A 207 ? 0.2620 0.1859 0.2925 -0.0115 -0.0474 0.0078  207 PHE A CG  
1607 C  CD1 . PHE A 207 ? 0.2719 0.2049 0.3526 -0.0128 -0.0060 -0.0156 207 PHE A CD1 
1608 C  CD2 . PHE A 207 ? 0.2646 0.1850 0.3732 0.0020  -0.0803 -0.0325 207 PHE A CD2 
1609 C  CE1 . PHE A 207 ? 0.2529 0.2046 0.3303 -0.0158 0.0041  -0.0048 207 PHE A CE1 
1610 C  CE2 . PHE A 207 ? 0.2560 0.1560 0.3520 0.0135  -0.0455 -0.0102 207 PHE A CE2 
1611 C  CZ  . PHE A 207 ? 0.2372 0.2026 0.2768 0.0059  -0.0043 -0.0015 207 PHE A CZ  
1612 N  N   . LEU A 208 ? 0.2510 0.1818 0.2898 0.0150  -0.0489 0.0222  208 LEU A N   
1613 C  CA  . LEU A 208 ? 0.2856 0.1768 0.2922 0.0217  -0.0371 0.0406  208 LEU A CA  
1614 C  C   . LEU A 208 ? 0.2270 0.1346 0.2955 0.0066  -0.0355 0.0417  208 LEU A C   
1615 O  O   . LEU A 208 ? 0.2432 0.1595 0.3296 0.0232  -0.0267 0.0321  208 LEU A O   
1616 C  CB  . LEU A 208 ? 0.3362 0.1681 0.3378 0.0372  0.0324  0.0630  208 LEU A CB  
1617 C  CG  . LEU A 208 ? 0.3256 0.2429 0.3285 0.0159  0.0444  0.0213  208 LEU A CG  
1618 C  CD1 . LEU A 208 ? 0.4206 0.2670 0.3338 -0.0726 0.0096  0.0718  208 LEU A CD1 
1619 C  CD2 . LEU A 208 ? 0.4212 0.2857 0.3832 0.0262  -0.1222 -0.0259 208 LEU A CD2 
1620 N  N   . LEU A 209 ? 0.2578 0.1760 0.2861 0.0373  -0.0134 0.0579  209 LEU A N   
1621 C  CA  . LEU A 209 ? 0.1931 0.1609 0.2766 0.0346  -0.0375 0.0084  209 LEU A CA  
1622 C  C   . LEU A 209 ? 0.2058 0.1797 0.2337 0.0213  -0.0502 0.0139  209 LEU A C   
1623 O  O   . LEU A 209 ? 0.2315 0.2104 0.2502 0.0085  -0.0148 0.0168  209 LEU A O   
1624 C  CB  . LEU A 209 ? 0.2140 0.1359 0.3206 -0.0056 -0.0814 0.0303  209 LEU A CB  
1625 C  CG  . LEU A 209 ? 0.2002 0.1594 0.3091 0.0060  -0.0690 -0.0187 209 LEU A CG  
1626 C  CD1 . LEU A 209 ? 0.2089 0.2203 0.3305 0.0505  0.0096  0.0235  209 LEU A CD1 
1627 C  CD2 . LEU A 209 ? 0.2141 0.1842 0.3255 -0.0052 -0.0509 -0.0360 209 LEU A CD2 
1628 N  N   . ASN A 210 ? 0.2296 0.1609 0.2732 0.0109  -0.0473 0.0184  210 ASN A N   
1629 C  CA  . ASN A 210 ? 0.2366 0.1520 0.3085 0.0052  -0.0344 0.0193  210 ASN A CA  
1630 C  C   . ASN A 210 ? 0.2306 0.2009 0.2516 0.0199  -0.0401 0.0133  210 ASN A C   
1631 O  O   . ASN A 210 ? 0.2505 0.1778 0.3413 0.0146  0.0143  0.0342  210 ASN A O   
1632 C  CB  . ASN A 210 ? 0.2705 0.1650 0.2810 -0.0149 -0.0355 0.0203  210 ASN A CB  
1633 C  CG  . ASN A 210 ? 0.2368 0.1394 0.2589 -0.0384 -0.0097 0.0167  210 ASN A CG  
1634 O  OD1 . ASN A 210 ? 0.2919 0.1829 0.3272 -0.0796 0.0180  0.0387  210 ASN A OD1 
1635 N  ND2 . ASN A 210 ? 0.2610 0.1622 0.3057 -0.0101 0.0163  0.0131  210 ASN A ND2 
1636 N  N   . ILE A 211 ? 0.2263 0.2047 0.2574 0.0007  -0.0546 0.0167  211 ILE A N   
1637 C  CA  . ILE A 211 ? 0.3023 0.2087 0.2854 0.0219  -0.0783 0.0280  211 ILE A CA  
1638 C  C   . ILE A 211 ? 0.2726 0.1788 0.3091 -0.0047 -0.0297 0.0359  211 ILE A C   
1639 O  O   . ILE A 211 ? 0.2708 0.2634 0.3074 0.0316  -0.0549 0.0315  211 ILE A O   
1640 C  CB  . ILE A 211 ? 0.2348 0.1739 0.2994 0.0045  -0.0739 0.0241  211 ILE A CB  
1641 C  CG1 . ILE A 211 ? 0.3113 0.2834 0.3258 -0.0299 -0.0310 -0.0444 211 ILE A CG1 
1642 C  CG2 . ILE A 211 ? 0.2873 0.3076 0.2815 0.0955  -0.1263 0.0381  211 ILE A CG2 
1643 C  CD1 . ILE A 211 ? 0.4701 0.2859 0.2717 0.0207  -0.0551 0.0312  211 ILE A CD1 
1644 N  N   . GLN A 212 ? 0.2692 0.1560 0.2963 0.0143  -0.0414 0.0474  212 GLN A N   
1645 C  CA  . GLN A 212 ? 0.3053 0.1377 0.3078 -0.0290 -0.0125 0.0531  212 GLN A CA  
1646 C  C   . GLN A 212 ? 0.2539 0.1476 0.2842 0.0295  -0.0421 0.0708  212 GLN A C   
1647 O  O   . GLN A 212 ? 0.2295 0.1799 0.3421 0.0161  -0.0335 0.0208  212 GLN A O   
1648 C  CB  . GLN A 212 ? 0.2945 0.2124 0.3386 -0.0278 -0.0050 0.0023  212 GLN A CB  
1649 C  CG  . GLN A 212 ? 0.2758 0.3504 0.7050 0.0128  -0.0060 0.0912  212 GLN A CG  
1650 C  CD  . GLN A 212 ? 0.3287 0.6058 0.8863 -0.0949 -0.1574 0.2174  212 GLN A CD  
1651 O  OE1 . GLN A 212 ? 0.4823 0.9893 0.8574 -0.3943 -0.1988 0.3694  212 GLN A OE1 
1652 N  NE2 . GLN A 212 ? 0.6535 0.8887 1.0893 -0.2247 -0.4628 0.3291  212 GLN A NE2 
1653 N  N   . LEU A 213 ? 0.2396 0.1296 0.3035 -0.0143 -0.0644 0.0634  213 LEU A N   
1654 C  CA  . LEU A 213 ? 0.2356 0.1326 0.3001 -0.0344 -0.0777 0.0610  213 LEU A CA  
1655 C  C   . LEU A 213 ? 0.2356 0.1763 0.2754 -0.0039 -0.0660 0.0509  213 LEU A C   
1656 O  O   . LEU A 213 ? 0.2536 0.1918 0.3074 -0.0359 -0.0295 0.0469  213 LEU A O   
1657 C  CB  . LEU A 213 ? 0.2586 0.1551 0.2859 -0.0088 -0.0805 0.0808  213 LEU A CB  
1658 C  CG  . LEU A 213 ? 0.3433 0.1627 0.2910 0.0011  -0.0434 0.0911  213 LEU A CG  
1659 C  CD1 . LEU A 213 ? 0.3101 0.3092 0.2879 -0.0451 -0.0637 0.0648  213 LEU A CD1 
1660 C  CD2 . LEU A 213 ? 0.3993 0.2222 0.3707 0.0824  0.0453  0.1787  213 LEU A CD2 
1661 N  N   . PHE A 214 ? 0.2708 0.2154 0.3133 0.0153  -0.1073 0.0143  214 PHE A N   
1662 C  CA  . PHE A 214 ? 0.2620 0.1886 0.2850 0.0141  -0.0737 -0.0124 214 PHE A CA  
1663 C  C   . PHE A 214 ? 0.2508 0.1895 0.2467 0.0114  -0.0315 0.0040  214 PHE A C   
1664 O  O   . PHE A 214 ? 0.2316 0.2531 0.3015 0.0378  -0.0417 0.0706  214 PHE A O   
1665 C  CB  . PHE A 214 ? 0.3285 0.2209 0.3389 0.0149  -0.1146 -0.0679 214 PHE A CB  
1666 C  CG  . PHE A 214 ? 0.2933 0.2497 0.3943 0.0381  -0.0970 -0.0943 214 PHE A CG  
1667 C  CD1 . PHE A 214 ? 0.4248 0.2190 0.4410 0.0741  -0.0904 -0.0858 214 PHE A CD1 
1668 C  CD2 . PHE A 214 ? 0.3364 0.3011 0.4051 -0.0024 -0.1206 -0.1531 214 PHE A CD2 
1669 C  CE1 . PHE A 214 ? 0.4643 0.2328 0.4467 0.0780  -0.0977 -0.1268 214 PHE A CE1 
1670 C  CE2 . PHE A 214 ? 0.3289 0.3149 0.4317 0.0030  -0.0657 -0.1503 214 PHE A CE2 
1671 C  CZ  . PHE A 214 ? 0.4349 0.2614 0.4518 -0.0334 -0.1060 -0.1632 214 PHE A CZ  
1672 N  N   . GLU A 215 ? 0.2542 0.2036 0.2626 -0.0054 -0.0616 0.0252  215 GLU A N   
1673 C  CA  . GLU A 215 ? 0.3076 0.2079 0.2788 0.0111  -0.0541 0.0516  215 GLU A CA  
1674 C  C   . GLU A 215 ? 0.3479 0.2055 0.2788 0.0882  -0.0572 0.0548  215 GLU A C   
1675 O  O   . GLU A 215 ? 0.2931 0.2011 0.3213 0.0428  -0.0526 0.0522  215 GLU A O   
1676 C  CB  . GLU A 215 ? 0.3389 0.2353 0.3420 0.0230  -0.0336 0.1120  215 GLU A CB  
1677 C  CG  . GLU A 215 ? 0.4197 0.3609 0.3334 -0.0093 -0.0039 0.1278  215 GLU A CG  
1678 C  CD  . GLU A 215 ? 0.4434 0.4186 0.3373 -0.0796 -0.0369 0.1334  215 GLU A CD  
1679 O  OE1 . GLU A 215 ? 0.5210 0.4143 0.4961 -0.1233 -0.0521 -0.0011 215 GLU A OE1 
1680 O  OE2 . GLU A 215 ? 0.4854 0.4310 0.3274 0.0232  0.0268  0.1290  215 GLU A OE2 
1681 N  N   . GLU A 216 ? 0.2951 0.1604 0.2770 0.0351  -0.0451 0.0378  216 GLU A N   
1682 C  CA  . GLU A 216 ? 0.2541 0.1606 0.2791 0.0110  -0.0482 0.0361  216 GLU A CA  
1683 C  C   . GLU A 216 ? 0.2236 0.1556 0.2909 0.0124  -0.0500 -0.0060 216 GLU A C   
1684 O  O   . GLU A 216 ? 0.2373 0.1711 0.2935 0.0334  -0.0517 -0.0069 216 GLU A O   
1685 C  CB  . GLU A 216 ? 0.2353 0.1312 0.3163 -0.0099 -0.0752 -0.0300 216 GLU A CB  
1686 C  CG  . GLU A 216 ? 0.2214 0.1230 0.3113 0.0115  -0.0631 -0.0209 216 GLU A CG  
1687 C  CD  . GLU A 216 ? 0.2536 0.1090 0.3283 -0.0012 -0.0826 0.0016  216 GLU A CD  
1688 O  OE1 . GLU A 216 ? 0.3321 0.1071 0.2836 0.0077  -0.0481 -0.0147 216 GLU A OE1 
1689 O  OE2 . GLU A 216 ? 0.2696 0.1388 0.2743 0.0100  -0.0766 -0.0247 216 GLU A OE2 
1690 N  N   . LEU A 217 ? 0.2221 0.1522 0.3262 0.0204  -0.0223 0.0046  217 LEU A N   
1691 C  CA  . LEU A 217 ? 0.2458 0.1548 0.2737 0.0065  -0.0193 -0.0104 217 LEU A CA  
1692 C  C   . LEU A 217 ? 0.2292 0.1545 0.3093 -0.0227 -0.0069 0.0564  217 LEU A C   
1693 O  O   . LEU A 217 ? 0.2270 0.2128 0.3008 -0.0091 -0.0255 0.0008  217 LEU A O   
1694 C  CB  . LEU A 217 ? 0.2600 0.1580 0.3150 0.0063  0.0291  -0.0229 217 LEU A CB  
1695 C  CG  . LEU A 217 ? 0.2524 0.1382 0.3201 -0.0022 0.0444  0.0017  217 LEU A CG  
1696 C  CD1 . LEU A 217 ? 0.4199 0.1347 0.3391 0.0067  -0.0281 0.0074  217 LEU A CD1 
1697 C  CD2 . LEU A 217 ? 0.4018 0.1599 0.3546 -0.0427 -0.0569 0.0045  217 LEU A CD2 
1698 N  N   . GLN A 218 ? 0.2669 0.1719 0.3060 0.0262  -0.0137 0.0452  218 GLN A N   
1699 C  CA  . GLN A 218 ? 0.2598 0.1780 0.3193 0.0101  -0.0350 0.0155  218 GLN A CA  
1700 C  C   . GLN A 218 ? 0.2284 0.1875 0.3026 0.0242  -0.0486 0.0212  218 GLN A C   
1701 O  O   . GLN A 218 ? 0.2309 0.2329 0.3900 0.0438  -0.0391 0.0217  218 GLN A O   
1702 C  CB  . GLN A 218 ? 0.2911 0.3044 0.3116 0.1032  -0.0469 -0.0037 218 GLN A CB  
1703 C  CG  . GLN A 218 ? 0.3233 0.3368 0.3877 0.1175  -0.0821 0.0222  218 GLN A CG  
1704 C  CD  . GLN A 218 ? 0.3166 0.4315 0.4517 0.1033  -0.0999 -0.0781 218 GLN A CD  
1705 O  OE1 . GLN A 218 ? 0.2906 0.4072 0.4472 0.0343  0.0071  -0.0229 218 GLN A OE1 
1706 N  NE2 . GLN A 218 ? 0.2930 0.5627 0.6044 0.1356  -0.0526 -0.0789 218 GLN A NE2 
1707 N  N   . GLU A 219 ? 0.2362 0.1865 0.3134 0.0284  -0.0566 -0.0033 219 GLU A N   
1708 C  CA  . GLU A 219 ? 0.2939 0.1496 0.3276 0.0288  -0.0308 0.0334  219 GLU A CA  
1709 C  C   . GLU A 219 ? 0.2666 0.1317 0.3174 0.0690  -0.0382 0.0237  219 GLU A C   
1710 O  O   . GLU A 219 ? 0.2842 0.1541 0.3887 0.0709  -0.0202 -0.0198 219 GLU A O   
1711 C  CB  . GLU A 219 ? 0.4194 0.1992 0.4977 -0.0906 0.0466  -0.0351 219 GLU A CB  
1712 C  CG  . GLU A 219 ? 0.7092 0.3063 0.6964 -0.0692 -0.0727 -0.2169 219 GLU A CG  
1713 C  CD  . GLU A 219 ? 0.9239 0.4244 0.7545 -0.0969 -0.1606 -0.2853 219 GLU A CD  
1714 O  OE1 . GLU A 219 ? 1.1828 0.3868 0.7603 -0.5599 -0.2231 0.0414  219 GLU A OE1 
1715 O  OE2 . GLU A 219 ? 1.2352 0.6331 1.1346 0.0760  -0.2517 -0.6089 219 GLU A OE2 
1716 N  N   . LEU A 220 ? 0.2762 0.1576 0.3019 0.0483  -0.1038 0.0072  220 LEU A N   
1717 C  CA  . LEU A 220 ? 0.2650 0.2255 0.2982 0.0201  -0.1233 0.0209  220 LEU A CA  
1718 C  C   . LEU A 220 ? 0.2657 0.1649 0.3571 0.0391  -0.0744 -0.0205 220 LEU A C   
1719 O  O   . LEU A 220 ? 0.3348 0.1713 0.3596 -0.0023 -0.0408 -0.0346 220 LEU A O   
1720 C  CB  . LEU A 220 ? 0.2730 0.2093 0.2563 0.0374  -0.0959 -0.0046 220 LEU A CB  
1721 C  CG  . LEU A 220 ? 0.2591 0.2286 0.2687 0.0695  -0.1000 -0.0457 220 LEU A CG  
1722 C  CD1 . LEU A 220 ? 0.2654 0.2826 0.3217 0.1143  0.0102  0.0348  220 LEU A CD1 
1723 C  CD2 . LEU A 220 ? 0.3546 0.2936 0.3173 0.0569  -0.1105 -0.1072 220 LEU A CD2 
1724 N  N   . LEU A 221 ? 0.2672 0.1584 0.3165 -0.0175 -0.0367 0.0114  221 LEU A N   
1725 C  CA  . LEU A 221 ? 0.2762 0.1866 0.3502 -0.0293 -0.0081 -0.0093 221 LEU A CA  
1726 C  C   . LEU A 221 ? 0.2585 0.2539 0.3652 -0.0311 -0.0233 0.0230  221 LEU A C   
1727 O  O   . LEU A 221 ? 0.2585 0.3313 0.4660 -0.0218 0.0409  0.0251  221 LEU A O   
1728 C  CB  . LEU A 221 ? 0.2804 0.2405 0.2985 -0.0708 0.0126  -0.0301 221 LEU A CB  
1729 C  CG  . LEU A 221 ? 0.4259 0.1645 0.3154 -0.0593 0.0248  -0.0399 221 LEU A CG  
1730 C  CD1 . LEU A 221 ? 0.5276 0.1930 0.3592 -0.0826 0.0038  -0.0941 221 LEU A CD1 
1731 C  CD2 . LEU A 221 ? 0.3759 0.2411 0.3474 -0.1207 -0.0183 -0.0064 221 LEU A CD2 
1732 N  N   . THR A 222 ? 0.2862 0.2228 0.3735 -0.0257 -0.0889 0.0098  222 THR A N   
1733 C  CA  . THR A 222 ? 0.3990 0.3093 0.3743 0.0233  -0.1866 -0.0049 222 THR A CA  
1734 C  C   . THR A 222 ? 0.4114 0.2962 0.3468 0.0692  -0.0831 0.0452  222 THR A C   
1735 O  O   . THR A 222 ? 0.8580 0.3474 0.4023 0.1742  -0.1545 0.0714  222 THR A O   
1736 C  CB  . THR A 222 ? 0.3361 0.3506 0.4100 0.1877  -0.0963 -0.0021 222 THR A CB  
1737 O  OG1 . THR A 222 ? 0.3922 0.5809 0.6212 0.0781  -0.0150 -0.0546 222 THR A OG1 
1738 C  CG2 . THR A 222 ? 0.3667 0.4580 0.5232 0.1877  0.0021  -0.1523 222 THR A CG2 
1739 N  N   . HIS A 223 ? 0.4092 0.2722 0.3637 0.0273  -0.1090 0.0061  223 HIS A N   
1740 C  CA  . HIS A 223 ? 0.4004 0.3071 0.4006 0.0533  -0.0622 -0.0012 223 HIS A CA  
1741 C  C   . HIS A 223 ? 0.4001 0.6237 0.5062 0.1001  -0.0397 -0.0011 223 HIS A C   
1742 O  O   . HIS A 223 ? 0.3398 0.8781 0.6067 0.0799  -0.0704 0.3414  223 HIS A O   
1743 C  CB  . HIS A 223 ? 0.4443 0.2040 0.4137 -0.0114 -0.0817 -0.0152 223 HIS A CB  
1744 C  CG  . HIS A 223 ? 0.4587 0.2127 0.4265 -0.0580 -0.0843 -0.0393 223 HIS A CG  
1745 N  ND1 . HIS A 223 ? 0.5409 0.2229 0.3805 -0.0310 0.0078  -0.0298 223 HIS A ND1 
1746 C  CD2 . HIS A 223 ? 0.4976 0.2157 0.3719 -0.0395 0.0982  -0.0165 223 HIS A CD2 
1747 C  CE1 . HIS A 223 ? 0.5270 0.1865 0.4442 -0.0372 -0.0130 0.0021  223 HIS A CE1 
1748 N  NE2 . HIS A 223 ? 0.5392 0.1259 0.4404 -0.0716 0.0873  -0.0487 223 HIS A NE2 
1749 N  N   . PRO B 10  ? 0.9786 0.8414 0.5991 -0.1300 -0.2577 0.0026  10  PRO B N   
1750 C  CA  . PRO B 10  ? 0.9053 0.8198 0.5145 -0.1170 -0.1958 0.0251  10  PRO B CA  
1751 C  C   . PRO B 10  ? 1.0114 0.7540 0.4535 -0.0950 -0.1477 0.1324  10  PRO B C   
1752 O  O   . PRO B 10  ? 1.2272 0.7665 0.4366 -0.0891 -0.0412 0.1871  10  PRO B O   
1753 C  CB  . PRO B 10  ? 0.9399 0.8452 0.5401 -0.1149 -0.3435 0.0107  10  PRO B CB  
1754 C  CG  . PRO B 10  ? 1.0398 0.7968 0.5132 -0.1394 -0.3063 -0.0222 10  PRO B CG  
1755 C  CD  . PRO B 10  ? 1.0150 0.8128 0.5975 -0.1117 -0.3074 0.0189  10  PRO B CD  
1756 N  N   . GLN B 11  ? 1.0658 0.6898 0.4421 -0.1127 -0.1616 0.2149  11  GLN B N   
1757 C  CA  . GLN B 11  ? 1.0514 0.7461 0.4723 -0.1199 -0.2593 0.2654  11  GLN B CA  
1758 C  C   . GLN B 11  ? 0.9258 0.5306 0.4492 -0.0324 -0.1870 0.1809  11  GLN B C   
1759 O  O   . GLN B 11  ? 0.9226 0.4629 0.4097 0.0332  -0.3031 0.0412  11  GLN B O   
1760 C  CB  . GLN B 11  ? 1.1459 0.9670 0.4305 -0.1739 -0.3549 0.2156  11  GLN B CB  
1761 C  CG  . GLN B 11  ? 1.1382 1.2322 0.5519 -0.1632 -0.3733 0.2377  11  GLN B CG  
1762 C  CD  . GLN B 11  ? 1.0032 1.4159 0.6152 -0.0812 -0.3318 0.3704  11  GLN B CD  
1763 O  OE1 . GLN B 11  ? 0.8782 1.7175 0.9121 -0.4077 -0.3478 0.5215  11  GLN B OE1 
1764 N  NE2 . GLN B 11  ? 0.9752 1.7668 0.7624 0.0885  -0.6260 0.3528  11  GLN B NE2 
1765 N  N   . ASP B 12  ? 0.8543 0.3270 0.3192 -0.0828 -0.1315 0.0362  12  ASP B N   
1766 C  CA  . ASP B 12  ? 0.8708 0.2387 0.3188 0.0214  -0.0776 0.0121  12  ASP B CA  
1767 C  C   . ASP B 12  ? 0.8396 0.1548 0.3185 0.0249  -0.0705 0.0513  12  ASP B C   
1768 O  O   . ASP B 12  ? 0.7188 0.2245 0.3137 0.0929  -0.1197 0.0340  12  ASP B O   
1769 C  CB  . ASP B 12  ? 0.8941 0.2576 0.3160 0.0710  -0.0142 -0.0268 12  ASP B CB  
1770 C  CG  . ASP B 12  ? 1.0172 0.2814 0.4638 0.0507  -0.0357 -0.0817 12  ASP B CG  
1771 O  OD1 . ASP B 12  ? 1.1101 0.3744 0.4968 0.0068  -0.1863 -0.0620 12  ASP B OD1 
1772 O  OD2 . ASP B 12  ? 1.2510 0.3362 0.5806 0.1955  -0.1000 -0.1468 12  ASP B OD2 
1773 N  N   . LEU B 13  ? 0.7270 0.2193 0.2956 0.0406  -0.1446 0.0191  13  LEU B N   
1774 C  CA  . LEU B 13  ? 0.6812 0.1835 0.3257 0.0779  -0.1510 0.0134  13  LEU B CA  
1775 C  C   . LEU B 13  ? 0.6749 0.1945 0.2779 0.0810  -0.1286 0.0198  13  LEU B C   
1776 O  O   . LEU B 13  ? 0.6503 0.2539 0.3106 0.0412  -0.0986 0.0018  13  LEU B O   
1777 C  CB  . LEU B 13  ? 0.6688 0.2050 0.3501 0.0442  -0.1435 -0.0369 13  LEU B CB  
1778 C  CG  . LEU B 13  ? 0.6529 0.1872 0.3276 0.0484  -0.1637 -0.0123 13  LEU B CG  
1779 C  CD1 . LEU B 13  ? 0.5874 0.1890 0.3900 -0.0024 -0.1754 -0.0114 13  LEU B CD1 
1780 C  CD2 . LEU B 13  ? 0.6589 0.1752 0.2871 0.0730  -0.1821 0.0331  13  LEU B CD2 
1781 N  N   . SER B 14  ? 0.7289 0.2166 0.2901 0.1187  -0.1213 0.0412  14  SER B N   
1782 C  CA  . SER B 14  ? 0.7463 0.2602 0.4406 0.1041  -0.1714 0.1051  14  SER B CA  
1783 C  C   . SER B 14  ? 0.7283 0.2632 0.3756 0.1096  -0.1388 -0.0057 14  SER B C   
1784 O  O   . SER B 14  ? 0.7264 0.4823 0.3063 0.0502  -0.1563 0.0415  14  SER B O   
1785 C  CB  . SER B 14  ? 0.7580 0.2630 0.5523 0.1317  -0.2015 0.0892  14  SER B CB  
1786 O  OG  . SER B 14  ? 0.7230 0.2593 0.5854 0.0849  -0.1784 0.0582  14  SER B OG  
1787 N  N   . GLU B 15  ? 0.7980 0.2121 0.3749 0.0560  -0.1741 -0.0136 15  GLU B N   
1788 C  CA  . GLU B 15  ? 0.8147 0.2831 0.3567 0.0672  -0.1242 -0.0422 15  GLU B CA  
1789 C  C   . GLU B 15  ? 0.6658 0.2790 0.4450 0.0295  -0.1408 0.0043  15  GLU B C   
1790 O  O   . GLU B 15  ? 0.6200 0.3446 0.3951 0.0432  -0.0734 0.0039  15  GLU B O   
1791 C  CB  . GLU B 15  ? 0.9927 0.3938 0.3263 0.0976  -0.1613 -0.0342 15  GLU B CB  
1792 C  CG  . GLU B 15  ? 1.0702 0.5254 0.5861 0.2113  -0.1458 -0.2455 15  GLU B CG  
1793 C  CD  . GLU B 15  ? 1.0552 0.6267 0.7799 0.2430  -0.1699 -0.1604 15  GLU B CD  
1794 O  OE1 . GLU B 15  ? 1.0506 1.0120 0.7958 -0.0607 0.0807  0.2160  15  GLU B OE1 
1795 O  OE2 . GLU B 15  ? 1.4000 0.8423 0.9267 0.4706  -0.4035 -0.1997 15  GLU B OE2 
1796 N  N   . ALA B 16  ? 0.6272 0.2516 0.3417 -0.0252 -0.1555 0.0463  16  ALA B N   
1797 C  CA  . ALA B 16  ? 0.6360 0.2570 0.3331 0.0073  -0.1221 0.0216  16  ALA B CA  
1798 C  C   . ALA B 16  ? 0.6099 0.2557 0.3197 -0.0208 -0.0993 0.0328  16  ALA B C   
1799 O  O   . ALA B 16  ? 0.7653 0.2232 0.3830 -0.0431 -0.1059 0.0178  16  ALA B O   
1800 C  CB  . ALA B 16  ? 0.6116 0.2451 0.3049 -0.0190 -0.0853 -0.0579 16  ALA B CB  
1801 N  N   . LEU B 17  ? 0.5515 0.2764 0.3125 0.0334  -0.0482 0.0230  17  LEU B N   
1802 C  CA  . LEU B 17  ? 0.5200 0.3521 0.3106 0.0386  -0.0562 0.0177  17  LEU B CA  
1803 C  C   . LEU B 17  ? 0.5221 0.3479 0.3290 0.0238  -0.0237 -0.0111 17  LEU B C   
1804 O  O   . LEU B 17  ? 0.5500 0.3896 0.4102 -0.0398 0.0752  -0.0568 17  LEU B O   
1805 C  CB  . LEU B 17  ? 0.5074 0.3318 0.3032 0.0403  -0.0326 -0.0116 17  LEU B CB  
1806 C  CG  . LEU B 17  ? 0.4979 0.2617 0.3350 0.0247  -0.0452 -0.0636 17  LEU B CG  
1807 C  CD1 . LEU B 17  ? 0.4671 0.4428 0.3105 0.0215  -0.0976 0.0732  17  LEU B CD1 
1808 C  CD2 . LEU B 17  ? 0.5989 0.4099 0.5221 0.0084  -0.0331 -0.2555 17  LEU B CD2 
1809 N  N   . LYS B 18  ? 0.5533 0.3316 0.4106 0.0403  0.0206  0.0233  18  LYS B N   
1810 C  CA  . LYS B 18  ? 0.5506 0.3641 0.4161 0.0299  0.0248  -0.0363 18  LYS B CA  
1811 C  C   . LYS B 18  ? 0.5444 0.3434 0.3636 -0.0006 0.0099  -0.0876 18  LYS B C   
1812 O  O   . LYS B 18  ? 0.5824 0.4130 0.4381 -0.0448 -0.0111 -0.0950 18  LYS B O   
1813 C  CB  . LYS B 18  ? 0.4973 0.3625 0.5210 -0.0572 0.1580  -0.0761 18  LYS B CB  
1814 C  CG  . LYS B 18  ? 0.5142 0.3921 0.7082 -0.0260 0.1671  -0.1079 18  LYS B CG  
1815 C  CD  . LYS B 18  ? 0.6049 0.3896 0.8818 -0.0029 -0.0149 -0.1477 18  LYS B CD  
1816 C  CE  . LYS B 18  ? 0.6408 0.4664 0.9590 0.0056  -0.1055 -0.1573 18  LYS B CE  
1817 N  NZ  . LYS B 18  ? 0.9674 0.6720 1.0205 -0.2186 -0.2438 -0.1663 18  LYS B NZ  
1818 N  N   . GLU B 19  ? 0.6578 0.4198 0.3563 -0.0445 -0.0150 -0.0625 19  GLU B N   
1819 C  CA  . GLU B 19  ? 0.7615 0.5220 0.3989 -0.0546 0.0628  -0.0142 19  GLU B CA  
1820 C  C   . GLU B 19  ? 0.6399 0.4708 0.3865 -0.1129 0.0686  0.0360  19  GLU B C   
1821 O  O   . GLU B 19  ? 0.5778 0.6371 0.3743 -0.1871 -0.0146 -0.0707 19  GLU B O   
1822 C  CB  . GLU B 19  ? 0.9083 0.5935 0.3760 -0.1120 0.0662  -0.0093 19  GLU B CB  
1823 C  CG  . GLU B 19  ? 1.1636 0.6825 0.4536 -0.1967 0.0736  0.0864  19  GLU B CG  
1824 C  CD  . GLU B 19  ? 1.3155 0.7831 0.5662 -0.1734 -0.0081 0.1821  19  GLU B CD  
1825 O  OE1 . GLU B 19  ? 1.4418 1.2125 0.5678 -0.1824 -0.1816 0.0913  19  GLU B OE1 
1826 O  OE2 . GLU B 19  ? 1.5924 0.7059 0.7611 0.0524  -0.1273 0.0642  19  GLU B OE2 
1827 N  N   . ALA B 20  ? 0.5961 0.4180 0.2994 -0.1185 0.0011  0.0607  20  ALA B N   
1828 C  CA  . ALA B 20  ? 0.5208 0.3926 0.3986 -0.0890 -0.0560 0.0902  20  ALA B CA  
1829 C  C   . ALA B 20  ? 0.5994 0.3447 0.4244 -0.0573 -0.0873 0.0414  20  ALA B C   
1830 O  O   . ALA B 20  ? 0.4808 0.3446 0.5269 -0.0512 -0.0404 0.0262  20  ALA B O   
1831 C  CB  . ALA B 20  ? 0.5316 0.4051 0.4272 -0.1340 0.0098  0.1050  20  ALA B CB  
1832 N  N   . THR B 21  ? 0.5252 0.3480 0.3725 -0.0322 -0.0557 0.0088  21  THR B N   
1833 C  CA  . THR B 21  ? 0.4983 0.3188 0.3245 -0.0367 0.0053  -0.0135 21  THR B CA  
1834 C  C   . THR B 21  ? 0.4932 0.3053 0.3574 -0.0569 -0.0056 -0.0773 21  THR B C   
1835 O  O   . THR B 21  ? 0.5097 0.4952 0.2900 -0.0224 -0.0086 0.0011  21  THR B O   
1836 C  CB  . THR B 21  ? 0.5259 0.3168 0.3707 -0.0978 -0.0236 0.0214  21  THR B CB  
1837 O  OG1 . THR B 21  ? 0.4682 0.3371 0.3560 -0.1139 -0.0512 -0.0186 21  THR B OG1 
1838 C  CG2 . THR B 21  ? 0.5363 0.3194 0.3274 -0.1033 0.0060  0.0177  21  THR B CG2 
1839 N  N   . LYS B 22  ? 0.4814 0.4065 0.3311 -0.0540 -0.0014 -0.0467 22  LYS B N   
1840 C  CA  . LYS B 22  ? 0.4830 0.5119 0.3998 -0.0535 0.0419  -0.0002 22  LYS B CA  
1841 C  C   . LYS B 22  ? 0.4275 0.4538 0.4260 -0.0228 0.0796  0.0439  22  LYS B C   
1842 O  O   . LYS B 22  ? 0.4609 0.4520 0.4897 -0.0593 0.0282  0.0571  22  LYS B O   
1843 C  CB  . LYS B 22  ? 0.5770 0.5303 0.4270 -0.0748 0.1340  -0.0008 22  LYS B CB  
1844 C  CG  . LYS B 22  ? 0.8165 0.6330 0.5422 0.0879  0.1313  -0.0596 22  LYS B CG  
1845 C  CD  . LYS B 22  ? 0.9871 0.8266 0.6098 0.1084  0.2059  -0.1679 22  LYS B CD  
1846 C  CE  . LYS B 22  ? 1.0001 0.9194 0.6797 0.1552  0.2632  -0.1951 22  LYS B CE  
1847 N  NZ  . LYS B 22  ? 1.1017 1.1496 0.6191 0.1622  0.2374  -0.2756 22  LYS B NZ  
1848 N  N   . GLU B 23  ? 0.5479 0.4867 0.3788 0.0310  0.0861  0.0505  23  GLU B N   
1849 C  CA  . GLU B 23  ? 0.6875 0.4521 0.4009 0.0000  0.0124  0.1391  23  GLU B CA  
1850 C  C   . GLU B 23  ? 0.6517 0.3856 0.4103 -0.0551 0.0368  0.1190  23  GLU B C   
1851 O  O   . GLU B 23  ? 0.5998 0.3613 0.3868 -0.0300 0.0863  0.0957  23  GLU B O   
1852 C  CB  . GLU B 23  ? 0.7220 0.5128 0.4270 0.1112  0.0416  0.1312  23  GLU B CB  
1853 C  CG  . GLU B 23  ? 0.7360 0.6287 0.5738 0.1495  0.0694  0.1137  23  GLU B CG  
1854 C  CD  . GLU B 23  ? 0.7587 0.6825 0.6129 0.1282  0.1156  0.0515  23  GLU B CD  
1855 O  OE1 . GLU B 23  ? 0.9894 0.7020 0.5644 0.1501  0.0982  0.4065  23  GLU B OE1 
1856 O  OE2 . GLU B 23  ? 0.8388 0.9516 0.8854 0.2450  0.1965  -0.0654 23  GLU B OE2 
1857 N  N   . VAL B 24  ? 0.6119 0.3644 0.3843 -0.1133 -0.0077 0.1602  24  VAL B N   
1858 C  CA  . VAL B 24  ? 0.5232 0.3145 0.4040 -0.0958 0.0010  0.1166  24  VAL B CA  
1859 C  C   . VAL B 24  ? 0.5784 0.2272 0.3352 -0.1175 -0.0428 0.0393  24  VAL B C   
1860 O  O   . VAL B 24  ? 0.5895 0.3172 0.3651 -0.0921 -0.0708 0.0036  24  VAL B O   
1861 C  CB  . VAL B 24  ? 0.4993 0.3816 0.4578 -0.1333 0.0037  0.1396  24  VAL B CB  
1862 C  CG1 . VAL B 24  ? 0.4528 0.4849 0.4840 -0.0477 -0.1378 0.1135  24  VAL B CG1 
1863 C  CG2 . VAL B 24  ? 0.5241 0.5112 0.3974 -0.1567 -0.1422 0.1534  24  VAL B CG2 
1864 N  N   . HIS B 25  ? 0.6270 0.2494 0.3926 -0.1372 0.0140  0.0025  25  HIS B N   
1865 C  CA  . HIS B 25  ? 0.6302 0.2228 0.4758 -0.0883 0.0524  -0.0121 25  HIS B CA  
1866 C  C   . HIS B 25  ? 0.6260 0.3208 0.4192 -0.0816 0.0442  -0.0119 25  HIS B C   
1867 O  O   . HIS B 25  ? 0.6581 0.2507 0.4214 -0.0840 0.0302  -0.0061 25  HIS B O   
1868 C  CB  . HIS B 25  ? 0.6685 0.2692 0.5630 -0.0453 0.0164  -0.0966 25  HIS B CB  
1869 C  CG  . HIS B 25  ? 0.7291 0.2397 0.6258 0.0160  0.0531  -0.1181 25  HIS B CG  
1870 N  ND1 . HIS B 25  ? 0.7417 0.3233 0.6511 0.0492  0.0518  -0.1139 25  HIS B ND1 
1871 C  CD2 . HIS B 25  ? 0.7594 0.2691 0.6134 0.0194  0.0324  -0.0781 25  HIS B CD2 
1872 C  CE1 . HIS B 25  ? 0.8009 0.2964 0.6159 0.0954  0.0493  -0.1558 25  HIS B CE1 
1873 N  NE2 . HIS B 25  ? 0.8110 0.2519 0.5992 0.0503  0.0167  -0.1299 25  HIS B NE2 
1874 N  N   . THR B 26  ? 0.6271 0.3567 0.4146 -0.1373 0.0168  -0.0033 26  THR B N   
1875 C  CA  . THR B 26  ? 0.6448 0.4281 0.4579 -0.1770 0.0146  -0.0040 26  THR B CA  
1876 C  C   . THR B 26  ? 0.5640 0.3843 0.4080 -0.1148 -0.0202 0.0365  26  THR B C   
1877 O  O   . THR B 26  ? 0.6286 0.4981 0.4445 -0.0408 -0.0914 -0.0059 26  THR B O   
1878 C  CB  . THR B 26  ? 0.6766 0.5467 0.4432 -0.2852 0.0300  -0.0477 26  THR B CB  
1879 O  OG1 . THR B 26  ? 0.7652 0.6191 0.5149 -0.1647 0.0064  -0.1245 26  THR B OG1 
1880 C  CG2 . THR B 26  ? 0.6398 0.7027 0.7086 -0.2375 0.3128  -0.2494 26  THR B CG2 
1881 N  N   . GLN B 27  ? 0.6142 0.4267 0.4279 -0.0593 -0.0338 0.0617  27  GLN B N   
1882 C  CA  . GLN B 27  ? 0.5449 0.3805 0.4383 -0.0646 0.0086  0.0752  27  GLN B CA  
1883 C  C   . GLN B 27  ? 0.5351 0.3854 0.4305 -0.0935 -0.0210 0.0612  27  GLN B C   
1884 O  O   . GLN B 27  ? 0.6463 0.2383 0.4720 -0.0401 -0.0559 -0.0010 27  GLN B O   
1885 C  CB  . GLN B 27  ? 0.4987 0.4010 0.5009 -0.0711 0.0452  0.1185  27  GLN B CB  
1886 C  CG  . GLN B 27  ? 0.5134 0.4376 0.5890 -0.0904 0.0615  0.2145  27  GLN B CG  
1887 C  CD  . GLN B 27  ? 0.5710 0.5396 0.7505 -0.0214 0.0888  0.3205  27  GLN B CD  
1888 O  OE1 . GLN B 27  ? 0.6819 0.5445 0.9174 0.0684  0.2542  0.3953  27  GLN B OE1 
1889 N  NE2 . GLN B 27  ? 0.6147 0.8296 0.8653 0.0146  0.1081  0.5388  27  GLN B NE2 
1890 N  N   . ALA B 28  ? 0.4888 0.3783 0.4197 -0.0641 -0.0133 0.0709  28  ALA B N   
1891 C  CA  . ALA B 28  ? 0.6145 0.3262 0.4090 -0.0595 -0.0219 0.0514  28  ALA B CA  
1892 C  C   . ALA B 28  ? 0.6605 0.2994 0.3531 -0.0270 -0.0533 -0.0002 28  ALA B C   
1893 O  O   . ALA B 28  ? 0.8523 0.3275 0.3269 0.0654  -0.1033 0.0575  28  ALA B O   
1894 C  CB  . ALA B 28  ? 0.6674 0.3017 0.4036 -0.0788 -0.0144 0.0759  28  ALA B CB  
1895 N  N   . GLU B 29  ? 0.6694 0.3559 0.4042 -0.0511 -0.0303 -0.0547 29  GLU B N   
1896 C  CA  . GLU B 29  ? 0.6317 0.4865 0.4308 -0.0409 0.0655  0.0008  29  GLU B CA  
1897 C  C   . GLU B 29  ? 0.6472 0.4695 0.4985 -0.0188 -0.0218 0.0084  29  GLU B C   
1898 O  O   . GLU B 29  ? 0.6579 0.3387 0.6029 0.0409  -0.0322 -0.0213 29  GLU B O   
1899 C  CB  . GLU B 29  ? 0.6327 0.5557 0.4461 -0.0191 0.0394  -0.0391 29  GLU B CB  
1900 C  CG  . GLU B 29  ? 0.6529 0.5265 0.5367 0.0155  -0.0172 -0.0648 29  GLU B CG  
1901 C  CD  . GLU B 29  ? 0.6563 0.5097 0.6365 0.1627  -0.0430 -0.1094 29  GLU B CD  
1902 O  OE1 . GLU B 29  ? 0.6913 0.5468 1.0869 0.1985  -0.1121 -0.1579 29  GLU B OE1 
1903 O  OE2 . GLU B 29  ? 0.8298 0.5221 0.5197 0.0830  0.1187  0.0066  29  GLU B OE2 
1904 N  N   . ASN B 30  ? 0.4945 0.4934 0.4381 -0.0211 -0.0377 0.0242  30  ASN B N   
1905 C  CA  . ASN B 30  ? 0.4659 0.5401 0.4470 -0.0359 0.0149  0.0421  30  ASN B CA  
1906 C  C   . ASN B 30  ? 0.4131 0.4584 0.4739 -0.0795 0.0273  0.0601  30  ASN B C   
1907 O  O   . ASN B 30  ? 0.4262 0.6161 0.6469 -0.1513 0.0737  -0.0496 30  ASN B O   
1908 C  CB  . ASN B 30  ? 0.5423 0.6849 0.4504 -0.0787 0.0066  0.0755  30  ASN B CB  
1909 C  CG  . ASN B 30  ? 0.6348 0.8628 0.4414 0.0116  0.0228  0.0279  30  ASN B CG  
1910 O  OD1 . ASN B 30  ? 0.8449 1.2581 0.3795 -0.0831 0.1119  0.0972  30  ASN B OD1 
1911 N  ND2 . ASN B 30  ? 0.8026 0.7816 0.8129 0.0357  0.0386  -0.0420 30  ASN B ND2 
1912 N  N   . ALA B 31  ? 0.4316 0.4702 0.4483 -0.1216 0.0307  0.0357  31  ALA B N   
1913 C  CA  . ALA B 31  ? 0.3761 0.4009 0.5290 -0.0495 0.0061  -0.0132 31  ALA B CA  
1914 C  C   . ALA B 31  ? 0.4240 0.3341 0.5057 -0.0378 -0.0149 -0.0326 31  ALA B C   
1915 O  O   . ALA B 31  ? 0.6117 0.3393 0.5291 0.0122  -0.1151 -0.0972 31  ALA B O   
1916 C  CB  . ALA B 31  ? 0.4142 0.2579 0.5231 -0.0362 0.0390  -0.0099 31  ALA B CB  
1917 N  N   . GLU B 32  ? 0.4429 0.2959 0.5046 -0.0582 -0.0204 0.0173  32  GLU B N   
1918 C  CA  . GLU B 32  ? 0.4137 0.2910 0.5198 -0.0691 -0.0071 -0.0001 32  GLU B CA  
1919 C  C   . GLU B 32  ? 0.4035 0.3371 0.4642 -0.0175 0.0166  -0.0014 32  GLU B C   
1920 O  O   . GLU B 32  ? 0.4526 0.3192 0.4759 0.0169  0.0784  -0.0049 32  GLU B O   
1921 C  CB  . GLU B 32  ? 0.5728 0.3538 0.6136 -0.1223 -0.0599 -0.0495 32  GLU B CB  
1922 C  CG  . GLU B 32  ? 0.6693 0.5667 0.7517 -0.2494 -0.2046 0.0212  32  GLU B CG  
1923 C  CD  . GLU B 32  ? 0.8476 0.6550 0.8780 -0.3311 -0.2363 -0.0560 32  GLU B CD  
1924 O  OE1 . GLU B 32  ? 1.2247 0.5224 0.7709 -0.3419 0.0564  0.1522  32  GLU B OE1 
1925 O  OE2 . GLU B 32  ? 0.9005 1.1716 1.0930 -0.5022 -0.3485 -0.1485 32  GLU B OE2 
1926 N  N   . PHE B 33  ? 0.3925 0.2848 0.4963 -0.0269 0.0169  -0.0253 33  PHE B N   
1927 C  CA  . PHE B 33  ? 0.3462 0.2862 0.5069 -0.0546 0.0112  -0.0239 33  PHE B CA  
1928 C  C   . PHE B 33  ? 0.3351 0.2838 0.4988 0.0136  -0.0319 -0.0188 33  PHE B C   
1929 O  O   . PHE B 33  ? 0.3596 0.3502 0.6110 0.0513  -0.0899 -0.0025 33  PHE B O   
1930 C  CB  . PHE B 33  ? 0.3856 0.3442 0.4672 -0.0612 0.0279  -0.1033 33  PHE B CB  
1931 C  CG  . PHE B 33  ? 0.4533 0.3876 0.4407 -0.0776 0.0714  -0.1121 33  PHE B CG  
1932 C  CD1 . PHE B 33  ? 0.5487 0.4264 0.4472 -0.1480 0.0551  -0.0697 33  PHE B CD1 
1933 C  CD2 . PHE B 33  ? 0.4976 0.3530 0.4365 -0.0236 0.0720  -0.1341 33  PHE B CD2 
1934 C  CE1 . PHE B 33  ? 0.5899 0.4673 0.4980 -0.1531 -0.0131 -0.0098 33  PHE B CE1 
1935 C  CE2 . PHE B 33  ? 0.5412 0.4573 0.4504 -0.0761 0.0554  -0.0886 33  PHE B CE2 
1936 C  CZ  . PHE B 33  ? 0.5542 0.5210 0.4403 -0.1454 0.0816  -0.0530 33  PHE B CZ  
1937 N  N   . MET B 34  ? 0.5828 0.2481 0.5489 0.0239  -0.1538 -0.0071 34  MET B N   
1938 C  CA  . MET B 34  ? 0.6162 0.2624 0.5727 0.0664  -0.1827 -0.0384 34  MET B CA  
1939 C  C   . MET B 34  ? 0.6589 0.2969 0.5723 0.0490  -0.1359 -0.0371 34  MET B C   
1940 O  O   . MET B 34  ? 0.6184 0.3011 0.5172 0.0430  -0.0583 -0.0020 34  MET B O   
1941 C  CB  . MET B 34  ? 0.6405 0.3418 0.5699 -0.0596 -0.1962 0.0339  34  MET B CB  
1942 C  CG  . MET B 34  ? 0.6346 0.5168 0.6980 -0.1145 -0.1202 0.0485  34  MET B CG  
1943 S  SD  . MET B 34  ? 0.8440 0.6976 0.6503 -0.1785 0.1863  0.1997  34  MET B SD  
1944 C  CE  . MET B 34  ? 1.7971 0.4337 0.9569 -0.2848 0.7200  0.1221  34  MET B CE  
1945 N  N   . ARG B 35  ? 0.7135 0.2355 0.5377 0.0398  -0.1266 -0.0887 35  ARG B N   
1946 C  CA  . ARG B 35  ? 0.8246 0.3053 0.4902 0.0881  -0.0350 -0.0425 35  ARG B CA  
1947 C  C   . ARG B 35  ? 0.7552 0.3552 0.4611 0.2116  0.0818  0.0019  35  ARG B C   
1948 O  O   . ARG B 35  ? 0.8189 0.4859 0.5374 0.2853  0.2312  0.0526  35  ARG B O   
1949 C  CB  . ARG B 35  ? 0.9465 0.4272 0.4868 0.0869  -0.0310 0.0634  35  ARG B CB  
1950 C  CG  . ARG B 35  ? 0.9583 0.5948 0.5704 0.0369  0.0258  0.0582  35  ARG B CG  
1951 C  CD  . ARG B 35  ? 0.9990 0.5986 0.6530 0.0366  0.0324  0.1176  35  ARG B CD  
1952 N  NE  . ARG B 35  ? 1.1223 0.6411 0.8350 0.0466  -0.0738 0.1712  35  ARG B NE  
1953 C  CZ  . ARG B 35  ? 1.1655 0.6074 0.8272 -0.0407 -0.2036 0.2170  35  ARG B CZ  
1954 N  NH1 . ARG B 35  ? 1.2182 0.7270 0.7629 -0.0635 -0.1383 0.1734  35  ARG B NH1 
1955 N  NH2 . ARG B 35  ? 1.1796 0.6253 0.9066 -0.1582 -0.2299 0.3486  35  ARG B NH2 
1956 N  N   . ASN B 36  ? 0.6253 0.3716 0.3940 0.1907  0.0893  0.0626  36  ASN B N   
1957 C  CA  . ASN B 36  ? 0.5011 0.3478 0.4790 0.1010  0.0971  0.1216  36  ASN B CA  
1958 C  C   . ASN B 36  ? 0.4866 0.3612 0.4687 0.0910  0.1103  0.1304  36  ASN B C   
1959 O  O   . ASN B 36  ? 0.4823 0.3163 0.6939 0.0695  0.0925  0.1297  36  ASN B O   
1960 C  CB  . ASN B 36  ? 0.4895 0.3942 0.5574 0.0773  -0.0101 0.0615  36  ASN B CB  
1961 C  CG  . ASN B 36  ? 0.5352 0.4444 0.5933 0.0107  -0.0348 0.0771  36  ASN B CG  
1962 O  OD1 . ASN B 36  ? 0.5155 0.5193 0.7047 -0.1164 -0.0677 -0.0417 36  ASN B OD1 
1963 N  ND2 . ASN B 36  ? 0.5432 0.5498 0.7002 0.0319  0.0372  0.1439  36  ASN B ND2 
1964 N  N   . PHE B 37  ? 0.4978 0.4057 0.4204 0.0819  0.1374  0.0911  37  PHE B N   
1965 C  CA  . PHE B 37  ? 0.5534 0.4083 0.4061 0.0075  0.1159  0.0454  37  PHE B CA  
1966 C  C   . PHE B 37  ? 0.7242 0.4274 0.4098 0.0804  0.0883  0.0383  37  PHE B C   
1967 O  O   . PHE B 37  ? 0.7262 0.4901 0.3603 0.1305  0.0392  0.0079  37  PHE B O   
1968 C  CB  . PHE B 37  ? 0.5319 0.4378 0.4848 -0.0245 0.0527  0.0509  37  PHE B CB  
1969 C  CG  . PHE B 37  ? 0.5884 0.5532 0.5548 -0.1249 0.0296  0.1021  37  PHE B CG  
1970 C  CD1 . PHE B 37  ? 0.5120 0.5561 0.5138 -0.2056 0.0306  0.1927  37  PHE B CD1 
1971 C  CD2 . PHE B 37  ? 0.6135 0.5838 0.5557 -0.0866 0.1060  0.1100  37  PHE B CD2 
1972 C  CE1 . PHE B 37  ? 0.4562 0.6175 0.5524 -0.2471 0.0736  0.1833  37  PHE B CE1 
1973 C  CE2 . PHE B 37  ? 0.6184 0.6549 0.5694 -0.0824 0.1292  0.1758  37  PHE B CE2 
1974 C  CZ  . PHE B 37  ? 0.4951 0.6514 0.5982 -0.1186 0.1777  0.2008  37  PHE B CZ  
1975 N  N   . GLN B 38  ? 0.8301 0.4000 0.4091 0.1588  0.1042  0.0514  38  GLN B N   
1976 C  CA  . GLN B 38  ? 0.9535 0.4569 0.4322 0.2036  0.1206  0.0227  38  GLN B CA  
1977 C  C   . GLN B 38  ? 0.9588 0.5128 0.5030 0.2379  0.2128  0.0756  38  GLN B C   
1978 O  O   . GLN B 38  ? 1.1209 0.6245 0.5854 0.3992  0.0974  0.0260  38  GLN B O   
1979 C  CB  . GLN B 38  ? 1.1266 0.5870 0.4161 0.2540  0.1029  0.0148  38  GLN B CB  
1980 C  CG  . GLN B 38  ? 1.3086 0.7000 0.5111 0.1937  -0.0382 -0.0638 38  GLN B CG  
1981 C  CD  . GLN B 38  ? 1.3599 0.8122 0.4795 0.1823  -0.1254 -0.0726 38  GLN B CD  
1982 O  OE1 . GLN B 38  ? 1.6819 0.9244 0.8153 0.3922  -0.1103 0.0998  38  GLN B OE1 
1983 N  NE2 . GLN B 38  ? 1.0140 1.0216 0.7766 -0.2284 0.0681  0.1975  38  GLN B NE2 
1984 N  N   . LYS B 39  ? 0.9077 0.5470 0.6511 0.1628  0.2077  0.1676  39  LYS B N   
1985 C  CA  . LYS B 39  ? 0.8843 0.5503 0.7751 0.1970  0.3507  0.2071  39  LYS B CA  
1986 C  C   . LYS B 39  ? 0.7580 0.6129 0.7598 0.2460  0.3127  0.1481  39  LYS B C   
1987 O  O   . LYS B 39  ? 0.7432 0.9088 0.8001 0.4580  0.4353  0.0635  39  LYS B O   
1988 C  CB  . LYS B 39  ? 0.9629 0.5839 0.9494 0.1008  0.4073  0.2061  39  LYS B CB  
1989 C  CG  . LYS B 39  ? 1.0193 0.6152 1.0129 0.1188  0.5429  0.1434  39  LYS B CG  
1990 C  CD  . LYS B 39  ? 1.2098 0.6147 1.0581 0.0319  0.4686  0.2289  39  LYS B CD  
1991 C  CE  . LYS B 39  ? 1.3865 0.6261 1.0734 0.0761  0.3461  0.1464  39  LYS B CE  
1992 N  NZ  . LYS B 39  ? 1.7004 0.5046 1.0959 0.0168  0.3260  -0.0075 39  LYS B NZ  
1993 N  N   . GLY B 40  ? 0.7410 0.4792 0.6326 0.1532  0.1867  0.1115  40  GLY B N   
1994 C  CA  . GLY B 40  ? 0.7261 0.4707 0.7042 0.1106  0.0864  0.1351  40  GLY B CA  
1995 C  C   . GLY B 40  ? 0.6160 0.4932 0.6823 0.0940  0.0689  0.1412  40  GLY B C   
1996 O  O   . GLY B 40  ? 0.4444 0.5233 0.6451 -0.0501 0.1636  0.2220  40  GLY B O   
1997 N  N   . GLN B 41  ? 0.5343 0.4779 0.6461 0.0745  0.1286  0.1294  41  GLN B N   
1998 C  CA  . GLN B 41  ? 0.4431 0.4834 0.5785 0.0428  0.1281  0.1588  41  GLN B CA  
1999 C  C   . GLN B 41  ? 0.4312 0.4668 0.6112 0.1082  0.1044  0.1934  41  GLN B C   
2000 O  O   . GLN B 41  ? 0.3916 0.5126 0.8608 0.0480  -0.0088 0.2730  41  GLN B O   
2001 C  CB  . GLN B 41  ? 0.5320 0.5171 0.6207 -0.0055 0.1128  0.1882  41  GLN B CB  
2002 C  CG  . GLN B 41  ? 0.5239 0.5725 0.7297 -0.0576 0.1755  0.2149  41  GLN B CG  
2003 C  CD  . GLN B 41  ? 0.6057 0.8258 0.8572 -0.2320 0.0751  0.2095  41  GLN B CD  
2004 O  OE1 . GLN B 41  ? 0.8371 0.7595 0.9084 -0.4112 -0.2389 0.3864  41  GLN B OE1 
2005 N  NE2 . GLN B 41  ? 0.6477 1.2355 1.1062 -0.2329 -0.3803 0.0620  41  GLN B NE2 
2006 N  N   . VAL B 42  ? 0.3866 0.4583 0.5042 0.0574  0.0788  0.1062  42  VAL B N   
2007 C  CA  . VAL B 42  ? 0.3562 0.3997 0.4706 0.0388  0.0353  0.0185  42  VAL B CA  
2008 C  C   . VAL B 42  ? 0.3502 0.4335 0.4709 0.0553  0.0367  0.0073  42  VAL B C   
2009 O  O   . VAL B 42  ? 0.3223 0.4284 0.4465 0.0448  0.0425  -0.0017 42  VAL B O   
2010 C  CB  . VAL B 42  ? 0.3533 0.3697 0.4972 0.0867  0.0592  -0.0803 42  VAL B CB  
2011 C  CG1 . VAL B 42  ? 0.4629 0.3854 0.5614 0.0947  -0.0947 -0.0261 42  VAL B CG1 
2012 C  CG2 . VAL B 42  ? 0.3645 0.4983 0.5477 0.0401  0.1112  0.0637  42  VAL B CG2 
2013 N  N   . THR B 43  ? 0.2814 0.3462 0.4738 -0.0087 0.0388  0.0164  43  THR B N   
2014 C  CA  . THR B 43  ? 0.3359 0.3568 0.4709 -0.0449 0.0249  -0.0043 43  THR B CA  
2015 C  C   . THR B 43  ? 0.2950 0.2768 0.4176 -0.0192 -0.0226 0.0017  43  THR B C   
2016 O  O   . THR B 43  ? 0.3254 0.2691 0.4349 -0.0333 -0.0580 0.0788  43  THR B O   
2017 C  CB  . THR B 43  ? 0.3656 0.2719 0.4400 -0.0448 0.0239  0.0820  43  THR B CB  
2018 O  OG1 . THR B 43  ? 0.3718 0.3093 0.5564 -0.0498 -0.0534 0.0907  43  THR B OG1 
2019 C  CG2 . THR B 43  ? 0.3897 0.3743 0.6284 -0.0859 0.0604  0.1251  43  THR B CG2 
2020 N  N   . ARG B 44  ? 0.2657 0.2747 0.4103 -0.0277 -0.0490 -0.0208 44  ARG B N   
2021 C  CA  . ARG B 44  ? 0.2734 0.2362 0.3538 -0.0257 -0.0497 -0.0558 44  ARG B CA  
2022 C  C   . ARG B 44  ? 0.2758 0.2087 0.3572 -0.0410 -0.0586 -0.0753 44  ARG B C   
2023 O  O   . ARG B 44  ? 0.2727 0.2067 0.3862 -0.0330 -0.0914 -0.0324 44  ARG B O   
2024 C  CB  . ARG B 44  ? 0.2744 0.2518 0.3731 -0.0533 -0.0858 -0.0447 44  ARG B CB  
2025 C  CG  . ARG B 44  ? 0.2966 0.2550 0.4120 -0.0436 -0.0794 -0.0134 44  ARG B CG  
2026 C  CD  . ARG B 44  ? 0.3033 0.3134 0.3911 0.0168  -0.0160 -0.0036 44  ARG B CD  
2027 N  NE  . ARG B 44  ? 0.3852 0.2727 0.3801 0.0000  -0.0153 0.0075  44  ARG B NE  
2028 C  CZ  . ARG B 44  ? 0.4106 0.2646 0.3782 -0.0492 -0.0265 0.0112  44  ARG B CZ  
2029 N  NH1 . ARG B 44  ? 0.4087 0.3489 0.3774 0.0088  -0.0286 0.0255  44  ARG B NH1 
2030 N  NH2 . ARG B 44  ? 0.4012 0.2894 0.3573 -0.0082 -0.0725 0.0232  44  ARG B NH2 
2031 N  N   . ASP B 45  ? 0.3483 0.1932 0.3736 -0.0655 -0.0869 -0.0167 45  ASP B N   
2032 C  CA  . ASP B 45  ? 0.4132 0.1856 0.3865 -0.0379 -0.0923 -0.0376 45  ASP B CA  
2033 C  C   . ASP B 45  ? 0.3612 0.1801 0.3535 -0.0359 -0.0512 -0.0232 45  ASP B C   
2034 O  O   . ASP B 45  ? 0.3561 0.2289 0.4398 -0.0319 -0.0501 -0.0188 45  ASP B O   
2035 C  CB  . ASP B 45  ? 0.4721 0.1952 0.4213 -0.0637 -0.1231 -0.0332 45  ASP B CB  
2036 C  CG  . ASP B 45  ? 0.6544 0.3786 0.5063 -0.1456 -0.2370 -0.0492 45  ASP B CG  
2037 O  OD1 . ASP B 45  ? 0.9789 0.6746 0.4949 -0.0741 -0.2625 0.0954  45  ASP B OD1 
2038 O  OD2 . ASP B 45  ? 0.6477 0.7320 0.8430 -0.3086 -0.2282 -0.2125 45  ASP B OD2 
2039 N  N   . GLY B 46  ? 0.4059 0.1501 0.3722 -0.0834 -0.0193 0.0004  46  GLY B N   
2040 C  CA  . GLY B 46  ? 0.2984 0.1782 0.3665 -0.0715 0.0087  0.0144  46  GLY B CA  
2041 C  C   . GLY B 46  ? 0.2497 0.1625 0.3914 -0.0472 -0.0291 0.0479  46  GLY B C   
2042 O  O   . GLY B 46  ? 0.2411 0.1753 0.4228 0.0021  -0.0249 0.0035  46  GLY B O   
2043 N  N   . PHE B 47  ? 0.2721 0.1707 0.3171 -0.0487 -0.0773 0.0288  47  PHE B N   
2044 C  CA  . PHE B 47  ? 0.2551 0.1505 0.3080 -0.0245 -0.0466 0.0066  47  PHE B CA  
2045 C  C   . PHE B 47  ? 0.2578 0.1056 0.3156 -0.0128 -0.0465 0.0168  47  PHE B C   
2046 O  O   . PHE B 47  ? 0.2432 0.1258 0.3116 0.0121  -0.0395 -0.0297 47  PHE B O   
2047 C  CB  . PHE B 47  ? 0.2737 0.1745 0.3085 0.0091  -0.0551 -0.0368 47  PHE B CB  
2048 C  CG  . PHE B 47  ? 0.3014 0.1655 0.3004 0.0045  -0.0398 -0.0416 47  PHE B CG  
2049 C  CD1 . PHE B 47  ? 0.3943 0.1493 0.2911 0.0050  -0.0518 -0.0247 47  PHE B CD1 
2050 C  CD2 . PHE B 47  ? 0.2929 0.1839 0.2877 -0.0025 -0.0582 -0.0319 47  PHE B CD2 
2051 C  CE1 . PHE B 47  ? 0.4020 0.1819 0.2919 -0.0141 -0.0840 -0.0274 47  PHE B CE1 
2052 C  CE2 . PHE B 47  ? 0.2731 0.2224 0.3184 -0.0345 -0.0254 -0.0509 47  PHE B CE2 
2053 C  CZ  . PHE B 47  ? 0.3338 0.1719 0.3121 -0.0060 -0.0794 -0.0356 47  PHE B CZ  
2054 N  N   . LYS B 48  ? 0.2175 0.1992 0.3215 -0.0425 -0.0439 -0.0037 48  LYS B N   
2055 C  CA  . LYS B 48  ? 0.2140 0.2644 0.3165 -0.0040 -0.0476 0.0262  48  LYS B CA  
2056 C  C   . LYS B 48  ? 0.2228 0.1505 0.3404 -0.0377 -0.0850 -0.0307 48  LYS B C   
2057 O  O   . LYS B 48  ? 0.2131 0.1913 0.3169 -0.0248 -0.0616 0.0010  48  LYS B O   
2058 C  CB  . LYS B 48  ? 0.2805 0.2967 0.2954 0.0187  -0.0469 0.0389  48  LYS B CB  
2059 C  CG  . LYS B 48  ? 0.3510 0.3068 0.3717 0.0069  -0.1197 0.0596  48  LYS B CG  
2060 C  CD  . LYS B 48  ? 0.3917 0.3487 0.4055 0.0028  -0.1723 0.0555  48  LYS B CD  
2061 C  CE  . LYS B 48  ? 0.4398 0.3426 0.3992 0.0458  -0.2092 -0.0028 48  LYS B CE  
2062 N  NZ  . LYS B 48  ? 0.5965 0.6552 0.5690 0.0629  -0.3336 -0.3235 48  LYS B NZ  
2063 N  N   . LEU B 49  ? 0.2536 0.1607 0.3541 -0.0514 -0.0604 -0.0372 49  LEU B N   
2064 C  CA  . LEU B 49  ? 0.2745 0.1442 0.3218 -0.0353 -0.0160 -0.0245 49  LEU B CA  
2065 C  C   . LEU B 49  ? 0.2606 0.1065 0.3341 -0.0064 -0.0343 -0.0144 49  LEU B C   
2066 O  O   . LEU B 49  ? 0.2370 0.1181 0.3275 -0.0329 0.0082  -0.0280 49  LEU B O   
2067 C  CB  . LEU B 49  ? 0.2399 0.1507 0.4262 -0.0393 -0.0072 -0.0324 49  LEU B CB  
2068 C  CG  . LEU B 49  ? 0.3454 0.1586 0.4684 -0.0689 0.0407  -0.0576 49  LEU B CG  
2069 C  CD1 . LEU B 49  ? 0.4528 0.1901 0.3743 -0.1259 0.0411  -0.0567 49  LEU B CD1 
2070 C  CD2 . LEU B 49  ? 0.3782 0.2081 0.3797 0.0001  0.0137  -0.0422 49  LEU B CD2 
2071 N  N   . VAL B 50  ? 0.2143 0.1159 0.3305 -0.0219 -0.0463 -0.0234 50  VAL B N   
2072 C  CA  . VAL B 50  ? 0.2854 0.1409 0.3530 -0.0658 -0.0498 -0.0437 50  VAL B CA  
2073 C  C   . VAL B 50  ? 0.2335 0.1152 0.3407 -0.0246 -0.0530 -0.0277 50  VAL B C   
2074 O  O   . VAL B 50  ? 0.2367 0.1254 0.3275 -0.0067 -0.0536 -0.0210 50  VAL B O   
2075 C  CB  . VAL B 50  ? 0.3174 0.3152 0.2693 -0.0762 -0.0046 -0.0577 50  VAL B CB  
2076 C  CG1 . VAL B 50  ? 0.6042 0.3288 0.5603 0.0250  -0.0983 -0.2384 50  VAL B CG1 
2077 C  CG2 . VAL B 50  ? 0.5617 0.3738 0.3550 0.0414  0.0833  0.0792  50  VAL B CG2 
2078 N  N   . MET B 51  ? 0.2208 0.0964 0.3400 -0.0022 -0.0572 -0.0469 51  MET B N   
2079 C  CA  . MET B 51  ? 0.2316 0.1161 0.3166 -0.0166 -0.0628 -0.0310 51  MET B CA  
2080 C  C   . MET B 51  ? 0.2278 0.0940 0.2745 -0.0180 -0.0763 -0.0168 51  MET B C   
2081 O  O   . MET B 51  ? 0.2294 0.1110 0.2642 -0.0161 -0.0798 -0.0232 51  MET B O   
2082 C  CB  . MET B 51  ? 0.1791 0.1424 0.3445 -0.0162 -0.0508 -0.0179 51  MET B CB  
2083 C  CG  . MET B 51  ? 0.2423 0.1918 0.3518 0.0307  -0.0399 -0.0401 51  MET B CG  
2084 S  SD  . MET B 51  ? 0.3811 0.1483 0.3868 0.0050  -0.0502 -0.0424 51  MET B SD  
2085 C  CE  . MET B 51  ? 0.5259 0.3091 0.4112 -0.1688 -0.2085 0.0634  51  MET B CE  
2086 N  N   . ALA B 52  ? 0.2500 0.1129 0.2516 -0.0404 -0.0503 -0.0206 52  ALA B N   
2087 C  CA  . ALA B 52  ? 0.2734 0.1326 0.2136 -0.0319 -0.0347 -0.0136 52  ALA B CA  
2088 C  C   . ALA B 52  ? 0.2923 0.1242 0.1919 0.0117  -0.0271 -0.0448 52  ALA B C   
2089 O  O   . ALA B 52  ? 0.2951 0.0789 0.2564 0.0018  -0.0435 0.0265  52  ALA B O   
2090 C  CB  . ALA B 52  ? 0.2680 0.1468 0.2444 -0.0209 -0.0542 -0.0338 52  ALA B CB  
2091 N  N   . SER B 53  ? 0.2991 0.1043 0.2300 -0.0098 -0.0424 -0.0108 53  SER B N   
2092 C  CA  . SER B 53  ? 0.2608 0.1053 0.2285 -0.0131 -0.0298 -0.0113 53  SER B CA  
2093 C  C   . SER B 53  ? 0.2426 0.0994 0.2482 -0.0104 -0.0261 -0.0056 53  SER B C   
2094 O  O   . SER B 53  ? 0.2421 0.1035 0.2536 -0.0076 -0.0247 0.0061  53  SER B O   
2095 C  CB  . SER B 53  ? 0.2567 0.1374 0.2434 -0.0370 -0.0427 0.0078  53  SER B CB  
2096 O  OG  . SER B 53  ? 0.2646 0.1107 0.2935 -0.0216 -0.0195 -0.0272 53  SER B OG  
2097 N  N   . LEU B 54  ? 0.2613 0.1042 0.2312 0.0034  -0.0482 -0.0149 54  LEU B N   
2098 C  CA  . LEU B 54  ? 0.2393 0.1163 0.2241 0.0039  -0.0379 -0.0229 54  LEU B CA  
2099 C  C   . LEU B 54  ? 0.2402 0.1298 0.2151 0.0024  -0.0384 -0.0313 54  LEU B C   
2100 O  O   . LEU B 54  ? 0.2505 0.1097 0.2294 -0.0097 -0.0607 -0.0008 54  LEU B O   
2101 C  CB  . LEU B 54  ? 0.2420 0.1127 0.2817 0.0028  -0.0189 -0.0231 54  LEU B CB  
2102 C  CG  . LEU B 54  ? 0.2436 0.1748 0.2609 -0.0228 -0.0213 -0.0837 54  LEU B CG  
2103 C  CD1 . LEU B 54  ? 0.3088 0.2111 0.2979 0.0406  0.0108  -0.1011 54  LEU B CD1 
2104 C  CD2 . LEU B 54  ? 0.2877 0.3079 0.2727 -0.0339 -0.0361 -0.1283 54  LEU B CD2 
2105 N  N   . TYR B 55  ? 0.2277 0.0844 0.2161 0.0126  -0.0446 -0.0295 55  TYR B N   
2106 C  CA  . TYR B 55  ? 0.2325 0.0899 0.2296 0.0182  -0.0446 0.0131  55  TYR B CA  
2107 C  C   . TYR B 55  ? 0.2220 0.0502 0.2185 -0.0093 -0.0258 -0.0084 55  TYR B C   
2108 O  O   . TYR B 55  ? 0.2265 0.0676 0.2955 -0.0182 -0.0666 0.0303  55  TYR B O   
2109 C  CB  . TYR B 55  ? 0.2199 0.1135 0.2304 -0.0278 -0.0441 -0.0006 55  TYR B CB  
2110 C  CG  . TYR B 55  ? 0.2288 0.1062 0.2368 -0.0211 -0.0355 -0.0123 55  TYR B CG  
2111 C  CD1 . TYR B 55  ? 0.2241 0.1012 0.2076 -0.0176 -0.0332 -0.0204 55  TYR B CD1 
2112 C  CD2 . TYR B 55  ? 0.3122 0.0995 0.2204 -0.0301 -0.0077 -0.0142 55  TYR B CD2 
2113 C  CE1 . TYR B 55  ? 0.2861 0.1170 0.2288 -0.0132 0.0180  -0.0116 55  TYR B CE1 
2114 C  CE2 . TYR B 55  ? 0.2926 0.0988 0.2225 0.0236  -0.0130 0.0365  55  TYR B CE2 
2115 C  CZ  . TYR B 55  ? 0.2782 0.1009 0.2215 0.0161  0.0014  0.0167  55  TYR B CZ  
2116 O  OH  . TYR B 55  ? 0.2652 0.1298 0.2797 0.0079  0.0195  -0.0106 55  TYR B OH  
2117 N  N   . HIS B 56  ? 0.2380 0.0575 0.2454 -0.0089 -0.0412 -0.0147 56  HIS B N   
2118 C  CA  . HIS B 56  ? 0.2656 0.0631 0.2300 0.0141  -0.0449 -0.0338 56  HIS B CA  
2119 C  C   . HIS B 56  ? 0.2652 0.0456 0.2251 -0.0025 -0.0418 0.0032  56  HIS B C   
2120 O  O   . HIS B 56  ? 0.2610 0.0995 0.2591 0.0145  -0.0510 -0.0146 56  HIS B O   
2121 C  CB  . HIS B 56  ? 0.2439 0.0689 0.3169 0.0086  -0.0557 -0.0435 56  HIS B CB  
2122 C  CG  . HIS B 56  ? 0.2467 0.1015 0.3297 -0.0392 -0.0460 -0.0682 56  HIS B CG  
2123 N  ND1 . HIS B 56  ? 0.2413 0.1377 0.3625 -0.0131 -0.0788 -0.0424 56  HIS B ND1 
2124 C  CD2 . HIS B 56  ? 0.2508 0.0595 0.3072 0.0263  -0.0606 -0.0126 56  HIS B CD2 
2125 C  CE1 . HIS B 56  ? 0.3072 0.0537 0.3616 -0.0168 -0.1134 -0.0260 56  HIS B CE1 
2126 N  NE2 . HIS B 56  ? 0.3294 0.1472 0.3355 -0.0018 -0.0709 -0.0658 56  HIS B NE2 
2127 N  N   . ILE B 57  ? 0.2596 0.0762 0.2188 -0.0061 -0.0508 -0.0052 57  ILE B N   
2128 C  CA  . ILE B 57  ? 0.2960 0.0830 0.2140 -0.0484 -0.0547 0.0339  57  ILE B CA  
2129 C  C   . ILE B 57  ? 0.2453 0.0726 0.2647 -0.0155 -0.0695 0.0049  57  ILE B C   
2130 O  O   . ILE B 57  ? 0.2301 0.0966 0.2833 0.0055  -0.0585 -0.0117 57  ILE B O   
2131 C  CB  . ILE B 57  ? 0.3474 0.1673 0.2173 -0.0620 -0.0279 0.0789  57  ILE B CB  
2132 C  CG1 . ILE B 57  ? 0.2538 0.1700 0.2927 -0.0376 -0.0490 0.0868  57  ILE B CG1 
2133 C  CG2 . ILE B 57  ? 0.3790 0.1491 0.2196 -0.0042 -0.0297 0.0492  57  ILE B CG2 
2134 C  CD1 . ILE B 57  ? 0.2710 0.1793 0.3172 0.0002  -0.0130 0.0788  57  ILE B CD1 
2135 N  N   . TYR B 58  ? 0.2400 0.0608 0.2558 -0.0048 -0.0533 -0.0148 58  TYR B N   
2136 C  CA  . TYR B 58  ? 0.2507 0.0588 0.2244 -0.0045 -0.0627 -0.0143 58  TYR B CA  
2137 C  C   . TYR B 58  ? 0.2667 0.0683 0.2751 -0.0334 -0.0412 -0.0418 58  TYR B C   
2138 O  O   . TYR B 58  ? 0.2529 0.0787 0.2832 -0.0244 -0.0800 0.0103  58  TYR B O   
2139 C  CB  . TYR B 58  ? 0.2827 0.0648 0.2348 0.0080  -0.0942 -0.0332 58  TYR B CB  
2140 C  CG  . TYR B 58  ? 0.2885 0.0740 0.2486 0.0318  -0.0909 -0.0353 58  TYR B CG  
2141 C  CD1 . TYR B 58  ? 0.3766 0.1034 0.2524 -0.0083 -0.0899 -0.0645 58  TYR B CD1 
2142 C  CD2 . TYR B 58  ? 0.2853 0.1926 0.2680 0.0440  -0.0835 0.0121  58  TYR B CD2 
2143 C  CE1 . TYR B 58  ? 0.3679 0.0585 0.2845 0.0250  -0.0763 -0.0677 58  TYR B CE1 
2144 C  CE2 . TYR B 58  ? 0.3078 0.2038 0.2878 0.0265  -0.0601 -0.0021 58  TYR B CE2 
2145 C  CZ  . TYR B 58  ? 0.3536 0.2196 0.2401 0.0554  -0.1081 0.0376  58  TYR B CZ  
2146 O  OH  . TYR B 58  ? 0.3525 0.2326 0.2892 0.0002  -0.0710 -0.0011 58  TYR B OH  
2147 N  N   . VAL B 59  ? 0.2337 0.0896 0.2774 0.0341  -0.0463 -0.0486 59  VAL B N   
2148 C  CA  . VAL B 59  ? 0.2299 0.0853 0.2611 0.0136  -0.0547 -0.0008 59  VAL B CA  
2149 C  C   . VAL B 59  ? 0.2194 0.0682 0.2522 0.0105  -0.0438 -0.0005 59  VAL B C   
2150 O  O   . VAL B 59  ? 0.2457 0.1263 0.2609 -0.0378 -0.0768 0.0223  59  VAL B O   
2151 C  CB  . VAL B 59  ? 0.2365 0.0988 0.2170 -0.0517 -0.0199 0.0353  59  VAL B CB  
2152 C  CG1 . VAL B 59  ? 0.2210 0.1612 0.2332 -0.0482 -0.0490 -0.0207 59  VAL B CG1 
2153 C  CG2 . VAL B 59  ? 0.2302 0.1204 0.2415 -0.0540 -0.0290 0.0476  59  VAL B CG2 
2154 N  N   . ALA B 60  ? 0.2360 0.1169 0.2721 -0.0162 -0.0641 0.0424  60  ALA B N   
2155 C  CA  . ALA B 60  ? 0.2464 0.0679 0.2415 0.0101  -0.0502 0.0028  60  ALA B CA  
2156 C  C   . ALA B 60  ? 0.2192 0.0917 0.2686 0.0078  -0.0560 -0.0168 60  ALA B C   
2157 O  O   . ALA B 60  ? 0.2162 0.1284 0.2785 0.0021  -0.0600 0.0080  60  ALA B O   
2158 C  CB  . ALA B 60  ? 0.2613 0.0766 0.3117 -0.0124 -0.0665 0.0127  60  ALA B CB  
2159 N  N   . LEU B 61  ? 0.2160 0.1008 0.2524 0.0081  -0.0682 -0.0258 61  LEU B N   
2160 C  CA  . LEU B 61  ? 0.2313 0.1165 0.2309 -0.0280 -0.0543 -0.0088 61  LEU B CA  
2161 C  C   . LEU B 61  ? 0.2285 0.1067 0.2775 -0.0229 -0.0833 0.0092  61  LEU B C   
2162 O  O   . LEU B 61  ? 0.2264 0.1134 0.3212 -0.0140 -0.0977 -0.0101 61  LEU B O   
2163 C  CB  . LEU B 61  ? 0.2526 0.1005 0.2594 -0.0165 -0.0415 -0.0258 61  LEU B CB  
2164 C  CG  . LEU B 61  ? 0.2847 0.0957 0.2177 -0.0196 -0.0373 0.0108  61  LEU B CG  
2165 C  CD1 . LEU B 61  ? 0.3858 0.1072 0.2287 0.0407  -0.0508 0.0122  61  LEU B CD1 
2166 C  CD2 . LEU B 61  ? 0.3129 0.1570 0.2591 0.0046  -0.0101 -0.0223 61  LEU B CD2 
2167 N  N   . GLU B 62  ? 0.3037 0.0819 0.2802 -0.0314 -0.1099 0.0004  62  GLU B N   
2168 C  CA  . GLU B 62  ? 0.2396 0.0889 0.3129 -0.0157 -0.1110 0.0132  62  GLU B CA  
2169 C  C   . GLU B 62  ? 0.2419 0.1245 0.3127 0.0045  -0.1174 -0.0072 62  GLU B C   
2170 O  O   . GLU B 62  ? 0.2584 0.1242 0.3052 -0.0272 -0.0718 0.0125  62  GLU B O   
2171 C  CB  . GLU B 62  ? 0.2068 0.1274 0.2699 -0.0277 -0.0734 0.0457  62  GLU B CB  
2172 C  CG  . GLU B 62  ? 0.2435 0.0962 0.2696 -0.0103 -0.0757 0.0247  62  GLU B CG  
2173 C  CD  . GLU B 62  ? 0.2263 0.1079 0.2631 -0.0188 -0.0907 0.0122  62  GLU B CD  
2174 O  OE1 . GLU B 62  ? 0.3430 0.0982 0.2459 0.0346  -0.1085 -0.0156 62  GLU B OE1 
2175 O  OE2 . GLU B 62  ? 0.2738 0.1217 0.2737 0.0163  -0.0917 -0.0211 62  GLU B OE2 
2176 N  N   . GLU B 63  ? 0.2616 0.0897 0.3144 0.0200  -0.1314 0.0204  63  GLU B N   
2177 C  CA  . GLU B 63  ? 0.2738 0.0834 0.3779 0.0576  -0.1389 0.0101  63  GLU B CA  
2178 C  C   . GLU B 63  ? 0.2429 0.1022 0.3565 0.0117  -0.1144 0.0214  63  GLU B C   
2179 O  O   . GLU B 63  ? 0.2604 0.1523 0.3951 -0.0264 -0.1196 0.0242  63  GLU B O   
2180 C  CB  . GLU B 63  ? 0.3136 0.1475 0.4120 0.0383  -0.1340 -0.0524 63  GLU B CB  
2181 C  CG  . GLU B 63  ? 0.4551 0.1833 0.4528 -0.0129 -0.2143 -0.0484 63  GLU B CG  
2182 C  CD  . GLU B 63  ? 0.6056 0.2020 0.5207 0.0261  -0.3504 -0.0803 63  GLU B CD  
2183 O  OE1 . GLU B 63  ? 0.9161 0.2179 0.3616 0.1388  -0.0520 -0.0428 63  GLU B OE1 
2184 O  OE2 . GLU B 63  ? 0.4054 0.3115 0.4228 0.0232  -0.1771 -0.0803 63  GLU B OE2 
2185 N  N   . GLU B 64  ? 0.2568 0.1073 0.3610 0.0174  -0.0928 0.0209  64  GLU B N   
2186 C  CA  . GLU B 64  ? 0.3113 0.0732 0.3721 0.0359  -0.1100 0.0249  64  GLU B CA  
2187 C  C   . GLU B 64  ? 0.3191 0.0976 0.3694 0.0202  -0.1130 0.0167  64  GLU B C   
2188 O  O   . GLU B 64  ? 0.2656 0.1163 0.3853 0.0092  -0.0728 0.0056  64  GLU B O   
2189 C  CB  . GLU B 64  ? 0.3080 0.1082 0.3329 0.0120  -0.0896 0.0056  64  GLU B CB  
2190 C  CG  . GLU B 64  ? 0.2843 0.1064 0.3596 -0.0192 -0.0495 -0.0036 64  GLU B CG  
2191 C  CD  . GLU B 64  ? 0.2873 0.1547 0.3522 0.0195  -0.0852 -0.0144 64  GLU B CD  
2192 O  OE1 . GLU B 64  ? 0.2935 0.1293 0.3859 0.0024  -0.0955 -0.0038 64  GLU B OE1 
2193 O  OE2 . GLU B 64  ? 0.2948 0.1558 0.3921 0.0123  -0.0671 -0.0438 64  GLU B OE2 
2194 N  N   . ILE B 65  ? 0.2646 0.0980 0.3502 -0.0093 -0.0974 -0.0242 65  ILE B N   
2195 C  CA  . ILE B 65  ? 0.2661 0.0975 0.3694 -0.0319 -0.1089 -0.0255 65  ILE B CA  
2196 C  C   . ILE B 65  ? 0.2786 0.0940 0.3971 -0.0165 -0.0838 -0.0123 65  ILE B C   
2197 O  O   . ILE B 65  ? 0.2586 0.1404 0.3480 -0.0417 -0.0595 0.0212  65  ILE B O   
2198 C  CB  . ILE B 65  ? 0.2701 0.1077 0.3166 -0.0282 -0.1109 -0.0590 65  ILE B CB  
2199 C  CG1 . ILE B 65  ? 0.2777 0.0964 0.3513 0.0059  -0.1046 -0.0116 65  ILE B CG1 
2200 C  CG2 . ILE B 65  ? 0.3387 0.0832 0.3825 -0.0163 -0.1402 -0.0160 65  ILE B CG2 
2201 C  CD1 . ILE B 65  ? 0.2753 0.1133 0.3234 0.0080  -0.1018 -0.0228 65  ILE B CD1 
2202 N  N   . GLU B 66  ? 0.2300 0.1307 0.4017 -0.0204 -0.0948 -0.0086 66  GLU B N   
2203 C  CA  . GLU B 66  ? 0.2512 0.1771 0.4307 -0.0240 -0.0397 -0.0249 66  GLU B CA  
2204 C  C   . GLU B 66  ? 0.2407 0.1418 0.5192 -0.0590 -0.0803 0.0420  66  GLU B C   
2205 O  O   . GLU B 66  ? 0.2596 0.1811 0.5466 -0.0779 -0.0820 0.0198  66  GLU B O   
2206 C  CB  . GLU B 66  ? 0.2932 0.1584 0.4590 -0.0624 -0.0802 0.0442  66  GLU B CB  
2207 C  CG  . GLU B 66  ? 0.3312 0.1830 0.5260 -0.0252 -0.1490 -0.0527 66  GLU B CG  
2208 C  CD  . GLU B 66  ? 0.3943 0.1860 0.5409 -0.0460 -0.1279 -0.0640 66  GLU B CD  
2209 O  OE1 . GLU B 66  ? 0.4879 0.2118 0.5606 -0.1109 -0.1126 -0.0014 66  GLU B OE1 
2210 O  OE2 . GLU B 66  ? 0.4846 0.1927 0.4073 0.0236  -0.1676 -0.0071 66  GLU B OE2 
2211 N  N   . ARG B 67  ? 0.3237 0.1400 0.4237 -0.0440 -0.1219 0.0449  67  ARG B N   
2212 C  CA  . ARG B 67  ? 0.3109 0.1398 0.3505 -0.0323 -0.0847 -0.0102 67  ARG B CA  
2213 C  C   . ARG B 67  ? 0.2819 0.1646 0.3581 -0.0399 -0.0834 -0.0155 67  ARG B C   
2214 O  O   . ARG B 67  ? 0.2865 0.2858 0.4156 -0.0695 -0.0925 -0.0158 67  ARG B O   
2215 C  CB  . ARG B 67  ? 0.3678 0.1365 0.3957 -0.0156 -0.0329 -0.0512 67  ARG B CB  
2216 C  CG  . ARG B 67  ? 0.3694 0.1650 0.5757 -0.0079 0.0290  -0.0787 67  ARG B CG  
2217 C  CD  A ARG B 67  ? 0.4921 0.1593 0.6925 0.0505  0.0587  -0.0737 67  ARG B CD  
2218 C  CD  B ARG B 67  ? 0.4464 0.1443 0.6404 0.0408  0.0149  -0.1036 67  ARG B CD  
2219 N  NE  A ARG B 67  ? 0.4673 0.2353 0.8011 0.1233  0.0521  -0.0733 67  ARG B NE  
2220 N  NE  B ARG B 67  ? 0.3882 0.1138 0.5906 0.0271  0.1106  -0.1243 67  ARG B NE  
2221 C  CZ  A ARG B 67  ? 0.4138 0.3761 0.9706 0.2707  -0.1076 -0.0149 67  ARG B CZ  
2222 C  CZ  B ARG B 67  ? 0.3947 0.1929 0.5581 -0.0629 0.0814  -0.0385 67  ARG B CZ  
2223 N  NH1 A ARG B 67  ? 0.4812 0.7929 1.1063 0.2972  0.0467  -0.1540 67  ARG B NH1 
2224 N  NH1 B ARG B 67  ? 0.3074 0.4114 0.5295 -0.1130 0.1921  -0.1257 67  ARG B NH1 
2225 N  NH2 A ARG B 67  ? 0.4628 0.3826 1.1849 0.1315  -0.1428 0.0363  67  ARG B NH2 
2226 N  NH2 B ARG B 67  ? 0.4360 0.3183 0.4751 -0.2266 -0.0215 0.0077  67  ARG B NH2 
2227 N  N   . ASN B 68  ? 0.3141 0.1399 0.3541 -0.0294 -0.0735 -0.0177 68  ASN B N   
2228 C  CA  . ASN B 68  ? 0.2855 0.1487 0.3591 -0.0078 -0.0796 -0.0027 68  ASN B CA  
2229 C  C   . ASN B 68  ? 0.2557 0.1600 0.3513 -0.0276 -0.1018 -0.0188 68  ASN B C   
2230 O  O   . ASN B 68  ? 0.3356 0.1998 0.3673 -0.0360 -0.1435 -0.0282 68  ASN B O   
2231 C  CB  . ASN B 68  ? 0.3224 0.1617 0.3714 -0.0202 -0.0872 0.0160  68  ASN B CB  
2232 C  CG  . ASN B 68  ? 0.3528 0.1545 0.4010 -0.0257 -0.1191 0.0140  68  ASN B CG  
2233 O  OD1 . ASN B 68  ? 0.4383 0.1751 0.4539 -0.0400 -0.1870 0.0105  68  ASN B OD1 
2234 N  ND2 . ASN B 68  ? 0.3364 0.1430 0.3569 -0.0254 -0.0792 0.0329  68  ASN B ND2 
2235 N  N   . LYS B 69  ? 0.3107 0.1307 0.3716 -0.0293 -0.1287 -0.0326 69  LYS B N   
2236 C  CA  . LYS B 69  ? 0.3132 0.1573 0.3903 -0.0132 -0.1317 -0.0501 69  LYS B CA  
2237 C  C   . LYS B 69  ? 0.3146 0.1401 0.3852 -0.0544 -0.0975 -0.0420 69  LYS B C   
2238 O  O   . LYS B 69  ? 0.3962 0.1523 0.4377 0.0200  -0.1543 -0.0815 69  LYS B O   
2239 C  CB  . LYS B 69  ? 0.2603 0.1684 0.5072 -0.0045 -0.1304 0.0131  69  LYS B CB  
2240 C  CG  . LYS B 69  ? 0.2693 0.1695 0.4886 0.0261  -0.1361 0.0482  69  LYS B CG  
2241 C  CD  . LYS B 69  ? 0.3790 0.1894 0.5199 0.0037  -0.2043 0.0574  69  LYS B CD  
2242 C  CE  . LYS B 69  ? 0.4683 0.2897 0.4730 -0.0022 -0.1987 0.0825  69  LYS B CE  
2243 N  NZ  . LYS B 69  ? 0.7463 0.3555 0.5945 -0.2762 -0.3578 0.2282  69  LYS B NZ  
2244 N  N   . GLU B 70  ? 0.3095 0.1706 0.3638 -0.0395 -0.1025 0.0234  70  GLU B N   
2245 C  CA  . GLU B 70  ? 0.3263 0.2687 0.4412 -0.1025 -0.1316 0.0659  70  GLU B CA  
2246 C  C   . GLU B 70  ? 0.2298 0.2289 0.5045 -0.0804 -0.1645 0.0719  70  GLU B C   
2247 O  O   . GLU B 70  ? 0.3336 0.2670 0.5605 -0.0250 -0.2377 -0.0064 70  GLU B O   
2248 C  CB  . GLU B 70  ? 0.4006 0.5148 0.5224 -0.2101 -0.0651 0.0536  70  GLU B CB  
2249 C  CG  . GLU B 70  ? 0.5576 0.7550 0.5899 -0.2004 -0.0037 0.2287  70  GLU B CG  
2250 C  CD  . GLU B 70  ? 0.8387 0.7349 0.7102 -0.2236 -0.0941 0.2870  70  GLU B CD  
2251 O  OE1 . GLU B 70  ? 1.1872 0.6265 0.8989 -0.2852 -0.4498 0.4234  70  GLU B OE1 
2252 O  OE2 . GLU B 70  ? 1.0632 0.7695 0.5213 -0.2671 0.1536  0.1812  70  GLU B OE2 
2253 N  N   . SER B 71  ? 0.3084 0.1643 0.5313 -0.0233 -0.0819 0.0300  71  SER B N   
2254 C  CA  . SER B 71  ? 0.3742 0.1416 0.5327 -0.0365 -0.0978 0.0213  71  SER B CA  
2255 C  C   . SER B 71  ? 0.3031 0.0986 0.5087 0.0202  -0.1907 -0.0069 71  SER B C   
2256 O  O   . SER B 71  ? 0.3237 0.1661 0.5858 0.0635  -0.1909 -0.0086 71  SER B O   
2257 C  CB  . SER B 71  ? 0.4601 0.1051 0.5827 0.0440  -0.0980 -0.0342 71  SER B CB  
2258 O  OG  . SER B 71  ? 0.4668 0.1259 0.8157 -0.0545 -0.3170 0.0453  71  SER B OG  
2259 N  N   . PRO B 72  ? 0.3558 0.1601 0.5401 -0.0289 -0.2334 0.0171  72  PRO B N   
2260 C  CA  . PRO B 72  ? 0.4042 0.2157 0.4862 -0.0264 -0.2452 0.0403  72  PRO B CA  
2261 C  C   . PRO B 72  ? 0.4165 0.1371 0.5043 0.0079  -0.2083 0.0424  72  PRO B C   
2262 O  O   . PRO B 72  ? 0.4377 0.1624 0.4905 -0.0213 -0.2078 -0.0028 72  PRO B O   
2263 C  CB  . PRO B 72  ? 0.4523 0.3684 0.5594 0.0026  -0.3032 -0.0047 72  PRO B CB  
2264 C  CG  . PRO B 72  ? 0.4034 0.4729 0.5823 0.0301  -0.2764 0.0252  72  PRO B CG  
2265 C  CD  . PRO B 72  ? 0.3819 0.3415 0.5821 0.0239  -0.2711 0.0363  72  PRO B CD  
2266 N  N   . VAL B 73  ? 0.4011 0.1507 0.4588 0.0166  -0.1931 0.0402  73  VAL B N   
2267 C  CA  . VAL B 73  ? 0.4153 0.1759 0.4084 -0.0158 -0.1797 -0.0268 73  VAL B CA  
2268 C  C   . VAL B 73  ? 0.4005 0.1432 0.3349 -0.0026 -0.1430 -0.0551 73  VAL B C   
2269 O  O   . VAL B 73  ? 0.4022 0.1989 0.4365 -0.0027 -0.1425 0.0267  73  VAL B O   
2270 C  CB  . VAL B 73  ? 0.3721 0.1747 0.5052 -0.0039 -0.2103 -0.0296 73  VAL B CB  
2271 C  CG1 . VAL B 73  ? 0.4333 0.2419 0.6344 0.0114  -0.2859 0.0441  73  VAL B CG1 
2272 C  CG2 . VAL B 73  ? 0.3809 0.1746 0.5206 0.0371  -0.2074 -0.0832 73  VAL B CG2 
2273 N  N   . PHE B 74  ? 0.3889 0.1356 0.4014 0.0015  -0.1337 -0.0294 74  PHE B N   
2274 C  CA  . PHE B 74  ? 0.3322 0.1554 0.3564 -0.0398 -0.0922 0.0058  74  PHE B CA  
2275 C  C   . PHE B 74  ? 0.3153 0.1462 0.3777 -0.0414 -0.1648 -0.0166 74  PHE B C   
2276 O  O   . PHE B 74  ? 0.3194 0.1835 0.3534 -0.0105 -0.1016 -0.0383 74  PHE B O   
2277 C  CB  . PHE B 74  ? 0.3475 0.1361 0.4059 0.0179  -0.1318 -0.0289 74  PHE B CB  
2278 C  CG  . PHE B 74  ? 0.3495 0.0869 0.3842 0.0127  -0.1248 0.0029  74  PHE B CG  
2279 C  CD1 . PHE B 74  ? 0.3445 0.0648 0.3352 0.0271  -0.1037 -0.0108 74  PHE B CD1 
2280 C  CD2 . PHE B 74  ? 0.3842 0.1528 0.3452 -0.0293 -0.1360 0.0536  74  PHE B CD2 
2281 C  CE1 . PHE B 74  ? 0.3847 0.0977 0.4065 -0.0314 -0.1815 0.0329  74  PHE B CE1 
2282 C  CE2 . PHE B 74  ? 0.4142 0.1271 0.2962 -0.0380 -0.1838 0.0283  74  PHE B CE2 
2283 C  CZ  . PHE B 74  ? 0.3923 0.1064 0.3129 -0.0278 -0.1893 0.0054  74  PHE B CZ  
2284 N  N   . ALA B 75  ? 0.3206 0.1274 0.4492 -0.0308 -0.1629 -0.0187 75  ALA B N   
2285 C  CA  . ALA B 75  ? 0.3287 0.1241 0.4483 -0.0333 -0.1431 -0.0242 75  ALA B CA  
2286 C  C   . ALA B 75  ? 0.3345 0.1212 0.3381 -0.0188 -0.1798 0.0083  75  ALA B C   
2287 O  O   . ALA B 75  ? 0.3695 0.1420 0.3230 0.0063  -0.1892 0.0030  75  ALA B O   
2288 C  CB  . ALA B 75  ? 0.3210 0.1246 0.5314 -0.0212 -0.1706 0.0159  75  ALA B CB  
2289 N  N   . PRO B 76  ? 0.4055 0.1628 0.3365 -0.0119 -0.2082 0.0194  76  PRO B N   
2290 C  CA  . PRO B 76  ? 0.4449 0.1946 0.2935 -0.0152 -0.1951 -0.0014 76  PRO B CA  
2291 C  C   . PRO B 76  ? 0.4295 0.0869 0.2895 -0.0100 -0.1668 0.0108  76  PRO B C   
2292 O  O   . PRO B 76  ? 0.4713 0.1074 0.3596 0.0060  -0.1628 -0.0259 76  PRO B O   
2293 C  CB  . PRO B 76  ? 0.4453 0.1904 0.3253 -0.0514 -0.2038 0.0402  76  PRO B CB  
2294 C  CG  . PRO B 76  ? 0.4509 0.2057 0.3283 -0.0419 -0.1987 0.0410  76  PRO B CG  
2295 C  CD  . PRO B 76  ? 0.4966 0.1545 0.3553 -0.0113 -0.2330 0.0203  76  PRO B CD  
2296 N  N   . VAL B 77  ? 0.4245 0.0787 0.3013 -0.0017 -0.1673 0.0120  77  VAL B N   
2297 C  CA  . VAL B 77  ? 0.4094 0.1341 0.2886 -0.0390 -0.1327 0.0018  77  VAL B CA  
2298 C  C   . VAL B 77  ? 0.3536 0.0450 0.2876 -0.0089 -0.1279 -0.0080 77  VAL B C   
2299 O  O   . VAL B 77  ? 0.3298 0.1400 0.2921 -0.0010 -0.1170 -0.0162 77  VAL B O   
2300 C  CB  . VAL B 77  ? 0.4345 0.1115 0.2602 -0.0195 -0.1260 0.0004  77  VAL B CB  
2301 C  CG1 . VAL B 77  ? 0.5961 0.1521 0.2769 0.0545  -0.0696 0.0278  77  VAL B CG1 
2302 C  CG2 . VAL B 77  ? 0.4233 0.1374 0.2960 -0.0143 -0.0821 0.0054  77  VAL B CG2 
2303 N  N   . TYR B 78  ? 0.3629 0.1172 0.3085 -0.0363 -0.1318 0.0159  78  TYR B N   
2304 C  CA  . TYR B 78  ? 0.2893 0.1106 0.3117 -0.0009 -0.1326 0.0200  78  TYR B CA  
2305 C  C   . TYR B 78  ? 0.3164 0.0933 0.3005 0.0166  -0.1455 -0.0291 78  TYR B C   
2306 O  O   . TYR B 78  ? 0.4359 0.1044 0.3297 -0.0037 -0.2124 -0.0322 78  TYR B O   
2307 C  CB  . TYR B 78  ? 0.2989 0.0995 0.3269 -0.0022 -0.1228 -0.0408 78  TYR B CB  
2308 C  CG  . TYR B 78  ? 0.3130 0.1378 0.3233 -0.0220 -0.1176 -0.0121 78  TYR B CG  
2309 C  CD1 . TYR B 78  ? 0.3083 0.1275 0.2922 -0.0364 -0.0631 -0.0225 78  TYR B CD1 
2310 C  CD2 . TYR B 78  ? 0.3576 0.1423 0.3499 -0.0598 -0.1936 0.0313  78  TYR B CD2 
2311 C  CE1 . TYR B 78  ? 0.3199 0.0970 0.2973 -0.0208 -0.0579 -0.0136 78  TYR B CE1 
2312 C  CE2 . TYR B 78  ? 0.3306 0.1356 0.3534 -0.0494 -0.1925 0.0625  78  TYR B CE2 
2313 C  CZ  . TYR B 78  ? 0.3752 0.1151 0.3084 -0.0553 -0.1362 0.0482  78  TYR B CZ  
2314 O  OH  . TYR B 78  ? 0.3712 0.1475 0.3116 -0.0310 -0.0751 0.0300  78  TYR B OH  
2315 N  N   . PHE B 79  ? 0.2945 0.1344 0.2204 0.0102  -0.1040 0.0277  79  PHE B N   
2316 C  CA  . PHE B 79  ? 0.3160 0.1274 0.2378 0.0062  -0.1329 0.0234  79  PHE B CA  
2317 C  C   . PHE B 79  ? 0.2963 0.1000 0.2384 0.0123  -0.1233 -0.0002 79  PHE B C   
2318 O  O   . PHE B 79  ? 0.3059 0.0966 0.2387 -0.0107 -0.1156 -0.0182 79  PHE B O   
2319 C  CB  . PHE B 79  ? 0.3461 0.0950 0.2389 0.0301  -0.1239 -0.0122 79  PHE B CB  
2320 C  CG  . PHE B 79  ? 0.3486 0.1075 0.2644 0.0521  -0.1565 -0.0326 79  PHE B CG  
2321 C  CD1 . PHE B 79  ? 0.4634 0.1135 0.2689 -0.0264 -0.1447 -0.0215 79  PHE B CD1 
2322 C  CD2 . PHE B 79  ? 0.4031 0.1110 0.2600 0.0818  -0.1763 -0.0465 79  PHE B CD2 
2323 C  CE1 . PHE B 79  ? 0.4765 0.1198 0.2834 0.0329  -0.1613 -0.0475 79  PHE B CE1 
2324 C  CE2 . PHE B 79  ? 0.4227 0.1203 0.2724 0.0467  -0.1865 -0.0523 79  PHE B CE2 
2325 C  CZ  . PHE B 79  ? 0.4610 0.1181 0.2683 0.0748  -0.1444 -0.0609 79  PHE B CZ  
2326 N  N   . PRO B 80  ? 0.3270 0.1055 0.2502 -0.0379 -0.1071 -0.0079 80  PRO B N   
2327 C  CA  . PRO B 80  ? 0.3206 0.1002 0.2477 -0.0026 -0.1057 -0.0035 80  PRO B CA  
2328 C  C   . PRO B 80  ? 0.3148 0.0873 0.2690 0.0073  -0.1104 -0.0279 80  PRO B C   
2329 O  O   . PRO B 80  ? 0.2984 0.1057 0.2728 -0.0067 -0.0986 -0.0192 80  PRO B O   
2330 C  CB  . PRO B 80  ? 0.3192 0.1478 0.2894 0.0147  -0.0826 -0.0554 80  PRO B CB  
2331 C  CG  . PRO B 80  ? 0.3199 0.1709 0.2710 -0.0207 -0.0791 -0.0325 80  PRO B CG  
2332 C  CD  . PRO B 80  ? 0.3291 0.1111 0.2745 -0.0400 -0.1040 -0.0025 80  PRO B CD  
2333 N  N   . GLU B 81  ? 0.3275 0.0898 0.2556 0.0059  -0.0917 -0.0294 81  GLU B N   
2334 C  CA  . GLU B 81  ? 0.3272 0.0695 0.2498 -0.0071 -0.0869 -0.0178 81  GLU B CA  
2335 C  C   . GLU B 81  ? 0.3237 0.0624 0.2376 -0.0079 -0.0992 0.0240  81  GLU B C   
2336 O  O   . GLU B 81  ? 0.3249 0.1112 0.2225 -0.0040 -0.0896 -0.0126 81  GLU B O   
2337 C  CB  . GLU B 81  ? 0.3452 0.0875 0.2630 -0.0381 -0.1039 0.0114  81  GLU B CB  
2338 C  CG  . GLU B 81  ? 0.3806 0.1928 0.3594 -0.0551 -0.0550 0.0577  81  GLU B CG  
2339 C  CD  . GLU B 81  ? 0.4046 0.3582 0.3203 -0.0651 -0.0164 0.0937  81  GLU B CD  
2340 O  OE1 . GLU B 81  ? 0.4964 0.2749 0.3742 -0.0549 -0.0964 0.0638  81  GLU B OE1 
2341 O  OE2 . GLU B 81  ? 0.5566 0.7294 0.3234 0.1494  -0.0766 -0.0285 81  GLU B OE2 
2342 N  N   . GLU B 82  ? 0.3347 0.0720 0.2424 0.0250  -0.0988 0.0375  82  GLU B N   
2343 C  CA  . GLU B 82  ? 0.3432 0.0637 0.2215 0.0157  -0.0994 0.0006  82  GLU B CA  
2344 C  C   . GLU B 82  ? 0.3181 0.0620 0.2343 0.0198  -0.1709 0.0431  82  GLU B C   
2345 O  O   . GLU B 82  ? 0.3144 0.1060 0.2209 0.0302  -0.1230 -0.0065 82  GLU B O   
2346 C  CB  . GLU B 82  ? 0.3836 0.0889 0.2296 0.0687  -0.1081 -0.0481 82  GLU B CB  
2347 C  CG  . GLU B 82  ? 0.4340 0.1032 0.3166 0.0644  -0.1383 -0.0810 82  GLU B CG  
2348 C  CD  . GLU B 82  ? 0.4491 0.1473 0.3280 0.0094  -0.1753 -0.0026 82  GLU B CD  
2349 O  OE1 . GLU B 82  ? 0.3885 0.1400 0.2623 -0.0303 -0.0949 0.0506  82  GLU B OE1 
2350 O  OE2 . GLU B 82  ? 0.5305 0.1565 0.3953 -0.0128 -0.1733 -0.0373 82  GLU B OE2 
2351 N  N   . LEU B 83  ? 0.2931 0.0562 0.2425 -0.0020 -0.0803 0.0199  83  LEU B N   
2352 C  CA  . LEU B 83  ? 0.3506 0.0630 0.2085 -0.0145 -0.0917 0.0125  83  LEU B CA  
2353 C  C   . LEU B 83  ? 0.2819 0.1174 0.2294 0.0083  -0.0977 -0.0228 83  LEU B C   
2354 O  O   . LEU B 83  ? 0.3073 0.1121 0.2434 -0.0054 -0.0844 -0.0282 83  LEU B O   
2355 C  CB  . LEU B 83  ? 0.4294 0.0862 0.2127 0.0122  -0.0734 0.0369  83  LEU B CB  
2356 C  CG  . LEU B 83  ? 0.4094 0.0980 0.2093 0.0321  -0.0753 0.0447  83  LEU B CG  
2357 C  CD1 . LEU B 83  ? 0.4204 0.0936 0.2223 0.0534  -0.0962 0.0186  83  LEU B CD1 
2358 C  CD2 . LEU B 83  ? 0.3979 0.1199 0.2015 0.0207  -0.1041 -0.0034 83  LEU B CD2 
2359 N  N   . HIS B 84  ? 0.2977 0.0708 0.2144 0.0021  -0.1110 -0.0125 84  HIS B N   
2360 C  CA  . HIS B 84  ? 0.3061 0.0990 0.1952 -0.0083 -0.1153 -0.0158 84  HIS B CA  
2361 C  C   . HIS B 84  ? 0.2973 0.0712 0.2197 -0.0028 -0.1149 -0.0103 84  HIS B C   
2362 O  O   . HIS B 84  ? 0.2948 0.0644 0.2209 -0.0054 -0.0999 -0.0094 84  HIS B O   
2363 C  CB  . HIS B 84  ? 0.2826 0.1301 0.2506 0.0245  -0.0862 -0.0047 84  HIS B CB  
2364 C  CG  . HIS B 84  ? 0.3597 0.0963 0.2223 0.0183  -0.0491 -0.0202 84  HIS B CG  
2365 N  ND1 . HIS B 84  ? 0.5202 0.1201 0.3370 0.0981  -0.2034 -0.0679 84  HIS B ND1 
2366 C  CD2 . HIS B 84  ? 0.2136 0.1120 0.2205 0.0054  -0.0372 -0.0132 84  HIS B CD2 
2367 C  CE1 . HIS B 84  ? 0.2921 0.0919 0.3397 -0.0049 -0.0775 -0.0002 84  HIS B CE1 
2368 N  NE2 . HIS B 84  ? 0.3366 0.1452 0.2792 0.0245  -0.0626 0.0232  84  HIS B NE2 
2369 N  N   . ARG B 85  ? 0.2465 0.0724 0.1994 0.0063  -0.0626 -0.0218 85  ARG B N   
2370 C  CA  . ARG B 85  ? 0.2457 0.0819 0.2293 -0.0063 -0.0633 -0.0282 85  ARG B CA  
2371 C  C   . ARG B 85  ? 0.2334 0.0431 0.2194 0.0203  -0.0929 -0.0041 85  ARG B C   
2372 O  O   . ARG B 85  ? 0.2489 0.0814 0.2561 -0.0036 -0.1159 -0.0147 85  ARG B O   
2373 C  CB  . ARG B 85  ? 0.2391 0.0910 0.2423 0.0115  -0.0652 -0.0010 85  ARG B CB  
2374 C  CG  . ARG B 85  ? 0.2568 0.1102 0.2429 0.0177  -0.0570 0.0020  85  ARG B CG  
2375 C  CD  . ARG B 85  ? 0.2138 0.0996 0.3355 -0.0061 -0.0127 0.0114  85  ARG B CD  
2376 N  NE  . ARG B 85  ? 0.2568 0.0978 0.2831 -0.0052 -0.0413 0.0051  85  ARG B NE  
2377 C  CZ  . ARG B 85  ? 0.3581 0.0656 0.2764 -0.0117 -0.1584 -0.0608 85  ARG B CZ  
2378 N  NH1 . ARG B 85  ? 0.3403 0.0744 0.2408 0.0087  -0.1280 -0.0276 85  ARG B NH1 
2379 N  NH2 . ARG B 85  ? 0.2986 0.0626 0.3593 0.0357  0.0009  -0.0403 85  ARG B NH2 
2380 N  N   . LYS B 86  ? 0.2451 0.1028 0.2478 0.0172  -0.0738 -0.0472 86  LYS B N   
2381 C  CA  . LYS B 86  ? 0.2648 0.0884 0.2241 0.0019  -0.0690 -0.0164 86  LYS B CA  
2382 C  C   . LYS B 86  ? 0.2158 0.1024 0.2657 -0.0270 -0.0833 0.0166  86  LYS B C   
2383 O  O   . LYS B 86  ? 0.2763 0.0855 0.2549 -0.0377 -0.0925 0.0169  86  LYS B O   
2384 C  CB  . LYS B 86  ? 0.2880 0.1263 0.2129 0.0508  -0.0610 -0.0005 86  LYS B CB  
2385 C  CG  . LYS B 86  ? 0.2875 0.1541 0.2036 0.0010  -0.0500 -0.0078 86  LYS B CG  
2386 C  CD  . LYS B 86  ? 0.3087 0.1449 0.2829 0.0095  0.0000  -0.0158 86  LYS B CD  
2387 C  CE  A LYS B 86  ? 0.2912 0.1740 0.3765 -0.0601 -0.0894 -0.0055 86  LYS B CE  
2388 C  CE  B LYS B 86  ? 0.2871 0.1814 0.3890 -0.0380 -0.0928 -0.0044 86  LYS B CE  
2389 N  NZ  A LYS B 86  ? 0.3346 0.2087 0.4678 -0.1187 0.0443  0.0380  86  LYS B NZ  
2390 N  NZ  B LYS B 86  ? 0.2502 0.2151 0.3306 -0.0655 -0.1676 -0.0720 86  LYS B NZ  
2391 N  N   . ALA B 87  ? 0.2120 0.0829 0.2450 -0.0010 -0.0656 -0.0181 87  ALA B N   
2392 C  CA  . ALA B 87  ? 0.2302 0.0822 0.2586 -0.0296 -0.0680 0.0004  87  ALA B CA  
2393 C  C   . ALA B 87  ? 0.2421 0.0852 0.2135 0.0064  -0.0741 -0.0084 87  ALA B C   
2394 O  O   . ALA B 87  ? 0.2466 0.0934 0.2030 -0.0019 -0.0665 -0.0128 87  ALA B O   
2395 C  CB  . ALA B 87  ? 0.2856 0.0634 0.3255 -0.0243 -0.0647 -0.0273 87  ALA B CB  
2396 N  N   . ALA B 88  ? 0.2366 0.0853 0.2028 -0.0086 -0.0840 -0.0195 88  ALA B N   
2397 C  CA  . ALA B 88  ? 0.2327 0.0756 0.2082 0.0055  -0.0848 0.0116  88  ALA B CA  
2398 C  C   . ALA B 88  ? 0.2274 0.0904 0.1943 -0.0154 -0.0622 0.0149  88  ALA B C   
2399 O  O   . ALA B 88  ? 0.2156 0.0922 0.2324 0.0115  -0.0676 -0.0327 88  ALA B O   
2400 C  CB  . ALA B 88  ? 0.2312 0.1282 0.2262 0.0119  -0.0768 -0.0183 88  ALA B CB  
2401 N  N   . LEU B 89  ? 0.2352 0.0821 0.1823 -0.0242 -0.0636 0.0133  89  LEU B N   
2402 C  CA  . LEU B 89  ? 0.2456 0.0849 0.2184 -0.0299 -0.0469 0.0136  89  LEU B CA  
2403 C  C   . LEU B 89  ? 0.2236 0.0570 0.2230 -0.0173 -0.0428 -0.0087 89  LEU B C   
2404 O  O   . LEU B 89  ? 0.2264 0.0908 0.2430 -0.0263 -0.0590 -0.0038 89  LEU B O   
2405 C  CB  . LEU B 89  ? 0.2524 0.0748 0.2093 0.0052  -0.0744 -0.0302 89  LEU B CB  
2406 C  CG  . LEU B 89  ? 0.2782 0.0914 0.1921 0.0049  -0.0859 -0.0074 89  LEU B CG  
2407 C  CD1 . LEU B 89  ? 0.3724 0.1282 0.2338 0.0314  -0.1449 -0.0075 89  LEU B CD1 
2408 C  CD2 . LEU B 89  ? 0.2902 0.0967 0.2411 -0.0100 -0.0536 -0.0078 89  LEU B CD2 
2409 N  N   . GLU B 90  ? 0.2369 0.0914 0.2368 -0.0396 -0.0359 -0.0048 90  GLU B N   
2410 C  CA  . GLU B 90  ? 0.2272 0.0795 0.2308 0.0018  -0.0371 0.0062  90  GLU B CA  
2411 C  C   . GLU B 90  ? 0.2478 0.1008 0.2698 0.0208  -0.0862 -0.0395 90  GLU B C   
2412 O  O   . GLU B 90  ? 0.2489 0.1210 0.2271 -0.0110 -0.0552 -0.0218 90  GLU B O   
2413 C  CB  . GLU B 90  ? 0.2307 0.0593 0.2504 0.0071  -0.0215 0.0003  90  GLU B CB  
2414 C  CG  . GLU B 90  ? 0.2341 0.0979 0.2510 0.0172  -0.0401 0.0050  90  GLU B CG  
2415 C  CD  . GLU B 90  ? 0.2354 0.1015 0.2352 0.0188  -0.0264 0.0232  90  GLU B CD  
2416 O  OE1 . GLU B 90  ? 0.2363 0.1019 0.2874 0.0143  -0.0604 0.0242  90  GLU B OE1 
2417 O  OE2 . GLU B 90  ? 0.2339 0.1265 0.3200 0.0245  -0.0782 0.0117  90  GLU B OE2 
2418 N  N   . GLN B 91  ? 0.2110 0.0878 0.2262 0.0047  -0.0538 -0.0091 91  GLN B N   
2419 C  CA  . GLN B 91  ? 0.2065 0.0834 0.2008 -0.0038 -0.0471 -0.0185 91  GLN B CA  
2420 C  C   . GLN B 91  ? 0.2116 0.0667 0.2151 -0.0088 -0.0562 -0.0094 91  GLN B C   
2421 O  O   . GLN B 91  ? 0.2035 0.1060 0.2168 -0.0235 -0.0557 0.0143  91  GLN B O   
2422 C  CB  . GLN B 91  ? 0.2278 0.0781 0.2328 -0.0064 -0.0793 -0.0320 91  GLN B CB  
2423 C  CG  . GLN B 91  ? 0.2077 0.0700 0.2521 0.0121  -0.0850 -0.0075 91  GLN B CG  
2424 C  CD  . GLN B 91  ? 0.3206 0.0440 0.2794 -0.0634 -0.1540 -0.0005 91  GLN B CD  
2425 O  OE1 . GLN B 91  ? 0.2724 0.1696 0.2572 0.0335  -0.1123 -0.0092 91  GLN B OE1 
2426 N  NE2 . GLN B 91  ? 0.2677 0.0393 0.2083 0.0047  -0.0889 -0.0276 91  GLN B NE2 
2427 N  N   . ASP B 92  ? 0.2005 0.1358 0.2198 -0.0189 -0.0593 0.0113  92  ASP B N   
2428 C  CA  . ASP B 92  ? 0.1887 0.1098 0.2531 -0.0036 -0.0479 0.0051  92  ASP B CA  
2429 C  C   . ASP B 92  ? 0.2114 0.0992 0.2257 -0.0176 -0.0455 0.0304  92  ASP B C   
2430 O  O   . ASP B 92  ? 0.2337 0.1150 0.2511 0.0029  -0.0794 0.0074  92  ASP B O   
2431 C  CB  . ASP B 92  ? 0.2148 0.1192 0.2540 -0.0304 -0.0332 -0.0083 92  ASP B CB  
2432 C  CG  . ASP B 92  ? 0.3074 0.1232 0.2490 -0.0054 -0.0813 -0.0172 92  ASP B CG  
2433 O  OD1 . ASP B 92  ? 0.2809 0.1249 0.2261 -0.0112 -0.0761 -0.0068 92  ASP B OD1 
2434 O  OD2 . ASP B 92  ? 0.2976 0.0990 0.2515 -0.0022 -0.0690 0.0029  92  ASP B OD2 
2435 N  N   . LEU B 93  ? 0.2243 0.1105 0.2450 -0.0059 -0.0702 -0.0185 93  LEU B N   
2436 C  CA  . LEU B 93  ? 0.2642 0.0898 0.2402 -0.0245 -0.0810 0.0006  93  LEU B CA  
2437 C  C   . LEU B 93  ? 0.2074 0.1176 0.2322 -0.0402 -0.0565 -0.0107 93  LEU B C   
2438 O  O   . LEU B 93  ? 0.2806 0.0959 0.2532 -0.0338 -0.0726 -0.0299 93  LEU B O   
2439 C  CB  . LEU B 93  ? 0.2261 0.1055 0.2053 -0.0249 -0.0383 -0.0269 93  LEU B CB  
2440 C  CG  . LEU B 93  ? 0.1970 0.1019 0.2312 -0.0089 -0.0555 -0.0023 93  LEU B CG  
2441 C  CD1 . LEU B 93  ? 0.2496 0.1396 0.3885 0.0386  -0.1268 -0.0375 93  LEU B CD1 
2442 C  CD2 . LEU B 93  ? 0.2541 0.1386 0.2602 -0.0556 -0.0398 0.0026  93  LEU B CD2 
2443 N  N   . ALA B 94  ? 0.2807 0.0936 0.2079 -0.0388 -0.0407 -0.0353 94  ALA B N   
2444 C  CA  . ALA B 94  ? 0.2672 0.1374 0.2198 -0.0366 -0.0253 -0.0102 94  ALA B CA  
2445 C  C   . ALA B 94  ? 0.2626 0.1313 0.2219 -0.0555 -0.0372 -0.0071 94  ALA B C   
2446 O  O   . ALA B 94  ? 0.2983 0.2198 0.2210 -0.0452 -0.0438 -0.0197 94  ALA B O   
2447 C  CB  . ALA B 94  ? 0.2356 0.1420 0.2727 -0.0210 -0.0079 0.0163  94  ALA B CB  
2448 N  N   . PHE B 95  ? 0.2438 0.1467 0.2123 -0.0368 -0.0564 0.0026  95  PHE B N   
2449 C  CA  . PHE B 95  ? 0.2590 0.1339 0.2639 -0.0060 -0.0658 -0.0019 95  PHE B CA  
2450 C  C   . PHE B 95  ? 0.2265 0.1718 0.2490 -0.0320 -0.0525 -0.0094 95  PHE B C   
2451 O  O   . PHE B 95  ? 0.2600 0.2035 0.3158 -0.0099 -0.0935 -0.0517 95  PHE B O   
2452 C  CB  . PHE B 95  ? 0.2428 0.1636 0.2344 -0.0007 -0.0895 -0.0027 95  PHE B CB  
2453 C  CG  . PHE B 95  ? 0.2416 0.1760 0.2632 0.0016  -0.0867 -0.0201 95  PHE B CG  
2454 C  CD1 . PHE B 95  ? 0.2575 0.1889 0.2881 0.0541  -0.0683 -0.0191 95  PHE B CD1 
2455 C  CD2 . PHE B 95  ? 0.2508 0.2099 0.2563 -0.0114 -0.0732 -0.0240 95  PHE B CD2 
2456 C  CE1 . PHE B 95  ? 0.2600 0.2357 0.3429 0.0825  -0.0387 0.0402  95  PHE B CE1 
2457 C  CE2 . PHE B 95  ? 0.2474 0.1788 0.3144 -0.0303 -0.0990 -0.0004 95  PHE B CE2 
2458 C  CZ  . PHE B 95  ? 0.2724 0.2291 0.3245 0.0021  -0.0906 0.0191  95  PHE B CZ  
2459 N  N   . TRP B 96  ? 0.2922 0.1448 0.2784 -0.0470 -0.0519 -0.0003 96  TRP B N   
2460 C  CA  . TRP B 96  ? 0.2779 0.1604 0.2632 -0.0544 -0.0347 -0.0251 96  TRP B CA  
2461 C  C   . TRP B 96  ? 0.2820 0.1812 0.2819 -0.0483 -0.0545 -0.0534 96  TRP B C   
2462 O  O   . TRP B 96  ? 0.3187 0.2114 0.3343 -0.0710 -0.0856 -0.0594 96  TRP B O   
2463 C  CB  . TRP B 96  ? 0.2879 0.1324 0.2709 -0.0486 -0.0185 -0.0187 96  TRP B CB  
2464 C  CG  . TRP B 96  ? 0.2894 0.1166 0.2815 -0.1006 0.0202  -0.0236 96  TRP B CG  
2465 C  CD1 . TRP B 96  ? 0.2908 0.0978 0.2860 -0.0796 -0.0025 -0.0146 96  TRP B CD1 
2466 C  CD2 . TRP B 96  ? 0.2875 0.1509 0.2962 -0.0851 0.0071  -0.0453 96  TRP B CD2 
2467 N  NE1 . TRP B 96  ? 0.2914 0.1742 0.2666 -0.0519 -0.0254 -0.0416 96  TRP B NE1 
2468 C  CE2 . TRP B 96  ? 0.3023 0.1693 0.2888 -0.1200 0.0420  -0.0497 96  TRP B CE2 
2469 C  CE3 . TRP B 96  ? 0.2847 0.1903 0.2812 -0.0882 0.0021  -0.0450 96  TRP B CE3 
2470 C  CZ2 . TRP B 96  ? 0.3110 0.2317 0.3541 -0.1104 0.0618  -0.0851 96  TRP B CZ2 
2471 C  CZ3 . TRP B 96  ? 0.2890 0.2916 0.2918 -0.0990 0.0179  -0.0523 96  TRP B CZ3 
2472 C  CH2 . TRP B 96  ? 0.2829 0.2439 0.3625 -0.0570 0.0193  -0.0687 96  TRP B CH2 
2473 N  N   . TYR B 97  ? 0.2872 0.1396 0.2894 -0.0079 -0.0492 -0.0184 97  TYR B N   
2474 C  CA  . TYR B 97  ? 0.2974 0.1120 0.3277 -0.0424 -0.0157 -0.0170 97  TYR B CA  
2475 C  C   . TYR B 97  ? 0.2907 0.1353 0.3087 -0.0596 -0.0177 -0.0389 97  TYR B C   
2476 O  O   . TYR B 97  ? 0.3780 0.1887 0.3404 -0.0108 -0.0165 -0.0747 97  TYR B O   
2477 C  CB  . TYR B 97  ? 0.2405 0.1205 0.3163 -0.0524 0.0183  -0.0249 97  TYR B CB  
2478 C  CG  . TYR B 97  ? 0.2711 0.1032 0.2959 -0.0477 0.0018  -0.0335 97  TYR B CG  
2479 C  CD1 . TYR B 97  ? 0.2569 0.1322 0.2994 -0.0234 -0.0125 -0.0439 97  TYR B CD1 
2480 C  CD2 . TYR B 97  ? 0.4383 0.1163 0.3187 -0.0983 -0.0439 -0.0274 97  TYR B CD2 
2481 C  CE1 . TYR B 97  ? 0.2953 0.1485 0.2859 -0.0144 -0.0096 -0.0406 97  TYR B CE1 
2482 C  CE2 . TYR B 97  ? 0.3962 0.0998 0.3426 -0.0706 -0.0025 -0.0308 97  TYR B CE2 
2483 C  CZ  . TYR B 97  ? 0.3158 0.1657 0.3278 -0.0740 -0.0001 -0.0252 97  TYR B CZ  
2484 O  OH  . TYR B 97  ? 0.3829 0.1994 0.3571 -0.0676 0.0092  0.0065  97  TYR B OH  
2485 N  N   . GLY B 98  ? 0.2574 0.1353 0.2750 -0.0289 -0.0871 -0.0008 98  GLY B N   
2486 C  CA  . GLY B 98  ? 0.2743 0.1644 0.2661 -0.0471 -0.0958 -0.0055 98  GLY B CA  
2487 C  C   . GLY B 98  ? 0.2781 0.1675 0.2392 -0.0332 -0.0840 0.0040  98  GLY B C   
2488 O  O   . GLY B 98  ? 0.2607 0.1675 0.2578 -0.0437 -0.0819 0.0194  98  GLY B O   
2489 N  N   . PRO B 99  ? 0.3134 0.1862 0.2410 -0.0366 -0.0744 0.0060  99  PRO B N   
2490 C  CA  . PRO B 99  ? 0.3182 0.1982 0.2522 -0.0312 -0.0550 0.0269  99  PRO B CA  
2491 C  C   . PRO B 99  ? 0.3080 0.1982 0.2975 -0.0378 -0.0999 -0.0038 99  PRO B C   
2492 O  O   . PRO B 99  ? 0.3144 0.2297 0.3742 -0.0511 -0.1240 0.0030  99  PRO B O   
2493 C  CB  . PRO B 99  ? 0.3584 0.2740 0.2682 -0.0390 -0.0608 0.0615  99  PRO B CB  
2494 C  CG  . PRO B 99  ? 0.3875 0.3602 0.2488 -0.0578 -0.0742 0.0425  99  PRO B CG  
2495 C  CD  . PRO B 99  ? 0.3677 0.2908 0.2262 -0.0843 -0.0971 0.0167  99  PRO B CD  
2496 N  N   . ARG B 100 ? 0.3070 0.2067 0.2653 -0.0338 -0.0627 -0.0448 100 ARG B N   
2497 C  CA  . ARG B 100 ? 0.3748 0.2126 0.2633 -0.0043 -0.0704 -0.0221 100 ARG B CA  
2498 C  C   . ARG B 100 ? 0.3804 0.1429 0.2719 -0.0776 -0.0507 -0.0488 100 ARG B C   
2499 O  O   . ARG B 100 ? 0.3573 0.1462 0.3437 -0.0632 -0.0275 -0.0380 100 ARG B O   
2500 C  CB  . ARG B 100 ? 0.5041 0.2442 0.2689 0.0482  -0.0426 -0.0458 100 ARG B CB  
2501 C  CG  . ARG B 100 ? 0.5595 0.2258 0.2644 0.0938  -0.0890 -0.0197 100 ARG B CG  
2502 C  CD  . ARG B 100 ? 0.7111 0.5486 0.2930 0.0319  -0.0115 -0.1676 100 ARG B CD  
2503 N  NE  . ARG B 100 ? 0.8824 0.7071 0.3789 -0.0887 0.0926  -0.1854 100 ARG B NE  
2504 C  CZ  . ARG B 100 ? 0.9718 0.7382 0.5871 -0.2067 0.1240  -0.2076 100 ARG B CZ  
2505 N  NH1 . ARG B 100 ? 1.0561 1.0438 0.8423 -0.4587 -0.1024 -0.0661 100 ARG B NH1 
2506 N  NH2 . ARG B 100 ? 1.0286 0.5755 0.7107 -0.0494 0.3428  -0.2376 100 ARG B NH2 
2507 N  N   . TRP B 101 ? 0.3394 0.1325 0.2940 -0.0570 -0.0158 -0.0147 101 TRP B N   
2508 C  CA  . TRP B 101 ? 0.2643 0.0982 0.3013 -0.0402 -0.0012 -0.0265 101 TRP B CA  
2509 C  C   . TRP B 101 ? 0.2750 0.1080 0.3048 -0.0378 -0.0134 -0.0304 101 TRP B C   
2510 O  O   . TRP B 101 ? 0.2949 0.1346 0.3133 -0.0518 -0.0486 0.0006  101 TRP B O   
2511 C  CB  . TRP B 101 ? 0.2944 0.0843 0.2859 -0.0336 -0.0608 -0.0351 101 TRP B CB  
2512 C  CG  . TRP B 101 ? 0.2560 0.1241 0.2349 -0.0403 -0.0490 -0.0063 101 TRP B CG  
2513 C  CD1 . TRP B 101 ? 0.2941 0.1412 0.2743 -0.0667 -0.1004 0.0217  101 TRP B CD1 
2514 C  CD2 . TRP B 101 ? 0.2159 0.1271 0.2490 -0.0121 -0.0311 0.0063  101 TRP B CD2 
2515 N  NE1 . TRP B 101 ? 0.2965 0.1186 0.2741 -0.0524 -0.0939 0.0065  101 TRP B NE1 
2516 C  CE2 . TRP B 101 ? 0.2504 0.0983 0.2231 -0.0155 -0.0517 -0.0180 101 TRP B CE2 
2517 C  CE3 . TRP B 101 ? 0.3012 0.0976 0.2959 -0.0343 -0.0923 0.0068  101 TRP B CE3 
2518 C  CZ2 . TRP B 101 ? 0.2461 0.1496 0.2623 -0.0314 -0.0609 0.0147  101 TRP B CZ2 
2519 C  CZ3 . TRP B 101 ? 0.3214 0.1168 0.2761 -0.0266 -0.1003 0.0000  101 TRP B CZ3 
2520 C  CH2 . TRP B 101 ? 0.2594 0.1328 0.2630 -0.0172 -0.0808 -0.0002 101 TRP B CH2 
2521 N  N   . GLN B 102 ? 0.2717 0.1470 0.2999 -0.0446 -0.0427 0.0008  102 GLN B N   
2522 C  CA  . GLN B 102 ? 0.2982 0.2073 0.3794 -0.0379 -0.0795 0.0312  102 GLN B CA  
2523 C  C   . GLN B 102 ? 0.2885 0.2576 0.4351 0.0581  -0.0255 -0.0111 102 GLN B C   
2524 O  O   . GLN B 102 ? 0.3939 0.2574 0.4390 0.0825  -0.0946 -0.0442 102 GLN B O   
2525 C  CB  . GLN B 102 ? 0.2531 0.2931 0.4114 -0.0049 -0.0198 0.1012  102 GLN B CB  
2526 C  CG  . GLN B 102 ? 0.2570 0.4216 0.4694 0.1003  -0.0854 -0.0469 102 GLN B CG  
2527 C  CD  . GLN B 102 ? 0.3429 0.3528 0.5221 0.0660  -0.1251 -0.0979 102 GLN B CD  
2528 O  OE1 . GLN B 102 ? 0.4487 0.4245 0.4889 -0.0080 -0.1737 -0.1432 102 GLN B OE1 
2529 N  NE2 . GLN B 102 ? 0.5187 0.4474 0.5210 -0.0763 -0.1593 -0.0655 102 GLN B NE2 
2530 N  N   . GLU B 103 ? 0.3421 0.1387 0.4277 0.0375  -0.0247 0.0122  103 GLU B N   
2531 C  CA  . GLU B 103 ? 0.3857 0.1133 0.4598 0.0223  -0.0068 0.0275  103 GLU B CA  
2532 C  C   . GLU B 103 ? 0.4093 0.1427 0.4675 0.0050  -0.0127 0.0536  103 GLU B C   
2533 O  O   . GLU B 103 ? 0.3759 0.1423 0.7762 -0.0052 0.0178  0.0467  103 GLU B O   
2534 C  CB  . GLU B 103 ? 0.5103 0.1722 0.4386 0.0066  0.0706  -0.0122 103 GLU B CB  
2535 C  CG  . GLU B 103 ? 0.5992 0.3265 0.5329 -0.0743 0.0487  0.1096  103 GLU B CG  
2536 C  CD  . GLU B 103 ? 0.7799 0.4258 0.4791 -0.1127 0.0667  0.0859  103 GLU B CD  
2537 O  OE1 . GLU B 103 ? 1.1967 0.3429 0.4523 0.0731  0.0954  -0.0729 103 GLU B OE1 
2538 O  OE2 . GLU B 103 ? 0.6735 0.4204 0.4515 -0.0477 0.0582  0.1103  103 GLU B OE2 
2539 N  N   . VAL B 104 ? 0.3841 0.1512 0.2855 -0.0231 -0.0576 0.0191  104 VAL B N   
2540 C  CA  . VAL B 104 ? 0.3977 0.1935 0.2500 -0.0569 -0.0875 -0.0087 104 VAL B CA  
2541 C  C   . VAL B 104 ? 0.3763 0.1187 0.2509 -0.0523 -0.0924 0.0065  104 VAL B C   
2542 O  O   . VAL B 104 ? 0.3172 0.1540 0.3030 -0.0572 -0.0651 -0.0418 104 VAL B O   
2543 C  CB  . VAL B 104 ? 0.4100 0.2498 0.2273 -0.0427 -0.0863 -0.0055 104 VAL B CB  
2544 C  CG1 . VAL B 104 ? 0.6510 0.5456 0.2150 0.0333  -0.0894 -0.0022 104 VAL B CG1 
2545 C  CG2 . VAL B 104 ? 0.3585 0.2181 0.3506 -0.0610 -0.0668 0.0217  104 VAL B CG2 
2546 N  N   . ILE B 105 ? 0.2640 0.1298 0.2629 -0.0317 -0.0492 -0.0280 105 ILE B N   
2547 C  CA  . ILE B 105 ? 0.3079 0.1080 0.2646 -0.0298 -0.0537 -0.0327 105 ILE B CA  
2548 C  C   . ILE B 105 ? 0.3189 0.0971 0.2717 -0.0287 -0.0416 -0.0394 105 ILE B C   
2549 O  O   . ILE B 105 ? 0.3408 0.1191 0.2453 -0.0068 -0.0217 -0.0329 105 ILE B O   
2550 C  CB  . ILE B 105 ? 0.3215 0.0815 0.2655 0.0035  -0.1058 -0.0154 105 ILE B CB  
2551 C  CG1 . ILE B 105 ? 0.3197 0.1124 0.2650 0.0148  -0.1356 -0.0266 105 ILE B CG1 
2552 C  CG2 . ILE B 105 ? 0.3353 0.1131 0.2927 0.0472  -0.0436 -0.0211 105 ILE B CG2 
2553 C  CD1 . ILE B 105 ? 0.3328 0.1218 0.2721 -0.0018 -0.1115 -0.0435 105 ILE B CD1 
2554 N  N   . PRO B 106 ? 0.2787 0.1341 0.2372 -0.0113 -0.0751 -0.0119 106 PRO B N   
2555 C  CA  . PRO B 106 ? 0.2860 0.1300 0.2822 -0.0176 -0.0763 -0.0011 106 PRO B CA  
2556 C  C   . PRO B 106 ? 0.3229 0.1010 0.2558 -0.0227 -0.0845 0.0093  106 PRO B C   
2557 O  O   . PRO B 106 ? 0.3271 0.1152 0.3057 -0.0448 -0.0741 -0.0126 106 PRO B O   
2558 C  CB  . PRO B 106 ? 0.3186 0.1955 0.2664 -0.0412 -0.0585 0.0140  106 PRO B CB  
2559 C  CG  . PRO B 106 ? 0.2827 0.2191 0.3268 -0.0079 -0.0355 0.0369  106 PRO B CG  
2560 C  CD  . PRO B 106 ? 0.2653 0.1961 0.2309 0.0085  -0.1010 -0.0111 106 PRO B CD  
2561 N  N   . TYR B 107 ? 0.3107 0.1173 0.2943 -0.0156 -0.0907 0.0175  107 TYR B N   
2562 C  CA  . TYR B 107 ? 0.2971 0.0942 0.2175 -0.0041 -0.0644 -0.0447 107 TYR B CA  
2563 C  C   . TYR B 107 ? 0.2572 0.1065 0.2617 0.0295  -0.0579 -0.0173 107 TYR B C   
2564 O  O   . TYR B 107 ? 0.3450 0.0964 0.3526 0.0269  0.0020  -0.0223 107 TYR B O   
2565 C  CB  . TYR B 107 ? 0.2968 0.0989 0.2733 0.0018  -0.0558 -0.0328 107 TYR B CB  
2566 C  CG  . TYR B 107 ? 0.2921 0.0785 0.2795 -0.0021 -0.0540 -0.0226 107 TYR B CG  
2567 C  CD1 . TYR B 107 ? 0.3017 0.1102 0.3156 0.0030  -0.0845 -0.0622 107 TYR B CD1 
2568 C  CD2 . TYR B 107 ? 0.2748 0.1327 0.2997 0.0029  -0.0352 -0.0216 107 TYR B CD2 
2569 C  CE1 . TYR B 107 ? 0.3269 0.1082 0.3338 0.0139  -0.1062 -0.0561 107 TYR B CE1 
2570 C  CE2 . TYR B 107 ? 0.2843 0.1263 0.3212 0.0053  -0.0481 -0.0055 107 TYR B CE2 
2571 C  CZ  . TYR B 107 ? 0.2646 0.1313 0.3096 -0.0262 -0.0446 -0.0060 107 TYR B CZ  
2572 O  OH  . TYR B 107 ? 0.2419 0.1519 0.3499 -0.0428 -0.0480 -0.0186 107 TYR B OH  
2573 N  N   . THR B 108 ? 0.3290 0.1280 0.2408 -0.0418 -0.0504 -0.0393 108 THR B N   
2574 C  CA  . THR B 108 ? 0.2555 0.1100 0.3137 -0.0376 -0.0586 -0.0371 108 THR B CA  
2575 C  C   . THR B 108 ? 0.2528 0.0593 0.3025 -0.0040 -0.0391 -0.0625 108 THR B C   
2576 O  O   . THR B 108 ? 0.2880 0.1001 0.2823 -0.0437 -0.0586 -0.0315 108 THR B O   
2577 C  CB  . THR B 108 ? 0.2516 0.1120 0.3987 -0.0116 -0.0522 -0.0279 108 THR B CB  
2578 O  OG1 . THR B 108 ? 0.3328 0.1140 0.3764 -0.0042 0.0068  -0.0129 108 THR B OG1 
2579 C  CG2 . THR B 108 ? 0.2672 0.0983 0.4506 -0.0259 -0.0617 0.0227  108 THR B CG2 
2580 N  N   . PRO B 109 ? 0.3086 0.0704 0.2903 -0.0250 -0.0186 -0.0500 109 PRO B N   
2581 C  CA  . PRO B 109 ? 0.2967 0.0890 0.3106 -0.0366 -0.0176 -0.0140 109 PRO B CA  
2582 C  C   . PRO B 109 ? 0.2774 0.0729 0.3104 0.0119  -0.0567 -0.0024 109 PRO B C   
2583 O  O   . PRO B 109 ? 0.2721 0.0817 0.3312 -0.0085 -0.0551 0.0017  109 PRO B O   
2584 C  CB  . PRO B 109 ? 0.3504 0.1153 0.3094 -0.0729 -0.0355 -0.0075 109 PRO B CB  
2585 C  CG  . PRO B 109 ? 0.3443 0.0707 0.3114 -0.0207 -0.0358 -0.0195 109 PRO B CG  
2586 C  CD  . PRO B 109 ? 0.3156 0.0578 0.3453 -0.0266 -0.0421 -0.0306 109 PRO B CD  
2587 N  N   . ALA B 110 ? 0.2753 0.0768 0.3352 0.0109  -0.0451 -0.0143 110 ALA B N   
2588 C  CA  . ALA B 110 ? 0.2729 0.0761 0.3218 -0.0185 -0.0402 -0.0079 110 ALA B CA  
2589 C  C   . ALA B 110 ? 0.2868 0.0890 0.3130 -0.0343 -0.0536 0.0079  110 ALA B C   
2590 O  O   . ALA B 110 ? 0.2676 0.0917 0.3371 -0.0271 -0.0832 0.0093  110 ALA B O   
2591 C  CB  . ALA B 110 ? 0.3032 0.1118 0.3071 -0.0207 -0.0042 0.0301  110 ALA B CB  
2592 N  N   . MET B 111 ? 0.2783 0.0986 0.3078 -0.0155 -0.0353 0.0054  111 MET B N   
2593 C  CA  . MET B 111 ? 0.2655 0.0827 0.2609 -0.0082 -0.0458 -0.0074 111 MET B CA  
2594 C  C   . MET B 111 ? 0.2692 0.0798 0.2549 -0.0147 -0.0675 -0.0392 111 MET B C   
2595 O  O   . MET B 111 ? 0.3016 0.1093 0.2460 -0.0235 -0.0840 -0.0456 111 MET B O   
2596 C  CB  . MET B 111 ? 0.2594 0.1515 0.2776 -0.0632 -0.0762 0.0165  111 MET B CB  
2597 C  CG  . MET B 111 ? 0.2724 0.1056 0.3164 -0.0522 -0.0957 0.0148  111 MET B CG  
2598 S  SD  . MET B 111 ? 0.2689 0.1158 0.2889 -0.0090 -0.0612 -0.0142 111 MET B SD  
2599 C  CE  . MET B 111 ? 0.2750 0.1882 0.3416 0.0054  -0.0970 -0.0071 111 MET B CE  
2600 N  N   . GLN B 112 ? 0.2534 0.0658 0.3497 -0.0104 -0.0787 -0.0517 112 GLN B N   
2601 C  CA  . GLN B 112 ? 0.2456 0.1062 0.2826 -0.0302 -0.0310 -0.0285 112 GLN B CA  
2602 C  C   . GLN B 112 ? 0.2637 0.0802 0.3155 0.0194  -0.0490 -0.0122 112 GLN B C   
2603 O  O   . GLN B 112 ? 0.2847 0.1057 0.3423 0.0022  -0.0808 -0.0183 112 GLN B O   
2604 C  CB  . GLN B 112 ? 0.2407 0.0913 0.3541 -0.0295 -0.0457 -0.0572 112 GLN B CB  
2605 C  CG  . GLN B 112 ? 0.2549 0.0686 0.4609 -0.0052 -0.0756 -0.0786 112 GLN B CG  
2606 C  CD  . GLN B 112 ? 0.2582 0.0771 0.4267 0.0113  -0.0921 -0.0706 112 GLN B CD  
2607 O  OE1 . GLN B 112 ? 0.4409 0.1900 0.4461 -0.0279 0.0167  -0.0925 112 GLN B OE1 
2608 N  NE2 . GLN B 112 ? 0.3418 0.0699 0.4552 -0.0180 -0.0850 -0.0867 112 GLN B NE2 
2609 N  N   . ARG B 113 ? 0.3331 0.0767 0.3073 -0.0060 -0.0523 -0.0055 113 ARG B N   
2610 C  CA  . ARG B 113 ? 0.2962 0.1076 0.2832 0.0199  -0.0297 -0.0381 113 ARG B CA  
2611 C  C   . ARG B 113 ? 0.2217 0.0996 0.3151 0.0093  -0.0412 -0.0203 113 ARG B C   
2612 O  O   . ARG B 113 ? 0.2580 0.1218 0.3139 0.0244  -0.0714 -0.0110 113 ARG B O   
2613 C  CB  . ARG B 113 ? 0.5279 0.1121 0.3581 -0.0854 -0.0119 0.0229  113 ARG B CB  
2614 C  CG  . ARG B 113 ? 0.7764 0.1149 0.6956 -0.0550 0.0797  0.0242  113 ARG B CG  
2615 C  CD  . ARG B 113 ? 0.9207 0.1647 0.8905 -0.1245 0.0446  0.2362  113 ARG B CD  
2616 N  NE  . ARG B 113 ? 1.0206 0.3738 1.0116 -0.2870 0.0057  0.2057  113 ARG B NE  
2617 C  CZ  . ARG B 113 ? 1.0831 0.3695 1.0958 -0.2291 -0.1080 0.2286  113 ARG B CZ  
2618 N  NH1 . ARG B 113 ? 1.3651 0.2943 1.2804 -0.2418 -0.4950 0.3660  113 ARG B NH1 
2619 N  NH2 . ARG B 113 ? 1.2673 0.3823 1.1012 -0.1141 -0.1946 0.4284  113 ARG B NH2 
2620 N  N   . TYR B 114 ? 0.2699 0.0780 0.2864 0.0085  -0.0818 -0.0115 114 TYR B N   
2621 C  CA  . TYR B 114 ? 0.2554 0.0830 0.2603 0.0073  -0.0992 -0.0077 114 TYR B CA  
2622 C  C   . TYR B 114 ? 0.2677 0.0591 0.2879 0.0249  -0.0741 0.0003  114 TYR B C   
2623 O  O   . TYR B 114 ? 0.2300 0.1181 0.2454 0.0052  -0.0342 0.0122  114 TYR B O   
2624 C  CB  . TYR B 114 ? 0.2688 0.0927 0.3299 0.0199  -0.0590 -0.0146 114 TYR B CB  
2625 C  CG  . TYR B 114 ? 0.2531 0.0900 0.2966 -0.0046 -0.0358 -0.0015 114 TYR B CG  
2626 C  CD1 . TYR B 114 ? 0.2593 0.1082 0.3402 -0.0163 -0.0377 -0.0184 114 TYR B CD1 
2627 C  CD2 . TYR B 114 ? 0.2552 0.1378 0.2860 0.0041  -0.0259 -0.0099 114 TYR B CD2 
2628 C  CE1 . TYR B 114 ? 0.2653 0.0844 0.3197 -0.0134 -0.0627 0.0023  114 TYR B CE1 
2629 C  CE2 . TYR B 114 ? 0.2475 0.1873 0.2490 0.0141  -0.0303 -0.0217 114 TYR B CE2 
2630 C  CZ  . TYR B 114 ? 0.2930 0.1301 0.2635 0.0489  -0.0935 0.0041  114 TYR B CZ  
2631 O  OH  . TYR B 114 ? 0.3207 0.0948 0.2670 0.0013  -0.0340 0.0219  114 TYR B OH  
2632 N  N   . VAL B 115 ? 0.2612 0.0817 0.2803 0.0174  -0.0819 -0.0035 115 VAL B N   
2633 C  CA  . VAL B 115 ? 0.2509 0.0895 0.2737 0.0005  -0.0804 -0.0402 115 VAL B CA  
2634 C  C   . VAL B 115 ? 0.2572 0.0993 0.3330 -0.0072 -0.0885 0.0203  115 VAL B C   
2635 O  O   . VAL B 115 ? 0.2206 0.1242 0.3023 0.0099  -0.0288 -0.0548 115 VAL B O   
2636 C  CB  . VAL B 115 ? 0.2137 0.0795 0.2755 -0.0235 -0.0794 -0.0651 115 VAL B CB  
2637 C  CG1 . VAL B 115 ? 0.2741 0.0773 0.3319 0.0041  -0.0143 -0.0230 115 VAL B CG1 
2638 C  CG2 . VAL B 115 ? 0.2458 0.1239 0.3228 -0.0063 -0.0870 0.0049  115 VAL B CG2 
2639 N  N   . LYS B 116 ? 0.2464 0.1018 0.3367 0.0106  -0.0296 -0.0004 116 LYS B N   
2640 C  CA  . LYS B 116 ? 0.2217 0.0947 0.3606 0.0050  -0.0022 0.0078  116 LYS B CA  
2641 C  C   . LYS B 116 ? 0.2872 0.1084 0.3685 0.0567  -0.0481 0.0235  116 LYS B C   
2642 O  O   . LYS B 116 ? 0.2909 0.1357 0.3659 0.0340  -0.0354 -0.0373 116 LYS B O   
2643 C  CB  . LYS B 116 ? 0.2774 0.0982 0.5778 0.0004  -0.1277 0.0101  116 LYS B CB  
2644 C  CG  . LYS B 116 ? 0.4679 0.1718 0.7613 0.1625  -0.1855 -0.0814 116 LYS B CG  
2645 C  CD  . LYS B 116 ? 0.6366 0.1532 1.0127 0.1781  -0.2794 -0.1336 116 LYS B CD  
2646 C  CE  . LYS B 116 ? 0.7401 0.1748 1.1848 0.2689  -0.3261 -0.1659 116 LYS B CE  
2647 N  NZ  . LYS B 116 ? 0.7020 0.4838 1.5444 0.2648  -0.2338 -0.4514 116 LYS B NZ  
2648 N  N   . ARG B 117 ? 0.2604 0.0901 0.3317 0.0182  -0.0842 -0.0068 117 ARG B N   
2649 C  CA  . ARG B 117 ? 0.2666 0.0947 0.3329 -0.0001 -0.1048 0.0308  117 ARG B CA  
2650 C  C   . ARG B 117 ? 0.2922 0.1163 0.2990 -0.0286 -0.1122 0.0388  117 ARG B C   
2651 O  O   . ARG B 117 ? 0.2720 0.1061 0.3243 0.0093  -0.1058 -0.0141 117 ARG B O   
2652 C  CB  . ARG B 117 ? 0.2808 0.0785 0.3155 0.0018  -0.1018 0.0374  117 ARG B CB  
2653 C  CG  . ARG B 117 ? 0.3199 0.0875 0.3123 -0.0286 -0.1208 0.0732  117 ARG B CG  
2654 C  CD  . ARG B 117 ? 0.3154 0.1124 0.3069 -0.0048 -0.1185 0.0327  117 ARG B CD  
2655 N  NE  . ARG B 117 ? 0.3787 0.0895 0.3041 0.0809  -0.1331 0.0132  117 ARG B NE  
2656 C  CZ  . ARG B 117 ? 0.3974 0.0745 0.2504 0.0772  -0.1361 0.0556  117 ARG B CZ  
2657 N  NH1 . ARG B 117 ? 0.4834 0.1567 0.2713 0.0142  -0.1570 0.0330  117 ARG B NH1 
2658 N  NH2 . ARG B 117 ? 0.3452 0.1237 0.3956 0.0408  -0.1185 -0.0288 117 ARG B NH2 
2659 N  N   . LEU B 118 ? 0.3076 0.0848 0.2762 -0.0199 -0.1084 0.0094  118 LEU B N   
2660 C  CA  . LEU B 118 ? 0.2955 0.0975 0.2495 -0.0370 -0.0971 0.0025  118 LEU B CA  
2661 C  C   . LEU B 118 ? 0.2956 0.1325 0.3070 -0.0260 -0.0870 -0.0049 118 LEU B C   
2662 O  O   . LEU B 118 ? 0.2757 0.1112 0.3434 0.0028  -0.1033 -0.0151 118 LEU B O   
2663 C  CB  . LEU B 118 ? 0.2900 0.0922 0.2083 -0.0262 -0.0372 0.0228  118 LEU B CB  
2664 C  CG  . LEU B 118 ? 0.3030 0.1085 0.1764 -0.0189 -0.0380 0.0124  118 LEU B CG  
2665 C  CD1 . LEU B 118 ? 0.3072 0.1120 0.2357 -0.0121 -0.0616 0.0229  118 LEU B CD1 
2666 C  CD2 . LEU B 118 ? 0.3182 0.1740 0.2684 -0.0056 -0.0621 -0.0614 118 LEU B CD2 
2667 N  N   . HIS B 119 ? 0.2784 0.0983 0.3302 -0.0363 -0.0736 -0.0103 119 HIS B N   
2668 C  CA  . HIS B 119 ? 0.2734 0.1097 0.3416 -0.0283 -0.0831 -0.0069 119 HIS B CA  
2669 C  C   . HIS B 119 ? 0.2927 0.1607 0.3555 -0.0174 -0.0963 0.0053  119 HIS B C   
2670 O  O   . HIS B 119 ? 0.2551 0.1727 0.3471 0.0197  -0.0592 -0.0296 119 HIS B O   
2671 C  CB  . HIS B 119 ? 0.2419 0.1211 0.3533 -0.0010 -0.0862 -0.0236 119 HIS B CB  
2672 C  CG  . HIS B 119 ? 0.2967 0.1326 0.3424 -0.0040 -0.0907 -0.0170 119 HIS B CG  
2673 N  ND1 . HIS B 119 ? 0.2776 0.1221 0.4006 0.0089  -0.1175 -0.0106 119 HIS B ND1 
2674 C  CD2 . HIS B 119 ? 0.2503 0.1393 0.3423 -0.0039 -0.0728 -0.0036 119 HIS B CD2 
2675 C  CE1 . HIS B 119 ? 0.2447 0.1213 0.3335 0.0156  -0.0763 -0.0329 119 HIS B CE1 
2676 N  NE2 . HIS B 119 ? 0.2648 0.1233 0.3187 -0.0028 -0.0643 -0.0249 119 HIS B NE2 
2677 N  N   . GLU B 120 ? 0.3202 0.1412 0.3090 0.0003  -0.1040 -0.0093 120 GLU B N   
2678 C  CA  . GLU B 120 ? 0.2622 0.1561 0.3478 0.0172  -0.0936 -0.0083 120 GLU B CA  
2679 C  C   . GLU B 120 ? 0.2823 0.1661 0.3348 0.0339  -0.1230 0.0002  120 GLU B C   
2680 O  O   . GLU B 120 ? 0.2847 0.1293 0.3800 0.0078  -0.1359 0.0241  120 GLU B O   
2681 C  CB  . GLU B 120 ? 0.3345 0.1380 0.4140 0.0250  -0.0883 0.0246  120 GLU B CB  
2682 C  CG  . GLU B 120 ? 0.4775 0.1032 0.5368 0.0459  -0.1441 0.0079  120 GLU B CG  
2683 C  CD  . GLU B 120 ? 0.5833 0.0902 0.5211 0.0068  -0.1372 0.0042  120 GLU B CD  
2684 O  OE1 . GLU B 120 ? 0.4997 0.1793 0.5847 -0.0503 -0.1055 -0.0652 120 GLU B OE1 
2685 O  OE2 . GLU B 120 ? 0.8162 0.1560 0.5229 -0.0884 -0.1131 -0.0340 120 GLU B OE2 
2686 N  N   . VAL B 121 ? 0.2880 0.1559 0.3030 0.0228  -0.1135 0.0027  121 VAL B N   
2687 C  CA  . VAL B 121 ? 0.3532 0.1557 0.2856 0.0136  -0.1080 0.0149  121 VAL B CA  
2688 C  C   . VAL B 121 ? 0.3107 0.1473 0.3139 0.0259  -0.1092 -0.0084 121 VAL B C   
2689 O  O   . VAL B 121 ? 0.3532 0.1618 0.3698 0.0242  -0.1645 0.0093  121 VAL B O   
2690 C  CB  . VAL B 121 ? 0.3448 0.1093 0.2944 -0.0160 -0.0967 0.0064  121 VAL B CB  
2691 C  CG1 . VAL B 121 ? 0.3565 0.0970 0.3562 -0.0465 -0.0765 -0.0018 121 VAL B CG1 
2692 C  CG2 . VAL B 121 ? 0.3335 0.0787 0.3945 -0.0197 -0.1052 0.0103  121 VAL B CG2 
2693 N  N   . GLY B 122 ? 0.2956 0.1259 0.2912 -0.0340 -0.1122 -0.0252 122 GLY B N   
2694 C  CA  . GLY B 122 ? 0.2540 0.1426 0.3555 -0.0337 -0.1249 -0.0092 122 GLY B CA  
2695 C  C   . GLY B 122 ? 0.2672 0.1537 0.3904 -0.0031 -0.1228 0.0349  122 GLY B C   
2696 O  O   . GLY B 122 ? 0.2497 0.1750 0.3560 -0.0122 -0.0448 -0.0091 122 GLY B O   
2697 N  N   . ARG B 123 ? 0.2491 0.1767 0.4688 -0.0061 -0.1258 -0.0115 123 ARG B N   
2698 C  CA  . ARG B 123 ? 0.2547 0.2177 0.4434 -0.0148 -0.1119 -0.0417 123 ARG B CA  
2699 C  C   . ARG B 123 ? 0.2343 0.1769 0.4789 0.0101  -0.1035 -0.0422 123 ARG B C   
2700 O  O   . ARG B 123 ? 0.2372 0.2204 0.5919 -0.0008 -0.1248 0.0191  123 ARG B O   
2701 C  CB  . ARG B 123 ? 0.2963 0.2861 0.4616 -0.0917 -0.0616 -0.0852 123 ARG B CB  
2702 C  CG  . ARG B 123 ? 0.4463 0.4783 0.4433 -0.1399 -0.1152 -0.0514 123 ARG B CG  
2703 C  CD  . ARG B 123 ? 0.6422 0.5115 0.4580 -0.1756 -0.0997 -0.0716 123 ARG B CD  
2704 N  NE  . ARG B 123 ? 0.8143 0.6266 0.4426 -0.1413 -0.1424 -0.0802 123 ARG B NE  
2705 C  CZ  . ARG B 123 ? 0.7800 0.5544 0.3422 -0.0915 -0.0503 -0.1319 123 ARG B CZ  
2706 N  NH1 . ARG B 123 ? 0.5807 0.6052 0.8233 -0.1283 -0.1282 -0.0650 123 ARG B NH1 
2707 N  NH2 . ARG B 123 ? 0.7318 0.8587 0.3980 -0.1650 -0.0630 0.0259  123 ARG B NH2 
2708 N  N   . THR B 124 ? 0.2588 0.1879 0.4937 0.0173  -0.1016 -0.0125 124 THR B N   
2709 C  CA  . THR B 124 ? 0.3064 0.1619 0.5392 0.0423  -0.1208 -0.0098 124 THR B CA  
2710 C  C   . THR B 124 ? 0.3164 0.1540 0.5074 -0.0029 -0.0982 0.0453  124 THR B C   
2711 O  O   . THR B 124 ? 0.2988 0.1947 0.5306 0.0152  -0.1024 0.0373  124 THR B O   
2712 C  CB  . THR B 124 ? 0.3446 0.1797 0.5856 -0.0119 -0.1424 -0.0028 124 THR B CB  
2713 O  OG1 . THR B 124 ? 0.3626 0.1504 0.4766 0.0325  -0.1010 0.0267  124 THR B OG1 
2714 C  CG2 . THR B 124 ? 0.2923 0.2171 0.6905 0.0467  -0.0315 -0.1099 124 THR B CG2 
2715 N  N   . GLU B 125 ? 0.3175 0.1320 0.4448 -0.0071 -0.1475 0.0005  125 GLU B N   
2716 C  CA  . GLU B 125 ? 0.3059 0.1183 0.4211 -0.0378 -0.1560 0.0273  125 GLU B CA  
2717 C  C   . GLU B 125 ? 0.3144 0.1324 0.4166 -0.0236 -0.1345 0.0057  125 GLU B C   
2718 O  O   . GLU B 125 ? 0.3417 0.1562 0.3056 -0.0173 -0.1248 0.0052  125 GLU B O   
2719 C  CB  . GLU B 125 ? 0.3541 0.1668 0.4931 -0.0737 -0.1287 0.0503  125 GLU B CB  
2720 C  CG  . GLU B 125 ? 0.4129 0.1764 0.4548 -0.1124 -0.1643 0.0891  125 GLU B CG  
2721 C  CD  . GLU B 125 ? 0.3219 0.1035 0.4576 -0.0178 -0.2192 0.0990  125 GLU B CD  
2722 O  OE1 . GLU B 125 ? 0.4754 0.1438 0.4579 -0.0068 -0.2358 0.1020  125 GLU B OE1 
2723 O  OE2 . GLU B 125 ? 0.4958 0.1456 0.5086 -0.1042 -0.2786 0.1197  125 GLU B OE2 
2724 N  N   . PRO B 126 ? 0.2747 0.1277 0.4432 0.0091  -0.1402 0.0367  126 PRO B N   
2725 C  CA  . PRO B 126 ? 0.2934 0.1209 0.4431 0.0272  -0.1380 -0.0064 126 PRO B CA  
2726 C  C   . PRO B 126 ? 0.3008 0.1525 0.4204 0.0152  -0.1474 0.0053  126 PRO B C   
2727 O  O   . PRO B 126 ? 0.3044 0.1191 0.3868 0.0072  -0.1044 0.0199  126 PRO B O   
2728 C  CB  . PRO B 126 ? 0.3565 0.1187 0.4350 0.0427  -0.1217 0.0382  126 PRO B CB  
2729 C  CG  . PRO B 126 ? 0.3119 0.1024 0.5105 0.0067  -0.1034 0.0361  126 PRO B CG  
2730 C  CD  . PRO B 126 ? 0.2448 0.1034 0.5263 -0.0017 -0.1638 0.0209  126 PRO B CD  
2731 N  N   . GLU B 127 ? 0.3303 0.1141 0.4254 -0.0203 -0.1315 0.0546  127 GLU B N   
2732 C  CA  . GLU B 127 ? 0.3637 0.1587 0.4155 -0.0386 -0.1371 0.0501  127 GLU B CA  
2733 C  C   . GLU B 127 ? 0.3665 0.0661 0.4377 -0.0195 -0.1069 0.0141  127 GLU B C   
2734 O  O   . GLU B 127 ? 0.3876 0.1443 0.3920 0.0057  -0.1507 -0.0203 127 GLU B O   
2735 C  CB  . GLU B 127 ? 0.4101 0.1832 0.4253 0.0056  -0.1558 0.0257  127 GLU B CB  
2736 C  CG  . GLU B 127 ? 0.5239 0.1827 0.3861 0.0464  -0.1589 0.0126  127 GLU B CG  
2737 C  CD  . GLU B 127 ? 0.5732 0.2077 0.4154 0.0590  -0.1099 0.0242  127 GLU B CD  
2738 O  OE1 . GLU B 127 ? 0.3825 0.2270 0.4581 0.0525  -0.1225 0.0614  127 GLU B OE1 
2739 O  OE2 . GLU B 127 ? 0.3354 0.1920 0.4606 0.0087  -0.1794 0.0370  127 GLU B OE2 
2740 N  N   . LEU B 128 ? 0.3279 0.0840 0.3965 0.0030  -0.0954 0.0059  128 LEU B N   
2741 C  CA  . LEU B 128 ? 0.3330 0.0707 0.3597 -0.0022 -0.0822 0.0123  128 LEU B CA  
2742 C  C   . LEU B 128 ? 0.3211 0.0712 0.3713 -0.0246 -0.0975 0.0134  128 LEU B C   
2743 O  O   . LEU B 128 ? 0.3231 0.1595 0.3440 -0.0364 -0.0980 0.0291  128 LEU B O   
2744 C  CB  . LEU B 128 ? 0.3255 0.0722 0.3855 0.0127  -0.0898 -0.0014 128 LEU B CB  
2745 C  CG  . LEU B 128 ? 0.3706 0.0803 0.3810 0.0223  -0.0701 0.0260  128 LEU B CG  
2746 C  CD1 . LEU B 128 ? 0.3355 0.0852 0.3871 0.0207  -0.0693 0.0327  128 LEU B CD1 
2747 C  CD2 . LEU B 128 ? 0.3741 0.1152 0.3870 0.0345  -0.0884 0.0161  128 LEU B CD2 
2748 N  N   . LEU B 129 ? 0.3099 0.0996 0.3039 0.0147  -0.0624 -0.0105 129 LEU B N   
2749 C  CA  . LEU B 129 ? 0.3081 0.1173 0.3418 -0.0168 -0.0917 0.0074  129 LEU B CA  
2750 C  C   . LEU B 129 ? 0.3507 0.1059 0.2704 0.0143  -0.1295 0.0156  129 LEU B C   
2751 O  O   . LEU B 129 ? 0.3308 0.1264 0.2588 0.0086  -0.1104 0.0349  129 LEU B O   
2752 C  CB  . LEU B 129 ? 0.3515 0.1479 0.3283 -0.0341 -0.0941 0.0228  129 LEU B CB  
2753 C  CG  . LEU B 129 ? 0.4128 0.1868 0.3215 -0.0696 -0.1256 0.0040  129 LEU B CG  
2754 C  CD1 . LEU B 129 ? 0.4265 0.1325 0.3839 -0.0324 -0.1724 0.0151  129 LEU B CD1 
2755 C  CD2 . LEU B 129 ? 0.5303 0.2281 0.3451 -0.1352 -0.0906 0.0478  129 LEU B CD2 
2756 N  N   . VAL B 130 ? 0.3815 0.1644 0.2496 -0.0223 -0.1113 0.0186  130 VAL B N   
2757 C  CA  . VAL B 130 ? 0.3855 0.1250 0.2453 -0.0513 -0.0969 0.0116  130 VAL B CA  
2758 C  C   . VAL B 130 ? 0.3468 0.0869 0.3262 -0.0382 -0.1351 -0.0234 130 VAL B C   
2759 O  O   . VAL B 130 ? 0.3786 0.1319 0.2989 0.0016  -0.1028 0.0141  130 VAL B O   
2760 C  CB  . VAL B 130 ? 0.3172 0.0576 0.3180 -0.0011 -0.1603 0.0134  130 VAL B CB  
2761 C  CG1 . VAL B 130 ? 0.3498 0.1217 0.3600 0.0232  -0.1931 0.0439  130 VAL B CG1 
2762 C  CG2 . VAL B 130 ? 0.4931 0.0933 0.3564 0.0656  -0.1553 -0.0290 130 VAL B CG2 
2763 N  N   . ALA B 131 ? 0.3452 0.0926 0.2581 -0.0296 -0.0976 -0.0307 131 ALA B N   
2764 C  CA  . ALA B 131 ? 0.3402 0.0858 0.2876 -0.0176 -0.1255 0.0283  131 ALA B CA  
2765 C  C   . ALA B 131 ? 0.3139 0.1527 0.2782 -0.0203 -0.1083 0.0599  131 ALA B C   
2766 O  O   . ALA B 131 ? 0.3283 0.1263 0.2900 0.0301  -0.1113 -0.0113 131 ALA B O   
2767 C  CB  . ALA B 131 ? 0.3759 0.1337 0.3831 0.0146  -0.1006 0.1128  131 ALA B CB  
2768 N  N   . HIS B 132 ? 0.3128 0.1072 0.2828 0.0080  -0.1111 0.0467  132 HIS B N   
2769 C  CA  . HIS B 132 ? 0.2736 0.0671 0.2805 -0.0168 -0.0914 0.0250  132 HIS B CA  
2770 C  C   . HIS B 132 ? 0.3118 0.0678 0.2472 -0.0086 -0.1088 0.0235  132 HIS B C   
2771 O  O   . HIS B 132 ? 0.3662 0.1107 0.3374 0.0117  -0.1786 0.0222  132 HIS B O   
2772 C  CB  . HIS B 132 ? 0.3366 0.0993 0.3243 -0.0020 -0.0787 -0.0208 132 HIS B CB  
2773 C  CG  . HIS B 132 ? 0.3223 0.1043 0.2502 0.0003  -0.1078 -0.0109 132 HIS B CG  
2774 N  ND1 . HIS B 132 ? 0.3048 0.1178 0.2797 -0.0265 -0.0924 0.0508  132 HIS B ND1 
2775 C  CD2 . HIS B 132 ? 0.3495 0.1303 0.3294 -0.0122 -0.1547 0.0290  132 HIS B CD2 
2776 C  CE1 . HIS B 132 ? 0.3677 0.1198 0.3102 -0.0345 -0.1579 0.0725  132 HIS B CE1 
2777 N  NE2 . HIS B 132 ? 0.3362 0.1175 0.2859 -0.0068 -0.1171 0.0253  132 HIS B NE2 
2778 N  N   . ALA B 133 ? 0.3656 0.0526 0.2447 -0.0101 -0.1071 -0.0105 133 ALA B N   
2779 C  CA  . ALA B 133 ? 0.3727 0.0568 0.2684 -0.0021 -0.0961 -0.0155 133 ALA B CA  
2780 C  C   . ALA B 133 ? 0.3680 0.1061 0.2544 0.0313  -0.1008 0.0121  133 ALA B C   
2781 O  O   . ALA B 133 ? 0.3969 0.1047 0.2718 0.0443  -0.1201 0.0059  133 ALA B O   
2782 C  CB  . ALA B 133 ? 0.3871 0.0695 0.3509 -0.0195 -0.0861 0.0285  133 ALA B CB  
2783 N  N   . TYR B 134 ? 0.4020 0.1673 0.2565 0.0229  -0.1014 0.0356  134 TYR B N   
2784 C  CA  . TYR B 134 ? 0.4515 0.2486 0.2113 0.0673  -0.1298 -0.0394 134 TYR B CA  
2785 C  C   . TYR B 134 ? 0.4006 0.2225 0.2364 0.0823  -0.0770 -0.0281 134 TYR B C   
2786 O  O   . TYR B 134 ? 0.4349 0.2936 0.2445 0.1335  -0.0753 -0.0340 134 TYR B O   
2787 C  CB  . TYR B 134 ? 0.4611 0.3104 0.2472 0.0516  -0.1074 0.0332  134 TYR B CB  
2788 C  CG  . TYR B 134 ? 0.4935 0.3193 0.2785 0.0460  -0.0730 0.0129  134 TYR B CG  
2789 C  CD1 . TYR B 134 ? 0.4664 0.3487 0.2798 -0.0127 -0.0966 -0.0506 134 TYR B CD1 
2790 C  CD2 . TYR B 134 ? 0.4382 0.2982 0.3040 0.0802  -0.0649 0.0113  134 TYR B CD2 
2791 C  CE1 . TYR B 134 ? 0.5677 0.3731 0.2375 -0.0346 -0.0556 -0.0647 134 TYR B CE1 
2792 C  CE2 . TYR B 134 ? 0.4663 0.3720 0.3589 -0.0014 -0.0252 -0.0938 134 TYR B CE2 
2793 C  CZ  . TYR B 134 ? 0.5415 0.3785 0.3425 -0.0315 0.0136  -0.1007 134 TYR B CZ  
2794 O  OH  . TYR B 134 ? 0.5194 0.3617 0.3169 0.0433  -0.0063 -0.0220 134 TYR B OH  
2795 N  N   . THR B 135 ? 0.4277 0.2024 0.2832 0.0566  -0.1021 0.0257  135 THR B N   
2796 C  CA  . THR B 135 ? 0.4163 0.2303 0.2678 0.0780  -0.1049 -0.0376 135 THR B CA  
2797 C  C   . THR B 135 ? 0.3697 0.2153 0.2986 0.0644  -0.0737 0.0271  135 THR B C   
2798 O  O   . THR B 135 ? 0.3716 0.2319 0.3491 0.0597  -0.0409 0.1078  135 THR B O   
2799 C  CB  . THR B 135 ? 0.4397 0.1862 0.3783 0.0401  -0.0799 0.0514  135 THR B CB  
2800 O  OG1 . THR B 135 ? 0.6271 0.2287 0.3473 0.0807  -0.1306 -0.0023 135 THR B OG1 
2801 C  CG2 . THR B 135 ? 0.4327 0.2307 0.5254 0.0433  -0.0833 -0.0257 135 THR B CG2 
2802 N  N   . ARG B 136 ? 0.3444 0.1312 0.3367 0.0204  -0.0705 0.0368  136 ARG B N   
2803 C  CA  . ARG B 136 ? 0.2571 0.1388 0.3114 -0.0138 -0.0416 0.0233  136 ARG B CA  
2804 C  C   . ARG B 136 ? 0.2819 0.1349 0.2850 -0.0039 -0.0178 0.0570  136 ARG B C   
2805 O  O   . ARG B 136 ? 0.3080 0.1751 0.3234 0.0309  -0.0721 -0.0132 136 ARG B O   
2806 C  CB  . ARG B 136 ? 0.2652 0.1327 0.3636 -0.0433 0.0032  0.0093  136 ARG B CB  
2807 C  CG  . ARG B 136 ? 0.3738 0.1876 0.3916 0.0141  -0.0597 -0.0541 136 ARG B CG  
2808 C  CD  . ARG B 136 ? 0.3747 0.2255 0.3373 -0.0203 -0.0247 -0.0188 136 ARG B CD  
2809 N  NE  . ARG B 136 ? 0.3809 0.1239 0.3128 0.0065  -0.0450 0.0155  136 ARG B NE  
2810 C  CZ  . ARG B 136 ? 0.4228 0.1293 0.3051 0.0435  0.1203  0.0678  136 ARG B CZ  
2811 N  NH1 . ARG B 136 ? 0.3928 0.1121 0.3617 0.0169  -0.1012 -0.0066 136 ARG B NH1 
2812 N  NH2 . ARG B 136 ? 0.3786 0.2160 0.3128 0.0296  0.0205  -0.0860 136 ARG B NH2 
2813 N  N   . TYR B 137 ? 0.3088 0.1260 0.2572 -0.0095 -0.0348 0.0474  137 TYR B N   
2814 C  CA  . TYR B 137 ? 0.3729 0.1250 0.2831 -0.0056 -0.0484 0.0261  137 TYR B CA  
2815 C  C   . TYR B 137 ? 0.3715 0.1433 0.2881 0.0075  -0.0546 0.0077  137 TYR B C   
2816 O  O   . TYR B 137 ? 0.3577 0.1762 0.3431 0.0069  -0.0380 0.0503  137 TYR B O   
2817 C  CB  . TYR B 137 ? 0.3749 0.1025 0.2726 0.0024  -0.0507 -0.0091 137 TYR B CB  
2818 C  CG  . TYR B 137 ? 0.3372 0.0900 0.2418 -0.0154 -0.0879 -0.0218 137 TYR B CG  
2819 C  CD1 . TYR B 137 ? 0.3551 0.1146 0.2553 0.0158  -0.0961 -0.0167 137 TYR B CD1 
2820 C  CD2 . TYR B 137 ? 0.3647 0.1728 0.2543 0.0441  -0.0710 0.0298  137 TYR B CD2 
2821 C  CE1 . TYR B 137 ? 0.3689 0.1057 0.2450 0.0200  -0.0932 0.0252  137 TYR B CE1 
2822 C  CE2 . TYR B 137 ? 0.3525 0.2324 0.2384 0.0404  -0.0825 0.0250  137 TYR B CE2 
2823 C  CZ  . TYR B 137 ? 0.3696 0.2140 0.2359 0.0514  -0.1031 -0.0236 137 TYR B CZ  
2824 O  OH  . TYR B 137 ? 0.4687 0.3690 0.2200 0.2103  -0.0941 -0.0065 137 TYR B OH  
2825 N  N   . LEU B 138 ? 0.4271 0.1657 0.2696 0.0129  -0.0862 -0.0351 138 LEU B N   
2826 C  CA  . LEU B 138 ? 0.4662 0.2207 0.2702 0.0289  -0.0849 -0.0526 138 LEU B CA  
2827 C  C   . LEU B 138 ? 0.4498 0.1798 0.3030 0.0522  -0.0492 0.0100  138 LEU B C   
2828 O  O   . LEU B 138 ? 0.4738 0.2804 0.3316 0.1103  -0.0871 -0.0393 138 LEU B O   
2829 C  CB  . LEU B 138 ? 0.6161 0.3883 0.2790 0.0440  -0.1345 -0.1004 138 LEU B CB  
2830 C  CG  . LEU B 138 ? 0.7339 0.3887 0.4635 0.0090  -0.2819 -0.1566 138 LEU B CG  
2831 C  CD1 . LEU B 138 ? 0.7911 0.8268 0.5655 0.0905  -0.3188 -0.3784 138 LEU B CD1 
2832 C  CD2 . LEU B 138 ? 0.6724 0.4026 0.8031 -0.0433 -0.2896 -0.0093 138 LEU B CD2 
2833 N  N   . GLY B 139 ? 0.4563 0.1775 0.2977 0.0175  -0.0416 0.0285  139 GLY B N   
2834 C  CA  . GLY B 139 ? 0.4565 0.2139 0.2820 -0.0074 -0.0137 0.0786  139 GLY B CA  
2835 C  C   . GLY B 139 ? 0.3893 0.2424 0.3080 0.0316  0.0139  0.0891  139 GLY B C   
2836 O  O   . GLY B 139 ? 0.3686 0.2626 0.3069 -0.0105 0.0229  0.0460  139 GLY B O   
2837 N  N   . ASP B 140 ? 0.3473 0.1993 0.2758 0.0591  -0.0141 0.0752  140 ASP B N   
2838 C  CA  . ASP B 140 ? 0.4151 0.1859 0.3029 0.0356  -0.0817 0.0675  140 ASP B CA  
2839 C  C   . ASP B 140 ? 0.3555 0.1759 0.3439 0.0243  -0.0527 0.0871  140 ASP B C   
2840 O  O   . ASP B 140 ? 0.2922 0.2203 0.4175 0.0233  0.0049  0.0734  140 ASP B O   
2841 C  CB  . ASP B 140 ? 0.5037 0.2106 0.2566 0.0881  -0.0973 0.0751  140 ASP B CB  
2842 C  CG  . ASP B 140 ? 0.5314 0.2503 0.2402 0.0155  -0.1715 -0.0119 140 ASP B CG  
2843 O  OD1 . ASP B 140 ? 0.7991 0.2883 0.4794 -0.1078 0.1258  -0.1811 140 ASP B OD1 
2844 O  OD2 . ASP B 140 ? 0.5838 0.1402 0.3143 -0.0190 -0.1038 0.0013  140 ASP B OD2 
2845 N  N   . LEU B 141 ? 0.3560 0.1774 0.4067 0.0384  -0.0558 0.0501  141 LEU B N   
2846 C  CA  . LEU B 141 ? 0.3690 0.2110 0.4926 0.0891  -0.1171 -0.0087 141 LEU B CA  
2847 C  C   . LEU B 141 ? 0.4262 0.3083 0.5026 0.1532  -0.0876 -0.0093 141 LEU B C   
2848 O  O   . LEU B 141 ? 0.3759 0.2037 0.6554 0.0838  -0.0584 0.0121  141 LEU B O   
2849 C  CB  . LEU B 141 ? 0.4507 0.2038 0.4595 0.0502  -0.1654 0.0272  141 LEU B CB  
2850 C  CG  . LEU B 141 ? 0.4989 0.2351 0.4216 0.0525  -0.1224 -0.0216 141 LEU B CG  
2851 C  CD1 . LEU B 141 ? 0.3519 0.1560 0.4318 -0.0127 -0.0969 -0.0228 141 LEU B CD1 
2852 C  CD2 . LEU B 141 ? 0.4860 0.2349 0.3627 0.0262  -0.0898 -0.0105 141 LEU B CD2 
2853 N  N   . SER B 142 ? 0.5283 0.4275 0.3505 0.2469  -0.0824 -0.0584 142 SER B N   
2854 C  CA  . SER B 142 ? 0.5768 0.5006 0.4323 0.2255  -0.0161 -0.0968 142 SER B CA  
2855 C  C   . SER B 142 ? 0.5758 0.5157 0.4526 0.1664  0.0179  -0.1029 142 SER B C   
2856 O  O   . SER B 142 ? 0.5487 0.5240 0.3575 0.1420  0.0456  -0.0304 142 SER B O   
2857 C  CB  . SER B 142 ? 0.6160 0.5093 0.3998 0.2522  0.0564  -0.1012 142 SER B CB  
2858 O  OG  . SER B 142 ? 0.7362 0.7887 0.4203 0.2536  -0.0694 -0.0687 142 SER B OG  
2859 N  N   . GLY B 143 ? 0.6568 0.5341 0.4666 0.1905  -0.0392 -0.1172 143 GLY B N   
2860 C  CA  . GLY B 143 ? 0.7324 0.5800 0.4826 0.0384  -0.0772 0.0059  143 GLY B CA  
2861 C  C   . GLY B 143 ? 0.6946 0.5359 0.4419 0.0339  -0.0517 -0.0413 143 GLY B C   
2862 O  O   . GLY B 143 ? 0.8245 0.4507 0.5866 -0.1742 -0.1859 0.1296  143 GLY B O   
2863 N  N   . GLY B 144 ? 0.6187 0.4358 0.4147 0.1354  -0.0075 -0.1140 144 GLY B N   
2864 C  CA  . GLY B 144 ? 0.5916 0.4137 0.4724 0.1019  -0.0506 -0.0259 144 GLY B CA  
2865 C  C   . GLY B 144 ? 0.4647 0.4188 0.5439 0.0442  -0.0219 -0.0384 144 GLY B C   
2866 O  O   . GLY B 144 ? 0.4965 0.3545 0.6774 0.1220  -0.1398 -0.1896 144 GLY B O   
2867 N  N   . GLN B 145 ? 0.5311 0.3693 0.5337 0.0735  -0.1509 -0.0493 145 GLN B N   
2868 C  CA  . GLN B 145 ? 0.5036 0.4573 0.5857 0.1067  -0.1904 -0.1051 145 GLN B CA  
2869 C  C   . GLN B 145 ? 0.5260 0.4277 0.6009 0.1018  -0.1228 -0.1025 145 GLN B C   
2870 O  O   . GLN B 145 ? 0.4836 0.4151 0.5227 -0.0249 -0.0836 -0.0548 145 GLN B O   
2871 C  CB  . GLN B 145 ? 0.4017 0.4689 0.7069 0.1172  -0.0383 -0.1695 145 GLN B CB  
2872 C  CG  . GLN B 145 ? 0.5136 0.5255 0.8787 0.0090  -0.0313 -0.0575 145 GLN B CG  
2873 C  CD  . GLN B 145 ? 0.5336 0.6695 0.9159 0.1080  0.0433  0.0323  145 GLN B CD  
2874 O  OE1 . GLN B 145 ? 0.5432 1.1693 1.0794 0.0306  0.2317  -0.0226 145 GLN B OE1 
2875 N  NE2 . GLN B 145 ? 0.8920 0.8573 1.1352 0.2597  -0.1872 0.0994  145 GLN B NE2 
2876 N  N   . VAL B 146 ? 0.5562 0.3810 0.5879 0.1216  -0.1738 -0.1145 146 VAL B N   
2877 C  CA  . VAL B 146 ? 0.5998 0.5387 0.5571 0.0515  -0.0374 -0.1333 146 VAL B CA  
2878 C  C   . VAL B 146 ? 0.4306 0.5377 0.5119 -0.0168 -0.0301 -0.1022 146 VAL B C   
2879 O  O   . VAL B 146 ? 0.3319 0.9294 0.4819 -0.1098 0.0866  -0.1417 146 VAL B O   
2880 C  CB  . VAL B 146 ? 0.6425 0.6347 0.5209 0.0391  -0.0500 -0.1487 146 VAL B CB  
2881 C  CG1 . VAL B 146 ? 0.7726 0.8924 0.4862 -0.1581 -0.1797 0.0193  146 VAL B CG1 
2882 C  CG2 . VAL B 146 ? 0.4925 0.7468 0.5917 0.1944  0.0990  -0.1667 146 VAL B CG2 
2883 N  N   . LEU B 147 ? 0.4628 0.3987 0.4927 0.0191  -0.0936 -0.0557 147 LEU B N   
2884 C  CA  . LEU B 147 ? 0.4645 0.3497 0.5468 -0.0099 -0.1122 -0.0594 147 LEU B CA  
2885 C  C   . LEU B 147 ? 0.3900 0.3826 0.4898 -0.0130 -0.0531 -0.0878 147 LEU B C   
2886 O  O   . LEU B 147 ? 0.3644 0.3524 0.5346 0.0206  -0.0796 -0.0960 147 LEU B O   
2887 C  CB  . LEU B 147 ? 0.4647 0.2625 0.6857 -0.0486 -0.1240 -0.0759 147 LEU B CB  
2888 C  CG  . LEU B 147 ? 0.6489 0.3031 0.7712 -0.0055 -0.0953 -0.0108 147 LEU B CG  
2889 C  CD1 . LEU B 147 ? 0.8039 0.3164 0.9818 0.0863  -0.2911 -0.0621 147 LEU B CD1 
2890 C  CD2 . LEU B 147 ? 0.6024 0.3729 0.8753 -0.1113 0.1303  -0.0460 147 LEU B CD2 
2891 N  N   . LYS B 148 ? 0.3078 0.4212 0.4652 -0.0211 -0.0451 -0.0733 148 LYS B N   
2892 C  CA  . LYS B 148 ? 0.3151 0.3870 0.3878 -0.0198 0.0104  -0.1317 148 LYS B CA  
2893 C  C   . LYS B 148 ? 0.3114 0.3366 0.4108 -0.0184 0.0291  -0.0093 148 LYS B C   
2894 O  O   . LYS B 148 ? 0.3035 0.3709 0.4501 -0.0121 0.0041  -0.0400 148 LYS B O   
2895 C  CB  . LYS B 148 ? 0.3329 0.3800 0.3952 -0.0239 -0.0746 -0.1281 148 LYS B CB  
2896 C  CG  . LYS B 148 ? 0.4364 0.3357 0.3906 0.0320  -0.0024 -0.1333 148 LYS B CG  
2897 C  CD  . LYS B 148 ? 0.4540 0.3984 0.6385 -0.0401 -0.1103 -0.0343 148 LYS B CD  
2898 C  CE  . LYS B 148 ? 0.4591 0.5845 0.8116 -0.0599 0.0352  -0.1246 148 LYS B CE  
2899 N  NZ  . LYS B 148 ? 0.7065 1.0014 0.9181 0.2420  0.0701  -0.2631 148 LYS B NZ  
2900 N  N   . LYS B 149 ? 0.3215 0.3455 0.4442 0.0017  0.0406  -0.0207 149 LYS B N   
2901 C  CA  . LYS B 149 ? 0.3181 0.3396 0.5916 -0.0080 0.0553  -0.0502 149 LYS B CA  
2902 C  C   . LYS B 149 ? 0.3574 0.3468 0.4802 -0.0307 -0.0062 0.0129  149 LYS B C   
2903 O  O   . LYS B 149 ? 0.4884 0.3780 0.3724 0.0172  -0.0439 -0.0736 149 LYS B O   
2904 C  CB  . LYS B 149 ? 0.4215 0.3377 0.7080 0.0549  0.1074  -0.1182 149 LYS B CB  
2905 C  CG  . LYS B 149 ? 0.4285 0.7137 0.9092 0.1386  0.1775  -0.1010 149 LYS B CG  
2906 C  CD  . LYS B 149 ? 0.5562 0.9579 0.9680 0.2028  0.2779  -0.0854 149 LYS B CD  
2907 C  CE  . LYS B 149 ? 0.6295 1.0191 1.0839 0.2852  0.3498  -0.1119 149 LYS B CE  
2908 N  NZ  . LYS B 149 ? 0.7599 1.0832 1.2834 0.2431  0.2366  -0.3639 149 LYS B NZ  
2909 N  N   . ILE B 150 ? 0.3178 0.3629 0.4297 -0.0052 0.0707  0.0222  150 ILE B N   
2910 C  CA  . ILE B 150 ? 0.3986 0.3805 0.3896 -0.0541 0.0491  0.0858  150 ILE B CA  
2911 C  C   . ILE B 150 ? 0.2986 0.3186 0.4136 0.0110  0.0344  0.0584  150 ILE B C   
2912 O  O   . ILE B 150 ? 0.2686 0.3790 0.4561 0.0328  0.0441  -0.0022 150 ILE B O   
2913 C  CB  . ILE B 150 ? 0.5882 0.3871 0.4417 -0.0744 -0.1397 0.0650  150 ILE B CB  
2914 C  CG1 . ILE B 150 ? 0.6852 0.4126 0.4152 -0.1736 -0.1327 0.1288  150 ILE B CG1 
2915 C  CG2 . ILE B 150 ? 0.5661 0.3817 0.4777 -0.1304 -0.1212 0.1053  150 ILE B CG2 
2916 C  CD1 . ILE B 150 ? 1.0049 0.4360 0.5345 -0.2309 -0.3331 0.1905  150 ILE B CD1 
2917 N  N   . ALA B 151 ? 0.2663 0.2883 0.4852 0.0585  0.0221  -0.0064 151 ALA B N   
2918 C  CA  . ALA B 151 ? 0.2384 0.3188 0.4897 0.0561  0.0378  -0.0080 151 ALA B CA  
2919 C  C   . ALA B 151 ? 0.3182 0.2926 0.4949 0.0129  -0.0393 -0.0207 151 ALA B C   
2920 O  O   . ALA B 151 ? 0.3385 0.3202 0.4803 0.0235  -0.0063 -0.0649 151 ALA B O   
2921 C  CB  . ALA B 151 ? 0.2406 0.2054 0.5379 -0.0270 0.0473  -0.0260 151 ALA B CB  
2922 N  N   . GLN B 152 ? 0.3409 0.2943 0.4000 -0.0083 -0.0090 -0.0066 152 GLN B N   
2923 C  CA  . GLN B 152 ? 0.3662 0.2928 0.4418 -0.0410 0.0101  0.0582  152 GLN B CA  
2924 C  C   . GLN B 152 ? 0.3474 0.2852 0.4880 -0.0030 -0.0089 0.0964  152 GLN B C   
2925 O  O   . GLN B 152 ? 0.3540 0.3009 0.4801 0.0547  -0.0040 -0.0197 152 GLN B O   
2926 C  CB  . GLN B 152 ? 0.4307 0.3003 0.4021 -0.0355 0.0188  0.0468  152 GLN B CB  
2927 C  CG  . GLN B 152 ? 0.4817 0.3563 0.4409 -0.1160 -0.0201 0.0411  152 GLN B CG  
2928 C  CD  . GLN B 152 ? 0.4600 0.2905 0.4696 -0.0309 -0.0709 0.0750  152 GLN B CD  
2929 O  OE1 . GLN B 152 ? 0.3818 0.3392 0.6286 -0.0532 -0.0252 -0.0707 152 GLN B OE1 
2930 N  NE2 . GLN B 152 ? 0.3782 0.2695 0.8635 -0.0052 0.0752  -0.0414 152 GLN B NE2 
2931 N  N   . LYS B 153 ? 0.3666 0.3758 0.4763 -0.0833 0.0279  -0.0239 153 LYS B N   
2932 C  CA  . LYS B 153 ? 0.3504 0.3140 0.4694 -0.0436 -0.0057 0.0267  153 LYS B CA  
2933 C  C   . LYS B 153 ? 0.3287 0.3151 0.4523 -0.0284 -0.0515 0.0385  153 LYS B C   
2934 O  O   . LYS B 153 ? 0.3574 0.3917 0.5074 0.0169  -0.0984 -0.0135 153 LYS B O   
2935 C  CB  . LYS B 153 ? 0.3930 0.4561 0.5231 -0.0179 0.0766  -0.0356 153 LYS B CB  
2936 C  CG  . LYS B 153 ? 0.4564 0.5716 0.6982 -0.0802 0.1670  -0.0166 153 LYS B CG  
2937 C  CD  . LYS B 153 ? 0.6802 0.6683 0.6914 -0.1081 0.2815  0.0562  153 LYS B CD  
2938 C  CE  . LYS B 153 ? 0.7094 0.7070 0.7836 -0.0312 0.3309  0.0514  153 LYS B CE  
2939 N  NZ  . LYS B 153 ? 1.0380 0.7267 0.8049 -0.1678 0.4910  0.0412  153 LYS B NZ  
2940 N  N   . ALA B 154 ? 0.2884 0.3439 0.3718 -0.0126 -0.0055 0.0098  154 ALA B N   
2941 C  CA  . ALA B 154 ? 0.2609 0.3499 0.3806 -0.0004 0.0115  -0.0013 154 ALA B CA  
2942 C  C   . ALA B 154 ? 0.3441 0.2996 0.3562 -0.0844 -0.0270 0.0303  154 ALA B C   
2943 O  O   . ALA B 154 ? 0.3545 0.3241 0.4244 -0.0589 -0.0522 -0.0210 154 ALA B O   
2944 C  CB  . ALA B 154 ? 0.4455 0.3969 0.3284 0.0945  0.0117  0.0004  154 ALA B CB  
2945 N  N   . LEU B 155 ? 0.3045 0.2561 0.3997 -0.0225 0.0062  0.0415  155 LEU B N   
2946 C  CA  . LEU B 155 ? 0.2989 0.2499 0.3943 -0.0302 -0.0107 0.0295  155 LEU B CA  
2947 C  C   . LEU B 155 ? 0.2726 0.2416 0.3837 -0.0566 -0.0418 0.0105  155 LEU B C   
2948 O  O   . LEU B 155 ? 0.3911 0.2251 0.3896 -0.0433 -0.0999 -0.0359 155 LEU B O   
2949 C  CB  . LEU B 155 ? 0.2957 0.2909 0.3949 0.0158  -0.0050 0.0488  155 LEU B CB  
2950 C  CG  . LEU B 155 ? 0.3247 0.3412 0.4080 0.0982  0.0588  0.0769  155 LEU B CG  
2951 C  CD1 . LEU B 155 ? 0.2355 0.6854 0.4304 0.1592  0.1198  0.2196  155 LEU B CD1 
2952 C  CD2 . LEU B 155 ? 0.6390 0.3698 0.4821 0.3248  -0.0950 -0.0521 155 LEU B CD2 
2953 N  N   . ASP B 156 ? 0.3257 0.2628 0.3579 -0.0219 -0.0328 0.0275  156 ASP B N   
2954 C  CA  . ASP B 156 ? 0.3122 0.2921 0.3327 -0.0153 -0.0819 -0.0086 156 ASP B CA  
2955 C  C   . ASP B 156 ? 0.2611 0.3056 0.3252 0.0074  -0.1052 0.0217  156 ASP B C   
2956 O  O   . ASP B 156 ? 0.2941 0.2987 0.3289 -0.0251 -0.0868 0.0063  156 ASP B O   
2957 C  CB  . ASP B 156 ? 0.2708 0.4027 0.6524 -0.0595 -0.1157 0.0237  156 ASP B CB  
2958 C  CG  . ASP B 156 ? 0.3227 0.6845 0.6299 -0.1451 -0.1212 0.0422  156 ASP B CG  
2959 O  OD1 . ASP B 156 ? 0.5378 1.1304 0.8619 -0.4730 -0.0550 0.1579  156 ASP B OD1 
2960 O  OD2 . ASP B 156 ? 0.5722 1.1262 0.6720 -0.1090 -0.1458 -0.1556 156 ASP B OD2 
2961 N  N   . LEU B 157 ? 0.2696 0.2787 0.3606 0.0082  -0.0945 -0.0148 157 LEU B N   
2962 C  CA  . LEU B 157 ? 0.3080 0.2242 0.3600 -0.0377 -0.0874 -0.0400 157 LEU B CA  
2963 C  C   . LEU B 157 ? 0.3057 0.2643 0.3855 0.0024  -0.0667 -0.0128 157 LEU B C   
2964 O  O   . LEU B 157 ? 0.2349 0.3288 0.3827 -0.0066 -0.0669 0.0007  157 LEU B O   
2965 C  CB  . LEU B 157 ? 0.2790 0.2708 0.3939 -0.0128 -0.0784 -0.0900 157 LEU B CB  
2966 C  CG  . LEU B 157 ? 0.2751 0.3326 0.5983 -0.0056 -0.1591 -0.0268 157 LEU B CG  
2967 C  CD1 . LEU B 157 ? 0.3354 0.3360 0.8414 0.0126  -0.2943 -0.0374 157 LEU B CD1 
2968 C  CD2 . LEU B 157 ? 0.5661 0.2417 0.7336 -0.0012 -0.1643 -0.0044 157 LEU B CD2 
2969 N  N   . PRO B 158 ? 0.2594 0.1891 0.3990 -0.0122 -0.0724 -0.0087 158 PRO B N   
2970 C  CA  . PRO B 158 ? 0.2787 0.1855 0.3931 -0.0119 -0.0683 -0.0216 158 PRO B CA  
2971 C  C   . PRO B 158 ? 0.3215 0.1945 0.3410 -0.0295 -0.1433 0.0191  158 PRO B C   
2972 O  O   . PRO B 158 ? 0.3785 0.3087 0.3528 0.0035  -0.1748 0.0046  158 PRO B O   
2973 C  CB  . PRO B 158 ? 0.2593 0.2669 0.3790 0.0086  -0.0858 -0.0241 158 PRO B CB  
2974 C  CG  . PRO B 158 ? 0.2207 0.2195 0.4587 -0.0223 -0.0546 0.0187  158 PRO B CG  
2975 C  CD  . PRO B 158 ? 0.2208 0.1926 0.4712 -0.0253 -0.0436 0.0073  158 PRO B CD  
2976 N  N   . SER B 159 ? 0.3366 0.1867 0.5052 -0.0120 -0.2088 0.0177  159 SER B N   
2977 C  CA  . SER B 159 ? 0.3382 0.1917 0.6494 0.0069  -0.1513 -0.0541 159 SER B CA  
2978 C  C   . SER B 159 ? 0.4077 0.1742 0.4986 -0.0418 -0.1650 -0.0235 159 SER B C   
2979 O  O   . SER B 159 ? 0.5468 0.2284 0.6506 -0.0234 -0.1832 0.0766  159 SER B O   
2980 C  CB  . SER B 159 ? 0.4684 0.2367 0.8739 0.0960  -0.1478 0.0013  159 SER B CB  
2981 O  OG  . SER B 159 ? 0.7561 0.5189 0.9782 0.0987  -0.4161 0.1111  159 SER B OG  
2982 N  N   . SER B 160 ? 0.3252 0.1956 0.4339 -0.0720 -0.1405 0.0049  160 SER B N   
2983 C  CA  . SER B 160 ? 0.3822 0.1621 0.3534 -0.1204 -0.1518 0.0101  160 SER B CA  
2984 C  C   . SER B 160 ? 0.3118 0.2132 0.3021 -0.0526 -0.1029 0.0112  160 SER B C   
2985 O  O   . SER B 160 ? 0.3351 0.1769 0.3275 -0.0300 -0.0670 -0.0239 160 SER B O   
2986 C  CB  . SER B 160 ? 0.3698 0.1789 0.4035 -0.0621 -0.1539 -0.0082 160 SER B CB  
2987 O  OG  . SER B 160 ? 0.3431 0.1887 0.5457 0.0122  -0.1337 0.0314  160 SER B OG  
2988 N  N   . GLY B 161 ? 0.2798 0.1790 0.2972 -0.0142 -0.1017 0.0351  161 GLY B N   
2989 C  CA  . GLY B 161 ? 0.2820 0.1939 0.3146 0.0025  -0.0961 -0.0289 161 GLY B CA  
2990 C  C   . GLY B 161 ? 0.2386 0.1949 0.3216 -0.0053 -0.0870 -0.0834 161 GLY B C   
2991 O  O   . GLY B 161 ? 0.2411 0.1975 0.2917 -0.0525 -0.0551 -0.0021 161 GLY B O   
2992 N  N   . GLU B 162 ? 0.1741 0.1957 0.3393 -0.0030 -0.0740 -0.0662 162 GLU B N   
2993 C  CA  . GLU B 162 ? 0.1925 0.2088 0.3043 0.0030  -0.0735 -0.0338 162 GLU B CA  
2994 C  C   . GLU B 162 ? 0.2672 0.2122 0.3108 -0.0286 -0.0961 -0.0303 162 GLU B C   
2995 O  O   . GLU B 162 ? 0.2514 0.2095 0.3255 -0.0136 -0.0692 0.0140  162 GLU B O   
2996 C  CB  . GLU B 162 ? 0.3433 0.3597 0.3609 0.1523  0.0293  0.0284  162 GLU B CB  
2997 C  CG  . GLU B 162 ? 0.4391 0.3898 0.3277 0.1174  0.0165  0.0155  162 GLU B CG  
2998 C  CD  . GLU B 162 ? 0.3893 0.3057 0.2959 0.1289  -0.0590 0.0300  162 GLU B CD  
2999 O  OE1 . GLU B 162 ? 0.3416 0.2491 0.2640 0.0433  -0.0600 0.0131  162 GLU B OE1 
3000 O  OE2 . GLU B 162 ? 0.3155 0.4061 0.2647 0.0759  -0.0244 0.0965  162 GLU B OE2 
3001 N  N   . GLY B 163 ? 0.2170 0.2074 0.2599 -0.0150 -0.0089 -0.0242 163 GLY B N   
3002 C  CA  . GLY B 163 ? 0.2264 0.1858 0.2761 -0.0141 -0.0198 -0.0546 163 GLY B CA  
3003 C  C   . GLY B 163 ? 0.2700 0.1371 0.2798 -0.0617 -0.0379 -0.0363 163 GLY B C   
3004 O  O   . GLY B 163 ? 0.2901 0.1384 0.3360 -0.0370 -0.0381 -0.0275 163 GLY B O   
3005 N  N   . LEU B 164 ? 0.2716 0.1435 0.2707 0.0015  -0.0504 -0.0384 164 LEU B N   
3006 C  CA  . LEU B 164 ? 0.2412 0.1398 0.2716 -0.0305 -0.0345 -0.0304 164 LEU B CA  
3007 C  C   . LEU B 164 ? 0.2358 0.0919 0.2529 -0.0130 -0.0271 -0.0209 164 LEU B C   
3008 O  O   . LEU B 164 ? 0.2622 0.1294 0.2479 -0.0088 -0.0388 -0.0236 164 LEU B O   
3009 C  CB  . LEU B 164 ? 0.2406 0.1415 0.3010 -0.0240 -0.0314 -0.0244 164 LEU B CB  
3010 C  CG  . LEU B 164 ? 0.2313 0.1889 0.3312 -0.0333 -0.0490 -0.0067 164 LEU B CG  
3011 C  CD1 . LEU B 164 ? 0.2352 0.1851 0.4422 -0.0139 -0.0430 -0.0219 164 LEU B CD1 
3012 C  CD2 . LEU B 164 ? 0.1944 0.1626 0.4526 -0.0420 -0.0310 -0.0176 164 LEU B CD2 
3013 N  N   . ALA B 165 ? 0.2254 0.1124 0.2587 0.0022  -0.0359 0.0163  165 ALA B N   
3014 C  CA  . ALA B 165 ? 0.2237 0.1190 0.2283 -0.0070 -0.0303 0.0378  165 ALA B CA  
3015 C  C   . ALA B 165 ? 0.2437 0.0971 0.2170 -0.0104 -0.0241 0.0289  165 ALA B C   
3016 O  O   . ALA B 165 ? 0.2196 0.1285 0.2349 -0.0175 -0.0355 0.0158  165 ALA B O   
3017 C  CB  . ALA B 165 ? 0.2716 0.1370 0.1900 -0.0385 -0.0266 0.0043  165 ALA B CB  
3018 N  N   . PHE B 166 ? 0.2950 0.0966 0.2335 -0.0123 -0.0344 0.0387  166 PHE B N   
3019 C  CA  . PHE B 166 ? 0.2942 0.0851 0.2152 0.0123  -0.0530 -0.0044 166 PHE B CA  
3020 C  C   . PHE B 166 ? 0.3019 0.0939 0.2228 0.0298  -0.0369 0.0029  166 PHE B C   
3021 O  O   . PHE B 166 ? 0.2976 0.1079 0.2086 0.0076  -0.0262 0.0032  166 PHE B O   
3022 C  CB  . PHE B 166 ? 0.2821 0.0790 0.2432 0.0264  -0.0229 0.0071  166 PHE B CB  
3023 C  CG  . PHE B 166 ? 0.3091 0.0894 0.2290 0.0307  -0.0289 -0.0022 166 PHE B CG  
3024 C  CD1 . PHE B 166 ? 0.3134 0.1260 0.2608 0.0240  -0.0515 0.0221  166 PHE B CD1 
3025 C  CD2 . PHE B 166 ? 0.3372 0.0884 0.2174 -0.0155 -0.0363 -0.0129 166 PHE B CD2 
3026 C  CE1 . PHE B 166 ? 0.3403 0.1205 0.2604 0.0173  -0.0688 0.0151  166 PHE B CE1 
3027 C  CE2 . PHE B 166 ? 0.3720 0.1592 0.2145 0.0094  -0.0275 0.0048  166 PHE B CE2 
3028 C  CZ  . PHE B 166 ? 0.3784 0.1276 0.2753 -0.0304 -0.0783 0.0379  166 PHE B CZ  
3029 N  N   . PHE B 167 ? 0.2774 0.0964 0.2494 -0.0146 -0.0262 0.0113  167 PHE B N   
3030 C  CA  . PHE B 167 ? 0.2699 0.1382 0.2724 -0.0233 -0.0035 0.0030  167 PHE B CA  
3031 C  C   . PHE B 167 ? 0.2882 0.1791 0.2924 -0.0508 0.0345  -0.0479 167 PHE B C   
3032 O  O   . PHE B 167 ? 0.4257 0.1737 0.2545 -0.0104 0.0361  -0.0071 167 PHE B O   
3033 C  CB  . PHE B 167 ? 0.2670 0.1205 0.3153 -0.0234 -0.0180 0.0512  167 PHE B CB  
3034 C  CG  . PHE B 167 ? 0.2651 0.1152 0.3537 -0.0138 0.0258  0.0413  167 PHE B CG  
3035 C  CD1 . PHE B 167 ? 0.3379 0.1410 0.4080 -0.0605 0.0222  0.0838  167 PHE B CD1 
3036 C  CD2 . PHE B 167 ? 0.4418 0.1324 0.4143 0.0018  -0.1125 0.0141  167 PHE B CD2 
3037 C  CE1 . PHE B 167 ? 0.4866 0.1397 0.4846 -0.0715 -0.1260 0.1006  167 PHE B CE1 
3038 C  CE2 . PHE B 167 ? 0.5381 0.1595 0.4733 -0.0909 -0.1942 0.0329  167 PHE B CE2 
3039 C  CZ  . PHE B 167 ? 0.5596 0.1574 0.5224 -0.0601 -0.1583 0.0622  167 PHE B CZ  
3040 N  N   . THR B 168 ? 0.2640 0.1019 0.2292 0.0030  -0.0347 -0.0105 168 THR B N   
3041 C  CA  . THR B 168 ? 0.2875 0.1203 0.2174 0.0001  -0.0233 -0.0344 168 THR B CA  
3042 C  C   . THR B 168 ? 0.2961 0.1126 0.2150 -0.0335 -0.0170 0.0024  168 THR B C   
3043 O  O   . THR B 168 ? 0.2792 0.1140 0.2178 0.0125  -0.0298 0.0053  168 THR B O   
3044 C  CB  . THR B 168 ? 0.2849 0.1006 0.2946 0.0122  0.0231  0.0003  168 THR B CB  
3045 O  OG1 . THR B 168 ? 0.2793 0.1152 0.2704 0.0159  -0.0107 -0.0401 168 THR B OG1 
3046 C  CG2 . THR B 168 ? 0.3111 0.1304 0.2733 -0.0027 -0.0492 -0.0073 168 THR B CG2 
3047 N  N   . PHE B 169 ? 0.2904 0.1440 0.2234 0.0090  -0.0404 -0.0059 169 PHE B N   
3048 C  CA  . PHE B 169 ? 0.2988 0.1250 0.2359 -0.0068 -0.0494 0.0327  169 PHE B CA  
3049 C  C   . PHE B 169 ? 0.3047 0.1159 0.2154 0.0160  -0.0417 0.0180  169 PHE B C   
3050 O  O   . PHE B 169 ? 0.2954 0.1416 0.2175 0.0334  -0.0242 0.0146  169 PHE B O   
3051 C  CB  . PHE B 169 ? 0.3157 0.1276 0.2476 0.0171  -0.0588 0.0406  169 PHE B CB  
3052 C  CG  . PHE B 169 ? 0.3621 0.1109 0.1894 0.0059  -0.0188 0.0110  169 PHE B CG  
3053 C  CD1 . PHE B 169 ? 0.3699 0.1489 0.2399 -0.0094 -0.0339 0.0401  169 PHE B CD1 
3054 C  CD2 . PHE B 169 ? 0.3608 0.0828 0.2533 -0.0004 -0.0556 0.0105  169 PHE B CD2 
3055 C  CE1 . PHE B 169 ? 0.3511 0.1583 0.2504 -0.0251 -0.0368 0.0681  169 PHE B CE1 
3056 C  CE2 . PHE B 169 ? 0.3398 0.0769 0.3065 -0.0314 -0.0733 0.0099  169 PHE B CE2 
3057 C  CZ  . PHE B 169 ? 0.3426 0.1288 0.2377 -0.0366 -0.0611 0.0364  169 PHE B CZ  
3058 N  N   . PRO B 170 ? 0.2986 0.1037 0.2097 0.0043  -0.0576 0.0100  170 PRO B N   
3059 C  CA  . PRO B 170 ? 0.3036 0.1112 0.2245 0.0254  -0.0433 0.0187  170 PRO B CA  
3060 C  C   . PRO B 170 ? 0.3483 0.0751 0.2191 0.0330  -0.0568 0.0002  170 PRO B C   
3061 O  O   . PRO B 170 ? 0.3929 0.0891 0.2232 0.0623  -0.0348 -0.0087 170 PRO B O   
3062 C  CB  . PRO B 170 ? 0.3007 0.0782 0.2211 0.0150  -0.0476 0.0012  170 PRO B CB  
3063 C  CG  . PRO B 170 ? 0.2602 0.0614 0.2173 -0.0007 -0.0690 0.0052  170 PRO B CG  
3064 C  CD  . PRO B 170 ? 0.3011 0.0897 0.1849 0.0025  -0.0882 0.0275  170 PRO B CD  
3065 N  N   . ASN B 171 ? 0.3464 0.0731 0.1969 0.0325  -0.0735 -0.0224 171 ASN B N   
3066 C  CA  . ASN B 171 ? 0.3672 0.0873 0.1946 -0.0061 -0.0705 0.0038  171 ASN B CA  
3067 C  C   . ASN B 171 ? 0.3317 0.1086 0.1954 0.0233  -0.0942 0.0248  171 ASN B C   
3068 O  O   . ASN B 171 ? 0.3729 0.1398 0.2361 0.0194  -0.1168 -0.0286 171 ASN B O   
3069 C  CB  . ASN B 171 ? 0.3574 0.1072 0.2083 -0.0164 -0.0767 -0.0005 171 ASN B CB  
3070 C  CG  . ASN B 171 ? 0.3341 0.0938 0.2006 0.0110  -0.0852 -0.0249 171 ASN B CG  
3071 O  OD1 . ASN B 171 ? 0.3146 0.1285 0.2841 0.0278  -0.0207 -0.0346 171 ASN B OD1 
3072 N  ND2 . ASN B 171 ? 0.2610 0.1060 0.1877 0.0107  -0.0506 -0.0140 171 ASN B ND2 
3073 N  N   . ILE B 172 ? 0.3482 0.1288 0.2181 0.0287  -0.0548 0.0211  172 ILE B N   
3074 C  CA  . ILE B 172 ? 0.3567 0.1533 0.2177 0.0516  -0.0597 0.0245  172 ILE B CA  
3075 C  C   . ILE B 172 ? 0.3707 0.1713 0.2180 0.0701  -0.0742 -0.0033 172 ILE B C   
3076 O  O   . ILE B 172 ? 0.3939 0.2128 0.3544 0.1019  -0.1514 -0.0267 172 ILE B O   
3077 C  CB  . ILE B 172 ? 0.3481 0.1454 0.2119 0.0536  0.0093  0.0018  172 ILE B CB  
3078 C  CG1 . ILE B 172 ? 0.3072 0.1056 0.2816 0.0123  -0.0372 -0.0009 172 ILE B CG1 
3079 C  CG2 . ILE B 172 ? 0.4648 0.1402 0.1728 0.0576  -0.0056 -0.0289 172 ILE B CG2 
3080 C  CD1 . ILE B 172 ? 0.4474 0.1123 0.2950 0.0380  -0.0142 0.0307  172 ILE B CD1 
3081 N  N   . ALA B 173 ? 0.4094 0.1246 0.2967 0.0515  -0.0662 0.0211  173 ALA B N   
3082 C  CA  . ALA B 173 ? 0.4481 0.1829 0.2685 0.0916  -0.0641 -0.0173 173 ALA B CA  
3083 C  C   . ALA B 173 ? 0.4735 0.2662 0.3075 0.1250  -0.0278 0.0168  173 ALA B C   
3084 O  O   . ALA B 173 ? 0.4831 0.3068 0.3119 0.1546  -0.0025 0.0218  173 ALA B O   
3085 C  CB  . ALA B 173 ? 0.5046 0.2095 0.2666 0.0932  -0.0229 -0.0977 173 ALA B CB  
3086 N  N   . SER B 174 ? 0.5128 0.3427 0.2961 0.1890  0.0104  0.0479  174 SER B N   
3087 C  CA  . SER B 174 ? 0.5488 0.3200 0.2763 0.2749  0.0754  -0.0039 174 SER B CA  
3088 C  C   . SER B 174 ? 0.4859 0.3169 0.2466 0.2503  0.0935  0.0113  174 SER B C   
3089 O  O   . SER B 174 ? 0.5316 0.3515 0.2503 0.2158  0.0226  0.0872  174 SER B O   
3090 C  CB  . SER B 174 ? 0.7260 0.4229 0.3692 0.3601  0.0568  -0.1304 174 SER B CB  
3091 O  OG  . SER B 174 ? 0.9704 0.5645 0.3031 0.4208  0.0972  -0.0841 174 SER B OG  
3092 N  N   . ALA B 175 ? 0.5429 0.3538 0.3248 0.2076  0.0113  0.0657  175 ALA B N   
3093 C  CA  . ALA B 175 ? 0.5301 0.3461 0.3288 0.1889  -0.0318 0.0584  175 ALA B CA  
3094 C  C   . ALA B 175 ? 0.5133 0.3437 0.3316 0.2132  -0.0291 0.0392  175 ALA B C   
3095 O  O   . ALA B 175 ? 0.5879 0.3634 0.3492 0.2547  -0.0306 0.0897  175 ALA B O   
3096 C  CB  . ALA B 175 ? 0.5371 0.3834 0.3424 0.1704  -0.0528 0.0797  175 ALA B CB  
3097 N  N   . THR B 176 ? 0.5778 0.3870 0.3458 0.2268  0.0612  0.0867  176 THR B N   
3098 C  CA  . THR B 176 ? 0.5939 0.5002 0.3351 0.2387  0.0971  0.1342  176 THR B CA  
3099 C  C   . THR B 176 ? 0.6200 0.3998 0.2811 0.2398  0.0672  0.1365  176 THR B C   
3100 O  O   . THR B 176 ? 0.6220 0.3983 0.2329 0.2556  0.1004  0.1318  176 THR B O   
3101 C  CB  . THR B 176 ? 0.6537 0.6315 0.3381 0.2915  0.1527  0.1467  176 THR B CB  
3102 O  OG1 . THR B 176 ? 0.6023 0.8908 0.4502 0.2796  0.1331  0.2084  176 THR B OG1 
3103 C  CG2 . THR B 176 ? 0.7832 0.7313 0.3651 0.4087  0.0925  0.0774  176 THR B CG2 
3104 N  N   . LYS B 177 ? 0.7214 0.3224 0.2573 0.2427  0.0053  0.0683  177 LYS B N   
3105 C  CA  . LYS B 177 ? 0.7789 0.2676 0.2913 0.2130  -0.0068 -0.0210 177 LYS B CA  
3106 C  C   . LYS B 177 ? 0.7073 0.2489 0.2441 0.1670  -0.0089 0.0161  177 LYS B C   
3107 O  O   . LYS B 177 ? 0.8089 0.2483 0.2513 0.2425  -0.0782 -0.0175 177 LYS B O   
3108 C  CB  . LYS B 177 ? 0.9390 0.2545 0.3754 0.2203  -0.0374 -0.0309 177 LYS B CB  
3109 C  CG  . LYS B 177 ? 1.1141 0.4027 0.5375 0.3990  -0.0582 -0.1564 177 LYS B CG  
3110 C  CD  . LYS B 177 ? 1.2220 0.5057 0.5834 0.4905  -0.0979 -0.1084 177 LYS B CD  
3111 C  CE  . LYS B 177 ? 1.2599 0.6013 0.7840 0.6394  -0.1001 -0.1617 177 LYS B CE  
3112 N  NZ  . LYS B 177 ? 1.5277 0.7582 1.0128 0.7900  -0.2200 -0.1125 177 LYS B NZ  
3113 N  N   . PHE B 178 ? 0.6476 0.2387 0.1984 0.1794  0.0010  0.0614  178 PHE B N   
3114 C  CA  . PHE B 178 ? 0.5260 0.2249 0.2450 0.1010  -0.0323 0.0100  178 PHE B CA  
3115 C  C   . PHE B 178 ? 0.4879 0.2042 0.2386 0.1132  -0.0331 -0.0168 178 PHE B C   
3116 O  O   . PHE B 178 ? 0.4952 0.2779 0.2506 0.1298  -0.0493 -0.0153 178 PHE B O   
3117 C  CB  . PHE B 178 ? 0.4235 0.2765 0.2388 0.1129  -0.0106 0.0066  178 PHE B CB  
3118 C  CG  . PHE B 178 ? 0.3467 0.2312 0.2423 0.0845  -0.0614 0.0137  178 PHE B CG  
3119 C  CD1 . PHE B 178 ? 0.3791 0.2367 0.2985 0.0602  -0.0443 0.0236  178 PHE B CD1 
3120 C  CD2 . PHE B 178 ? 0.3636 0.2358 0.2508 0.0488  -0.0577 -0.0272 178 PHE B CD2 
3121 C  CE1 . PHE B 178 ? 0.3693 0.1964 0.2234 0.0290  -0.0329 0.0373  178 PHE B CE1 
3122 C  CE2 . PHE B 178 ? 0.3305 0.1840 0.2274 0.0215  -0.0862 -0.0210 178 PHE B CE2 
3123 C  CZ  . PHE B 178 ? 0.3765 0.2027 0.2258 0.0001  -0.0438 -0.0202 178 PHE B CZ  
3124 N  N   . LYS B 179 ? 0.5075 0.2541 0.2467 0.1154  0.0016  0.0250  179 LYS B N   
3125 C  CA  . LYS B 179 ? 0.5736 0.2615 0.2724 0.0995  -0.0325 0.0447  179 LYS B CA  
3126 C  C   . LYS B 179 ? 0.5956 0.2337 0.2979 0.0950  -0.0610 0.0474  179 LYS B C   
3127 O  O   . LYS B 179 ? 0.7055 0.2616 0.2576 0.1507  -0.0563 0.0559  179 LYS B O   
3128 C  CB  . LYS B 179 ? 0.5839 0.3362 0.2780 0.0690  -0.0855 0.1420  179 LYS B CB  
3129 C  CG  . LYS B 179 ? 0.5969 0.3618 0.3749 0.0710  -0.0840 0.0425  179 LYS B CG  
3130 C  CD  . LYS B 179 ? 0.6439 0.5398 0.5450 -0.0352 -0.1317 0.0896  179 LYS B CD  
3131 C  CE  . LYS B 179 ? 0.5053 0.6582 0.5978 -0.0536 -0.1933 0.0647  179 LYS B CE  
3132 N  NZ  . LYS B 179 ? 0.5941 0.9955 0.5705 -0.2233 -0.1636 -0.1613 179 LYS B NZ  
3133 N  N   . GLN B 180 ? 0.5994 0.2776 0.2325 0.1385  -0.0063 0.0434  180 GLN B N   
3134 C  CA  . GLN B 180 ? 0.6623 0.2325 0.2428 0.1125  -0.0323 0.0624  180 GLN B CA  
3135 C  C   . GLN B 180 ? 0.6541 0.1847 0.2896 0.0869  -0.0676 0.0770  180 GLN B C   
3136 O  O   . GLN B 180 ? 0.6625 0.2558 0.2654 0.0556  -0.0871 0.0863  180 GLN B O   
3137 C  CB  . GLN B 180 ? 0.7819 0.2904 0.2925 0.1331  0.0236  -0.0004 180 GLN B CB  
3138 C  CG  . GLN B 180 ? 0.8042 0.5247 0.3680 0.1912  0.0670  -0.0836 180 GLN B CG  
3139 C  CD  . GLN B 180 ? 0.8503 0.5849 0.5816 0.2695  0.0079  -0.1377 180 GLN B CD  
3140 O  OE1 . GLN B 180 ? 0.8868 0.7576 0.9630 0.3102  0.1200  -0.2244 180 GLN B OE1 
3141 N  NE2 . GLN B 180 ? 0.9172 0.5523 0.8126 0.2639  -0.1242 -0.3367 180 GLN B NE2 
3142 N  N   . LEU B 181 ? 0.6163 0.1625 0.2296 0.0983  -0.0709 0.0251  181 LEU B N   
3143 C  CA  . LEU B 181 ? 0.6072 0.1391 0.2585 0.0950  -0.0890 0.0212  181 LEU B CA  
3144 C  C   . LEU B 181 ? 0.5670 0.1164 0.2458 0.0586  -0.1030 0.0271  181 LEU B C   
3145 O  O   . LEU B 181 ? 0.6029 0.1210 0.2609 0.0877  -0.1415 -0.0324 181 LEU B O   
3146 C  CB  . LEU B 181 ? 0.5626 0.1426 0.2979 0.1051  -0.0811 0.0523  181 LEU B CB  
3147 C  CG  . LEU B 181 ? 0.5254 0.2386 0.2214 0.0966  -0.1361 0.0250  181 LEU B CG  
3148 C  CD1 . LEU B 181 ? 0.6415 0.1562 0.4531 0.0837  -0.2803 -0.0309 181 LEU B CD1 
3149 C  CD2 . LEU B 181 ? 0.5877 0.2621 0.3118 0.1111  -0.0496 0.0805  181 LEU B CD2 
3150 N  N   . TYR B 182 ? 0.5777 0.1328 0.2540 0.0524  -0.1220 0.0294  182 TYR B N   
3151 C  CA  . TYR B 182 ? 0.5627 0.1420 0.2451 0.0494  -0.1319 0.0133  182 TYR B CA  
3152 C  C   . TYR B 182 ? 0.5468 0.1159 0.2629 0.0487  -0.1169 0.0174  182 TYR B C   
3153 O  O   . TYR B 182 ? 0.5192 0.1559 0.2804 0.0445  -0.1621 0.0021  182 TYR B O   
3154 C  CB  . TYR B 182 ? 0.4901 0.1778 0.2176 0.0121  -0.0595 0.0074  182 TYR B CB  
3155 C  CG  . TYR B 182 ? 0.4527 0.1480 0.2332 0.0085  -0.0820 0.0176  182 TYR B CG  
3156 C  CD1 . TYR B 182 ? 0.4573 0.1433 0.1937 0.0588  -0.1048 0.0183  182 TYR B CD1 
3157 C  CD2 . TYR B 182 ? 0.5100 0.1565 0.3244 -0.0113 -0.0544 0.0288  182 TYR B CD2 
3158 C  CE1 . TYR B 182 ? 0.4847 0.1506 0.2628 0.0623  -0.0905 -0.0073 182 TYR B CE1 
3159 C  CE2 . TYR B 182 ? 0.5113 0.1464 0.3768 0.0083  -0.0862 0.0177  182 TYR B CE2 
3160 C  CZ  . TYR B 182 ? 0.4236 0.1449 0.3668 0.0692  -0.1017 0.0063  182 TYR B CZ  
3161 O  OH  . TYR B 182 ? 0.5461 0.1649 0.4375 0.0520  -0.1045 -0.0685 182 TYR B OH  
3162 N  N   . ARG B 183 ? 0.5833 0.1934 0.2148 0.0799  -0.1266 -0.0033 183 ARG B N   
3163 C  CA  . ARG B 183 ? 0.5595 0.1881 0.2582 -0.0003 -0.1422 0.0355  183 ARG B CA  
3164 C  C   . ARG B 183 ? 0.5893 0.1700 0.2891 0.0109  -0.1802 0.0340  183 ARG B C   
3165 O  O   . ARG B 183 ? 0.5413 0.1894 0.2471 0.0408  -0.1175 0.0265  183 ARG B O   
3166 C  CB  . ARG B 183 ? 0.5783 0.1680 0.3290 0.0378  -0.1048 0.0775  183 ARG B CB  
3167 C  CG  . ARG B 183 ? 0.5948 0.2148 0.3858 -0.0341 -0.0534 0.0687  183 ARG B CG  
3168 C  CD  . ARG B 183 ? 0.5985 0.3225 0.4743 0.0221  -0.0151 0.1044  183 ARG B CD  
3169 N  NE  . ARG B 183 ? 0.5527 0.3806 0.5336 0.0841  -0.0185 0.0568  183 ARG B NE  
3170 C  CZ  . ARG B 183 ? 0.6201 0.4191 0.6187 0.1172  -0.0466 0.1388  183 ARG B CZ  
3171 N  NH1 . ARG B 183 ? 0.6524 0.4093 0.6379 0.1243  -0.0535 0.1680  183 ARG B NH1 
3172 N  NH2 . ARG B 183 ? 0.4821 0.4397 0.7923 0.1620  0.0163  0.0692  183 ARG B NH2 
3173 N  N   . SER B 184 ? 0.5814 0.1663 0.2534 0.0542  -0.1463 -0.0330 184 SER B N   
3174 C  CA  . SER B 184 ? 0.5927 0.1909 0.2731 0.0012  -0.1372 -0.0045 184 SER B CA  
3175 C  C   . SER B 184 ? 0.5808 0.1579 0.2614 0.0134  -0.1608 0.0259  184 SER B C   
3176 O  O   . SER B 184 ? 0.6411 0.1692 0.2768 0.0530  -0.1901 0.0146  184 SER B O   
3177 C  CB  A SER B 184 ? 0.6423 0.1897 0.3989 0.0267  -0.1648 -0.0642 184 SER B CB  
3178 C  CB  B SER B 184 ? 0.6178 0.1866 0.3859 0.0266  -0.1712 -0.0429 184 SER B CB  
3179 O  OG  A SER B 184 ? 0.5261 0.1794 0.3577 0.0200  -0.2467 0.0202  184 SER B OG  
3180 O  OG  B SER B 184 ? 0.6284 0.1542 0.2891 0.0351  -0.1552 -0.0161 184 SER B OG  
3181 N  N   . ARG B 185 ? 0.5537 0.1471 0.2610 0.0024  -0.1524 0.0186  185 ARG B N   
3182 C  CA  . ARG B 185 ? 0.5227 0.1625 0.2569 0.0311  -0.1764 0.0570  185 ARG B CA  
3183 C  C   . ARG B 185 ? 0.5018 0.1728 0.2806 0.0297  -0.1563 0.0867  185 ARG B C   
3184 O  O   . ARG B 185 ? 0.4887 0.1307 0.3548 0.0379  -0.1338 0.0104  185 ARG B O   
3185 C  CB  . ARG B 185 ? 0.5318 0.1133 0.2478 0.0436  -0.1739 0.0366  185 ARG B CB  
3186 C  CG  . ARG B 185 ? 0.5064 0.1250 0.2712 0.0315  -0.1706 0.0465  185 ARG B CG  
3187 C  CD  . ARG B 185 ? 0.5451 0.1817 0.2454 -0.0139 -0.1613 -0.0045 185 ARG B CD  
3188 N  NE  . ARG B 185 ? 0.4790 0.1378 0.2442 0.0180  -0.1957 -0.0301 185 ARG B NE  
3189 C  CZ  . ARG B 185 ? 0.4859 0.0929 0.2408 0.0127  -0.1967 -0.0207 185 ARG B CZ  
3190 N  NH1 . ARG B 185 ? 0.4371 0.1389 0.3000 0.0521  -0.1648 -0.0370 185 ARG B NH1 
3191 N  NH2 . ARG B 185 ? 0.5633 0.1110 0.3119 -0.0328 -0.2193 0.0066  185 ARG B NH2 
3192 N  N   . MET B 186 ? 0.4879 0.1448 0.2542 0.0512  -0.1369 0.0115  186 MET B N   
3193 C  CA  . MET B 186 ? 0.5151 0.1437 0.3063 0.0468  -0.1586 0.0177  186 MET B CA  
3194 C  C   . MET B 186 ? 0.5751 0.1210 0.3260 0.0183  -0.1907 0.0324  186 MET B C   
3195 O  O   . MET B 186 ? 0.5416 0.1610 0.2939 0.0257  -0.1565 0.0538  186 MET B O   
3196 C  CB  . MET B 186 ? 0.5439 0.1524 0.3786 0.0155  -0.1766 -0.0143 186 MET B CB  
3197 C  CG  . MET B 186 ? 0.6712 0.1586 0.4203 -0.0379 -0.2697 0.0500  186 MET B CG  
3198 S  SD  . MET B 186 ? 0.6105 0.5075 0.3659 -0.1653 -0.1012 -0.1041 186 MET B SD  
3199 C  CE  . MET B 186 ? 0.5339 0.4112 0.8102 0.0388  -0.1192 -0.3985 186 MET B CE  
3200 N  N   . ASN B 187 ? 0.6062 0.1439 0.2819 0.0520  -0.1676 0.0714  187 ASN B N   
3201 C  CA  . ASN B 187 ? 0.6252 0.2022 0.2958 0.0697  -0.1896 0.0725  187 ASN B CA  
3202 C  C   . ASN B 187 ? 0.6447 0.1324 0.3581 0.0666  -0.2194 0.0272  187 ASN B C   
3203 O  O   . ASN B 187 ? 0.6579 0.2530 0.3635 0.0537  -0.2329 0.0418  187 ASN B O   
3204 C  CB  . ASN B 187 ? 0.6466 0.2277 0.2881 0.0571  -0.2225 0.0024  187 ASN B CB  
3205 C  CG  . ASN B 187 ? 0.6565 0.2309 0.2859 0.0409  -0.1473 0.0714  187 ASN B CG  
3206 O  OD1 . ASN B 187 ? 0.6103 0.2897 0.3497 0.0131  -0.0454 -0.0474 187 ASN B OD1 
3207 N  ND2 . ASN B 187 ? 0.6562 0.1908 0.4202 0.0396  -0.1609 0.0839  187 ASN B ND2 
3208 N  N   . SER B 188 ? 0.6498 0.1558 0.4141 0.0091  -0.2442 0.0608  188 SER B N   
3209 C  CA  . SER B 188 ? 0.6682 0.1529 0.4611 -0.0182 -0.2735 0.0463  188 SER B CA  
3210 C  C   . SER B 188 ? 0.6123 0.1669 0.4606 -0.0391 -0.2643 0.0471  188 SER B C   
3211 O  O   . SER B 188 ? 0.6081 0.1931 0.5254 -0.0699 -0.2497 0.0670  188 SER B O   
3212 C  CB  . SER B 188 ? 0.6582 0.1772 0.4342 -0.0164 -0.2565 0.0521  188 SER B CB  
3213 O  OG  . SER B 188 ? 0.7413 0.1945 0.4288 0.0570  -0.2985 0.0454  188 SER B OG  
3214 N  N   . LEU B 189 ? 0.6326 0.1334 0.4594 -0.0383 -0.2597 0.0583  189 LEU B N   
3215 C  CA  . LEU B 189 ? 0.5501 0.1514 0.4990 -0.0606 -0.2532 0.0489  189 LEU B CA  
3216 C  C   . LEU B 189 ? 0.6422 0.1627 0.5151 -0.0119 -0.3005 0.0177  189 LEU B C   
3217 O  O   . LEU B 189 ? 0.6731 0.2286 0.5470 0.0171  -0.3017 0.1143  189 LEU B O   
3218 C  CB  . LEU B 189 ? 0.6448 0.2363 0.5005 -0.0560 -0.2798 -0.0361 189 LEU B CB  
3219 C  CG  . LEU B 189 ? 0.7162 0.3546 0.4707 -0.0928 -0.3000 0.0551  189 LEU B CG  
3220 C  CD1 . LEU B 189 ? 0.7081 0.1271 0.5416 0.0360  -0.3254 0.0580  189 LEU B CD1 
3221 C  CD2 . LEU B 189 ? 0.6655 0.2836 0.3474 0.0755  -0.2615 0.1244  189 LEU B CD2 
3222 N  N   . GLU B 190 ? 0.6043 0.1238 0.6693 -0.0644 -0.3130 0.0986  190 GLU B N   
3223 C  CA  . GLU B 190 ? 0.7396 0.1629 0.7426 0.0314  -0.3756 0.0825  190 GLU B CA  
3224 C  C   . GLU B 190 ? 0.6201 0.1865 0.6292 0.0370  -0.2195 0.0919  190 GLU B C   
3225 O  O   . GLU B 190 ? 0.4783 0.3017 0.6557 -0.0540 -0.1287 0.1174  190 GLU B O   
3226 C  CB  . GLU B 190 ? 0.7809 0.1828 0.8187 0.0180  -0.4892 0.1644  190 GLU B CB  
3227 C  CG  . GLU B 190 ? 1.0284 0.1551 0.8561 -0.0416 -0.4586 0.1132  190 GLU B CG  
3228 C  CD  . GLU B 190 ? 1.0845 0.2820 0.9022 -0.1287 -0.4197 0.0666  190 GLU B CD  
3229 O  OE1 . GLU B 190 ? 1.0337 0.6205 0.9942 -0.1644 -0.4771 0.0371  190 GLU B OE1 
3230 O  OE2 . GLU B 190 ? 1.0849 0.7444 0.9489 -0.2736 -0.2410 0.1546  190 GLU B OE2 
3231 N  N   . MET B 191 ? 0.5823 0.1527 0.5126 0.0030  -0.2862 0.0243  191 MET B N   
3232 C  CA  . MET B 191 ? 0.5293 0.1645 0.4122 0.0048  -0.2237 0.0110  191 MET B CA  
3233 C  C   . MET B 191 ? 0.5360 0.1660 0.4324 -0.0054 -0.2097 0.0293  191 MET B C   
3234 O  O   . MET B 191 ? 0.6036 0.1905 0.4031 0.0135  -0.2502 0.0187  191 MET B O   
3235 C  CB  . MET B 191 ? 0.5536 0.1896 0.4666 -0.0262 -0.2454 0.0210  191 MET B CB  
3236 C  CG  . MET B 191 ? 0.5353 0.1527 0.5589 -0.0110 -0.2658 -0.0817 191 MET B CG  
3237 S  SD  . MET B 191 ? 0.5582 0.1917 0.4500 -0.0421 -0.2558 0.0289  191 MET B SD  
3238 C  CE  . MET B 191 ? 0.6349 0.2332 0.3819 0.0702  -0.0355 0.0247  191 MET B CE  
3239 N  N   . THR B 192 ? 0.5765 0.1322 0.4705 -0.0288 -0.2105 0.0270  192 THR B N   
3240 C  CA  . THR B 192 ? 0.5254 0.1357 0.4677 -0.0338 -0.2262 0.0203  192 THR B CA  
3241 C  C   . THR B 192 ? 0.4994 0.1792 0.3534 -0.0272 -0.2461 0.0004  192 THR B C   
3242 O  O   . THR B 192 ? 0.5202 0.1351 0.4215 0.0293  -0.2899 0.0053  192 THR B O   
3243 C  CB  . THR B 192 ? 0.5162 0.1311 0.5840 -0.0409 -0.1585 0.0770  192 THR B CB  
3244 O  OG1 . THR B 192 ? 0.4543 0.1439 0.5621 0.0302  -0.1128 0.0406  192 THR B OG1 
3245 C  CG2 . THR B 192 ? 0.5088 0.2053 0.7424 -0.0555 -0.1798 0.1284  192 THR B CG2 
3246 N  N   . PRO B 193 ? 0.5777 0.2007 0.3847 -0.0608 -0.2652 0.0406  193 PRO B N   
3247 C  CA  . PRO B 193 ? 0.5961 0.1315 0.3960 -0.0462 -0.2491 0.0432  193 PRO B CA  
3248 C  C   . PRO B 193 ? 0.5332 0.1595 0.4519 0.0070  -0.2835 -0.0073 193 PRO B C   
3249 O  O   . PRO B 193 ? 0.5141 0.1467 0.4569 -0.0046 -0.2426 0.0063  193 PRO B O   
3250 C  CB  . PRO B 193 ? 0.6714 0.2276 0.4176 -0.1116 -0.2958 0.0841  193 PRO B CB  
3251 C  CG  . PRO B 193 ? 0.6344 0.1940 0.4088 -0.0990 -0.2842 0.1147  193 PRO B CG  
3252 C  CD  . PRO B 193 ? 0.5891 0.1661 0.3835 -0.0255 -0.2726 0.0655  193 PRO B CD  
3253 N  N   . ALA B 194 ? 0.5008 0.1055 0.5195 -0.0254 -0.2697 0.0214  194 ALA B N   
3254 C  CA  . ALA B 194 ? 0.5929 0.1128 0.4537 0.0525  -0.2950 0.0271  194 ALA B CA  
3255 C  C   . ALA B 194 ? 0.5611 0.1401 0.4852 -0.0135 -0.2971 0.0849  194 ALA B C   
3256 O  O   . ALA B 194 ? 0.4986 0.1209 0.4379 0.0217  -0.2443 0.0547  194 ALA B O   
3257 C  CB  . ALA B 194 ? 0.6033 0.2175 0.4981 0.0887  -0.2872 0.0049  194 ALA B CB  
3258 N  N   . VAL B 195 ? 0.3904 0.2002 0.4162 0.0083  -0.1732 0.0659  195 VAL B N   
3259 C  CA  . VAL B 195 ? 0.4179 0.1379 0.4072 0.0036  -0.1949 0.0427  195 VAL B CA  
3260 C  C   . VAL B 195 ? 0.4346 0.1119 0.3747 0.0101  -0.1902 0.0342  195 VAL B C   
3261 O  O   . VAL B 195 ? 0.4037 0.1437 0.3723 0.0015  -0.1700 0.0207  195 VAL B O   
3262 C  CB  . VAL B 195 ? 0.4136 0.1702 0.4162 -0.0140 -0.2277 0.0664  195 VAL B CB  
3263 C  CG1 . VAL B 195 ? 0.4300 0.1844 0.5205 -0.0301 -0.2602 0.1260  195 VAL B CG1 
3264 C  CG2 . VAL B 195 ? 0.4112 0.2230 0.5581 0.0073  -0.1679 0.1239  195 VAL B CG2 
3265 N  N   . ARG B 196 ? 0.4601 0.1060 0.3991 -0.0061 -0.1999 0.0148  196 ARG B N   
3266 C  CA  . ARG B 196 ? 0.4771 0.1295 0.3689 0.0079  -0.1955 0.0014  196 ARG B CA  
3267 C  C   . ARG B 196 ? 0.4593 0.1539 0.3291 0.0057  -0.1804 0.0249  196 ARG B C   
3268 O  O   . ARG B 196 ? 0.4737 0.1736 0.3189 -0.0047 -0.1952 0.0480  196 ARG B O   
3269 C  CB  . ARG B 196 ? 0.4528 0.1916 0.3091 -0.0454 -0.1641 0.0383  196 ARG B CB  
3270 C  CG  . ARG B 196 ? 0.4876 0.3727 0.4710 0.0014  -0.1379 -0.1109 196 ARG B CG  
3271 C  CD  . ARG B 196 ? 0.5683 0.5765 0.4916 0.1010  -0.1655 -0.1689 196 ARG B CD  
3272 N  NE  . ARG B 196 ? 0.6329 0.6310 0.4998 0.1753  -0.1702 -0.1779 196 ARG B NE  
3273 C  CZ  . ARG B 196 ? 0.5919 0.6751 0.5768 0.2481  -0.2577 0.0156  196 ARG B CZ  
3274 N  NH1 . ARG B 196 ? 0.8590 0.7918 0.5659 0.2872  -0.1644 0.3297  196 ARG B NH1 
3275 N  NH2 . ARG B 196 ? 0.6543 0.7850 0.6577 0.3244  -0.2343 -0.0734 196 ARG B NH2 
3276 N  N   . GLN B 197 ? 0.4079 0.1656 0.3128 0.0137  -0.1338 0.0389  197 GLN B N   
3277 C  CA  . GLN B 197 ? 0.4135 0.1698 0.3932 0.0088  -0.1536 0.0392  197 GLN B CA  
3278 C  C   . GLN B 197 ? 0.3974 0.1338 0.4144 0.0315  -0.1434 0.0037  197 GLN B C   
3279 O  O   . GLN B 197 ? 0.3925 0.1589 0.3650 0.0038  -0.1109 0.0144  197 GLN B O   
3280 C  CB  . GLN B 197 ? 0.5218 0.1536 0.4497 -0.0108 -0.1725 0.0611  197 GLN B CB  
3281 C  CG  . GLN B 197 ? 0.5666 0.1934 0.4582 -0.0576 -0.1272 0.0376  197 GLN B CG  
3282 C  CD  . GLN B 197 ? 0.5975 0.4199 0.4737 -0.1168 -0.0564 -0.0440 197 GLN B CD  
3283 O  OE1 . GLN B 197 ? 0.6651 0.5408 0.4412 0.0578  -0.1495 -0.0603 197 GLN B OE1 
3284 N  NE2 . GLN B 197 ? 0.5964 0.7488 0.4739 -0.2112 -0.0333 -0.0976 197 GLN B NE2 
3285 N  N   . ARG B 198 ? 0.3722 0.1672 0.3590 -0.0233 -0.1703 0.0826  198 ARG B N   
3286 C  CA  . ARG B 198 ? 0.3619 0.1082 0.3812 -0.0079 -0.1633 0.0461  198 ARG B CA  
3287 C  C   . ARG B 198 ? 0.4086 0.1020 0.2851 0.0443  -0.1333 -0.0103 198 ARG B C   
3288 O  O   . ARG B 198 ? 0.3407 0.1195 0.3032 -0.0007 -0.1196 0.0192  198 ARG B O   
3289 C  CB  . ARG B 198 ? 0.3636 0.1253 0.4099 0.0128  -0.1570 0.0604  198 ARG B CB  
3290 C  CG  . ARG B 198 ? 0.4524 0.1545 0.4278 0.0698  -0.2103 0.0449  198 ARG B CG  
3291 C  CD  . ARG B 198 ? 0.4605 0.1494 0.4403 0.0583  -0.2264 -0.0228 198 ARG B CD  
3292 N  NE  . ARG B 198 ? 0.4329 0.1407 0.4688 0.0820  -0.2238 0.0313  198 ARG B NE  
3293 C  CZ  . ARG B 198 ? 0.4301 0.1394 0.5006 0.0826  -0.2382 0.0345  198 ARG B CZ  
3294 N  NH1 . ARG B 198 ? 0.5858 0.0919 0.4072 0.0764  -0.2521 -0.0306 198 ARG B NH1 
3295 N  NH2 . ARG B 198 ? 0.4841 0.1690 0.5859 0.0319  -0.2611 -0.0277 198 ARG B NH2 
3296 N  N   . VAL B 199 ? 0.3975 0.0979 0.2874 0.0215  -0.1206 0.0127  199 VAL B N   
3297 C  CA  . VAL B 199 ? 0.3981 0.0981 0.2890 0.0270  -0.1495 -0.0073 199 VAL B CA  
3298 C  C   . VAL B 199 ? 0.4095 0.1205 0.3389 0.0433  -0.1205 0.0371  199 VAL B C   
3299 O  O   . VAL B 199 ? 0.3740 0.1443 0.3187 -0.0059 -0.1047 0.0368  199 VAL B O   
3300 C  CB  . VAL B 199 ? 0.4666 0.0958 0.3311 0.0292  -0.2266 0.0057  199 VAL B CB  
3301 C  CG1 . VAL B 199 ? 0.4991 0.1080 0.3689 0.0567  -0.2399 -0.0048 199 VAL B CG1 
3302 C  CG2 . VAL B 199 ? 0.4387 0.1223 0.5012 -0.0192 -0.2425 0.0117  199 VAL B CG2 
3303 N  N   . ILE B 200 ? 0.3919 0.1263 0.3210 0.0285  -0.1365 -0.0091 200 ILE B N   
3304 C  CA  . ILE B 200 ? 0.4064 0.1356 0.3420 0.0003  -0.1327 0.0546  200 ILE B CA  
3305 C  C   . ILE B 200 ? 0.4235 0.1601 0.3707 -0.0154 -0.1231 0.0366  200 ILE B C   
3306 O  O   . ILE B 200 ? 0.4253 0.1360 0.3348 -0.0222 -0.1188 0.0436  200 ILE B O   
3307 C  CB  . ILE B 200 ? 0.4472 0.2602 0.3364 -0.0260 -0.1311 0.0574  200 ILE B CB  
3308 C  CG1 . ILE B 200 ? 0.6422 0.3215 0.3559 -0.0461 -0.0442 -0.0371 200 ILE B CG1 
3309 C  CG2 . ILE B 200 ? 0.4097 0.4352 0.3461 0.0364  -0.0236 -0.1000 200 ILE B CG2 
3310 C  CD1 . ILE B 200 ? 0.7312 0.3513 0.6943 0.0138  0.1170  -0.1000 200 ILE B CD1 
3311 N  N   . GLU B 201 ? 0.4268 0.1440 0.3348 -0.0255 -0.1484 0.0344  201 GLU B N   
3312 C  CA  . GLU B 201 ? 0.3734 0.1585 0.3146 -0.0409 -0.1221 0.0399  201 GLU B CA  
3313 C  C   . GLU B 201 ? 0.3607 0.1597 0.3227 -0.0334 -0.1380 0.0462  201 GLU B C   
3314 O  O   . GLU B 201 ? 0.3660 0.1690 0.3324 -0.0370 -0.1339 0.0293  201 GLU B O   
3315 C  CB  . GLU B 201 ? 0.4702 0.1564 0.3157 -0.0057 -0.1812 0.0130  201 GLU B CB  
3316 C  CG  . GLU B 201 ? 0.7345 0.2538 0.3465 -0.0360 -0.2618 0.0746  201 GLU B CG  
3317 C  CD  . GLU B 201 ? 0.7652 0.2926 0.3916 -0.0396 -0.3354 0.0771  201 GLU B CD  
3318 O  OE1 . GLU B 201 ? 0.7824 0.2508 0.5683 0.0262  -0.2546 -0.0429 201 GLU B OE1 
3319 O  OE2 . GLU B 201 ? 0.9589 0.3142 0.5155 -0.1401 -0.4450 0.1843  201 GLU B OE2 
3320 N  N   . GLU B 202 ? 0.3805 0.1389 0.3175 -0.0363 -0.1571 0.0629  202 GLU B N   
3321 C  CA  . GLU B 202 ? 0.3750 0.1115 0.2976 0.0290  -0.1092 0.0080  202 GLU B CA  
3322 C  C   . GLU B 202 ? 0.3686 0.1192 0.2709 0.0277  -0.1239 -0.0075 202 GLU B C   
3323 O  O   . GLU B 202 ? 0.3972 0.1500 0.2480 0.0013  -0.1148 0.0344  202 GLU B O   
3324 C  CB  . GLU B 202 ? 0.3670 0.1609 0.2956 0.0274  -0.1258 0.0368  202 GLU B CB  
3325 C  CG  . GLU B 202 ? 0.3951 0.1293 0.2903 0.0087  -0.1308 0.0301  202 GLU B CG  
3326 C  CD  . GLU B 202 ? 0.4017 0.1115 0.3153 -0.0054 -0.1197 0.0340  202 GLU B CD  
3327 O  OE1 . GLU B 202 ? 0.3757 0.1397 0.3324 0.0131  -0.0901 0.0577  202 GLU B OE1 
3328 O  OE2 . GLU B 202 ? 0.3932 0.1310 0.2937 0.0208  -0.0825 0.0258  202 GLU B OE2 
3329 N  N   . ALA B 203 ? 0.3545 0.1177 0.2916 0.0049  -0.0630 -0.0002 203 ALA B N   
3330 C  CA  . ALA B 203 ? 0.3451 0.1441 0.2822 0.0052  -0.0436 0.0117  203 ALA B CA  
3331 C  C   . ALA B 203 ? 0.3527 0.1637 0.2578 -0.0022 -0.0668 0.0312  203 ALA B C   
3332 O  O   . ALA B 203 ? 0.3911 0.1722 0.2858 0.0092  -0.1034 0.0034  203 ALA B O   
3333 C  CB  . ALA B 203 ? 0.3902 0.1433 0.3494 0.0250  -0.0402 -0.0223 203 ALA B CB  
3334 N  N   . LYS B 204 ? 0.3978 0.1405 0.2681 0.0003  -0.0599 0.0254  204 LYS B N   
3335 C  CA  . LYS B 204 ? 0.3929 0.1368 0.2903 0.0088  -0.0912 0.0438  204 LYS B CA  
3336 C  C   . LYS B 204 ? 0.3889 0.1622 0.2957 -0.0404 -0.0564 0.0301  204 LYS B C   
3337 O  O   . LYS B 204 ? 0.3957 0.1749 0.3168 -0.0152 -0.0779 0.0112  204 LYS B O   
3338 C  CB  . LYS B 204 ? 0.4706 0.1924 0.3047 -0.0586 -0.1232 0.0770  204 LYS B CB  
3339 C  CG  . LYS B 204 ? 0.6047 0.2997 0.2992 -0.0469 0.0141  0.0844  204 LYS B CG  
3340 C  CD  . LYS B 204 ? 0.8820 0.4738 0.3444 0.0228  0.0234  0.1874  204 LYS B CD  
3341 C  CE  . LYS B 204 ? 1.1470 0.5017 0.4466 0.0406  -0.1813 0.2060  204 LYS B CE  
3342 N  NZ  . LYS B 204 ? 1.6993 0.6003 0.4077 0.0949  -0.1932 0.2139  204 LYS B NZ  
3343 N  N   . THR B 205 ? 0.3928 0.1210 0.2924 -0.0131 -0.0796 0.0420  205 THR B N   
3344 C  CA  . THR B 205 ? 0.3249 0.1091 0.3065 -0.0247 -0.0973 0.0218  205 THR B CA  
3345 C  C   . THR B 205 ? 0.3619 0.1142 0.2856 0.0443  -0.0849 -0.0152 205 THR B C   
3346 O  O   . THR B 205 ? 0.3265 0.1670 0.2731 0.0107  -0.0740 0.0014  205 THR B O   
3347 C  CB  . THR B 205 ? 0.3206 0.1808 0.2990 -0.0184 -0.1047 0.0411  205 THR B CB  
3348 O  OG1 . THR B 205 ? 0.4141 0.1656 0.3274 0.0474  -0.1414 0.0058  205 THR B OG1 
3349 C  CG2 . THR B 205 ? 0.3565 0.2090 0.3219 -0.0095 -0.0631 0.0285  205 THR B CG2 
3350 N  N   . ALA B 206 ? 0.3370 0.1237 0.2849 0.0225  -0.0709 0.0214  206 ALA B N   
3351 C  CA  . ALA B 206 ? 0.3161 0.1410 0.2626 -0.0195 -0.0788 0.0317  206 ALA B CA  
3352 C  C   . ALA B 206 ? 0.3137 0.1303 0.2343 -0.0121 -0.0632 0.0192  206 ALA B C   
3353 O  O   . ALA B 206 ? 0.2871 0.1399 0.2258 -0.0024 -0.0448 0.0204  206 ALA B O   
3354 C  CB  . ALA B 206 ? 0.3323 0.1355 0.2560 -0.0210 -0.1022 0.0408  206 ALA B CB  
3355 N  N   . PHE B 207 ? 0.3353 0.1575 0.2287 -0.0139 -0.0682 0.0148  207 PHE B N   
3356 C  CA  . PHE B 207 ? 0.3331 0.1358 0.2766 0.0036  -0.0289 -0.0305 207 PHE B CA  
3357 C  C   . PHE B 207 ? 0.3006 0.1389 0.2724 0.0230  -0.0565 -0.0367 207 PHE B C   
3358 O  O   . PHE B 207 ? 0.3260 0.2012 0.2692 -0.0224 -0.0724 0.0160  207 PHE B O   
3359 C  CB  . PHE B 207 ? 0.3593 0.1871 0.2647 0.0431  -0.0431 -0.0459 207 PHE B CB  
3360 C  CG  . PHE B 207 ? 0.3519 0.1730 0.2493 0.0427  -0.0396 -0.0204 207 PHE B CG  
3361 C  CD1 . PHE B 207 ? 0.3586 0.1845 0.4199 0.0494  -0.0348 0.0357  207 PHE B CD1 
3362 C  CD2 . PHE B 207 ? 0.4069 0.1639 0.2962 0.0083  -0.0611 -0.0007 207 PHE B CD2 
3363 C  CE1 . PHE B 207 ? 0.3669 0.1860 0.3893 0.0581  -0.0601 0.0352  207 PHE B CE1 
3364 C  CE2 . PHE B 207 ? 0.3930 0.1959 0.3440 0.0373  -0.0693 -0.0534 207 PHE B CE2 
3365 C  CZ  . PHE B 207 ? 0.4002 0.2085 0.3669 0.0326  -0.0629 0.0405  207 PHE B CZ  
3366 N  N   . LEU B 208 ? 0.3357 0.1282 0.2724 0.0009  -0.0496 0.0059  208 LEU B N   
3367 C  CA  . LEU B 208 ? 0.3234 0.1201 0.2715 -0.0074 -0.0384 0.0226  208 LEU B CA  
3368 C  C   . LEU B 208 ? 0.2871 0.1197 0.2636 -0.0184 -0.0598 0.0208  208 LEU B C   
3369 O  O   . LEU B 208 ? 0.3283 0.1737 0.3111 -0.0511 -0.0933 0.0234  208 LEU B O   
3370 C  CB  . LEU B 208 ? 0.4227 0.1156 0.3244 -0.0403 -0.1458 0.0442  208 LEU B CB  
3371 C  CG  . LEU B 208 ? 0.4251 0.2847 0.3781 -0.0995 -0.1209 0.1550  208 LEU B CG  
3372 C  CD1 . LEU B 208 ? 0.6428 0.5187 0.5000 0.0057  -0.2170 0.2760  208 LEU B CD1 
3373 C  CD2 . LEU B 208 ? 0.5279 0.4273 0.5144 -0.2596 -0.1176 0.1254  208 LEU B CD2 
3374 N  N   . LEU B 209 ? 0.3279 0.1398 0.2699 -0.0442 -0.0641 0.0471  209 LEU B N   
3375 C  CA  . LEU B 209 ? 0.2438 0.1508 0.2777 -0.0162 -0.0544 0.0278  209 LEU B CA  
3376 C  C   . LEU B 209 ? 0.2533 0.1514 0.2649 -0.0081 -0.0635 -0.0004 209 LEU B C   
3377 O  O   . LEU B 209 ? 0.2838 0.1623 0.2568 -0.0334 -0.0685 0.0159  209 LEU B O   
3378 C  CB  . LEU B 209 ? 0.2435 0.1036 0.3529 0.0102  -0.0083 -0.0049 209 LEU B CB  
3379 C  CG  . LEU B 209 ? 0.2490 0.1269 0.2788 0.0132  -0.0282 -0.0117 209 LEU B CG  
3380 C  CD1 . LEU B 209 ? 0.2640 0.1433 0.3003 -0.0028 -0.0601 -0.0035 209 LEU B CD1 
3381 C  CD2 . LEU B 209 ? 0.2623 0.1193 0.3536 0.0092  -0.0102 -0.0413 209 LEU B CD2 
3382 N  N   . ASN B 210 ? 0.3043 0.1083 0.3178 -0.0102 -0.0598 0.0045  210 ASN B N   
3383 C  CA  . ASN B 210 ? 0.2843 0.1318 0.3064 -0.0065 -0.0312 0.0198  210 ASN B CA  
3384 C  C   . ASN B 210 ? 0.3030 0.1583 0.2419 -0.0262 -0.0351 0.0039  210 ASN B C   
3385 O  O   . ASN B 210 ? 0.3505 0.1522 0.2551 -0.0380 -0.0651 -0.0031 210 ASN B O   
3386 C  CB  . ASN B 210 ? 0.3044 0.1164 0.2874 -0.0016 -0.0494 0.0380  210 ASN B CB  
3387 C  CG  . ASN B 210 ? 0.2763 0.1252 0.2515 0.0025  -0.0537 0.0253  210 ASN B CG  
3388 O  OD1 . ASN B 210 ? 0.3346 0.1620 0.2470 -0.0030 -0.0425 0.0442  210 ASN B OD1 
3389 N  ND2 . ASN B 210 ? 0.2564 0.1722 0.3379 0.0217  -0.0635 0.0278  210 ASN B ND2 
3390 N  N   . ILE B 211 ? 0.3248 0.1832 0.2273 -0.0270 -0.0074 -0.0029 211 ILE B N   
3391 C  CA  . ILE B 211 ? 0.3353 0.2265 0.2773 -0.0504 0.0239  -0.0047 211 ILE B CA  
3392 C  C   . ILE B 211 ? 0.3073 0.2042 0.2819 -0.0527 -0.0126 0.0052  211 ILE B C   
3393 O  O   . ILE B 211 ? 0.3211 0.1823 0.3701 -0.0295 -0.0678 0.0128  211 ILE B O   
3394 C  CB  . ILE B 211 ? 0.4092 0.2288 0.2809 -0.1249 -0.0070 -0.0002 211 ILE B CB  
3395 C  CG1 . ILE B 211 ? 0.4012 0.3144 0.2778 -0.1240 -0.0068 -0.0405 211 ILE B CG1 
3396 C  CG2 . ILE B 211 ? 0.4337 0.3105 0.2944 -0.1829 -0.0495 0.0220  211 ILE B CG2 
3397 C  CD1 . ILE B 211 ? 0.4024 0.3260 0.2714 -0.1032 0.0309  -0.0071 211 ILE B CD1 
3398 N  N   . GLN B 212 ? 0.2965 0.1796 0.2819 -0.0713 -0.0189 -0.0089 212 GLN B N   
3399 C  CA  . GLN B 212 ? 0.3387 0.1625 0.2558 -0.0415 -0.0385 0.0173  212 GLN B CA  
3400 C  C   . GLN B 212 ? 0.2747 0.1415 0.2782 -0.0643 -0.0673 0.0174  212 GLN B C   
3401 O  O   . GLN B 212 ? 0.3328 0.1417 0.2895 -0.0731 -0.0746 -0.0033 212 GLN B O   
3402 C  CB  A GLN B 212 ? 0.4066 0.1435 0.3241 0.0291  -0.0753 0.0443  212 GLN B CB  
3403 C  CB  B GLN B 212 ? 0.4035 0.1503 0.3312 0.0407  -0.0703 0.0389  212 GLN B CB  
3404 C  CG  A GLN B 212 ? 0.3794 0.1974 0.3859 0.0471  -0.0772 -0.0133 212 GLN B CG  
3405 C  CG  B GLN B 212 ? 0.4342 0.0792 0.3841 -0.0487 -0.0747 0.0705  212 GLN B CG  
3406 C  CD  A GLN B 212 ? 0.3801 0.1892 0.4471 -0.0110 -0.0669 -0.0546 212 GLN B CD  
3407 C  CD  B GLN B 212 ? 0.4758 0.1842 0.5138 0.0303  -0.1316 0.1354  212 GLN B CD  
3408 O  OE1 A GLN B 212 ? 0.4846 0.2083 0.6240 -0.1513 0.0540  0.1462  212 GLN B OE1 
3409 O  OE1 B GLN B 212 ? 0.3084 0.4332 0.6545 -0.0378 -0.0420 0.0191  212 GLN B OE1 
3410 N  NE2 A GLN B 212 ? 0.4571 0.1872 0.5840 -0.0133 -0.2105 -0.0134 212 GLN B NE2 
3411 N  NE2 B GLN B 212 ? 0.6664 0.3855 0.7228 0.0583  -0.3752 -0.0408 212 GLN B NE2 
3412 N  N   . LEU B 213 ? 0.2752 0.0987 0.2580 -0.0244 -0.0145 -0.0159 213 LEU B N   
3413 C  CA  . LEU B 213 ? 0.2783 0.1313 0.2697 -0.0317 -0.0110 0.0075  213 LEU B CA  
3414 C  C   . LEU B 213 ? 0.2800 0.1589 0.2583 -0.0226 -0.0200 -0.0103 213 LEU B C   
3415 O  O   . LEU B 213 ? 0.3136 0.1336 0.2691 -0.0286 -0.0423 -0.0028 213 LEU B O   
3416 C  CB  . LEU B 213 ? 0.2999 0.1317 0.2844 -0.0342 -0.0326 0.0169  213 LEU B CB  
3417 C  CG  . LEU B 213 ? 0.4030 0.0702 0.2910 0.0050  -0.0576 -0.0112 213 LEU B CG  
3418 C  CD1 . LEU B 213 ? 0.2688 0.1941 0.2788 -0.0068 -0.0434 0.0019  213 LEU B CD1 
3419 C  CD2 . LEU B 213 ? 0.3458 0.1155 0.3996 -0.0598 -0.0546 0.0176  213 LEU B CD2 
3420 N  N   . PHE B 214 ? 0.2779 0.1560 0.2893 -0.0384 -0.0074 -0.0289 214 PHE B N   
3421 C  CA  . PHE B 214 ? 0.2784 0.1345 0.3541 -0.0105 -0.0132 -0.0114 214 PHE B CA  
3422 C  C   . PHE B 214 ? 0.2332 0.1445 0.3127 -0.0032 -0.0073 -0.0013 214 PHE B C   
3423 O  O   . PHE B 214 ? 0.3343 0.2501 0.3140 -0.0633 -0.0817 0.0241  214 PHE B O   
3424 C  CB  . PHE B 214 ? 0.2728 0.2345 0.4324 -0.0223 -0.0061 -0.1025 214 PHE B CB  
3425 C  CG  . PHE B 214 ? 0.3135 0.2244 0.4404 -0.0160 -0.0260 -0.1042 214 PHE B CG  
3426 C  CD1 . PHE B 214 ? 0.4200 0.2086 0.4795 0.0088  0.0175  -0.0852 214 PHE B CD1 
3427 C  CD2 . PHE B 214 ? 0.4284 0.2382 0.4620 0.0118  -0.0811 -0.1166 214 PHE B CD2 
3428 C  CE1 . PHE B 214 ? 0.5713 0.2179 0.4663 -0.0247 -0.0311 -0.0770 214 PHE B CE1 
3429 C  CE2 . PHE B 214 ? 0.6066 0.2489 0.4496 -0.0405 -0.0936 -0.1047 214 PHE B CE2 
3430 C  CZ  . PHE B 214 ? 0.6756 0.2277 0.4809 0.0218  -0.1074 -0.0697 214 PHE B CZ  
3431 N  N   . GLU B 215 ? 0.2669 0.1398 0.3193 -0.0105 0.0011  0.0081  215 GLU B N   
3432 C  CA  . GLU B 215 ? 0.3485 0.1559 0.3180 -0.0479 -0.0237 0.0237  215 GLU B CA  
3433 C  C   . GLU B 215 ? 0.3115 0.1774 0.3270 -0.1048 -0.0187 0.0123  215 GLU B C   
3434 O  O   . GLU B 215 ? 0.2762 0.1810 0.3670 -0.0635 -0.0455 -0.0013 215 GLU B O   
3435 C  CB  . GLU B 215 ? 0.3508 0.1154 0.3350 -0.0024 -0.0338 -0.0238 215 GLU B CB  
3436 C  CG  . GLU B 215 ? 0.4665 0.2545 0.3006 -0.0822 -0.0308 0.0102  215 GLU B CG  
3437 C  CD  . GLU B 215 ? 0.4786 0.3738 0.3572 -0.0366 -0.0444 0.0575  215 GLU B CD  
3438 O  OE1 . GLU B 215 ? 0.5305 0.6201 0.4196 0.1033  -0.0162 0.1098  215 GLU B OE1 
3439 O  OE2 . GLU B 215 ? 0.4815 0.3438 0.3560 -0.0594 -0.0339 0.1021  215 GLU B OE2 
3440 N  N   . GLU B 216 ? 0.2704 0.1618 0.3215 -0.0535 -0.0440 0.0158  216 GLU B N   
3441 C  CA  . GLU B 216 ? 0.3264 0.1136 0.3375 -0.0265 -0.0087 0.0157  216 GLU B CA  
3442 C  C   . GLU B 216 ? 0.2876 0.0919 0.2630 -0.0434 0.0275  -0.0117 216 GLU B C   
3443 O  O   . GLU B 216 ? 0.3309 0.1349 0.3038 -0.0420 -0.0043 -0.0477 216 GLU B O   
3444 C  CB  . GLU B 216 ? 0.3112 0.1380 0.2910 -0.0485 -0.0477 -0.0303 216 GLU B CB  
3445 C  CG  . GLU B 216 ? 0.3127 0.1650 0.2956 -0.0542 -0.0452 -0.0511 216 GLU B CG  
3446 C  CD  . GLU B 216 ? 0.2973 0.1667 0.2995 -0.0153 -0.0485 0.0079  216 GLU B CD  
3447 O  OE1 . GLU B 216 ? 0.4080 0.1640 0.3585 -0.0597 -0.0259 0.0025  216 GLU B OE1 
3448 O  OE2 . GLU B 216 ? 0.2904 0.2583 0.3438 0.0224  -0.1042 -0.0684 216 GLU B OE2 
3449 N  N   . LEU B 217 ? 0.2716 0.0954 0.3425 -0.0214 -0.0130 -0.0295 217 LEU B N   
3450 C  CA  . LEU B 217 ? 0.2565 0.1191 0.3162 -0.0087 0.0124  -0.0194 217 LEU B CA  
3451 C  C   . LEU B 217 ? 0.2976 0.2081 0.2505 -0.0894 -0.0413 0.0430  217 LEU B C   
3452 O  O   . LEU B 217 ? 0.3622 0.1684 0.2885 -0.0250 -0.0894 -0.0088 217 LEU B O   
3453 C  CB  . LEU B 217 ? 0.3128 0.1201 0.3844 -0.0062 -0.1451 -0.0231 217 LEU B CB  
3454 C  CG  . LEU B 217 ? 0.3387 0.1405 0.3809 -0.0336 -0.1247 -0.0330 217 LEU B CG  
3455 C  CD1 . LEU B 217 ? 0.3876 0.1301 0.4131 -0.0440 -0.0692 0.0210  217 LEU B CD1 
3456 C  CD2 . LEU B 217 ? 0.3940 0.1727 0.3900 -0.0267 -0.0848 -0.0007 217 LEU B CD2 
3457 N  N   . GLN B 218 ? 0.3158 0.1674 0.2786 -0.0494 0.0157  0.0064  218 GLN B N   
3458 C  CA  . GLN B 218 ? 0.3240 0.2444 0.3602 -0.0629 0.0864  -0.0742 218 GLN B CA  
3459 C  C   . GLN B 218 ? 0.3405 0.2087 0.3799 -0.0582 -0.0203 -0.0399 218 GLN B C   
3460 O  O   . GLN B 218 ? 0.3106 0.2734 0.4509 -0.0906 -0.0173 -0.0156 218 GLN B O   
3461 C  CB  . GLN B 218 ? 0.3542 0.3251 0.3651 -0.0913 0.0889  -0.0453 218 GLN B CB  
3462 C  CG  . GLN B 218 ? 0.3561 0.3446 0.4115 -0.0784 0.1150  -0.0326 218 GLN B CG  
3463 C  CD  . GLN B 218 ? 0.3681 0.3957 0.4518 -0.0492 0.0574  -0.0526 218 GLN B CD  
3464 O  OE1 . GLN B 218 ? 0.3076 0.3580 0.5226 -0.0214 -0.0010 -0.0955 218 GLN B OE1 
3465 N  NE2 . GLN B 218 ? 0.3730 0.4222 0.5871 -0.0729 -0.0220 0.0184  218 GLN B NE2 
3466 N  N   . GLU B 219 ? 0.4068 0.1613 0.3466 -0.0523 -0.0790 -0.0092 219 GLU B N   
3467 C  CA  . GLU B 219 ? 0.4154 0.1545 0.3572 -0.0932 -0.0004 -0.0063 219 GLU B CA  
3468 C  C   . GLU B 219 ? 0.2924 0.2150 0.3484 -0.0949 -0.0153 -0.0377 219 GLU B C   
3469 O  O   . GLU B 219 ? 0.2910 0.2027 0.4337 -0.0529 -0.0810 -0.0483 219 GLU B O   
3470 C  CB  . GLU B 219 ? 0.5474 0.1674 0.3975 -0.0207 -0.0614 -0.0317 219 GLU B CB  
3471 C  CG  . GLU B 219 ? 0.5834 0.2084 0.6147 -0.0156 -0.0587 -0.1273 219 GLU B CG  
3472 C  CD  . GLU B 219 ? 0.6925 0.2132 0.8424 -0.1011 -0.0332 -0.0893 219 GLU B CD  
3473 O  OE1 . GLU B 219 ? 0.5772 0.5390 1.2169 -0.0710 0.0522  -0.1469 219 GLU B OE1 
3474 O  OE2 . GLU B 219 ? 1.1023 0.3526 0.9271 -0.3004 -0.1017 -0.1723 219 GLU B OE2 
3475 N  N   . LEU B 220 ? 0.2864 0.1739 0.3341 -0.0547 -0.0124 -0.0110 220 LEU B N   
3476 C  CA  . LEU B 220 ? 0.2696 0.1667 0.3169 -0.0272 -0.0139 -0.0511 220 LEU B CA  
3477 C  C   . LEU B 220 ? 0.2996 0.1695 0.3661 -0.0052 -0.0517 -0.0584 220 LEU B C   
3478 O  O   . LEU B 220 ? 0.3233 0.1918 0.3349 0.0162  -0.0392 -0.0213 220 LEU B O   
3479 C  CB  . LEU B 220 ? 0.3047 0.1723 0.3350 -0.0285 -0.0144 0.0082  220 LEU B CB  
3480 C  CG  . LEU B 220 ? 0.2830 0.1652 0.3157 -0.0613 -0.0282 0.0182  220 LEU B CG  
3481 C  CD1 . LEU B 220 ? 0.3153 0.1745 0.3983 -0.0684 0.0809  0.0473  220 LEU B CD1 
3482 C  CD2 . LEU B 220 ? 0.3755 0.1776 0.4125 0.0570  -0.1191 -0.0193 220 LEU B CD2 
3483 N  N   . LEU B 221 ? 0.3030 0.1559 0.3703 0.0149  -0.0761 -0.0605 221 LEU B N   
3484 C  CA  . LEU B 221 ? 0.3024 0.1789 0.3704 0.0124  -0.0884 -0.0645 221 LEU B CA  
3485 C  C   . LEU B 221 ? 0.2840 0.2628 0.3828 0.0082  -0.0138 -0.0697 221 LEU B C   
3486 O  O   . LEU B 221 ? 0.2779 0.3542 0.5045 -0.0078 -0.0534 -0.0222 221 LEU B O   
3487 C  CB  . LEU B 221 ? 0.3447 0.2026 0.3311 0.0519  -0.0310 -0.0567 221 LEU B CB  
3488 C  CG  . LEU B 221 ? 0.5061 0.2002 0.4024 -0.0599 -0.1739 -0.0234 221 LEU B CG  
3489 C  CD1 . LEU B 221 ? 0.4394 0.2018 0.3681 0.0078  -0.0621 -0.0174 221 LEU B CD1 
3490 C  CD2 . LEU B 221 ? 0.4307 0.1826 0.3865 -0.0037 -0.1079 -0.0298 221 LEU B CD2 
3491 N  N   . THR B 222 ? 0.2973 0.2327 0.4611 0.0073  0.0127  -0.0611 222 THR B N   
3492 C  CA  . THR B 222 ? 0.4052 0.3186 0.5691 -0.1075 0.0098  -0.0629 222 THR B CA  
3493 C  C   . THR B 222 ? 0.4428 0.3088 0.6859 -0.1100 -0.0353 -0.0594 222 THR B C   
3494 O  O   . THR B 222 ? 0.4499 0.3450 0.8433 -0.1246 -0.0614 -0.1319 222 THR B O   
3495 C  CB  . THR B 222 ? 0.4195 0.3074 0.5700 -0.1366 0.0304  0.0277  222 THR B CB  
3496 O  OG1 . THR B 222 ? 0.4268 0.3185 0.5879 -0.1409 -0.0388 -0.0688 222 THR B OG1 
3497 C  CG2 . THR B 222 ? 0.5756 0.3269 0.4218 -0.1036 0.0408  0.0342  222 THR B CG2 
3498 N  N   . HIS B 223 ? 0.4582 0.2777 0.8375 -0.1005 -0.0136 -0.0755 223 HIS B N   
3499 C  CA  . HIS B 223 ? 0.6705 0.2834 0.8596 -0.0519 0.0369  -0.0565 223 HIS B CA  
3500 C  C   . HIS B 223 ? 0.7385 0.3492 0.8782 0.0417  0.0439  0.0418  223 HIS B C   
3501 O  O   . HIS B 223 ? 0.6534 0.7995 0.8650 -0.2969 0.0226  -0.0633 223 HIS B O   
3502 C  CB  . HIS B 223 ? 0.7918 0.3623 0.8430 -0.0399 0.1292  -0.1711 223 HIS B CB  
3503 C  CG  . HIS B 223 ? 0.7014 0.3171 0.9023 -0.0682 0.1127  -0.1853 223 HIS B CG  
3504 N  ND1 . HIS B 223 ? 0.5610 0.3467 0.9442 -0.1382 0.1199  -0.2352 223 HIS B ND1 
3505 C  CD2 . HIS B 223 ? 0.5044 0.3413 1.0130 -0.0812 0.0219  -0.2440 223 HIS B CD2 
3506 C  CE1 . HIS B 223 ? 0.4531 0.3500 1.0083 -0.1201 0.0959  -0.2188 223 HIS B CE1 
3507 N  NE2 . HIS B 223 ? 0.3894 0.3260 1.0659 -0.0831 0.0249  -0.2006 223 HIS B NE2 
3508 S  S   . SO4 C .   ? 1.2305 0.5103 1.1062 0.0196  0.0088  -0.0524 234 SO4 A S   
3509 O  O1  . SO4 C .   ? 1.2463 0.4615 1.2550 -0.0292 0.1799  0.0334  234 SO4 A O1  
3510 O  O2  . SO4 C .   ? 1.0984 0.5734 0.9668 -0.0424 0.2371  0.1047  234 SO4 A O2  
3511 O  O3  . SO4 C .   ? 1.4764 0.6746 0.9547 -0.2352 -0.0046 -0.0178 234 SO4 A O3  
3512 O  O4  . SO4 C .   ? 1.0142 0.8292 0.7501 -0.1081 -0.3396 -0.2833 234 SO4 A O4  
3513 C  CHA . HEM D .   ? 0.3589 0.2449 0.4886 -0.0088 -0.1404 0.0274  300 HEM A CHA 
3514 C  CHB . HEM D .   ? 0.4326 0.2999 0.7051 0.0834  -0.1250 0.0870  300 HEM A CHB 
3515 C  CHC . HEM D .   ? 0.3522 0.3722 0.5035 0.0869  0.0167  0.0437  300 HEM A CHC 
3516 C  CHD . HEM D .   ? 0.3480 0.1837 0.3144 0.0492  -0.0232 0.0502  300 HEM A CHD 
3517 C  C1A . HEM D .   ? 0.3798 0.2645 0.6800 0.0266  -0.2260 -0.0839 300 HEM A C1A 
3518 C  C2A . HEM D .   ? 0.4132 0.3827 0.8424 0.0036  -0.2547 -0.2323 300 HEM A C2A 
3519 C  C3A . HEM D .   ? 0.4248 0.3523 0.7642 -0.0485 -0.2103 -0.1139 300 HEM A C3A 
3520 C  C4A . HEM D .   ? 0.3777 0.3032 0.7747 0.0298  -0.2086 -0.0893 300 HEM A C4A 
3521 C  CMA . HEM D .   ? 0.5440 0.5124 0.5855 -0.2935 -0.0660 0.0361  300 HEM A CMA 
3522 C  CAA . HEM D .   ? 0.6229 0.4783 0.9452 -0.0414 -0.1786 -0.3308 300 HEM A CAA 
3523 C  CBA . HEM D .   ? 0.7307 0.6624 0.9652 -0.0581 -0.0984 -0.3832 300 HEM A CBA 
3524 C  CGA . HEM D .   ? 0.6646 0.7184 0.9454 -0.0504 -0.1548 -0.4089 300 HEM A CGA 
3525 O  O1A . HEM D .   ? 0.9159 0.6319 1.1897 0.0245  -0.3297 -0.5137 300 HEM A O1A 
3526 O  O2A . HEM D .   ? 0.6923 0.5964 1.1943 -0.1812 -0.2716 -0.2939 300 HEM A O2A 
3527 C  C1B . HEM D .   ? 0.4276 0.3192 0.7767 0.1295  -0.1506 0.0159  300 HEM A C1B 
3528 C  C2B . HEM D .   ? 0.3959 0.3569 0.7503 0.1183  -0.1287 0.0539  300 HEM A C2B 
3529 C  C3B . HEM D .   ? 0.3866 0.3275 0.6853 0.1462  -0.1065 0.0664  300 HEM A C3B 
3530 C  C4B . HEM D .   ? 0.3741 0.3407 0.6046 0.1271  -0.0738 0.0440  300 HEM A C4B 
3531 C  CMB . HEM D .   ? 0.4330 0.3578 0.9721 0.1543  -0.2481 0.0591  300 HEM A CMB 
3532 C  CAB . HEM D .   ? 0.4496 0.4183 0.6846 0.2030  -0.0422 0.0372  300 HEM A CAB 
3533 C  CBB . HEM D .   ? 0.4413 0.5318 0.9303 0.2020  0.1077  0.0671  300 HEM A CBB 
3534 C  C1C . HEM D .   ? 0.3321 0.2921 0.3720 0.0487  0.0478  0.0764  300 HEM A C1C 
3535 C  C2C . HEM D .   ? 0.4181 0.2139 0.3910 0.1170  -0.0214 0.0557  300 HEM A C2C 
3536 C  C3C . HEM D .   ? 0.4216 0.2275 0.3030 0.1360  -0.0826 0.0413  300 HEM A C3C 
3537 C  C4C . HEM D .   ? 0.3676 0.1963 0.3029 0.0814  -0.0401 0.0650  300 HEM A C4C 
3538 C  CMC . HEM D .   ? 0.5384 0.3031 0.4397 0.1992  -0.0166 0.0082  300 HEM A CMC 
3539 C  CAC . HEM D .   ? 0.5017 0.2549 0.3614 0.1098  -0.1633 0.0588  300 HEM A CAC 
3540 C  CBC . HEM D .   ? 0.9423 0.5461 0.4316 -0.0497 -0.2548 -0.1036 300 HEM A CBC 
3541 C  C1D . HEM D .   ? 0.2646 0.1877 0.3128 0.0133  -0.0130 0.0531  300 HEM A C1D 
3542 C  C2D . HEM D .   ? 0.2544 0.2379 0.3622 0.0140  -0.0193 0.0012  300 HEM A C2D 
3543 C  C3D . HEM D .   ? 0.2860 0.2127 0.3726 0.0039  -0.0136 0.0082  300 HEM A C3D 
3544 C  C4D . HEM D .   ? 0.2846 0.2140 0.4411 -0.0027 -0.0533 0.0070  300 HEM A C4D 
3545 C  CMD . HEM D .   ? 0.2711 0.2252 0.3929 0.0245  -0.0666 0.0817  300 HEM A CMD 
3546 C  CAD . HEM D .   ? 0.3298 0.3057 0.4062 -0.0028 0.0302  -0.0589 300 HEM A CAD 
3547 C  CBD . HEM D .   ? 0.3757 0.2878 0.4475 -0.0722 0.0681  -0.0643 300 HEM A CBD 
3548 C  CGD . HEM D .   ? 0.4488 0.3404 0.4740 -0.0482 0.1199  -0.0975 300 HEM A CGD 
3549 O  O1D . HEM D .   ? 0.4131 0.3812 0.3785 -0.0107 0.0774  -0.0614 300 HEM A O1D 
3550 O  O2D . HEM D .   ? 0.4882 0.3512 0.8641 -0.0233 0.0964  -0.1893 300 HEM A O2D 
3551 N  NA  . HEM D .   ? 0.3684 0.2793 0.7813 0.0368  -0.2434 -0.1352 300 HEM A NA  
3552 N  NB  . HEM D .   ? 0.3959 0.3007 0.7523 0.1312  -0.1114 0.0161  300 HEM A NB  
3553 N  NC  . HEM D .   ? 0.3149 0.2114 0.3824 0.0077  0.0142  0.0708  300 HEM A NC  
3554 N  ND  . HEM D .   ? 0.2528 0.1958 0.3990 0.0096  -0.0155 0.0589  300 HEM A ND  
3555 FE FE  . HEM D .   ? 0.2979 0.2199 0.5396 0.0457  -0.0399 0.0523  300 HEM A FE  
3556 C  CHA . HEM E .   ? 0.4533 0.4482 0.6145 0.0973  0.0413  -0.1253 300 HEM B CHA 
3557 C  CHB . HEM E .   ? 0.5823 0.6067 0.9941 0.1393  -0.2299 -0.2312 300 HEM B CHB 
3558 C  CHC . HEM E .   ? 0.4946 0.4406 0.5269 -0.1144 -0.0373 -0.0125 300 HEM B CHC 
3559 C  CHD . HEM E .   ? 0.4959 0.2829 0.3084 -0.0430 -0.0136 -0.0161 300 HEM B CHD 
3560 C  C1A . HEM E .   ? 0.4615 0.5203 0.7843 0.1410  0.0021  -0.2543 300 HEM B C1A 
3561 C  C2A . HEM E .   ? 0.5595 0.6631 0.9798 0.2641  -0.1203 -0.4099 300 HEM B C2A 
3562 C  C3A . HEM E .   ? 0.5682 0.6263 1.1459 0.2540  -0.1794 -0.3974 300 HEM B C3A 
3563 C  C4A . HEM E .   ? 0.5493 0.5736 1.0311 0.1640  -0.1438 -0.3267 300 HEM B C4A 
3564 C  CMA . HEM E .   ? 0.7276 0.7674 1.2588 0.3982  -0.2546 -0.4254 300 HEM B CMA 
3565 C  CAA . HEM E .   ? 0.6559 0.8339 0.9923 0.3058  -0.0898 -0.5068 300 HEM B CAA 
3566 C  CBA . HEM E .   ? 0.9312 0.9945 1.0326 0.2630  -0.2410 -0.4835 300 HEM B CBA 
3567 C  CGA . HEM E .   ? 1.0032 1.0328 1.0953 0.2897  -0.2810 -0.5793 300 HEM B CGA 
3568 O  O1A . HEM E .   ? 1.3134 1.1976 1.0362 0.2832  -0.2498 -0.5942 300 HEM B O1A 
3569 O  O2A . HEM E .   ? 0.8430 0.9463 1.5304 0.4925  -0.4122 -0.7321 300 HEM B O2A 
3570 C  C1B . HEM E .   ? 0.4838 0.5755 0.8179 0.0759  -0.1792 -0.1614 300 HEM B C1B 
3571 C  C2B . HEM E .   ? 0.4680 0.5733 0.7506 0.0325  -0.1508 -0.0594 300 HEM B C2B 
3572 C  C3B . HEM E .   ? 0.4789 0.5026 0.7038 -0.0450 -0.1302 -0.0349 300 HEM B C3B 
3573 C  C4B . HEM E .   ? 0.4761 0.5108 0.6171 -0.0507 -0.0961 -0.0675 300 HEM B C4B 
3574 C  CMB . HEM E .   ? 0.4661 0.6957 0.7897 0.0132  -0.0690 0.0117  300 HEM B CMB 
3575 C  CAB . HEM E .   ? 0.5494 0.4647 0.7640 -0.1345 -0.1680 -0.0072 300 HEM B CAB 
3576 C  CBB . HEM E .   ? 0.4535 0.7030 0.7942 -0.0479 -0.1004 -0.3164 300 HEM B CBB 
3577 C  C1C . HEM E .   ? 0.4951 0.4156 0.4946 -0.1156 -0.0246 -0.0712 300 HEM B C1C 
3578 C  C2C . HEM E .   ? 0.5057 0.4384 0.5246 -0.1736 0.0180  -0.1321 300 HEM B C2C 
3579 C  C3C . HEM E .   ? 0.5021 0.3777 0.4708 -0.0971 -0.0462 -0.1078 300 HEM B C3C 
3580 C  C4C . HEM E .   ? 0.4985 0.3364 0.4296 -0.0972 -0.0278 -0.0603 300 HEM B C4C 
3581 C  CMC . HEM E .   ? 0.4725 0.6105 0.5153 -0.2696 0.0883  -0.1996 300 HEM B CMC 
3582 C  CAC . HEM E .   ? 0.5438 0.3102 0.4806 -0.0832 0.0174  -0.0235 300 HEM B CAC 
3583 C  CBC . HEM E .   ? 0.7152 0.3310 0.5992 0.0383  0.1748  0.0561  300 HEM B CBC 
3584 C  C1D . HEM E .   ? 0.4129 0.2663 0.3210 -0.0361 0.0042  -0.0050 300 HEM B C1D 
3585 C  C2D . HEM E .   ? 0.3975 0.2126 0.3807 0.0107  -0.0199 -0.0229 300 HEM B C2D 
3586 C  C3D . HEM E .   ? 0.4053 0.2588 0.3615 0.0172  -0.0078 -0.0329 300 HEM B C3D 
3587 C  C4D . HEM E .   ? 0.3896 0.2708 0.3997 -0.0124 0.0376  -0.0009 300 HEM B C4D 
3588 C  CMD . HEM E .   ? 0.4074 0.2889 0.3844 0.0489  -0.0204 -0.0106 300 HEM B CMD 
3589 C  CAD . HEM E .   ? 0.4450 0.3331 0.3663 0.0389  -0.0340 -0.0940 300 HEM B CAD 
3590 C  CBD . HEM E .   ? 0.6265 0.3602 0.3688 0.0520  -0.0420 -0.0868 300 HEM B CBD 
3591 C  CGD . HEM E .   ? 0.6809 0.3885 0.3777 0.1302  -0.0704 -0.1664 300 HEM B CGD 
3592 O  O1D . HEM E .   ? 0.6246 0.3061 0.5558 -0.0293 -0.1162 -0.0174 300 HEM B O1D 
3593 O  O2D . HEM E .   ? 0.9794 0.3664 0.5829 0.1664  -0.2516 -0.1571 300 HEM B O2D 
3594 N  NA  . HEM E .   ? 0.5122 0.3755 0.8945 0.0926  -0.0470 -0.2180 300 HEM B NA  
3595 N  NB  . HEM E .   ? 0.4740 0.5505 0.6617 -0.0205 -0.1133 -0.1198 300 HEM B NB  
3596 N  NC  . HEM E .   ? 0.5036 0.4069 0.3820 -0.0791 -0.0249 -0.0428 300 HEM B NC  
3597 N  ND  . HEM E .   ? 0.4003 0.3039 0.3992 -0.0086 -0.0263 -0.0012 300 HEM B ND  
3598 FE FE  . HEM E .   ? 0.4584 0.3084 0.5119 -0.0087 -0.0535 0.0265  300 HEM B FE  
3599 O  O   . HOH F .   ? 0.5503 0.3375 0.6397 0.1981  -0.0195 0.1431  301 HOH A O   
3600 O  O   . HOH F .   ? 0.2711 0.1697 0.2911 -0.0050 -0.0296 0.0178  302 HOH A O   
3601 O  O   . HOH F .   ? 0.2367 0.1961 0.3305 0.0138  -0.0351 0.0748  303 HOH A O   
3602 O  O   . HOH F .   ? 0.2450 0.1302 0.2616 0.0031  -0.0598 -0.0112 304 HOH A O   
3603 O  O   . HOH F .   ? 0.3636 0.1443 0.3538 0.0356  -0.0600 0.0187  305 HOH A O   
3604 O  O   . HOH F .   ? 0.2274 0.1107 0.2390 -0.0090 -0.0319 -0.0036 306 HOH A O   
3605 O  O   . HOH F .   ? 0.2362 0.1247 0.3064 -0.0076 -0.0626 0.0450  307 HOH A O   
3606 O  O   . HOH F .   ? 0.2757 0.1953 0.3567 -0.0054 0.0052  0.0706  308 HOH A O   
3607 O  O   . HOH F .   ? 0.2661 0.1585 0.3200 -0.0260 -0.0008 -0.0225 309 HOH A O   
3608 O  O   . HOH F .   ? 0.2628 0.1105 0.2427 -0.0093 -0.0224 -0.0166 310 HOH A O   
3609 O  O   . HOH F .   ? 0.2576 0.0895 0.2593 0.0065  -0.0283 0.0009  311 HOH A O   
3610 O  O   . HOH F .   ? 0.3236 0.1161 0.3286 -0.0004 -0.0413 -0.0026 312 HOH A O   
3611 O  O   . HOH F .   ? 0.4260 0.1493 0.2476 0.0378  -0.1147 0.0014  313 HOH A O   
3612 O  O   . HOH F .   ? 0.3496 0.2853 0.3910 -0.0226 0.0470  0.0005  314 HOH A O   
3613 O  O   . HOH F .   ? 0.3021 0.2278 0.5137 0.0251  -0.0167 -0.0210 315 HOH A O   
3614 O  O   . HOH F .   ? 0.4440 0.1660 0.5034 -0.0167 -0.0485 0.0351  316 HOH A O   
3615 O  O   . HOH F .   ? 0.4455 0.1975 0.4112 -0.0497 0.0240  -0.0324 317 HOH A O   
3616 O  O   . HOH F .   ? 0.3058 0.1639 0.4026 0.0597  -0.0211 -0.0231 318 HOH A O   
3617 O  O   . HOH F .   ? 0.2415 0.1730 0.3006 0.0445  -0.0046 0.0107  319 HOH A O   
3618 O  O   . HOH F .   ? 0.4029 0.2464 0.4211 0.0472  -0.0793 -0.0198 320 HOH A O   
3619 O  O   . HOH F .   ? 0.2733 0.3080 0.4193 0.0066  0.0277  0.0197  321 HOH A O   
3620 O  O   . HOH F .   ? 0.4221 0.1941 0.2886 0.0511  -0.0062 -0.0334 322 HOH A O   
3621 O  O   . HOH F .   ? 0.5823 0.2257 0.3597 -0.0148 -0.0857 0.0035  323 HOH A O   
3622 O  O   . HOH F .   ? 0.3218 0.2355 0.3166 -0.0576 -0.0151 0.0262  324 HOH A O   
3623 O  O   . HOH F .   ? 0.3003 0.2572 0.4691 -0.0332 -0.1063 0.0597  325 HOH A O   
3624 O  O   . HOH F .   ? 0.4198 0.4409 0.6841 0.0940  -0.1125 0.1606  326 HOH A O   
3625 O  O   . HOH F .   ? 0.7090 0.2741 0.4045 -0.1144 0.0252  -0.0494 327 HOH A O   
3626 O  O   . HOH F .   ? 0.3227 0.2872 0.2509 -0.0559 -0.0456 -0.0296 328 HOH A O   
3627 O  O   . HOH F .   ? 0.3378 0.3296 0.2815 0.1145  -0.0897 0.0310  329 HOH A O   
3628 O  O   . HOH F .   ? 0.3741 0.1876 0.2945 0.0219  -0.0512 -0.0141 330 HOH A O   
3629 O  O   . HOH F .   ? 0.4695 0.3121 0.3351 -0.0985 -0.0709 0.0536  331 HOH A O   
3630 O  O   . HOH F .   ? 0.3082 0.3529 0.5200 0.1205  -0.0925 -0.0214 332 HOH A O   
3631 O  O   . HOH F .   ? 0.4139 0.3240 0.3631 -0.0100 -0.0975 -0.1550 333 HOH A O   
3632 O  O   . HOH F .   ? 0.3533 0.4695 0.5262 -0.1151 -0.0421 -0.0346 334 HOH A O   
3633 O  O   . HOH F .   ? 0.6745 0.5285 0.6563 0.1109  0.0454  0.0617  335 HOH A O   
3634 O  O   . HOH F .   ? 0.5080 0.4901 0.6333 -0.0539 -0.2435 -0.1959 336 HOH A O   
3635 O  O   . HOH F .   ? 0.3557 0.4202 0.4275 0.0043  -0.1016 -0.1231 337 HOH A O   
3636 O  O   . HOH F .   ? 0.6840 0.2506 0.6192 0.1745  -0.3511 -0.2160 338 HOH A O   
3637 O  O   . HOH F .   ? 0.4574 0.5360 0.4912 0.0005  0.0560  0.0191  339 HOH A O   
3638 O  O   . HOH F .   ? 0.4414 0.4572 0.4786 0.0109  -0.1085 0.0762  340 HOH A O   
3639 O  O   . HOH F .   ? 0.2887 0.5507 0.4270 0.0947  -0.1559 -0.1498 341 HOH A O   
3640 O  O   . HOH F .   ? 0.3442 0.2887 0.3433 0.0260  -0.0738 -0.0023 342 HOH A O   
3641 O  O   . HOH F .   ? 0.3004 0.1575 0.2911 0.0219  -0.0882 -0.0392 343 HOH A O   
3642 O  O   . HOH F .   ? 0.6442 0.4326 0.4272 -0.0241 -0.0829 0.0384  344 HOH A O   
3643 O  O   . HOH F .   ? 0.4521 0.2692 0.3480 0.0715  0.0451  0.1155  345 HOH A O   
3644 O  O   . HOH F .   ? 0.3008 0.3039 0.2361 0.0406  -0.0289 0.0334  346 HOH A O   
3645 O  O   . HOH F .   ? 0.7149 0.4324 0.4449 0.0992  -0.1538 -0.0602 347 HOH A O   
3646 O  O   . HOH F .   ? 0.5064 0.4865 0.7317 -0.0694 -0.0426 0.2660  348 HOH A O   
3647 O  O   . HOH F .   ? 0.3304 0.3042 0.3978 0.0027  0.0024  -0.0727 349 HOH A O   
3648 O  O   . HOH F .   ? 0.3773 0.4458 0.5203 0.0402  0.0074  -0.1267 350 HOH A O   
3649 O  O   . HOH F .   ? 0.7117 0.7170 0.7618 0.0794  -0.1989 -0.0933 351 HOH A O   
3650 O  O   . HOH F .   ? 0.5089 0.3132 0.5115 -0.0109 -0.0536 0.0041  352 HOH A O   
3651 O  O   . HOH F .   ? 0.3827 0.5709 0.5017 -0.0011 -0.1147 -0.1542 353 HOH A O   
3652 O  O   . HOH F .   ? 0.6441 0.4671 0.6493 0.1198  0.0115  -0.1634 354 HOH A O   
3653 O  O   . HOH F .   ? 0.4104 0.4098 0.5851 -0.0070 -0.0301 -0.0600 355 HOH A O   
3654 O  O   . HOH F .   ? 0.5320 0.2250 0.4521 0.0880  0.1573  0.0995  356 HOH A O   
3655 O  O   . HOH F .   ? 0.5798 0.6594 0.6268 -0.2343 -0.0197 -0.1412 357 HOH A O   
3656 O  O   . HOH F .   ? 0.4142 0.4055 0.4380 0.0442  0.1388  0.0314  358 HOH A O   
3657 O  O   . HOH F .   ? 0.6006 0.6453 0.8843 0.0983  -0.0025 0.0671  359 HOH A O   
3658 O  O   . HOH F .   ? 0.4377 0.2394 0.3828 0.0504  0.0009  -0.0094 360 HOH A O   
3659 O  O   . HOH F .   ? 0.4697 0.3927 0.3670 -0.0105 -0.0310 0.0362  361 HOH A O   
3660 O  O   . HOH F .   ? 0.4887 0.7401 0.3753 0.1997  -0.1082 -0.1514 362 HOH A O   
3661 O  O   . HOH F .   ? 0.3557 0.3893 0.4754 -0.0622 -0.0556 -0.0665 363 HOH A O   
3662 O  O   . HOH F .   ? 0.4761 0.5298 0.5960 0.1371  -0.0612 0.0230  364 HOH A O   
3663 O  O   . HOH F .   ? 0.4116 0.1355 0.4004 0.0115  -0.1515 0.0005  365 HOH A O   
3664 O  O   . HOH F .   ? 0.5255 0.6421 0.7197 -0.0270 0.0434  0.0916  366 HOH A O   
3665 O  O   . HOH F .   ? 0.3567 0.6589 0.5587 0.0385  -0.0223 -0.0758 367 HOH A O   
3666 O  O   . HOH F .   ? 0.4829 0.2887 0.4299 -0.0354 -0.0853 0.0477  368 HOH A O   
3667 O  O   . HOH F .   ? 0.3345 0.5103 0.5223 -0.0335 -0.0103 0.0940  369 HOH A O   
3668 O  O   . HOH F .   ? 0.4551 0.3689 0.5472 0.1328  -0.0638 0.1252  370 HOH A O   
3669 O  O   . HOH F .   ? 0.3857 0.2519 0.6421 0.0102  0.1891  0.0276  371 HOH A O   
3670 O  O   . HOH F .   ? 0.5475 0.5806 0.4880 0.0044  0.0877  0.0165  372 HOH A O   
3671 O  O   . HOH F .   ? 0.7134 0.6381 0.6162 -0.0313 0.0837  -0.0079 373 HOH A O   
3672 O  O   . HOH F .   ? 0.5556 0.3425 0.3853 0.0570  -0.0957 -0.0406 374 HOH A O   
3673 O  O   . HOH F .   ? 0.5125 0.4421 0.6369 -0.0021 0.1045  -0.0216 375 HOH A O   
3674 O  O   . HOH F .   ? 0.3454 0.3098 0.4592 0.0990  0.0408  0.0822  376 HOH A O   
3675 O  O   . HOH F .   ? 0.4705 0.3528 0.5919 0.0877  -0.0505 -0.0475 377 HOH A O   
3676 O  O   . HOH F .   ? 0.3769 0.2146 0.3394 -0.0325 -0.1152 -0.0166 378 HOH A O   
3677 O  O   . HOH F .   ? 0.2894 0.2055 0.3800 -0.0017 -0.0212 0.0520  379 HOH A O   
3678 O  O   . HOH F .   ? 0.6051 0.4811 0.7753 -0.0793 -0.0082 -0.1469 380 HOH A O   
3679 O  O   . HOH F .   ? 0.3095 0.1435 0.2406 0.0106  -0.0966 0.0210  381 HOH A O   
3680 O  O   . HOH F .   ? 0.5880 0.3432 0.5513 0.0545  -0.1037 -0.0282 382 HOH A O   
3681 O  O   . HOH F .   ? 0.6317 0.3917 0.6077 -0.1428 0.0541  0.0258  383 HOH A O   
3682 O  O   . HOH F .   ? 0.2222 0.1445 0.2246 -0.0296 -0.0196 0.0030  384 HOH A O   
3683 O  O   . HOH F .   ? 0.6206 0.1483 0.5071 -0.0878 0.1733  -0.0817 385 HOH A O   
3684 O  O   . HOH F .   ? 0.3566 0.2339 0.5302 -0.0238 -0.0288 -0.0239 386 HOH A O   
3685 O  O   . HOH F .   ? 0.3347 0.3243 0.3514 0.0606  -0.0352 0.1620  387 HOH A O   
3686 O  O   . HOH F .   ? 0.5785 0.2733 0.5775 -0.0572 -0.1539 -0.0491 388 HOH A O   
3687 O  O   . HOH F .   ? 0.3363 0.4955 0.5782 0.0481  0.0053  0.1069  389 HOH A O   
3688 O  O   . HOH F .   ? 0.5901 0.5685 0.3569 0.1921  -0.0264 0.0246  390 HOH A O   
3689 O  O   . HOH F .   ? 0.3068 0.6624 0.4064 -0.0425 -0.1224 0.0138  391 HOH A O   
3690 O  O   . HOH F .   ? 0.4755 0.3768 0.3698 0.0541  0.0375  -0.0103 392 HOH A O   
3691 O  O   . HOH F .   ? 0.3133 0.4374 0.5257 0.1004  -0.1043 -0.1253 393 HOH A O   
3692 O  O   . HOH F .   ? 0.4304 0.5233 0.5945 -0.0642 0.1264  0.1490  394 HOH A O   
3693 O  O   . HOH F .   ? 0.4982 0.2275 0.3983 -0.0697 -0.0393 0.0227  395 HOH A O   
3694 O  O   . HOH F .   ? 0.5714 0.6504 0.4661 0.0406  -0.1315 -0.1135 396 HOH A O   
3695 O  O   . HOH F .   ? 0.4530 0.3984 0.5827 -0.0450 -0.1154 0.0241  397 HOH A O   
3696 O  O   . HOH F .   ? 0.4304 0.3852 0.5626 0.0559  -0.1302 -0.0084 398 HOH A O   
3697 O  O   . HOH F .   ? 0.7855 0.7915 0.6225 0.2003  -0.1022 0.1846  399 HOH A O   
3698 O  O   . HOH F .   ? 0.7145 0.8047 0.7415 -0.2127 -0.0301 0.0561  400 HOH A O   
3699 O  O   . HOH F .   ? 0.6900 0.5598 0.6539 0.0724  0.0309  0.0204  401 HOH A O   
3700 O  O   . HOH F .   ? 0.4734 0.2230 0.4603 0.0161  -0.1370 0.1156  402 HOH A O   
3701 O  O   . HOH F .   ? 0.4685 0.2887 0.6936 -0.0038 0.0144  -0.0915 403 HOH A O   
3702 O  O   . HOH F .   ? 0.5069 0.5563 0.4207 0.1383  0.0109  0.0785  404 HOH A O   
3703 O  O   . HOH F .   ? 0.5821 0.2559 0.3759 -0.0072 -0.1187 0.0978  405 HOH A O   
3704 O  O   . HOH F .   ? 0.5221 0.3739 0.5951 0.0492  -0.0420 0.0737  406 HOH A O   
3705 O  O   . HOH F .   ? 0.6731 0.6287 0.6315 0.0651  -0.0301 -0.2134 407 HOH A O   
3706 O  O   . HOH F .   ? 0.5567 0.2619 0.3985 -0.0174 -0.0100 0.0053  408 HOH A O   
3707 O  O   . HOH F .   ? 0.3682 0.5962 0.5006 -0.0015 0.0254  0.0576  409 HOH A O   
3708 O  O   . HOH F .   ? 1.0167 0.9459 1.0289 -0.0083 -0.0170 0.0061  410 HOH A O   
3709 O  O   . HOH F .   ? 0.6406 0.4903 0.4642 0.2135  -0.0997 0.0342  411 HOH A O   
3710 O  O   . HOH F .   ? 0.4934 0.4326 0.5575 0.1088  -0.0984 0.0042  412 HOH A O   
3711 O  O   . HOH F .   ? 0.5229 0.5225 0.6339 0.0224  -0.0069 -0.0722 413 HOH A O   
3712 O  O   . HOH F .   ? 0.5468 0.3943 0.4176 -0.0149 0.0247  0.0891  414 HOH A O   
3713 O  O   . HOH F .   ? 0.5344 0.2803 0.6261 0.0280  0.0269  -0.0275 415 HOH A O   
3714 O  O   . HOH F .   ? 0.3925 0.3772 0.4568 -0.0059 -0.0773 0.0436  416 HOH A O   
3715 O  O   . HOH F .   ? 0.4892 0.5626 0.3785 -0.0640 -0.0823 -0.0145 417 HOH A O   
3716 O  O   . HOH F .   ? 0.4634 0.6228 0.6565 -0.0883 0.0250  -0.0150 418 HOH A O   
3717 O  O   . HOH F .   ? 0.5923 0.7204 0.7555 0.0390  0.1024  -0.0056 419 HOH A O   
3718 O  O   . HOH F .   ? 0.5276 0.6926 0.6450 -0.1103 0.1963  -0.2482 420 HOH A O   
3719 O  O   . HOH F .   ? 0.5876 0.6522 0.3926 -0.0020 -0.0897 0.0055  421 HOH A O   
3720 O  O   . HOH F .   ? 0.4161 0.3944 0.7596 0.1044  0.1003  0.0801  422 HOH A O   
3721 O  O   . HOH F .   ? 0.3157 0.3649 0.4758 0.0534  0.0619  0.0300  423 HOH A O   
3722 O  O   . HOH F .   ? 0.5320 0.2648 0.7959 -0.1387 0.0270  -0.0272 424 HOH A O   
3723 O  O   . HOH F .   ? 0.6699 0.7603 0.7089 -0.0165 -0.0032 0.0009  425 HOH A O   
3724 O  O   . HOH F .   ? 0.5978 0.5188 0.6802 0.2356  -0.0030 -0.1779 426 HOH A O   
3725 O  O   . HOH F .   ? 0.3677 0.4213 0.5326 0.0705  0.0347  0.0309  427 HOH A O   
3726 O  O   . HOH F .   ? 0.4345 0.4801 0.6318 -0.0185 0.0431  -0.0975 428 HOH A O   
3727 O  O   . HOH F .   ? 0.6880 0.3184 0.6212 0.1222  -0.0284 0.0366  429 HOH A O   
3728 O  O   . HOH F .   ? 0.4509 0.5048 0.6125 0.0184  0.0618  0.0910  430 HOH A O   
3729 O  O   . HOH F .   ? 0.8014 0.6561 0.6783 0.0536  -0.1624 -0.0206 431 HOH A O   
3730 O  O   . HOH F .   ? 0.4626 0.4478 0.5542 -0.0627 0.1960  -0.1173 432 HOH A O   
3731 O  O   . HOH F .   ? 0.4914 0.4874 0.5001 -0.0050 0.0069  -0.1897 433 HOH A O   
3732 O  O   . HOH F .   ? 0.7955 0.4614 0.8273 0.2284  -0.1179 0.0172  434 HOH A O   
3733 O  O   . HOH F .   ? 0.8156 0.5362 0.7564 0.1279  0.0723  0.0462  435 HOH A O   
3734 O  O   . HOH F .   ? 0.5666 0.4910 0.6187 -0.0056 0.0786  0.1282  436 HOH A O   
3735 O  O   . HOH F .   ? 0.6000 0.5757 0.5917 0.0767  0.0969  0.0685  437 HOH A O   
3736 O  O   . HOH F .   ? 0.4108 0.2664 0.4281 -0.0076 0.0467  0.0996  438 HOH A O   
3737 O  O   . HOH F .   ? 0.4727 0.5964 0.6447 0.0165  0.0360  -0.0204 439 HOH A O   
3738 O  O   . HOH F .   ? 0.5991 0.5907 0.8418 0.1846  0.0554  -0.0193 440 HOH A O   
3739 O  O   . HOH F .   ? 0.6333 0.5398 0.8402 -0.2118 -0.1283 -0.0900 441 HOH A O   
3740 O  O   . HOH F .   ? 0.5436 0.3094 0.5776 -0.1167 0.1600  -0.0092 442 HOH A O   
3741 O  O   . HOH F .   ? 0.5981 0.5076 0.5795 -0.1310 -0.1118 -0.0625 443 HOH A O   
3742 O  O   . HOH F .   ? 0.6352 0.5206 0.3772 0.0257  -0.0783 0.0486  444 HOH A O   
3743 O  O   . HOH F .   ? 0.5828 0.3102 0.5288 0.0014  -0.0322 -0.0376 445 HOH A O   
3744 O  O   . HOH F .   ? 0.7367 0.4390 0.7979 -0.0237 -0.0646 0.0046  446 HOH A O   
3745 O  O   . HOH F .   ? 0.4654 0.3562 0.6032 -0.1129 -0.0659 0.1644  447 HOH A O   
3746 O  O   . HOH F .   ? 0.4598 0.5797 0.5325 0.0016  0.0030  -0.0932 448 HOH A O   
3747 O  O   . HOH F .   ? 0.8018 0.5547 0.5272 0.0367  -0.0323 -0.0651 449 HOH A O   
3748 O  O   . HOH F .   ? 0.4541 0.2708 0.4365 -0.0203 -0.1205 -0.0959 450 HOH A O   
3749 O  O   . HOH F .   ? 0.4497 0.5734 0.5738 0.1049  -0.1206 -0.0736 451 HOH A O   
3750 O  O   . HOH F .   ? 0.6581 0.5529 0.8357 0.1274  0.0085  -0.0837 452 HOH A O   
3751 O  O   . HOH F .   ? 0.7797 0.6356 0.7253 -0.0046 -0.2248 0.0376  453 HOH A O   
3752 O  O   . HOH F .   ? 0.5886 0.4684 0.5674 0.1937  0.0128  -0.0136 454 HOH A O   
3753 O  O   . HOH F .   ? 0.7843 0.5565 0.7738 0.1403  -0.1150 -0.3178 455 HOH A O   
3754 O  O   . HOH F .   ? 0.3583 0.3803 0.5397 -0.0894 -0.1450 0.1651  456 HOH A O   
3755 O  O   . HOH F .   ? 0.6090 0.2156 0.4389 -0.0731 -0.0514 -0.0127 457 HOH A O   
3756 O  O   . HOH F .   ? 0.5364 0.6708 0.8899 0.0554  -0.0343 0.1178  458 HOH A O   
3757 O  O   . HOH F .   ? 0.6312 0.5377 0.6321 0.0308  0.0013  -0.0871 459 HOH A O   
3758 O  O   . HOH F .   ? 0.4346 0.5613 0.5050 -0.2188 -0.0185 -0.2042 460 HOH A O   
3759 O  O   . HOH F .   ? 0.6029 0.3417 0.7432 -0.0074 0.0380  -0.1882 461 HOH A O   
3760 O  O   . HOH F .   ? 0.8495 0.2498 0.7423 0.0069  0.1850  0.0038  462 HOH A O   
3761 O  O   . HOH F .   ? 0.4358 0.4118 0.6757 0.0075  -0.1808 -0.0798 463 HOH A O   
3762 O  O   . HOH F .   ? 0.7884 0.4976 0.5312 -0.1915 0.0588  -0.1005 464 HOH A O   
3763 O  O   . HOH F .   ? 0.5972 0.5285 0.7292 0.0443  -0.1907 -0.2000 465 HOH A O   
3764 O  O   . HOH F .   ? 0.8231 0.6279 0.8602 0.1752  -0.1067 -0.0950 466 HOH A O   
3765 O  O   . HOH F .   ? 0.7203 0.7692 0.5736 -0.1416 -0.0429 0.0960  467 HOH A O   
3766 O  O   . HOH F .   ? 0.7409 0.6703 0.6351 0.1499  -0.1864 -0.0190 468 HOH A O   
3767 O  O   . HOH F .   ? 0.4553 0.4318 0.6874 -0.0542 0.0803  -0.0139 469 HOH A O   
3768 O  O   . HOH F .   ? 0.5029 0.8491 0.4548 -0.0272 -0.1617 0.1188  470 HOH A O   
3769 O  O   . HOH F .   ? 0.4271 0.3478 0.6574 -0.1249 0.0437  0.1025  471 HOH A O   
3770 O  O   . HOH F .   ? 0.6089 0.8159 0.6870 0.0210  0.0296  -0.0400 472 HOH A O   
3771 O  O   . HOH F .   ? 0.7619 0.7061 0.7167 0.1164  -0.0778 -0.0025 473 HOH A O   
3772 O  O   . HOH F .   ? 0.6828 0.4799 0.5690 0.1407  0.0212  -0.0085 474 HOH A O   
3773 O  O   . HOH F .   ? 0.6767 0.3888 0.7671 0.1198  0.0207  -0.0283 475 HOH A O   
3774 O  O   . HOH F .   ? 0.8135 0.6134 0.6155 0.0259  -0.1676 0.0755  476 HOH A O   
3775 O  O   . HOH F .   ? 0.7777 0.5821 0.8093 0.0851  0.0989  -0.0684 477 HOH A O   
3776 O  O   . HOH F .   ? 0.4444 0.4501 0.4904 0.0560  0.0031  -0.0389 478 HOH A O   
3777 O  O   . HOH F .   ? 0.5704 0.3816 0.7126 0.0231  -0.0093 -0.0045 479 HOH A O   
3778 O  O   . HOH F .   ? 0.6860 0.4941 0.6049 -0.1327 0.1083  0.0810  480 HOH A O   
3779 O  O   . HOH F .   ? 0.5310 0.6643 0.7938 -0.1396 -0.0223 -0.0237 481 HOH A O   
3780 O  O   . HOH F .   ? 0.5944 0.6988 0.6609 -0.0684 -0.0043 0.0353  482 HOH A O   
3781 O  O   . HOH F .   ? 0.7267 0.6763 0.8197 0.2241  -0.0996 -0.0854 483 HOH A O   
3782 O  O   . HOH F .   ? 0.5863 0.5601 0.6531 -0.0258 0.0980  -0.0703 484 HOH A O   
3783 O  O   . HOH F .   ? 0.6236 0.7067 0.6564 -0.1589 0.0242  -0.0442 485 HOH A O   
3784 O  O   . HOH F .   ? 0.6184 0.7785 0.7403 0.0910  0.1363  -0.2138 486 HOH A O   
3785 O  O   . HOH F .   ? 0.3959 0.7324 0.7778 0.0985  -0.1003 0.0089  487 HOH A O   
3786 O  O   . HOH F .   ? 0.8136 0.5579 0.8618 -0.0570 -0.1433 -0.1034 488 HOH A O   
3787 O  O   . HOH F .   ? 0.6607 0.5969 0.6970 -0.0020 -0.0966 -0.0646 489 HOH A O   
3788 O  O   . HOH F .   ? 0.7379 0.7293 0.7260 -0.0041 -0.0350 -0.0466 490 HOH A O   
3789 O  O   . HOH F .   ? 0.5446 0.5221 0.6803 0.1152  0.0347  -0.0828 491 HOH A O   
3790 O  O   . HOH F .   ? 0.8230 0.4887 0.6423 -0.0201 0.0151  0.0190  492 HOH A O   
3791 O  O   . HOH F .   ? 0.8479 0.6095 0.6278 0.0872  -0.2187 -0.0564 493 HOH A O   
3792 O  O   . HOH F .   ? 0.5488 0.6219 0.5907 -0.0821 0.0258  0.0341  494 HOH A O   
3793 O  O   . HOH F .   ? 0.6396 0.5804 0.7062 0.0446  0.1258  0.0452  495 HOH A O   
3794 O  O   . HOH F .   ? 0.7926 0.7606 0.7330 0.0065  -0.2909 -0.0912 496 HOH A O   
3795 O  O   . HOH F .   ? 0.6552 0.5818 0.5537 -0.1322 -0.1318 -0.0224 497 HOH A O   
3796 O  O   . HOH F .   ? 0.7840 0.6180 0.6722 0.1045  -0.1826 0.2028  498 HOH A O   
3797 O  O   . HOH F .   ? 0.6573 0.4948 0.5913 -0.1124 -0.1879 -0.0675 499 HOH A O   
3798 O  O   . HOH F .   ? 1.4932 1.4895 1.5177 0.0189  0.0043  -0.0423 500 HOH A O   
3799 O  O   . HOH F .   ? 0.9993 0.8106 0.9006 -0.1209 -0.0613 0.2806  501 HOH A O   
3800 O  O   . HOH F .   ? 1.0641 0.8528 0.8921 0.0730  -0.0324 -0.0478 502 HOH A O   
3801 O  O   . HOH F .   ? 0.8858 1.0263 0.9933 -0.1621 -0.1251 0.0311  503 HOH A O   
3802 O  O   . HOH F .   ? 0.6857 0.5580 0.8514 0.0577  0.1021  -0.0669 504 HOH A O   
3803 O  O   . HOH F .   ? 1.0447 0.9293 0.9346 -0.1386 -0.0004 0.1699  505 HOH A O   
3804 O  O   . HOH F .   ? 0.8975 0.8141 0.7474 0.1738  -0.1964 0.2770  506 HOH A O   
3805 O  O   . HOH F .   ? 0.9293 0.8769 0.9043 -0.0369 -0.0497 0.1211  507 HOH A O   
3806 O  O   . HOH F .   ? 1.5517 1.5856 1.5675 0.0329  0.0420  -0.0252 508 HOH A O   
3807 O  O   . HOH F .   ? 1.7710 1.7696 1.7917 0.0264  0.0547  -0.0113 509 HOH A O   
3808 O  O   . HOH F .   ? 0.9992 1.0884 1.1654 0.1755  0.0222  -0.0261 510 HOH A O   
3809 O  O   . HOH F .   ? 0.9919 0.9045 0.9126 0.0624  -0.1540 -0.0919 511 HOH A O   
3810 O  O   . HOH F .   ? 0.7846 1.0570 0.6948 0.0235  -0.1943 -0.0089 512 HOH A O   
3811 O  O   . HOH F .   ? 0.7282 0.6508 0.8786 0.1685  -0.1794 0.0587  513 HOH A O   
3812 O  O   . HOH F .   ? 0.7802 0.8403 0.7783 -0.0541 -0.1062 0.0667  514 HOH A O   
3813 O  O   . HOH F .   ? 0.7916 0.6343 0.6773 -0.0008 0.0357  -0.0808 515 HOH A O   
3814 O  O   . HOH F .   ? 0.8175 0.5989 0.9125 -0.1891 -0.2144 -0.0103 516 HOH A O   
3815 O  O   . HOH F .   ? 0.7469 0.8758 0.8143 -0.0588 0.1068  0.0177  517 HOH A O   
3816 O  O   . HOH F .   ? 0.6461 0.7321 0.7928 0.1671  0.0316  0.1363  518 HOH A O   
3817 O  O   . HOH F .   ? 1.4563 1.5014 1.5093 0.0292  0.0087  -0.0402 519 HOH A O   
3818 O  O   . HOH G .   ? 0.6834 0.3554 0.5921 0.0624  -0.1835 0.0673  301 HOH B O   
3819 O  O   . HOH G .   ? 0.2124 0.1046 0.2135 0.0118  -0.0518 -0.0113 302 HOH B O   
3820 O  O   . HOH G .   ? 0.3374 0.1172 0.2955 0.0132  -0.1115 0.0015  303 HOH B O   
3821 O  O   . HOH G .   ? 0.3329 0.1238 0.2723 0.0114  -0.0646 0.0153  304 HOH B O   
3822 O  O   . HOH G .   ? 0.4628 0.2621 0.3935 -0.0071 -0.1112 0.0747  305 HOH B O   
3823 O  O   . HOH G .   ? 0.2348 0.1383 0.2624 -0.0179 -0.0528 -0.0173 306 HOH B O   
3824 O  O   . HOH G .   ? 0.2494 0.0856 0.2482 0.0125  -0.0636 0.0116  307 HOH B O   
3825 O  O   . HOH G .   ? 0.2380 0.2542 0.3619 0.0122  -0.0232 0.0317  308 HOH B O   
3826 O  O   . HOH G .   ? 0.2756 0.1402 0.4141 -0.0187 0.0729  -0.0329 309 HOH B O   
3827 O  O   . HOH G .   ? 0.2688 0.1507 0.2819 0.0158  -0.0052 0.0037  310 HOH B O   
3828 O  O   . HOH G .   ? 0.4417 0.3930 0.3678 -0.0260 0.0081  -0.0814 311 HOH B O   
3829 O  O   . HOH G .   ? 0.4799 0.2371 0.5522 -0.1484 -0.0506 0.0274  312 HOH B O   
3830 O  O   . HOH G .   ? 0.4426 0.2084 0.4056 0.0228  -0.1390 -0.0024 313 HOH B O   
3831 O  O   . HOH G .   ? 0.3810 0.1663 0.3668 0.0170  -0.0106 -0.0251 314 HOH B O   
3832 O  O   . HOH G .   ? 0.2755 0.2260 0.2701 0.0115  -0.0857 0.0485  315 HOH B O   
3833 O  O   . HOH G .   ? 0.3060 0.1908 0.3275 0.0007  -0.0175 0.0043  316 HOH B O   
3834 O  O   . HOH G .   ? 0.3022 0.1244 0.2797 -0.0076 -0.0828 -0.0138 317 HOH B O   
3835 O  O   . HOH G .   ? 0.2814 0.1391 0.2522 0.0055  -0.0365 0.0442  318 HOH B O   
3836 O  O   . HOH G .   ? 0.2658 0.2441 0.2895 0.0140  -0.0077 0.0234  319 HOH B O   
3837 O  O   . HOH G .   ? 0.5200 0.2348 0.3953 0.0250  -0.1901 -0.0163 320 HOH B O   
3838 O  O   . HOH G .   ? 0.3231 0.1399 0.2700 -0.0242 -0.0782 0.0406  321 HOH B O   
3839 O  O   . HOH G .   ? 0.4638 0.4017 0.4703 -0.1138 -0.2104 0.1207  322 HOH B O   
3840 O  O   . HOH G .   ? 0.2821 0.2097 0.3235 0.0040  -0.0129 0.0188  323 HOH B O   
3841 O  O   . HOH G .   ? 0.2891 0.1247 0.2812 -0.0072 -0.1106 -0.0025 324 HOH B O   
3842 O  O   . HOH G .   ? 0.3746 0.1677 0.3749 -0.0126 -0.1283 -0.0857 325 HOH B O   
3843 O  O   . HOH G .   ? 0.7081 0.2753 0.4712 0.0012  0.0145  -0.0300 326 HOH B O   
3844 O  O   . HOH G .   ? 0.5005 0.5297 0.3964 -0.1194 0.0120  -0.1334 327 HOH B O   
3845 O  O   . HOH G .   ? 0.3797 0.3237 0.4679 0.0066  -0.0158 0.0575  328 HOH B O   
3846 O  O   . HOH G .   ? 0.3820 0.2632 0.8666 0.0379  0.0333  0.0816  329 HOH B O   
3847 O  O   . HOH G .   ? 0.4033 0.2517 0.4580 -0.0706 -0.1305 -0.0595 330 HOH B O   
3848 O  O   . HOH G .   ? 0.4406 0.3072 0.4022 -0.0854 0.0595  -0.0797 331 HOH B O   
3849 O  O   . HOH G .   ? 0.6204 0.2336 0.3266 0.1929  -0.1836 -0.0786 332 HOH B O   
3850 O  O   . HOH G .   ? 0.3531 0.2994 0.3737 -0.0817 -0.0280 -0.0011 333 HOH B O   
3851 O  O   . HOH G .   ? 0.2813 0.2591 0.3823 -0.0208 -0.1008 0.0121  334 HOH B O   
3852 O  O   . HOH G .   ? 0.4219 0.3498 0.3095 0.1067  -0.2375 -0.1030 335 HOH B O   
3853 O  O   . HOH G .   ? 0.4044 0.4622 0.4745 -0.0849 -0.0403 0.0006  336 HOH B O   
3854 O  O   . HOH G .   ? 0.1873 0.2037 0.6023 -0.0024 -0.1108 -0.1369 337 HOH B O   
3855 O  O   . HOH G .   ? 0.4365 0.2614 0.4860 0.0013  -0.1681 -0.0467 338 HOH B O   
3856 O  O   . HOH G .   ? 0.3072 0.2925 0.4924 -0.0039 -0.0163 -0.0350 339 HOH B O   
3857 O  O   . HOH G .   ? 0.3941 0.2188 0.5249 0.0136  -0.1614 0.0489  340 HOH B O   
3858 O  O   . HOH G .   ? 0.7982 0.6114 0.7581 0.1011  -0.0137 -0.1995 341 HOH B O   
3859 O  O   . HOH G .   ? 0.5217 0.2704 0.3932 -0.1038 -0.2121 0.0584  342 HOH B O   
3860 O  O   . HOH G .   ? 0.4979 0.1329 0.4310 0.0151  -0.2110 0.0098  343 HOH B O   
3861 O  O   . HOH G .   ? 0.5831 0.3675 0.3855 0.0346  -0.1496 -0.0239 344 HOH B O   
3862 O  O   . HOH G .   ? 0.2762 0.5698 0.2873 -0.0627 -0.0214 -0.1248 345 HOH B O   
3863 O  O   . HOH G .   ? 0.2780 0.1046 0.2470 -0.0013 -0.0678 0.0138  346 HOH B O   
3864 O  O   . HOH G .   ? 0.4549 0.1522 0.3854 0.0435  -0.1131 0.0342  347 HOH B O   
3865 O  O   . HOH G .   ? 0.6118 0.2659 0.5647 -0.0408 -0.1330 0.0516  348 HOH B O   
3866 O  O   . HOH G .   ? 0.5230 0.2757 0.4318 -0.0163 -0.2185 -0.0164 349 HOH B O   
3867 O  O   . HOH G .   ? 0.4974 0.3254 0.5506 0.0471  -0.1949 0.0411  350 HOH B O   
3868 O  O   . HOH G .   ? 0.4894 0.4462 0.5658 -0.0849 -0.1341 -0.1095 351 HOH B O   
3869 O  O   . HOH G .   ? 0.6108 0.3710 0.6168 -0.0773 0.0712  0.0560  352 HOH B O   
3870 O  O   . HOH G .   ? 0.5044 0.2814 0.5005 0.0118  -0.1615 -0.0927 353 HOH B O   
3871 O  O   . HOH G .   ? 0.4512 0.4299 0.2710 0.0918  -0.0659 -0.0446 354 HOH B O   
3872 O  O   . HOH G .   ? 0.5293 0.4641 0.7236 -0.1299 0.0375  -0.1818 355 HOH B O   
3873 O  O   . HOH G .   ? 0.6286 0.4794 0.6604 -0.1429 0.0051  -0.0503 356 HOH B O   
3874 O  O   . HOH G .   ? 0.7494 0.3771 0.9601 -0.0823 -0.1386 -0.0760 357 HOH B O   
3875 O  O   . HOH G .   ? 0.4508 0.3276 0.3486 0.0386  -0.0076 0.0002  358 HOH B O   
3876 O  O   . HOH G .   ? 0.7587 0.5824 0.5944 0.0101  -0.2271 -0.1481 359 HOH B O   
3877 O  O   . HOH G .   ? 0.7017 0.2672 0.6013 -0.0812 -0.0891 0.0257  360 HOH B O   
3878 O  O   . HOH G .   ? 0.3523 0.3446 0.5043 -0.0892 -0.1738 -0.0653 361 HOH B O   
3879 O  O   . HOH G .   ? 0.4389 0.2001 0.4900 -0.0634 -0.1790 0.0677  362 HOH B O   
3880 O  O   . HOH G .   ? 0.6762 0.3910 0.7452 0.1330  -0.0447 -0.2795 363 HOH B O   
3881 O  O   . HOH G .   ? 0.3468 0.5524 0.6773 -0.1252 -0.1446 0.1812  364 HOH B O   
3882 O  O   . HOH G .   ? 0.4738 0.6554 0.6956 -0.1465 0.0281  0.0859  365 HOH B O   
3883 O  O   . HOH G .   ? 0.4621 0.2747 0.4603 0.0477  -0.0311 -0.0040 366 HOH B O   
3884 O  O   . HOH G .   ? 0.4470 0.2963 0.5542 0.0583  -0.2482 -0.0754 367 HOH B O   
3885 O  O   . HOH G .   ? 0.5507 0.4619 0.3132 -0.0064 0.0271  -0.0876 368 HOH B O   
3886 O  O   . HOH G .   ? 0.6041 0.5526 0.4186 0.1157  0.0366  0.0334  369 HOH B O   
3887 O  O   . HOH G .   ? 0.6581 0.7831 0.4608 0.0571  0.0609  -0.0359 370 HOH B O   
3888 O  O   . HOH G .   ? 0.5469 0.3357 0.4204 0.0933  -0.0184 0.0470  371 HOH B O   
3889 O  O   . HOH G .   ? 0.5540 0.3860 0.4976 -0.0459 -0.0456 0.0217  372 HOH B O   
3890 O  O   . HOH G .   ? 0.6192 0.4495 0.5022 -0.1204 -0.1705 -0.0367 373 HOH B O   
3891 O  O   . HOH G .   ? 0.6238 0.2570 0.4486 -0.1311 -0.2299 0.0335  374 HOH B O   
3892 O  O   . HOH G .   ? 0.4595 0.4946 0.5227 0.1151  0.0595  -0.0906 375 HOH B O   
3893 O  O   . HOH G .   ? 0.5896 0.5016 0.5555 0.0662  -0.2007 0.0339  376 HOH B O   
3894 O  O   . HOH G .   ? 0.5256 0.3505 0.4152 0.0320  -0.1446 0.0598  377 HOH B O   
3895 O  O   . HOH G .   ? 0.7134 0.6382 0.7697 0.0644  0.0836  -0.0273 378 HOH B O   
3896 O  O   . HOH G .   ? 0.7117 0.2479 0.5442 0.0725  -0.0435 0.0541  379 HOH B O   
3897 O  O   . HOH G .   ? 0.2614 0.2715 0.3766 -0.0002 0.0141  -0.0699 380 HOH B O   
3898 O  O   . HOH G .   ? 0.6970 0.5366 0.7202 0.1649  0.0190  0.1533  381 HOH B O   
3899 O  O   . HOH G .   ? 0.4665 0.3682 0.4705 -0.1565 0.0891  -0.0386 382 HOH B O   
3900 O  O   . HOH G .   ? 0.5149 0.3365 0.5491 -0.0847 0.0933  -0.0862 383 HOH B O   
3901 O  O   . HOH G .   ? 0.3603 0.1809 0.3637 -0.0573 -0.0556 0.0133  384 HOH B O   
3902 O  O   . HOH G .   ? 0.6105 0.4214 0.5214 0.0229  0.0331  -0.0144 385 HOH B O   
3903 O  O   . HOH G .   ? 0.6187 0.5032 0.5488 -0.2797 -0.1722 0.0554  386 HOH B O   
3904 O  O   . HOH G .   ? 0.3555 0.5771 0.6353 -0.0410 0.0899  -0.0685 387 HOH B O   
3905 O  O   . HOH G .   ? 0.3867 0.1960 0.3999 -0.0694 0.0108  0.0475  388 HOH B O   
3906 O  O   . HOH G .   ? 0.6107 0.2254 0.4708 0.1155  -0.1753 -0.0097 389 HOH B O   
3907 O  O   . HOH G .   ? 0.5488 0.4648 0.4705 0.0212  -0.1239 -0.0243 390 HOH B O   
3908 O  O   . HOH G .   ? 0.4257 0.2591 0.5368 0.0033  -0.0693 0.0410  391 HOH B O   
3909 O  O   . HOH G .   ? 0.6591 0.4684 0.5893 0.0609  0.0182  -0.1380 392 HOH B O   
3910 O  O   . HOH G .   ? 0.4684 0.4747 0.5133 -0.0902 -0.0402 0.1108  393 HOH B O   
3911 O  O   . HOH G .   ? 0.4884 0.6902 0.6730 -0.0809 -0.0061 -0.1812 394 HOH B O   
3912 O  O   . HOH G .   ? 0.4632 0.4621 0.5728 -0.0198 -0.1610 -0.0512 395 HOH B O   
3913 O  O   . HOH G .   ? 0.5956 0.7060 0.7928 -0.0277 0.1452  0.0841  396 HOH B O   
3914 O  O   . HOH G .   ? 0.5393 0.4493 0.3955 0.0227  -0.0696 -0.1142 397 HOH B O   
3915 O  O   . HOH G .   ? 0.8060 0.4293 0.5820 0.0360  0.1237  -0.0981 398 HOH B O   
3916 O  O   . HOH G .   ? 0.7565 0.3410 0.4006 0.1224  -0.0861 0.0210  399 HOH B O   
3917 O  O   . HOH G .   ? 0.5980 0.5184 0.6350 0.0399  -0.0345 0.0355  400 HOH B O   
3918 O  O   . HOH G .   ? 0.5594 0.4090 0.6516 0.0919  -0.1527 -0.0400 401 HOH B O   
3919 O  O   . HOH G .   ? 0.5824 0.2717 0.3803 0.0379  -0.1884 0.0070  402 HOH B O   
3920 O  O   . HOH G .   ? 0.5225 0.3282 0.4947 0.0698  0.0287  0.0424  403 HOH B O   
3921 O  O   . HOH G .   ? 0.4143 0.3953 0.5207 0.0099  -0.0381 0.1137  404 HOH B O   
3922 O  O   . HOH G .   ? 0.5506 0.2128 0.4634 -0.0683 -0.0643 -0.0055 405 HOH B O   
3923 O  O   . HOH G .   ? 0.5061 0.5729 0.4290 -0.0842 -0.1334 0.1792  406 HOH B O   
3924 O  O   . HOH G .   ? 0.6866 0.4522 0.7591 0.0757  -0.1060 0.0268  407 HOH B O   
3925 O  O   . HOH G .   ? 0.7824 0.7219 0.6803 0.0562  0.0122  -0.1214 408 HOH B O   
3926 O  O   . HOH G .   ? 0.6641 0.3248 0.5551 0.0575  -0.0980 -0.0257 409 HOH B O   
3927 O  O   . HOH G .   ? 0.8226 0.4238 0.4534 0.0391  0.0274  0.0304  410 HOH B O   
3928 O  O   . HOH G .   ? 0.5221 0.5508 0.7160 -0.0841 -0.2373 0.0213  411 HOH B O   
3929 O  O   . HOH G .   ? 0.4655 0.4111 0.5247 0.1036  -0.1552 -0.0379 412 HOH B O   
3930 O  O   . HOH G .   ? 0.5880 0.4966 0.5178 0.0053  0.0750  0.0257  413 HOH B O   
3931 O  O   . HOH G .   ? 0.5777 0.2328 0.5820 0.0359  -0.2152 0.0918  414 HOH B O   
3932 O  O   . HOH G .   ? 0.5948 0.6734 0.6001 0.3169  0.0988  0.1553  415 HOH B O   
3933 O  O   . HOH G .   ? 0.5796 0.7131 0.4867 0.1563  0.0611  -0.0741 416 HOH B O   
3934 O  O   . HOH G .   ? 0.6183 0.5607 0.5786 0.0704  -0.0358 -0.0687 417 HOH B O   
3935 O  O   . HOH G .   ? 0.5236 0.6174 0.4848 -0.0337 0.1371  -0.0250 418 HOH B O   
3936 O  O   . HOH G .   ? 0.7870 0.3813 0.5228 -0.0918 0.0074  0.0675  419 HOH B O   
3937 O  O   . HOH G .   ? 0.4962 0.5706 0.6154 0.0564  0.0197  -0.0068 420 HOH B O   
3938 O  O   . HOH G .   ? 0.6671 0.6337 0.4329 0.1128  -0.0172 0.1359  421 HOH B O   
3939 O  O   . HOH G .   ? 0.7463 0.5402 0.5921 -0.0390 0.0243  0.1082  422 HOH B O   
3940 O  O   . HOH G .   ? 0.3805 0.4010 0.5618 0.0555  0.1054  0.1807  423 HOH B O   
3941 O  O   . HOH G .   ? 0.7934 0.6688 0.5691 -0.0702 -0.0779 -0.1217 424 HOH B O   
3942 O  O   . HOH G .   ? 0.4190 0.1689 0.5923 0.0130  -0.0484 0.0181  425 HOH B O   
3943 O  O   . HOH G .   ? 0.5286 0.5414 0.5060 -0.0098 -0.0082 0.0272  426 HOH B O   
3944 O  O   . HOH G .   ? 0.4029 0.5980 0.6120 -0.0505 -0.0393 0.0307  427 HOH B O   
3945 O  O   . HOH G .   ? 0.7885 0.2151 0.6215 0.0088  -0.0320 0.0876  428 HOH B O   
3946 O  O   . HOH G .   ? 0.4309 0.2930 0.4927 -0.0535 -0.1483 -0.0401 429 HOH B O   
3947 O  O   . HOH G .   ? 0.7412 0.2414 0.3943 -0.0001 -0.0645 -0.0869 430 HOH B O   
3948 O  O   . HOH G .   ? 0.3636 0.4664 0.5926 -0.0421 -0.0238 -0.1164 431 HOH B O   
3949 O  O   . HOH G .   ? 0.7438 0.6884 0.4888 -0.0040 -0.1104 0.0060  432 HOH B O   
3950 O  O   . HOH G .   ? 0.7858 0.4938 0.4074 0.0955  0.0244  -0.1159 433 HOH B O   
3951 O  O   . HOH G .   ? 0.8381 0.6150 0.6358 -0.1694 -0.0585 0.0611  434 HOH B O   
3952 O  O   . HOH G .   ? 0.7203 0.5640 0.7518 0.1120  -0.0663 -0.2312 435 HOH B O   
3953 O  O   . HOH G .   ? 0.7231 0.7991 0.8353 -0.0296 -0.2415 -0.0452 436 HOH B O   
3954 O  O   . HOH G .   ? 0.7483 0.6777 0.7830 0.0317  -0.0462 0.0936  437 HOH B O   
3955 O  O   . HOH G .   ? 0.4721 0.4622 0.7167 0.1549  0.0425  0.1199  438 HOH B O   
3956 O  O   . HOH G .   ? 0.4963 0.4583 0.6997 -0.0816 -0.2182 0.1405  439 HOH B O   
3957 O  O   . HOH G .   ? 0.7873 0.7447 0.5899 0.2076  -0.1001 0.0373  440 HOH B O   
3958 O  O   . HOH G .   ? 0.5432 0.5302 0.6418 0.0683  0.0747  -0.0608 441 HOH B O   
3959 O  O   . HOH G .   ? 0.5379 0.6386 0.6405 0.0175  0.0443  -0.1042 442 HOH B O   
3960 O  O   . HOH G .   ? 0.4392 0.2857 0.4439 0.0265  -0.1670 -0.0424 443 HOH B O   
3961 O  O   . HOH G .   ? 0.5733 0.7216 0.7350 0.0263  -0.1112 -0.2144 444 HOH B O   
3962 O  O   . HOH G .   ? 0.6992 0.3885 0.4967 -0.1165 -0.2614 0.1071  445 HOH B O   
3963 O  O   . HOH G .   ? 0.4730 0.6171 0.6357 0.1259  -0.1564 0.0124  446 HOH B O   
3964 O  O   . HOH G .   ? 0.7894 0.6129 0.4595 -0.0751 -0.1223 0.1716  447 HOH B O   
3965 O  O   . HOH G .   ? 0.2675 0.1002 0.2228 0.0086  -0.0520 -0.0295 448 HOH B O   
3966 O  O   . HOH G .   ? 0.3928 0.4811 0.6331 -0.0088 0.0762  0.0615  449 HOH B O   
3967 O  O   . HOH G .   ? 0.9507 0.9253 1.0184 -0.0012 -0.0376 0.0018  450 HOH B O   
3968 O  O   . HOH G .   ? 0.6434 0.4178 0.6801 0.0038  -0.1828 -0.1523 451 HOH B O   
3969 O  O   . HOH G .   ? 0.8037 0.5153 0.4409 -0.0877 -0.0705 0.0585  452 HOH B O   
3970 O  O   . HOH G .   ? 0.7058 0.6223 0.6896 -0.0874 0.0265  -0.1319 453 HOH B O   
3971 O  O   . HOH G .   ? 0.5297 0.5640 0.7040 -0.2256 0.0746  -0.1465 454 HOH B O   
3972 O  O   . HOH G .   ? 0.6639 0.6303 0.5344 0.0257  -0.2548 -0.0195 455 HOH B O   
3973 O  O   . HOH G .   ? 0.4650 0.6259 0.5058 -0.0013 -0.0049 0.1710  456 HOH B O   
3974 O  O   . HOH G .   ? 0.5658 0.5366 0.3969 0.2119  -0.0806 -0.0128 457 HOH B O   
3975 O  O   . HOH G .   ? 0.8036 0.7473 0.7401 -0.0284 -0.0586 0.1202  458 HOH B O   
3976 O  O   . HOH G .   ? 0.7584 0.4309 0.6061 -0.0281 -0.1214 -0.2617 459 HOH B O   
3977 O  O   . HOH G .   ? 0.5096 0.5731 0.6204 0.1077  -0.0669 0.0650  460 HOH B O   
3978 O  O   . HOH G .   ? 0.6662 0.6785 0.6213 -0.0636 -0.0635 0.0395  461 HOH B O   
3979 O  O   . HOH G .   ? 0.3764 0.4507 0.4951 0.0209  -0.0044 -0.0580 462 HOH B O   
3980 O  O   . HOH G .   ? 0.7236 0.7232 0.6990 -0.0224 0.0294  0.0267  463 HOH B O   
3981 O  O   . HOH G .   ? 0.5835 0.3675 0.7139 -0.0770 -0.0612 0.0890  464 HOH B O   
3982 O  O   . HOH G .   ? 0.5302 0.5751 0.6156 0.1062  -0.0122 0.1274  465 HOH B O   
3983 O  O   . HOH G .   ? 0.5908 0.5113 0.7268 -0.1791 -0.0701 0.0140  466 HOH B O   
3984 O  O   . HOH G .   ? 0.9033 0.5373 0.7884 0.0075  -0.1574 -0.2952 467 HOH B O   
3985 O  O   . HOH G .   ? 0.7578 0.6605 0.5907 0.0299  0.0933  0.0481  468 HOH B O   
3986 O  O   . HOH G .   ? 0.6768 0.8040 0.7972 0.0111  0.0185  0.0239  469 HOH B O   
3987 O  O   . HOH G .   ? 0.7586 0.6577 0.7160 -0.0861 -0.0212 -0.1376 470 HOH B O   
3988 O  O   . HOH G .   ? 0.7183 0.6341 0.6771 -0.0033 -0.1927 -0.1212 471 HOH B O   
3989 O  O   . HOH G .   ? 0.6973 0.5842 0.8023 0.0099  0.0777  -0.0205 472 HOH B O   
3990 O  O   . HOH G .   ? 0.4680 0.5392 0.6584 0.1329  0.1146  -0.1771 473 HOH B O   
3991 O  O   . HOH G .   ? 0.5695 0.5570 0.6462 -0.0133 -0.1270 -0.0720 474 HOH B O   
3992 O  O   . HOH G .   ? 0.6820 0.4049 0.6792 -0.0871 -0.1641 0.1580  475 HOH B O   
3993 O  O   . HOH G .   ? 0.5383 0.3390 0.5191 -0.1570 0.0618  -0.0224 476 HOH B O   
3994 O  O   . HOH G .   ? 0.7279 0.5097 0.5420 -0.1229 -0.0196 0.1139  477 HOH B O   
3995 O  O   . HOH G .   ? 0.5816 0.8254 0.6936 0.2150  0.1120  0.1273  478 HOH B O   
3996 O  O   . HOH G .   ? 0.6732 0.5217 0.6410 -0.0601 0.0051  -0.0122 479 HOH B O   
3997 O  O   . HOH G .   ? 0.8666 0.8040 0.8317 -0.1566 0.1207  0.2226  480 HOH B O   
3998 O  O   . HOH G .   ? 0.6815 0.4439 0.5774 -0.0031 -0.0168 0.0551  481 HOH B O   
3999 O  O   . HOH G .   ? 0.5725 0.5446 0.5382 -0.0122 -0.0437 -0.0160 482 HOH B O   
4000 O  O   . HOH G .   ? 0.7649 0.7421 0.7244 -0.0313 -0.2598 0.0236  483 HOH B O   
4001 O  O   . HOH G .   ? 1.4168 1.4082 1.4415 0.0460  -0.0323 -0.0484 484 HOH B O   
4002 O  O   . HOH G .   ? 1.2262 1.1955 1.2136 0.0218  -0.1330 0.0039  485 HOH B O   
4003 O  O   . HOH G .   ? 0.9586 1.0134 0.8319 -0.1220 -0.0252 -0.0482 486 HOH B O   
4004 O  O   . HOH G .   ? 0.8374 0.7846 0.8606 -0.0235 -0.0414 -0.0615 487 HOH B O   
4005 O  O   . HOH G .   ? 0.7788 0.6052 0.6829 -0.0004 -0.0549 -0.0689 488 HOH B O   
4006 O  O   . HOH G .   ? 0.9271 0.8228 0.9428 -0.0165 0.0773  0.0217  489 HOH B O   
4007 O  O   . HOH G .   ? 0.9166 0.9306 0.8052 0.0041  0.0650  0.0180  490 HOH B O   
4008 O  O   . HOH G .   ? 0.8207 0.7238 0.8686 -0.0492 -0.1002 0.1303  491 HOH B O   
4009 O  O   . HOH G .   ? 1.4705 1.3568 1.4291 -0.0440 -0.1258 0.0139  492 HOH B O   
4010 O  O   . HOH G .   ? 0.8758 0.8949 0.8867 -0.0729 -0.0187 0.0137  493 HOH B O   
4011 O  O   . HOH G .   ? 0.6768 0.9248 0.8811 -0.1200 0.1345  0.0636  494 HOH B O   
4012 O  O   . HOH G .   ? 0.6758 0.6912 0.6916 -0.1040 -0.0787 0.0257  495 HOH B O   
4013 O  O   . HOH G .   ? 0.7264 0.6371 0.7200 -0.0085 0.0984  0.0188  496 HOH B O   
4014 O  O   . HOH G .   ? 0.7488 0.5795 0.6082 0.1026  -0.0453 -0.1660 497 HOH B O   
4015 O  O   . HOH G .   ? 0.5845 0.6263 0.7096 0.0421  0.0052  -0.0331 498 HOH B O   
4016 O  O   . HOH G .   ? 0.7739 0.6795 0.7905 0.1824  -0.1507 0.0262  499 HOH B O   
4017 O  O   . HOH G .   ? 1.4122 1.4283 1.4673 0.0553  -0.0093 -0.0172 500 HOH B O   
4018 O  O   . HOH G .   ? 0.7311 0.4977 0.5999 -0.0547 -0.1887 0.0831  501 HOH B O   
4019 O  O   . HOH G .   ? 0.8438 0.8736 0.8635 -0.0942 0.1000  0.0438  502 HOH B O   
4020 O  O   . HOH G .   ? 1.2044 1.1903 1.2310 0.0151  -0.1181 0.0189  503 HOH B O   
4021 O  O   . HOH G .   ? 0.6657 0.7827 0.8655 0.0244  -0.0188 -0.1866 504 HOH B O   
4022 O  O   . HOH G .   ? 1.0045 1.1030 0.9105 -0.0100 -0.0183 0.0068  505 HOH B O   
4023 O  O   . HOH G .   ? 0.8021 0.8198 0.7727 0.2079  0.0402  -0.2259 506 HOH B O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   ?   ?   ?   A . n 
A 1 4   PRO 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   MET 9   9   ?   ?   ?   A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  GLN 11  11  11  GLN GLN A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  HIS 25  25  25  HIS HIS A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  MET 34  34  34  MET MET A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ARG 44  44  44  ARG ARG A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  SER 53  53  53  SER SER A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  PHE 79  79  79  PHE PHE A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 TRP 101 101 101 TRP TRP A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 LYS 116 116 116 LYS LYS A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 TYR 134 134 134 TYR TYR A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 GLN 145 145 145 GLN GLN A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 GLN 152 152 152 GLN GLN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LEU 155 155 155 LEU LEU A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 PHE 169 169 169 PHE PHE A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 LYS 179 179 179 LYS LYS A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 GLU 190 190 190 GLU GLU A . n 
A 1 191 MET 191 191 191 MET MET A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 GLU 201 201 201 GLU GLU A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ALA 203 203 203 ALA ALA A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 GLN 212 212 212 GLN GLN A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 PHE 214 214 214 PHE PHE A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 ASP 224 224 ?   ?   ?   A . n 
A 1 225 THR 225 225 ?   ?   ?   A . n 
A 1 226 LYS 226 226 ?   ?   ?   A . n 
A 1 227 ASP 227 227 ?   ?   ?   A . n 
A 1 228 GLN 228 228 ?   ?   ?   A . n 
A 1 229 SER 229 229 ?   ?   ?   A . n 
A 1 230 PRO 230 230 ?   ?   ?   A . n 
A 1 231 SER 231 231 ?   ?   ?   A . n 
A 1 232 ARG 232 232 ?   ?   ?   A . n 
A 1 233 ALA 233 233 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   PRO 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   PRO 6   6   ?   ?   ?   B . n 
B 1 7   ASP 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   MET 9   9   ?   ?   ?   B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  GLN 11  11  11  GLN GLN B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  GLU 23  23  23  GLU GLU B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  HIS 25  25  25  HIS HIS B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  MET 34  34  34  MET MET B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  GLY 40  40  40  GLY GLY B . n 
B 1 41  GLN 41  41  41  GLN GLN B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  ARG 44  44  44  ARG ARG B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  MET 51  51  51  MET MET B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  SER 53  53  53  SER SER B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  TYR 55  55  55  TYR TYR B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  TYR 58  58  58  TYR TYR B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  SER 71  71  71  SER SER B . n 
B 1 72  PRO 72  72  72  PRO PRO B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  PHE 74  74  74  PHE PHE B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  PRO 76  76  76  PRO PRO B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  PHE 79  79  79  PHE PHE B . n 
B 1 80  PRO 80  80  80  PRO PRO B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  HIS 84  84  84  HIS HIS B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  LYS 86  86  86  LYS LYS B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  ALA 88  88  88  ALA ALA B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLN 91  91  91  GLN GLN B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  TRP 96  96  96  TRP TRP B . n 
B 1 97  TYR 97  97  97  TYR TYR B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 ARG 100 100 100 ARG ARG B . n 
B 1 101 TRP 101 101 101 TRP TRP B . n 
B 1 102 GLN 102 102 102 GLN GLN B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 MET 111 111 111 MET MET B . n 
B 1 112 GLN 112 112 112 GLN GLN B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 LYS 116 116 116 LYS LYS B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 VAL 130 130 130 VAL VAL B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 HIS 132 132 132 HIS HIS B . n 
B 1 133 ALA 133 133 133 ALA ALA B . n 
B 1 134 TYR 134 134 134 TYR TYR B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 GLY 144 144 144 GLY GLY B . n 
B 1 145 GLN 145 145 145 GLN GLN B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 GLN 152 152 152 GLN GLN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 LEU 155 155 155 LEU LEU B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 PRO 158 158 158 PRO PRO B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 PHE 166 166 166 PHE PHE B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 PHE 169 169 169 PHE PHE B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASN 171 171 171 ASN ASN B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LYS 177 177 177 LYS LYS B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 LYS 179 179 179 LYS LYS B . n 
B 1 180 GLN 180 180 180 GLN GLN B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 ASN 187 187 187 ASN ASN B . n 
B 1 188 SER 188 188 188 SER SER B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 GLU 190 190 190 GLU GLU B . n 
B 1 191 MET 191 191 191 MET MET B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 PRO 193 193 193 PRO PRO B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 ARG 196 196 196 ARG ARG B . n 
B 1 197 GLN 197 197 197 GLN GLN B . n 
B 1 198 ARG 198 198 198 ARG ARG B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 GLU 201 201 201 GLU GLU B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 ALA 203 203 203 ALA ALA B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 PHE 207 207 207 PHE PHE B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 ASN 210 210 210 ASN ASN B . n 
B 1 211 ILE 211 211 211 ILE ILE B . n 
B 1 212 GLN 212 212 212 GLN GLN B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 PHE 214 214 214 PHE PHE B . n 
B 1 215 GLU 215 215 215 GLU GLU B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 GLN 218 218 218 GLN GLN B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 THR 222 222 222 THR THR B . n 
B 1 223 HIS 223 223 223 HIS HIS B . n 
B 1 224 ASP 224 224 ?   ?   ?   B . n 
B 1 225 THR 225 225 ?   ?   ?   B . n 
B 1 226 LYS 226 226 ?   ?   ?   B . n 
B 1 227 ASP 227 227 ?   ?   ?   B . n 
B 1 228 GLN 228 228 ?   ?   ?   B . n 
B 1 229 SER 229 229 ?   ?   ?   B . n 
B 1 230 PRO 230 230 ?   ?   ?   B . n 
B 1 231 SER 231 231 ?   ?   ?   B . n 
B 1 232 ARG 232 232 ?   ?   ?   B . n 
B 1 233 ALA 233 233 ?   ?   ?   B . n 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? B HIS 25 ? B HIS 25  ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NA ? E HEM . ? B HEM 300 ? 1_555 101.9 ? 
2  NE2 ? B HIS 25 ? B HIS 25  ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NB ? E HEM . ? B HEM 300 ? 1_555 99.0  ? 
3  NA  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NB ? E HEM . ? B HEM 300 ? 1_555 90.3  ? 
4  NE2 ? B HIS 25 ? B HIS 25  ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NC ? E HEM . ? B HEM 300 ? 1_555 85.7  ? 
5  NA  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NC ? E HEM . ? B HEM 300 ? 1_555 172.4 ? 
6  NB  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 NC ? E HEM . ? B HEM 300 ? 1_555 88.6  ? 
7  NE2 ? B HIS 25 ? B HIS 25  ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 ND ? E HEM . ? B HEM 300 ? 1_555 83.3  ? 
8  NA  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 ND ? E HEM . ? B HEM 300 ? 1_555 88.9  ? 
9  NB  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 ND ? E HEM . ? B HEM 300 ? 1_555 177.7 ? 
10 NC  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 ND ? E HEM . ? B HEM 300 ? 1_555 91.9  ? 
11 NE2 ? B HIS 25 ? B HIS 25  ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 O  ? G HOH . ? B HOH 301 ? 1_555 167.9 ? 
12 NA  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 O  ? G HOH . ? B HOH 301 ? 1_555 87.3  ? 
13 NB  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 O  ? G HOH . ? B HOH 301 ? 1_555 88.7  ? 
14 NC  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 O  ? G HOH . ? B HOH 301 ? 1_555 85.1  ? 
15 ND  ? E HEM .  ? B HEM 300 ? 1_555 FE ? E HEM . ? B HEM 300 ? 1_555 O  ? G HOH . ? B HOH 301 ? 1_555 89.1  ? 
16 NE2 ? A HIS 25 ? A HIS 25  ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NA ? D HEM . ? A HEM 300 ? 1_555 88.9  ? 
17 NE2 ? A HIS 25 ? A HIS 25  ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NB ? D HEM . ? A HEM 300 ? 1_555 87.7  ? 
18 NA  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NB ? D HEM . ? A HEM 300 ? 1_555 89.1  ? 
19 NE2 ? A HIS 25 ? A HIS 25  ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NC ? D HEM . ? A HEM 300 ? 1_555 91.3  ? 
20 NA  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NC ? D HEM . ? A HEM 300 ? 1_555 178.1 ? 
21 NB  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 NC ? D HEM . ? A HEM 300 ? 1_555 89.1  ? 
22 NE2 ? A HIS 25 ? A HIS 25  ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 ND ? D HEM . ? A HEM 300 ? 1_555 93.1  ? 
23 NA  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 ND ? D HEM . ? A HEM 300 ? 1_555 90.9  ? 
24 NB  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 ND ? D HEM . ? A HEM 300 ? 1_555 179.2 ? 
25 NC  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 ND ? D HEM . ? A HEM 300 ? 1_555 91.0  ? 
26 NE2 ? A HIS 25 ? A HIS 25  ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 O  ? F HOH . ? A HOH 301 ? 1_555 178.4 ? 
27 NA  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 O  ? F HOH . ? A HOH 301 ? 1_555 90.6  ? 
28 NB  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 O  ? F HOH . ? A HOH 301 ? 1_555 93.8  ? 
29 NC  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 O  ? F HOH . ? A HOH 301 ? 1_555 89.3  ? 
30 ND  ? D HEM .  ? A HEM 300 ? 1_555 FE ? D HEM . ? A HEM 300 ? 1_555 O  ? F HOH . ? A HOH 301 ? 1_555 85.4  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2002-11-13 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       'data reduction' . ? 1 
SCALEPACK   'data scaling'   . ? 2 
MAGICSQUASH 'model building' . ? 3 
AMoRE       phasing          . ? 4 
SHELXL-97   refinement       . ? 5 
MAGICSQUASH phasing          . ? 6 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 NH1 A ARG 85  ? ? CZ A ARG 85  ? ? NH2 A ARG 85  ? ? 126.62 119.40 7.22  1.10 N 
2  1 NE  A ARG 85  ? ? CZ A ARG 85  ? ? NH2 A ARG 85  ? ? 114.46 120.30 -5.84 0.50 N 
3  1 NE  A ARG 100 ? ? CZ A ARG 100 ? ? NH2 A ARG 100 ? ? 116.71 120.30 -3.59 0.50 N 
4  1 CD  A ARG 113 ? ? NE A ARG 113 ? ? CZ  A ARG 113 ? ? 136.04 123.60 12.44 1.40 N 
5  1 NH1 A ARG 123 ? ? CZ A ARG 123 ? ? NH2 A ARG 123 ? ? 128.11 119.40 8.71  1.10 N 
6  1 NE  A ARG 123 ? ? CZ A ARG 123 ? ? NH1 A ARG 123 ? ? 116.64 120.30 -3.66 0.50 N 
7  1 NE  A ARG 123 ? ? CZ A ARG 123 ? ? NH2 A ARG 123 ? ? 115.25 120.30 -5.05 0.50 N 
8  1 NE  A ARG 136 ? ? CZ A ARG 136 ? ? NH1 A ARG 136 ? ? 124.44 120.30 4.14  0.50 N 
9  1 CA  A LEU 157 ? ? CB A LEU 157 ? ? CG  A LEU 157 ? ? 131.68 115.30 16.38 2.30 N 
10 1 CA  A THR 176 ? ? CB A THR 176 ? ? OG1 A THR 176 ? ? 121.73 109.00 12.73 2.10 N 
11 1 NE  A ARG 183 ? ? CZ A ARG 183 ? ? NH1 A ARG 183 ? ? 123.75 120.30 3.45  0.50 N 
12 1 NE  A ARG 196 ? ? CZ A ARG 196 ? ? NH1 A ARG 196 ? ? 125.01 120.30 4.71  0.50 N 
13 1 NE  A ARG 196 ? ? CZ A ARG 196 ? ? NH2 A ARG 196 ? ? 116.86 120.30 -3.44 0.50 N 
14 1 CB  B PHE 37  ? ? CG B PHE 37  ? ? CD1 B PHE 37  ? ? 125.74 120.80 4.94  0.70 N 
15 1 C   B ASP 45  ? ? N  B GLY 46  ? ? CA  B GLY 46  ? ? 135.90 122.30 13.60 2.10 Y 
16 1 NH1 B ARG 85  ? ? CZ B ARG 85  ? ? NH2 B ARG 85  ? ? 126.30 119.40 6.90  1.10 N 
17 1 NE  B ARG 85  ? ? CZ B ARG 85  ? ? NH2 B ARG 85  ? ? 113.45 120.30 -6.85 0.50 N 
18 1 CG  B GLN 91  ? ? CD B GLN 91  ? ? OE1 B GLN 91  ? ? 135.39 121.60 13.79 2.00 N 
19 1 CB  B TYR 97  ? ? CG B TYR 97  ? ? CD1 B TYR 97  ? ? 124.63 121.00 3.63  0.60 N 
20 1 NE  B ARG 100 ? ? CZ B ARG 100 ? ? NH2 B ARG 100 ? ? 116.84 120.30 -3.46 0.50 N 
21 1 CD  B ARG 113 ? ? NE B ARG 113 ? ? CZ  B ARG 113 ? ? 132.03 123.60 8.43  1.40 N 
22 1 NE  B ARG 113 ? ? CZ B ARG 113 ? ? NH1 B ARG 113 ? ? 116.89 120.30 -3.41 0.50 N 
23 1 NE  B ARG 113 ? ? CZ B ARG 113 ? ? NH2 B ARG 113 ? ? 124.58 120.30 4.28  0.50 N 
24 1 NE  B ARG 123 ? ? CZ B ARG 123 ? ? NH2 B ARG 123 ? ? 123.71 120.30 3.41  0.50 N 
25 1 CB  B ASP 156 ? ? CG B ASP 156 ? ? OD2 B ASP 156 ? ? 112.77 118.30 -5.53 0.90 N 
26 1 CA  B GLU 162 ? ? CB B GLU 162 ? ? CG  B GLU 162 ? ? 128.13 113.40 14.73 2.20 N 
27 1 CA  B LEU 189 ? ? CB B LEU 189 ? ? CG  B LEU 189 ? ? 129.80 115.30 14.50 2.30 N 
28 1 NE  B ARG 196 ? ? CZ B ARG 196 ? ? NH2 B ARG 196 ? ? 116.22 120.30 -4.08 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN A 41  ? ? -98.82  51.31  
2 1 PHE A 74  ? ? -137.85 -31.94 
3 1 GLU B 125 ? ? -151.08 61.90  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLU 2   ? A GLU 2   
3  1 Y 1 A ARG 3   ? A ARG 3   
4  1 Y 1 A PRO 4   ? A PRO 4   
5  1 Y 1 A GLN 5   ? A GLN 5   
6  1 Y 1 A PRO 6   ? A PRO 6   
7  1 Y 1 A ASP 7   ? A ASP 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A MET 9   ? A MET 9   
10 1 Y 1 A ASP 224 ? A ASP 224 
11 1 Y 1 A THR 225 ? A THR 225 
12 1 Y 1 A LYS 226 ? A LYS 226 
13 1 Y 1 A ASP 227 ? A ASP 227 
14 1 Y 1 A GLN 228 ? A GLN 228 
15 1 Y 1 A SER 229 ? A SER 229 
16 1 Y 1 A PRO 230 ? A PRO 230 
17 1 Y 1 A SER 231 ? A SER 231 
18 1 Y 1 A ARG 232 ? A ARG 232 
19 1 Y 1 A ALA 233 ? A ALA 233 
20 1 Y 1 B MET 1   ? B MET 1   
21 1 Y 1 B GLU 2   ? B GLU 2   
22 1 Y 1 B ARG 3   ? B ARG 3   
23 1 Y 1 B PRO 4   ? B PRO 4   
24 1 Y 1 B GLN 5   ? B GLN 5   
25 1 Y 1 B PRO 6   ? B PRO 6   
26 1 Y 1 B ASP 7   ? B ASP 7   
27 1 Y 1 B SER 8   ? B SER 8   
28 1 Y 1 B MET 9   ? B MET 9   
29 1 Y 1 B ASP 224 ? B ASP 224 
30 1 Y 1 B THR 225 ? B THR 225 
31 1 Y 1 B LYS 226 ? B LYS 226 
32 1 Y 1 B ASP 227 ? B ASP 227 
33 1 Y 1 B GLN 228 ? B GLN 228 
34 1 Y 1 B SER 229 ? B SER 229 
35 1 Y 1 B PRO 230 ? B PRO 230 
36 1 Y 1 B SER 231 ? B SER 231 
37 1 Y 1 B ARG 232 ? B ARG 232 
38 1 Y 1 B ALA 233 ? B ALA 233 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                     SO4 
3 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
4 water                             HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1   234 1   SO4 SO4 A . 
D 3 HEM 1   300 300 HEM HEM A . 
E 3 HEM 1   300 300 HEM HEM B . 
F 4 HOH 1   301 2   HOH HOH A . 
F 4 HOH 2   302 4   HOH HOH A . 
F 4 HOH 3   303 5   HOH HOH A . 
F 4 HOH 4   304 9   HOH HOH A . 
F 4 HOH 5   305 12  HOH HOH A . 
F 4 HOH 6   306 14  HOH HOH A . 
F 4 HOH 7   307 16  HOH HOH A . 
F 4 HOH 8   308 19  HOH HOH A . 
F 4 HOH 9   309 20  HOH HOH A . 
F 4 HOH 10  310 22  HOH HOH A . 
F 4 HOH 11  311 24  HOH HOH A . 
F 4 HOH 12  312 25  HOH HOH A . 
F 4 HOH 13  313 29  HOH HOH A . 
F 4 HOH 14  314 32  HOH HOH A . 
F 4 HOH 15  315 33  HOH HOH A . 
F 4 HOH 16  316 37  HOH HOH A . 
F 4 HOH 17  317 39  HOH HOH A . 
F 4 HOH 18  318 40  HOH HOH A . 
F 4 HOH 19  319 44  HOH HOH A . 
F 4 HOH 20  320 45  HOH HOH A . 
F 4 HOH 21  321 48  HOH HOH A . 
F 4 HOH 22  322 51  HOH HOH A . 
F 4 HOH 23  323 53  HOH HOH A . 
F 4 HOH 24  324 55  HOH HOH A . 
F 4 HOH 25  325 60  HOH HOH A . 
F 4 HOH 26  326 63  HOH HOH A . 
F 4 HOH 27  327 72  HOH HOH A . 
F 4 HOH 28  328 73  HOH HOH A . 
F 4 HOH 29  329 75  HOH HOH A . 
F 4 HOH 30  330 76  HOH HOH A . 
F 4 HOH 31  331 77  HOH HOH A . 
F 4 HOH 32  332 82  HOH HOH A . 
F 4 HOH 33  333 83  HOH HOH A . 
F 4 HOH 34  334 85  HOH HOH A . 
F 4 HOH 35  335 86  HOH HOH A . 
F 4 HOH 36  336 87  HOH HOH A . 
F 4 HOH 37  337 88  HOH HOH A . 
F 4 HOH 38  338 89  HOH HOH A . 
F 4 HOH 39  339 90  HOH HOH A . 
F 4 HOH 40  340 92  HOH HOH A . 
F 4 HOH 41  341 95  HOH HOH A . 
F 4 HOH 42  342 96  HOH HOH A . 
F 4 HOH 43  343 98  HOH HOH A . 
F 4 HOH 44  344 102 HOH HOH A . 
F 4 HOH 45  345 103 HOH HOH A . 
F 4 HOH 46  346 104 HOH HOH A . 
F 4 HOH 47  347 105 HOH HOH A . 
F 4 HOH 48  348 106 HOH HOH A . 
F 4 HOH 49  349 107 HOH HOH A . 
F 4 HOH 50  350 108 HOH HOH A . 
F 4 HOH 51  351 109 HOH HOH A . 
F 4 HOH 52  352 110 HOH HOH A . 
F 4 HOH 53  353 111 HOH HOH A . 
F 4 HOH 54  354 112 HOH HOH A . 
F 4 HOH 55  355 113 HOH HOH A . 
F 4 HOH 56  356 114 HOH HOH A . 
F 4 HOH 57  357 115 HOH HOH A . 
F 4 HOH 58  358 116 HOH HOH A . 
F 4 HOH 59  359 117 HOH HOH A . 
F 4 HOH 60  360 118 HOH HOH A . 
F 4 HOH 61  361 119 HOH HOH A . 
F 4 HOH 62  362 120 HOH HOH A . 
F 4 HOH 63  363 121 HOH HOH A . 
F 4 HOH 64  364 127 HOH HOH A . 
F 4 HOH 65  365 128 HOH HOH A . 
F 4 HOH 66  366 129 HOH HOH A . 
F 4 HOH 67  367 130 HOH HOH A . 
F 4 HOH 68  368 131 HOH HOH A . 
F 4 HOH 69  369 132 HOH HOH A . 
F 4 HOH 70  370 134 HOH HOH A . 
F 4 HOH 71  371 135 HOH HOH A . 
F 4 HOH 72  372 136 HOH HOH A . 
F 4 HOH 73  373 143 HOH HOH A . 
F 4 HOH 74  374 144 HOH HOH A . 
F 4 HOH 75  375 145 HOH HOH A . 
F 4 HOH 76  376 147 HOH HOH A . 
F 4 HOH 77  377 148 HOH HOH A . 
F 4 HOH 78  378 149 HOH HOH A . 
F 4 HOH 79  379 150 HOH HOH A . 
F 4 HOH 80  380 151 HOH HOH A . 
F 4 HOH 81  381 152 HOH HOH A . 
F 4 HOH 82  382 153 HOH HOH A . 
F 4 HOH 83  383 154 HOH HOH A . 
F 4 HOH 84  384 165 HOH HOH A . 
F 4 HOH 85  385 166 HOH HOH A . 
F 4 HOH 86  386 168 HOH HOH A . 
F 4 HOH 87  387 169 HOH HOH A . 
F 4 HOH 88  388 177 HOH HOH A . 
F 4 HOH 89  389 178 HOH HOH A . 
F 4 HOH 90  390 183 HOH HOH A . 
F 4 HOH 91  391 185 HOH HOH A . 
F 4 HOH 92  392 188 HOH HOH A . 
F 4 HOH 93  393 191 HOH HOH A . 
F 4 HOH 94  394 192 HOH HOH A . 
F 4 HOH 95  395 193 HOH HOH A . 
F 4 HOH 96  396 194 HOH HOH A . 
F 4 HOH 97  397 198 HOH HOH A . 
F 4 HOH 98  398 199 HOH HOH A . 
F 4 HOH 99  399 200 HOH HOH A . 
F 4 HOH 100 400 202 HOH HOH A . 
F 4 HOH 101 401 203 HOH HOH A . 
F 4 HOH 102 402 204 HOH HOH A . 
F 4 HOH 103 403 205 HOH HOH A . 
F 4 HOH 104 404 206 HOH HOH A . 
F 4 HOH 105 405 207 HOH HOH A . 
F 4 HOH 106 406 208 HOH HOH A . 
F 4 HOH 107 407 209 HOH HOH A . 
F 4 HOH 108 408 212 HOH HOH A . 
F 4 HOH 109 409 216 HOH HOH A . 
F 4 HOH 110 410 218 HOH HOH A . 
F 4 HOH 111 411 219 HOH HOH A . 
F 4 HOH 112 412 220 HOH HOH A . 
F 4 HOH 113 413 221 HOH HOH A . 
F 4 HOH 114 414 222 HOH HOH A . 
F 4 HOH 115 415 223 HOH HOH A . 
F 4 HOH 116 416 224 HOH HOH A . 
F 4 HOH 117 417 225 HOH HOH A . 
F 4 HOH 118 418 226 HOH HOH A . 
F 4 HOH 119 419 227 HOH HOH A . 
F 4 HOH 120 420 228 HOH HOH A . 
F 4 HOH 121 421 229 HOH HOH A . 
F 4 HOH 122 422 230 HOH HOH A . 
F 4 HOH 123 423 231 HOH HOH A . 
F 4 HOH 124 424 232 HOH HOH A . 
F 4 HOH 125 425 237 HOH HOH A . 
F 4 HOH 126 426 238 HOH HOH A . 
F 4 HOH 127 427 247 HOH HOH A . 
F 4 HOH 128 428 248 HOH HOH A . 
F 4 HOH 129 429 249 HOH HOH A . 
F 4 HOH 130 430 251 HOH HOH A . 
F 4 HOH 131 431 254 HOH HOH A . 
F 4 HOH 132 432 255 HOH HOH A . 
F 4 HOH 133 433 256 HOH HOH A . 
F 4 HOH 134 434 264 HOH HOH A . 
F 4 HOH 135 435 265 HOH HOH A . 
F 4 HOH 136 436 266 HOH HOH A . 
F 4 HOH 137 437 267 HOH HOH A . 
F 4 HOH 138 438 268 HOH HOH A . 
F 4 HOH 139 439 269 HOH HOH A . 
F 4 HOH 140 440 270 HOH HOH A . 
F 4 HOH 141 441 272 HOH HOH A . 
F 4 HOH 142 442 273 HOH HOH A . 
F 4 HOH 143 443 274 HOH HOH A . 
F 4 HOH 144 444 275 HOH HOH A . 
F 4 HOH 145 445 277 HOH HOH A . 
F 4 HOH 146 446 278 HOH HOH A . 
F 4 HOH 147 447 279 HOH HOH A . 
F 4 HOH 148 448 280 HOH HOH A . 
F 4 HOH 149 449 281 HOH HOH A . 
F 4 HOH 150 450 282 HOH HOH A . 
F 4 HOH 151 451 283 HOH HOH A . 
F 4 HOH 152 452 284 HOH HOH A . 
F 4 HOH 153 453 294 HOH HOH A . 
F 4 HOH 154 454 295 HOH HOH A . 
F 4 HOH 155 455 296 HOH HOH A . 
F 4 HOH 156 456 297 HOH HOH A . 
F 4 HOH 157 457 298 HOH HOH A . 
F 4 HOH 158 458 299 HOH HOH A . 
F 4 HOH 159 459 300 HOH HOH A . 
F 4 HOH 160 460 307 HOH HOH A . 
F 4 HOH 161 461 308 HOH HOH A . 
F 4 HOH 162 462 309 HOH HOH A . 
F 4 HOH 163 463 312 HOH HOH A . 
F 4 HOH 164 464 313 HOH HOH A . 
F 4 HOH 165 465 314 HOH HOH A . 
F 4 HOH 166 466 315 HOH HOH A . 
F 4 HOH 167 467 316 HOH HOH A . 
F 4 HOH 168 468 317 HOH HOH A . 
F 4 HOH 169 469 319 HOH HOH A . 
F 4 HOH 170 470 320 HOH HOH A . 
F 4 HOH 171 471 321 HOH HOH A . 
F 4 HOH 172 472 322 HOH HOH A . 
F 4 HOH 173 473 323 HOH HOH A . 
F 4 HOH 174 474 324 HOH HOH A . 
F 4 HOH 175 475 330 HOH HOH A . 
F 4 HOH 176 476 331 HOH HOH A . 
F 4 HOH 177 477 333 HOH HOH A . 
F 4 HOH 178 478 335 HOH HOH A . 
F 4 HOH 179 479 336 HOH HOH A . 
F 4 HOH 180 480 337 HOH HOH A . 
F 4 HOH 181 481 344 HOH HOH A . 
F 4 HOH 182 482 346 HOH HOH A . 
F 4 HOH 183 483 349 HOH HOH A . 
F 4 HOH 184 484 355 HOH HOH A . 
F 4 HOH 185 485 361 HOH HOH A . 
F 4 HOH 186 486 363 HOH HOH A . 
F 4 HOH 187 487 365 HOH HOH A . 
F 4 HOH 188 488 367 HOH HOH A . 
F 4 HOH 189 489 368 HOH HOH A . 
F 4 HOH 190 490 369 HOH HOH A . 
F 4 HOH 191 491 370 HOH HOH A . 
F 4 HOH 192 492 372 HOH HOH A . 
F 4 HOH 193 493 374 HOH HOH A . 
F 4 HOH 194 494 375 HOH HOH A . 
F 4 HOH 195 495 377 HOH HOH A . 
F 4 HOH 196 496 379 HOH HOH A . 
F 4 HOH 197 497 380 HOH HOH A . 
F 4 HOH 198 498 381 HOH HOH A . 
F 4 HOH 199 499 382 HOH HOH A . 
F 4 HOH 200 500 386 HOH HOH A . 
F 4 HOH 201 501 387 HOH HOH A . 
F 4 HOH 202 502 388 HOH HOH A . 
F 4 HOH 203 503 389 HOH HOH A . 
F 4 HOH 204 504 392 HOH HOH A . 
F 4 HOH 205 505 393 HOH HOH A . 
F 4 HOH 206 506 396 HOH HOH A . 
F 4 HOH 207 507 400 HOH HOH A . 
F 4 HOH 208 508 401 HOH HOH A . 
F 4 HOH 209 509 404 HOH HOH A . 
F 4 HOH 210 510 405 HOH HOH A . 
F 4 HOH 211 511 408 HOH HOH A . 
F 4 HOH 212 512 410 HOH HOH A . 
F 4 HOH 213 513 411 HOH HOH A . 
F 4 HOH 214 514 412 HOH HOH A . 
F 4 HOH 215 515 414 HOH HOH A . 
F 4 HOH 216 516 415 HOH HOH A . 
F 4 HOH 217 517 416 HOH HOH A . 
F 4 HOH 218 518 419 HOH HOH A . 
F 4 HOH 219 519 424 HOH HOH A . 
G 4 HOH 1   301 3   HOH HOH B . 
G 4 HOH 2   302 6   HOH HOH B . 
G 4 HOH 3   303 7   HOH HOH B . 
G 4 HOH 4   304 8   HOH HOH B . 
G 4 HOH 5   305 10  HOH HOH B . 
G 4 HOH 6   306 11  HOH HOH B . 
G 4 HOH 7   307 13  HOH HOH B . 
G 4 HOH 8   308 15  HOH HOH B . 
G 4 HOH 9   309 17  HOH HOH B . 
G 4 HOH 10  310 18  HOH HOH B . 
G 4 HOH 11  311 21  HOH HOH B . 
G 4 HOH 12  312 23  HOH HOH B . 
G 4 HOH 13  313 26  HOH HOH B . 
G 4 HOH 14  314 27  HOH HOH B . 
G 4 HOH 15  315 28  HOH HOH B . 
G 4 HOH 16  316 30  HOH HOH B . 
G 4 HOH 17  317 31  HOH HOH B . 
G 4 HOH 18  318 34  HOH HOH B . 
G 4 HOH 19  319 35  HOH HOH B . 
G 4 HOH 20  320 36  HOH HOH B . 
G 4 HOH 21  321 38  HOH HOH B . 
G 4 HOH 22  322 41  HOH HOH B . 
G 4 HOH 23  323 42  HOH HOH B . 
G 4 HOH 24  324 43  HOH HOH B . 
G 4 HOH 25  325 46  HOH HOH B . 
G 4 HOH 26  326 47  HOH HOH B . 
G 4 HOH 27  327 49  HOH HOH B . 
G 4 HOH 28  328 50  HOH HOH B . 
G 4 HOH 29  329 52  HOH HOH B . 
G 4 HOH 30  330 54  HOH HOH B . 
G 4 HOH 31  331 56  HOH HOH B . 
G 4 HOH 32  332 57  HOH HOH B . 
G 4 HOH 33  333 58  HOH HOH B . 
G 4 HOH 34  334 59  HOH HOH B . 
G 4 HOH 35  335 61  HOH HOH B . 
G 4 HOH 36  336 62  HOH HOH B . 
G 4 HOH 37  337 64  HOH HOH B . 
G 4 HOH 38  338 65  HOH HOH B . 
G 4 HOH 39  339 66  HOH HOH B . 
G 4 HOH 40  340 67  HOH HOH B . 
G 4 HOH 41  341 68  HOH HOH B . 
G 4 HOH 42  342 69  HOH HOH B . 
G 4 HOH 43  343 70  HOH HOH B . 
G 4 HOH 44  344 71  HOH HOH B . 
G 4 HOH 45  345 74  HOH HOH B . 
G 4 HOH 46  346 78  HOH HOH B . 
G 4 HOH 47  347 79  HOH HOH B . 
G 4 HOH 48  348 80  HOH HOH B . 
G 4 HOH 49  349 81  HOH HOH B . 
G 4 HOH 50  350 84  HOH HOH B . 
G 4 HOH 51  351 91  HOH HOH B . 
G 4 HOH 52  352 93  HOH HOH B . 
G 4 HOH 53  353 94  HOH HOH B . 
G 4 HOH 54  354 97  HOH HOH B . 
G 4 HOH 55  355 99  HOH HOH B . 
G 4 HOH 56  356 100 HOH HOH B . 
G 4 HOH 57  357 101 HOH HOH B . 
G 4 HOH 58  358 122 HOH HOH B . 
G 4 HOH 59  359 123 HOH HOH B . 
G 4 HOH 60  360 124 HOH HOH B . 
G 4 HOH 61  361 125 HOH HOH B . 
G 4 HOH 62  362 126 HOH HOH B . 
G 4 HOH 63  363 133 HOH HOH B . 
G 4 HOH 64  364 137 HOH HOH B . 
G 4 HOH 65  365 138 HOH HOH B . 
G 4 HOH 66  366 139 HOH HOH B . 
G 4 HOH 67  367 140 HOH HOH B . 
G 4 HOH 68  368 141 HOH HOH B . 
G 4 HOH 69  369 142 HOH HOH B . 
G 4 HOH 70  370 146 HOH HOH B . 
G 4 HOH 71  371 155 HOH HOH B . 
G 4 HOH 72  372 156 HOH HOH B . 
G 4 HOH 73  373 157 HOH HOH B . 
G 4 HOH 74  374 158 HOH HOH B . 
G 4 HOH 75  375 159 HOH HOH B . 
G 4 HOH 76  376 160 HOH HOH B . 
G 4 HOH 77  377 161 HOH HOH B . 
G 4 HOH 78  378 162 HOH HOH B . 
G 4 HOH 79  379 163 HOH HOH B . 
G 4 HOH 80  380 164 HOH HOH B . 
G 4 HOH 81  381 167 HOH HOH B . 
G 4 HOH 82  382 170 HOH HOH B . 
G 4 HOH 83  383 171 HOH HOH B . 
G 4 HOH 84  384 172 HOH HOH B . 
G 4 HOH 85  385 173 HOH HOH B . 
G 4 HOH 86  386 174 HOH HOH B . 
G 4 HOH 87  387 175 HOH HOH B . 
G 4 HOH 88  388 176 HOH HOH B . 
G 4 HOH 89  389 179 HOH HOH B . 
G 4 HOH 90  390 180 HOH HOH B . 
G 4 HOH 91  391 181 HOH HOH B . 
G 4 HOH 92  392 182 HOH HOH B . 
G 4 HOH 93  393 184 HOH HOH B . 
G 4 HOH 94  394 186 HOH HOH B . 
G 4 HOH 95  395 187 HOH HOH B . 
G 4 HOH 96  396 189 HOH HOH B . 
G 4 HOH 97  397 190 HOH HOH B . 
G 4 HOH 98  398 195 HOH HOH B . 
G 4 HOH 99  399 196 HOH HOH B . 
G 4 HOH 100 400 197 HOH HOH B . 
G 4 HOH 101 401 201 HOH HOH B . 
G 4 HOH 102 402 210 HOH HOH B . 
G 4 HOH 103 403 211 HOH HOH B . 
G 4 HOH 104 404 213 HOH HOH B . 
G 4 HOH 105 405 214 HOH HOH B . 
G 4 HOH 106 406 215 HOH HOH B . 
G 4 HOH 107 407 217 HOH HOH B . 
G 4 HOH 108 408 233 HOH HOH B . 
G 4 HOH 109 409 234 HOH HOH B . 
G 4 HOH 110 410 235 HOH HOH B . 
G 4 HOH 111 411 236 HOH HOH B . 
G 4 HOH 112 412 239 HOH HOH B . 
G 4 HOH 113 413 240 HOH HOH B . 
G 4 HOH 114 414 241 HOH HOH B . 
G 4 HOH 115 415 242 HOH HOH B . 
G 4 HOH 116 416 243 HOH HOH B . 
G 4 HOH 117 417 244 HOH HOH B . 
G 4 HOH 118 418 245 HOH HOH B . 
G 4 HOH 119 419 246 HOH HOH B . 
G 4 HOH 120 420 250 HOH HOH B . 
G 4 HOH 121 421 252 HOH HOH B . 
G 4 HOH 122 422 253 HOH HOH B . 
G 4 HOH 123 423 257 HOH HOH B . 
G 4 HOH 124 424 258 HOH HOH B . 
G 4 HOH 125 425 259 HOH HOH B . 
G 4 HOH 126 426 260 HOH HOH B . 
G 4 HOH 127 427 261 HOH HOH B . 
G 4 HOH 128 428 262 HOH HOH B . 
G 4 HOH 129 429 263 HOH HOH B . 
G 4 HOH 130 430 271 HOH HOH B . 
G 4 HOH 131 431 276 HOH HOH B . 
G 4 HOH 132 432 285 HOH HOH B . 
G 4 HOH 133 433 286 HOH HOH B . 
G 4 HOH 134 434 287 HOH HOH B . 
G 4 HOH 135 435 288 HOH HOH B . 
G 4 HOH 136 436 289 HOH HOH B . 
G 4 HOH 137 437 290 HOH HOH B . 
G 4 HOH 138 438 291 HOH HOH B . 
G 4 HOH 139 439 292 HOH HOH B . 
G 4 HOH 140 440 293 HOH HOH B . 
G 4 HOH 141 441 301 HOH HOH B . 
G 4 HOH 142 442 302 HOH HOH B . 
G 4 HOH 143 443 303 HOH HOH B . 
G 4 HOH 144 444 304 HOH HOH B . 
G 4 HOH 145 445 305 HOH HOH B . 
G 4 HOH 146 446 306 HOH HOH B . 
G 4 HOH 147 447 310 HOH HOH B . 
G 4 HOH 148 448 311 HOH HOH B . 
G 4 HOH 149 449 318 HOH HOH B . 
G 4 HOH 150 450 325 HOH HOH B . 
G 4 HOH 151 451 326 HOH HOH B . 
G 4 HOH 152 452 327 HOH HOH B . 
G 4 HOH 153 453 328 HOH HOH B . 
G 4 HOH 154 454 329 HOH HOH B . 
G 4 HOH 155 455 332 HOH HOH B . 
G 4 HOH 156 456 334 HOH HOH B . 
G 4 HOH 157 457 338 HOH HOH B . 
G 4 HOH 158 458 339 HOH HOH B . 
G 4 HOH 159 459 340 HOH HOH B . 
G 4 HOH 160 460 341 HOH HOH B . 
G 4 HOH 161 461 342 HOH HOH B . 
G 4 HOH 162 462 343 HOH HOH B . 
G 4 HOH 163 463 345 HOH HOH B . 
G 4 HOH 164 464 347 HOH HOH B . 
G 4 HOH 165 465 348 HOH HOH B . 
G 4 HOH 166 466 350 HOH HOH B . 
G 4 HOH 167 467 351 HOH HOH B . 
G 4 HOH 168 468 352 HOH HOH B . 
G 4 HOH 169 469 353 HOH HOH B . 
G 4 HOH 170 470 354 HOH HOH B . 
G 4 HOH 171 471 356 HOH HOH B . 
G 4 HOH 172 472 357 HOH HOH B . 
G 4 HOH 173 473 358 HOH HOH B . 
G 4 HOH 174 474 359 HOH HOH B . 
G 4 HOH 175 475 360 HOH HOH B . 
G 4 HOH 176 476 362 HOH HOH B . 
G 4 HOH 177 477 364 HOH HOH B . 
G 4 HOH 178 478 366 HOH HOH B . 
G 4 HOH 179 479 371 HOH HOH B . 
G 4 HOH 180 480 373 HOH HOH B . 
G 4 HOH 181 481 376 HOH HOH B . 
G 4 HOH 182 482 378 HOH HOH B . 
G 4 HOH 183 483 383 HOH HOH B . 
G 4 HOH 184 484 384 HOH HOH B . 
G 4 HOH 185 485 385 HOH HOH B . 
G 4 HOH 186 486 390 HOH HOH B . 
G 4 HOH 187 487 391 HOH HOH B . 
G 4 HOH 188 488 394 HOH HOH B . 
G 4 HOH 189 489 395 HOH HOH B . 
G 4 HOH 190 490 397 HOH HOH B . 
G 4 HOH 191 491 398 HOH HOH B . 
G 4 HOH 192 492 399 HOH HOH B . 
G 4 HOH 193 493 402 HOH HOH B . 
G 4 HOH 194 494 403 HOH HOH B . 
G 4 HOH 195 495 406 HOH HOH B . 
G 4 HOH 196 496 407 HOH HOH B . 
G 4 HOH 197 497 409 HOH HOH B . 
G 4 HOH 198 498 413 HOH HOH B . 
G 4 HOH 199 499 417 HOH HOH B . 
G 4 HOH 200 500 418 HOH HOH B . 
G 4 HOH 201 501 420 HOH HOH B . 
G 4 HOH 202 502 421 HOH HOH B . 
G 4 HOH 203 503 422 HOH HOH B . 
G 4 HOH 204 504 423 HOH HOH B . 
G 4 HOH 205 505 425 HOH HOH B . 
G 4 HOH 206 506 426 HOH HOH B . 
# 
