data_1QAE
# 
_entry.id   1QAE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1QAE         
RCSB  RCSB009007   
WWPDB D_1000009007 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1QAE 
_pdbx_database_status.recvd_initial_deposition_date   1999-03-03 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Miller, M.D.' 1 
'Krause, K.L.' 2 
# 
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 'The active site of Serratia endonuclease contains a conserved magnesium-water cluster.'                   J.Mol.Biol. 288 
975 988 1999 JMOBAK UK 0022-2836 0070 ? 10329193 10.1006/jmbi.1999.2729 
1       'Identification of the Serratia Endonuclease Dimer: Structural Basis and Implications for Catalysis'       'Protein Sci.' 
5   24  ?   1996 PRCIEI US 0961-8368 0795 ? ?        ?                      
2       '2.1 Angstroms Structure of Serratia Endonuclease Suggests a Mechanism for Binding to Double-Stranded DNA' 
Nat.Struct.Biol. 1   461 ?   1994 NSBIEW US 1072-8368 2024 ? ?        ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Miller, M.D.'  1  
primary 'Cai, J.'       2  
primary 'Krause, K.L.'  3  
1       'Miller, M.D.'  4  
1       'Krause, K.L.'  5  
2       'Miller, M.D.'  6  
2       'Tanner, J.'    7  
2       'Alpaugh, M.'   8  
2       'Benedik, M.J.' 9  
2       'Krause, K.L.'  10 
# 
_cell.entry_id           1QAE 
_cell.length_a           106.700 
_cell.length_b           74.500 
_cell.length_c           68.900 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         1QAE 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
# 
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 'PROTEIN (EXTRACELLULAR ENDONUCLEASE)' 26738.896 2   3.1.30.2 ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'                        24.305    2   ?        ? ? ? 
3 water       nat water                                  18.015    251 ?        ? ? ? 
# 
_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       
;DTLESIDNCAVGCPTGGSSNVSIVRHAYTLNNNSTTKFANWVAYHITKDTPASGKTRNWKTDPALNPADTLAPADYTGAN
AALKVDRGHQAPLASLAGVSDWESLNYLSNITPQKSDLNQGAWARLEDQERKLIDRADISSVYTVTGPLYERDMGKLPGT
QKAHTIPSAYWKVIFINNSPAVNHYAAFLFDQNTPKGADFCQFRVTVDEIEKRTGLIIWAGLPDDVQASLKSKPGVLPEL
MGCKN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DTLESIDNCAVGCPTGGSSNVSIVRHAYTLNNNSTTKFANWVAYHITKDTPASGKTRNWKTDPALNPADTLAPADYTGAN
AALKVDRGHQAPLASLAGVSDWESLNYLSNITPQKSDLNQGAWARLEDQERKLIDRADISSVYTVTGPLYERDMGKLPGT
QKAHTIPSAYWKVIFINNSPAVNHYAAFLFDQNTPKGADFCQFRVTVDEIEKRTGLIIWAGLPDDVQASLKSKPGVLPEL
MGCKN
;
_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   ASP n 
1 2   THR n 
1 3   LEU n 
1 4   GLU n 
1 5   SER n 
1 6   ILE n 
1 7   ASP n 
1 8   ASN n 
1 9   CYS n 
1 10  ALA n 
1 11  VAL n 
1 12  GLY n 
1 13  CYS n 
1 14  PRO n 
1 15  THR n 
1 16  GLY n 
1 17  GLY n 
1 18  SER n 
1 19  SER n 
1 20  ASN n 
1 21  VAL n 
1 22  SER n 
1 23  ILE n 
1 24  VAL n 
1 25  ARG n 
1 26  HIS n 
1 27  ALA n 
1 28  TYR n 
1 29  THR n 
1 30  LEU n 
1 31  ASN n 
1 32  ASN n 
1 33  ASN n 
1 34  SER n 
1 35  THR n 
1 36  THR n 
1 37  LYS n 
1 38  PHE n 
1 39  ALA n 
1 40  ASN n 
1 41  TRP n 
1 42  VAL n 
1 43  ALA n 
1 44  TYR n 
1 45  HIS n 
1 46  ILE n 
1 47  THR n 
1 48  LYS n 
1 49  ASP n 
1 50  THR n 
1 51  PRO n 
1 52  ALA n 
1 53  SER n 
1 54  GLY n 
1 55  LYS n 
1 56  THR n 
1 57  ARG n 
1 58  ASN n 
1 59  TRP n 
1 60  LYS n 
1 61  THR n 
1 62  ASP n 
1 63  PRO n 
1 64  ALA n 
1 65  LEU n 
1 66  ASN n 
1 67  PRO n 
1 68  ALA n 
1 69  ASP n 
1 70  THR n 
1 71  LEU n 
1 72  ALA n 
1 73  PRO n 
1 74  ALA n 
1 75  ASP n 
1 76  TYR n 
1 77  THR n 
1 78  GLY n 
1 79  ALA n 
1 80  ASN n 
1 81  ALA n 
1 82  ALA n 
1 83  LEU n 
1 84  LYS n 
1 85  VAL n 
1 86  ASP n 
1 87  ARG n 
1 88  GLY n 
1 89  HIS n 
1 90  GLN n 
1 91  ALA n 
1 92  PRO n 
1 93  LEU n 
1 94  ALA n 
1 95  SER n 
1 96  LEU n 
1 97  ALA n 
1 98  GLY n 
1 99  VAL n 
1 100 SER n 
1 101 ASP n 
1 102 TRP n 
1 103 GLU n 
1 104 SER n 
1 105 LEU n 
1 106 ASN n 
1 107 TYR n 
1 108 LEU n 
1 109 SER n 
1 110 ASN n 
1 111 ILE n 
1 112 THR n 
1 113 PRO n 
1 114 GLN n 
1 115 LYS n 
1 116 SER n 
1 117 ASP n 
1 118 LEU n 
1 119 ASN n 
1 120 GLN n 
1 121 GLY n 
1 122 ALA n 
1 123 TRP n 
1 124 ALA n 
1 125 ARG n 
1 126 LEU n 
1 127 GLU n 
1 128 ASP n 
1 129 GLN n 
1 130 GLU n 
1 131 ARG n 
1 132 LYS n 
1 133 LEU n 
1 134 ILE n 
1 135 ASP n 
1 136 ARG n 
1 137 ALA n 
1 138 ASP n 
1 139 ILE n 
1 140 SER n 
1 141 SER n 
1 142 VAL n 
1 143 TYR n 
1 144 THR n 
1 145 VAL n 
1 146 THR n 
1 147 GLY n 
1 148 PRO n 
1 149 LEU n 
1 150 TYR n 
1 151 GLU n 
1 152 ARG n 
1 153 ASP n 
1 154 MET n 
1 155 GLY n 
1 156 LYS n 
1 157 LEU n 
1 158 PRO n 
1 159 GLY n 
1 160 THR n 
1 161 GLN n 
1 162 LYS n 
1 163 ALA n 
1 164 HIS n 
1 165 THR n 
1 166 ILE n 
1 167 PRO n 
1 168 SER n 
1 169 ALA n 
1 170 TYR n 
1 171 TRP n 
1 172 LYS n 
1 173 VAL n 
1 174 ILE n 
1 175 PHE n 
1 176 ILE n 
1 177 ASN n 
1 178 ASN n 
1 179 SER n 
1 180 PRO n 
1 181 ALA n 
1 182 VAL n 
1 183 ASN n 
1 184 HIS n 
1 185 TYR n 
1 186 ALA n 
1 187 ALA n 
1 188 PHE n 
1 189 LEU n 
1 190 PHE n 
1 191 ASP n 
1 192 GLN n 
1 193 ASN n 
1 194 THR n 
1 195 PRO n 
1 196 LYS n 
1 197 GLY n 
1 198 ALA n 
1 199 ASP n 
1 200 PHE n 
1 201 CYS n 
1 202 GLN n 
1 203 PHE n 
1 204 ARG n 
1 205 VAL n 
1 206 THR n 
1 207 VAL n 
1 208 ASP n 
1 209 GLU n 
1 210 ILE n 
1 211 GLU n 
1 212 LYS n 
1 213 ARG n 
1 214 THR n 
1 215 GLY n 
1 216 LEU n 
1 217 ILE n 
1 218 ILE n 
1 219 TRP n 
1 220 ALA n 
1 221 GLY n 
1 222 LEU n 
1 223 PRO n 
1 224 ASP n 
1 225 ASP n 
1 226 VAL n 
1 227 GLN n 
1 228 ALA n 
1 229 SER n 
1 230 LEU n 
1 231 LYS n 
1 232 SER n 
1 233 LYS n 
1 234 PRO n 
1 235 GLY n 
1 236 VAL n 
1 237 LEU n 
1 238 PRO n 
1 239 GLU n 
1 240 LEU n 
1 241 MET n 
1 242 GLY n 
1 243 CYS n 
1 244 LYS n 
1 245 ASN 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               ? 
_entity_src_gen.gene_src_genus                     Serratia 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    SM6 
_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      'Serratia marcescens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     615 
_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    EXTRACELLULAR 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Serratia marcescens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     615 
_entity_src_gen.host_org_genus                     Serratia 
_entity_src_gen.pdbx_host_org_gene                 NUCA 
_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               'PROTEASE DEFICIENT STRAIN' 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PUC19NUC4OC 
_entity_src_gen.plasmid_details                    'PLASMID WHICH ENCODES THE GENE AND CARRIES AN OPERATOR CONSTITUTIVE MUTATION' 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NUCA_SERMA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P13717 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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 1QAE A 1 ? 245 ? P13717 22 ? 266 ? 1 245 
2 1 1QAE B 1 ? 245 ? P13717 22 ? 266 ? 1 245 
# 
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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
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  
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 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
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 
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          1QAE 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.57 
_exptl_crystal.density_percent_sol   52.0 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.2 
_exptl_crystal_grow.pdbx_details    
;CRYSTALLIZATION METHOD: VAPOR DIFFUSION SITTING DROP   
CRYSTALLIZATION TEMPERATURE: 277 K   
CRYSTALLIZATION PH: 4.6   
CRYSTALS WERE GROWN FROM PEG 3350, AMMONIUM SULFATE,    
SODIUM ACETATE, AND STORED IN A STABILIZATION SOLUTION CONTAINING    
20% PEG 3000, 400mM GLYCINE, 40mM TRIS, PH8.2 (293 K), 20% PEG    
3000, 10% PEG 400.  THIS SOLUTION WAS EXCHANGED THREE TIMES TO MINIMIZE    
CARRY OVER FROM THE STORAGE SOLUTION.    
AFTER 3 DAYS IN THE MAGNESIUM STABILIZATION SOLUTION, THE CRYSTAL    
OF DIMENSION 0.4 X 0.4 X 0.3 MM**2 WAS MOUNTED IN A SILICONIZED SPECIAL GLASS     
CAPILLARY.    
, VAPOR DIFFUSION, SITTING DROP
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           288 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'AREA DETECTOR' 
_diffrn_detector.type                   'ENRAF-NONIUS FAST' 
_diffrn_detector.pdbx_collection_date   1998-02-02 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1QAE 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             45.0 
_reflns.d_resolution_high            2.05 
_reflns.number_obs                   30574 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         84.3 
_reflns.pdbx_Rmerge_I_obs            0.025 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        40.87 
_reflns.B_iso_Wilson_estimate        6.6 
_reflns.pdbx_redundancy              3.1 
_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_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.05 
_reflns_shell.d_res_low              2.10 
_reflns_shell.percent_possible_all   20.4 
_reflns_shell.Rmerge_I_obs           0.045 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    18.9 
_reflns_shell.pdbx_redundancy        1.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1QAE 
_refine.ls_number_reflns_obs                     29209 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2.0 
_refine.pdbx_data_cutoff_high_absF               10000000.00 
_refine.pdbx_data_cutoff_low_absF                0.00 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             50.00 
_refine.ls_d_res_high                            2.05 
_refine.ls_percent_reflns_obs                    83.0 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.167 
_refine.ls_R_factor_R_free                       0.21 
_refine.ls_R_factor_R_free_error                 0.005 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1483 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               14.8 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
;BULK SOLVENT MODEL USED, NCS B-FACTORS RESTRAINTS WERE APPLIED TO PROTEIN   
ATOMS AND PAIRS OF WATER MOLECULES WHICH DEVIATED LESS THAN 1.0 ANGSTROMS FROM   
  
NCS. THE PROTEIN ATOMS ARE IN GROUP 1 AND THE WATER IS IN GROUP 2. WATER HOH   
  1 SITS ON THE NON-CRYSTALLOGRAPHIC 2-FOLD AXIS AND IT IS ITS OWN NCS MATE. THE   
  
WATER PAIRS IN GROUP 2 BEGIN WITH (HOH  2,HOH  3) AND END WITH (HOH  188,   
HOH  189). WATERS HOH  190 TO HOH  241 DO NOT HAVE NCS MATES WITHIN 1.0   
ANGSTROMS.

CRYST1
  THERE IS STRONG PSEUDO-CENTERING ARISING FROM THE
  NON-CRYSTALLOGRAPHIC SYMMETRY.  SHIFTING ONE MONOMER BY
  ONLY 1.4 ANGSTROMS WITH A 1 DEGREE ROTATION WOULD CHANGE
  THE SPACE GROUP TO I 2 2 2.
;
_refine.pdbx_starting_model                      
;1.4 ANGSTROM STRUCTURE OF THE SERRATIAL ENDONUCLEASE (CAI, MILLER AND KRAUSE) WITH WATER AND ALTERNATE SIDE CHAIN CONFORMERS REMOVED AND THE SIDE 
CHAINS FOR THE ACTIVE SITE RESIDUES ARG 57, HIS 89, ASN 199 AND GLU 127 OMITTED
;
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.pdbx_overall_phase_error                 ? 
_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.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1QAE 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             0.15 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.24 
_refine_analyze.Luzzati_sigma_a_free            0.15 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3690 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             251 
_refine_hist.number_atoms_total               3943 
_refine_hist.d_res_high                       2.05 
_refine_hist.d_res_low                        50.00 
# 
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 
x_bond_d                0.005 ?    ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      26.6  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      0.61  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             1.12  1.50 ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            1.83  2.00 ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             2.32  2.25 ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            3.53  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_number 
1 ? ? ? 0.782 1.0 . . 1 'X-RAY DIFFRACTION' 1 ? 
2 ? ? ? 0.275 0.3 . . 2 'X-RAY DIFFRACTION' 2 ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.05 
_refine_ls_shell.d_res_low                        2.18 
_refine_ls_shell.number_reflns_R_work             2728 
_refine_ls_shell.R_factor_R_work                  0.192 
_refine_ls_shell.percent_reflns_obs               49.4 
_refine_ls_shell.R_factor_R_free                  0.21 
_refine_ls_shell.R_factor_R_free_error            0.019 
_refine_ls_shell.percent_reflns_R_free            4.3 
_refine_ls_shell.number_reflns_R_free             122 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM TOPHCSDX.PRO 'X-RAY DIFFRACTION' 
2 ?                 TOPH19.SOL   'X-RAY DIFFRACTION' 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   -0.999819 
_struct_ncs_oper.matrix[1][2]   -0.018722 
_struct_ncs_oper.matrix[1][3]   -0.003478 
_struct_ncs_oper.matrix[2][1]   -0.018758 
_struct_ncs_oper.matrix[2][2]   0.999769 
_struct_ncs_oper.matrix[2][3]   0.010535 
_struct_ncs_oper.matrix[3][1]   0.003280 
_struct_ncs_oper.matrix[3][2]   0.010599 
_struct_ncs_oper.matrix[3][3]   -0.999938 
_struct_ncs_oper.vector[1]      -1.0876 
_struct_ncs_oper.vector[2]      -0.5639 
_struct_ncs_oper.vector[3]      103.2304 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 ? 
2 2 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 ? 
2 ? 
# 
_struct.entry_id                  1QAE 
_struct.title                     'THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER' 
_struct.pdbx_descriptor           'EXTRACELLULAR ENDONUCLEASE' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1QAE 
_struct_keywords.pdbx_keywords   ENDONUCLEASE 
_struct_keywords.text            'NUCLEASE, DNASE, RNASE, SUGAR-NONSPECIFIC NUCLEASE, MAGNESIUM, ENDONUCLEASE' 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               
;MTRIX
 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
 VARIOUS DOMAINS IN THIS ENTRY.  APPLYING THE APPROPRIATE
 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
 SECOND.

           APPLIED TO           TRANSFORMED TO
 MTRIX      RESIDUES               RESIDUES         RMSD
   M1   A    5  ..  A  245     B    5  ..  B  245   0.131
;
_struct_biol.pdbx_parent_biol_id   ? 
# 
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  PRO A 67  ? ASP A 69  ? PRO A 67  ASP A 69  5 ? 3  
HELX_P HELX_P2  2  PRO A 73  ? TYR A 76  ? PRO A 73  TYR A 76  5 ? 4  
HELX_P HELX_P3  3  ALA A 79  ? LEU A 83  ? ALA A 79  LEU A 83  1 ? 5  
HELX_P HELX_P4  4  LEU A 93  ? LEU A 96  ? LEU A 93  LEU A 96  1 ? 4  
HELX_P HELX_P5  5  TRP A 102 ? ASN A 106 ? TRP A 102 ASN A 106 5 ? 5  
HELX_P HELX_P6  6  LEU A 108 ? ASN A 110 ? LEU A 108 ASN A 110 5 ? 3  
HELX_P HELX_P7  7  SER A 116 ? ASN A 119 ? SER A 116 ASN A 119 1 ? 4  
HELX_P HELX_P8  8  ALA A 122 ? LEU A 133 ? ALA A 122 LEU A 133 1 ? 12 
HELX_P HELX_P9  9  PHE A 200 ? PHE A 203 ? PHE A 200 PHE A 203 5 ? 4  
HELX_P HELX_P10 10 VAL A 207 ? THR A 214 ? VAL A 207 THR A 214 1 ? 8  
HELX_P HELX_P11 11 ASP A 224 ? LEU A 230 ? ASP A 224 LEU A 230 1 ? 7  
HELX_P HELX_P12 12 LEU A 237 ? MET A 241 ? LEU A 237 MET A 241 5 ? 5  
HELX_P HELX_P13 13 PRO B 67  ? ASP B 69  ? PRO B 67  ASP B 69  5 ? 3  
HELX_P HELX_P14 14 PRO B 73  ? TYR B 76  ? PRO B 73  TYR B 76  5 ? 4  
HELX_P HELX_P15 15 ALA B 79  ? LEU B 83  ? ALA B 79  LEU B 83  1 ? 5  
HELX_P HELX_P16 16 LEU B 93  ? LEU B 96  ? LEU B 93  LEU B 96  1 ? 4  
HELX_P HELX_P17 17 TRP B 102 ? ASN B 106 ? TRP B 102 ASN B 106 5 ? 5  
HELX_P HELX_P18 18 LEU B 108 ? ASN B 110 ? LEU B 108 ASN B 110 5 ? 3  
HELX_P HELX_P19 19 SER B 116 ? ASN B 119 ? SER B 116 ASN B 119 1 ? 4  
HELX_P HELX_P20 20 ALA B 122 ? LEU B 133 ? ALA B 122 LEU B 133 1 ? 12 
HELX_P HELX_P21 21 PHE B 200 ? PHE B 203 ? PHE B 200 PHE B 203 5 ? 4  
HELX_P HELX_P22 22 VAL B 207 ? THR B 214 ? VAL B 207 THR B 214 1 ? 8  
HELX_P HELX_P23 23 ASP B 224 ? LEU B 230 ? ASP B 224 LEU B 230 1 ? 7  
HELX_P HELX_P24 24 LEU B 237 ? MET B 241 ? LEU B 237 MET B 241 5 ? 5  
# 
_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 
disulf1  disulf ? ? A CYS 9   SG  ? ? ? 1_555 A CYS 13  SG ? ? A CYS 9   A CYS 13  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf2  disulf ? ? A CYS 201 SG  ? ? ? 1_555 A CYS 243 SG ? ? A CYS 201 A CYS 243 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf3  disulf ? ? B CYS 9   SG  ? ? ? 1_555 B CYS 13  SG ? ? B CYS 9   B CYS 13  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf4  disulf ? ? B CYS 201 SG  ? ? ? 1_555 B CYS 243 SG ? ? B CYS 201 B CYS 243 1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc1  metalc ? ? A ASN 119 OD1 ? ? ? 1_555 C MG  .   MG ? ? A ASN 119 A MG  251 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc2  metalc ? ? B ASN 119 OD1 ? ? ? 1_555 D MG  .   MG ? ? B ASN 119 B MG  251 1_555 ? ? ? ? ? ? ? 2.176 ? 
metalc3  metalc ? ? C MG  .   MG  ? ? ? 1_555 E HOH .   O  ? ? A MG  251 A HOH 253 1_555 ? ? ? ? ? ? ? 2.232 ? 
metalc4  metalc ? ? C MG  .   MG  ? ? ? 1_555 E HOH .   O  ? ? A MG  251 A HOH 256 1_555 ? ? ? ? ? ? ? 2.164 ? 
metalc5  metalc ? ? C MG  .   MG  ? ? ? 1_555 E HOH .   O  ? ? A MG  251 A HOH 254 1_555 ? ? ? ? ? ? ? 2.216 ? 
metalc6  metalc ? ? C MG  .   MG  ? ? ? 1_555 E HOH .   O  ? ? A MG  251 A HOH 252 1_555 ? ? ? ? ? ? ? 2.242 ? 
metalc7  metalc ? ? C MG  .   MG  ? ? ? 1_555 E HOH .   O  ? ? A MG  251 A HOH 255 1_555 ? ? ? ? ? ? ? 2.290 ? 
metalc8  metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH .   O  ? ? B MG  251 B HOH 255 1_555 ? ? ? ? ? ? ? 2.211 ? 
metalc9  metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH .   O  ? ? B MG  251 B HOH 256 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc10 metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH .   O  ? ? B MG  251 B HOH 252 1_555 ? ? ? ? ? ? ? 2.193 ? 
metalc11 metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH .   O  ? ? B MG  251 B HOH 254 1_555 ? ? ? ? ? ? ? 2.160 ? 
metalc12 metalc ? ? D MG  .   MG  ? ? ? 1_555 F HOH .   O  ? ? B MG  251 B HOH 253 1_555 ? ? ? ? ? ? ? 2.198 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6 ? 
B ? 2 ? 
C ? 6 ? 
D ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
A 5 6 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
C 5 6 ? anti-parallel 
D 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 23  ? VAL A 24  ? ILE A 23  VAL A 24  
A 2 THR A 29  ? ASN A 32  ? THR A 29  ASN A 32  
A 3 ALA A 39  ? ILE A 46  ? ALA A 39  ILE A 46  
A 4 VAL A 142 ? LEU A 149 ? VAL A 142 LEU A 149 
A 5 ALA A 169 ? ILE A 176 ? ALA A 169 ILE A 176 
A 6 TYR A 185 ? ASP A 191 ? TYR A 185 ASP A 191 
B 1 VAL A 85  ? HIS A 89  ? VAL A 85  HIS A 89  
B 2 ILE A 111 ? LYS A 115 ? ILE A 111 LYS A 115 
C 1 ILE B 23  ? VAL B 24  ? ILE B 23  VAL B 24  
C 2 THR B 29  ? ASN B 32  ? THR B 29  ASN B 32  
C 3 ALA B 39  ? ILE B 46  ? ALA B 39  ILE B 46  
C 4 VAL B 142 ? LEU B 149 ? VAL B 142 LEU B 149 
C 5 ALA B 169 ? ILE B 176 ? ALA B 169 ILE B 176 
C 6 TYR B 185 ? ASP B 191 ? TYR B 185 ASP B 191 
D 1 VAL B 85  ? HIS B 89  ? VAL B 85  HIS B 89  
D 2 ILE B 111 ? LYS B 115 ? ILE B 111 LYS B 115 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N ILE A 23  ? N ILE A 23  O LEU A 30  ? O LEU A 30  
A 2 3 O ASN A 31  ? O ASN A 31  N ASN A 40  ? N ASN A 40  
A 3 4 N ILE A 46  ? N ILE A 46  O VAL A 142 ? O VAL A 142 
A 4 5 N LEU A 149 ? N LEU A 149 O ALA A 169 ? O ALA A 169 
A 5 6 N ILE A 174 ? N ILE A 174 O ALA A 186 ? O ALA A 186 
B 1 2 N GLY A 88  ? N GLY A 88  O THR A 112 ? O THR A 112 
C 1 2 N ILE B 23  ? N ILE B 23  O LEU B 30  ? O LEU B 30  
C 2 3 O ASN B 31  ? O ASN B 31  N ASN B 40  ? N ASN B 40  
C 3 4 N ILE B 46  ? N ILE B 46  O VAL B 142 ? O VAL B 142 
C 4 5 N LEU B 149 ? N LEU B 149 O ALA B 169 ? O ALA B 169 
C 5 6 N ILE B 174 ? N ILE B 174 O ALA B 186 ? O ALA B 186 
D 1 2 N GLY B 88  ? N GLY B 88  O THR B 112 ? O THR B 112 
# 
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 
ASA Author   ? ? ? ? 9 'ACTIVE SITE REGION IN MONOMER A WITH CATALYTIC MAGNESIUM WATER CLUSTER' 
ASB Author   ? ? ? ? 9 'ACTIVE SITE REGION IN MONOMER B WITH CATALYTIC MAGNESIUM WATER CLUSTER' 
AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MG A 251'                                      
AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MG B 251'                                      
# 
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  ASA 9 HIS A 89  ? HIS A 89  . ? 1_555 ? 
2  ASA 9 GLU A 127 ? GLU A 127 . ? 1_555 ? 
3  ASA 9 ASN A 119 ? ASN A 119 . ? 1_555 ? 
4  ASA 9 MG  C .   ? MG  A 251 . ? 1_555 ? 
5  ASA 9 HOH E .   ? HOH A 252 . ? 1_555 ? 
6  ASA 9 HOH E .   ? HOH A 253 . ? 1_555 ? 
7  ASA 9 HOH E .   ? HOH A 254 . ? 1_555 ? 
8  ASA 9 HOH E .   ? HOH A 255 . ? 1_555 ? 
9  ASA 9 HOH E .   ? HOH A 256 . ? 1_555 ? 
10 ASB 9 HIS B 89  ? HIS B 89  . ? 1_555 ? 
11 ASB 9 GLU B 127 ? GLU B 127 . ? 1_555 ? 
12 ASB 9 ASN B 119 ? ASN B 119 . ? 1_555 ? 
13 ASB 9 MG  D .   ? MG  B 251 . ? 1_555 ? 
14 ASB 9 HOH F .   ? HOH B 252 . ? 1_555 ? 
15 ASB 9 HOH F .   ? HOH B 253 . ? 1_555 ? 
16 ASB 9 HOH F .   ? HOH B 254 . ? 1_555 ? 
17 ASB 9 HOH F .   ? HOH B 255 . ? 1_555 ? 
18 ASB 9 HOH F .   ? HOH B 256 . ? 1_555 ? 
19 AC1 6 ASN A 119 ? ASN A 119 . ? 1_555 ? 
20 AC1 6 HOH E .   ? HOH A 252 . ? 1_555 ? 
21 AC1 6 HOH E .   ? HOH A 253 . ? 1_555 ? 
22 AC1 6 HOH E .   ? HOH A 254 . ? 1_555 ? 
23 AC1 6 HOH E .   ? HOH A 255 . ? 1_555 ? 
24 AC1 6 HOH E .   ? HOH A 256 . ? 1_555 ? 
25 AC2 6 ASN B 119 ? ASN B 119 . ? 1_555 ? 
26 AC2 6 HOH F .   ? HOH B 252 . ? 1_555 ? 
27 AC2 6 HOH F .   ? HOH B 253 . ? 1_555 ? 
28 AC2 6 HOH F .   ? HOH B 254 . ? 1_555 ? 
29 AC2 6 HOH F .   ? HOH B 255 . ? 1_555 ? 
30 AC2 6 HOH F .   ? HOH B 256 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1QAE 
_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                    1QAE 
_atom_sites.fract_transf_matrix[1][1]   0.009372 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013423 
_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]   0.014514 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
MG 
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   . ILE A 1 6   ? 19.538  4.851  54.058 1.00 30.02 ? 6   ILE A N   1 
ATOM   2    C  CA  . ILE A 1 6   ? 18.837  5.802  54.915 1.00 25.10 ? 6   ILE A CA  1 
ATOM   3    C  C   . ILE A 1 6   ? 18.556  7.097  54.160 1.00 23.21 ? 6   ILE A C   1 
ATOM   4    O  O   . ILE A 1 6   ? 19.478  7.808  53.759 1.00 22.80 ? 6   ILE A O   1 
ATOM   5    C  CB  . ILE A 1 6   ? 19.661  6.140  56.181 1.00 22.63 ? 6   ILE A CB  1 
ATOM   6    C  CG1 . ILE A 1 6   ? 19.897  4.876  57.008 1.00 21.63 ? 6   ILE A CG1 1 
ATOM   7    C  CG2 . ILE A 1 6   ? 18.930  7.169  57.025 1.00 21.80 ? 6   ILE A CG2 1 
ATOM   8    C  CD1 . ILE A 1 6   ? 21.146  4.945  57.855 1.00 23.79 ? 6   ILE A CD1 1 
ATOM   9    N  N   . ASP A 1 7   ? 17.274  7.393  53.972 1.00 20.77 ? 7   ASP A N   1 
ATOM   10   C  CA  . ASP A 1 7   ? 16.848  8.600  53.273 1.00 17.80 ? 7   ASP A CA  1 
ATOM   11   C  C   . ASP A 1 7   ? 16.179  9.553  54.259 1.00 15.95 ? 7   ASP A C   1 
ATOM   12   O  O   . ASP A 1 7   ? 15.039  9.340  54.665 1.00 16.59 ? 7   ASP A O   1 
ATOM   13   C  CB  . ASP A 1 7   ? 15.870  8.241  52.155 1.00 16.57 ? 7   ASP A CB  1 
ATOM   14   C  CG  . ASP A 1 7   ? 15.423  9.452  51.355 1.00 19.03 ? 7   ASP A CG  1 
ATOM   15   O  OD1 . ASP A 1 7   ? 15.881  10.579 51.654 1.00 17.12 ? 7   ASP A OD1 1 
ATOM   16   O  OD2 . ASP A 1 7   ? 14.609  9.275  50.423 1.00 21.80 ? 7   ASP A OD2 1 
ATOM   17   N  N   . ASN A 1 8   ? 16.896  10.604 54.640 1.00 11.64 ? 8   ASN A N   1 
ATOM   18   C  CA  . ASN A 1 8   ? 16.381  11.585 55.589 1.00 10.84 ? 8   ASN A CA  1 
ATOM   19   C  C   . ASN A 1 8   ? 15.813  12.806 54.877 1.00 9.91  ? 8   ASN A C   1 
ATOM   20   O  O   . ASN A 1 8   ? 15.480  13.803 55.521 1.00 9.84  ? 8   ASN A O   1 
ATOM   21   C  CB  . ASN A 1 8   ? 17.502  12.038 56.530 1.00 11.31 ? 8   ASN A CB  1 
ATOM   22   C  CG  . ASN A 1 8   ? 17.959  10.939 57.466 1.00 12.17 ? 8   ASN A CG  1 
ATOM   23   O  OD1 . ASN A 1 8   ? 17.143  10.267 58.085 1.00 14.83 ? 8   ASN A OD1 1 
ATOM   24   N  ND2 . ASN A 1 8   ? 19.273  10.753 57.574 1.00 10.21 ? 8   ASN A ND2 1 
ATOM   25   N  N   . CYS A 1 9   ? 15.701  12.725 53.554 1.00 10.56 ? 9   CYS A N   1 
ATOM   26   C  CA  . CYS A 1 9   ? 15.203  13.848 52.763 1.00 11.09 ? 9   CYS A CA  1 
ATOM   27   C  C   . CYS A 1 9   ? 13.901  13.570 52.010 1.00 11.41 ? 9   CYS A C   1 
ATOM   28   O  O   . CYS A 1 9   ? 13.122  14.491 51.753 1.00 13.02 ? 9   CYS A O   1 
ATOM   29   C  CB  . CYS A 1 9   ? 16.290  14.293 51.782 1.00 11.06 ? 9   CYS A CB  1 
ATOM   30   S  SG  . CYS A 1 9   ? 17.836  14.793 52.605 1.00 12.18 ? 9   CYS A SG  1 
ATOM   31   N  N   . ALA A 1 10  ? 13.682  12.308 51.651 1.00 9.89  ? 10  ALA A N   1 
ATOM   32   C  CA  . ALA A 1 10  ? 12.475  11.884 50.944 1.00 9.86  ? 10  ALA A CA  1 
ATOM   33   C  C   . ALA A 1 10  ? 12.329  12.391 49.506 1.00 10.29 ? 10  ALA A C   1 
ATOM   34   O  O   . ALA A 1 10  ? 12.085  11.603 48.595 1.00 11.23 ? 10  ALA A O   1 
ATOM   35   C  CB  . ALA A 1 10  ? 11.243  12.272 51.751 1.00 8.03  ? 10  ALA A CB  1 
ATOM   36   N  N   . VAL A 1 11  ? 12.469  13.697 49.296 1.00 9.53  ? 11  VAL A N   1 
ATOM   37   C  CA  . VAL A 1 11  ? 12.321  14.258 47.953 1.00 8.32  ? 11  VAL A CA  1 
ATOM   38   C  C   . VAL A 1 11  ? 13.625  14.832 47.412 1.00 9.00  ? 11  VAL A C   1 
ATOM   39   O  O   . VAL A 1 11  ? 13.622  15.771 46.607 1.00 7.68  ? 11  VAL A O   1 
ATOM   40   C  CB  . VAL A 1 11  ? 11.226  15.360 47.927 1.00 8.61  ? 11  VAL A CB  1 
ATOM   41   C  CG1 . VAL A 1 11  ? 9.875   14.742 48.247 1.00 8.76  ? 11  VAL A CG1 1 
ATOM   42   C  CG2 . VAL A 1 11  ? 11.551  16.456 48.929 1.00 8.71  ? 11  VAL A CG2 1 
ATOM   43   N  N   . GLY A 1 12  ? 14.737  14.259 47.862 1.00 8.58  ? 12  GLY A N   1 
ATOM   44   C  CA  . GLY A 1 12  ? 16.041  14.707 47.416 1.00 9.33  ? 12  GLY A CA  1 
ATOM   45   C  C   . GLY A 1 12  ? 16.704  15.690 48.361 1.00 10.15 ? 12  GLY A C   1 
ATOM   46   O  O   . GLY A 1 12  ? 16.166  16.767 48.631 1.00 11.17 ? 12  GLY A O   1 
ATOM   47   N  N   . CYS A 1 13  ? 17.876  15.321 48.869 1.00 7.66  ? 13  CYS A N   1 
ATOM   48   C  CA  . CYS A 1 13  ? 18.609  16.190 49.772 1.00 7.74  ? 13  CYS A CA  1 
ATOM   49   C  C   . CYS A 1 13  ? 19.064  17.404 48.969 1.00 7.52  ? 13  CYS A C   1 
ATOM   50   O  O   . CYS A 1 13  ? 19.163  17.341 47.749 1.00 7.55  ? 13  CYS A O   1 
ATOM   51   C  CB  . CYS A 1 13  ? 19.800  15.437 50.367 1.00 9.19  ? 13  CYS A CB  1 
ATOM   52   S  SG  . CYS A 1 13  ? 19.301  14.031 51.420 1.00 11.60 ? 13  CYS A SG  1 
ATOM   53   N  N   . PRO A 1 14  ? 19.345  18.528 49.643 1.00 8.45  ? 14  PRO A N   1 
ATOM   54   C  CA  . PRO A 1 14  ? 19.779  19.746 48.944 1.00 8.86  ? 14  PRO A CA  1 
ATOM   55   C  C   . PRO A 1 14  ? 21.085  19.644 48.159 1.00 9.64  ? 14  PRO A C   1 
ATOM   56   O  O   . PRO A 1 14  ? 22.008  18.925 48.548 1.00 9.72  ? 14  PRO A O   1 
ATOM   57   C  CB  . PRO A 1 14  ? 19.880  20.794 50.057 1.00 7.18  ? 14  PRO A CB  1 
ATOM   58   C  CG  . PRO A 1 14  ? 19.123  20.213 51.220 1.00 7.33  ? 14  PRO A CG  1 
ATOM   59   C  CD  . PRO A 1 14  ? 19.281  18.726 51.099 1.00 7.21  ? 14  PRO A CD  1 
ATOM   60   N  N   . THR A 1 15  ? 21.145  20.368 47.044 1.00 9.41  ? 15  THR A N   1 
ATOM   61   C  CA  . THR A 1 15  ? 22.343  20.417 46.219 1.00 10.35 ? 15  THR A CA  1 
ATOM   62   C  C   . THR A 1 15  ? 22.905  21.816 46.441 1.00 10.46 ? 15  THR A C   1 
ATOM   63   O  O   . THR A 1 15  ? 22.196  22.700 46.925 1.00 10.01 ? 15  THR A O   1 
ATOM   64   C  CB  . THR A 1 15  ? 22.029  20.216 44.711 1.00 8.25  ? 15  THR A CB  1 
ATOM   65   O  OG1 . THR A 1 15  ? 21.126  21.231 44.260 1.00 7.83  ? 15  THR A OG1 1 
ATOM   66   C  CG2 . THR A 1 15  ? 21.406  18.857 44.474 1.00 9.40  ? 15  THR A CG2 1 
ATOM   67   N  N   . GLY A 1 16  ? 24.175  22.021 46.111 1.00 11.10 ? 16  GLY A N   1 
ATOM   68   C  CA  . GLY A 1 16  ? 24.760  23.336 46.301 1.00 11.69 ? 16  GLY A CA  1 
ATOM   69   C  C   . GLY A 1 16  ? 25.679  23.440 47.506 1.00 13.11 ? 16  GLY A C   1 
ATOM   70   O  O   . GLY A 1 16  ? 26.337  24.462 47.697 1.00 13.97 ? 16  GLY A O   1 
ATOM   71   N  N   . GLY A 1 17  ? 25.727  22.389 48.319 1.00 14.08 ? 17  GLY A N   1 
ATOM   72   C  CA  . GLY A 1 17  ? 26.586  22.402 49.490 1.00 14.77 ? 17  GLY A CA  1 
ATOM   73   C  C   . GLY A 1 17  ? 28.059  22.456 49.120 1.00 17.25 ? 17  GLY A C   1 
ATOM   74   O  O   . GLY A 1 17  ? 28.466  21.948 48.068 1.00 16.85 ? 17  GLY A O   1 
ATOM   75   N  N   . SER A 1 18  ? 28.862  23.065 49.990 1.00 16.27 ? 18  SER A N   1 
ATOM   76   C  CA  . SER A 1 18  ? 30.300  23.205 49.761 1.00 16.40 ? 18  SER A CA  1 
ATOM   77   C  C   . SER A 1 18  ? 31.018  21.866 49.667 1.00 17.42 ? 18  SER A C   1 
ATOM   78   O  O   . SER A 1 18  ? 31.994  21.726 48.933 1.00 18.36 ? 18  SER A O   1 
ATOM   79   C  CB  . SER A 1 18  ? 30.931  24.043 50.879 1.00 16.17 ? 18  SER A CB  1 
ATOM   80   O  OG  . SER A 1 18  ? 30.993  23.309 52.092 1.00 14.44 ? 18  SER A OG  1 
ATOM   81   N  N   . SER A 1 19  ? 30.543  20.883 50.420 1.00 19.31 ? 19  SER A N   1 
ATOM   82   C  CA  . SER A 1 19  ? 31.157  19.565 50.396 1.00 21.01 ? 19  SER A CA  1 
ATOM   83   C  C   . SER A 1 19  ? 30.422  18.702 49.379 1.00 22.97 ? 19  SER A C   1 
ATOM   84   O  O   . SER A 1 19  ? 29.200  18.794 49.246 1.00 23.04 ? 19  SER A O   1 
ATOM   85   C  CB  . SER A 1 19  ? 31.086  18.925 51.781 1.00 21.64 ? 19  SER A CB  1 
ATOM   86   O  OG  . SER A 1 19  ? 31.587  17.603 51.742 1.00 30.64 ? 19  SER A OG  1 
ATOM   87   N  N   . ASN A 1 20  ? 31.166  17.869 48.659 1.00 24.98 ? 20  ASN A N   1 
ATOM   88   C  CA  . ASN A 1 20  ? 30.570  17.008 47.643 1.00 26.53 ? 20  ASN A CA  1 
ATOM   89   C  C   . ASN A 1 20  ? 29.975  15.744 48.236 1.00 26.60 ? 20  ASN A C   1 
ATOM   90   O  O   . ASN A 1 20  ? 29.102  15.124 47.635 1.00 27.80 ? 20  ASN A O   1 
ATOM   91   C  CB  . ASN A 1 20  ? 31.608  16.649 46.580 1.00 36.64 ? 20  ASN A CB  1 
ATOM   92   C  CG  . ASN A 1 20  ? 31.905  17.810 45.649 1.00 39.71 ? 20  ASN A CG  1 
ATOM   93   O  OD1 . ASN A 1 20  ? 31.014  18.598 45.314 1.00 41.52 ? 20  ASN A OD1 1 
ATOM   94   N  ND2 . ASN A 1 20  ? 33.161  17.927 45.230 1.00 40.76 ? 20  ASN A ND2 1 
ATOM   95   N  N   . VAL A 1 21  ? 30.449  15.363 49.416 1.00 24.24 ? 21  VAL A N   1 
ATOM   96   C  CA  . VAL A 1 21  ? 29.940  14.176 50.087 1.00 23.28 ? 21  VAL A CA  1 
ATOM   97   C  C   . VAL A 1 21  ? 29.283  14.589 51.402 1.00 21.60 ? 21  VAL A C   1 
ATOM   98   O  O   . VAL A 1 21  ? 29.773  15.475 52.101 1.00 22.26 ? 21  VAL A O   1 
ATOM   99   C  CB  . VAL A 1 21  ? 31.071  13.166 50.378 1.00 25.71 ? 21  VAL A CB  1 
ATOM   100  C  CG1 . VAL A 1 21  ? 32.178  13.840 51.170 1.00 27.21 ? 21  VAL A CG1 1 
ATOM   101  C  CG2 . VAL A 1 21  ? 30.518  11.970 51.138 1.00 27.40 ? 21  VAL A CG2 1 
ATOM   102  N  N   . SER A 1 22  ? 28.165  13.952 51.726 1.00 18.60 ? 22  SER A N   1 
ATOM   103  C  CA  . SER A 1 22  ? 27.452  14.258 52.956 1.00 16.88 ? 22  SER A CA  1 
ATOM   104  C  C   . SER A 1 22  ? 27.537  13.078 53.910 1.00 16.37 ? 22  SER A C   1 
ATOM   105  O  O   . SER A 1 22  ? 27.744  11.942 53.488 1.00 16.78 ? 22  SER A O   1 
ATOM   106  C  CB  . SER A 1 22  ? 25.979  14.563 52.661 1.00 14.81 ? 22  SER A CB  1 
ATOM   107  O  OG  . SER A 1 22  ? 25.844  15.731 51.872 1.00 15.94 ? 22  SER A OG  1 
ATOM   108  N  N   . ILE A 1 23  ? 27.384  13.361 55.199 1.00 13.91 ? 23  ILE A N   1 
ATOM   109  C  CA  . ILE A 1 23  ? 27.412  12.333 56.229 1.00 12.98 ? 23  ILE A CA  1 
ATOM   110  C  C   . ILE A 1 23  ? 25.978  11.859 56.442 1.00 12.46 ? 23  ILE A C   1 
ATOM   111  O  O   . ILE A 1 23  ? 25.088  12.661 56.732 1.00 11.41 ? 23  ILE A O   1 
ATOM   112  C  CB  . ILE A 1 23  ? 27.951  12.894 57.557 1.00 14.88 ? 23  ILE A CB  1 
ATOM   113  C  CG1 . ILE A 1 23  ? 29.435  13.225 57.411 1.00 15.64 ? 23  ILE A CG1 1 
ATOM   114  C  CG2 . ILE A 1 23  ? 27.721  11.892 58.679 1.00 15.24 ? 23  ILE A CG2 1 
ATOM   115  C  CD1 . ILE A 1 23  ? 30.009  13.964 58.595 1.00 21.15 ? 23  ILE A CD1 1 
ATOM   116  N  N   . VAL A 1 24  ? 25.755  10.559 56.290 1.00 10.89 ? 24  VAL A N   1 
ATOM   117  C  CA  . VAL A 1 24  ? 24.423  10.000 56.457 1.00 11.28 ? 24  VAL A CA  1 
ATOM   118  C  C   . VAL A 1 24  ? 24.362  9.131  57.704 1.00 12.24 ? 24  VAL A C   1 
ATOM   119  O  O   . VAL A 1 24  ? 25.118  8.170  57.839 1.00 12.90 ? 24  VAL A O   1 
ATOM   120  C  CB  . VAL A 1 24  ? 24.019  9.148  55.231 1.00 12.18 ? 24  VAL A CB  1 
ATOM   121  C  CG1 . VAL A 1 24  ? 22.613  8.597  55.411 1.00 12.26 ? 24  VAL A CG1 1 
ATOM   122  C  CG2 . VAL A 1 24  ? 24.101  9.992  53.967 1.00 12.55 ? 24  VAL A CG2 1 
ATOM   123  N  N   . ARG A 1 25  ? 23.460  9.482  58.614 1.00 10.06 ? 25  ARG A N   1 
ATOM   124  C  CA  . ARG A 1 25  ? 23.277  8.740  59.853 1.00 10.32 ? 25  ARG A CA  1 
ATOM   125  C  C   . ARG A 1 25  ? 21.784  8.557  60.038 1.00 11.42 ? 25  ARG A C   1 
ATOM   126  O  O   . ARG A 1 25  ? 20.990  9.094  59.263 1.00 11.52 ? 25  ARG A O   1 
ATOM   127  C  CB  . ARG A 1 25  ? 23.845  9.526  61.041 1.00 11.05 ? 25  ARG A CB  1 
ATOM   128  C  CG  . ARG A 1 25  ? 25.346  9.701  60.990 1.00 10.24 ? 25  ARG A CG  1 
ATOM   129  C  CD  . ARG A 1 25  ? 25.860  10.647 62.060 1.00 10.79 ? 25  ARG A CD  1 
ATOM   130  N  NE  . ARG A 1 25  ? 27.302  10.481 62.205 1.00 11.00 ? 25  ARG A NE  1 
ATOM   131  C  CZ  . ARG A 1 25  ? 28.182  11.474 62.266 1.00 11.88 ? 25  ARG A CZ  1 
ATOM   132  N  NH1 . ARG A 1 25  ? 27.776  12.733 62.196 1.00 11.04 ? 25  ARG A NH1 1 
ATOM   133  N  NH2 . ARG A 1 25  ? 29.477  11.199 62.379 1.00 12.79 ? 25  ARG A NH2 1 
ATOM   134  N  N   . HIS A 1 26  ? 21.398  7.798  61.056 1.00 10.55 ? 26  HIS A N   1 
ATOM   135  C  CA  . HIS A 1 26  ? 19.986  7.594  61.318 1.00 11.41 ? 26  HIS A CA  1 
ATOM   136  C  C   . HIS A 1 26  ? 19.421  8.887  61.875 1.00 10.77 ? 26  HIS A C   1 
ATOM   137  O  O   . HIS A 1 26  ? 18.296  9.267  61.565 1.00 11.01 ? 26  HIS A O   1 
ATOM   138  C  CB  . HIS A 1 26  ? 19.789  6.464  62.323 1.00 14.60 ? 26  HIS A CB  1 
ATOM   139  C  CG  . HIS A 1 26  ? 20.300  5.144  61.842 1.00 18.08 ? 26  HIS A CG  1 
ATOM   140  N  ND1 . HIS A 1 26  ? 19.581  4.336  60.988 1.00 20.16 ? 26  HIS A ND1 1 
ATOM   141  C  CD2 . HIS A 1 26  ? 21.474  4.507  62.066 1.00 19.28 ? 26  HIS A CD2 1 
ATOM   142  C  CE1 . HIS A 1 26  ? 20.291  3.257  60.707 1.00 20.53 ? 26  HIS A CE1 1 
ATOM   143  N  NE2 . HIS A 1 26  ? 21.443  3.337  61.348 1.00 21.37 ? 26  HIS A NE2 1 
ATOM   144  N  N   . ALA A 1 27  ? 20.222  9.573  62.685 1.00 11.05 ? 27  ALA A N   1 
ATOM   145  C  CA  . ALA A 1 27  ? 19.796  10.822 63.301 1.00 10.12 ? 27  ALA A CA  1 
ATOM   146  C  C   . ALA A 1 27  ? 19.598  11.939 62.286 1.00 10.43 ? 27  ALA A C   1 
ATOM   147  O  O   . ALA A 1 27  ? 18.697  12.762 62.436 1.00 11.07 ? 27  ALA A O   1 
ATOM   148  C  CB  . ALA A 1 27  ? 20.805  11.256 64.362 1.00 9.27  ? 27  ALA A CB  1 
ATOM   149  N  N   . TYR A 1 28  ? 20.435  11.967 61.253 1.00 9.23  ? 28  TYR A N   1 
ATOM   150  C  CA  . TYR A 1 28  ? 20.334  13.010 60.238 1.00 9.33  ? 28  TYR A CA  1 
ATOM   151  C  C   . TYR A 1 28  ? 21.313  12.781 59.100 1.00 9.82  ? 28  TYR A C   1 
ATOM   152  O  O   . TYR A 1 28  ? 22.084  11.822 59.103 1.00 9.98  ? 28  TYR A O   1 
ATOM   153  C  CB  . TYR A 1 28  ? 20.635  14.382 60.861 1.00 8.10  ? 28  TYR A CB  1 
ATOM   154  C  CG  . TYR A 1 28  ? 21.974  14.437 61.580 1.00 9.31  ? 28  TYR A CG  1 
ATOM   155  C  CD1 . TYR A 1 28  ? 23.178  14.449 60.865 1.00 9.45  ? 28  TYR A CD1 1 
ATOM   156  C  CD2 . TYR A 1 28  ? 22.039  14.427 62.975 1.00 8.71  ? 28  TYR A CD2 1 
ATOM   157  C  CE1 . TYR A 1 28  ? 24.416  14.442 61.526 1.00 11.03 ? 28  TYR A CE1 1 
ATOM   158  C  CE2 . TYR A 1 28  ? 23.268  14.421 63.645 1.00 10.16 ? 28  TYR A CE2 1 
ATOM   159  C  CZ  . TYR A 1 28  ? 24.450  14.426 62.917 1.00 10.33 ? 28  TYR A CZ  1 
ATOM   160  O  OH  . TYR A 1 28  ? 25.660  14.408 63.581 1.00 11.27 ? 28  TYR A OH  1 
ATOM   161  N  N   . THR A 1 29  ? 21.257  13.679 58.123 1.00 10.19 ? 29  THR A N   1 
ATOM   162  C  CA  . THR A 1 29  ? 22.163  13.667 56.983 1.00 9.60  ? 29  THR A CA  1 
ATOM   163  C  C   . THR A 1 29  ? 22.696  15.090 57.012 1.00 10.29 ? 29  THR A C   1 
ATOM   164  O  O   . THR A 1 29  ? 21.924  16.046 57.129 1.00 9.45  ? 29  THR A O   1 
ATOM   165  C  CB  . THR A 1 29  ? 21.438  13.389 55.659 1.00 9.29  ? 29  THR A CB  1 
ATOM   166  O  OG1 . THR A 1 29  ? 21.003  12.023 55.639 1.00 10.79 ? 29  THR A OG1 1 
ATOM   167  C  CG2 . THR A 1 29  ? 22.379  13.620 54.485 1.00 6.76  ? 29  THR A CG2 1 
ATOM   168  N  N   . LEU A 1 30  ? 24.010  15.237 56.917 1.00 8.99  ? 30  LEU A N   1 
ATOM   169  C  CA  . LEU A 1 30  ? 24.604  16.557 57.019 1.00 10.82 ? 30  LEU A CA  1 
ATOM   170  C  C   . LEU A 1 30  ? 25.688  16.833 55.991 1.00 10.54 ? 30  LEU A C   1 
ATOM   171  O  O   . LEU A 1 30  ? 26.434  15.940 55.605 1.00 10.72 ? 30  LEU A O   1 
ATOM   172  C  CB  . LEU A 1 30  ? 25.148  16.705 58.445 1.00 13.39 ? 30  LEU A CB  1 
ATOM   173  C  CG  . LEU A 1 30  ? 26.268  17.639 58.895 1.00 16.47 ? 30  LEU A CG  1 
ATOM   174  C  CD1 . LEU A 1 30  ? 26.240  17.668 60.422 1.00 14.30 ? 30  LEU A CD1 1 
ATOM   175  C  CD2 . LEU A 1 30  ? 27.633  17.166 58.395 1.00 13.99 ? 30  LEU A CD2 1 
ATOM   176  N  N   . ASN A 1 31  ? 25.754  18.081 55.543 1.00 10.14 ? 31  ASN A N   1 
ATOM   177  C  CA  . ASN A 1 31  ? 26.758  18.504 54.581 1.00 9.92  ? 31  ASN A CA  1 
ATOM   178  C  C   . ASN A 1 31  ? 27.634  19.529 55.294 1.00 9.37  ? 31  ASN A C   1 
ATOM   179  O  O   . ASN A 1 31  ? 27.180  20.623 55.619 1.00 9.50  ? 31  ASN A O   1 
ATOM   180  C  CB  . ASN A 1 31  ? 26.096  19.141 53.361 1.00 9.70  ? 31  ASN A CB  1 
ATOM   181  C  CG  . ASN A 1 31  ? 27.072  19.359 52.227 1.00 11.61 ? 31  ASN A CG  1 
ATOM   182  O  OD1 . ASN A 1 31  ? 27.616  20.451 52.060 1.00 13.73 ? 31  ASN A OD1 1 
ATOM   183  N  ND2 . ASN A 1 31  ? 27.308  18.315 51.443 1.00 13.05 ? 31  ASN A ND2 1 
ATOM   184  N  N   . ASN A 1 32  ? 28.889  19.172 55.540 1.00 9.80  ? 32  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 32  ? 29.804  20.055 56.250 1.00 9.14  ? 32  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 32  ? 30.503  21.086 55.381 1.00 11.01 ? 32  ASN A C   1 
ATOM   187  O  O   . ASN A 1 32  ? 30.670  20.903 54.176 1.00 13.10 ? 32  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 32  ? 30.858  19.227 56.986 1.00 10.75 ? 32  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 32  ? 31.622  20.036 58.016 1.00 13.03 ? 32  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 32  ? 31.030  20.633 58.917 1.00 12.47 ? 32  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 32  ? 32.946  20.058 57.890 1.00 13.29 ? 32  ASN A ND2 1 
ATOM   192  N  N   . ASN A 1 33  ? 30.902  22.183 56.014 1.00 10.63 ? 33  ASN A N   1 
ATOM   193  C  CA  . ASN A 1 33  ? 31.622  23.252 55.340 1.00 11.19 ? 33  ASN A CA  1 
ATOM   194  C  C   . ASN A 1 33  ? 32.942  23.379 56.091 1.00 11.66 ? 33  ASN A C   1 
ATOM   195  O  O   . ASN A 1 33  ? 32.983  23.901 57.207 1.00 11.85 ? 33  ASN A O   1 
ATOM   196  C  CB  . ASN A 1 33  ? 30.839  24.562 55.421 1.00 12.35 ? 33  ASN A CB  1 
ATOM   197  C  CG  . ASN A 1 33  ? 31.459  25.662 54.586 1.00 13.51 ? 33  ASN A CG  1 
ATOM   198  O  OD1 . ASN A 1 33  ? 32.660  25.919 54.671 1.00 11.82 ? 33  ASN A OD1 1 
ATOM   199  N  ND2 . ASN A 1 33  ? 30.641  26.320 53.773 1.00 11.18 ? 33  ASN A ND2 1 
ATOM   200  N  N   . SER A 1 34  ? 34.016  22.889 55.482 1.00 10.23 ? 34  SER A N   1 
ATOM   201  C  CA  . SER A 1 34  ? 35.327  22.926 56.113 1.00 12.10 ? 34  SER A CA  1 
ATOM   202  C  C   . SER A 1 34  ? 35.900  24.330 56.279 1.00 12.45 ? 34  SER A C   1 
ATOM   203  O  O   . SER A 1 34  ? 36.884  24.521 56.988 1.00 13.58 ? 34  SER A O   1 
ATOM   204  C  CB  . SER A 1 34  ? 36.306  22.043 55.335 1.00 12.24 ? 34  SER A CB  1 
ATOM   205  O  OG  . SER A 1 34  ? 36.560  22.576 54.054 1.00 16.40 ? 34  SER A OG  1 
ATOM   206  N  N   . THR A 1 35  ? 35.282  25.316 55.639 1.00 12.39 ? 35  THR A N   1 
ATOM   207  C  CA  . THR A 1 35  ? 35.753  26.692 55.754 1.00 12.38 ? 35  THR A CA  1 
ATOM   208  C  C   . THR A 1 35  ? 35.121  27.408 56.953 1.00 13.38 ? 35  THR A C   1 
ATOM   209  O  O   . THR A 1 35  ? 35.813  28.074 57.726 1.00 13.44 ? 35  THR A O   1 
ATOM   210  C  CB  . THR A 1 35  ? 35.447  27.496 54.473 1.00 14.81 ? 35  THR A CB  1 
ATOM   211  O  OG1 . THR A 1 35  ? 36.140  26.911 53.364 1.00 15.45 ? 35  THR A OG1 1 
ATOM   212  C  CG2 . THR A 1 35  ? 35.893  28.943 54.632 1.00 14.54 ? 35  THR A CG2 1 
ATOM   213  N  N   . THR A 1 36  ? 33.806  27.276 57.107 1.00 12.71 ? 36  THR A N   1 
ATOM   214  C  CA  . THR A 1 36  ? 33.110  27.918 58.219 1.00 11.17 ? 36  THR A CA  1 
ATOM   215  C  C   . THR A 1 36  ? 33.202  27.067 59.487 1.00 10.56 ? 36  THR A C   1 
ATOM   216  O  O   . THR A 1 36  ? 33.112  27.588 60.603 1.00 10.21 ? 36  THR A O   1 
ATOM   217  C  CB  . THR A 1 36  ? 31.627  28.146 57.886 1.00 9.39  ? 36  THR A CB  1 
ATOM   218  O  OG1 . THR A 1 36  ? 30.975  26.882 57.718 1.00 9.95  ? 36  THR A OG1 1 
ATOM   219  C  CG2 . THR A 1 36  ? 31.493  28.954 56.603 1.00 9.02  ? 36  THR A CG2 1 
ATOM   220  N  N   . LYS A 1 37  ? 33.387  25.760 59.291 1.00 9.16  ? 37  LYS A N   1 
ATOM   221  C  CA  . LYS A 1 37  ? 33.496  24.768 60.369 1.00 9.61  ? 37  LYS A CA  1 
ATOM   222  C  C   . LYS A 1 37  ? 32.127  24.300 60.857 1.00 9.69  ? 37  LYS A C   1 
ATOM   223  O  O   . LYS A 1 37  ? 32.022  23.556 61.835 1.00 10.11 ? 37  LYS A O   1 
ATOM   224  C  CB  . LYS A 1 37  ? 34.310  25.323 61.548 1.00 9.77  ? 37  LYS A CB  1 
ATOM   225  C  CG  . LYS A 1 37  ? 35.755  25.681 61.203 1.00 10.17 ? 37  LYS A CG  1 
ATOM   226  C  CD  . LYS A 1 37  ? 36.490  24.513 60.558 1.00 11.35 ? 37  LYS A CD  1 
ATOM   227  C  CE  . LYS A 1 37  ? 37.914  24.892 60.178 1.00 13.41 ? 37  LYS A CE  1 
ATOM   228  N  NZ  . LYS A 1 37  ? 37.951  26.079 59.280 1.00 13.13 ? 37  LYS A NZ  1 
ATOM   229  N  N   . PHE A 1 38  ? 31.082  24.735 60.163 1.00 9.30  ? 38  PHE A N   1 
ATOM   230  C  CA  . PHE A 1 38  ? 29.712  24.371 60.507 1.00 9.11  ? 38  PHE A CA  1 
ATOM   231  C  C   . PHE A 1 38  ? 29.003  23.778 59.285 1.00 9.75  ? 38  PHE A C   1 
ATOM   232  O  O   . PHE A 1 38  ? 29.385  24.043 58.144 1.00 9.86  ? 38  PHE A O   1 
ATOM   233  C  CB  . PHE A 1 38  ? 28.964  25.608 61.020 1.00 8.83  ? 38  PHE A CB  1 
ATOM   234  C  CG  . PHE A 1 38  ? 29.690  26.337 62.122 1.00 10.11 ? 38  PHE A CG  1 
ATOM   235  C  CD1 . PHE A 1 38  ? 29.869  25.739 63.372 1.00 9.48  ? 38  PHE A CD1 1 
ATOM   236  C  CD2 . PHE A 1 38  ? 30.240  27.595 61.899 1.00 8.80  ? 38  PHE A CD2 1 
ATOM   237  C  CE1 . PHE A 1 38  ? 30.589  26.386 64.378 1.00 10.22 ? 38  PHE A CE1 1 
ATOM   238  C  CE2 . PHE A 1 38  ? 30.961  28.248 62.898 1.00 9.62  ? 38  PHE A CE2 1 
ATOM   239  C  CZ  . PHE A 1 38  ? 31.137  27.643 64.137 1.00 9.44  ? 38  PHE A CZ  1 
ATOM   240  N  N   . ALA A 1 39  ? 27.971  22.977 59.527 1.00 9.43  ? 39  ALA A N   1 
ATOM   241  C  CA  . ALA A 1 39  ? 27.227  22.335 58.445 1.00 9.74  ? 39  ALA A CA  1 
ATOM   242  C  C   . ALA A 1 39  ? 26.422  23.321 57.598 1.00 9.23  ? 39  ALA A C   1 
ATOM   243  O  O   . ALA A 1 39  ? 25.783  24.230 58.129 1.00 9.36  ? 39  ALA A O   1 
ATOM   244  C  CB  . ALA A 1 39  ? 26.295  21.257 59.020 1.00 8.72  ? 39  ALA A CB  1 
ATOM   245  N  N   . ASN A 1 40  ? 26.461  23.132 56.280 1.00 8.74  ? 40  ASN A N   1 
ATOM   246  C  CA  . ASN A 1 40  ? 25.723  23.988 55.350 1.00 8.97  ? 40  ASN A CA  1 
ATOM   247  C  C   . ASN A 1 40  ? 24.230  23.717 55.508 1.00 8.60  ? 40  ASN A C   1 
ATOM   248  O  O   . ASN A 1 40  ? 23.396  24.618 55.399 1.00 8.30  ? 40  ASN A O   1 
ATOM   249  C  CB  . ASN A 1 40  ? 26.146  23.690 53.913 1.00 8.16  ? 40  ASN A CB  1 
ATOM   250  C  CG  . ASN A 1 40  ? 27.591  24.032 53.656 1.00 6.69  ? 40  ASN A CG  1 
ATOM   251  O  OD1 . ASN A 1 40  ? 28.024  25.149 53.915 1.00 9.82  ? 40  ASN A OD1 1 
ATOM   252  N  ND2 . ASN A 1 40  ? 28.348  23.071 53.145 1.00 8.42  ? 40  ASN A ND2 1 
ATOM   253  N  N   . TRP A 1 41  ? 23.903  22.455 55.752 1.00 8.05  ? 41  TRP A N   1 
ATOM   254  C  CA  . TRP A 1 41  ? 22.526  22.053 55.954 1.00 7.56  ? 41  TRP A CA  1 
ATOM   255  C  C   . TRP A 1 41  ? 22.488  20.714 56.657 1.00 7.66  ? 41  TRP A C   1 
ATOM   256  O  O   . TRP A 1 41  ? 23.427  19.922 56.565 1.00 7.62  ? 41  TRP A O   1 
ATOM   257  C  CB  . TRP A 1 41  ? 21.758  21.977 54.622 1.00 6.83  ? 41  TRP A CB  1 
ATOM   258  C  CG  . TRP A 1 41  ? 22.356  21.091 53.561 1.00 6.26  ? 41  TRP A CG  1 
ATOM   259  C  CD1 . TRP A 1 41  ? 23.113  21.488 52.492 1.00 6.49  ? 41  TRP A CD1 1 
ATOM   260  C  CD2 . TRP A 1 41  ? 22.192  19.670 53.429 1.00 6.56  ? 41  TRP A CD2 1 
ATOM   261  N  NE1 . TRP A 1 41  ? 23.427  20.405 51.702 1.00 7.16  ? 41  TRP A NE1 1 
ATOM   262  C  CE2 . TRP A 1 41  ? 22.875  19.278 52.253 1.00 6.53  ? 41  TRP A CE2 1 
ATOM   263  C  CE3 . TRP A 1 41  ? 21.533  18.692 54.186 1.00 6.44  ? 41  TRP A CE3 1 
ATOM   264  C  CZ2 . TRP A 1 41  ? 22.919  17.948 51.818 1.00 6.45  ? 41  TRP A CZ2 1 
ATOM   265  C  CZ3 . TRP A 1 41  ? 21.576  17.367 53.753 1.00 6.34  ? 41  TRP A CZ3 1 
ATOM   266  C  CH2 . TRP A 1 41  ? 22.266  17.010 52.577 1.00 6.89  ? 41  TRP A CH2 1 
ATOM   267  N  N   . VAL A 1 42  ? 21.400  20.486 57.383 1.00 6.97  ? 42  VAL A N   1 
ATOM   268  C  CA  . VAL A 1 42  ? 21.194  19.250 58.115 1.00 6.26  ? 42  VAL A CA  1 
ATOM   269  C  C   . VAL A 1 42  ? 19.750  18.840 57.870 1.00 7.05  ? 42  VAL A C   1 
ATOM   270  O  O   . VAL A 1 42  ? 18.829  19.603 58.146 1.00 7.37  ? 42  VAL A O   1 
ATOM   271  C  CB  . VAL A 1 42  ? 21.408  19.446 59.634 1.00 5.84  ? 42  VAL A CB  1 
ATOM   272  C  CG1 . VAL A 1 42  ? 21.208  18.124 60.358 1.00 6.58  ? 42  VAL A CG1 1 
ATOM   273  C  CG2 . VAL A 1 42  ? 22.803  19.985 59.900 1.00 5.37  ? 42  VAL A CG2 1 
ATOM   274  N  N   . ALA A 1 43  ? 19.560  17.643 57.331 1.00 6.68  ? 43  ALA A N   1 
ATOM   275  C  CA  . ALA A 1 43  ? 18.226  17.141 57.052 1.00 7.28  ? 43  ALA A CA  1 
ATOM   276  C  C   . ALA A 1 43  ? 17.921  15.991 58.005 1.00 8.43  ? 43  ALA A C   1 
ATOM   277  O  O   . ALA A 1 43  ? 18.773  15.138 58.254 1.00 8.53  ? 43  ALA A O   1 
ATOM   278  C  CB  . ALA A 1 43  ? 18.144  16.661 55.610 1.00 5.75  ? 43  ALA A CB  1 
ATOM   279  N  N   . TYR A 1 44  ? 16.715  15.979 58.559 1.00 7.46  ? 44  TYR A N   1 
ATOM   280  C  CA  . TYR A 1 44  ? 16.341  14.909 59.462 1.00 7.84  ? 44  TYR A CA  1 
ATOM   281  C  C   . TYR A 1 44  ? 14.890  14.496 59.267 1.00 9.47  ? 44  TYR A C   1 
ATOM   282  O  O   . TYR A 1 44  ? 14.081  15.232 58.688 1.00 9.03  ? 44  TYR A O   1 
ATOM   283  C  CB  . TYR A 1 44  ? 16.623  15.290 60.923 1.00 6.89  ? 44  TYR A CB  1 
ATOM   284  C  CG  . TYR A 1 44  ? 16.031  16.601 61.379 1.00 6.96  ? 44  TYR A CG  1 
ATOM   285  C  CD1 . TYR A 1 44  ? 16.731  17.796 61.224 1.00 6.78  ? 44  TYR A CD1 1 
ATOM   286  C  CD2 . TYR A 1 44  ? 14.791  16.641 62.015 1.00 6.02  ? 44  TYR A CD2 1 
ATOM   287  C  CE1 . TYR A 1 44  ? 16.213  18.999 61.695 1.00 7.15  ? 44  TYR A CE1 1 
ATOM   288  C  CE2 . TYR A 1 44  ? 14.266  17.837 62.488 1.00 6.22  ? 44  TYR A CE2 1 
ATOM   289  C  CZ  . TYR A 1 44  ? 14.981  19.008 62.326 1.00 5.77  ? 44  TYR A CZ  1 
ATOM   290  O  OH  . TYR A 1 44  ? 14.468  20.186 62.805 1.00 7.49  ? 44  TYR A OH  1 
ATOM   291  N  N   . HIS A 1 45  ? 14.576  13.306 59.760 1.00 10.67 ? 45  HIS A N   1 
ATOM   292  C  CA  . HIS A 1 45  ? 13.258  12.714 59.609 1.00 10.89 ? 45  HIS A CA  1 
ATOM   293  C  C   . HIS A 1 45  ? 12.660  12.295 60.952 1.00 12.07 ? 45  HIS A C   1 
ATOM   294  O  O   . HIS A 1 45  ? 13.080  11.309 61.558 1.00 12.38 ? 45  HIS A O   1 
ATOM   295  C  CB  . HIS A 1 45  ? 13.400  11.505 58.674 1.00 9.87  ? 45  HIS A CB  1 
ATOM   296  C  CG  . HIS A 1 45  ? 12.127  10.767 58.414 1.00 9.80  ? 45  HIS A CG  1 
ATOM   297  N  ND1 . HIS A 1 45  ? 12.107  9.445  58.023 1.00 10.21 ? 45  HIS A ND1 1 
ATOM   298  C  CD2 . HIS A 1 45  ? 10.834  11.163 58.470 1.00 10.00 ? 45  HIS A CD2 1 
ATOM   299  C  CE1 . HIS A 1 45  ? 10.857  9.059  57.849 1.00 10.12 ? 45  HIS A CE1 1 
ATOM   300  N  NE2 . HIS A 1 45  ? 10.065  10.082 58.114 1.00 10.12 ? 45  HIS A NE2 1 
ATOM   301  N  N   . ILE A 1 46  ? 11.680  13.053 61.421 1.00 11.10 ? 46  ILE A N   1 
ATOM   302  C  CA  . ILE A 1 46  ? 11.037  12.730 62.681 1.00 10.78 ? 46  ILE A CA  1 
ATOM   303  C  C   . ILE A 1 46  ? 9.879   11.770 62.441 1.00 11.38 ? 46  ILE A C   1 
ATOM   304  O  O   . ILE A 1 46  ? 9.076   11.967 61.528 1.00 10.93 ? 46  ILE A O   1 
ATOM   305  C  CB  . ILE A 1 46  ? 10.473  13.993 63.372 1.00 9.73  ? 46  ILE A CB  1 
ATOM   306  C  CG1 . ILE A 1 46  ? 11.595  14.996 63.639 1.00 8.40  ? 46  ILE A CG1 1 
ATOM   307  C  CG2 . ILE A 1 46  ? 9.791   13.608 64.686 1.00 9.91  ? 46  ILE A CG2 1 
ATOM   308  C  CD1 . ILE A 1 46  ? 11.102  16.322 64.179 1.00 9.77  ? 46  ILE A CD1 1 
ATOM   309  N  N   . THR A 1 47  ? 9.815   10.717 63.247 1.00 12.22 ? 47  THR A N   1 
ATOM   310  C  CA  . THR A 1 47  ? 8.721   9.753  63.170 1.00 14.29 ? 47  THR A CA  1 
ATOM   311  C  C   . THR A 1 47  ? 8.257   9.548  64.604 1.00 14.43 ? 47  THR A C   1 
ATOM   312  O  O   . THR A 1 47  ? 8.844   10.094 65.537 1.00 13.23 ? 47  THR A O   1 
ATOM   313  C  CB  . THR A 1 47  ? 9.151   8.388  62.584 1.00 14.19 ? 47  THR A CB  1 
ATOM   314  O  OG1 . THR A 1 47  ? 9.928   7.669  63.550 1.00 14.46 ? 47  THR A OG1 1 
ATOM   315  C  CG2 . THR A 1 47  ? 9.958   8.582  61.317 1.00 15.17 ? 47  THR A CG2 1 
ATOM   316  N  N   . LYS A 1 48  ? 7.208   8.761  64.785 1.00 15.67 ? 48  LYS A N   1 
ATOM   317  C  CA  . LYS A 1 48  ? 6.689   8.521  66.121 1.00 17.78 ? 48  LYS A CA  1 
ATOM   318  C  C   . LYS A 1 48  ? 7.704   7.852  67.044 1.00 17.87 ? 48  LYS A C   1 
ATOM   319  O  O   . LYS A 1 48  ? 7.639   8.013  68.261 1.00 19.42 ? 48  LYS A O   1 
ATOM   320  C  CB  . LYS A 1 48  ? 5.423   7.666  66.039 1.00 19.98 ? 48  LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 48  ? 4.142   8.476  66.051 1.00 23.58 ? 48  LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 48  ? 3.585   8.643  64.652 1.00 29.05 ? 48  LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 48  ? 2.069   8.694  64.666 1.00 25.67 ? 48  LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 48  ? 1.570   10.080 64.485 1.00 21.32 ? 48  LYS A NZ  1 
ATOM   325  N  N   . ASP A 1 49  ? 8.653   7.122  66.468 1.00 17.24 ? 49  ASP A N   1 
ATOM   326  C  CA  . ASP A 1 49  ? 9.654   6.415  67.261 1.00 18.10 ? 49  ASP A CA  1 
ATOM   327  C  C   . ASP A 1 49  ? 10.988  7.122  67.468 1.00 17.93 ? 49  ASP A C   1 
ATOM   328  O  O   . ASP A 1 49  ? 11.882  6.555  68.097 1.00 17.86 ? 49  ASP A O   1 
ATOM   329  C  CB  . ASP A 1 49  ? 9.937   5.045  66.643 1.00 22.87 ? 49  ASP A CB  1 
ATOM   330  C  CG  . ASP A 1 49  ? 8.676   4.320  66.228 1.00 27.26 ? 49  ASP A CG  1 
ATOM   331  O  OD1 . ASP A 1 49  ? 7.753   4.192  67.063 1.00 30.90 ? 49  ASP A OD1 1 
ATOM   332  O  OD2 . ASP A 1 49  ? 8.610   3.878  65.063 1.00 31.81 ? 49  ASP A OD2 1 
ATOM   333  N  N   . THR A 1 50  ? 11.142  8.341  66.956 1.00 16.20 ? 50  THR A N   1 
ATOM   334  C  CA  . THR A 1 50  ? 12.419  9.035  67.114 1.00 15.00 ? 50  THR A CA  1 
ATOM   335  C  C   . THR A 1 50  ? 12.567  9.932  68.345 1.00 15.87 ? 50  THR A C   1 
ATOM   336  O  O   . THR A 1 50  ? 13.653  10.027 68.907 1.00 17.29 ? 50  THR A O   1 
ATOM   337  C  CB  . THR A 1 50  ? 12.782  9.868  65.851 1.00 14.61 ? 50  THR A CB  1 
ATOM   338  O  OG1 . THR A 1 50  ? 11.797  10.884 65.633 1.00 13.79 ? 50  THR A OG1 1 
ATOM   339  C  CG2 . THR A 1 50  ? 12.866  8.969  64.626 1.00 11.97 ? 50  THR A CG2 1 
ATOM   340  N  N   . PRO A 1 51  ? 11.489  10.604 68.783 1.00 16.13 ? 51  PRO A N   1 
ATOM   341  C  CA  . PRO A 1 51  ? 11.655  11.459 69.964 1.00 16.01 ? 51  PRO A CA  1 
ATOM   342  C  C   . PRO A 1 51  ? 12.000  10.691 71.239 1.00 17.55 ? 51  PRO A C   1 
ATOM   343  O  O   . PRO A 1 51  ? 11.596  9.546  71.422 1.00 17.42 ? 51  PRO A O   1 
ATOM   344  C  CB  . PRO A 1 51  ? 10.312  12.187 70.083 1.00 15.81 ? 51  PRO A CB  1 
ATOM   345  C  CG  . PRO A 1 51  ? 9.636   11.986 68.770 1.00 16.77 ? 51  PRO A CG  1 
ATOM   346  C  CD  . PRO A 1 51  ? 10.113  10.657 68.269 1.00 16.47 ? 51  PRO A CD  1 
ATOM   347  N  N   . ALA A 1 52  ? 12.753  11.341 72.116 1.00 18.35 ? 52  ALA A N   1 
ATOM   348  C  CA  . ALA A 1 52  ? 13.160  10.752 73.381 1.00 19.41 ? 52  ALA A CA  1 
ATOM   349  C  C   . ALA A 1 52  ? 13.649  11.883 74.274 1.00 21.30 ? 52  ALA A C   1 
ATOM   350  O  O   . ALA A 1 52  ? 14.383  12.764 73.821 1.00 20.72 ? 52  ALA A O   1 
ATOM   351  C  CB  . ALA A 1 52  ? 14.270  9.749  73.153 1.00 17.47 ? 52  ALA A CB  1 
ATOM   352  N  N   . SER A 1 53  ? 13.239  11.874 75.537 1.00 21.35 ? 53  SER A N   1 
ATOM   353  C  CA  . SER A 1 53  ? 13.666  12.923 76.452 1.00 23.97 ? 53  SER A CA  1 
ATOM   354  C  C   . SER A 1 53  ? 14.629  12.396 77.512 1.00 23.67 ? 53  SER A C   1 
ATOM   355  O  O   . SER A 1 53  ? 14.838  11.188 77.631 1.00 23.73 ? 53  SER A O   1 
ATOM   356  C  CB  . SER A 1 53  ? 12.449  13.562 77.124 1.00 25.72 ? 53  SER A CB  1 
ATOM   357  O  OG  . SER A 1 53  ? 11.622  12.574 77.707 1.00 32.00 ? 53  SER A OG  1 
ATOM   358  N  N   . GLY A 1 54  ? 15.229  13.314 78.264 1.00 28.67 ? 54  GLY A N   1 
ATOM   359  C  CA  . GLY A 1 54  ? 16.149  12.931 79.320 1.00 29.83 ? 54  GLY A CA  1 
ATOM   360  C  C   . GLY A 1 54  ? 17.549  12.510 78.908 1.00 30.33 ? 54  GLY A C   1 
ATOM   361  O  O   . GLY A 1 54  ? 18.321  12.035 79.744 1.00 33.66 ? 54  GLY A O   1 
ATOM   362  N  N   . LYS A 1 55  ? 17.892  12.669 77.636 1.00 24.05 ? 55  LYS A N   1 
ATOM   363  C  CA  . LYS A 1 55  ? 19.225  12.288 77.187 1.00 21.65 ? 55  LYS A CA  1 
ATOM   364  C  C   . LYS A 1 55  ? 20.221  13.382 77.561 1.00 20.21 ? 55  LYS A C   1 
ATOM   365  O  O   . LYS A 1 55  ? 19.868  14.560 77.619 1.00 19.65 ? 55  LYS A O   1 
ATOM   366  C  CB  . LYS A 1 55  ? 19.229  12.048 75.678 1.00 23.02 ? 55  LYS A CB  1 
ATOM   367  C  CG  . LYS A 1 55  ? 18.314  10.918 75.243 1.00 21.69 ? 55  LYS A CG  1 
ATOM   368  C  CD  . LYS A 1 55  ? 19.006  9.574  75.330 1.00 23.37 ? 55  LYS A CD  1 
ATOM   369  C  CE  . LYS A 1 55  ? 18.110  8.466  74.801 1.00 24.12 ? 55  LYS A CE  1 
ATOM   370  N  NZ  . LYS A 1 55  ? 18.863  7.408  74.073 1.00 25.84 ? 55  LYS A NZ  1 
ATOM   371  N  N   . THR A 1 56  ? 21.461  12.983 77.824 1.00 19.59 ? 56  THR A N   1 
ATOM   372  C  CA  . THR A 1 56  ? 22.505  13.923 78.217 1.00 19.65 ? 56  THR A CA  1 
ATOM   373  C  C   . THR A 1 56  ? 23.221  14.543 77.026 1.00 18.76 ? 56  THR A C   1 
ATOM   374  O  O   . THR A 1 56  ? 23.112  14.065 75.896 1.00 19.17 ? 56  THR A O   1 
ATOM   375  C  CB  . THR A 1 56  ? 23.543  13.241 79.122 1.00 22.29 ? 56  THR A CB  1 
ATOM   376  O  OG1 . THR A 1 56  ? 24.073  12.087 78.460 1.00 24.85 ? 56  THR A OG1 1 
ATOM   377  C  CG2 . THR A 1 56  ? 22.894  12.808 80.427 1.00 23.78 ? 56  THR A CG2 1 
ATOM   378  N  N   . ARG A 1 57  ? 23.964  15.609 77.292 1.00 17.10 ? 57  ARG A N   1 
ATOM   379  C  CA  . ARG A 1 57  ? 24.681  16.320 76.247 1.00 16.10 ? 57  ARG A CA  1 
ATOM   380  C  C   . ARG A 1 57  ? 26.198  16.237 76.394 1.00 15.30 ? 57  ARG A C   1 
ATOM   381  O  O   . ARG A 1 57  ? 26.821  17.115 76.988 1.00 15.29 ? 57  ARG A O   1 
ATOM   382  C  CB  . ARG A 1 57  ? 24.245  17.787 76.238 1.00 23.32 ? 57  ARG A CB  1 
ATOM   383  C  CG  . ARG A 1 57  ? 22.973  18.060 75.442 1.00 29.19 ? 57  ARG A CG  1 
ATOM   384  C  CD  . ARG A 1 57  ? 21.765  18.327 76.336 1.00 35.37 ? 57  ARG A CD  1 
ATOM   385  N  NE  . ARG A 1 57  ? 22.121  18.950 77.610 1.00 39.15 ? 57  ARG A NE  1 
ATOM   386  C  CZ  . ARG A 1 57  ? 21.731  18.499 78.802 1.00 40.19 ? 57  ARG A CZ  1 
ATOM   387  N  NH1 . ARG A 1 57  ? 20.968  17.415 78.892 1.00 40.32 ? 57  ARG A NH1 1 
ATOM   388  N  NH2 . ARG A 1 57  ? 22.102  19.131 79.909 1.00 40.40 ? 57  ARG A NH2 1 
ATOM   389  N  N   . ASN A 1 58  ? 26.787  15.179 75.848 1.00 13.87 ? 58  ASN A N   1 
ATOM   390  C  CA  . ASN A 1 58  ? 28.236  15.004 75.901 1.00 14.06 ? 58  ASN A CA  1 
ATOM   391  C  C   . ASN A 1 58  ? 28.834  15.466 74.571 1.00 13.29 ? 58  ASN A C   1 
ATOM   392  O  O   . ASN A 1 58  ? 28.972  14.676 73.635 1.00 13.32 ? 58  ASN A O   1 
ATOM   393  C  CB  . ASN A 1 58  ? 28.591  13.531 76.144 1.00 12.58 ? 58  ASN A CB  1 
ATOM   394  C  CG  . ASN A 1 58  ? 28.743  13.198 77.622 1.00 13.17 ? 58  ASN A CG  1 
ATOM   395  O  OD1 . ASN A 1 58  ? 28.385  12.107 78.064 1.00 14.69 ? 58  ASN A OD1 1 
ATOM   396  N  ND2 . ASN A 1 58  ? 29.278  14.137 78.389 1.00 8.99  ? 58  ASN A ND2 1 
ATOM   397  N  N   . TRP A 1 59  ? 29.178  16.747 74.489 1.00 13.05 ? 59  TRP A N   1 
ATOM   398  C  CA  . TRP A 1 59  ? 29.754  17.305 73.268 1.00 13.95 ? 59  TRP A CA  1 
ATOM   399  C  C   . TRP A 1 59  ? 31.003  16.539 72.835 1.00 14.42 ? 59  TRP A C   1 
ATOM   400  O  O   . TRP A 1 59  ? 31.847  16.192 73.666 1.00 14.95 ? 59  TRP A O   1 
ATOM   401  C  CB  . TRP A 1 59  ? 30.107  18.781 73.475 1.00 11.86 ? 59  TRP A CB  1 
ATOM   402  C  CG  . TRP A 1 59  ? 29.068  19.552 74.229 1.00 11.84 ? 59  TRP A CG  1 
ATOM   403  C  CD1 . TRP A 1 59  ? 29.216  20.151 75.448 1.00 11.24 ? 59  TRP A CD1 1 
ATOM   404  C  CD2 . TRP A 1 59  ? 27.721  19.816 73.811 1.00 12.79 ? 59  TRP A CD2 1 
ATOM   405  N  NE1 . TRP A 1 59  ? 28.046  20.771 75.817 1.00 11.21 ? 59  TRP A NE1 1 
ATOM   406  C  CE2 . TRP A 1 59  ? 27.111  20.582 74.833 1.00 12.00 ? 59  TRP A CE2 1 
ATOM   407  C  CE3 . TRP A 1 59  ? 26.968  19.481 72.674 1.00 12.71 ? 59  TRP A CE3 1 
ATOM   408  C  CZ2 . TRP A 1 59  ? 25.781  21.020 74.752 1.00 12.87 ? 59  TRP A CZ2 1 
ATOM   409  C  CZ3 . TRP A 1 59  ? 25.643  19.917 72.594 1.00 12.18 ? 59  TRP A CZ3 1 
ATOM   410  C  CH2 . TRP A 1 59  ? 25.066  20.678 73.629 1.00 12.93 ? 59  TRP A CH2 1 
ATOM   411  N  N   . LYS A 1 60  ? 31.116  16.284 71.533 1.00 13.07 ? 60  LYS A N   1 
ATOM   412  C  CA  . LYS A 1 60  ? 32.258  15.559 70.981 1.00 13.49 ? 60  LYS A CA  1 
ATOM   413  C  C   . LYS A 1 60  ? 32.564  15.980 69.551 1.00 12.18 ? 60  LYS A C   1 
ATOM   414  O  O   . LYS A 1 60  ? 31.679  16.385 68.803 1.00 10.77 ? 60  LYS A O   1 
ATOM   415  C  CB  . LYS A 1 60  ? 31.994  14.051 70.984 1.00 18.72 ? 60  LYS A CB  1 
ATOM   416  C  CG  . LYS A 1 60  ? 32.130  13.394 72.336 1.00 28.77 ? 60  LYS A CG  1 
ATOM   417  C  CD  . LYS A 1 60  ? 32.408  11.909 72.194 1.00 32.93 ? 60  LYS A CD  1 
ATOM   418  C  CE  . LYS A 1 60  ? 32.427  11.229 73.557 1.00 35.31 ? 60  LYS A CE  1 
ATOM   419  N  NZ  . LYS A 1 60  ? 31.278  11.665 74.405 1.00 36.00 ? 60  LYS A NZ  1 
ATOM   420  N  N   . THR A 1 61  ? 33.829  15.872 69.175 1.00 11.34 ? 61  THR A N   1 
ATOM   421  C  CA  . THR A 1 61  ? 34.242  16.207 67.825 1.00 11.71 ? 61  THR A CA  1 
ATOM   422  C  C   . THR A 1 61  ? 33.702  15.103 66.921 1.00 12.02 ? 61  THR A C   1 
ATOM   423  O  O   . THR A 1 61  ? 33.794  13.924 67.265 1.00 12.05 ? 61  THR A O   1 
ATOM   424  C  CB  . THR A 1 61  ? 35.775  16.245 67.725 1.00 11.57 ? 61  THR A CB  1 
ATOM   425  O  OG1 . THR A 1 61  ? 36.280  17.206 68.659 1.00 12.47 ? 61  THR A OG1 1 
ATOM   426  C  CG2 . THR A 1 61  ? 36.218  16.619 66.313 1.00 11.31 ? 61  THR A CG2 1 
ATOM   427  N  N   . ASP A 1 62  ? 33.124  15.473 65.781 1.00 11.36 ? 62  ASP A N   1 
ATOM   428  C  CA  . ASP A 1 62  ? 32.599  14.468 64.866 1.00 11.19 ? 62  ASP A CA  1 
ATOM   429  C  C   . ASP A 1 62  ? 33.749  13.583 64.394 1.00 12.63 ? 62  ASP A C   1 
ATOM   430  O  O   . ASP A 1 62  ? 34.671  14.052 63.736 1.00 12.17 ? 62  ASP A O   1 
ATOM   431  C  CB  . ASP A 1 62  ? 31.937  15.119 63.656 1.00 11.02 ? 62  ASP A CB  1 
ATOM   432  C  CG  . ASP A 1 62  ? 31.087  14.139 62.874 1.00 13.71 ? 62  ASP A CG  1 
ATOM   433  O  OD1 . ASP A 1 62  ? 31.518  12.977 62.709 1.00 11.08 ? 62  ASP A OD1 1 
ATOM   434  O  OD2 . ASP A 1 62  ? 29.985  14.523 62.432 1.00 13.88 ? 62  ASP A OD2 1 
ATOM   435  N  N   . PRO A 1 63  ? 33.699  12.284 64.718 1.00 13.91 ? 63  PRO A N   1 
ATOM   436  C  CA  . PRO A 1 63  ? 34.766  11.365 64.312 1.00 15.05 ? 63  PRO A CA  1 
ATOM   437  C  C   . PRO A 1 63  ? 34.826  11.070 62.814 1.00 16.64 ? 63  PRO A C   1 
ATOM   438  O  O   . PRO A 1 63  ? 35.832  10.563 62.317 1.00 17.15 ? 63  PRO A O   1 
ATOM   439  C  CB  . PRO A 1 63  ? 34.484  10.110 65.134 1.00 14.69 ? 63  PRO A CB  1 
ATOM   440  C  CG  . PRO A 1 63  ? 33.005  10.150 65.362 1.00 14.73 ? 63  PRO A CG  1 
ATOM   441  C  CD  . PRO A 1 63  ? 32.640  11.602 65.484 1.00 13.19 ? 63  PRO A CD  1 
ATOM   442  N  N   . ALA A 1 64  ? 33.759  11.395 62.093 1.00 15.50 ? 64  ALA A N   1 
ATOM   443  C  CA  . ALA A 1 64  ? 33.712  11.135 60.659 1.00 15.67 ? 64  ALA A CA  1 
ATOM   444  C  C   . ALA A 1 64  ? 34.384  12.218 59.823 1.00 16.07 ? 64  ALA A C   1 
ATOM   445  O  O   . ALA A 1 64  ? 34.626  12.029 58.634 1.00 17.13 ? 64  ALA A O   1 
ATOM   446  C  CB  . ALA A 1 64  ? 32.265  10.964 60.217 1.00 16.28 ? 64  ALA A CB  1 
ATOM   447  N  N   . LEU A 1 65  ? 34.690  13.353 60.441 1.00 15.71 ? 65  LEU A N   1 
ATOM   448  C  CA  . LEU A 1 65  ? 35.318  14.453 59.722 1.00 15.61 ? 65  LEU A CA  1 
ATOM   449  C  C   . LEU A 1 65  ? 36.773  14.654 60.107 1.00 17.03 ? 65  LEU A C   1 
ATOM   450  O  O   . LEU A 1 65  ? 37.228  14.166 61.139 1.00 18.54 ? 65  LEU A O   1 
ATOM   451  C  CB  . LEU A 1 65  ? 34.566  15.757 59.993 1.00 14.99 ? 65  LEU A CB  1 
ATOM   452  C  CG  . LEU A 1 65  ? 33.056  15.771 59.758 1.00 13.90 ? 65  LEU A CG  1 
ATOM   453  C  CD1 . LEU A 1 65  ? 32.446  16.978 60.454 1.00 13.65 ? 65  LEU A CD1 1 
ATOM   454  C  CD2 . LEU A 1 65  ? 32.778  15.819 58.264 1.00 15.46 ? 65  LEU A CD2 1 
ATOM   455  N  N   . ASN A 1 66  ? 37.501  15.378 59.266 1.00 18.31 ? 66  ASN A N   1 
ATOM   456  C  CA  . ASN A 1 66  ? 38.894  15.688 59.546 1.00 19.38 ? 66  ASN A CA  1 
ATOM   457  C  C   . ASN A 1 66  ? 38.822  16.726 60.667 1.00 18.34 ? 66  ASN A C   1 
ATOM   458  O  O   . ASN A 1 66  ? 38.126  17.733 60.546 1.00 17.85 ? 66  ASN A O   1 
ATOM   459  C  CB  . ASN A 1 66  ? 39.566  16.288 58.306 1.00 22.40 ? 66  ASN A CB  1 
ATOM   460  C  CG  . ASN A 1 66  ? 41.014  16.668 58.553 1.00 27.62 ? 66  ASN A CG  1 
ATOM   461  O  OD1 . ASN A 1 66  ? 41.331  17.370 59.512 1.00 32.25 ? 66  ASN A OD1 1 
ATOM   462  N  ND2 . ASN A 1 66  ? 41.902  16.204 57.685 1.00 32.62 ? 66  ASN A ND2 1 
ATOM   463  N  N   . PRO A 1 67  ? 39.527  16.486 61.780 1.00 17.71 ? 67  PRO A N   1 
ATOM   464  C  CA  . PRO A 1 67  ? 39.522  17.414 62.918 1.00 16.87 ? 67  PRO A CA  1 
ATOM   465  C  C   . PRO A 1 67  ? 39.783  18.881 62.578 1.00 16.96 ? 67  PRO A C   1 
ATOM   466  O  O   . PRO A 1 67  ? 39.367  19.778 63.315 1.00 16.58 ? 67  PRO A O   1 
ATOM   467  C  CB  . PRO A 1 67  ? 40.584  16.844 63.861 1.00 18.49 ? 67  PRO A CB  1 
ATOM   468  C  CG  . PRO A 1 67  ? 41.326  15.812 63.058 1.00 18.73 ? 67  PRO A CG  1 
ATOM   469  C  CD  . PRO A 1 67  ? 40.369  15.309 62.036 1.00 17.72 ? 67  PRO A CD  1 
ATOM   470  N  N   . ALA A 1 68  ? 40.463  19.126 61.462 1.00 15.42 ? 68  ALA A N   1 
ATOM   471  C  CA  . ALA A 1 68  ? 40.772  20.489 61.044 1.00 14.14 ? 68  ALA A CA  1 
ATOM   472  C  C   . ALA A 1 68  ? 39.607  21.167 60.320 1.00 13.35 ? 68  ALA A C   1 
ATOM   473  O  O   . ALA A 1 68  ? 39.601  22.385 60.165 1.00 14.47 ? 68  ALA A O   1 
ATOM   474  C  CB  . ALA A 1 68  ? 42.005  20.487 60.145 1.00 15.29 ? 68  ALA A CB  1 
ATOM   475  N  N   . ASP A 1 69  ? 38.625  20.381 59.886 1.00 11.75 ? 69  ASP A N   1 
ATOM   476  C  CA  . ASP A 1 69  ? 37.474  20.918 59.157 1.00 12.08 ? 69  ASP A CA  1 
ATOM   477  C  C   . ASP A 1 69  ? 36.230  21.123 60.016 1.00 12.90 ? 69  ASP A C   1 
ATOM   478  O  O   . ASP A 1 69  ? 35.175  21.503 59.506 1.00 12.36 ? 69  ASP A O   1 
ATOM   479  C  CB  . ASP A 1 69  ? 37.111  19.991 57.993 1.00 15.22 ? 69  ASP A CB  1 
ATOM   480  C  CG  . ASP A 1 69  ? 38.283  19.724 57.069 1.00 17.94 ? 69  ASP A CG  1 
ATOM   481  O  OD1 . ASP A 1 69  ? 39.155  20.611 56.938 1.00 19.30 ? 69  ASP A OD1 1 
ATOM   482  O  OD2 . ASP A 1 69  ? 38.329  18.625 56.475 1.00 19.12 ? 69  ASP A OD2 1 
ATOM   483  N  N   . THR A 1 70  ? 36.355  20.865 61.312 1.00 12.68 ? 70  THR A N   1 
ATOM   484  C  CA  . THR A 1 70  ? 35.238  21.005 62.232 1.00 11.85 ? 70  THR A CA  1 
ATOM   485  C  C   . THR A 1 70  ? 35.765  21.519 63.575 1.00 12.97 ? 70  THR A C   1 
ATOM   486  O  O   . THR A 1 70  ? 36.974  21.685 63.746 1.00 13.89 ? 70  THR A O   1 
ATOM   487  C  CB  . THR A 1 70  ? 34.521  19.636 62.405 1.00 12.77 ? 70  THR A CB  1 
ATOM   488  O  OG1 . THR A 1 70  ? 33.267  19.816 63.077 1.00 12.39 ? 70  THR A OG1 1 
ATOM   489  C  CG2 . THR A 1 70  ? 35.398  18.666 63.185 1.00 12.79 ? 70  THR A CG2 1 
ATOM   490  N  N   . LEU A 1 71  ? 34.868  21.788 64.519 1.00 10.90 ? 71  LEU A N   1 
ATOM   491  C  CA  . LEU A 1 71  ? 35.281  22.282 65.831 1.00 11.14 ? 71  LEU A CA  1 
ATOM   492  C  C   . LEU A 1 71  ? 35.351  21.169 66.878 1.00 10.85 ? 71  LEU A C   1 
ATOM   493  O  O   . LEU A 1 71  ? 34.729  20.116 66.724 1.00 11.78 ? 71  LEU A O   1 
ATOM   494  C  CB  . LEU A 1 71  ? 34.319  23.370 66.320 1.00 10.40 ? 71  LEU A CB  1 
ATOM   495  C  CG  . LEU A 1 71  ? 34.292  24.705 65.568 1.00 11.13 ? 71  LEU A CG  1 
ATOM   496  C  CD1 . LEU A 1 71  ? 33.501  25.717 66.377 1.00 10.55 ? 71  LEU A CD1 1 
ATOM   497  C  CD2 . LEU A 1 71  ? 35.711  25.201 65.328 1.00 10.36 ? 71  LEU A CD2 1 
ATOM   498  N  N   . ALA A 1 72  ? 36.122  21.412 67.936 1.00 10.84 ? 72  ALA A N   1 
ATOM   499  C  CA  . ALA A 1 72  ? 36.270  20.462 69.039 1.00 10.92 ? 72  ALA A CA  1 
ATOM   500  C  C   . ALA A 1 72  ? 35.659  21.124 70.278 1.00 10.92 ? 72  ALA A C   1 
ATOM   501  O  O   . ALA A 1 72  ? 35.533  22.350 70.330 1.00 11.85 ? 72  ALA A O   1 
ATOM   502  C  CB  . ALA A 1 72  ? 37.750  20.151 69.276 1.00 10.11 ? 72  ALA A CB  1 
ATOM   503  N  N   . PRO A 1 73  ? 35.269  20.328 71.289 1.00 10.15 ? 73  PRO A N   1 
ATOM   504  C  CA  . PRO A 1 73  ? 34.674  20.922 72.494 1.00 9.47  ? 73  PRO A CA  1 
ATOM   505  C  C   . PRO A 1 73  ? 35.490  22.064 73.095 1.00 10.02 ? 73  PRO A C   1 
ATOM   506  O  O   . PRO A 1 73  ? 34.929  23.038 73.594 1.00 9.65  ? 73  PRO A O   1 
ATOM   507  C  CB  . PRO A 1 73  ? 34.539  19.738 73.451 1.00 11.05 ? 73  PRO A CB  1 
ATOM   508  C  CG  . PRO A 1 73  ? 34.449  18.541 72.550 1.00 10.22 ? 73  PRO A CG  1 
ATOM   509  C  CD  . PRO A 1 73  ? 35.340  18.858 71.376 1.00 10.11 ? 73  PRO A CD  1 
ATOM   510  N  N   . ALA A 1 74  ? 36.813  21.948 73.032 1.00 10.41 ? 74  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 74  ? 37.702  22.967 73.582 1.00 11.71 ? 74  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 74  ? 37.532  24.325 72.906 1.00 12.32 ? 74  ALA A C   1 
ATOM   513  O  O   . ALA A 1 74  ? 37.766  25.370 73.521 1.00 12.70 ? 74  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 74  ? 39.156  22.505 73.461 1.00 12.63 ? 74  ALA A CB  1 
ATOM   515  N  N   . ASP A 1 75  ? 37.117  24.310 71.644 1.00 12.07 ? 75  ASP A N   1 
ATOM   516  C  CA  . ASP A 1 75  ? 36.940  25.543 70.883 1.00 11.89 ? 75  ASP A CA  1 
ATOM   517  C  C   . ASP A 1 75  ? 35.849  26.468 71.414 1.00 11.90 ? 75  ASP A C   1 
ATOM   518  O  O   . ASP A 1 75  ? 35.849  27.658 71.109 1.00 13.41 ? 75  ASP A O   1 
ATOM   519  C  CB  . ASP A 1 75  ? 36.662  25.212 69.411 1.00 10.55 ? 75  ASP A CB  1 
ATOM   520  C  CG  . ASP A 1 75  ? 37.849  24.542 68.726 1.00 14.84 ? 75  ASP A CG  1 
ATOM   521  O  OD1 . ASP A 1 75  ? 39.002  24.966 68.970 1.00 14.01 ? 75  ASP A OD1 1 
ATOM   522  O  OD2 . ASP A 1 75  ? 37.631  23.592 67.943 1.00 13.30 ? 75  ASP A OD2 1 
ATOM   523  N  N   . TYR A 1 76  ? 34.929  25.937 72.214 1.00 11.71 ? 76  TYR A N   1 
ATOM   524  C  CA  . TYR A 1 76  ? 33.840  26.752 72.747 1.00 11.86 ? 76  TYR A CA  1 
ATOM   525  C  C   . TYR A 1 76  ? 34.129  27.399 74.097 1.00 13.11 ? 76  TYR A C   1 
ATOM   526  O  O   . TYR A 1 76  ? 33.261  28.055 74.674 1.00 13.06 ? 76  TYR A O   1 
ATOM   527  C  CB  . TYR A 1 76  ? 32.563  25.916 72.853 1.00 13.04 ? 76  TYR A CB  1 
ATOM   528  C  CG  . TYR A 1 76  ? 31.809  25.812 71.548 1.00 12.70 ? 76  TYR A CG  1 
ATOM   529  C  CD1 . TYR A 1 76  ? 32.106  24.804 70.631 1.00 12.10 ? 76  TYR A CD1 1 
ATOM   530  C  CD2 . TYR A 1 76  ? 30.818  26.739 71.215 1.00 12.18 ? 76  TYR A CD2 1 
ATOM   531  C  CE1 . TYR A 1 76  ? 31.439  24.724 69.409 1.00 13.25 ? 76  TYR A CE1 1 
ATOM   532  C  CE2 . TYR A 1 76  ? 30.144  26.668 69.994 1.00 12.09 ? 76  TYR A CE2 1 
ATOM   533  C  CZ  . TYR A 1 76  ? 30.462  25.659 69.098 1.00 11.63 ? 76  TYR A CZ  1 
ATOM   534  O  OH  . TYR A 1 76  ? 29.820  25.585 67.888 1.00 14.04 ? 76  TYR A OH  1 
ATOM   535  N  N   . THR A 1 77  ? 35.347  27.221 74.596 1.00 14.52 ? 77  THR A N   1 
ATOM   536  C  CA  . THR A 1 77  ? 35.734  27.791 75.884 1.00 15.41 ? 77  THR A CA  1 
ATOM   537  C  C   . THR A 1 77  ? 35.578  29.312 75.913 1.00 14.50 ? 77  THR A C   1 
ATOM   538  O  O   . THR A 1 77  ? 36.139  30.021 75.076 1.00 13.77 ? 77  THR A O   1 
ATOM   539  C  CB  . THR A 1 77  ? 37.198  27.437 76.228 1.00 16.50 ? 77  THR A CB  1 
ATOM   540  O  OG1 . THR A 1 77  ? 37.336  26.014 76.322 1.00 17.19 ? 77  THR A OG1 1 
ATOM   541  C  CG2 . THR A 1 77  ? 37.601  28.067 77.560 1.00 16.27 ? 77  THR A CG2 1 
ATOM   542  N  N   . GLY A 1 78  ? 34.814  29.801 76.886 1.00 15.78 ? 78  GLY A N   1 
ATOM   543  C  CA  . GLY A 1 78  ? 34.592  31.231 77.019 1.00 16.79 ? 78  GLY A CA  1 
ATOM   544  C  C   . GLY A 1 78  ? 33.629  31.830 76.006 1.00 17.76 ? 78  GLY A C   1 
ATOM   545  O  O   . GLY A 1 78  ? 33.366  33.031 76.033 1.00 19.22 ? 78  GLY A O   1 
ATOM   546  N  N   . ALA A 1 79  ? 33.089  31.000 75.121 1.00 17.04 ? 79  ALA A N   1 
ATOM   547  C  CA  . ALA A 1 79  ? 32.167  31.479 74.096 1.00 17.99 ? 79  ALA A CA  1 
ATOM   548  C  C   . ALA A 1 79  ? 30.915  32.158 74.649 1.00 18.52 ? 79  ALA A C   1 
ATOM   549  O  O   . ALA A 1 79  ? 30.477  33.183 74.122 1.00 18.24 ? 79  ALA A O   1 
ATOM   550  C  CB  . ALA A 1 79  ? 31.767  30.328 73.180 1.00 16.19 ? 79  ALA A CB  1 
ATOM   551  N  N   . ASN A 1 80  ? 30.338  31.591 75.704 1.00 18.37 ? 80  ASN A N   1 
ATOM   552  C  CA  . ASN A 1 80  ? 29.124  32.149 76.295 1.00 20.95 ? 80  ASN A CA  1 
ATOM   553  C  C   . ASN A 1 80  ? 29.311  33.515 76.951 1.00 22.60 ? 80  ASN A C   1 
ATOM   554  O  O   . ASN A 1 80  ? 28.465  34.400 76.813 1.00 22.68 ? 80  ASN A O   1 
ATOM   555  C  CB  . ASN A 1 80  ? 28.539  31.179 77.320 1.00 24.25 ? 80  ASN A CB  1 
ATOM   556  C  CG  . ASN A 1 80  ? 27.183  31.628 77.831 1.00 31.46 ? 80  ASN A CG  1 
ATOM   557  O  OD1 . ASN A 1 80  ? 27.071  32.183 78.927 1.00 32.45 ? 80  ASN A OD1 1 
ATOM   558  N  ND2 . ASN A 1 80  ? 26.141  31.396 77.034 1.00 31.55 ? 80  ASN A ND2 1 
ATOM   559  N  N   . ALA A 1 81  ? 30.414  33.683 77.669 1.00 26.01 ? 81  ALA A N   1 
ATOM   560  C  CA  . ALA A 1 81  ? 30.690  34.945 78.346 1.00 25.90 ? 81  ALA A CA  1 
ATOM   561  C  C   . ALA A 1 81  ? 31.058  36.056 77.367 1.00 25.60 ? 81  ALA A C   1 
ATOM   562  O  O   . ALA A 1 81  ? 30.756  37.226 77.599 1.00 28.06 ? 81  ALA A O   1 
ATOM   563  C  CB  . ALA A 1 81  ? 31.811  34.753 79.360 1.00 23.28 ? 81  ALA A CB  1 
ATOM   564  N  N   . ALA A 1 82  ? 31.704  35.689 76.268 1.00 21.62 ? 82  ALA A N   1 
ATOM   565  C  CA  . ALA A 1 82  ? 32.123  36.671 75.279 1.00 21.22 ? 82  ALA A CA  1 
ATOM   566  C  C   . ALA A 1 82  ? 31.049  37.065 74.268 1.00 22.01 ? 82  ALA A C   1 
ATOM   567  O  O   . ALA A 1 82  ? 30.825  38.253 74.027 1.00 22.24 ? 82  ALA A O   1 
ATOM   568  C  CB  . ALA A 1 82  ? 33.355  36.165 74.541 1.00 19.88 ? 82  ALA A CB  1 
ATOM   569  N  N   . LEU A 1 83  ? 30.383  36.073 73.682 1.00 20.69 ? 83  LEU A N   1 
ATOM   570  C  CA  . LEU A 1 83  ? 29.370  36.341 72.662 1.00 19.08 ? 83  LEU A CA  1 
ATOM   571  C  C   . LEU A 1 83  ? 27.930  36.022 73.041 1.00 17.75 ? 83  LEU A C   1 
ATOM   572  O  O   . LEU A 1 83  ? 27.024  36.199 72.227 1.00 17.40 ? 83  LEU A O   1 
ATOM   573  C  CB  . LEU A 1 83  ? 29.729  35.583 71.385 1.00 19.40 ? 83  LEU A CB  1 
ATOM   574  C  CG  . LEU A 1 83  ? 31.163  35.797 70.898 1.00 21.27 ? 83  LEU A CG  1 
ATOM   575  C  CD1 . LEU A 1 83  ? 31.713  34.508 70.314 1.00 22.63 ? 83  LEU A CD1 1 
ATOM   576  C  CD2 . LEU A 1 83  ? 31.177  36.903 69.860 1.00 23.12 ? 83  LEU A CD2 1 
ATOM   577  N  N   . LYS A 1 84  ? 27.718  35.554 74.264 1.00 16.91 ? 84  LYS A N   1 
ATOM   578  C  CA  . LYS A 1 84  ? 26.378  35.209 74.722 1.00 17.27 ? 84  LYS A CA  1 
ATOM   579  C  C   . LYS A 1 84  ? 25.733  34.186 73.791 1.00 17.33 ? 84  LYS A C   1 
ATOM   580  O  O   . LYS A 1 84  ? 24.558  34.304 73.424 1.00 15.65 ? 84  LYS A O   1 
ATOM   581  C  CB  . LYS A 1 84  ? 25.503  36.458 74.796 1.00 24.44 ? 84  LYS A CB  1 
ATOM   582  C  CG  . LYS A 1 84  ? 24.851  36.659 76.148 1.00 33.25 ? 84  LYS A CG  1 
ATOM   583  C  CD  . LYS A 1 84  ? 25.830  37.268 77.139 1.00 36.16 ? 84  LYS A CD  1 
ATOM   584  C  CE  . LYS A 1 84  ? 25.979  38.768 76.919 1.00 38.14 ? 84  LYS A CE  1 
ATOM   585  N  NZ  . LYS A 1 84  ? 24.843  39.346 76.141 1.00 38.59 ? 84  LYS A NZ  1 
ATOM   586  N  N   . VAL A 1 85  ? 26.516  33.186 73.403 1.00 14.71 ? 85  VAL A N   1 
ATOM   587  C  CA  . VAL A 1 85  ? 26.020  32.135 72.532 1.00 13.71 ? 85  VAL A CA  1 
ATOM   588  C  C   . VAL A 1 85  ? 25.988  30.801 73.273 1.00 14.05 ? 85  VAL A C   1 
ATOM   589  O  O   . VAL A 1 85  ? 26.706  30.605 74.258 1.00 14.54 ? 85  VAL A O   1 
ATOM   590  C  CB  . VAL A 1 85  ? 26.902  31.977 71.270 1.00 13.01 ? 85  VAL A CB  1 
ATOM   591  C  CG1 . VAL A 1 85  ? 26.801  33.219 70.415 1.00 11.18 ? 85  VAL A CG1 1 
ATOM   592  C  CG2 . VAL A 1 85  ? 28.343  31.704 71.665 1.00 13.41 ? 85  VAL A CG2 1 
ATOM   593  N  N   . ASP A 1 86  ? 25.133  29.901 72.797 1.00 12.52 ? 86  ASP A N   1 
ATOM   594  C  CA  . ASP A 1 86  ? 24.992  28.563 73.362 1.00 12.68 ? 86  ASP A CA  1 
ATOM   595  C  C   . ASP A 1 86  ? 25.521  27.602 72.308 1.00 12.17 ? 86  ASP A C   1 
ATOM   596  O  O   . ASP A 1 86  ? 25.811  28.002 71.179 1.00 12.19 ? 86  ASP A O   1 
ATOM   597  C  CB  . ASP A 1 86  ? 23.516  28.212 73.582 1.00 13.15 ? 86  ASP A CB  1 
ATOM   598  C  CG  . ASP A 1 86  ? 22.916  28.871 74.808 1.00 14.85 ? 86  ASP A CG  1 
ATOM   599  O  OD1 . ASP A 1 86  ? 23.676  29.324 75.690 1.00 16.36 ? 86  ASP A OD1 1 
ATOM   600  O  OD2 . ASP A 1 86  ? 21.668  28.926 74.884 1.00 12.14 ? 86  ASP A OD2 1 
ATOM   601  N  N   . ARG A 1 87  ? 25.656  26.336 72.680 1.00 12.41 ? 87  ARG A N   1 
ATOM   602  C  CA  . ARG A 1 87  ? 26.061  25.325 71.717 1.00 12.86 ? 87  ARG A CA  1 
ATOM   603  C  C   . ARG A 1 87  ? 24.695  24.896 71.176 1.00 12.59 ? 87  ARG A C   1 
ATOM   604  O  O   . ARG A 1 87  ? 24.031  24.035 71.754 1.00 13.61 ? 87  ARG A O   1 
ATOM   605  C  CB  . ARG A 1 87  ? 26.752  24.153 72.413 1.00 12.28 ? 87  ARG A CB  1 
ATOM   606  C  CG  . ARG A 1 87  ? 28.169  24.450 72.880 1.00 14.20 ? 87  ARG A CG  1 
ATOM   607  C  CD  . ARG A 1 87  ? 28.545  23.526 74.016 1.00 16.55 ? 87  ARG A CD  1 
ATOM   608  N  NE  . ARG A 1 87  ? 29.818  23.870 74.640 1.00 18.53 ? 87  ARG A NE  1 
ATOM   609  C  CZ  . ARG A 1 87  ? 29.938  24.632 75.723 1.00 19.63 ? 87  ARG A CZ  1 
ATOM   610  N  NH1 . ARG A 1 87  ? 28.860  25.137 76.308 1.00 16.86 ? 87  ARG A NH1 1 
ATOM   611  N  NH2 . ARG A 1 87  ? 31.138  24.868 76.237 1.00 19.00 ? 87  ARG A NH2 1 
ATOM   612  N  N   . GLY A 1 88  ? 24.266  25.527 70.086 1.00 10.76 ? 88  GLY A N   1 
ATOM   613  C  CA  . GLY A 1 88  ? 22.961  25.225 69.522 1.00 10.24 ? 88  GLY A CA  1 
ATOM   614  C  C   . GLY A 1 88  ? 22.875  24.097 68.515 1.00 9.04  ? 88  GLY A C   1 
ATOM   615  O  O   . GLY A 1 88  ? 23.603  24.076 67.521 1.00 10.75 ? 88  GLY A O   1 
ATOM   616  N  N   . HIS A 1 89  ? 21.966  23.162 68.772 1.00 9.43  ? 89  HIS A N   1 
ATOM   617  C  CA  . HIS A 1 89  ? 21.754  22.017 67.891 1.00 10.36 ? 89  HIS A CA  1 
ATOM   618  C  C   . HIS A 1 89  ? 21.072  22.467 66.602 1.00 10.32 ? 89  HIS A C   1 
ATOM   619  O  O   . HIS A 1 89  ? 20.243  23.383 66.618 1.00 10.22 ? 89  HIS A O   1 
ATOM   620  C  CB  . HIS A 1 89  ? 20.832  20.977 68.550 1.00 10.46 ? 89  HIS A CB  1 
ATOM   621  C  CG  . HIS A 1 89  ? 21.433  20.261 69.719 1.00 11.48 ? 89  HIS A CG  1 
ATOM   622  N  ND1 . HIS A 1 89  ? 21.371  20.752 71.006 1.00 13.31 ? 89  HIS A ND1 1 
ATOM   623  C  CD2 . HIS A 1 89  ? 22.057  19.061 69.805 1.00 12.06 ? 89  HIS A CD2 1 
ATOM   624  C  CE1 . HIS A 1 89  ? 21.930  19.887 71.834 1.00 12.05 ? 89  HIS A CE1 1 
ATOM   625  N  NE2 . HIS A 1 89  ? 22.355  18.853 71.131 1.00 12.26 ? 89  HIS A NE2 1 
ATOM   626  N  N   . GLN A 1 90  ? 21.428  21.831 65.490 1.00 8.12  ? 90  GLN A N   1 
ATOM   627  C  CA  . GLN A 1 90  ? 20.785  22.119 64.213 1.00 8.97  ? 90  GLN A CA  1 
ATOM   628  C  C   . GLN A 1 90  ? 19.663  21.074 64.190 1.00 9.30  ? 90  GLN A C   1 
ATOM   629  O  O   . GLN A 1 90  ? 18.488  21.424 64.201 1.00 10.55 ? 90  GLN A O   1 
ATOM   630  C  CB  . GLN A 1 90  ? 21.769  21.937 63.049 1.00 9.18  ? 90  GLN A CB  1 
ATOM   631  C  CG  . GLN A 1 90  ? 22.914  22.954 63.074 1.00 8.33  ? 90  GLN A CG  1 
ATOM   632  C  CD  . GLN A 1 90  ? 23.194  23.596 61.720 1.00 9.86  ? 90  GLN A CD  1 
ATOM   633  O  OE1 . GLN A 1 90  ? 24.348  23.699 61.299 1.00 12.00 ? 90  GLN A OE1 1 
ATOM   634  N  NE2 . GLN A 1 90  ? 22.143  24.035 61.039 1.00 6.21  ? 90  GLN A NE2 1 
ATOM   635  N  N   . ALA A 1 91  ? 20.023  19.791 64.176 1.00 8.98  ? 91  ALA A N   1 
ATOM   636  C  CA  . ALA A 1 91  ? 19.014  18.734 64.246 1.00 8.66  ? 91  ALA A CA  1 
ATOM   637  C  C   . ALA A 1 91  ? 18.747  18.671 65.751 1.00 9.77  ? 91  ALA A C   1 
ATOM   638  O  O   . ALA A 1 91  ? 19.677  18.489 66.538 1.00 11.08 ? 91  ALA A O   1 
ATOM   639  C  CB  . ALA A 1 91  ? 19.579  17.411 63.750 1.00 5.64  ? 91  ALA A CB  1 
ATOM   640  N  N   . PRO A 1 92  ? 17.479  18.820 66.170 1.00 11.35 ? 92  PRO A N   1 
ATOM   641  C  CA  . PRO A 1 92  ? 17.099  18.796 67.590 1.00 11.76 ? 92  PRO A CA  1 
ATOM   642  C  C   . PRO A 1 92  ? 17.267  17.474 68.339 1.00 12.70 ? 92  PRO A C   1 
ATOM   643  O  O   . PRO A 1 92  ? 16.827  16.418 67.881 1.00 13.99 ? 92  PRO A O   1 
ATOM   644  C  CB  . PRO A 1 92  ? 15.649  19.272 67.581 1.00 10.22 ? 92  PRO A CB  1 
ATOM   645  C  CG  . PRO A 1 92  ? 15.146  18.888 66.231 1.00 12.22 ? 92  PRO A CG  1 
ATOM   646  C  CD  . PRO A 1 92  ? 16.311  19.003 65.291 1.00 10.10 ? 92  PRO A CD  1 
ATOM   647  N  N   . LEU A 1 93  ? 17.892  17.556 69.510 1.00 10.46 ? 93  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 93  ? 18.145  16.385 70.346 1.00 11.44 ? 93  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 93  ? 16.891  15.625 70.783 1.00 11.63 ? 93  LEU A C   1 
ATOM   650  O  O   . LEU A 1 93  ? 16.765  14.430 70.528 1.00 11.92 ? 93  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 93  ? 18.947  16.798 71.587 1.00 10.81 ? 93  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 93  ? 19.361  15.686 72.560 1.00 10.42 ? 93  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 93  ? 20.197  14.642 71.840 1.00 9.56  ? 93  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 93  ? 20.146  16.292 73.710 1.00 11.00 ? 93  LEU A CD2 1 
ATOM   655  N  N   . ALA A 1 94  ? 15.962  16.317 71.433 1.00 13.90 ? 94  ALA A N   1 
ATOM   656  C  CA  . ALA A 1 94  ? 14.745  15.673 71.929 1.00 14.70 ? 94  ALA A CA  1 
ATOM   657  C  C   . ALA A 1 94  ? 13.845  15.038 70.865 1.00 15.25 ? 94  ALA A C   1 
ATOM   658  O  O   . ALA A 1 94  ? 13.170  14.042 71.133 1.00 16.06 ? 94  ALA A O   1 
ATOM   659  C  CB  . ALA A 1 94  ? 13.938  16.669 72.760 1.00 11.03 ? 94  ALA A CB  1 
ATOM   660  N  N   . SER A 1 95  ? 13.826  15.604 69.665 1.00 13.60 ? 95  SER A N   1 
ATOM   661  C  CA  . SER A 1 95  ? 12.976  15.071 68.602 1.00 12.45 ? 95  SER A CA  1 
ATOM   662  C  C   . SER A 1 95  ? 13.544  13.830 67.931 1.00 11.36 ? 95  SER A C   1 
ATOM   663  O  O   . SER A 1 95  ? 12.809  13.067 67.294 1.00 10.85 ? 95  SER A O   1 
ATOM   664  C  CB  . SER A 1 95  ? 12.733  16.141 67.538 1.00 8.52  ? 95  SER A CB  1 
ATOM   665  O  OG  . SER A 1 95  ? 12.302  17.350 68.132 1.00 12.56 ? 95  SER A OG  1 
ATOM   666  N  N   . LEU A 1 96  ? 14.846  13.614 68.083 1.00 10.04 ? 96  LEU A N   1 
ATOM   667  C  CA  . LEU A 1 96  ? 15.481  12.476 67.435 1.00 10.37 ? 96  LEU A CA  1 
ATOM   668  C  C   . LEU A 1 96  ? 16.309  11.552 68.326 1.00 11.28 ? 96  LEU A C   1 
ATOM   669  O  O   . LEU A 1 96  ? 16.811  10.536 67.847 1.00 10.56 ? 96  LEU A O   1 
ATOM   670  C  CB  . LEU A 1 96  ? 16.369  12.990 66.298 1.00 11.42 ? 96  LEU A CB  1 
ATOM   671  C  CG  . LEU A 1 96  ? 15.701  13.901 65.264 1.00 11.15 ? 96  LEU A CG  1 
ATOM   672  C  CD1 . LEU A 1 96  ? 16.701  14.926 64.753 1.00 10.33 ? 96  LEU A CD1 1 
ATOM   673  C  CD2 . LEU A 1 96  ? 15.158  13.049 64.120 1.00 10.67 ? 96  LEU A CD2 1 
ATOM   674  N  N   . ALA A 1 97  ? 16.446  11.887 69.607 1.00 12.38 ? 97  ALA A N   1 
ATOM   675  C  CA  . ALA A 1 97  ? 17.267  11.088 70.523 1.00 14.70 ? 97  ALA A CA  1 
ATOM   676  C  C   . ALA A 1 97  ? 16.900  9.606  70.653 1.00 16.19 ? 97  ALA A C   1 
ATOM   677  O  O   . ALA A 1 97  ? 17.575  8.863  71.363 1.00 16.80 ? 97  ALA A O   1 
ATOM   678  C  CB  . ALA A 1 97  ? 17.285  11.737 71.906 1.00 14.88 ? 97  ALA A CB  1 
ATOM   679  N  N   . GLY A 1 98  ? 15.844  9.179  69.967 1.00 14.75 ? 98  GLY A N   1 
ATOM   680  C  CA  . GLY A 1 98  ? 15.436  7.789  70.036 1.00 14.77 ? 98  GLY A CA  1 
ATOM   681  C  C   . GLY A 1 98  ? 16.094  6.906  68.990 1.00 15.62 ? 98  GLY A C   1 
ATOM   682  O  O   . GLY A 1 98  ? 15.908  5.691  68.998 1.00 17.00 ? 98  GLY A O   1 
ATOM   683  N  N   . VAL A 1 99  ? 16.862  7.501  68.083 1.00 14.12 ? 99  VAL A N   1 
ATOM   684  C  CA  . VAL A 1 99  ? 17.531  6.718  67.047 1.00 13.19 ? 99  VAL A CA  1 
ATOM   685  C  C   . VAL A 1 99  ? 18.767  6.013  67.611 1.00 13.93 ? 99  VAL A C   1 
ATOM   686  O  O   . VAL A 1 99  ? 19.313  6.420  68.639 1.00 13.41 ? 99  VAL A O   1 
ATOM   687  C  CB  . VAL A 1 99  ? 17.936  7.605  65.843 1.00 12.16 ? 99  VAL A CB  1 
ATOM   688  C  CG1 . VAL A 1 99  ? 16.700  8.297  65.281 1.00 12.34 ? 99  VAL A CG1 1 
ATOM   689  C  CG2 . VAL A 1 99  ? 18.980  8.631  66.266 1.00 10.11 ? 99  VAL A CG2 1 
ATOM   690  N  N   . SER A 1 100 ? 19.202  4.959  66.926 1.00 15.53 ? 100 SER A N   1 
ATOM   691  C  CA  . SER A 1 100 ? 20.345  4.163  67.358 1.00 16.62 ? 100 SER A CA  1 
ATOM   692  C  C   . SER A 1 100 ? 21.652  4.928  67.518 1.00 16.99 ? 100 SER A C   1 
ATOM   693  O  O   . SER A 1 100 ? 22.426  4.639  68.427 1.00 19.01 ? 100 SER A O   1 
ATOM   694  C  CB  . SER A 1 100 ? 20.553  2.982  66.404 1.00 17.72 ? 100 SER A CB  1 
ATOM   695  O  OG  . SER A 1 100 ? 20.582  3.404  65.051 1.00 22.72 ? 100 SER A OG  1 
ATOM   696  N  N   . ASP A 1 101 ? 21.915  5.892  66.642 1.00 14.76 ? 101 ASP A N   1 
ATOM   697  C  CA  . ASP A 1 101 ? 23.149  6.668  66.747 1.00 13.65 ? 101 ASP A CA  1 
ATOM   698  C  C   . ASP A 1 101 ? 22.875  8.065  67.295 1.00 13.60 ? 101 ASP A C   1 
ATOM   699  O  O   . ASP A 1 101 ? 23.521  9.031  66.893 1.00 12.75 ? 101 ASP A O   1 
ATOM   700  C  CB  . ASP A 1 101 ? 23.842  6.773  65.381 1.00 14.76 ? 101 ASP A CB  1 
ATOM   701  C  CG  . ASP A 1 101 ? 22.902  7.223  64.268 1.00 16.52 ? 101 ASP A CG  1 
ATOM   702  O  OD1 . ASP A 1 101 ? 21.838  7.808  64.564 1.00 15.82 ? 101 ASP A OD1 1 
ATOM   703  O  OD2 . ASP A 1 101 ? 23.236  6.988  63.086 1.00 14.97 ? 101 ASP A OD2 1 
ATOM   704  N  N   . TRP A 1 102 ? 21.927  8.155  68.227 1.00 13.70 ? 102 TRP A N   1 
ATOM   705  C  CA  . TRP A 1 102 ? 21.531  9.429  68.829 1.00 13.53 ? 102 TRP A CA  1 
ATOM   706  C  C   . TRP A 1 102 ? 22.682  10.277 69.367 1.00 13.53 ? 102 TRP A C   1 
ATOM   707  O  O   . TRP A 1 102 ? 22.587  11.505 69.397 1.00 13.37 ? 102 TRP A O   1 
ATOM   708  C  CB  . TRP A 1 102 ? 20.516  9.186  69.951 1.00 13.90 ? 102 TRP A CB  1 
ATOM   709  C  CG  . TRP A 1 102 ? 21.131  8.609  71.184 1.00 15.39 ? 102 TRP A CG  1 
ATOM   710  C  CD1 . TRP A 1 102 ? 21.313  7.286  71.468 1.00 16.34 ? 102 TRP A CD1 1 
ATOM   711  C  CD2 . TRP A 1 102 ? 21.685  9.338  72.287 1.00 15.95 ? 102 TRP A CD2 1 
ATOM   712  N  NE1 . TRP A 1 102 ? 21.949  7.145  72.679 1.00 16.81 ? 102 TRP A NE1 1 
ATOM   713  C  CE2 . TRP A 1 102 ? 22.189  8.389  73.203 1.00 17.36 ? 102 TRP A CE2 1 
ATOM   714  C  CE3 . TRP A 1 102 ? 21.805  10.702 72.589 1.00 16.20 ? 102 TRP A CE3 1 
ATOM   715  C  CZ2 . TRP A 1 102 ? 22.807  8.760  74.405 1.00 17.68 ? 102 TRP A CZ2 1 
ATOM   716  C  CZ3 . TRP A 1 102 ? 22.419  11.072 73.784 1.00 17.11 ? 102 TRP A CZ3 1 
ATOM   717  C  CH2 . TRP A 1 102 ? 22.912  10.102 74.676 1.00 17.08 ? 102 TRP A CH2 1 
ATOM   718  N  N   . GLU A 1 103 ? 23.764  9.635  69.796 1.00 11.24 ? 103 GLU A N   1 
ATOM   719  C  CA  . GLU A 1 103 ? 24.906  10.374 70.331 1.00 12.30 ? 103 GLU A CA  1 
ATOM   720  C  C   . GLU A 1 103 ? 25.467  11.382 69.334 1.00 10.39 ? 103 GLU A C   1 
ATOM   721  O  O   . GLU A 1 103 ? 26.000  12.421 69.730 1.00 9.82  ? 103 GLU A O   1 
ATOM   722  C  CB  . GLU A 1 103 ? 26.014  9.411  70.755 1.00 20.76 ? 103 GLU A CB  1 
ATOM   723  C  CG  . GLU A 1 103 ? 25.960  9.038  72.221 1.00 29.55 ? 103 GLU A CG  1 
ATOM   724  C  CD  . GLU A 1 103 ? 26.701  7.747  72.520 1.00 36.50 ? 103 GLU A CD  1 
ATOM   725  O  OE1 . GLU A 1 103 ? 26.098  6.658  72.372 1.00 37.38 ? 103 GLU A OE1 1 
ATOM   726  O  OE2 . GLU A 1 103 ? 27.888  7.824  72.903 1.00 38.37 ? 103 GLU A OE2 1 
ATOM   727  N  N   . SER A 1 104 ? 25.342  11.074 68.045 1.00 10.00 ? 104 SER A N   1 
ATOM   728  C  CA  . SER A 1 104 ? 25.837  11.951 66.986 1.00 8.54  ? 104 SER A CA  1 
ATOM   729  C  C   . SER A 1 104 ? 25.118  13.301 66.961 1.00 8.98  ? 104 SER A C   1 
ATOM   730  O  O   . SER A 1 104 ? 25.572  14.246 66.311 1.00 9.35  ? 104 SER A O   1 
ATOM   731  C  CB  . SER A 1 104 ? 25.686  11.267 65.628 1.00 8.30  ? 104 SER A CB  1 
ATOM   732  O  OG  . SER A 1 104 ? 24.331  11.243 65.215 1.00 9.90  ? 104 SER A OG  1 
ATOM   733  N  N   . LEU A 1 105 ? 23.993  13.394 67.664 1.00 7.96  ? 105 LEU A N   1 
ATOM   734  C  CA  . LEU A 1 105 ? 23.240  14.643 67.717 1.00 7.82  ? 105 LEU A CA  1 
ATOM   735  C  C   . LEU A 1 105 ? 24.030  15.669 68.515 1.00 8.39  ? 105 LEU A C   1 
ATOM   736  O  O   . LEU A 1 105 ? 23.801  16.879 68.402 1.00 9.02  ? 105 LEU A O   1 
ATOM   737  C  CB  . LEU A 1 105 ? 21.875  14.418 68.373 1.00 8.13  ? 105 LEU A CB  1 
ATOM   738  C  CG  . LEU A 1 105 ? 20.838  13.722 67.491 1.00 9.66  ? 105 LEU A CG  1 
ATOM   739  C  CD1 . LEU A 1 105 ? 19.742  13.113 68.360 1.00 9.82  ? 105 LEU A CD1 1 
ATOM   740  C  CD2 . LEU A 1 105 ? 20.261  14.728 66.500 1.00 9.41  ? 105 LEU A CD2 1 
ATOM   741  N  N   . ASN A 1 106 ? 24.968  15.179 69.321 1.00 9.53  ? 106 ASN A N   1 
ATOM   742  C  CA  . ASN A 1 106 ? 25.791  16.058 70.139 1.00 9.28  ? 106 ASN A CA  1 
ATOM   743  C  C   . ASN A 1 106 ? 27.208  16.208 69.592 1.00 10.06 ? 106 ASN A C   1 
ATOM   744  O  O   . ASN A 1 106 ? 28.098  16.715 70.279 1.00 10.11 ? 106 ASN A O   1 
ATOM   745  C  CB  . ASN A 1 106 ? 25.808  15.559 71.586 1.00 8.63  ? 106 ASN A CB  1 
ATOM   746  C  CG  . ASN A 1 106 ? 24.445  15.681 72.252 1.00 10.72 ? 106 ASN A CG  1 
ATOM   747  O  OD1 . ASN A 1 106 ? 23.776  16.705 72.132 1.00 11.69 ? 106 ASN A OD1 1 
ATOM   748  N  ND2 . ASN A 1 106 ? 24.025  14.631 72.947 1.00 11.29 ? 106 ASN A ND2 1 
ATOM   749  N  N   . TYR A 1 107 ? 27.417  15.750 68.358 1.00 9.64  ? 107 TYR A N   1 
ATOM   750  C  CA  . TYR A 1 107 ? 28.715  15.906 67.706 1.00 9.49  ? 107 TYR A CA  1 
ATOM   751  C  C   . TYR A 1 107 ? 28.709  17.371 67.281 1.00 10.51 ? 107 TYR A C   1 
ATOM   752  O  O   . TYR A 1 107 ? 27.672  17.881 66.846 1.00 9.69  ? 107 TYR A O   1 
ATOM   753  C  CB  . TYR A 1 107 ? 28.821  15.020 66.466 1.00 10.23 ? 107 TYR A CB  1 
ATOM   754  C  CG  . TYR A 1 107 ? 29.054  13.556 66.753 1.00 10.63 ? 107 TYR A CG  1 
ATOM   755  C  CD1 . TYR A 1 107 ? 29.315  13.107 68.048 1.00 10.19 ? 107 TYR A CD1 1 
ATOM   756  C  CD2 . TYR A 1 107 ? 28.997  12.616 65.728 1.00 11.22 ? 107 TYR A CD2 1 
ATOM   757  C  CE1 . TYR A 1 107 ? 29.508  11.755 68.314 1.00 12.38 ? 107 TYR A CE1 1 
ATOM   758  C  CE2 . TYR A 1 107 ? 29.188  11.262 65.982 1.00 13.16 ? 107 TYR A CE2 1 
ATOM   759  C  CZ  . TYR A 1 107 ? 29.441  10.838 67.275 1.00 13.56 ? 107 TYR A CZ  1 
ATOM   760  O  OH  . TYR A 1 107 ? 29.609  9.495  67.527 1.00 16.45 ? 107 TYR A OH  1 
ATOM   761  N  N   . LEU A 1 108 ? 29.850  18.044 67.395 1.00 10.37 ? 108 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 108 ? 29.925  19.462 67.056 1.00 11.13 ? 108 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 108 ? 29.621  19.821 65.606 1.00 10.30 ? 108 LEU A C   1 
ATOM   764  O  O   . LEU A 1 108 ? 29.449  20.991 65.282 1.00 12.58 ? 108 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 108 ? 31.289  20.024 67.462 1.00 10.93 ? 108 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 108 ? 31.318  20.744 68.814 1.00 12.95 ? 108 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 108 ? 30.232  20.214 69.734 1.00 13.26 ? 108 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 108 ? 32.677  20.550 69.447 1.00 15.55 ? 108 LEU A CD2 1 
ATOM   769  N  N   . SER A 1 109 ? 29.558  18.824 64.735 1.00 9.81  ? 109 SER A N   1 
ATOM   770  C  CA  . SER A 1 109 ? 29.236  19.070 63.334 1.00 10.03 ? 109 SER A CA  1 
ATOM   771  C  C   . SER A 1 109 ? 27.762  19.477 63.253 1.00 11.06 ? 109 SER A C   1 
ATOM   772  O  O   . SER A 1 109 ? 27.332  20.121 62.295 1.00 11.21 ? 109 SER A O   1 
ATOM   773  C  CB  . SER A 1 109 ? 29.456  17.800 62.514 1.00 9.52  ? 109 SER A CB  1 
ATOM   774  O  OG  . SER A 1 109 ? 28.912  16.675 63.184 1.00 9.47  ? 109 SER A OG  1 
ATOM   775  N  N   . ASN A 1 110 ? 26.997  19.091 64.272 1.00 10.85 ? 110 ASN A N   1 
ATOM   776  C  CA  . ASN A 1 110 ? 25.568  19.392 64.342 1.00 9.44  ? 110 ASN A CA  1 
ATOM   777  C  C   . ASN A 1 110 ? 25.316  20.572 65.278 1.00 9.93  ? 110 ASN A C   1 
ATOM   778  O  O   . ASN A 1 110 ? 24.184  20.822 65.688 1.00 11.42 ? 110 ASN A O   1 
ATOM   779  C  CB  . ASN A 1 110 ? 24.800  18.162 64.847 1.00 5.87  ? 110 ASN A CB  1 
ATOM   780  C  CG  . ASN A 1 110 ? 23.293  18.380 64.874 1.00 9.41  ? 110 ASN A CG  1 
ATOM   781  O  OD1 . ASN A 1 110 ? 22.709  18.845 63.898 1.00 7.08  ? 110 ASN A OD1 1 
ATOM   782  N  ND2 . ASN A 1 110 ? 22.658  18.046 65.997 1.00 6.54  ? 110 ASN A ND2 1 
ATOM   783  N  N   . ILE A 1 111 ? 26.377  21.298 65.606 1.00 10.27 ? 111 ILE A N   1 
ATOM   784  C  CA  . ILE A 1 111 ? 26.279  22.440 66.508 1.00 10.46 ? 111 ILE A CA  1 
ATOM   785  C  C   . ILE A 1 111 ? 26.900  23.700 65.905 1.00 10.21 ? 111 ILE A C   1 
ATOM   786  O  O   . ILE A 1 111 ? 27.783  23.621 65.051 1.00 10.48 ? 111 ILE A O   1 
ATOM   787  C  CB  . ILE A 1 111 ? 27.011  22.132 67.844 1.00 11.02 ? 111 ILE A CB  1 
ATOM   788  C  CG1 . ILE A 1 111 ? 26.410  20.879 68.492 1.00 11.86 ? 111 ILE A CG1 1 
ATOM   789  C  CG2 . ILE A 1 111 ? 26.956  23.338 68.777 1.00 11.47 ? 111 ILE A CG2 1 
ATOM   790  C  CD1 . ILE A 1 111 ? 24.990  21.042 68.963 1.00 12.85 ? 111 ILE A CD1 1 
ATOM   791  N  N   . THR A 1 112 ? 26.415  24.860 66.343 1.00 9.07  ? 112 THR A N   1 
ATOM   792  C  CA  . THR A 1 112 ? 26.950  26.152 65.912 1.00 8.92  ? 112 THR A CA  1 
ATOM   793  C  C   . THR A 1 112 ? 26.758  27.119 67.079 1.00 9.36  ? 112 THR A C   1 
ATOM   794  O  O   . THR A 1 112 ? 25.919  26.885 67.950 1.00 9.48  ? 112 THR A O   1 
ATOM   795  C  CB  . THR A 1 112 ? 26.202  26.756 64.692 1.00 8.85  ? 112 THR A CB  1 
ATOM   796  O  OG1 . THR A 1 112 ? 24.973  27.343 65.137 1.00 10.09 ? 112 THR A OG1 1 
ATOM   797  C  CG2 . THR A 1 112 ? 25.917  25.703 63.640 1.00 9.32  ? 112 THR A CG2 1 
ATOM   798  N  N   . PRO A 1 113 ? 27.561  28.194 67.131 1.00 9.21  ? 113 PRO A N   1 
ATOM   799  C  CA  . PRO A 1 113 ? 27.432  29.179 68.211 1.00 9.24  ? 113 PRO A CA  1 
ATOM   800  C  C   . PRO A 1 113 ? 26.163  29.996 67.955 1.00 10.54 ? 113 PRO A C   1 
ATOM   801  O  O   . PRO A 1 113 ? 26.177  30.969 67.196 1.00 9.63  ? 113 PRO A O   1 
ATOM   802  C  CB  . PRO A 1 113 ? 28.704  30.028 68.092 1.00 10.26 ? 113 PRO A CB  1 
ATOM   803  C  CG  . PRO A 1 113 ? 29.590  29.303 67.094 1.00 10.31 ? 113 PRO A CG  1 
ATOM   804  C  CD  . PRO A 1 113 ? 28.663  28.528 66.215 1.00 8.98  ? 113 PRO A CD  1 
ATOM   805  N  N   . GLN A 1 114 ? 25.070  29.579 68.586 1.00 10.58 ? 114 GLN A N   1 
ATOM   806  C  CA  . GLN A 1 114 ? 23.769  30.220 68.429 1.00 10.08 ? 114 GLN A CA  1 
ATOM   807  C  C   . GLN A 1 114 ? 23.418  31.092 69.638 1.00 10.85 ? 114 GLN A C   1 
ATOM   808  O  O   . GLN A 1 114 ? 23.467  30.624 70.774 1.00 10.81 ? 114 GLN A O   1 
ATOM   809  C  CB  . GLN A 1 114 ? 22.711  29.130 68.244 1.00 9.52  ? 114 GLN A CB  1 
ATOM   810  C  CG  . GLN A 1 114 ? 21.379  29.600 67.699 1.00 10.49 ? 114 GLN A CG  1 
ATOM   811  C  CD  . GLN A 1 114 ? 20.425  28.445 67.475 1.00 10.77 ? 114 GLN A CD  1 
ATOM   812  O  OE1 . GLN A 1 114 ? 19.850  28.298 66.398 1.00 13.43 ? 114 GLN A OE1 1 
ATOM   813  N  NE2 . GLN A 1 114 ? 20.258  27.614 68.493 1.00 8.40  ? 114 GLN A NE2 1 
ATOM   814  N  N   . LYS A 1 115 ? 23.066  32.353 69.393 1.00 11.93 ? 115 LYS A N   1 
ATOM   815  C  CA  . LYS A 1 115 ? 22.707  33.271 70.478 1.00 13.10 ? 115 LYS A CA  1 
ATOM   816  C  C   . LYS A 1 115 ? 21.737  32.599 71.439 1.00 14.28 ? 115 LYS A C   1 
ATOM   817  O  O   . LYS A 1 115 ? 20.735  32.017 71.016 1.00 15.44 ? 115 LYS A O   1 
ATOM   818  C  CB  . LYS A 1 115 ? 22.071  34.542 69.917 1.00 11.06 ? 115 LYS A CB  1 
ATOM   819  C  CG  . LYS A 1 115 ? 23.069  35.510 69.305 1.00 15.14 ? 115 LYS A CG  1 
ATOM   820  C  CD  . LYS A 1 115 ? 24.004  36.099 70.355 1.00 15.17 ? 115 LYS A CD  1 
ATOM   821  C  CE  . LYS A 1 115 ? 24.629  37.401 69.862 1.00 20.66 ? 115 LYS A CE  1 
ATOM   822  N  NZ  . LYS A 1 115 ? 26.116  37.415 69.994 1.00 22.42 ? 115 LYS A NZ  1 
ATOM   823  N  N   . SER A 1 116 ? 22.038  32.681 72.731 1.00 12.63 ? 116 SER A N   1 
ATOM   824  C  CA  . SER A 1 116 ? 21.205  32.060 73.760 1.00 13.81 ? 116 SER A CA  1 
ATOM   825  C  C   . SER A 1 116 ? 19.735  32.446 73.692 1.00 12.49 ? 116 SER A C   1 
ATOM   826  O  O   . SER A 1 116 ? 18.862  31.610 73.912 1.00 12.84 ? 116 SER A O   1 
ATOM   827  C  CB  . SER A 1 116 ? 21.741  32.400 75.149 1.00 14.92 ? 116 SER A CB  1 
ATOM   828  O  OG  . SER A 1 116 ? 23.137  32.174 75.208 1.00 21.88 ? 116 SER A OG  1 
ATOM   829  N  N   . ASP A 1 117 ? 19.463  33.711 73.395 1.00 12.61 ? 117 ASP A N   1 
ATOM   830  C  CA  . ASP A 1 117 ? 18.086  34.183 73.325 1.00 14.05 ? 117 ASP A CA  1 
ATOM   831  C  C   . ASP A 1 117 ? 17.313  33.549 72.176 1.00 13.82 ? 117 ASP A C   1 
ATOM   832  O  O   . ASP A 1 117 ? 16.092  33.407 72.246 1.00 14.87 ? 117 ASP A O   1 
ATOM   833  C  CB  . ASP A 1 117 ? 18.058  35.706 73.213 1.00 16.57 ? 117 ASP A CB  1 
ATOM   834  C  CG  . ASP A 1 117 ? 18.345  36.385 74.540 1.00 19.81 ? 117 ASP A CG  1 
ATOM   835  O  OD1 . ASP A 1 117 ? 18.378  35.681 75.571 1.00 19.47 ? 117 ASP A OD1 1 
ATOM   836  O  OD2 . ASP A 1 117 ? 18.538  37.617 74.554 1.00 23.66 ? 117 ASP A OD2 1 
ATOM   837  N  N   . LEU A 1 118 ? 18.021  33.171 71.118 1.00 11.80 ? 118 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 118 ? 17.370  32.527 69.985 1.00 11.70 ? 118 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 118 ? 17.218  31.040 70.302 1.00 11.41 ? 118 LEU A C   1 
ATOM   840  O  O   . LEU A 1 118 ? 16.125  30.483 70.193 1.00 11.69 ? 118 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 118 ? 18.196  32.709 68.707 1.00 10.52 ? 118 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 118 ? 17.729  31.859 67.520 1.00 10.19 ? 118 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 118 ? 16.295  32.230 67.167 1.00 9.38  ? 118 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 118 ? 18.654  32.069 66.331 1.00 9.85  ? 118 LEU A CD2 1 
ATOM   845  N  N   . ASN A 1 119 ? 18.319  30.413 70.713 1.00 10.55 ? 119 ASN A N   1 
ATOM   846  C  CA  . ASN A 1 119 ? 18.339  28.989 71.057 1.00 12.71 ? 119 ASN A CA  1 
ATOM   847  C  C   . ASN A 1 119 ? 17.263  28.609 72.072 1.00 14.29 ? 119 ASN A C   1 
ATOM   848  O  O   . ASN A 1 119 ? 16.551  27.616 71.900 1.00 14.92 ? 119 ASN A O   1 
ATOM   849  C  CB  . ASN A 1 119 ? 19.715  28.604 71.615 1.00 12.30 ? 119 ASN A CB  1 
ATOM   850  C  CG  . ASN A 1 119 ? 19.784  27.154 72.049 1.00 14.95 ? 119 ASN A CG  1 
ATOM   851  O  OD1 . ASN A 1 119 ? 19.261  26.272 71.376 1.00 17.75 ? 119 ASN A OD1 1 
ATOM   852  N  ND2 . ASN A 1 119 ? 20.434  26.900 73.177 1.00 15.80 ? 119 ASN A ND2 1 
ATOM   853  N  N   . GLN A 1 120 ? 17.150  29.403 73.132 1.00 15.99 ? 120 GLN A N   1 
ATOM   854  C  CA  . GLN A 1 120 ? 16.174  29.146 74.186 1.00 17.05 ? 120 GLN A CA  1 
ATOM   855  C  C   . GLN A 1 120 ? 14.862  29.895 73.973 1.00 16.69 ? 120 GLN A C   1 
ATOM   856  O  O   . GLN A 1 120 ? 13.954  29.807 74.797 1.00 18.27 ? 120 GLN A O   1 
ATOM   857  C  CB  . GLN A 1 120 ? 16.769  29.529 75.544 1.00 18.01 ? 120 GLN A CB  1 
ATOM   858  C  CG  . GLN A 1 120 ? 17.928  28.641 75.970 1.00 20.87 ? 120 GLN A CG  1 
ATOM   859  C  CD  . GLN A 1 120 ? 18.810  29.296 77.010 1.00 26.89 ? 120 GLN A CD  1 
ATOM   860  O  OE1 . GLN A 1 120 ? 18.358  30.149 77.773 1.00 30.73 ? 120 GLN A OE1 1 
ATOM   861  N  NE2 . GLN A 1 120 ? 20.080  28.903 77.046 1.00 31.14 ? 120 GLN A NE2 1 
ATOM   862  N  N   . GLY A 1 121 ? 14.765  30.619 72.862 1.00 13.48 ? 121 GLY A N   1 
ATOM   863  C  CA  . GLY A 1 121 ? 13.560  31.377 72.574 1.00 12.70 ? 121 GLY A CA  1 
ATOM   864  C  C   . GLY A 1 121 ? 12.711  30.840 71.433 1.00 10.81 ? 121 GLY A C   1 
ATOM   865  O  O   . GLY A 1 121 ? 12.245  29.701 71.469 1.00 11.50 ? 121 GLY A O   1 
ATOM   866  N  N   . ALA A 1 122 ? 12.513  31.670 70.415 1.00 11.67 ? 122 ALA A N   1 
ATOM   867  C  CA  . ALA A 1 122 ? 11.700  31.311 69.257 1.00 11.18 ? 122 ALA A CA  1 
ATOM   868  C  C   . ALA A 1 122 ? 12.132  30.003 68.593 1.00 11.65 ? 122 ALA A C   1 
ATOM   869  O  O   . ALA A 1 122 ? 11.293  29.237 68.113 1.00 12.47 ? 122 ALA A O   1 
ATOM   870  C  CB  . ALA A 1 122 ? 11.729  32.446 68.242 1.00 10.17 ? 122 ALA A CB  1 
ATOM   871  N  N   . TRP A 1 123 ? 13.437  29.747 68.563 1.00 11.27 ? 123 TRP A N   1 
ATOM   872  C  CA  . TRP A 1 123 ? 13.954  28.525 67.954 1.00 10.97 ? 123 TRP A CA  1 
ATOM   873  C  C   . TRP A 1 123 ? 13.495  27.282 68.715 1.00 11.39 ? 123 TRP A C   1 
ATOM   874  O  O   . TRP A 1 123 ? 13.151  26.270 68.106 1.00 12.06 ? 123 TRP A O   1 
ATOM   875  C  CB  . TRP A 1 123 ? 15.485  28.558 67.897 1.00 8.27  ? 123 TRP A CB  1 
ATOM   876  C  CG  . TRP A 1 123 ? 16.072  27.477 67.031 1.00 9.24  ? 123 TRP A CG  1 
ATOM   877  C  CD1 . TRP A 1 123 ? 16.648  26.313 67.451 1.00 8.66  ? 123 TRP A CD1 1 
ATOM   878  C  CD2 . TRP A 1 123 ? 16.127  27.453 65.595 1.00 9.54  ? 123 TRP A CD2 1 
ATOM   879  N  NE1 . TRP A 1 123 ? 17.056  25.568 66.372 1.00 10.09 ? 123 TRP A NE1 1 
ATOM   880  C  CE2 . TRP A 1 123 ? 16.748  26.244 65.221 1.00 9.67  ? 123 TRP A CE2 1 
ATOM   881  C  CE3 . TRP A 1 123 ? 15.709  28.337 64.591 1.00 9.70  ? 123 TRP A CE3 1 
ATOM   882  C  CZ2 . TRP A 1 123 ? 16.964  25.894 63.882 1.00 9.67  ? 123 TRP A CZ2 1 
ATOM   883  C  CZ3 . TRP A 1 123 ? 15.924  27.987 63.259 1.00 8.84  ? 123 TRP A CZ3 1 
ATOM   884  C  CH2 . TRP A 1 123 ? 16.545  26.777 62.920 1.00 8.65  ? 123 TRP A CH2 1 
ATOM   885  N  N   . ALA A 1 124 ? 13.492  27.356 70.042 1.00 10.26 ? 124 ALA A N   1 
ATOM   886  C  CA  . ALA A 1 124 ? 13.065  26.224 70.861 1.00 10.83 ? 124 ALA A CA  1 
ATOM   887  C  C   . ALA A 1 124 ? 11.554  26.012 70.760 1.00 12.09 ? 124 ALA A C   1 
ATOM   888  O  O   . ALA A 1 124 ? 11.071  24.877 70.781 1.00 12.44 ? 124 ALA A O   1 
ATOM   889  C  CB  . ALA A 1 124 ? 13.462  26.447 72.318 1.00 9.90  ? 124 ALA A CB  1 
ATOM   890  N  N   . ARG A 1 125 ? 10.805  27.104 70.653 1.00 11.29 ? 125 ARG A N   1 
ATOM   891  C  CA  . ARG A 1 125 ? 9.360   26.992 70.546 1.00 11.95 ? 125 ARG A CA  1 
ATOM   892  C  C   . ARG A 1 125 ? 8.961   26.390 69.198 1.00 11.45 ? 125 ARG A C   1 
ATOM   893  O  O   . ARG A 1 125 ? 7.963   25.680 69.105 1.00 11.94 ? 125 ARG A O   1 
ATOM   894  C  CB  . ARG A 1 125 ? 8.709   28.361 70.766 1.00 13.61 ? 125 ARG A CB  1 
ATOM   895  C  CG  . ARG A 1 125 ? 8.755   28.788 72.234 1.00 19.61 ? 125 ARG A CG  1 
ATOM   896  C  CD  . ARG A 1 125 ? 7.955   30.046 72.496 1.00 26.07 ? 125 ARG A CD  1 
ATOM   897  N  NE  . ARG A 1 125 ? 8.663   31.254 72.074 1.00 30.92 ? 125 ARG A NE  1 
ATOM   898  C  CZ  . ARG A 1 125 ? 9.484   31.957 72.850 1.00 30.86 ? 125 ARG A CZ  1 
ATOM   899  N  NH1 . ARG A 1 125 ? 9.709   31.574 74.102 1.00 31.08 ? 125 ARG A NH1 1 
ATOM   900  N  NH2 . ARG A 1 125 ? 10.076  33.047 72.376 1.00 24.98 ? 125 ARG A NH2 1 
ATOM   901  N  N   . LEU A 1 126 ? 9.745   26.656 68.155 1.00 10.49 ? 126 LEU A N   1 
ATOM   902  C  CA  . LEU A 1 126 ? 9.448   26.086 66.843 1.00 10.33 ? 126 LEU A CA  1 
ATOM   903  C  C   . LEU A 1 126 ? 9.740   24.589 66.913 1.00 10.61 ? 126 LEU A C   1 
ATOM   904  O  O   . LEU A 1 126 ? 8.953   23.768 66.439 1.00 11.57 ? 126 LEU A O   1 
ATOM   905  C  CB  . LEU A 1 126 ? 10.304  26.743 65.749 1.00 9.08  ? 126 LEU A CB  1 
ATOM   906  C  CG  . LEU A 1 126 ? 10.286  26.099 64.353 1.00 9.05  ? 126 LEU A CG  1 
ATOM   907  C  CD1 . LEU A 1 126 ? 8.858   25.826 63.900 1.00 6.91  ? 126 LEU A CD1 1 
ATOM   908  C  CD2 . LEU A 1 126 ? 10.983  27.019 63.366 1.00 9.50  ? 126 LEU A CD2 1 
ATOM   909  N  N   . GLU A 1 127 ? 10.869  24.236 67.523 1.00 9.07  ? 127 GLU A N   1 
ATOM   910  C  CA  . GLU A 1 127 ? 11.248  22.835 67.669 1.00 8.71  ? 127 GLU A CA  1 
ATOM   911  C  C   . GLU A 1 127 ? 10.144  22.085 68.409 1.00 9.45  ? 127 GLU A C   1 
ATOM   912  O  O   . GLU A 1 127 ? 9.818   20.941 68.081 1.00 8.95  ? 127 GLU A O   1 
ATOM   913  C  CB  . GLU A 1 127 ? 12.551  22.717 68.461 1.00 9.17  ? 127 GLU A CB  1 
ATOM   914  C  CG  . GLU A 1 127 ? 13.801  22.972 67.645 1.00 10.23 ? 127 GLU A CG  1 
ATOM   915  C  CD  . GLU A 1 127 ? 15.038  23.089 68.507 1.00 13.24 ? 127 GLU A CD  1 
ATOM   916  O  OE1 . GLU A 1 127 ? 14.908  23.486 69.682 1.00 15.10 ? 127 GLU A OE1 1 
ATOM   917  O  OE2 . GLU A 1 127 ? 16.142  22.787 68.010 1.00 13.59 ? 127 GLU A OE2 1 
ATOM   918  N  N   . ASP A 1 128 ? 9.577   22.738 69.416 1.00 9.93  ? 128 ASP A N   1 
ATOM   919  C  CA  . ASP A 1 128 ? 8.515   22.139 70.211 1.00 11.81 ? 128 ASP A CA  1 
ATOM   920  C  C   . ASP A 1 128 ? 7.271   21.852 69.366 1.00 10.77 ? 128 ASP A C   1 
ATOM   921  O  O   . ASP A 1 128 ? 6.678   20.777 69.464 1.00 11.07 ? 128 ASP A O   1 
ATOM   922  C  CB  . ASP A 1 128 ? 8.157   23.062 71.380 1.00 22.27 ? 128 ASP A CB  1 
ATOM   923  C  CG  . ASP A 1 128 ? 6.983   22.549 72.184 1.00 30.85 ? 128 ASP A CG  1 
ATOM   924  O  OD1 . ASP A 1 128 ? 7.040   21.384 72.634 1.00 36.34 ? 128 ASP A OD1 1 
ATOM   925  O  OD2 . ASP A 1 128 ? 6.003   23.305 72.363 1.00 36.51 ? 128 ASP A OD2 1 
ATOM   926  N  N   . GLN A 1 129 ? 6.881   22.808 68.529 1.00 11.40 ? 129 GLN A N   1 
ATOM   927  C  CA  . GLN A 1 129 ? 5.709   22.632 67.676 1.00 11.96 ? 129 GLN A CA  1 
ATOM   928  C  C   . GLN A 1 129 ? 6.004   21.639 66.559 1.00 12.48 ? 129 GLN A C   1 
ATOM   929  O  O   . GLN A 1 129 ? 5.132   20.882 66.138 1.00 12.19 ? 129 GLN A O   1 
ATOM   930  C  CB  . GLN A 1 129 ? 5.280   23.973 67.079 1.00 12.72 ? 129 GLN A CB  1 
ATOM   931  C  CG  . GLN A 1 129 ? 4.575   24.889 68.065 1.00 15.10 ? 129 GLN A CG  1 
ATOM   932  C  CD  . GLN A 1 129 ? 3.489   24.175 68.846 1.00 17.92 ? 129 GLN A CD  1 
ATOM   933  O  OE1 . GLN A 1 129 ? 2.727   23.384 68.290 1.00 18.30 ? 129 GLN A OE1 1 
ATOM   934  N  NE2 . GLN A 1 129 ? 3.416   24.449 70.142 1.00 19.94 ? 129 GLN A NE2 1 
ATOM   935  N  N   . GLU A 1 130 ? 7.244   21.651 66.083 1.00 11.24 ? 130 GLU A N   1 
ATOM   936  C  CA  . GLU A 1 130 ? 7.674   20.750 65.021 1.00 10.91 ? 130 GLU A CA  1 
ATOM   937  C  C   . GLU A 1 130 ? 7.559   19.312 65.527 1.00 11.87 ? 130 GLU A C   1 
ATOM   938  O  O   . GLU A 1 130 ? 7.058   18.429 64.830 1.00 11.82 ? 130 GLU A O   1 
ATOM   939  C  CB  . GLU A 1 130 ? 9.122   21.083 64.638 1.00 11.55 ? 130 GLU A CB  1 
ATOM   940  C  CG  . GLU A 1 130 ? 9.818   20.085 63.730 1.00 11.84 ? 130 GLU A CG  1 
ATOM   941  C  CD  . GLU A 1 130 ? 11.286  20.430 63.526 1.00 12.27 ? 130 GLU A CD  1 
ATOM   942  O  OE1 . GLU A 1 130 ? 11.877  21.082 64.416 1.00 10.77 ? 130 GLU A OE1 1 
ATOM   943  O  OE2 . GLU A 1 130 ? 11.850  20.051 62.479 1.00 10.51 ? 130 GLU A OE2 1 
ATOM   944  N  N   . ARG A 1 131 ? 8.011   19.091 66.757 1.00 13.84 ? 131 ARG A N   1 
ATOM   945  C  CA  . ARG A 1 131 ? 7.961   17.774 67.377 1.00 15.53 ? 131 ARG A CA  1 
ATOM   946  C  C   . ARG A 1 131 ? 6.518   17.353 67.654 1.00 16.17 ? 131 ARG A C   1 
ATOM   947  O  O   . ARG A 1 131 ? 6.166   16.183 67.501 1.00 17.60 ? 131 ARG A O   1 
ATOM   948  C  CB  . ARG A 1 131 ? 8.758   17.788 68.685 1.00 22.80 ? 131 ARG A CB  1 
ATOM   949  C  CG  . ARG A 1 131 ? 8.758   16.469 69.445 1.00 28.45 ? 131 ARG A CG  1 
ATOM   950  C  CD  . ARG A 1 131 ? 9.768   16.489 70.586 1.00 34.04 ? 131 ARG A CD  1 
ATOM   951  N  NE  . ARG A 1 131 ? 9.792   17.773 71.287 1.00 36.85 ? 131 ARG A NE  1 
ATOM   952  C  CZ  . ARG A 1 131 ? 10.796  18.649 71.227 1.00 38.13 ? 131 ARG A CZ  1 
ATOM   953  N  NH1 . ARG A 1 131 ? 11.876  18.389 70.496 1.00 37.43 ? 131 ARG A NH1 1 
ATOM   954  N  NH2 . ARG A 1 131 ? 10.722  19.792 71.901 1.00 37.51 ? 131 ARG A NH2 1 
ATOM   955  N  N   . LYS A 1 132 ? 5.689   18.313 68.052 1.00 14.93 ? 132 LYS A N   1 
ATOM   956  C  CA  . LYS A 1 132 ? 4.285   18.052 68.363 1.00 15.10 ? 132 LYS A CA  1 
ATOM   957  C  C   . LYS A 1 132 ? 3.478   17.573 67.160 1.00 15.19 ? 132 LYS A C   1 
ATOM   958  O  O   . LYS A 1 132 ? 2.470   16.890 67.322 1.00 15.05 ? 132 LYS A O   1 
ATOM   959  C  CB  . LYS A 1 132 ? 3.629   19.311 68.927 1.00 18.29 ? 132 LYS A CB  1 
ATOM   960  C  CG  . LYS A 1 132 ? 3.663   19.411 70.441 1.00 26.88 ? 132 LYS A CG  1 
ATOM   961  C  CD  . LYS A 1 132 ? 3.057   20.729 70.910 1.00 32.61 ? 132 LYS A CD  1 
ATOM   962  C  CE  . LYS A 1 132 ? 3.145   20.887 72.423 1.00 34.28 ? 132 LYS A CE  1 
ATOM   963  N  NZ  . LYS A 1 132 ? 4.507   20.568 72.937 1.00 35.82 ? 132 LYS A NZ  1 
ATOM   964  N  N   . LEU A 1 133 ? 3.910   17.936 65.955 1.00 14.30 ? 133 LEU A N   1 
ATOM   965  C  CA  . LEU A 1 133 ? 3.198   17.525 64.746 1.00 13.41 ? 133 LEU A CA  1 
ATOM   966  C  C   . LEU A 1 133 ? 3.103   16.012 64.653 1.00 13.41 ? 133 LEU A C   1 
ATOM   967  O  O   . LEU A 1 133 ? 2.087   15.471 64.219 1.00 12.89 ? 133 LEU A O   1 
ATOM   968  C  CB  . LEU A 1 133 ? 3.911   18.041 63.495 1.00 12.60 ? 133 LEU A CB  1 
ATOM   969  C  CG  . LEU A 1 133 ? 3.786   19.523 63.148 1.00 13.57 ? 133 LEU A CG  1 
ATOM   970  C  CD1 . LEU A 1 133 ? 4.709   19.838 61.974 1.00 12.46 ? 133 LEU A CD1 1 
ATOM   971  C  CD2 . LEU A 1 133 ? 2.343   19.858 62.807 1.00 12.22 ? 133 LEU A CD2 1 
ATOM   972  N  N   . ILE A 1 134 ? 4.169   15.331 65.065 1.00 14.40 ? 134 ILE A N   1 
ATOM   973  C  CA  . ILE A 1 134 ? 4.212   13.878 64.993 1.00 16.11 ? 134 ILE A CA  1 
ATOM   974  C  C   . ILE A 1 134 ? 3.217   13.196 65.919 1.00 17.78 ? 134 ILE A C   1 
ATOM   975  O  O   . ILE A 1 134 ? 2.961   12.003 65.783 1.00 17.62 ? 134 ILE A O   1 
ATOM   976  C  CB  . ILE A 1 134 ? 5.640   13.346 65.279 1.00 16.71 ? 134 ILE A CB  1 
ATOM   977  C  CG1 . ILE A 1 134 ? 5.859   12.030 64.530 1.00 15.76 ? 134 ILE A CG1 1 
ATOM   978  C  CG2 . ILE A 1 134 ? 5.850   13.152 66.774 1.00 17.99 ? 134 ILE A CG2 1 
ATOM   979  C  CD1 . ILE A 1 134 ? 5.706   12.147 63.027 1.00 15.15 ? 134 ILE A CD1 1 
ATOM   980  N  N   . ASP A 1 135 ? 2.653   13.953 66.855 1.00 19.45 ? 135 ASP A N   1 
ATOM   981  C  CA  . ASP A 1 135 ? 1.674   13.401 67.783 1.00 20.91 ? 135 ASP A CA  1 
ATOM   982  C  C   . ASP A 1 135 ? 0.308   13.266 67.112 1.00 21.33 ? 135 ASP A C   1 
ATOM   983  O  O   . ASP A 1 135 ? -0.557  12.541 67.598 1.00 22.27 ? 135 ASP A O   1 
ATOM   984  C  CB  . ASP A 1 135 ? 1.553   14.288 69.024 1.00 23.51 ? 135 ASP A CB  1 
ATOM   985  C  CG  . ASP A 1 135 ? 2.704   14.093 69.991 1.00 27.28 ? 135 ASP A CG  1 
ATOM   986  O  OD1 . ASP A 1 135 ? 3.421   13.079 69.865 1.00 30.68 ? 135 ASP A OD1 1 
ATOM   987  O  OD2 . ASP A 1 135 ? 2.893   14.955 70.876 1.00 31.90 ? 135 ASP A OD2 1 
ATOM   988  N  N   . ARG A 1 136 ? 0.115   13.966 65.997 1.00 19.91 ? 136 ARG A N   1 
ATOM   989  C  CA  . ARG A 1 136 ? -1.152  13.899 65.273 1.00 19.24 ? 136 ARG A CA  1 
ATOM   990  C  C   . ARG A 1 136 ? -1.304  12.519 64.648 1.00 19.76 ? 136 ARG A C   1 
ATOM   991  O  O   . ARG A 1 136 ? -0.348  11.960 64.107 1.00 18.98 ? 136 ARG A O   1 
ATOM   992  C  CB  . ARG A 1 136 ? -1.206  14.973 64.186 1.00 21.05 ? 136 ARG A CB  1 
ATOM   993  C  CG  . ARG A 1 136 ? -1.475  16.365 64.716 1.00 21.92 ? 136 ARG A CG  1 
ATOM   994  C  CD  . ARG A 1 136 ? -1.862  17.315 63.604 1.00 24.47 ? 136 ARG A CD  1 
ATOM   995  N  NE  . ARG A 1 136 ? -1.978  18.688 64.089 1.00 31.83 ? 136 ARG A NE  1 
ATOM   996  C  CZ  . ARG A 1 136 ? -3.117  19.250 64.490 1.00 32.80 ? 136 ARG A CZ  1 
ATOM   997  N  NH1 . ARG A 1 136 ? -4.249  18.557 64.468 1.00 32.46 ? 136 ARG A NH1 1 
ATOM   998  N  NH2 . ARG A 1 136 ? -3.126  20.507 64.914 1.00 32.91 ? 136 ARG A NH2 1 
ATOM   999  N  N   . ALA A 1 137 ? -2.512  11.973 64.718 1.00 20.32 ? 137 ALA A N   1 
ATOM   1000 C  CA  . ALA A 1 137 ? -2.777  10.648 64.180 1.00 21.10 ? 137 ALA A CA  1 
ATOM   1001 C  C   . ALA A 1 137 ? -2.517  10.528 62.680 1.00 20.86 ? 137 ALA A C   1 
ATOM   1002 O  O   . ALA A 1 137 ? -1.977  9.519  62.221 1.00 22.26 ? 137 ALA A O   1 
ATOM   1003 C  CB  . ALA A 1 137 ? -4.213  10.241 64.494 1.00 24.08 ? 137 ALA A CB  1 
ATOM   1004 N  N   . ASP A 1 138 ? -2.891  11.554 61.920 1.00 18.43 ? 138 ASP A N   1 
ATOM   1005 C  CA  . ASP A 1 138 ? -2.709  11.526 60.471 1.00 17.89 ? 138 ASP A CA  1 
ATOM   1006 C  C   . ASP A 1 138 ? -1.328  11.957 59.966 1.00 15.82 ? 138 ASP A C   1 
ATOM   1007 O  O   . ASP A 1 138 ? -1.092  11.991 58.763 1.00 15.19 ? 138 ASP A O   1 
ATOM   1008 C  CB  . ASP A 1 138 ? -3.795  12.371 59.790 1.00 21.76 ? 138 ASP A CB  1 
ATOM   1009 C  CG  . ASP A 1 138 ? -3.973  13.733 60.436 1.00 26.09 ? 138 ASP A CG  1 
ATOM   1010 O  OD1 . ASP A 1 138 ? -3.193  14.073 61.354 1.00 30.30 ? 138 ASP A OD1 1 
ATOM   1011 O  OD2 . ASP A 1 138 ? -4.897  14.466 60.023 1.00 30.07 ? 138 ASP A OD2 1 
ATOM   1012 N  N   . ILE A 1 139 ? -0.419  12.288 60.877 1.00 14.54 ? 139 ILE A N   1 
ATOM   1013 C  CA  . ILE A 1 139 ? 0.925   12.693 60.483 1.00 13.54 ? 139 ILE A CA  1 
ATOM   1014 C  C   . ILE A 1 139 ? 1.906   11.590 60.878 1.00 14.25 ? 139 ILE A C   1 
ATOM   1015 O  O   . ILE A 1 139 ? 2.112   11.324 62.061 1.00 15.48 ? 139 ILE A O   1 
ATOM   1016 C  CB  . ILE A 1 139 ? 1.324   14.026 61.157 1.00 13.05 ? 139 ILE A CB  1 
ATOM   1017 C  CG1 . ILE A 1 139 ? 0.410   15.147 60.652 1.00 11.97 ? 139 ILE A CG1 1 
ATOM   1018 C  CG2 . ILE A 1 139 ? 2.792   14.352 60.858 1.00 11.11 ? 139 ILE A CG2 1 
ATOM   1019 C  CD1 . ILE A 1 139 ? 0.788   16.528 61.147 1.00 12.97 ? 139 ILE A CD1 1 
ATOM   1020 N  N   . SER A 1 140 ? 2.507   10.948 59.881 1.00 13.01 ? 140 SER A N   1 
ATOM   1021 C  CA  . SER A 1 140 ? 3.442   9.857  60.131 1.00 13.70 ? 140 SER A CA  1 
ATOM   1022 C  C   . SER A 1 140 ? 4.912   10.264 60.036 1.00 12.91 ? 140 SER A C   1 
ATOM   1023 O  O   . SER A 1 140 ? 5.782   9.599  60.597 1.00 14.49 ? 140 SER A O   1 
ATOM   1024 C  CB  . SER A 1 140 ? 3.169   8.717  59.152 1.00 14.35 ? 140 SER A CB  1 
ATOM   1025 O  OG  . SER A 1 140 ? 3.310   9.173  57.819 1.00 20.64 ? 140 SER A OG  1 
ATOM   1026 N  N   . SER A 1 141 ? 5.189   11.353 59.332 1.00 9.94  ? 141 SER A N   1 
ATOM   1027 C  CA  . SER A 1 141 ? 6.558   11.811 59.180 1.00 9.45  ? 141 SER A CA  1 
ATOM   1028 C  C   . SER A 1 141 ? 6.663   13.320 59.100 1.00 9.94  ? 141 SER A C   1 
ATOM   1029 O  O   . SER A 1 141 ? 5.748   14.007 58.643 1.00 9.62  ? 141 SER A O   1 
ATOM   1030 C  CB  . SER A 1 141 ? 7.180   11.227 57.908 1.00 9.57  ? 141 SER A CB  1 
ATOM   1031 O  OG  . SER A 1 141 ? 7.566   9.879  58.084 1.00 12.62 ? 141 SER A OG  1 
ATOM   1032 N  N   . VAL A 1 142 ? 7.797   13.825 59.565 1.00 10.15 ? 142 VAL A N   1 
ATOM   1033 C  CA  . VAL A 1 142 ? 8.097   15.240 59.495 1.00 8.85  ? 142 VAL A CA  1 
ATOM   1034 C  C   . VAL A 1 142 ? 9.494   15.249 58.894 1.00 8.72  ? 142 VAL A C   1 
ATOM   1035 O  O   . VAL A 1 142 ? 10.421  14.675 59.463 1.00 9.63  ? 142 VAL A O   1 
ATOM   1036 C  CB  . VAL A 1 142 ? 8.132   15.910 60.887 1.00 8.91  ? 142 VAL A CB  1 
ATOM   1037 C  CG1 . VAL A 1 142 ? 8.604   17.355 60.749 1.00 8.10  ? 142 VAL A CG1 1 
ATOM   1038 C  CG2 . VAL A 1 142 ? 6.746   15.871 61.529 1.00 8.36  ? 142 VAL A CG2 1 
ATOM   1039 N  N   . TYR A 1 143 ? 9.636   15.852 57.721 1.00 7.90  ? 143 TYR A N   1 
ATOM   1040 C  CA  . TYR A 1 143 ? 10.937  15.932 57.071 1.00 7.20  ? 143 TYR A CA  1 
ATOM   1041 C  C   . TYR A 1 143 ? 11.376  17.376 57.149 1.00 7.49  ? 143 TYR A C   1 
ATOM   1042 O  O   . TYR A 1 143 ? 10.689  18.269 56.652 1.00 6.65  ? 143 TYR A O   1 
ATOM   1043 C  CB  . TYR A 1 143 ? 10.845  15.501 55.609 1.00 7.29  ? 143 TYR A CB  1 
ATOM   1044 C  CG  . TYR A 1 143 ? 10.752  14.009 55.419 1.00 6.71  ? 143 TYR A CG  1 
ATOM   1045 C  CD1 . TYR A 1 143 ? 11.898  13.222 55.366 1.00 6.85  ? 143 TYR A CD1 1 
ATOM   1046 C  CD2 . TYR A 1 143 ? 9.516   13.385 55.263 1.00 6.86  ? 143 TYR A CD2 1 
ATOM   1047 C  CE1 . TYR A 1 143 ? 11.818  11.850 55.158 1.00 7.58  ? 143 TYR A CE1 1 
ATOM   1048 C  CE2 . TYR A 1 143 ? 9.425   12.012 55.054 1.00 7.60  ? 143 TYR A CE2 1 
ATOM   1049 C  CZ  . TYR A 1 143 ? 10.580  11.255 55.002 1.00 8.30  ? 143 TYR A CZ  1 
ATOM   1050 O  OH  . TYR A 1 143 ? 10.496  9.901  54.791 1.00 11.61 ? 143 TYR A OH  1 
ATOM   1051 N  N   . THR A 1 144 ? 12.528  17.600 57.770 1.00 6.59  ? 144 THR A N   1 
ATOM   1052 C  CA  . THR A 1 144 ? 13.037  18.948 57.937 1.00 6.27  ? 144 THR A CA  1 
ATOM   1053 C  C   . THR A 1 144 ? 14.459  19.138 57.416 1.00 7.66  ? 144 THR A C   1 
ATOM   1054 O  O   . THR A 1 144 ? 15.286  18.221 57.453 1.00 7.34  ? 144 THR A O   1 
ATOM   1055 C  CB  . THR A 1 144 ? 13.015  19.346 59.437 1.00 6.98  ? 144 THR A CB  1 
ATOM   1056 O  OG1 . THR A 1 144 ? 11.670  19.291 59.929 1.00 7.62  ? 144 THR A OG1 1 
ATOM   1057 C  CG2 . THR A 1 144 ? 13.575  20.748 59.640 1.00 5.34  ? 144 THR A CG2 1 
ATOM   1058 N  N   . VAL A 1 145 ? 14.720  20.338 56.907 1.00 7.34  ? 145 VAL A N   1 
ATOM   1059 C  CA  . VAL A 1 145 ? 16.047  20.711 56.447 1.00 6.76  ? 145 VAL A CA  1 
ATOM   1060 C  C   . VAL A 1 145 ? 16.296  22.032 57.157 1.00 6.49  ? 145 VAL A C   1 
ATOM   1061 O  O   . VAL A 1 145 ? 15.447  22.926 57.145 1.00 7.12  ? 145 VAL A O   1 
ATOM   1062 C  CB  . VAL A 1 145 ? 16.132  20.954 54.923 1.00 8.02  ? 145 VAL A CB  1 
ATOM   1063 C  CG1 . VAL A 1 145 ? 17.584  21.211 54.539 1.00 8.92  ? 145 VAL A CG1 1 
ATOM   1064 C  CG2 . VAL A 1 145 ? 15.608  19.755 54.156 1.00 8.46  ? 145 VAL A CG2 1 
ATOM   1065 N  N   . THR A 1 146 ? 17.449  22.152 57.794 1.00 6.28  ? 146 THR A N   1 
ATOM   1066 C  CA  . THR A 1 146 ? 17.777  23.372 58.509 1.00 5.71  ? 146 THR A CA  1 
ATOM   1067 C  C   . THR A 1 146 ? 19.248  23.699 58.277 1.00 6.30  ? 146 THR A C   1 
ATOM   1068 O  O   . THR A 1 146 ? 20.043  22.820 57.944 1.00 7.13  ? 146 THR A O   1 
ATOM   1069 C  CB  . THR A 1 146 ? 17.478  23.212 60.019 1.00 5.47  ? 146 THR A CB  1 
ATOM   1070 O  OG1 . THR A 1 146 ? 17.677  24.463 60.687 1.00 7.87  ? 146 THR A OG1 1 
ATOM   1071 C  CG2 . THR A 1 146 ? 18.373  22.150 60.637 1.00 5.04  ? 146 THR A CG2 1 
ATOM   1072 N  N   . GLY A 1 147 ? 19.602  24.970 58.422 1.00 5.21  ? 147 GLY A N   1 
ATOM   1073 C  CA  . GLY A 1 147 ? 20.978  25.373 58.215 1.00 4.95  ? 147 GLY A CA  1 
ATOM   1074 C  C   . GLY A 1 147 ? 21.169  26.837 58.547 1.00 5.90  ? 147 GLY A C   1 
ATOM   1075 O  O   . GLY A 1 147 ? 20.204  27.527 58.876 1.00 5.96  ? 147 GLY A O   1 
ATOM   1076 N  N   . PRO A 1 148 ? 22.410  27.339 58.485 1.00 9.41  ? 148 PRO A N   1 
ATOM   1077 C  CA  . PRO A 1 148 ? 22.709  28.738 58.786 1.00 10.07 ? 148 PRO A CA  1 
ATOM   1078 C  C   . PRO A 1 148 ? 22.841  29.635 57.559 1.00 10.83 ? 148 PRO A C   1 
ATOM   1079 O  O   . PRO A 1 148 ? 22.858  29.160 56.423 1.00 9.81  ? 148 PRO A O   1 
ATOM   1080 C  CB  . PRO A 1 148 ? 24.027  28.644 59.540 1.00 10.24 ? 148 PRO A CB  1 
ATOM   1081 C  CG  . PRO A 1 148 ? 24.713  27.416 58.925 1.00 11.99 ? 148 PRO A CG  1 
ATOM   1082 C  CD  . PRO A 1 148 ? 23.647  26.594 58.201 1.00 9.59  ? 148 PRO A CD  1 
ATOM   1083 N  N   . LEU A 1 149 ? 22.922  30.938 57.821 1.00 10.61 ? 149 LEU A N   1 
ATOM   1084 C  CA  . LEU A 1 149 ? 23.113  31.960 56.796 1.00 11.19 ? 149 LEU A CA  1 
ATOM   1085 C  C   . LEU A 1 149 ? 24.375  32.678 57.255 1.00 11.29 ? 149 LEU A C   1 
ATOM   1086 O  O   . LEU A 1 149 ? 24.637  32.750 58.455 1.00 10.86 ? 149 LEU A O   1 
ATOM   1087 C  CB  . LEU A 1 149 ? 21.950  32.964 56.774 1.00 11.57 ? 149 LEU A CB  1 
ATOM   1088 C  CG  . LEU A 1 149 ? 20.649  32.629 56.029 1.00 14.40 ? 149 LEU A CG  1 
ATOM   1089 C  CD1 . LEU A 1 149 ? 19.750  33.860 55.981 1.00 14.28 ? 149 LEU A CD1 1 
ATOM   1090 C  CD2 . LEU A 1 149 ? 20.960  32.150 54.628 1.00 15.67 ? 149 LEU A CD2 1 
ATOM   1091 N  N   . TYR A 1 150 ? 25.156  33.195 56.313 1.00 12.62 ? 150 TYR A N   1 
ATOM   1092 C  CA  . TYR A 1 150 ? 26.385  33.918 56.640 1.00 13.22 ? 150 TYR A CA  1 
ATOM   1093 C  C   . TYR A 1 150 ? 26.368  35.235 55.880 1.00 14.80 ? 150 TYR A C   1 
ATOM   1094 O  O   . TYR A 1 150 ? 27.024  35.370 54.845 1.00 16.53 ? 150 TYR A O   1 
ATOM   1095 C  CB  . TYR A 1 150 ? 27.605  33.103 56.218 1.00 10.95 ? 150 TYR A CB  1 
ATOM   1096 C  CG  . TYR A 1 150 ? 27.688  31.752 56.876 1.00 9.60  ? 150 TYR A CG  1 
ATOM   1097 C  CD1 . TYR A 1 150 ? 28.173  31.620 58.177 1.00 10.26 ? 150 TYR A CD1 1 
ATOM   1098 C  CD2 . TYR A 1 150 ? 27.276  30.602 56.203 1.00 8.39  ? 150 TYR A CD2 1 
ATOM   1099 C  CE1 . TYR A 1 150 ? 28.245  30.373 58.794 1.00 9.90  ? 150 TYR A CE1 1 
ATOM   1100 C  CE2 . TYR A 1 150 ? 27.343  29.356 56.807 1.00 9.06  ? 150 TYR A CE2 1 
ATOM   1101 C  CZ  . TYR A 1 150 ? 27.828  29.249 58.103 1.00 10.67 ? 150 TYR A CZ  1 
ATOM   1102 O  OH  . TYR A 1 150 ? 27.896  28.017 58.706 1.00 12.47 ? 150 TYR A OH  1 
ATOM   1103 N  N   . GLU A 1 151 ? 25.629  36.210 56.397 1.00 14.44 ? 151 GLU A N   1 
ATOM   1104 C  CA  . GLU A 1 151 ? 25.507  37.489 55.714 1.00 15.21 ? 151 GLU A CA  1 
ATOM   1105 C  C   . GLU A 1 151 ? 26.180  38.678 56.379 1.00 16.50 ? 151 GLU A C   1 
ATOM   1106 O  O   . GLU A 1 151 ? 26.213  39.766 55.812 1.00 19.02 ? 151 GLU A O   1 
ATOM   1107 C  CB  . GLU A 1 151 ? 24.026  37.792 55.474 1.00 10.54 ? 151 GLU A CB  1 
ATOM   1108 C  CG  . GLU A 1 151 ? 23.374  36.774 54.557 1.00 11.75 ? 151 GLU A CG  1 
ATOM   1109 C  CD  . GLU A 1 151 ? 21.870  36.883 54.517 1.00 11.09 ? 151 GLU A CD  1 
ATOM   1110 O  OE1 . GLU A 1 151 ? 21.282  37.446 55.463 1.00 10.87 ? 151 GLU A OE1 1 
ATOM   1111 O  OE2 . GLU A 1 151 ? 21.277  36.402 53.532 1.00 10.93 ? 151 GLU A OE2 1 
ATOM   1112 N  N   . ARG A 1 152 ? 26.711  38.480 57.577 1.00 18.00 ? 152 ARG A N   1 
ATOM   1113 C  CA  . ARG A 1 152 ? 27.386  39.561 58.277 1.00 18.60 ? 152 ARG A CA  1 
ATOM   1114 C  C   . ARG A 1 152 ? 28.312  39.013 59.350 1.00 20.09 ? 152 ARG A C   1 
ATOM   1115 O  O   . ARG A 1 152 ? 28.064  37.949 59.916 1.00 21.20 ? 152 ARG A O   1 
ATOM   1116 C  CB  . ARG A 1 152 ? 26.365  40.518 58.900 1.00 17.61 ? 152 ARG A CB  1 
ATOM   1117 C  CG  . ARG A 1 152 ? 25.808  40.064 60.237 1.00 17.62 ? 152 ARG A CG  1 
ATOM   1118 C  CD  . ARG A 1 152 ? 24.866  41.100 60.812 1.00 17.48 ? 152 ARG A CD  1 
ATOM   1119 N  NE  . ARG A 1 152 ? 24.308  40.673 62.092 1.00 20.58 ? 152 ARG A NE  1 
ATOM   1120 C  CZ  . ARG A 1 152 ? 23.099  40.140 62.242 1.00 21.02 ? 152 ARG A CZ  1 
ATOM   1121 N  NH1 . ARG A 1 152 ? 22.311  39.966 61.188 1.00 17.03 ? 152 ARG A NH1 1 
ATOM   1122 N  NH2 . ARG A 1 152 ? 22.680  39.775 63.448 1.00 21.11 ? 152 ARG A NH2 1 
ATOM   1123 N  N   . ASP A 1 153 ? 29.385  39.748 59.613 1.00 18.47 ? 153 ASP A N   1 
ATOM   1124 C  CA  . ASP A 1 153 ? 30.372  39.366 60.611 1.00 18.48 ? 153 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 153 ? 29.732  39.304 61.992 1.00 18.54 ? 153 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 153 ? 29.113  40.268 62.440 1.00 19.13 ? 153 ASP A O   1 
ATOM   1127 C  CB  . ASP A 1 153 ? 31.507  40.389 60.615 1.00 24.64 ? 153 ASP A CB  1 
ATOM   1128 C  CG  . ASP A 1 153 ? 32.761  39.872 61.283 1.00 32.20 ? 153 ASP A CG  1 
ATOM   1129 O  OD1 . ASP A 1 153 ? 32.688  38.847 61.994 1.00 32.99 ? 153 ASP A OD1 1 
ATOM   1130 O  OD2 . ASP A 1 153 ? 33.826  40.499 61.094 1.00 35.21 ? 153 ASP A OD2 1 
ATOM   1131 N  N   . MET A 1 154 ? 29.879  38.166 62.664 1.00 17.09 ? 154 MET A N   1 
ATOM   1132 C  CA  . MET A 1 154 ? 29.319  37.992 63.997 1.00 17.82 ? 154 MET A CA  1 
ATOM   1133 C  C   . MET A 1 154 ? 30.439  37.890 65.029 1.00 18.44 ? 154 MET A C   1 
ATOM   1134 O  O   . MET A 1 154 ? 30.192  37.635 66.205 1.00 20.51 ? 154 MET A O   1 
ATOM   1135 C  CB  . MET A 1 154 ? 28.456  36.726 64.050 1.00 19.25 ? 154 MET A CB  1 
ATOM   1136 C  CG  . MET A 1 154 ? 27.091  36.863 63.380 1.00 20.48 ? 154 MET A CG  1 
ATOM   1137 S  SD  . MET A 1 154 ? 26.034  38.111 64.147 1.00 22.25 ? 154 MET A SD  1 
ATOM   1138 C  CE  . MET A 1 154 ? 25.560  37.262 65.656 1.00 21.88 ? 154 MET A CE  1 
ATOM   1139 N  N   . GLY A 1 155 ? 31.673  38.097 64.587 1.00 17.57 ? 155 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 155 ? 32.795  38.006 65.500 1.00 18.04 ? 155 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 155 ? 33.368  36.604 65.487 1.00 18.05 ? 155 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 155 ? 32.999  35.792 64.638 1.00 19.29 ? 155 GLY A O   1 
ATOM   1143 N  N   . LYS A 1 156 ? 34.257  36.308 66.429 1.00 15.94 ? 156 LYS A N   1 
ATOM   1144 C  CA  . LYS A 1 156 ? 34.877  34.989 66.486 1.00 16.84 ? 156 LYS A CA  1 
ATOM   1145 C  C   . LYS A 1 156 ? 34.918  34.383 67.887 1.00 16.30 ? 156 LYS A C   1 
ATOM   1146 O  O   . LYS A 1 156 ? 34.964  35.099 68.893 1.00 16.09 ? 156 LYS A O   1 
ATOM   1147 C  CB  . LYS A 1 156 ? 36.301  35.062 65.924 1.00 22.42 ? 156 LYS A CB  1 
ATOM   1148 C  CG  . LYS A 1 156 ? 36.382  35.539 64.473 1.00 28.85 ? 156 LYS A CG  1 
ATOM   1149 C  CD  . LYS A 1 156 ? 35.811  34.502 63.500 1.00 33.72 ? 156 LYS A CD  1 
ATOM   1150 C  CE  . LYS A 1 156 ? 35.046  35.158 62.349 1.00 35.12 ? 156 LYS A CE  1 
ATOM   1151 N  NZ  . LYS A 1 156 ? 33.580  34.820 62.357 1.00 36.53 ? 156 LYS A NZ  1 
ATOM   1152 N  N   . LEU A 1 157 ? 34.896  33.055 67.941 1.00 14.75 ? 157 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 157 ? 34.960  32.339 69.209 1.00 14.36 ? 157 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 157 ? 36.306  32.684 69.848 1.00 14.85 ? 157 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 157 ? 37.350  32.593 69.204 1.00 15.23 ? 157 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 157 ? 34.857  30.831 68.967 1.00 12.81 ? 157 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 157 ? 33.514  30.321 68.430 1.00 13.92 ? 157 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 157 ? 33.643  28.856 68.033 1.00 12.72 ? 157 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 157 ? 32.439  30.489 69.488 1.00 12.07 ? 157 LEU A CD2 1 
ATOM   1160 N  N   . PRO A 1 158 ? 36.298  33.090 71.124 1.00 16.12 ? 158 PRO A N   1 
ATOM   1161 C  CA  . PRO A 1 158 ? 37.543  33.448 71.813 1.00 17.51 ? 158 PRO A CA  1 
ATOM   1162 C  C   . PRO A 1 158 ? 38.508  32.305 72.123 1.00 17.85 ? 158 PRO A C   1 
ATOM   1163 O  O   . PRO A 1 158 ? 39.713  32.523 72.220 1.00 18.53 ? 158 PRO A O   1 
ATOM   1164 C  CB  . PRO A 1 158 ? 37.057  34.128 73.089 1.00 17.44 ? 158 PRO A CB  1 
ATOM   1165 C  CG  . PRO A 1 158 ? 35.722  33.499 73.349 1.00 16.79 ? 158 PRO A CG  1 
ATOM   1166 C  CD  . PRO A 1 158 ? 35.119  33.247 71.995 1.00 16.41 ? 158 PRO A CD  1 
ATOM   1167 N  N   . GLY A 1 159 ? 37.984  31.092 72.266 1.00 18.31 ? 159 GLY A N   1 
ATOM   1168 C  CA  . GLY A 1 159 ? 38.832  29.964 72.611 1.00 18.09 ? 159 GLY A CA  1 
ATOM   1169 C  C   . GLY A 1 159 ? 39.413  29.098 71.510 1.00 18.37 ? 159 GLY A C   1 
ATOM   1170 O  O   . GLY A 1 159 ? 39.761  27.946 71.760 1.00 19.46 ? 159 GLY A O   1 
ATOM   1171 N  N   . THR A 1 160 ? 39.533  29.626 70.298 1.00 17.14 ? 160 THR A N   1 
ATOM   1172 C  CA  . THR A 1 160 ? 40.097  28.831 69.214 1.00 17.44 ? 160 THR A CA  1 
ATOM   1173 C  C   . THR A 1 160 ? 40.869  29.670 68.208 1.00 18.95 ? 160 THR A C   1 
ATOM   1174 O  O   . THR A 1 160 ? 40.586  30.854 68.022 1.00 19.34 ? 160 THR A O   1 
ATOM   1175 C  CB  . THR A 1 160 ? 39.002  28.043 68.462 1.00 16.81 ? 160 THR A CB  1 
ATOM   1176 O  OG1 . THR A 1 160 ? 39.619  27.128 67.548 1.00 16.47 ? 160 THR A OG1 1 
ATOM   1177 C  CG2 . THR A 1 160 ? 38.086  28.985 67.689 1.00 13.89 ? 160 THR A CG2 1 
ATOM   1178 N  N   . GLN A 1 161 ? 41.849  29.044 67.566 1.00 20.51 ? 161 GLN A N   1 
ATOM   1179 C  CA  . GLN A 1 161 ? 42.661  29.718 66.563 1.00 21.68 ? 161 GLN A CA  1 
ATOM   1180 C  C   . GLN A 1 161 ? 42.223  29.265 65.176 1.00 21.02 ? 161 GLN A C   1 
ATOM   1181 O  O   . GLN A 1 161 ? 42.697  29.777 64.163 1.00 22.97 ? 161 GLN A O   1 
ATOM   1182 C  CB  . GLN A 1 161 ? 44.136  29.392 66.777 1.00 30.44 ? 161 GLN A CB  1 
ATOM   1183 C  CG  . GLN A 1 161 ? 44.688  29.909 68.091 1.00 32.15 ? 161 GLN A CG  1 
ATOM   1184 C  CD  . GLN A 1 161 ? 46.185  29.700 68.204 1.00 37.45 ? 161 GLN A CD  1 
ATOM   1185 O  OE1 . GLN A 1 161 ? 46.655  28.574 68.392 1.00 38.07 ? 161 GLN A OE1 1 
ATOM   1186 N  NE2 . GLN A 1 161 ? 46.945  30.785 68.082 1.00 37.87 ? 161 GLN A NE2 1 
ATOM   1187 N  N   . LYS A 1 162 ? 41.312  28.296 65.143 1.00 18.21 ? 162 LYS A N   1 
ATOM   1188 C  CA  . LYS A 1 162 ? 40.785  27.769 63.889 1.00 16.64 ? 162 LYS A CA  1 
ATOM   1189 C  C   . LYS A 1 162 ? 40.008  28.862 63.170 1.00 15.72 ? 162 LYS A C   1 
ATOM   1190 O  O   . LYS A 1 162 ? 39.305  29.645 63.805 1.00 15.86 ? 162 LYS A O   1 
ATOM   1191 C  CB  . LYS A 1 162 ? 39.827  26.609 64.162 1.00 16.54 ? 162 LYS A CB  1 
ATOM   1192 C  CG  . LYS A 1 162 ? 40.472  25.262 64.345 1.00 18.26 ? 162 LYS A CG  1 
ATOM   1193 C  CD  . LYS A 1 162 ? 39.406  24.187 64.372 1.00 18.57 ? 162 LYS A CD  1 
ATOM   1194 C  CE  . LYS A 1 162 ? 39.956  22.870 64.877 1.00 20.51 ? 162 LYS A CE  1 
ATOM   1195 N  NZ  . LYS A 1 162 ? 39.357  22.495 66.188 1.00 22.16 ? 162 LYS A NZ  1 
ATOM   1196 N  N   . ALA A 1 163 ? 40.132  28.916 61.849 1.00 15.71 ? 163 ALA A N   1 
ATOM   1197 C  CA  . ALA A 1 163 ? 39.390  29.901 61.074 1.00 15.83 ? 163 ALA A CA  1 
ATOM   1198 C  C   . ALA A 1 163 ? 37.960  29.374 61.008 1.00 14.95 ? 163 ALA A C   1 
ATOM   1199 O  O   . ALA A 1 163 ? 37.738  28.211 60.673 1.00 15.56 ? 163 ALA A O   1 
ATOM   1200 C  CB  . ALA A 1 163 ? 39.972  30.024 59.674 1.00 15.85 ? 163 ALA A CB  1 
ATOM   1201 N  N   . HIS A 1 164 ? 36.993  30.221 61.334 1.00 14.46 ? 164 HIS A N   1 
ATOM   1202 C  CA  . HIS A 1 164 ? 35.594  29.810 61.319 1.00 13.52 ? 164 HIS A CA  1 
ATOM   1203 C  C   . HIS A 1 164 ? 34.716  31.023 61.082 1.00 13.43 ? 164 HIS A C   1 
ATOM   1204 O  O   . HIS A 1 164 ? 35.181  32.155 61.175 1.00 13.61 ? 164 HIS A O   1 
ATOM   1205 C  CB  . HIS A 1 164 ? 35.224  29.165 62.659 1.00 12.50 ? 164 HIS A CB  1 
ATOM   1206 C  CG  . HIS A 1 164 ? 35.299  30.107 63.823 1.00 13.48 ? 164 HIS A CG  1 
ATOM   1207 N  ND1 . HIS A 1 164 ? 36.489  30.453 64.426 1.00 14.58 ? 164 HIS A ND1 1 
ATOM   1208 C  CD2 . HIS A 1 164 ? 34.331  30.786 64.486 1.00 13.85 ? 164 HIS A CD2 1 
ATOM   1209 C  CE1 . HIS A 1 164 ? 36.252  31.304 65.409 1.00 14.58 ? 164 HIS A CE1 1 
ATOM   1210 N  NE2 . HIS A 1 164 ? 34.950  31.523 65.467 1.00 13.79 ? 164 HIS A NE2 1 
ATOM   1211 N  N   . THR A 1 165 ? 33.446  30.787 60.773 1.00 13.04 ? 165 THR A N   1 
ATOM   1212 C  CA  . THR A 1 165 ? 32.509  31.879 60.536 1.00 13.57 ? 165 THR A CA  1 
ATOM   1213 C  C   . THR A 1 165 ? 31.202  31.615 61.261 1.00 12.43 ? 165 THR A C   1 
ATOM   1214 O  O   . THR A 1 165 ? 30.481  30.673 60.936 1.00 12.71 ? 165 THR A O   1 
ATOM   1215 C  CB  . THR A 1 165 ? 32.195  32.054 59.037 1.00 15.31 ? 165 THR A CB  1 
ATOM   1216 O  OG1 . THR A 1 165 ? 33.416  32.098 58.292 1.00 17.06 ? 165 THR A OG1 1 
ATOM   1217 C  CG2 . THR A 1 165 ? 31.425  33.345 58.806 1.00 14.21 ? 165 THR A CG2 1 
ATOM   1218 N  N   . ILE A 1 166 ? 30.900  32.452 62.246 1.00 11.81 ? 166 ILE A N   1 
ATOM   1219 C  CA  . ILE A 1 166 ? 29.674  32.310 63.016 1.00 10.91 ? 166 ILE A CA  1 
ATOM   1220 C  C   . ILE A 1 166 ? 28.486  32.753 62.166 1.00 11.47 ? 166 ILE A C   1 
ATOM   1221 O  O   . ILE A 1 166 ? 28.527  33.811 61.528 1.00 11.53 ? 166 ILE A O   1 
ATOM   1222 C  CB  . ILE A 1 166 ? 29.737  33.156 64.305 1.00 10.07 ? 166 ILE A CB  1 
ATOM   1223 C  CG1 . ILE A 1 166 ? 30.888  32.654 65.187 1.00 10.65 ? 166 ILE A CG1 1 
ATOM   1224 C  CG2 . ILE A 1 166 ? 28.406  33.085 65.046 1.00 8.95  ? 166 ILE A CG2 1 
ATOM   1225 C  CD1 . ILE A 1 166 ? 31.017  33.378 66.519 1.00 10.85 ? 166 ILE A CD1 1 
ATOM   1226 N  N   . PRO A 1 167 ? 27.415  31.937 62.131 1.00 11.67 ? 167 PRO A N   1 
ATOM   1227 C  CA  . PRO A 1 167 ? 26.217  32.263 61.346 1.00 11.17 ? 167 PRO A CA  1 
ATOM   1228 C  C   . PRO A 1 167 ? 25.563  33.557 61.806 1.00 10.79 ? 167 PRO A C   1 
ATOM   1229 O  O   . PRO A 1 167 ? 25.730  33.969 62.952 1.00 11.73 ? 167 PRO A O   1 
ATOM   1230 C  CB  . PRO A 1 167 ? 25.296  31.059 61.564 1.00 9.63  ? 167 PRO A CB  1 
ATOM   1231 C  CG  . PRO A 1 167 ? 26.188  29.967 62.059 1.00 9.68  ? 167 PRO A CG  1 
ATOM   1232 C  CD  . PRO A 1 167 ? 27.280  30.644 62.823 1.00 9.63  ? 167 PRO A CD  1 
ATOM   1233 N  N   . SER A 1 168 ? 24.817  34.193 60.909 1.00 8.15  ? 168 SER A N   1 
ATOM   1234 C  CA  . SER A 1 168 ? 24.122  35.431 61.237 1.00 7.86  ? 168 SER A CA  1 
ATOM   1235 C  C   . SER A 1 168 ? 22.626  35.149 61.370 1.00 8.18  ? 168 SER A C   1 
ATOM   1236 O  O   . SER A 1 168 ? 21.880  35.941 61.940 1.00 9.44  ? 168 SER A O   1 
ATOM   1237 C  CB  . SER A 1 168 ? 24.356  36.469 60.142 1.00 8.23  ? 168 SER A CB  1 
ATOM   1238 O  OG  . SER A 1 168 ? 23.927  35.981 58.884 1.00 8.61  ? 168 SER A OG  1 
ATOM   1239 N  N   . ALA A 1 169 ? 22.199  34.006 60.843 1.00 9.74  ? 169 ALA A N   1 
ATOM   1240 C  CA  . ALA A 1 169 ? 20.797  33.607 60.886 1.00 8.85  ? 169 ALA A CA  1 
ATOM   1241 C  C   . ALA A 1 169 ? 20.657  32.099 60.685 1.00 8.78  ? 169 ALA A C   1 
ATOM   1242 O  O   . ALA A 1 169 ? 21.611  31.420 60.304 1.00 9.61  ? 169 ALA A O   1 
ATOM   1243 C  CB  . ALA A 1 169 ? 20.009  34.353 59.809 1.00 6.73  ? 169 ALA A CB  1 
ATOM   1244 N  N   . TYR A 1 170 ? 19.459  31.587 60.949 1.00 7.60  ? 170 TYR A N   1 
ATOM   1245 C  CA  . TYR A 1 170 ? 19.161  30.168 60.802 1.00 8.13  ? 170 TYR A CA  1 
ATOM   1246 C  C   . TYR A 1 170 ? 17.801  30.018 60.142 1.00 9.16  ? 170 TYR A C   1 
ATOM   1247 O  O   . TYR A 1 170 ? 16.888  30.802 60.401 1.00 8.72  ? 170 TYR A O   1 
ATOM   1248 C  CB  . TYR A 1 170 ? 19.126  29.479 62.169 1.00 9.02  ? 170 TYR A CB  1 
ATOM   1249 C  CG  . TYR A 1 170 ? 20.424  29.558 62.926 1.00 9.01  ? 170 TYR A CG  1 
ATOM   1250 C  CD1 . TYR A 1 170 ? 21.407  28.577 62.772 1.00 8.65  ? 170 TYR A CD1 1 
ATOM   1251 C  CD2 . TYR A 1 170 ? 20.685  30.629 63.777 1.00 9.68  ? 170 TYR A CD2 1 
ATOM   1252 C  CE1 . TYR A 1 170 ? 22.626  28.666 63.449 1.00 10.30 ? 170 TYR A CE1 1 
ATOM   1253 C  CE2 . TYR A 1 170 ? 21.895  30.729 64.457 1.00 11.48 ? 170 TYR A CE2 1 
ATOM   1254 C  CZ  . TYR A 1 170 ? 22.861  29.751 64.289 1.00 10.29 ? 170 TYR A CZ  1 
ATOM   1255 O  OH  . TYR A 1 170 ? 24.060  29.878 64.950 1.00 11.75 ? 170 TYR A OH  1 
ATOM   1256 N  N   . TRP A 1 171 ? 17.667  29.002 59.297 1.00 8.77  ? 171 TRP A N   1 
ATOM   1257 C  CA  . TRP A 1 171 ? 16.412  28.757 58.604 1.00 8.05  ? 171 TRP A CA  1 
ATOM   1258 C  C   . TRP A 1 171 ? 15.997  27.313 58.808 1.00 8.47  ? 171 TRP A C   1 
ATOM   1259 O  O   . TRP A 1 171 ? 16.811  26.469 59.187 1.00 9.77  ? 171 TRP A O   1 
ATOM   1260 C  CB  . TRP A 1 171 ? 16.564  29.047 57.105 1.00 6.77  ? 171 TRP A CB  1 
ATOM   1261 C  CG  . TRP A 1 171 ? 17.796  28.441 56.499 1.00 6.04  ? 171 TRP A CG  1 
ATOM   1262 C  CD1 . TRP A 1 171 ? 19.032  29.016 56.407 1.00 5.98  ? 171 TRP A CD1 1 
ATOM   1263 C  CD2 . TRP A 1 171 ? 17.918  27.134 55.921 1.00 7.39  ? 171 TRP A CD2 1 
ATOM   1264 N  NE1 . TRP A 1 171 ? 19.914  28.150 55.813 1.00 6.87  ? 171 TRP A NE1 1 
ATOM   1265 C  CE2 . TRP A 1 171 ? 19.258  26.986 55.505 1.00 7.31  ? 171 TRP A CE2 1 
ATOM   1266 C  CE3 . TRP A 1 171 ? 17.024  26.072 55.717 1.00 7.02  ? 171 TRP A CE3 1 
ATOM   1267 C  CZ2 . TRP A 1 171 ? 19.729  25.818 54.895 1.00 7.34  ? 171 TRP A CZ2 1 
ATOM   1268 C  CZ3 . TRP A 1 171 ? 17.492  24.911 55.110 1.00 7.70  ? 171 TRP A CZ3 1 
ATOM   1269 C  CH2 . TRP A 1 171 ? 18.834  24.795 54.708 1.00 8.35  ? 171 TRP A CH2 1 
ATOM   1270 N  N   . LYS A 1 172 ? 14.724  27.036 58.563 1.00 6.49  ? 172 LYS A N   1 
ATOM   1271 C  CA  . LYS A 1 172 ? 14.193  25.690 58.705 1.00 6.73  ? 172 LYS A CA  1 
ATOM   1272 C  C   . LYS A 1 172 ? 13.067  25.498 57.697 1.00 6.80  ? 172 LYS A C   1 
ATOM   1273 O  O   . LYS A 1 172 ? 12.155  26.319 57.613 1.00 8.69  ? 172 LYS A O   1 
ATOM   1274 C  CB  . LYS A 1 172 ? 13.664  25.472 60.127 1.00 8.27  ? 172 LYS A CB  1 
ATOM   1275 C  CG  . LYS A 1 172 ? 13.270  24.034 60.428 1.00 9.17  ? 172 LYS A CG  1 
ATOM   1276 C  CD  . LYS A 1 172 ? 13.010  23.820 61.909 1.00 10.62 ? 172 LYS A CD  1 
ATOM   1277 C  CE  . LYS A 1 172 ? 14.284  23.413 62.642 1.00 10.41 ? 172 LYS A CE  1 
ATOM   1278 N  NZ  . LYS A 1 172 ? 14.039  23.188 64.100 1.00 9.33  ? 172 LYS A NZ  1 
ATOM   1279 N  N   . VAL A 1 173 ? 13.153  24.420 56.926 1.00 7.01  ? 173 VAL A N   1 
ATOM   1280 C  CA  . VAL A 1 173 ? 12.152  24.090 55.920 1.00 5.93  ? 173 VAL A CA  1 
ATOM   1281 C  C   . VAL A 1 173 ? 11.536  22.764 56.344 1.00 6.01  ? 173 VAL A C   1 
ATOM   1282 O  O   . VAL A 1 173 ? 12.242  21.772 56.542 1.00 6.05  ? 173 VAL A O   1 
ATOM   1283 C  CB  . VAL A 1 173 ? 12.794  23.958 54.524 1.00 6.56  ? 173 VAL A CB  1 
ATOM   1284 C  CG1 . VAL A 1 173 ? 11.784  23.449 53.531 1.00 6.52  ? 173 VAL A CG1 1 
ATOM   1285 C  CG2 . VAL A 1 173 ? 13.322  25.312 54.079 1.00 6.37  ? 173 VAL A CG2 1 
ATOM   1286 N  N   . ILE A 1 174 ? 10.215  22.753 56.475 1.00 6.55  ? 174 ILE A N   1 
ATOM   1287 C  CA  . ILE A 1 174 ? 9.499   21.568 56.938 1.00 7.68  ? 174 ILE A CA  1 
ATOM   1288 C  C   . ILE A 1 174 ? 8.326   21.145 56.063 1.00 7.16  ? 174 ILE A C   1 
ATOM   1289 O  O   . ILE A 1 174 ? 7.660   21.979 55.450 1.00 9.19  ? 174 ILE A O   1 
ATOM   1290 C  CB  . ILE A 1 174 ? 8.921   21.814 58.368 1.00 7.42  ? 174 ILE A CB  1 
ATOM   1291 C  CG1 . ILE A 1 174 ? 9.986   22.442 59.269 1.00 10.35 ? 174 ILE A CG1 1 
ATOM   1292 C  CG2 . ILE A 1 174 ? 8.380   20.514 58.958 1.00 6.88  ? 174 ILE A CG2 1 
ATOM   1293 C  CD1 . ILE A 1 174 ? 9.413   23.089 60.521 1.00 11.53 ? 174 ILE A CD1 1 
ATOM   1294 N  N   . PHE A 1 175 ? 8.090   19.841 56.001 1.00 7.44  ? 175 PHE A N   1 
ATOM   1295 C  CA  . PHE A 1 175 ? 6.938   19.306 55.287 1.00 7.70  ? 175 PHE A CA  1 
ATOM   1296 C  C   . PHE A 1 175 ? 6.574   17.985 55.951 1.00 7.98  ? 175 PHE A C   1 
ATOM   1297 O  O   . PHE A 1 175 ? 7.426   17.303 56.530 1.00 8.31  ? 175 PHE A O   1 
ATOM   1298 C  CB  . PHE A 1 175 ? 7.195   19.167 53.772 1.00 6.77  ? 175 PHE A CB  1 
ATOM   1299 C  CG  . PHE A 1 175 ? 8.000   17.965 53.376 1.00 7.04  ? 175 PHE A CG  1 
ATOM   1300 C  CD1 . PHE A 1 175 ? 7.404   16.711 53.270 1.00 6.99  ? 175 PHE A CD1 1 
ATOM   1301 C  CD2 . PHE A 1 175 ? 9.346   18.098 53.049 1.00 6.81  ? 175 PHE A CD2 1 
ATOM   1302 C  CE1 . PHE A 1 175 ? 8.136   15.605 52.842 1.00 7.72  ? 175 PHE A CE1 1 
ATOM   1303 C  CE2 . PHE A 1 175 ? 10.090  16.996 52.618 1.00 8.04  ? 175 PHE A CE2 1 
ATOM   1304 C  CZ  . PHE A 1 175 ? 9.482   15.750 52.514 1.00 7.62  ? 175 PHE A CZ  1 
ATOM   1305 N  N   . ILE A 1 176 ? 5.300   17.635 55.898 1.00 7.90  ? 176 ILE A N   1 
ATOM   1306 C  CA  . ILE A 1 176 ? 4.845   16.415 56.541 1.00 8.90  ? 176 ILE A CA  1 
ATOM   1307 C  C   . ILE A 1 176 ? 4.512   15.275 55.591 1.00 9.20  ? 176 ILE A C   1 
ATOM   1308 O  O   . ILE A 1 176 ? 4.183   15.485 54.424 1.00 7.47  ? 176 ILE A O   1 
ATOM   1309 C  CB  . ILE A 1 176 ? 3.597   16.692 57.409 1.00 9.10  ? 176 ILE A CB  1 
ATOM   1310 C  CG1 . ILE A 1 176 ? 2.538   17.431 56.577 1.00 9.61  ? 176 ILE A CG1 1 
ATOM   1311 C  CG2 . ILE A 1 176 ? 3.984   17.531 58.616 1.00 9.23  ? 176 ILE A CG2 1 
ATOM   1312 C  CD1 . ILE A 1 176 ? 1.112   17.277 57.094 1.00 9.33  ? 176 ILE A CD1 1 
ATOM   1313 N  N   . ASN A 1 177 ? 4.624   14.065 56.126 1.00 10.81 ? 177 ASN A N   1 
ATOM   1314 C  CA  . ASN A 1 177 ? 4.310   12.836 55.423 1.00 13.62 ? 177 ASN A CA  1 
ATOM   1315 C  C   . ASN A 1 177 ? 5.109   12.439 54.187 1.00 15.25 ? 177 ASN A C   1 
ATOM   1316 O  O   . ASN A 1 177 ? 6.207   11.909 54.309 1.00 19.25 ? 177 ASN A O   1 
ATOM   1317 C  CB  . ASN A 1 177 ? 2.813   12.815 55.111 1.00 10.59 ? 177 ASN A CB  1 
ATOM   1318 C  CG  . ASN A 1 177 ? 1.975   12.712 56.366 1.00 14.05 ? 177 ASN A CG  1 
ATOM   1319 O  OD1 . ASN A 1 177 ? 2.514   12.574 57.464 1.00 14.13 ? 177 ASN A OD1 1 
ATOM   1320 N  ND2 . ASN A 1 177 ? 0.659   12.779 56.217 1.00 11.54 ? 177 ASN A ND2 1 
ATOM   1321 N  N   . ASN A 1 178 ? 4.564   12.695 53.003 1.00 13.92 ? 178 ASN A N   1 
ATOM   1322 C  CA  . ASN A 1 178 ? 5.211   12.283 51.759 1.00 13.93 ? 178 ASN A CA  1 
ATOM   1323 C  C   . ASN A 1 178 ? 6.054   13.270 50.969 1.00 11.34 ? 178 ASN A C   1 
ATOM   1324 O  O   . ASN A 1 178 ? 7.218   13.001 50.680 1.00 10.17 ? 178 ASN A O   1 
ATOM   1325 C  CB  . ASN A 1 178 ? 4.157   11.708 50.817 1.00 17.17 ? 178 ASN A CB  1 
ATOM   1326 C  CG  . ASN A 1 178 ? 3.302   10.664 51.485 1.00 22.17 ? 178 ASN A CG  1 
ATOM   1327 O  OD1 . ASN A 1 178 ? 3.801   9.624  51.911 1.00 27.99 ? 178 ASN A OD1 1 
ATOM   1328 N  ND2 . ASN A 1 178 ? 2.006   10.935 51.585 1.00 25.39 ? 178 ASN A ND2 1 
ATOM   1329 N  N   . SER A 1 179 ? 5.468   14.397 50.590 1.00 9.37  ? 179 SER A N   1 
ATOM   1330 C  CA  . SER A 1 179 ? 6.202   15.363 49.791 1.00 9.29  ? 179 SER A CA  1 
ATOM   1331 C  C   . SER A 1 179 ? 5.480   16.695 49.731 1.00 8.45  ? 179 SER A C   1 
ATOM   1332 O  O   . SER A 1 179 ? 4.252   16.746 49.773 1.00 8.62  ? 179 SER A O   1 
ATOM   1333 C  CB  . SER A 1 179 ? 6.381   14.806 48.371 1.00 12.04 ? 179 SER A CB  1 
ATOM   1334 O  OG  . SER A 1 179 ? 6.343   15.828 47.390 1.00 13.78 ? 179 SER A OG  1 
ATOM   1335 N  N   . PRO A 1 180 ? 6.235   17.798 49.641 1.00 9.31  ? 180 PRO A N   1 
ATOM   1336 C  CA  . PRO A 1 180 ? 5.587   19.110 49.575 1.00 9.73  ? 180 PRO A CA  1 
ATOM   1337 C  C   . PRO A 1 180 ? 4.717   19.231 48.324 1.00 10.04 ? 180 PRO A C   1 
ATOM   1338 O  O   . PRO A 1 180 ? 3.898   20.141 48.210 1.00 10.03 ? 180 PRO A O   1 
ATOM   1339 C  CB  . PRO A 1 180 ? 6.753   20.102 49.579 1.00 7.25  ? 180 PRO A CB  1 
ATOM   1340 C  CG  . PRO A 1 180 ? 7.949   19.316 49.241 1.00 7.48  ? 180 PRO A CG  1 
ATOM   1341 C  CD  . PRO A 1 180 ? 7.703   17.892 49.616 1.00 6.21  ? 180 PRO A CD  1 
ATOM   1342 N  N   . ALA A 1 181 ? 4.896   18.300 47.391 1.00 9.55  ? 181 ALA A N   1 
ATOM   1343 C  CA  . ALA A 1 181 ? 4.119   18.309 46.161 1.00 9.62  ? 181 ALA A CA  1 
ATOM   1344 C  C   . ALA A 1 181 ? 2.642   18.072 46.464 1.00 10.50 ? 181 ALA A C   1 
ATOM   1345 O  O   . ALA A 1 181 ? 1.775   18.487 45.696 1.00 12.75 ? 181 ALA A O   1 
ATOM   1346 C  CB  . ALA A 1 181 ? 4.638   17.239 45.202 1.00 9.29  ? 181 ALA A CB  1 
ATOM   1347 N  N   . VAL A 1 182 ? 2.350   17.407 47.580 1.00 8.90  ? 182 VAL A N   1 
ATOM   1348 C  CA  . VAL A 1 182 ? 0.963   17.135 47.950 1.00 7.92  ? 182 VAL A CA  1 
ATOM   1349 C  C   . VAL A 1 182 ? 0.636   17.405 49.424 1.00 8.58  ? 182 VAL A C   1 
ATOM   1350 O  O   . VAL A 1 182 ? -0.535  17.432 49.798 1.00 8.34  ? 182 VAL A O   1 
ATOM   1351 C  CB  . VAL A 1 182 ? 0.569   15.665 47.631 1.00 8.45  ? 182 VAL A CB  1 
ATOM   1352 C  CG1 . VAL A 1 182 ? 0.696   15.401 46.142 1.00 8.42  ? 182 VAL A CG1 1 
ATOM   1353 C  CG2 . VAL A 1 182 ? 1.445   14.696 48.418 1.00 9.21  ? 182 VAL A CG2 1 
ATOM   1354 N  N   . ASN A 1 183 ? 1.662   17.612 50.251 1.00 8.62  ? 183 ASN A N   1 
ATOM   1355 C  CA  . ASN A 1 183 ? 1.472   17.849 51.686 1.00 8.13  ? 183 ASN A CA  1 
ATOM   1356 C  C   . ASN A 1 183 ? 1.851   19.245 52.162 1.00 9.10  ? 183 ASN A C   1 
ATOM   1357 O  O   . ASN A 1 183 ? 2.639   19.942 51.524 1.00 10.93 ? 183 ASN A O   1 
ATOM   1358 C  CB  . ASN A 1 183 ? 2.287   16.843 52.502 1.00 6.89  ? 183 ASN A CB  1 
ATOM   1359 C  CG  . ASN A 1 183 ? 1.823   15.418 52.308 1.00 7.86  ? 183 ASN A CG  1 
ATOM   1360 O  OD1 . ASN A 1 183 ? 2.569   14.579 51.799 1.00 8.53  ? 183 ASN A OD1 1 
ATOM   1361 N  ND2 . ASN A 1 183 ? 0.590   15.132 52.718 1.00 8.04  ? 183 ASN A ND2 1 
ATOM   1362 N  N   . HIS A 1 184 ? 1.297   19.633 53.307 1.00 8.07  ? 184 HIS A N   1 
ATOM   1363 C  CA  . HIS A 1 184 ? 1.567   20.938 53.904 1.00 7.70  ? 184 HIS A CA  1 
ATOM   1364 C  C   . HIS A 1 184 ? 3.064   21.111 54.173 1.00 7.43  ? 184 HIS A C   1 
ATOM   1365 O  O   . HIS A 1 184 ? 3.753   20.159 54.540 1.00 7.31  ? 184 HIS A O   1 
ATOM   1366 C  CB  . HIS A 1 184 ? 0.811   21.085 55.230 1.00 7.13  ? 184 HIS A CB  1 
ATOM   1367 C  CG  . HIS A 1 184 ? -0.678  20.988 55.101 1.00 7.37  ? 184 HIS A CG  1 
ATOM   1368 N  ND1 . HIS A 1 184 ? -1.365  21.454 54.001 1.00 7.96  ? 184 HIS A ND1 1 
ATOM   1369 C  CD2 . HIS A 1 184 ? -1.613  20.491 55.947 1.00 7.54  ? 184 HIS A CD2 1 
ATOM   1370 C  CE1 . HIS A 1 184 ? -2.660  21.250 54.175 1.00 7.91  ? 184 HIS A CE1 1 
ATOM   1371 N  NE2 . HIS A 1 184 ? -2.836  20.667 55.347 1.00 7.21  ? 184 HIS A NE2 1 
ATOM   1372 N  N   . TYR A 1 185 ? 3.557   22.334 54.002 1.00 7.08  ? 185 TYR A N   1 
ATOM   1373 C  CA  . TYR A 1 185 ? 4.962   22.626 54.235 1.00 7.07  ? 185 TYR A CA  1 
ATOM   1374 C  C   . TYR A 1 185 ? 5.107   23.995 54.876 1.00 8.07  ? 185 TYR A C   1 
ATOM   1375 O  O   . TYR A 1 185 ? 4.148   24.770 54.958 1.00 8.03  ? 185 TYR A O   1 
ATOM   1376 C  CB  . TYR A 1 185 ? 5.751   22.587 52.917 1.00 6.47  ? 185 TYR A CB  1 
ATOM   1377 C  CG  . TYR A 1 185 ? 5.254   23.554 51.861 1.00 6.21  ? 185 TYR A CG  1 
ATOM   1378 C  CD1 . TYR A 1 185 ? 5.694   24.880 51.832 1.00 6.34  ? 185 TYR A CD1 1 
ATOM   1379 C  CD2 . TYR A 1 185 ? 4.334   23.143 50.892 1.00 7.32  ? 185 TYR A CD2 1 
ATOM   1380 C  CE1 . TYR A 1 185 ? 5.230   25.774 50.864 1.00 7.35  ? 185 TYR A CE1 1 
ATOM   1381 C  CE2 . TYR A 1 185 ? 3.863   24.028 49.919 1.00 8.08  ? 185 TYR A CE2 1 
ATOM   1382 C  CZ  . TYR A 1 185 ? 4.314   25.339 49.911 1.00 10.01 ? 185 TYR A CZ  1 
ATOM   1383 O  OH  . TYR A 1 185 ? 3.841   26.208 48.952 1.00 8.86  ? 185 TYR A OH  1 
ATOM   1384 N  N   . ALA A 1 186 ? 6.319   24.295 55.321 1.00 7.47  ? 186 ALA A N   1 
ATOM   1385 C  CA  . ALA A 1 186 ? 6.594   25.571 55.962 1.00 8.42  ? 186 ALA A CA  1 
ATOM   1386 C  C   . ALA A 1 186 ? 8.072   25.906 55.875 1.00 7.97  ? 186 ALA A C   1 
ATOM   1387 O  O   . ALA A 1 186 ? 8.910   25.032 55.654 1.00 7.77  ? 186 ALA A O   1 
ATOM   1388 C  CB  . ALA A 1 186 ? 6.161   25.523 57.422 1.00 7.96  ? 186 ALA A CB  1 
ATOM   1389 N  N   . ALA A 1 187 ? 8.382   27.186 56.041 1.00 7.85  ? 187 ALA A N   1 
ATOM   1390 C  CA  . ALA A 1 187 ? 9.760   27.650 56.017 1.00 8.28  ? 187 ALA A CA  1 
ATOM   1391 C  C   . ALA A 1 187 ? 9.846   28.846 56.956 1.00 9.02  ? 187 ALA A C   1 
ATOM   1392 O  O   . ALA A 1 187 ? 8.947   29.696 56.983 1.00 9.00  ? 187 ALA A O   1 
ATOM   1393 C  CB  . ALA A 1 187 ? 10.168  28.041 54.605 1.00 5.55  ? 187 ALA A CB  1 
ATOM   1394 N  N   . PHE A 1 188 ? 10.918  28.891 57.741 1.00 9.34  ? 188 PHE A N   1 
ATOM   1395 C  CA  . PHE A 1 188 ? 11.140  29.967 58.698 1.00 8.95  ? 188 PHE A CA  1 
ATOM   1396 C  C   . PHE A 1 188 ? 12.574  30.461 58.576 1.00 9.67  ? 188 PHE A C   1 
ATOM   1397 O  O   . PHE A 1 188 ? 13.460  29.722 58.142 1.00 10.42 ? 188 PHE A O   1 
ATOM   1398 C  CB  . PHE A 1 188 ? 10.910  29.466 60.127 1.00 9.99  ? 188 PHE A CB  1 
ATOM   1399 C  CG  . PHE A 1 188 ? 9.508   28.985 60.394 1.00 10.13 ? 188 PHE A CG  1 
ATOM   1400 C  CD1 . PHE A 1 188 ? 9.140   27.673 60.104 1.00 10.85 ? 188 PHE A CD1 1 
ATOM   1401 C  CD2 . PHE A 1 188 ? 8.564   29.834 60.967 1.00 11.25 ? 188 PHE A CD2 1 
ATOM   1402 C  CE1 . PHE A 1 188 ? 7.855   27.213 60.382 1.00 10.82 ? 188 PHE A CE1 1 
ATOM   1403 C  CE2 . PHE A 1 188 ? 7.275   29.384 61.249 1.00 11.73 ? 188 PHE A CE2 1 
ATOM   1404 C  CZ  . PHE A 1 188 ? 6.920   28.070 60.957 1.00 10.60 ? 188 PHE A CZ  1 
ATOM   1405 N  N   . LEU A 1 189 ? 12.795  31.709 58.967 1.00 10.35 ? 189 LEU A N   1 
ATOM   1406 C  CA  . LEU A 1 189 ? 14.123  32.311 58.927 1.00 11.54 ? 189 LEU A CA  1 
ATOM   1407 C  C   . LEU A 1 189 ? 14.259  33.227 60.145 1.00 11.77 ? 189 LEU A C   1 
ATOM   1408 O  O   . LEU A 1 189 ? 13.484  34.172 60.304 1.00 11.34 ? 189 LEU A O   1 
ATOM   1409 C  CB  . LEU A 1 189 ? 14.297  33.112 57.631 1.00 14.99 ? 189 LEU A CB  1 
ATOM   1410 C  CG  . LEU A 1 189 ? 15.642  33.776 57.299 1.00 17.43 ? 189 LEU A CG  1 
ATOM   1411 C  CD1 . LEU A 1 189 ? 16.793  32.971 57.866 1.00 19.79 ? 189 LEU A CD1 1 
ATOM   1412 C  CD2 . LEU A 1 189 ? 15.781  33.882 55.787 1.00 19.23 ? 189 LEU A CD2 1 
ATOM   1413 N  N   . PHE A 1 190 ? 15.235  32.933 61.003 1.00 11.37 ? 190 PHE A N   1 
ATOM   1414 C  CA  . PHE A 1 190 ? 15.474  33.715 62.217 1.00 10.44 ? 190 PHE A CA  1 
ATOM   1415 C  C   . PHE A 1 190 ? 16.858  34.353 62.243 1.00 11.32 ? 190 PHE A C   1 
ATOM   1416 O  O   . PHE A 1 190 ? 17.858  33.702 61.946 1.00 11.45 ? 190 PHE A O   1 
ATOM   1417 C  CB  . PHE A 1 190 ? 15.363  32.833 63.468 1.00 11.19 ? 190 PHE A CB  1 
ATOM   1418 C  CG  . PHE A 1 190 ? 14.039  32.151 63.629 1.00 11.97 ? 190 PHE A CG  1 
ATOM   1419 C  CD1 . PHE A 1 190 ? 13.788  30.941 62.996 1.00 12.30 ? 190 PHE A CD1 1 
ATOM   1420 C  CD2 . PHE A 1 190 ? 13.047  32.711 64.428 1.00 13.77 ? 190 PHE A CD2 1 
ATOM   1421 C  CE1 . PHE A 1 190 ? 12.564  30.294 63.156 1.00 12.94 ? 190 PHE A CE1 1 
ATOM   1422 C  CE2 . PHE A 1 190 ? 11.819  32.071 64.596 1.00 13.47 ? 190 PHE A CE2 1 
ATOM   1423 C  CZ  . PHE A 1 190 ? 11.577  30.862 63.959 1.00 13.80 ? 190 PHE A CZ  1 
ATOM   1424 N  N   . ASP A 1 191 ? 16.916  35.626 62.614 1.00 10.56 ? 191 ASP A N   1 
ATOM   1425 C  CA  . ASP A 1 191 ? 18.191  36.318 62.729 1.00 10.53 ? 191 ASP A CA  1 
ATOM   1426 C  C   . ASP A 1 191 ? 18.778  35.876 64.073 1.00 10.09 ? 191 ASP A C   1 
ATOM   1427 O  O   . ASP A 1 191 ? 18.039  35.497 64.982 1.00 9.57  ? 191 ASP A O   1 
ATOM   1428 C  CB  . ASP A 1 191 ? 17.979  37.836 62.734 1.00 10.82 ? 191 ASP A CB  1 
ATOM   1429 C  CG  . ASP A 1 191 ? 19.279  38.608 62.641 1.00 12.78 ? 191 ASP A CG  1 
ATOM   1430 O  OD1 . ASP A 1 191 ? 19.767  38.829 61.514 1.00 16.43 ? 191 ASP A OD1 1 
ATOM   1431 O  OD2 . ASP A 1 191 ? 19.815  38.998 63.694 1.00 14.98 ? 191 ASP A OD2 1 
ATOM   1432 N  N   . GLN A 1 192 ? 20.098  35.911 64.189 1.00 11.16 ? 192 GLN A N   1 
ATOM   1433 C  CA  . GLN A 1 192 ? 20.767  35.532 65.427 1.00 11.72 ? 192 GLN A CA  1 
ATOM   1434 C  C   . GLN A 1 192 ? 20.266  36.391 66.587 1.00 12.65 ? 192 GLN A C   1 
ATOM   1435 O  O   . GLN A 1 192 ? 20.112  35.914 67.712 1.00 13.82 ? 192 GLN A O   1 
ATOM   1436 C  CB  . GLN A 1 192 ? 22.276  35.730 65.282 1.00 9.95  ? 192 GLN A CB  1 
ATOM   1437 C  CG  . GLN A 1 192 ? 23.007  34.550 64.677 1.00 8.55  ? 192 GLN A CG  1 
ATOM   1438 C  CD  . GLN A 1 192 ? 23.441  33.548 65.720 1.00 8.07  ? 192 GLN A CD  1 
ATOM   1439 O  OE1 . GLN A 1 192 ? 22.703  33.258 66.662 1.00 9.30  ? 192 GLN A OE1 1 
ATOM   1440 N  NE2 . GLN A 1 192 ? 24.646  33.012 65.562 1.00 9.03  ? 192 GLN A NE2 1 
ATOM   1441 N  N   . ASN A 1 193 ? 19.998  37.659 66.306 1.00 12.00 ? 193 ASN A N   1 
ATOM   1442 C  CA  . ASN A 1 193 ? 19.553  38.580 67.338 1.00 15.01 ? 193 ASN A CA  1 
ATOM   1443 C  C   . ASN A 1 193 ? 18.050  38.638 67.582 1.00 16.14 ? 193 ASN A C   1 
ATOM   1444 O  O   . ASN A 1 193 ? 17.536  39.658 68.034 1.00 17.46 ? 193 ASN A O   1 
ATOM   1445 C  CB  . ASN A 1 193 ? 20.082  39.982 67.029 1.00 20.63 ? 193 ASN A CB  1 
ATOM   1446 C  CG  . ASN A 1 193 ? 21.600  40.050 67.075 1.00 26.13 ? 193 ASN A CG  1 
ATOM   1447 O  OD1 . ASN A 1 193 ? 22.226  40.771 66.297 1.00 31.24 ? 193 ASN A OD1 1 
ATOM   1448 N  ND2 . ASN A 1 193 ? 22.199  39.292 67.989 1.00 26.48 ? 193 ASN A ND2 1 
ATOM   1449 N  N   . THR A 1 194 ? 17.342  37.553 67.295 1.00 15.07 ? 194 THR A N   1 
ATOM   1450 C  CA  . THR A 1 194 ? 15.901  37.532 67.523 1.00 14.99 ? 194 THR A CA  1 
ATOM   1451 C  C   . THR A 1 194 ? 15.646  37.629 69.029 1.00 16.57 ? 194 THR A C   1 
ATOM   1452 O  O   . THR A 1 194 ? 16.281  36.928 69.820 1.00 16.76 ? 194 THR A O   1 
ATOM   1453 C  CB  . THR A 1 194 ? 15.271  36.232 66.978 1.00 15.98 ? 194 THR A CB  1 
ATOM   1454 O  OG1 . THR A 1 194 ? 15.377  36.217 65.549 1.00 15.16 ? 194 THR A OG1 1 
ATOM   1455 C  CG2 . THR A 1 194 ? 13.800  36.138 67.366 1.00 14.49 ? 194 THR A CG2 1 
ATOM   1456 N  N   . PRO A 1 195 ? 14.716  38.507 69.447 1.00 17.02 ? 195 PRO A N   1 
ATOM   1457 C  CA  . PRO A 1 195 ? 14.410  38.665 70.874 1.00 17.48 ? 195 PRO A CA  1 
ATOM   1458 C  C   . PRO A 1 195 ? 13.947  37.362 71.524 1.00 17.64 ? 195 PRO A C   1 
ATOM   1459 O  O   . PRO A 1 195 ? 13.288  36.538 70.891 1.00 17.54 ? 195 PRO A O   1 
ATOM   1460 C  CB  . PRO A 1 195 ? 13.321  39.741 70.900 1.00 17.59 ? 195 PRO A CB  1 
ATOM   1461 C  CG  . PRO A 1 195 ? 13.425  40.432 69.581 1.00 18.85 ? 195 PRO A CG  1 
ATOM   1462 C  CD  . PRO A 1 195 ? 13.894  39.396 68.608 1.00 17.07 ? 195 PRO A CD  1 
ATOM   1463 N  N   . LYS A 1 196 ? 14.291  37.193 72.795 1.00 17.70 ? 196 LYS A N   1 
ATOM   1464 C  CA  . LYS A 1 196 ? 13.940  35.993 73.546 1.00 19.58 ? 196 LYS A CA  1 
ATOM   1465 C  C   . LYS A 1 196 ? 12.449  35.645 73.546 1.00 19.14 ? 196 LYS A C   1 
ATOM   1466 O  O   . LYS A 1 196 ? 12.084  34.471 73.484 1.00 20.12 ? 196 LYS A O   1 
ATOM   1467 C  CB  . LYS A 1 196 ? 14.436  36.134 74.991 1.00 24.90 ? 196 LYS A CB  1 
ATOM   1468 C  CG  . LYS A 1 196 ? 13.812  35.156 75.967 1.00 31.41 ? 196 LYS A CG  1 
ATOM   1469 C  CD  . LYS A 1 196 ? 14.670  33.917 76.131 1.00 33.75 ? 196 LYS A CD  1 
ATOM   1470 C  CE  . LYS A 1 196 ? 15.128  33.756 77.572 1.00 34.91 ? 196 LYS A CE  1 
ATOM   1471 N  NZ  . LYS A 1 196 ? 15.863  32.478 77.784 1.00 35.74 ? 196 LYS A NZ  1 
ATOM   1472 N  N   . GLY A 1 197 ? 11.589  36.654 73.613 1.00 18.45 ? 197 GLY A N   1 
ATOM   1473 C  CA  . GLY A 1 197 ? 10.161  36.386 73.641 1.00 18.49 ? 197 GLY A CA  1 
ATOM   1474 C  C   . GLY A 1 197 ? 9.443   36.443 72.307 1.00 18.41 ? 197 GLY A C   1 
ATOM   1475 O  O   . GLY A 1 197 ? 8.217   36.412 72.261 1.00 18.64 ? 197 GLY A O   1 
ATOM   1476 N  N   . ALA A 1 198 ? 10.199  36.515 71.217 1.00 18.67 ? 198 ALA A N   1 
ATOM   1477 C  CA  . ALA A 1 198 ? 9.612   36.590 69.884 1.00 18.16 ? 198 ALA A CA  1 
ATOM   1478 C  C   . ALA A 1 198 ? 8.727   35.398 69.529 1.00 17.24 ? 198 ALA A C   1 
ATOM   1479 O  O   . ALA A 1 198 ? 9.012   34.258 69.903 1.00 17.47 ? 198 ALA A O   1 
ATOM   1480 C  CB  . ALA A 1 198 ? 10.717  36.739 68.840 1.00 19.91 ? 198 ALA A CB  1 
ATOM   1481 N  N   . ASP A 1 199 ? 7.650   35.682 68.801 1.00 17.47 ? 199 ASP A N   1 
ATOM   1482 C  CA  . ASP A 1 199 ? 6.702   34.668 68.342 1.00 15.90 ? 199 ASP A CA  1 
ATOM   1483 C  C   . ASP A 1 199 ? 7.288   34.105 67.049 1.00 14.90 ? 199 ASP A C   1 
ATOM   1484 O  O   . ASP A 1 199 ? 7.466   34.841 66.077 1.00 14.47 ? 199 ASP A O   1 
ATOM   1485 C  CB  . ASP A 1 199 ? 5.342   35.321 68.072 1.00 15.23 ? 199 ASP A CB  1 
ATOM   1486 C  CG  . ASP A 1 199 ? 4.338   34.368 67.438 1.00 16.20 ? 199 ASP A CG  1 
ATOM   1487 O  OD1 . ASP A 1 199 ? 4.650   33.176 67.247 1.00 14.89 ? 199 ASP A OD1 1 
ATOM   1488 O  OD2 . ASP A 1 199 ? 3.222   34.825 67.127 1.00 20.62 ? 199 ASP A OD2 1 
ATOM   1489 N  N   . PHE A 1 200 ? 7.591   32.810 67.040 1.00 11.97 ? 200 PHE A N   1 
ATOM   1490 C  CA  . PHE A 1 200 ? 8.189   32.188 65.866 1.00 13.31 ? 200 PHE A CA  1 
ATOM   1491 C  C   . PHE A 1 200 ? 7.342   32.299 64.606 1.00 12.49 ? 200 PHE A C   1 
ATOM   1492 O  O   . PHE A 1 200 ? 7.865   32.229 63.496 1.00 12.66 ? 200 PHE A O   1 
ATOM   1493 C  CB  . PHE A 1 200 ? 8.547   30.719 66.158 1.00 13.40 ? 200 PHE A CB  1 
ATOM   1494 C  CG  . PHE A 1 200 ? 7.379   29.769 66.114 1.00 14.41 ? 200 PHE A CG  1 
ATOM   1495 C  CD1 . PHE A 1 200 ? 6.929   29.250 64.903 1.00 13.72 ? 200 PHE A CD1 1 
ATOM   1496 C  CD2 . PHE A 1 200 ? 6.761   29.355 67.287 1.00 14.28 ? 200 PHE A CD2 1 
ATOM   1497 C  CE1 . PHE A 1 200 ? 5.880   28.328 64.862 1.00 13.37 ? 200 PHE A CE1 1 
ATOM   1498 C  CE2 . PHE A 1 200 ? 5.711   28.434 67.254 1.00 15.83 ? 200 PHE A CE2 1 
ATOM   1499 C  CZ  . PHE A 1 200 ? 5.272   27.920 66.038 1.00 12.76 ? 200 PHE A CZ  1 
ATOM   1500 N  N   . CYS A 1 201 ? 6.042   32.498 64.781 1.00 12.37 ? 201 CYS A N   1 
ATOM   1501 C  CA  . CYS A 1 201 ? 5.122   32.621 63.657 1.00 12.32 ? 201 CYS A CA  1 
ATOM   1502 C  C   . CYS A 1 201 ? 5.403   33.826 62.772 1.00 12.91 ? 201 CYS A C   1 
ATOM   1503 O  O   . CYS A 1 201 ? 5.063   33.825 61.590 1.00 13.99 ? 201 CYS A O   1 
ATOM   1504 C  CB  . CYS A 1 201 ? 3.688   32.719 64.169 1.00 12.92 ? 201 CYS A CB  1 
ATOM   1505 S  SG  . CYS A 1 201 ? 3.113   31.211 64.994 1.00 13.71 ? 201 CYS A SG  1 
ATOM   1506 N  N   . GLN A 1 202 ? 6.018   34.853 63.344 1.00 11.76 ? 202 GLN A N   1 
ATOM   1507 C  CA  . GLN A 1 202 ? 6.316   36.069 62.600 1.00 13.54 ? 202 GLN A CA  1 
ATOM   1508 C  C   . GLN A 1 202 ? 7.488   35.950 61.636 1.00 13.28 ? 202 GLN A C   1 
ATOM   1509 O  O   . GLN A 1 202 ? 7.759   36.878 60.879 1.00 14.20 ? 202 GLN A O   1 
ATOM   1510 C  CB  . GLN A 1 202 ? 6.591   37.216 63.571 1.00 18.04 ? 202 GLN A CB  1 
ATOM   1511 C  CG  . GLN A 1 202 ? 5.524   37.379 64.634 1.00 27.51 ? 202 GLN A CG  1 
ATOM   1512 C  CD  . GLN A 1 202 ? 5.819   38.518 65.588 1.00 32.51 ? 202 GLN A CD  1 
ATOM   1513 O  OE1 . GLN A 1 202 ? 6.909   39.101 65.567 1.00 33.57 ? 202 GLN A OE1 1 
ATOM   1514 N  NE2 . GLN A 1 202 ? 4.845   38.844 66.435 1.00 33.57 ? 202 GLN A NE2 1 
ATOM   1515 N  N   . PHE A 1 203 ? 8.171   34.810 61.646 1.00 13.21 ? 203 PHE A N   1 
ATOM   1516 C  CA  . PHE A 1 203 ? 9.330   34.631 60.785 1.00 12.41 ? 203 PHE A CA  1 
ATOM   1517 C  C   . PHE A 1 203 ? 9.149   33.623 59.661 1.00 11.75 ? 203 PHE A C   1 
ATOM   1518 O  O   . PHE A 1 203 ? 10.103  32.985 59.215 1.00 11.01 ? 203 PHE A O   1 
ATOM   1519 C  CB  . PHE A 1 203 ? 10.536  34.282 61.653 1.00 13.34 ? 203 PHE A CB  1 
ATOM   1520 C  CG  . PHE A 1 203 ? 10.714  35.222 62.807 1.00 15.32 ? 203 PHE A CG  1 
ATOM   1521 C  CD1 . PHE A 1 203 ? 11.379  36.430 62.635 1.00 16.57 ? 203 PHE A CD1 1 
ATOM   1522 C  CD2 . PHE A 1 203 ? 10.160  34.932 64.048 1.00 15.98 ? 203 PHE A CD2 1 
ATOM   1523 C  CE1 . PHE A 1 203 ? 11.487  37.344 63.685 1.00 18.51 ? 203 PHE A CE1 1 
ATOM   1524 C  CE2 . PHE A 1 203 ? 10.260  35.834 65.105 1.00 17.53 ? 203 PHE A CE2 1 
ATOM   1525 C  CZ  . PHE A 1 203 ? 10.923  37.043 64.925 1.00 17.89 ? 203 PHE A CZ  1 
ATOM   1526 N  N   . ARG A 1 204 ? 7.915   33.496 59.196 1.00 11.02 ? 204 ARG A N   1 
ATOM   1527 C  CA  . ARG A 1 204 ? 7.610   32.594 58.100 1.00 10.92 ? 204 ARG A CA  1 
ATOM   1528 C  C   . ARG A 1 204 ? 8.132   33.227 56.808 1.00 11.10 ? 204 ARG A C   1 
ATOM   1529 O  O   . ARG A 1 204 ? 7.981   34.429 56.596 1.00 11.61 ? 204 ARG A O   1 
ATOM   1530 C  CB  . ARG A 1 204 ? 6.099   32.391 58.000 1.00 12.29 ? 204 ARG A CB  1 
ATOM   1531 C  CG  . ARG A 1 204 ? 5.527   31.468 59.063 1.00 14.25 ? 204 ARG A CG  1 
ATOM   1532 C  CD  . ARG A 1 204 ? 4.006   31.454 59.012 1.00 17.94 ? 204 ARG A CD  1 
ATOM   1533 N  NE  . ARG A 1 204 ? 3.422   32.592 59.721 1.00 21.68 ? 204 ARG A NE  1 
ATOM   1534 C  CZ  . ARG A 1 204 ? 2.117   32.764 59.911 1.00 23.63 ? 204 ARG A CZ  1 
ATOM   1535 N  NH1 . ARG A 1 204 ? 1.256   31.868 59.440 1.00 21.03 ? 204 ARG A NH1 1 
ATOM   1536 N  NH2 . ARG A 1 204 ? 1.673   33.822 60.585 1.00 20.60 ? 204 ARG A NH2 1 
ATOM   1537 N  N   . VAL A 1 205 ? 8.758   32.422 55.956 1.00 9.31  ? 205 VAL A N   1 
ATOM   1538 C  CA  . VAL A 1 205 ? 9.286   32.909 54.682 1.00 8.36  ? 205 VAL A CA  1 
ATOM   1539 C  C   . VAL A 1 205 ? 9.016   31.851 53.615 1.00 8.39  ? 205 VAL A C   1 
ATOM   1540 O  O   . VAL A 1 205 ? 8.359   30.849 53.883 1.00 9.28  ? 205 VAL A O   1 
ATOM   1541 C  CB  . VAL A 1 205 ? 10.821  33.161 54.750 1.00 7.45  ? 205 VAL A CB  1 
ATOM   1542 C  CG1 . VAL A 1 205 ? 11.133  34.258 55.760 1.00 6.02  ? 205 VAL A CG1 1 
ATOM   1543 C  CG2 . VAL A 1 205 ? 11.547  31.870 55.108 1.00 6.52  ? 205 VAL A CG2 1 
ATOM   1544 N  N   . THR A 1 206 ? 9.512   32.073 52.405 1.00 9.31  ? 206 THR A N   1 
ATOM   1545 C  CA  . THR A 1 206 ? 9.327   31.095 51.338 1.00 8.78  ? 206 THR A CA  1 
ATOM   1546 C  C   . THR A 1 206 ? 10.617  30.291 51.198 1.00 9.46  ? 206 THR A C   1 
ATOM   1547 O  O   . THR A 1 206 ? 11.679  30.731 51.639 1.00 10.02 ? 206 THR A O   1 
ATOM   1548 C  CB  . THR A 1 206 ? 9.020   31.773 49.985 1.00 8.66  ? 206 THR A CB  1 
ATOM   1549 O  OG1 . THR A 1 206 ? 10.137  32.581 49.589 1.00 10.02 ? 206 THR A OG1 1 
ATOM   1550 C  CG2 . THR A 1 206 ? 7.776   32.643 50.090 1.00 8.47  ? 206 THR A CG2 1 
ATOM   1551 N  N   . VAL A 1 207 ? 10.523  29.110 50.594 1.00 9.18  ? 207 VAL A N   1 
ATOM   1552 C  CA  . VAL A 1 207 ? 11.694  28.270 50.387 1.00 8.53  ? 207 VAL A CA  1 
ATOM   1553 C  C   . VAL A 1 207 ? 12.611  28.983 49.400 1.00 9.48  ? 207 VAL A C   1 
ATOM   1554 O  O   . VAL A 1 207 ? 13.833  28.895 49.489 1.00 9.43  ? 207 VAL A O   1 
ATOM   1555 C  CB  . VAL A 1 207 ? 11.298  26.892 49.810 1.00 7.72  ? 207 VAL A CB  1 
ATOM   1556 C  CG1 . VAL A 1 207 ? 12.545  26.092 49.449 1.00 8.06  ? 207 VAL A CG1 1 
ATOM   1557 C  CG2 . VAL A 1 207 ? 10.461  26.130 50.826 1.00 6.89  ? 207 VAL A CG2 1 
ATOM   1558 N  N   . ASP A 1 208 ? 11.999  29.695 48.461 1.00 9.57  ? 208 ASP A N   1 
ATOM   1559 C  CA  . ASP A 1 208 ? 12.726  30.437 47.441 1.00 10.03 ? 208 ASP A CA  1 
ATOM   1560 C  C   . ASP A 1 208 ? 13.672  31.468 48.073 1.00 8.77  ? 208 ASP A C   1 
ATOM   1561 O  O   . ASP A 1 208 ? 14.808  31.631 47.631 1.00 9.43  ? 208 ASP A O   1 
ATOM   1562 C  CB  . ASP A 1 208 ? 11.721  31.125 46.511 1.00 14.62 ? 208 ASP A CB  1 
ATOM   1563 C  CG  . ASP A 1 208 ? 12.387  31.975 45.453 1.00 19.36 ? 208 ASP A CG  1 
ATOM   1564 O  OD1 . ASP A 1 208 ? 13.188  31.433 44.659 1.00 21.02 ? 208 ASP A OD1 1 
ATOM   1565 O  OD2 . ASP A 1 208 ? 12.105  33.191 45.415 1.00 25.01 ? 208 ASP A OD2 1 
ATOM   1566 N  N   . GLU A 1 209 ? 13.206  32.160 49.109 1.00 8.30  ? 209 GLU A N   1 
ATOM   1567 C  CA  . GLU A 1 209 ? 14.040  33.154 49.775 1.00 8.26  ? 209 GLU A CA  1 
ATOM   1568 C  C   . GLU A 1 209 ? 15.275  32.498 50.384 1.00 9.10  ? 209 GLU A C   1 
ATOM   1569 O  O   . GLU A 1 209 ? 16.381  33.033 50.304 1.00 9.55  ? 209 GLU A O   1 
ATOM   1570 C  CB  . GLU A 1 209 ? 13.263  33.875 50.880 1.00 9.33  ? 209 GLU A CB  1 
ATOM   1571 C  CG  . GLU A 1 209 ? 14.147  34.802 51.705 1.00 11.61 ? 209 GLU A CG  1 
ATOM   1572 C  CD  . GLU A 1 209 ? 13.366  35.711 52.627 1.00 14.72 ? 209 GLU A CD  1 
ATOM   1573 O  OE1 . GLU A 1 209 ? 12.153  35.903 52.403 1.00 15.09 ? 209 GLU A OE1 1 
ATOM   1574 O  OE2 . GLU A 1 209 ? 13.972  36.238 53.581 1.00 17.07 ? 209 GLU A OE2 1 
ATOM   1575 N  N   . ILE A 1 210 ? 15.080  31.338 50.997 1.00 8.81  ? 210 ILE A N   1 
ATOM   1576 C  CA  . ILE A 1 210 ? 16.179  30.616 51.622 1.00 8.80  ? 210 ILE A CA  1 
ATOM   1577 C  C   . ILE A 1 210 ? 17.214  30.176 50.586 1.00 9.26  ? 210 ILE A C   1 
ATOM   1578 O  O   . ILE A 1 210 ? 18.420  30.351 50.780 1.00 9.88  ? 210 ILE A O   1 
ATOM   1579 C  CB  . ILE A 1 210 ? 15.642  29.393 52.393 1.00 7.61  ? 210 ILE A CB  1 
ATOM   1580 C  CG1 . ILE A 1 210 ? 14.812  29.880 53.583 1.00 7.71  ? 210 ILE A CG1 1 
ATOM   1581 C  CG2 . ILE A 1 210 ? 16.793  28.514 52.869 1.00 6.95  ? 210 ILE A CG2 1 
ATOM   1582 C  CD1 . ILE A 1 210 ? 14.071  28.776 54.309 1.00 12.32 ? 210 ILE A CD1 1 
ATOM   1583 N  N   . GLU A 1 211 ? 16.739  29.611 49.483 1.00 9.35  ? 211 GLU A N   1 
ATOM   1584 C  CA  . GLU A 1 211 ? 17.624  29.162 48.414 1.00 9.73  ? 211 GLU A CA  1 
ATOM   1585 C  C   . GLU A 1 211 ? 18.452  30.330 47.873 1.00 9.48  ? 211 GLU A C   1 
ATOM   1586 O  O   . GLU A 1 211 ? 19.647  30.196 47.621 1.00 11.34 ? 211 GLU A O   1 
ATOM   1587 C  CB  . GLU A 1 211 ? 16.799  28.539 47.281 1.00 8.64  ? 211 GLU A CB  1 
ATOM   1588 C  CG  . GLU A 1 211 ? 16.149  27.207 47.654 1.00 8.85  ? 211 GLU A CG  1 
ATOM   1589 C  CD  . GLU A 1 211 ? 15.459  26.535 46.481 1.00 12.33 ? 211 GLU A CD  1 
ATOM   1590 O  OE1 . GLU A 1 211 ? 15.034  27.251 45.550 1.00 11.70 ? 211 GLU A OE1 1 
ATOM   1591 O  OE2 . GLU A 1 211 ? 15.339  25.291 46.491 1.00 10.63 ? 211 GLU A OE2 1 
ATOM   1592 N  N   . LYS A 1 212 ? 17.814  31.482 47.713 1.00 10.31 ? 212 LYS A N   1 
ATOM   1593 C  CA  . LYS A 1 212 ? 18.500  32.657 47.192 1.00 12.04 ? 212 LYS A CA  1 
ATOM   1594 C  C   . LYS A 1 212 ? 19.543  33.224 48.152 1.00 12.44 ? 212 LYS A C   1 
ATOM   1595 O  O   . LYS A 1 212 ? 20.501  33.864 47.719 1.00 14.32 ? 212 LYS A O   1 
ATOM   1596 C  CB  . LYS A 1 212 ? 17.481  33.746 46.838 1.00 13.94 ? 212 LYS A CB  1 
ATOM   1597 C  CG  . LYS A 1 212 ? 16.699  33.458 45.563 1.00 17.26 ? 212 LYS A CG  1 
ATOM   1598 C  CD  . LYS A 1 212 ? 15.454  34.327 45.450 1.00 22.24 ? 212 LYS A CD  1 
ATOM   1599 C  CE  . LYS A 1 212 ? 14.929  34.339 44.015 1.00 28.15 ? 212 LYS A CE  1 
ATOM   1600 N  NZ  . LYS A 1 212 ? 13.658  35.108 43.873 1.00 29.32 ? 212 LYS A NZ  1 
ATOM   1601 N  N   . ARG A 1 213 ? 19.373  32.986 49.447 1.00 10.26 ? 213 ARG A N   1 
ATOM   1602 C  CA  . ARG A 1 213 ? 20.320  33.514 50.421 1.00 10.36 ? 213 ARG A CA  1 
ATOM   1603 C  C   . ARG A 1 213 ? 21.345  32.491 50.898 1.00 11.93 ? 213 ARG A C   1 
ATOM   1604 O  O   . ARG A 1 213 ? 22.225  32.818 51.696 1.00 12.93 ? 213 ARG A O   1 
ATOM   1605 C  CB  . ARG A 1 213 ? 19.561  34.099 51.615 1.00 9.31  ? 213 ARG A CB  1 
ATOM   1606 C  CG  . ARG A 1 213 ? 18.722  35.323 51.263 1.00 8.67  ? 213 ARG A CG  1 
ATOM   1607 C  CD  . ARG A 1 213 ? 17.769  35.699 52.390 1.00 8.87  ? 213 ARG A CD  1 
ATOM   1608 N  NE  . ARG A 1 213 ? 18.470  36.357 53.490 1.00 10.31 ? 213 ARG A NE  1 
ATOM   1609 C  CZ  . ARG A 1 213 ? 17.871  37.077 54.435 1.00 13.28 ? 213 ARG A CZ  1 
ATOM   1610 N  NH1 . ARG A 1 213 ? 16.554  37.233 54.414 1.00 10.04 ? 213 ARG A NH1 1 
ATOM   1611 N  NH2 . ARG A 1 213 ? 18.588  37.642 55.399 1.00 12.03 ? 213 ARG A NH2 1 
ATOM   1612 N  N   . THR A 1 214 ? 21.239  31.259 50.404 1.00 10.37 ? 214 THR A N   1 
ATOM   1613 C  CA  . THR A 1 214 ? 22.166  30.195 50.785 1.00 9.62  ? 214 THR A CA  1 
ATOM   1614 C  C   . THR A 1 214 ? 22.908  29.598 49.586 1.00 10.22 ? 214 THR A C   1 
ATOM   1615 O  O   . THR A 1 214 ? 24.001  29.055 49.735 1.00 11.29 ? 214 THR A O   1 
ATOM   1616 C  CB  . THR A 1 214 ? 21.437  29.038 51.492 1.00 9.27  ? 214 THR A CB  1 
ATOM   1617 O  OG1 . THR A 1 214 ? 20.450  28.493 50.610 1.00 9.09  ? 214 THR A OG1 1 
ATOM   1618 C  CG2 . THR A 1 214 ? 20.761  29.520 52.758 1.00 8.46  ? 214 THR A CG2 1 
ATOM   1619 N  N   . GLY A 1 215 ? 22.312  29.685 48.401 1.00 10.38 ? 215 GLY A N   1 
ATOM   1620 C  CA  . GLY A 1 215 ? 22.953  29.125 47.225 1.00 9.10  ? 215 GLY A CA  1 
ATOM   1621 C  C   . GLY A 1 215 ? 22.663  27.641 47.073 1.00 11.09 ? 215 GLY A C   1 
ATOM   1622 O  O   . GLY A 1 215 ? 23.283  26.956 46.256 1.00 12.08 ? 215 GLY A O   1 
ATOM   1623 N  N   . LEU A 1 216 ? 21.714  27.140 47.859 1.00 10.53 ? 216 LEU A N   1 
ATOM   1624 C  CA  . LEU A 1 216 ? 21.337  25.730 47.805 1.00 10.12 ? 216 LEU A CA  1 
ATOM   1625 C  C   . LEU A 1 216 ? 19.997  25.539 47.109 1.00 9.64  ? 216 LEU A C   1 
ATOM   1626 O  O   . LEU A 1 216 ? 19.224  26.479 46.951 1.00 11.18 ? 216 LEU A O   1 
ATOM   1627 C  CB  . LEU A 1 216 ? 21.205  25.144 49.216 1.00 9.91  ? 216 LEU A CB  1 
ATOM   1628 C  CG  . LEU A 1 216 ? 22.296  25.352 50.261 1.00 9.27  ? 216 LEU A CG  1 
ATOM   1629 C  CD1 . LEU A 1 216 ? 21.707  25.135 51.646 1.00 9.37  ? 216 LEU A CD1 1 
ATOM   1630 C  CD2 . LEU A 1 216 ? 23.430  24.383 50.011 1.00 7.90  ? 216 LEU A CD2 1 
ATOM   1631 N  N   . ILE A 1 217 ? 19.732  24.311 46.693 1.00 8.73  ? 217 ILE A N   1 
ATOM   1632 C  CA  . ILE A 1 217 ? 18.453  23.984 46.084 1.00 9.49  ? 217 ILE A CA  1 
ATOM   1633 C  C   . ILE A 1 217 ? 17.875  22.909 46.995 1.00 8.76  ? 217 ILE A C   1 
ATOM   1634 O  O   . ILE A 1 217 ? 18.398  21.797 47.077 1.00 9.20  ? 217 ILE A O   1 
ATOM   1635 C  CB  . ILE A 1 217 ? 18.604  23.429 44.655 1.00 9.21  ? 217 ILE A CB  1 
ATOM   1636 C  CG1 . ILE A 1 217 ? 19.120  24.530 43.722 1.00 10.72 ? 217 ILE A CG1 1 
ATOM   1637 C  CG2 . ILE A 1 217 ? 17.255  22.924 44.153 1.00 8.35  ? 217 ILE A CG2 1 
ATOM   1638 C  CD1 . ILE A 1 217 ? 19.457  24.042 42.328 1.00 15.47 ? 217 ILE A CD1 1 
ATOM   1639 N  N   . ILE A 1 218 ? 16.812  23.262 47.705 1.00 8.47  ? 218 ILE A N   1 
ATOM   1640 C  CA  . ILE A 1 218 ? 16.159  22.343 48.627 1.00 9.60  ? 218 ILE A CA  1 
ATOM   1641 C  C   . ILE A 1 218 ? 15.114  21.515 47.877 1.00 9.50  ? 218 ILE A C   1 
ATOM   1642 O  O   . ILE A 1 218 ? 14.573  21.966 46.864 1.00 10.45 ? 218 ILE A O   1 
ATOM   1643 C  CB  . ILE A 1 218 ? 15.524  23.149 49.796 1.00 11.27 ? 218 ILE A CB  1 
ATOM   1644 C  CG1 . ILE A 1 218 ? 16.640  23.626 50.733 1.00 13.80 ? 218 ILE A CG1 1 
ATOM   1645 C  CG2 . ILE A 1 218 ? 14.530  22.304 50.573 1.00 10.60 ? 218 ILE A CG2 1 
ATOM   1646 C  CD1 . ILE A 1 218 ? 16.695  25.123 50.913 1.00 15.66 ? 218 ILE A CD1 1 
ATOM   1647 N  N   . TRP A 1 219 ? 14.843  20.302 48.359 1.00 9.67  ? 219 TRP A N   1 
ATOM   1648 C  CA  . TRP A 1 219 ? 13.869  19.423 47.707 1.00 10.40 ? 219 TRP A CA  1 
ATOM   1649 C  C   . TRP A 1 219 ? 14.301  19.286 46.247 1.00 10.86 ? 219 TRP A C   1 
ATOM   1650 O  O   . TRP A 1 219 ? 13.484  19.392 45.329 1.00 10.55 ? 219 TRP A O   1 
ATOM   1651 C  CB  . TRP A 1 219 ? 12.468  20.040 47.764 1.00 9.00  ? 219 TRP A CB  1 
ATOM   1652 C  CG  . TRP A 1 219 ? 11.953  20.344 49.154 1.00 9.80  ? 219 TRP A CG  1 
ATOM   1653 C  CD1 . TRP A 1 219 ? 12.370  19.788 50.334 1.00 8.93  ? 219 TRP A CD1 1 
ATOM   1654 C  CD2 . TRP A 1 219 ? 10.893  21.250 49.492 1.00 8.92  ? 219 TRP A CD2 1 
ATOM   1655 N  NE1 . TRP A 1 219 ? 11.633  20.292 51.384 1.00 9.10  ? 219 TRP A NE1 1 
ATOM   1656 C  CE2 . TRP A 1 219 ? 10.720  21.189 50.896 1.00 9.70  ? 219 TRP A CE2 1 
ATOM   1657 C  CE3 . TRP A 1 219 ? 10.071  22.105 48.744 1.00 8.75  ? 219 TRP A CE3 1 
ATOM   1658 C  CZ2 . TRP A 1 219 ? 9.754   21.954 51.568 1.00 9.63  ? 219 TRP A CZ2 1 
ATOM   1659 C  CZ3 . TRP A 1 219 ? 9.110   22.867 49.413 1.00 10.09 ? 219 TRP A CZ3 1 
ATOM   1660 C  CH2 . TRP A 1 219 ? 8.962   22.784 50.813 1.00 10.55 ? 219 TRP A CH2 1 
ATOM   1661 N  N   . ALA A 1 220 ? 15.595  19.050 46.055 1.00 11.69 ? 220 ALA A N   1 
ATOM   1662 C  CA  . ALA A 1 220 ? 16.203  18.945 44.731 1.00 10.76 ? 220 ALA A CA  1 
ATOM   1663 C  C   . ALA A 1 220 ? 15.707  17.829 43.810 1.00 10.54 ? 220 ALA A C   1 
ATOM   1664 O  O   . ALA A 1 220 ? 16.035  17.819 42.622 1.00 11.28 ? 220 ALA A O   1 
ATOM   1665 C  CB  . ALA A 1 220 ? 17.717  18.854 44.884 1.00 8.85  ? 220 ALA A CB  1 
ATOM   1666 N  N   . GLY A 1 221 ? 14.917  16.902 44.340 1.00 9.29  ? 221 GLY A N   1 
ATOM   1667 C  CA  . GLY A 1 221 ? 14.417  15.813 43.516 1.00 9.17  ? 221 GLY A CA  1 
ATOM   1668 C  C   . GLY A 1 221 ? 13.013  16.025 42.975 1.00 10.03 ? 221 GLY A C   1 
ATOM   1669 O  O   . GLY A 1 221 ? 12.488  15.182 42.250 1.00 10.88 ? 221 GLY A O   1 
ATOM   1670 N  N   . LEU A 1 222 ? 12.401  17.151 43.321 1.00 11.20 ? 222 LEU A N   1 
ATOM   1671 C  CA  . LEU A 1 222 ? 11.049  17.462 42.866 1.00 11.52 ? 222 LEU A CA  1 
ATOM   1672 C  C   . LEU A 1 222 ? 11.010  17.890 41.402 1.00 12.59 ? 222 LEU A C   1 
ATOM   1673 O  O   . LEU A 1 222 ? 11.951  18.516 40.900 1.00 11.66 ? 222 LEU A O   1 
ATOM   1674 C  CB  . LEU A 1 222 ? 10.449  18.590 43.709 1.00 10.08 ? 222 LEU A CB  1 
ATOM   1675 C  CG  . LEU A 1 222 ? 10.059  18.317 45.164 1.00 11.73 ? 222 LEU A CG  1 
ATOM   1676 C  CD1 . LEU A 1 222 ? 9.507   19.601 45.769 1.00 12.46 ? 222 LEU A CD1 1 
ATOM   1677 C  CD2 . LEU A 1 222 ? 9.030   17.199 45.245 1.00 12.29 ? 222 LEU A CD2 1 
ATOM   1678 N  N   . PRO A 1 223 ? 9.923   17.541 40.689 1.00 13.69 ? 223 PRO A N   1 
ATOM   1679 C  CA  . PRO A 1 223 ? 9.823   17.939 39.281 1.00 14.03 ? 223 PRO A CA  1 
ATOM   1680 C  C   . PRO A 1 223 ? 9.962   19.461 39.185 1.00 14.42 ? 223 PRO A C   1 
ATOM   1681 O  O   . PRO A 1 223 ? 9.574   20.186 40.106 1.00 14.06 ? 223 PRO A O   1 
ATOM   1682 C  CB  . PRO A 1 223 ? 8.430   17.458 38.866 1.00 12.74 ? 223 PRO A CB  1 
ATOM   1683 C  CG  . PRO A 1 223 ? 8.118   16.339 39.824 1.00 13.81 ? 223 PRO A CG  1 
ATOM   1684 C  CD  . PRO A 1 223 ? 8.760   16.745 41.125 1.00 13.55 ? 223 PRO A CD  1 
ATOM   1685 N  N   . ASP A 1 224 ? 10.520  19.938 38.076 1.00 13.34 ? 224 ASP A N   1 
ATOM   1686 C  CA  . ASP A 1 224 ? 10.728  21.368 37.862 1.00 12.40 ? 224 ASP A CA  1 
ATOM   1687 C  C   . ASP A 1 224 ? 9.487   22.231 38.104 1.00 13.11 ? 224 ASP A C   1 
ATOM   1688 O  O   . ASP A 1 224 ? 9.554   23.249 38.800 1.00 11.27 ? 224 ASP A O   1 
ATOM   1689 C  CB  . ASP A 1 224 ? 11.221  21.615 36.435 1.00 13.98 ? 224 ASP A CB  1 
ATOM   1690 C  CG  . ASP A 1 224 ? 12.673  21.225 36.235 1.00 15.37 ? 224 ASP A CG  1 
ATOM   1691 O  OD1 . ASP A 1 224 ? 13.317  20.744 37.192 1.00 14.64 ? 224 ASP A OD1 1 
ATOM   1692 O  OD2 . ASP A 1 224 ? 13.168  21.405 35.106 1.00 15.88 ? 224 ASP A OD2 1 
ATOM   1693 N  N   . ASP A 1 225 ? 8.360   21.831 37.519 1.00 13.94 ? 225 ASP A N   1 
ATOM   1694 C  CA  . ASP A 1 225 ? 7.119   22.593 37.660 1.00 15.25 ? 225 ASP A CA  1 
ATOM   1695 C  C   . ASP A 1 225 ? 6.665   22.738 39.110 1.00 13.82 ? 225 ASP A C   1 
ATOM   1696 O  O   . ASP A 1 225 ? 6.187   23.796 39.512 1.00 14.63 ? 225 ASP A O   1 
ATOM   1697 C  CB  . ASP A 1 225 ? 6.002   21.950 36.831 1.00 18.08 ? 225 ASP A CB  1 
ATOM   1698 C  CG  . ASP A 1 225 ? 5.687   20.535 37.271 1.00 22.43 ? 225 ASP A CG  1 
ATOM   1699 O  OD1 . ASP A 1 225 ? 6.619   19.708 37.352 1.00 30.47 ? 225 ASP A OD1 1 
ATOM   1700 O  OD2 . ASP A 1 225 ? 4.504   20.246 37.535 1.00 30.69 ? 225 ASP A OD2 1 
ATOM   1701 N  N   . VAL A 1 226 ? 6.809   21.672 39.891 1.00 15.05 ? 226 VAL A N   1 
ATOM   1702 C  CA  . VAL A 1 226 ? 6.413   21.699 41.294 1.00 14.39 ? 226 VAL A CA  1 
ATOM   1703 C  C   . VAL A 1 226 ? 7.301   22.672 42.061 1.00 14.70 ? 226 VAL A C   1 
ATOM   1704 O  O   . VAL A 1 226 ? 6.820   23.449 42.887 1.00 14.92 ? 226 VAL A O   1 
ATOM   1705 C  CB  . VAL A 1 226 ? 6.520   20.296 41.928 1.00 14.57 ? 226 VAL A CB  1 
ATOM   1706 C  CG1 . VAL A 1 226 ? 6.230   20.370 43.419 1.00 13.93 ? 226 VAL A CG1 1 
ATOM   1707 C  CG2 . VAL A 1 226 ? 5.547   19.348 41.243 1.00 14.25 ? 226 VAL A CG2 1 
ATOM   1708 N  N   . GLN A 1 227 ? 8.600   22.633 41.772 1.00 14.30 ? 227 GLN A N   1 
ATOM   1709 C  CA  . GLN A 1 227 ? 9.561   23.509 42.431 1.00 13.58 ? 227 GLN A CA  1 
ATOM   1710 C  C   . GLN A 1 227 ? 9.264   24.974 42.140 1.00 14.22 ? 227 GLN A C   1 
ATOM   1711 O  O   . GLN A 1 227 ? 9.259   25.810 43.044 1.00 15.11 ? 227 GLN A O   1 
ATOM   1712 C  CB  . GLN A 1 227 ? 10.977  23.186 41.956 1.00 12.16 ? 227 GLN A CB  1 
ATOM   1713 C  CG  . GLN A 1 227 ? 11.503  21.851 42.435 1.00 11.09 ? 227 GLN A CG  1 
ATOM   1714 C  CD  . GLN A 1 227 ? 12.994  21.706 42.206 1.00 13.17 ? 227 GLN A CD  1 
ATOM   1715 O  OE1 . GLN A 1 227 ? 13.470  20.649 41.792 1.00 15.15 ? 227 GLN A OE1 1 
ATOM   1716 N  NE2 . GLN A 1 227 ? 13.739  22.772 42.473 1.00 9.41  ? 227 GLN A NE2 1 
ATOM   1717 N  N   . ALA A 1 228 ? 9.012   25.276 40.870 1.00 13.36 ? 228 ALA A N   1 
ATOM   1718 C  CA  . ALA A 1 228 ? 8.734   26.640 40.446 1.00 15.00 ? 228 ALA A CA  1 
ATOM   1719 C  C   . ALA A 1 228 ? 7.466   27.233 41.051 1.00 16.43 ? 228 ALA A C   1 
ATOM   1720 O  O   . ALA A 1 228 ? 7.448   28.401 41.433 1.00 19.60 ? 228 ALA A O   1 
ATOM   1721 C  CB  . ALA A 1 228 ? 8.656   26.704 38.924 1.00 14.24 ? 228 ALA A CB  1 
ATOM   1722 N  N   . SER A 1 229 ? 6.411   26.433 41.154 1.00 16.99 ? 229 SER A N   1 
ATOM   1723 C  CA  . SER A 1 229 ? 5.150   26.935 41.683 1.00 17.59 ? 229 SER A CA  1 
ATOM   1724 C  C   . SER A 1 229 ? 4.986   26.927 43.199 1.00 17.93 ? 229 SER A C   1 
ATOM   1725 O  O   . SER A 1 229 ? 4.278   27.774 43.745 1.00 20.24 ? 229 SER A O   1 
ATOM   1726 C  CB  . SER A 1 229 ? 3.984   26.178 41.049 1.00 17.10 ? 229 SER A CB  1 
ATOM   1727 O  OG  . SER A 1 229 ? 4.043   24.807 41.373 1.00 24.17 ? 229 SER A OG  1 
ATOM   1728 N  N   . LEU A 1 230 ? 5.639   25.997 43.889 1.00 15.35 ? 230 LEU A N   1 
ATOM   1729 C  CA  . LEU A 1 230 ? 5.489   25.922 45.340 1.00 14.05 ? 230 LEU A CA  1 
ATOM   1730 C  C   . LEU A 1 230 ? 6.555   26.625 46.183 1.00 14.64 ? 230 LEU A C   1 
ATOM   1731 O  O   . LEU A 1 230 ? 6.265   27.079 47.291 1.00 14.49 ? 230 LEU A O   1 
ATOM   1732 C  CB  . LEU A 1 230 ? 5.391   24.457 45.777 1.00 12.21 ? 230 LEU A CB  1 
ATOM   1733 C  CG  . LEU A 1 230 ? 4.148   23.672 45.338 1.00 13.15 ? 230 LEU A CG  1 
ATOM   1734 C  CD1 . LEU A 1 230 ? 4.164   22.291 45.975 1.00 13.68 ? 230 LEU A CD1 1 
ATOM   1735 C  CD2 . LEU A 1 230 ? 2.882   24.429 45.736 1.00 15.14 ? 230 LEU A CD2 1 
ATOM   1736 N  N   . LYS A 1 231 ? 7.776   26.729 45.669 1.00 13.01 ? 231 LYS A N   1 
ATOM   1737 C  CA  . LYS A 1 231 ? 8.854   27.346 46.433 1.00 12.47 ? 231 LYS A CA  1 
ATOM   1738 C  C   . LYS A 1 231 ? 8.705   28.837 46.697 1.00 13.21 ? 231 LYS A C   1 
ATOM   1739 O  O   . LYS A 1 231 ? 9.280   29.359 47.650 1.00 14.44 ? 231 LYS A O   1 
ATOM   1740 C  CB  . LYS A 1 231 ? 10.202  27.063 45.764 1.00 7.92  ? 231 LYS A CB  1 
ATOM   1741 C  CG  . LYS A 1 231 ? 10.729  25.672 46.079 1.00 7.62  ? 231 LYS A CG  1 
ATOM   1742 C  CD  . LYS A 1 231 ? 12.078  25.408 45.447 1.00 9.10  ? 231 LYS A CD  1 
ATOM   1743 C  CE  . LYS A 1 231 ? 12.418  23.930 45.509 1.00 7.98  ? 231 LYS A CE  1 
ATOM   1744 N  NZ  . LYS A 1 231 ? 13.818  23.669 45.087 1.00 7.30  ? 231 LYS A NZ  1 
ATOM   1745 N  N   . SER A 1 232 ? 7.928   29.525 45.870 1.00 14.24 ? 232 SER A N   1 
ATOM   1746 C  CA  . SER A 1 232 ? 7.736   30.960 46.055 1.00 14.42 ? 232 SER A CA  1 
ATOM   1747 C  C   . SER A 1 232 ? 6.426   31.265 46.778 1.00 13.43 ? 232 SER A C   1 
ATOM   1748 O  O   . SER A 1 232 ? 6.003   32.415 46.843 1.00 13.56 ? 232 SER A O   1 
ATOM   1749 C  CB  . SER A 1 232 ? 7.746   31.664 44.703 1.00 17.53 ? 232 SER A CB  1 
ATOM   1750 O  OG  . SER A 1 232 ? 6.916   30.972 43.788 1.00 25.04 ? 232 SER A OG  1 
ATOM   1751 N  N   . LYS A 1 233 ? 5.797   30.232 47.329 1.00 12.25 ? 233 LYS A N   1 
ATOM   1752 C  CA  . LYS A 1 233 ? 4.532   30.391 48.041 1.00 12.50 ? 233 LYS A CA  1 
ATOM   1753 C  C   . LYS A 1 233 ? 4.639   29.896 49.486 1.00 13.07 ? 233 LYS A C   1 
ATOM   1754 O  O   . LYS A 1 233 ? 4.948   28.730 49.725 1.00 13.66 ? 233 LYS A O   1 
ATOM   1755 C  CB  . LYS A 1 233 ? 3.433   29.610 47.309 1.00 12.99 ? 233 LYS A CB  1 
ATOM   1756 C  CG  . LYS A 1 233 ? 2.047   29.728 47.919 1.00 13.26 ? 233 LYS A CG  1 
ATOM   1757 C  CD  . LYS A 1 233 ? 1.527   31.154 47.845 1.00 18.32 ? 233 LYS A CD  1 
ATOM   1758 C  CE  . LYS A 1 233 ? 0.106   31.246 48.385 1.00 20.57 ? 233 LYS A CE  1 
ATOM   1759 N  NZ  . LYS A 1 233 ? -0.639  32.389 47.779 1.00 23.46 ? 233 LYS A NZ  1 
ATOM   1760 N  N   . PRO A 1 234 ? 4.403   30.780 50.470 1.00 12.82 ? 234 PRO A N   1 
ATOM   1761 C  CA  . PRO A 1 234 ? 4.493   30.336 51.867 1.00 12.85 ? 234 PRO A CA  1 
ATOM   1762 C  C   . PRO A 1 234 ? 3.469   29.231 52.118 1.00 12.13 ? 234 PRO A C   1 
ATOM   1763 O  O   . PRO A 1 234 ? 2.333   29.316 51.650 1.00 12.77 ? 234 PRO A O   1 
ATOM   1764 C  CB  . PRO A 1 234 ? 4.191   31.602 52.678 1.00 14.17 ? 234 PRO A CB  1 
ATOM   1765 C  CG  . PRO A 1 234 ? 4.417   32.744 51.726 1.00 14.72 ? 234 PRO A CG  1 
ATOM   1766 C  CD  . PRO A 1 234 ? 4.064   32.210 50.362 1.00 14.69 ? 234 PRO A CD  1 
ATOM   1767 N  N   . GLY A 1 235 ? 3.873   28.198 52.850 1.00 10.32 ? 235 GLY A N   1 
ATOM   1768 C  CA  . GLY A 1 235 ? 2.972   27.089 53.118 1.00 10.52 ? 235 GLY A CA  1 
ATOM   1769 C  C   . GLY A 1 235 ? 1.987   27.318 54.249 1.00 10.47 ? 235 GLY A C   1 
ATOM   1770 O  O   . GLY A 1 235 ? 2.101   28.292 54.991 1.00 10.97 ? 235 GLY A O   1 
ATOM   1771 N  N   . VAL A 1 236 ? 1.025   26.408 54.388 1.00 10.43 ? 236 VAL A N   1 
ATOM   1772 C  CA  . VAL A 1 236 ? 0.016   26.518 55.439 1.00 11.08 ? 236 VAL A CA  1 
ATOM   1773 C  C   . VAL A 1 236 ? 0.277   25.615 56.651 1.00 10.95 ? 236 VAL A C   1 
ATOM   1774 O  O   . VAL A 1 236 ? -0.539  25.564 57.572 1.00 10.65 ? 236 VAL A O   1 
ATOM   1775 C  CB  . VAL A 1 236 ? -1.403  26.206 54.894 1.00 9.70  ? 236 VAL A CB  1 
ATOM   1776 C  CG1 . VAL A 1 236 ? -1.664  27.023 53.637 1.00 10.94 ? 236 VAL A CG1 1 
ATOM   1777 C  CG2 . VAL A 1 236 ? -1.544  24.721 54.614 1.00 8.29  ? 236 VAL A CG2 1 
ATOM   1778 N  N   . LEU A 1 237 ? 1.405   24.909 56.657 1.00 9.35  ? 237 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 237 ? 1.722   24.038 57.785 1.00 9.60  ? 237 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 237 ? 1.759   24.795 59.126 1.00 9.53  ? 237 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 237 ? 1.330   24.263 60.150 1.00 10.13 ? 237 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 237 ? 3.059   23.324 57.556 1.00 8.02  ? 237 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 237 ? 3.480   22.333 58.651 1.00 8.89  ? 237 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 237 ? 2.452   21.205 58.744 1.00 9.28  ? 237 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 237 ? 4.860   21.768 58.343 1.00 7.71  ? 237 LEU A CD2 1 
ATOM   1786 N  N   . PRO A 1 238 ? 2.278   26.040 59.141 1.00 9.10  ? 238 PRO A N   1 
ATOM   1787 C  CA  . PRO A 1 238 ? 2.331   26.801 60.399 1.00 9.19  ? 238 PRO A CA  1 
ATOM   1788 C  C   . PRO A 1 238 ? 0.976   26.936 61.104 1.00 10.18 ? 238 PRO A C   1 
ATOM   1789 O  O   . PRO A 1 238 ? 0.914   27.073 62.330 1.00 8.37  ? 238 PRO A O   1 
ATOM   1790 C  CB  . PRO A 1 238 ? 2.896   28.157 59.980 1.00 8.88  ? 238 PRO A CB  1 
ATOM   1791 C  CG  . PRO A 1 238 ? 3.647   27.881 58.716 1.00 8.89  ? 238 PRO A CG  1 
ATOM   1792 C  CD  . PRO A 1 238 ? 2.864   26.802 58.021 1.00 8.78  ? 238 PRO A CD  1 
ATOM   1793 N  N   . GLU A 1 239 ? -0.105  26.901 60.330 1.00 10.45 ? 239 GLU A N   1 
ATOM   1794 C  CA  . GLU A 1 239 ? -1.443  27.011 60.902 1.00 11.34 ? 239 GLU A CA  1 
ATOM   1795 C  C   . GLU A 1 239 ? -1.735  25.824 61.812 1.00 11.99 ? 239 GLU A C   1 
ATOM   1796 O  O   . GLU A 1 239 ? -2.517  25.934 62.755 1.00 13.52 ? 239 GLU A O   1 
ATOM   1797 C  CB  . GLU A 1 239 ? -2.492  27.080 59.794 1.00 14.12 ? 239 GLU A CB  1 
ATOM   1798 C  CG  . GLU A 1 239 ? -3.074  28.462 59.595 1.00 14.49 ? 239 GLU A CG  1 
ATOM   1799 C  CD  . GLU A 1 239 ? -2.029  29.466 59.168 1.00 20.03 ? 239 GLU A CD  1 
ATOM   1800 O  OE1 . GLU A 1 239 ? -0.974  29.040 58.649 1.00 21.24 ? 239 GLU A OE1 1 
ATOM   1801 O  OE2 . GLU A 1 239 ? -2.260  30.681 59.353 1.00 22.38 ? 239 GLU A OE2 1 
ATOM   1802 N  N   . LEU A 1 240 ? -1.109  24.687 61.527 1.00 11.31 ? 240 LEU A N   1 
ATOM   1803 C  CA  . LEU A 1 240 ? -1.308  23.493 62.343 1.00 12.74 ? 240 LEU A CA  1 
ATOM   1804 C  C   . LEU A 1 240 ? -0.387  23.561 63.553 1.00 14.11 ? 240 LEU A C   1 
ATOM   1805 O  O   . LEU A 1 240 ? -0.476  22.739 64.463 1.00 14.15 ? 240 LEU A O   1 
ATOM   1806 C  CB  . LEU A 1 240 ? -0.993  22.233 61.539 1.00 14.23 ? 240 LEU A CB  1 
ATOM   1807 C  CG  . LEU A 1 240 ? -1.980  21.824 60.444 1.00 16.83 ? 240 LEU A CG  1 
ATOM   1808 C  CD1 . LEU A 1 240 ? -1.567  20.468 59.905 1.00 17.24 ? 240 LEU A CD1 1 
ATOM   1809 C  CD2 . LEU A 1 240 ? -3.404  21.771 60.994 1.00 18.36 ? 240 LEU A CD2 1 
ATOM   1810 N  N   . MET A 1 241 ? 0.496   24.554 63.551 1.00 15.01 ? 241 MET A N   1 
ATOM   1811 C  CA  . MET A 1 241 ? 1.446   24.745 64.637 1.00 16.95 ? 241 MET A CA  1 
ATOM   1812 C  C   . MET A 1 241 ? 1.044   25.910 65.535 1.00 17.94 ? 241 MET A C   1 
ATOM   1813 O  O   . MET A 1 241 ? 1.842   26.369 66.350 1.00 18.90 ? 241 MET A O   1 
ATOM   1814 C  CB  . MET A 1 241 ? 2.846   24.997 64.074 1.00 17.37 ? 241 MET A CB  1 
ATOM   1815 C  CG  . MET A 1 241 ? 3.367   23.887 63.183 1.00 18.03 ? 241 MET A CG  1 
ATOM   1816 S  SD  . MET A 1 241 ? 5.109   24.122 62.778 1.00 22.73 ? 241 MET A SD  1 
ATOM   1817 C  CE  . MET A 1 241 ? 4.991   24.472 61.042 1.00 21.78 ? 241 MET A CE  1 
ATOM   1818 N  N   . GLY A 1 242 ? -0.184  26.397 65.366 1.00 19.24 ? 242 GLY A N   1 
ATOM   1819 C  CA  . GLY A 1 242 ? -0.664  27.493 66.192 1.00 19.56 ? 242 GLY A CA  1 
ATOM   1820 C  C   . GLY A 1 242 ? -0.597  28.895 65.612 1.00 20.94 ? 242 GLY A C   1 
ATOM   1821 O  O   . GLY A 1 242 ? -1.094  29.836 66.230 1.00 23.07 ? 242 GLY A O   1 
ATOM   1822 N  N   . CYS A 1 243 ? 0.010   29.051 64.439 1.00 17.49 ? 243 CYS A N   1 
ATOM   1823 C  CA  . CYS A 1 243 ? 0.119   30.370 63.816 1.00 16.74 ? 243 CYS A CA  1 
ATOM   1824 C  C   . CYS A 1 243 ? -1.186  30.804 63.145 1.00 18.92 ? 243 CYS A C   1 
ATOM   1825 O  O   . CYS A 1 243 ? -2.025  29.973 62.796 1.00 17.64 ? 243 CYS A O   1 
ATOM   1826 C  CB  . CYS A 1 243 ? 1.248   30.372 62.783 1.00 14.83 ? 243 CYS A CB  1 
ATOM   1827 S  SG  . CYS A 1 243 ? 2.869   29.907 63.462 1.00 13.40 ? 243 CYS A SG  1 
ATOM   1828 N  N   . LYS A 1 244 ? -1.348  32.111 62.966 1.00 23.50 ? 244 LYS A N   1 
ATOM   1829 C  CA  . LYS A 1 244 ? -2.542  32.657 62.329 1.00 28.00 ? 244 LYS A CA  1 
ATOM   1830 C  C   . LYS A 1 244 ? -2.177  33.459 61.084 1.00 31.91 ? 244 LYS A C   1 
ATOM   1831 O  O   . LYS A 1 244 ? -1.055  33.956 60.959 1.00 31.98 ? 244 LYS A O   1 
ATOM   1832 C  CB  . LYS A 1 244 ? -3.303  33.556 63.307 1.00 34.55 ? 244 LYS A CB  1 
ATOM   1833 C  CG  . LYS A 1 244 ? -4.378  32.835 64.102 1.00 36.78 ? 244 LYS A CG  1 
ATOM   1834 C  CD  . LYS A 1 244 ? -3.826  32.305 65.414 1.00 37.54 ? 244 LYS A CD  1 
ATOM   1835 C  CE  . LYS A 1 244 ? -4.942  31.995 66.397 1.00 39.18 ? 244 LYS A CE  1 
ATOM   1836 N  NZ  . LYS A 1 244 ? -4.411  31.750 67.769 1.00 40.36 ? 244 LYS A NZ  1 
ATOM   1837 N  N   . ASN A 1 245 ? -3.130  33.575 60.163 1.00 35.34 ? 245 ASN A N   1 
ATOM   1838 C  CA  . ASN A 1 245 ? -2.932  34.321 58.923 1.00 36.25 ? 245 ASN A CA  1 
ATOM   1839 C  C   . ASN A 1 245 ? -1.675  33.890 58.166 1.00 36.58 ? 245 ASN A C   1 
ATOM   1840 O  O   . ASN A 1 245 ? -1.317  32.694 58.242 1.00 36.56 ? 245 ASN A O   1 
ATOM   1841 C  CB  . ASN A 1 245 ? -2.864  35.822 59.226 1.00 37.98 ? 245 ASN A CB  1 
ATOM   1842 C  CG  . ASN A 1 245 ? -3.696  36.212 60.435 1.00 39.15 ? 245 ASN A CG  1 
ATOM   1843 O  OD1 . ASN A 1 245 ? -3.220  36.911 61.333 1.00 39.82 ? 245 ASN A OD1 1 
ATOM   1844 N  ND2 . ASN A 1 245 ? -4.948  35.759 60.464 1.00 38.43 ? 245 ASN A ND2 1 
ATOM   1845 O  OXT . ASN A 1 245 ? -1.064  34.757 57.501 1.00 37.19 ? 245 ASN A OXT 1 
ATOM   1846 N  N   . ILE B 1 6   ? -21.156 4.629  49.193 1.00 27.48 ? 6   ILE B N   1 
ATOM   1847 C  CA  . ILE B 1 6   ? -20.316 5.490  48.363 1.00 24.84 ? 6   ILE B CA  1 
ATOM   1848 C  C   . ILE B 1 6   ? -19.976 6.778  49.108 1.00 22.40 ? 6   ILE B C   1 
ATOM   1849 O  O   . ILE B 1 6   ? -20.868 7.499  49.550 1.00 23.27 ? 6   ILE B O   1 
ATOM   1850 C  CB  . ILE B 1 6   ? -21.027 5.846  47.037 1.00 23.15 ? 6   ILE B CB  1 
ATOM   1851 C  CG1 . ILE B 1 6   ? -21.324 4.567  46.250 1.00 22.45 ? 6   ILE B CG1 1 
ATOM   1852 C  CG2 . ILE B 1 6   ? -20.160 6.776  46.210 1.00 22.52 ? 6   ILE B CG2 1 
ATOM   1853 C  CD1 . ILE B 1 6   ? -22.117 4.798  44.981 1.00 25.18 ? 6   ILE B CD1 1 
ATOM   1854 N  N   . ASP B 1 7   ? -18.684 7.060  49.245 1.00 19.33 ? 7   ASP B N   1 
ATOM   1855 C  CA  . ASP B 1 7   ? -18.224 8.261  49.944 1.00 16.24 ? 7   ASP B CA  1 
ATOM   1856 C  C   . ASP B 1 7   ? -17.587 9.244  48.971 1.00 14.82 ? 7   ASP B C   1 
ATOM   1857 O  O   . ASP B 1 7   ? -16.470 9.030  48.497 1.00 15.39 ? 7   ASP B O   1 
ATOM   1858 C  CB  . ASP B 1 7   ? -17.211 7.884  51.028 1.00 17.17 ? 7   ASP B CB  1 
ATOM   1859 C  CG  . ASP B 1 7   ? -16.877 9.045  51.955 1.00 19.57 ? 7   ASP B CG  1 
ATOM   1860 O  OD1 . ASP B 1 7   ? -17.313 10.185 51.683 1.00 17.78 ? 7   ASP B OD1 1 
ATOM   1861 O  OD2 . ASP B 1 7   ? -16.174 8.810  52.962 1.00 21.97 ? 7   ASP B OD2 1 
ATOM   1862 N  N   . ASN B 1 8   ? -18.301 10.326 48.678 1.00 12.42 ? 8   ASN B N   1 
ATOM   1863 C  CA  . ASN B 1 8   ? -17.805 11.339 47.754 1.00 11.19 ? 8   ASN B CA  1 
ATOM   1864 C  C   . ASN B 1 8   ? -17.283 12.556 48.504 1.00 11.00 ? 8   ASN B C   1 
ATOM   1865 O  O   . ASN B 1 8   ? -16.979 13.580 47.893 1.00 11.56 ? 8   ASN B O   1 
ATOM   1866 C  CB  . ASN B 1 8   ? -18.926 11.774 46.805 1.00 12.03 ? 8   ASN B CB  1 
ATOM   1867 C  CG  . ASN B 1 8   ? -19.339 10.673 45.846 1.00 13.30 ? 8   ASN B CG  1 
ATOM   1868 O  OD1 . ASN B 1 8   ? -18.494 9.972  45.299 1.00 14.56 ? 8   ASN B OD1 1 
ATOM   1869 N  ND2 . ASN B 1 8   ? -20.644 10.517 45.640 1.00 10.76 ? 8   ASN B ND2 1 
ATOM   1870 N  N   . CYS B 1 9   ? -17.163 12.438 49.825 1.00 9.67  ? 9   CYS B N   1 
ATOM   1871 C  CA  . CYS B 1 9   ? -16.712 13.556 50.647 1.00 10.04 ? 9   CYS B CA  1 
ATOM   1872 C  C   . CYS B 1 9   ? -15.411 13.314 51.414 1.00 9.75  ? 9   CYS B C   1 
ATOM   1873 O  O   . CYS B 1 9   ? -14.684 14.261 51.715 1.00 10.74 ? 9   CYS B O   1 
ATOM   1874 C  CB  . CYS B 1 9   ? -17.836 13.947 51.609 1.00 11.09 ? 9   CYS B CB  1 
ATOM   1875 S  SG  . CYS B 1 9   ? -19.360 14.460 50.744 1.00 12.12 ? 9   CYS B SG  1 
ATOM   1876 N  N   . ALA B 1 10  ? -15.133 12.052 51.733 1.00 8.38  ? 10  ALA B N   1 
ATOM   1877 C  CA  . ALA B 1 10  ? -13.915 11.657 52.439 1.00 7.93  ? 10  ALA B CA  1 
ATOM   1878 C  C   . ALA B 1 10  ? -13.763 12.163 53.878 1.00 8.13  ? 10  ALA B C   1 
ATOM   1879 O  O   . ALA B 1 10  ? -13.413 11.397 54.766 1.00 9.22  ? 10  ALA B O   1 
ATOM   1880 C  CB  . ALA B 1 10  ? -12.691 12.059 51.618 1.00 8.59  ? 10  ALA B CB  1 
ATOM   1881 N  N   . VAL B 1 11  ? -14.009 13.445 54.113 1.00 7.69  ? 11  VAL B N   1 
ATOM   1882 C  CA  . VAL B 1 11  ? -13.871 13.995 55.459 1.00 7.45  ? 11  VAL B CA  1 
ATOM   1883 C  C   . VAL B 1 11  ? -15.190 14.553 55.983 1.00 8.55  ? 11  VAL B C   1 
ATOM   1884 O  O   . VAL B 1 11  ? -15.209 15.506 56.760 1.00 8.10  ? 11  VAL B O   1 
ATOM   1885 C  CB  . VAL B 1 11  ? -12.790 15.108 55.505 1.00 8.84  ? 11  VAL B CB  1 
ATOM   1886 C  CG1 . VAL B 1 11  ? -11.411 14.492 55.327 1.00 9.46  ? 11  VAL B CG1 1 
ATOM   1887 C  CG2 . VAL B 1 11  ? -13.046 16.145 54.422 1.00 9.38  ? 11  VAL B CG2 1 
ATOM   1888 N  N   . GLY B 1 12  ? -16.289 13.942 55.551 1.00 9.67  ? 12  GLY B N   1 
ATOM   1889 C  CA  . GLY B 1 12  ? -17.607 14.376 55.979 1.00 10.58 ? 12  GLY B CA  1 
ATOM   1890 C  C   . GLY B 1 12  ? -18.263 15.344 55.013 1.00 10.50 ? 12  GLY B C   1 
ATOM   1891 O  O   . GLY B 1 12  ? -17.706 16.398 54.704 1.00 10.29 ? 12  GLY B O   1 
ATOM   1892 N  N   . CYS B 1 13  ? -19.448 14.987 54.524 1.00 9.42  ? 13  CYS B N   1 
ATOM   1893 C  CA  . CYS B 1 13  ? -20.167 15.856 53.601 1.00 9.32  ? 13  CYS B CA  1 
ATOM   1894 C  C   . CYS B 1 13  ? -20.649 17.074 54.385 1.00 8.95  ? 13  CYS B C   1 
ATOM   1895 O  O   . CYS B 1 13  ? -20.768 17.026 55.606 1.00 9.25  ? 13  CYS B O   1 
ATOM   1896 C  CB  . CYS B 1 13  ? -21.351 15.114 52.973 1.00 9.94  ? 13  CYS B CB  1 
ATOM   1897 S  SG  . CYS B 1 13  ? -20.864 13.723 51.894 1.00 11.67 ? 13  CYS B SG  1 
ATOM   1898 N  N   . PRO B 1 14  ? -20.936 18.182 53.693 1.00 9.22  ? 14  PRO B N   1 
ATOM   1899 C  CA  . PRO B 1 14  ? -21.391 19.377 54.410 1.00 9.13  ? 14  PRO B CA  1 
ATOM   1900 C  C   . PRO B 1 14  ? -22.678 19.216 55.210 1.00 9.45  ? 14  PRO B C   1 
ATOM   1901 O  O   . PRO B 1 14  ? -23.554 18.429 54.853 1.00 8.85  ? 14  PRO B O   1 
ATOM   1902 C  CB  . PRO B 1 14  ? -21.542 20.433 53.307 1.00 9.21  ? 14  PRO B CB  1 
ATOM   1903 C  CG  . PRO B 1 14  ? -20.748 19.901 52.141 1.00 9.38  ? 14  PRO B CG  1 
ATOM   1904 C  CD  . PRO B 1 14  ? -20.867 18.405 52.238 1.00 9.44  ? 14  PRO B CD  1 
ATOM   1905 N  N   . THR B 1 15  ? -22.771 19.963 56.307 1.00 8.46  ? 15  THR B N   1 
ATOM   1906 C  CA  . THR B 1 15  ? -23.966 19.964 57.135 1.00 10.21 ? 15  THR B CA  1 
ATOM   1907 C  C   . THR B 1 15  ? -24.584 21.331 56.892 1.00 9.86  ? 15  THR B C   1 
ATOM   1908 O  O   . THR B 1 15  ? -23.915 22.230 56.379 1.00 9.25  ? 15  THR B O   1 
ATOM   1909 C  CB  . THR B 1 15  ? -23.644 19.820 58.645 1.00 8.79  ? 15  THR B CB  1 
ATOM   1910 O  OG1 . THR B 1 15  ? -22.731 20.847 59.044 1.00 8.53  ? 15  THR B OG1 1 
ATOM   1911 C  CG2 . THR B 1 15  ? -23.044 18.457 58.939 1.00 8.72  ? 15  THR B CG2 1 
ATOM   1912 N  N   . GLY B 1 16  ? -25.855 21.493 57.243 1.00 10.96 ? 16  GLY B N   1 
ATOM   1913 C  CA  . GLY B 1 16  ? -26.503 22.777 57.043 1.00 11.46 ? 16  GLY B CA  1 
ATOM   1914 C  C   . GLY B 1 16  ? -27.376 22.858 55.803 1.00 12.00 ? 16  GLY B C   1 
ATOM   1915 O  O   . GLY B 1 16  ? -27.983 23.893 55.547 1.00 11.72 ? 16  GLY B O   1 
ATOM   1916 N  N   . GLY B 1 17  ? -27.436 21.778 55.027 1.00 13.29 ? 17  GLY B N   1 
ATOM   1917 C  CA  . GLY B 1 17  ? -28.263 21.778 53.832 1.00 14.70 ? 17  GLY B CA  1 
ATOM   1918 C  C   . GLY B 1 17  ? -29.737 21.740 54.201 1.00 16.11 ? 17  GLY B C   1 
ATOM   1919 O  O   . GLY B 1 17  ? -30.106 21.168 55.227 1.00 16.22 ? 17  GLY B O   1 
ATOM   1920 N  N   . SER B 1 18  ? -30.583 22.333 53.363 1.00 16.22 ? 18  SER B N   1 
ATOM   1921 C  CA  . SER B 1 18  ? -32.022 22.382 53.624 1.00 16.20 ? 18  SER B CA  1 
ATOM   1922 C  C   . SER B 1 18  ? -32.714 21.024 53.715 1.00 17.10 ? 18  SER B C   1 
ATOM   1923 O  O   . SER B 1 18  ? -33.734 20.900 54.386 1.00 18.60 ? 18  SER B O   1 
ATOM   1924 C  CB  . SER B 1 18  ? -32.718 23.234 52.559 1.00 16.93 ? 18  SER B CB  1 
ATOM   1925 O  OG  . SER B 1 18  ? -32.602 22.643 51.277 1.00 16.72 ? 18  SER B OG  1 
ATOM   1926 N  N   . SER B 1 19  ? -32.175 20.014 53.039 1.00 17.38 ? 19  SER B N   1 
ATOM   1927 C  CA  . SER B 1 19  ? -32.762 18.675 53.071 1.00 19.83 ? 19  SER B CA  1 
ATOM   1928 C  C   . SER B 1 19  ? -32.003 17.794 54.049 1.00 21.90 ? 19  SER B C   1 
ATOM   1929 O  O   . SER B 1 19  ? -30.773 17.838 54.103 1.00 22.86 ? 19  SER B O   1 
ATOM   1930 C  CB  . SER B 1 19  ? -32.711 18.024 51.687 1.00 21.80 ? 19  SER B CB  1 
ATOM   1931 O  OG  . SER B 1 19  ? -33.455 18.767 50.742 1.00 30.88 ? 19  SER B OG  1 
ATOM   1932 N  N   . ASN B 1 20  ? -32.734 16.994 54.818 1.00 23.86 ? 20  ASN B N   1 
ATOM   1933 C  CA  . ASN B 1 20  ? -32.116 16.100 55.790 1.00 26.03 ? 20  ASN B CA  1 
ATOM   1934 C  C   . ASN B 1 20  ? -31.543 14.891 55.075 1.00 26.51 ? 20  ASN B C   1 
ATOM   1935 O  O   . ASN B 1 20  ? -30.688 14.188 55.610 1.00 30.39 ? 20  ASN B O   1 
ATOM   1936 C  CB  . ASN B 1 20  ? -33.145 15.642 56.821 1.00 36.98 ? 20  ASN B CB  1 
ATOM   1937 C  CG  . ASN B 1 20  ? -34.282 16.627 56.978 1.00 39.71 ? 20  ASN B CG  1 
ATOM   1938 O  OD1 . ASN B 1 20  ? -34.126 17.672 57.610 1.00 41.60 ? 20  ASN B OD1 1 
ATOM   1939 N  ND2 . ASN B 1 20  ? -35.435 16.302 56.399 1.00 40.96 ? 20  ASN B ND2 1 
ATOM   1940 N  N   . VAL B 1 21  ? -32.021 14.654 53.860 1.00 24.70 ? 21  VAL B N   1 
ATOM   1941 C  CA  . VAL B 1 21  ? -31.555 13.528 53.065 1.00 24.65 ? 21  VAL B CA  1 
ATOM   1942 C  C   . VAL B 1 21  ? -30.841 13.999 51.807 1.00 22.85 ? 21  VAL B C   1 
ATOM   1943 O  O   . VAL B 1 21  ? -31.304 14.910 51.116 1.00 23.71 ? 21  VAL B O   1 
ATOM   1944 C  CB  . VAL B 1 21  ? -32.724 12.621 52.635 1.00 27.42 ? 21  VAL B CB  1 
ATOM   1945 C  CG1 . VAL B 1 21  ? -32.635 11.290 53.355 1.00 28.88 ? 21  VAL B CG1 1 
ATOM   1946 C  CG2 . VAL B 1 21  ? -34.052 13.306 52.927 1.00 31.38 ? 21  VAL B CG2 1 
ATOM   1947 N  N   . SER B 1 22  ? -29.707 13.376 51.517 1.00 19.16 ? 22  SER B N   1 
ATOM   1948 C  CA  . SER B 1 22  ? -28.942 13.718 50.332 1.00 17.36 ? 22  SER B CA  1 
ATOM   1949 C  C   . SER B 1 22  ? -29.053 12.554 49.366 1.00 16.66 ? 22  SER B C   1 
ATOM   1950 O  O   . SER B 1 22  ? -29.312 11.426 49.779 1.00 17.79 ? 22  SER B O   1 
ATOM   1951 C  CB  . SER B 1 22  ? -27.471 13.948 50.688 1.00 16.24 ? 22  SER B CB  1 
ATOM   1952 O  OG  . SER B 1 22  ? -27.325 15.080 51.525 1.00 18.09 ? 22  SER B OG  1 
ATOM   1953 N  N   . ILE B 1 23  ? -28.873 12.833 48.081 1.00 12.89 ? 23  ILE B N   1 
ATOM   1954 C  CA  . ILE B 1 23  ? -28.927 11.799 47.057 1.00 12.13 ? 23  ILE B CA  1 
ATOM   1955 C  C   . ILE B 1 23  ? -27.492 11.354 46.810 1.00 11.46 ? 23  ILE B C   1 
ATOM   1956 O  O   . ILE B 1 23  ? -26.625 12.176 46.511 1.00 11.10 ? 23  ILE B O   1 
ATOM   1957 C  CB  . ILE B 1 23  ? -29.534 12.349 45.750 1.00 14.05 ? 23  ILE B CB  1 
ATOM   1958 C  CG1 . ILE B 1 23  ? -31.027 12.611 45.952 1.00 14.85 ? 23  ILE B CG1 1 
ATOM   1959 C  CG2 . ILE B 1 23  ? -29.312 11.363 44.611 1.00 15.16 ? 23  ILE B CG2 1 
ATOM   1960 C  CD1 . ILE B 1 23  ? -31.690 13.307 44.787 1.00 20.06 ? 23  ILE B CD1 1 
ATOM   1961 N  N   . VAL B 1 24  ? -27.237 10.058 46.952 1.00 10.53 ? 24  VAL B N   1 
ATOM   1962 C  CA  . VAL B 1 24  ? -25.895 9.527  46.762 1.00 11.12 ? 24  VAL B CA  1 
ATOM   1963 C  C   . VAL B 1 24  ? -25.787 8.707  45.482 1.00 12.24 ? 24  VAL B C   1 
ATOM   1964 O  O   . VAL B 1 24  ? -26.535 7.755  45.272 1.00 13.16 ? 24  VAL B O   1 
ATOM   1965 C  CB  . VAL B 1 24  ? -25.471 8.658  47.976 1.00 11.51 ? 24  VAL B CB  1 
ATOM   1966 C  CG1 . VAL B 1 24  ? -24.081 8.072  47.760 1.00 11.39 ? 24  VAL B CG1 1 
ATOM   1967 C  CG2 . VAL B 1 24  ? -25.489 9.506  49.239 1.00 11.16 ? 24  VAL B CG2 1 
ATOM   1968 N  N   . ARG B 1 25  ? -24.850 9.095  44.625 1.00 10.82 ? 25  ARG B N   1 
ATOM   1969 C  CA  . ARG B 1 25  ? -24.628 8.405  43.363 1.00 11.08 ? 25  ARG B CA  1 
ATOM   1970 C  C   . ARG B 1 25  ? -23.129 8.250  43.158 1.00 11.40 ? 25  ARG B C   1 
ATOM   1971 O  O   . ARG B 1 25  ? -22.336 8.807  43.916 1.00 10.93 ? 25  ARG B O   1 
ATOM   1972 C  CB  . ARG B 1 25  ? -25.235 9.212  42.210 1.00 12.04 ? 25  ARG B CB  1 
ATOM   1973 C  CG  . ARG B 1 25  ? -26.751 9.322  42.287 1.00 11.02 ? 25  ARG B CG  1 
ATOM   1974 C  CD  . ARG B 1 25  ? -27.317 10.284 41.258 1.00 11.97 ? 25  ARG B CD  1 
ATOM   1975 N  NE  . ARG B 1 25  ? -28.752 10.076 41.094 1.00 12.10 ? 25  ARG B NE  1 
ATOM   1976 C  CZ  . ARG B 1 25  ? -29.651 11.049 41.001 1.00 12.82 ? 25  ARG B CZ  1 
ATOM   1977 N  NH1 . ARG B 1 25  ? -29.274 12.318 41.054 1.00 10.47 ? 25  ARG B NH1 1 
ATOM   1978 N  NH2 . ARG B 1 25  ? -30.937 10.749 40.870 1.00 14.23 ? 25  ARG B NH2 1 
ATOM   1979 N  N   . HIS B 1 26  ? -22.735 7.483  42.149 1.00 11.72 ? 26  HIS B N   1 
ATOM   1980 C  CA  . HIS B 1 26  ? -21.321 7.307  41.876 1.00 12.29 ? 26  HIS B CA  1 
ATOM   1981 C  C   . HIS B 1 26  ? -20.806 8.627  41.320 1.00 12.71 ? 26  HIS B C   1 
ATOM   1982 O  O   . HIS B 1 26  ? -19.672 9.029  41.581 1.00 13.68 ? 26  HIS B O   1 
ATOM   1983 C  CB  . HIS B 1 26  ? -21.106 6.196  40.850 1.00 15.12 ? 26  HIS B CB  1 
ATOM   1984 C  CG  . HIS B 1 26  ? -21.328 4.818  41.392 1.00 18.35 ? 26  HIS B CG  1 
ATOM   1985 N  ND1 . HIS B 1 26  ? -20.361 4.126  42.091 1.00 19.27 ? 26  HIS B ND1 1 
ATOM   1986 C  CD2 . HIS B 1 26  ? -22.406 3.999  41.333 1.00 19.34 ? 26  HIS B CD2 1 
ATOM   1987 C  CE1 . HIS B 1 26  ? -20.833 2.942  42.438 1.00 19.92 ? 26  HIS B CE1 1 
ATOM   1988 N  NE2 . HIS B 1 26  ? -22.071 2.840  41.991 1.00 20.75 ? 26  HIS B NE2 1 
ATOM   1989 N  N   . ALA B 1 27  ? -21.658 9.309  40.560 1.00 10.90 ? 27  ALA B N   1 
ATOM   1990 C  CA  . ALA B 1 27  ? -21.286 10.578 39.951 1.00 10.40 ? 27  ALA B CA  1 
ATOM   1991 C  C   . ALA B 1 27  ? -21.097 11.686 40.980 1.00 10.39 ? 27  ALA B C   1 
ATOM   1992 O  O   . ALA B 1 27  ? -20.202 12.520 40.840 1.00 11.08 ? 27  ALA B O   1 
ATOM   1993 C  CB  . ALA B 1 27  ? -22.338 10.994 38.922 1.00 10.02 ? 27  ALA B CB  1 
ATOM   1994 N  N   . TYR B 1 28  ? -21.936 11.692 42.012 1.00 7.92  ? 28  TYR B N   1 
ATOM   1995 C  CA  . TYR B 1 28  ? -21.852 12.722 43.041 1.00 8.79  ? 28  TYR B CA  1 
ATOM   1996 C  C   . TYR B 1 28  ? -22.833 12.464 44.168 1.00 8.92  ? 28  TYR B C   1 
ATOM   1997 O  O   . TYR B 1 28  ? -23.627 11.526 44.122 1.00 9.25  ? 28  TYR B O   1 
ATOM   1998 C  CB  . TYR B 1 28  ? -22.181 14.090 42.433 1.00 9.51  ? 28  TYR B CB  1 
ATOM   1999 C  CG  . TYR B 1 28  ? -23.500 14.096 41.689 1.00 10.11 ? 28  TYR B CG  1 
ATOM   2000 C  CD1 . TYR B 1 28  ? -24.714 13.997 42.378 1.00 10.81 ? 28  TYR B CD1 1 
ATOM   2001 C  CD2 . TYR B 1 28  ? -23.538 14.143 40.294 1.00 9.30  ? 28  TYR B CD2 1 
ATOM   2002 C  CE1 . TYR B 1 28  ? -25.931 13.938 41.697 1.00 11.65 ? 28  TYR B CE1 1 
ATOM   2003 C  CE2 . TYR B 1 28  ? -24.752 14.086 39.601 1.00 10.13 ? 28  TYR B CE2 1 
ATOM   2004 C  CZ  . TYR B 1 28  ? -25.944 13.981 40.309 1.00 12.00 ? 28  TYR B CZ  1 
ATOM   2005 O  OH  . TYR B 1 28  ? -27.147 13.915 39.634 1.00 10.85 ? 28  TYR B OH  1 
ATOM   2006 N  N   . THR B 1 29  ? -22.757 13.316 45.182 1.00 10.51 ? 29  THR B N   1 
ATOM   2007 C  CA  . THR B 1 29  ? -23.668 13.268 46.317 1.00 10.22 ? 29  THR B CA  1 
ATOM   2008 C  C   . THR B 1 29  ? -24.238 14.679 46.307 1.00 10.34 ? 29  THR B C   1 
ATOM   2009 O  O   . THR B 1 29  ? -23.492 15.659 46.245 1.00 9.08  ? 29  THR B O   1 
ATOM   2010 C  CB  . THR B 1 29  ? -22.938 12.989 47.634 1.00 9.28  ? 29  THR B CB  1 
ATOM   2011 O  OG1 . THR B 1 29  ? -22.451 11.643 47.618 1.00 11.87 ? 29  THR B OG1 1 
ATOM   2012 C  CG2 . THR B 1 29  ? -23.890 13.156 48.818 1.00 7.66  ? 29  THR B CG2 1 
ATOM   2013 N  N   . LEU B 1 30  ? -25.558 14.782 46.363 1.00 9.73  ? 30  LEU B N   1 
ATOM   2014 C  CA  . LEU B 1 30  ? -26.200 16.081 46.280 1.00 10.73 ? 30  LEU B CA  1 
ATOM   2015 C  C   . LEU B 1 30  ? -27.290 16.311 47.321 1.00 10.49 ? 30  LEU B C   1 
ATOM   2016 O  O   . LEU B 1 30  ? -28.007 15.392 47.708 1.00 10.57 ? 30  LEU B O   1 
ATOM   2017 C  CB  . LEU B 1 30  ? -26.748 16.226 44.854 1.00 12.52 ? 30  LEU B CB  1 
ATOM   2018 C  CG  . LEU B 1 30  ? -27.894 17.129 44.420 1.00 15.79 ? 30  LEU B CG  1 
ATOM   2019 C  CD1 . LEU B 1 30  ? -27.822 17.243 42.902 1.00 14.77 ? 30  LEU B CD1 1 
ATOM   2020 C  CD2 . LEU B 1 30  ? -29.243 16.565 44.860 1.00 12.93 ? 30  LEU B CD2 1 
ATOM   2021 N  N   . ASN B 1 31  ? -27.390 17.552 47.782 1.00 10.79 ? 31  ASN B N   1 
ATOM   2022 C  CA  . ASN B 1 31  ? -28.395 17.938 48.760 1.00 10.21 ? 31  ASN B CA  1 
ATOM   2023 C  C   . ASN B 1 31  ? -29.249 18.973 48.057 1.00 10.11 ? 31  ASN B C   1 
ATOM   2024 O  O   . ASN B 1 31  ? -28.785 20.073 47.753 1.00 9.75  ? 31  ASN B O   1 
ATOM   2025 C  CB  . ASN B 1 31  ? -27.741 18.550 49.998 1.00 9.35  ? 31  ASN B CB  1 
ATOM   2026 C  CG  . ASN B 1 31  ? -28.730 18.793 51.114 1.00 9.86  ? 31  ASN B CG  1 
ATOM   2027 O  OD1 . ASN B 1 31  ? -29.175 19.920 51.332 1.00 12.00 ? 31  ASN B OD1 1 
ATOM   2028 N  ND2 . ASN B 1 31  ? -29.085 17.734 51.828 1.00 12.77 ? 31  ASN B ND2 1 
ATOM   2029 N  N   . ASN B 1 32  ? -30.499 18.611 47.795 1.00 10.15 ? 32  ASN B N   1 
ATOM   2030 C  CA  . ASN B 1 32  ? -31.417 19.492 47.092 1.00 9.82  ? 32  ASN B CA  1 
ATOM   2031 C  C   . ASN B 1 32  ? -32.133 20.495 47.977 1.00 10.57 ? 32  ASN B C   1 
ATOM   2032 O  O   . ASN B 1 32  ? -32.289 20.292 49.182 1.00 11.80 ? 32  ASN B O   1 
ATOM   2033 C  CB  . ASN B 1 32  ? -32.461 18.666 46.335 1.00 10.84 ? 32  ASN B CB  1 
ATOM   2034 C  CG  . ASN B 1 32  ? -33.242 19.496 45.341 1.00 11.90 ? 32  ASN B CG  1 
ATOM   2035 O  OD1 . ASN B 1 32  ? -32.658 20.197 44.516 1.00 11.74 ? 32  ASN B OD1 1 
ATOM   2036 N  ND2 . ASN B 1 32  ? -34.570 19.426 45.415 1.00 12.33 ? 32  ASN B ND2 1 
ATOM   2037 N  N   . ASN B 1 33  ? -32.557 21.589 47.357 1.00 10.36 ? 33  ASN B N   1 
ATOM   2038 C  CA  . ASN B 1 33  ? -33.292 22.639 48.040 1.00 11.17 ? 33  ASN B CA  1 
ATOM   2039 C  C   . ASN B 1 33  ? -34.619 22.755 47.302 1.00 11.87 ? 33  ASN B C   1 
ATOM   2040 O  O   . ASN B 1 33  ? -34.674 23.276 46.187 1.00 11.85 ? 33  ASN B O   1 
ATOM   2041 C  CB  . ASN B 1 33  ? -32.538 23.964 47.965 1.00 8.78  ? 33  ASN B CB  1 
ATOM   2042 C  CG  . ASN B 1 33  ? -33.199 25.049 48.784 1.00 12.44 ? 33  ASN B CG  1 
ATOM   2043 O  OD1 . ASN B 1 33  ? -34.408 25.260 48.694 1.00 11.44 ? 33  ASN B OD1 1 
ATOM   2044 N  ND2 . ASN B 1 33  ? -32.410 25.743 49.595 1.00 10.62 ? 33  ASN B ND2 1 
ATOM   2045 N  N   . SER B 1 34  ? -35.685 22.262 47.924 1.00 11.55 ? 34  SER B N   1 
ATOM   2046 C  CA  . SER B 1 34  ? -37.005 22.284 47.301 1.00 13.31 ? 34  SER B CA  1 
ATOM   2047 C  C   . SER B 1 34  ? -37.586 23.680 47.103 1.00 12.89 ? 34  SER B C   1 
ATOM   2048 O  O   . SER B 1 34  ? -38.532 23.852 46.338 1.00 13.84 ? 34  SER B O   1 
ATOM   2049 C  CB  . SER B 1 34  ? -37.980 21.429 48.112 1.00 12.73 ? 34  SER B CB  1 
ATOM   2050 O  OG  . SER B 1 34  ? -38.122 21.942 49.419 1.00 17.54 ? 34  SER B OG  1 
ATOM   2051 N  N   . THR B 1 35  ? -37.022 24.676 47.779 1.00 12.68 ? 35  THR B N   1 
ATOM   2052 C  CA  . THR B 1 35  ? -37.512 26.042 47.641 1.00 11.93 ? 35  THR B CA  1 
ATOM   2053 C  C   . THR B 1 35  ? -36.890 26.756 46.440 1.00 13.36 ? 35  THR B C   1 
ATOM   2054 O  O   . THR B 1 35  ? -37.610 27.313 45.607 1.00 13.34 ? 35  THR B O   1 
ATOM   2055 C  CB  . THR B 1 35  ? -37.245 26.864 48.915 1.00 14.29 ? 35  THR B CB  1 
ATOM   2056 O  OG1 . THR B 1 35  ? -37.917 26.250 50.020 1.00 16.33 ? 35  THR B OG1 1 
ATOM   2057 C  CG2 . THR B 1 35  ? -37.761 28.289 48.755 1.00 13.40 ? 35  THR B CG2 1 
ATOM   2058 N  N   . THR B 1 36  ? -35.560 26.736 46.342 1.00 12.51 ? 36  THR B N   1 
ATOM   2059 C  CA  . THR B 1 36  ? -34.877 27.389 45.223 1.00 10.29 ? 36  THR B CA  1 
ATOM   2060 C  C   . THR B 1 36  ? -34.948 26.537 43.953 1.00 9.61  ? 36  THR B C   1 
ATOM   2061 O  O   . THR B 1 36  ? -34.859 27.063 42.840 1.00 9.02  ? 36  THR B O   1 
ATOM   2062 C  CB  . THR B 1 36  ? -33.387 27.666 45.545 1.00 8.27  ? 36  THR B CB  1 
ATOM   2063 O  OG1 . THR B 1 36  ? -32.703 26.427 45.769 1.00 9.19  ? 36  THR B OG1 1 
ATOM   2064 C  CG2 . THR B 1 36  ? -33.260 28.542 46.784 1.00 8.63  ? 36  THR B CG2 1 
ATOM   2065 N  N   . LYS B 1 37  ? -35.110 25.227 44.140 1.00 9.03  ? 37  LYS B N   1 
ATOM   2066 C  CA  . LYS B 1 37  ? -35.197 24.236 43.057 1.00 9.77  ? 37  LYS B CA  1 
ATOM   2067 C  C   . LYS B 1 37  ? -33.821 23.801 42.553 1.00 10.27 ? 37  LYS B C   1 
ATOM   2068 O  O   . LYS B 1 37  ? -33.709 23.063 41.566 1.00 9.89  ? 37  LYS B O   1 
ATOM   2069 C  CB  . LYS B 1 37  ? -36.034 24.766 41.882 1.00 9.53  ? 37  LYS B CB  1 
ATOM   2070 C  CG  . LYS B 1 37  ? -37.482 25.131 42.234 1.00 9.77  ? 37  LYS B CG  1 
ATOM   2071 C  CD  . LYS B 1 37  ? -38.254 23.940 42.804 1.00 11.00 ? 37  LYS B CD  1 
ATOM   2072 C  CE  . LYS B 1 37  ? -39.680 24.325 43.209 1.00 11.57 ? 37  LYS B CE  1 
ATOM   2073 N  NZ  . LYS B 1 37  ? -39.707 25.453 44.190 1.00 12.64 ? 37  LYS B NZ  1 
ATOM   2074 N  N   . PHE B 1 38  ? -32.778 24.258 43.242 1.00 8.39  ? 38  PHE B N   1 
ATOM   2075 C  CA  . PHE B 1 38  ? -31.401 23.924 42.889 1.00 8.22  ? 38  PHE B CA  1 
ATOM   2076 C  C   . PHE B 1 38  ? -30.690 23.336 44.103 1.00 8.94  ? 38  PHE B C   1 
ATOM   2077 O  O   . PHE B 1 38  ? -31.066 23.606 45.243 1.00 10.53 ? 38  PHE B O   1 
ATOM   2078 C  CB  . PHE B 1 38  ? -30.670 25.173 42.389 1.00 8.38  ? 38  PHE B CB  1 
ATOM   2079 C  CG  . PHE B 1 38  ? -31.400 25.889 41.288 1.00 10.09 ? 38  PHE B CG  1 
ATOM   2080 C  CD1 . PHE B 1 38  ? -31.577 25.279 40.044 1.00 9.21  ? 38  PHE B CD1 1 
ATOM   2081 C  CD2 . PHE B 1 38  ? -31.959 27.146 41.505 1.00 8.88  ? 38  PHE B CD2 1 
ATOM   2082 C  CE1 . PHE B 1 38  ? -32.302 25.907 39.036 1.00 9.30  ? 38  PHE B CE1 1 
ATOM   2083 C  CE2 . PHE B 1 38  ? -32.687 27.782 40.503 1.00 9.69  ? 38  PHE B CE2 1 
ATOM   2084 C  CZ  . PHE B 1 38  ? -32.859 27.158 39.265 1.00 9.54  ? 38  PHE B CZ  1 
ATOM   2085 N  N   . ALA B 1 39  ? -29.666 22.530 43.855 1.00 8.14  ? 39  ALA B N   1 
ATOM   2086 C  CA  . ALA B 1 39  ? -28.920 21.882 44.927 1.00 8.71  ? 39  ALA B CA  1 
ATOM   2087 C  C   . ALA B 1 39  ? -28.160 22.862 45.811 1.00 8.33  ? 39  ALA B C   1 
ATOM   2088 O  O   . ALA B 1 39  ? -27.583 23.832 45.321 1.00 9.49  ? 39  ALA B O   1 
ATOM   2089 C  CB  . ALA B 1 39  ? -27.946 20.857 44.334 1.00 8.46  ? 39  ALA B CB  1 
ATOM   2090 N  N   . ASN B 1 40  ? -28.165 22.595 47.116 1.00 8.18  ? 40  ASN B N   1 
ATOM   2091 C  CA  . ASN B 1 40  ? -27.458 23.430 48.090 1.00 8.09  ? 40  ASN B CA  1 
ATOM   2092 C  C   . ASN B 1 40  ? -25.961 23.217 47.910 1.00 7.10  ? 40  ASN B C   1 
ATOM   2093 O  O   . ASN B 1 40  ? -25.163 24.151 47.992 1.00 7.17  ? 40  ASN B O   1 
ATOM   2094 C  CB  . ASN B 1 40  ? -27.858 23.036 49.510 1.00 6.25  ? 40  ASN B CB  1 
ATOM   2095 C  CG  . ASN B 1 40  ? -29.290 23.389 49.821 1.00 7.63  ? 40  ASN B CG  1 
ATOM   2096 O  OD1 . ASN B 1 40  ? -29.718 24.523 49.606 1.00 8.53  ? 40  ASN B OD1 1 
ATOM   2097 N  ND2 . ASN B 1 40  ? -30.045 22.422 50.324 1.00 8.18  ? 40  ASN B ND2 1 
ATOM   2098 N  N   . TRP B 1 41  ? -25.590 21.965 47.679 1.00 7.82  ? 41  TRP B N   1 
ATOM   2099 C  CA  . TRP B 1 41  ? -24.198 21.614 47.464 1.00 8.35  ? 41  TRP B CA  1 
ATOM   2100 C  C   . TRP B 1 41  ? -24.136 20.307 46.719 1.00 8.75  ? 41  TRP B C   1 
ATOM   2101 O  O   . TRP B 1 41  ? -25.055 19.496 46.794 1.00 7.88  ? 41  TRP B O   1 
ATOM   2102 C  CB  . TRP B 1 41  ? -23.431 21.487 48.787 1.00 6.54  ? 41  TRP B CB  1 
ATOM   2103 C  CG  . TRP B 1 41  ? -24.045 20.573 49.808 1.00 6.23  ? 41  TRP B CG  1 
ATOM   2104 C  CD1 . TRP B 1 41  ? -24.845 20.938 50.854 1.00 6.51  ? 41  TRP B CD1 1 
ATOM   2105 C  CD2 . TRP B 1 41  ? -23.854 19.155 49.928 1.00 7.35  ? 41  TRP B CD2 1 
ATOM   2106 N  NE1 . TRP B 1 41  ? -25.160 19.841 51.619 1.00 6.65  ? 41  TRP B NE1 1 
ATOM   2107 C  CE2 . TRP B 1 41  ? -24.566 18.733 51.075 1.00 7.02  ? 41  TRP B CE2 1 
ATOM   2108 C  CE3 . TRP B 1 41  ? -23.149 18.201 49.180 1.00 7.21  ? 41  TRP B CE3 1 
ATOM   2109 C  CZ2 . TRP B 1 41  ? -24.593 17.395 51.494 1.00 7.03  ? 41  TRP B CZ2 1 
ATOM   2110 C  CZ3 . TRP B 1 41  ? -23.177 16.869 49.598 1.00 6.63  ? 41  TRP B CZ3 1 
ATOM   2111 C  CH2 . TRP B 1 41  ? -23.895 16.481 50.745 1.00 6.45  ? 41  TRP B CH2 1 
ATOM   2112 N  N   . VAL B 1 42  ? -23.047 20.126 45.984 1.00 7.95  ? 42  VAL B N   1 
ATOM   2113 C  CA  . VAL B 1 42  ? -22.818 18.918 45.215 1.00 6.66  ? 42  VAL B CA  1 
ATOM   2114 C  C   . VAL B 1 42  ? -21.384 18.525 45.511 1.00 6.80  ? 42  VAL B C   1 
ATOM   2115 O  O   . VAL B 1 42  ? -20.469 19.322 45.334 1.00 7.24  ? 42  VAL B O   1 
ATOM   2116 C  CB  . VAL B 1 42  ? -22.974 19.170 43.700 1.00 7.94  ? 42  VAL B CB  1 
ATOM   2117 C  CG1 . VAL B 1 42  ? -22.706 17.885 42.932 1.00 9.16  ? 42  VAL B CG1 1 
ATOM   2118 C  CG2 . VAL B 1 42  ? -24.377 19.675 43.398 1.00 7.85  ? 42  VAL B CG2 1 
ATOM   2119 N  N   . ALA B 1 43  ? -21.196 17.304 45.986 1.00 7.53  ? 43  ALA B N   1 
ATOM   2120 C  CA  . ALA B 1 43  ? -19.866 16.820 46.309 1.00 7.26  ? 43  ALA B CA  1 
ATOM   2121 C  C   . ALA B 1 43  ? -19.499 15.720 45.331 1.00 7.50  ? 43  ALA B C   1 
ATOM   2122 O  O   . ALA B 1 43  ? -20.311 14.843 45.051 1.00 8.07  ? 43  ALA B O   1 
ATOM   2123 C  CB  . ALA B 1 43  ? -19.844 16.281 47.734 1.00 5.34  ? 43  ALA B CB  1 
ATOM   2124 N  N   . TYR B 1 44  ? -18.289 15.771 44.790 1.00 7.47  ? 44  TYR B N   1 
ATOM   2125 C  CA  . TYR B 1 44  ? -17.872 14.725 43.872 1.00 8.34  ? 44  TYR B CA  1 
ATOM   2126 C  C   . TYR B 1 44  ? -16.412 14.333 44.060 1.00 9.69  ? 44  TYR B C   1 
ATOM   2127 O  O   . TYR B 1 44  ? -15.604 15.089 44.608 1.00 10.13 ? 44  TYR B O   1 
ATOM   2128 C  CB  . TYR B 1 44  ? -18.160 15.118 42.419 1.00 6.60  ? 44  TYR B CB  1 
ATOM   2129 C  CG  . TYR B 1 44  ? -17.568 16.430 41.976 1.00 6.60  ? 44  TYR B CG  1 
ATOM   2130 C  CD1 . TYR B 1 44  ? -18.299 17.613 42.077 1.00 6.06  ? 44  TYR B CD1 1 
ATOM   2131 C  CD2 . TYR B 1 44  ? -16.299 16.482 41.401 1.00 5.78  ? 44  TYR B CD2 1 
ATOM   2132 C  CE1 . TYR B 1 44  ? -17.787 18.814 41.610 1.00 6.19  ? 44  TYR B CE1 1 
ATOM   2133 C  CE2 . TYR B 1 44  ? -15.776 17.679 40.930 1.00 7.16  ? 44  TYR B CE2 1 
ATOM   2134 C  CZ  . TYR B 1 44  ? -16.527 18.840 41.035 1.00 6.54  ? 44  TYR B CZ  1 
ATOM   2135 O  OH  . TYR B 1 44  ? -16.025 20.024 40.555 1.00 7.61  ? 44  TYR B OH  1 
ATOM   2136 N  N   . HIS B 1 45  ? -16.088 13.133 43.597 1.00 10.99 ? 45  HIS B N   1 
ATOM   2137 C  CA  . HIS B 1 45  ? -14.759 12.572 43.750 1.00 11.19 ? 45  HIS B CA  1 
ATOM   2138 C  C   . HIS B 1 45  ? -14.166 12.191 42.396 1.00 12.24 ? 45  HIS B C   1 
ATOM   2139 O  O   . HIS B 1 45  ? -14.613 11.245 41.750 1.00 12.03 ? 45  HIS B O   1 
ATOM   2140 C  CB  . HIS B 1 45  ? -14.874 11.348 44.675 1.00 10.07 ? 45  HIS B CB  1 
ATOM   2141 C  CG  . HIS B 1 45  ? -13.597 10.594 44.876 1.00 9.58  ? 45  HIS B CG  1 
ATOM   2142 N  ND1 . HIS B 1 45  ? -13.577 9.264  45.240 1.00 9.68  ? 45  HIS B ND1 1 
ATOM   2143 C  CD2 . HIS B 1 45  ? -12.303 10.979 44.789 1.00 9.93  ? 45  HIS B CD2 1 
ATOM   2144 C  CE1 . HIS B 1 45  ? -12.326 8.863  45.370 1.00 9.92  ? 45  HIS B CE1 1 
ATOM   2145 N  NE2 . HIS B 1 45  ? -11.533 9.885  45.102 1.00 10.40 ? 45  HIS B NE2 1 
ATOM   2146 N  N   . ILE B 1 46  ? -13.163 12.943 41.964 1.00 11.24 ? 46  ILE B N   1 
ATOM   2147 C  CA  . ILE B 1 46  ? -12.518 12.660 40.692 1.00 10.77 ? 46  ILE B CA  1 
ATOM   2148 C  C   . ILE B 1 46  ? -11.331 11.729 40.897 1.00 11.46 ? 46  ILE B C   1 
ATOM   2149 O  O   . ILE B 1 46  ? -10.510 11.944 41.792 1.00 10.09 ? 46  ILE B O   1 
ATOM   2150 C  CB  . ILE B 1 46  ? -11.985 13.942 40.023 1.00 10.42 ? 46  ILE B CB  1 
ATOM   2151 C  CG1 . ILE B 1 46  ? -13.126 14.922 39.761 1.00 10.45 ? 46  ILE B CG1 1 
ATOM   2152 C  CG2 . ILE B 1 46  ? -11.285 13.588 38.717 1.00 11.17 ? 46  ILE B CG2 1 
ATOM   2153 C  CD1 . ILE B 1 46  ? -12.650 16.272 39.248 1.00 11.71 ? 46  ILE B CD1 1 
ATOM   2154 N  N   . THR B 1 47  ? -11.257 10.690 40.074 1.00 13.34 ? 47  THR B N   1 
ATOM   2155 C  CA  . THR B 1 47  ? -10.143 9.745  40.112 1.00 15.91 ? 47  THR B CA  1 
ATOM   2156 C  C   . THR B 1 47  ? -9.706  9.559  38.664 1.00 16.89 ? 47  THR B C   1 
ATOM   2157 O  O   . THR B 1 47  ? -10.373 10.030 37.750 1.00 16.10 ? 47  THR B O   1 
ATOM   2158 C  CB  . THR B 1 47  ? -10.544 8.372  40.672 1.00 14.24 ? 47  THR B CB  1 
ATOM   2159 O  OG1 . THR B 1 47  ? -11.249 7.640  39.664 1.00 14.30 ? 47  THR B OG1 1 
ATOM   2160 C  CG2 . THR B 1 47  ? -11.416 8.527  41.905 1.00 14.83 ? 47  THR B CG2 1 
ATOM   2161 N  N   . LYS B 1 48  ? -8.594  8.868  38.452 1.00 18.01 ? 48  LYS B N   1 
ATOM   2162 C  CA  . LYS B 1 48  ? -8.094  8.653  37.101 1.00 18.22 ? 48  LYS B CA  1 
ATOM   2163 C  C   . LYS B 1 48  ? -9.075  7.877  36.224 1.00 17.76 ? 48  LYS B C   1 
ATOM   2164 O  O   . LYS B 1 48  ? -8.971  7.896  35.001 1.00 18.09 ? 48  LYS B O   1 
ATOM   2165 C  CB  . LYS B 1 48  ? -6.751  7.921  37.154 1.00 21.27 ? 48  LYS B CB  1 
ATOM   2166 C  CG  . LYS B 1 48  ? -5.585  8.812  37.570 1.00 25.61 ? 48  LYS B CG  1 
ATOM   2167 C  CD  . LYS B 1 48  ? -4.638  8.082  38.512 1.00 30.11 ? 48  LYS B CD  1 
ATOM   2168 C  CE  . LYS B 1 48  ? -3.838  9.053  39.367 1.00 30.16 ? 48  LYS B CE  1 
ATOM   2169 N  NZ  . LYS B 1 48  ? -3.034  9.994  38.535 1.00 25.96 ? 48  LYS B NZ  1 
ATOM   2170 N  N   . ASP B 1 49  ? -10.038 7.215  36.852 1.00 17.07 ? 49  ASP B N   1 
ATOM   2171 C  CA  . ASP B 1 49  ? -11.022 6.421  36.125 1.00 18.50 ? 49  ASP B CA  1 
ATOM   2172 C  C   . ASP B 1 49  ? -12.337 7.133  35.807 1.00 19.42 ? 49  ASP B C   1 
ATOM   2173 O  O   . ASP B 1 49  ? -13.142 6.611  35.036 1.00 19.30 ? 49  ASP B O   1 
ATOM   2174 C  CB  . ASP B 1 49  ? -11.350 5.152  36.915 1.00 22.86 ? 49  ASP B CB  1 
ATOM   2175 C  CG  . ASP B 1 49  ? -10.217 4.147  36.904 1.00 27.91 ? 49  ASP B CG  1 
ATOM   2176 O  OD1 . ASP B 1 49  ? -9.428  4.140  35.935 1.00 31.37 ? 49  ASP B OD1 1 
ATOM   2177 O  OD2 . ASP B 1 49  ? -10.119 3.360  37.868 1.00 32.18 ? 49  ASP B OD2 1 
ATOM   2178 N  N   . THR B 1 50  ? -12.567 8.312  36.380 1.00 18.99 ? 50  THR B N   1 
ATOM   2179 C  CA  . THR B 1 50  ? -13.833 9.003  36.138 1.00 17.46 ? 50  THR B CA  1 
ATOM   2180 C  C   . THR B 1 50  ? -13.941 9.911  34.914 1.00 17.66 ? 50  THR B C   1 
ATOM   2181 O  O   . THR B 1 50  ? -15.013 10.019 34.326 1.00 19.46 ? 50  THR B O   1 
ATOM   2182 C  CB  . THR B 1 50  ? -14.287 9.814  37.381 1.00 14.02 ? 50  THR B CB  1 
ATOM   2183 O  OG1 . THR B 1 50  ? -13.362 10.877 37.632 1.00 11.87 ? 50  THR B OG1 1 
ATOM   2184 C  CG2 . THR B 1 50  ? -14.373 8.914  38.605 1.00 10.72 ? 50  THR B CG2 1 
ATOM   2185 N  N   . PRO B 1 51  ? -12.850 10.582 34.513 1.00 16.30 ? 51  PRO B N   1 
ATOM   2186 C  CA  . PRO B 1 51  ? -12.996 11.446 33.335 1.00 16.98 ? 51  PRO B CA  1 
ATOM   2187 C  C   . PRO B 1 51  ? -13.374 10.683 32.063 1.00 18.70 ? 51  PRO B C   1 
ATOM   2188 O  O   . PRO B 1 51  ? -13.075 9.500  31.919 1.00 19.36 ? 51  PRO B O   1 
ATOM   2189 C  CB  . PRO B 1 51  ? -11.632 12.137 33.217 1.00 16.43 ? 51  PRO B CB  1 
ATOM   2190 C  CG  . PRO B 1 51  ? -10.994 11.968 34.562 1.00 16.41 ? 51  PRO B CG  1 
ATOM   2191 C  CD  . PRO B 1 51  ? -11.485 10.635 35.057 1.00 16.24 ? 51  PRO B CD  1 
ATOM   2192 N  N   . ALA B 1 52  ? -14.042 11.374 31.148 1.00 19.29 ? 52  ALA B N   1 
ATOM   2193 C  CA  . ALA B 1 52  ? -14.473 10.781 29.888 1.00 19.93 ? 52  ALA B CA  1 
ATOM   2194 C  C   . ALA B 1 52  ? -14.996 11.883 28.973 1.00 21.49 ? 52  ALA B C   1 
ATOM   2195 O  O   . ALA B 1 52  ? -15.770 12.747 29.399 1.00 20.61 ? 52  ALA B O   1 
ATOM   2196 C  CB  . ALA B 1 52  ? -15.559 9.743  30.143 1.00 17.54 ? 52  ALA B CB  1 
ATOM   2197 N  N   . SER B 1 53  ? -14.574 11.848 27.713 1.00 23.53 ? 53  SER B N   1 
ATOM   2198 C  CA  . SER B 1 53  ? -14.986 12.853 26.742 1.00 25.95 ? 53  SER B CA  1 
ATOM   2199 C  C   . SER B 1 53  ? -16.044 12.358 25.756 1.00 26.40 ? 53  SER B C   1 
ATOM   2200 O  O   . SER B 1 53  ? -16.303 11.160 25.651 1.00 26.69 ? 53  SER B O   1 
ATOM   2201 C  CB  . SER B 1 53  ? -13.764 13.342 25.961 1.00 28.70 ? 53  SER B CB  1 
ATOM   2202 O  OG  . SER B 1 53  ? -13.335 14.606 26.433 1.00 34.25 ? 53  SER B OG  1 
ATOM   2203 N  N   . GLY B 1 54  ? -16.659 13.301 25.048 1.00 29.89 ? 54  GLY B N   1 
ATOM   2204 C  CA  . GLY B 1 54  ? -17.656 12.969 24.045 1.00 30.20 ? 54  GLY B CA  1 
ATOM   2205 C  C   . GLY B 1 54  ? -19.005 12.429 24.480 1.00 30.00 ? 54  GLY B C   1 
ATOM   2206 O  O   . GLY B 1 54  ? -19.684 11.770 23.691 1.00 33.64 ? 54  GLY B O   1 
ATOM   2207 N  N   . LYS B 1 55  ? -19.413 12.692 25.716 1.00 23.73 ? 55  LYS B N   1 
ATOM   2208 C  CA  . LYS B 1 55  ? -20.706 12.201 26.174 1.00 21.28 ? 55  LYS B CA  1 
ATOM   2209 C  C   . LYS B 1 55  ? -21.789 13.204 25.800 1.00 19.84 ? 55  LYS B C   1 
ATOM   2210 O  O   . LYS B 1 55  ? -21.560 14.414 25.811 1.00 19.07 ? 55  LYS B O   1 
ATOM   2211 C  CB  . LYS B 1 55  ? -20.689 11.975 27.685 1.00 25.58 ? 55  LYS B CB  1 
ATOM   2212 C  CG  . LYS B 1 55  ? -19.716 10.895 28.128 1.00 25.20 ? 55  LYS B CG  1 
ATOM   2213 C  CD  . LYS B 1 55  ? -20.210 9.515  27.752 1.00 25.90 ? 55  LYS B CD  1 
ATOM   2214 C  CE  . LYS B 1 55  ? -20.197 8.590  28.955 1.00 30.58 ? 55  LYS B CE  1 
ATOM   2215 N  NZ  . LYS B 1 55  ? -19.333 7.395  28.744 1.00 31.39 ? 55  LYS B NZ  1 
ATOM   2216 N  N   . THR B 1 56  ? -22.968 12.696 25.456 1.00 20.26 ? 56  THR B N   1 
ATOM   2217 C  CA  . THR B 1 56  ? -24.076 13.557 25.064 1.00 20.53 ? 56  THR B CA  1 
ATOM   2218 C  C   . THR B 1 56  ? -24.793 14.157 26.274 1.00 20.53 ? 56  THR B C   1 
ATOM   2219 O  O   . THR B 1 56  ? -24.680 13.654 27.395 1.00 20.74 ? 56  THR B O   1 
ATOM   2220 C  CB  . THR B 1 56  ? -25.084 12.786 24.195 1.00 21.54 ? 56  THR B CB  1 
ATOM   2221 O  OG1 . THR B 1 56  ? -25.607 11.674 24.932 1.00 24.49 ? 56  THR B OG1 1 
ATOM   2222 C  CG2 . THR B 1 56  ? -24.401 12.269 22.936 1.00 22.03 ? 56  THR B CG2 1 
ATOM   2223 N  N   . ARG B 1 57  ? -25.530 15.237 26.039 1.00 18.07 ? 57  ARG B N   1 
ATOM   2224 C  CA  . ARG B 1 57  ? -26.246 15.913 27.109 1.00 16.74 ? 57  ARG B CA  1 
ATOM   2225 C  C   . ARG B 1 57  ? -27.762 15.847 26.959 1.00 15.57 ? 57  ARG B C   1 
ATOM   2226 O  O   . ARG B 1 57  ? -28.374 16.726 26.355 1.00 15.69 ? 57  ARG B O   1 
ATOM   2227 C  CB  . ARG B 1 57  ? -25.802 17.375 27.188 1.00 21.13 ? 57  ARG B CB  1 
ATOM   2228 C  CG  . ARG B 1 57  ? -24.353 17.557 27.621 1.00 27.50 ? 57  ARG B CG  1 
ATOM   2229 C  CD  . ARG B 1 57  ? -23.616 18.527 26.713 1.00 33.98 ? 57  ARG B CD  1 
ATOM   2230 N  NE  . ARG B 1 57  ? -24.390 19.743 26.465 1.00 38.16 ? 57  ARG B NE  1 
ATOM   2231 C  CZ  . ARG B 1 57  ? -24.929 20.067 25.289 1.00 39.46 ? 57  ARG B CZ  1 
ATOM   2232 N  NH1 . ARG B 1 57  ? -24.781 19.263 24.241 1.00 39.87 ? 57  ARG B NH1 1 
ATOM   2233 N  NH2 . ARG B 1 57  ? -25.615 21.199 25.159 1.00 39.49 ? 57  ARG B NH2 1 
ATOM   2234 N  N   . ASN B 1 58  ? -28.363 14.798 27.511 1.00 14.43 ? 58  ASN B N   1 
ATOM   2235 C  CA  . ASN B 1 58  ? -29.811 14.644 27.459 1.00 14.02 ? 58  ASN B CA  1 
ATOM   2236 C  C   . ASN B 1 58  ? -30.380 15.131 28.782 1.00 13.41 ? 58  ASN B C   1 
ATOM   2237 O  O   . ASN B 1 58  ? -30.489 14.370 29.743 1.00 12.72 ? 58  ASN B O   1 
ATOM   2238 C  CB  . ASN B 1 58  ? -30.197 13.180 27.234 1.00 14.31 ? 58  ASN B CB  1 
ATOM   2239 C  CG  . ASN B 1 58  ? -30.398 12.850 25.768 1.00 12.63 ? 58  ASN B CG  1 
ATOM   2240 O  OD1 . ASN B 1 58  ? -30.035 11.771 25.311 1.00 17.19 ? 58  ASN B OD1 1 
ATOM   2241 N  ND2 . ASN B 1 58  ? -30.977 13.777 25.026 1.00 9.28  ? 58  ASN B ND2 1 
ATOM   2242 N  N   . TRP B 1 59  ? -30.720 16.414 28.826 1.00 12.98 ? 59  TRP B N   1 
ATOM   2243 C  CA  . TRP B 1 59  ? -31.280 17.022 30.023 1.00 13.22 ? 59  TRP B CA  1 
ATOM   2244 C  C   . TRP B 1 59  ? -32.488 16.218 30.476 1.00 13.54 ? 59  TRP B C   1 
ATOM   2245 O  O   . TRP B 1 59  ? -33.283 15.768 29.651 1.00 13.76 ? 59  TRP B O   1 
ATOM   2246 C  CB  . TRP B 1 59  ? -31.675 18.466 29.723 1.00 11.72 ? 59  TRP B CB  1 
ATOM   2247 C  CG  . TRP B 1 59  ? -30.578 19.220 29.034 1.00 11.76 ? 59  TRP B CG  1 
ATOM   2248 C  CD1 . TRP B 1 59  ? -30.635 19.816 27.809 1.00 12.46 ? 59  TRP B CD1 1 
ATOM   2249 C  CD2 . TRP B 1 59  ? -29.251 19.450 29.531 1.00 12.68 ? 59  TRP B CD2 1 
ATOM   2250 N  NE1 . TRP B 1 59  ? -29.428 20.402 27.509 1.00 13.62 ? 59  TRP B NE1 1 
ATOM   2251 C  CE2 . TRP B 1 59  ? -28.560 20.192 28.548 1.00 13.07 ? 59  TRP B CE2 1 
ATOM   2252 C  CE3 . TRP B 1 59  ? -28.579 19.099 30.712 1.00 11.53 ? 59  TRP B CE3 1 
ATOM   2253 C  CZ2 . TRP B 1 59  ? -27.227 20.592 28.708 1.00 13.50 ? 59  TRP B CZ2 1 
ATOM   2254 C  CZ3 . TRP B 1 59  ? -27.257 19.496 30.871 1.00 11.91 ? 59  TRP B CZ3 1 
ATOM   2255 C  CH2 . TRP B 1 59  ? -26.595 20.235 29.874 1.00 13.58 ? 59  TRP B CH2 1 
ATOM   2256 N  N   . LYS B 1 60  ? -32.626 16.046 31.787 1.00 12.83 ? 60  LYS B N   1 
ATOM   2257 C  CA  . LYS B 1 60  ? -33.726 15.264 32.332 1.00 12.69 ? 60  LYS B CA  1 
ATOM   2258 C  C   . LYS B 1 60  ? -34.085 15.635 33.767 1.00 12.26 ? 60  LYS B C   1 
ATOM   2259 O  O   . LYS B 1 60  ? -33.231 16.055 34.549 1.00 11.47 ? 60  LYS B O   1 
ATOM   2260 C  CB  . LYS B 1 60  ? -33.355 13.784 32.286 1.00 16.64 ? 60  LYS B CB  1 
ATOM   2261 C  CG  . LYS B 1 60  ? -34.526 12.852 32.101 1.00 24.57 ? 60  LYS B CG  1 
ATOM   2262 C  CD  . LYS B 1 60  ? -34.116 11.639 31.285 1.00 31.00 ? 60  LYS B CD  1 
ATOM   2263 C  CE  . LYS B 1 60  ? -33.573 12.050 29.925 1.00 32.85 ? 60  LYS B CE  1 
ATOM   2264 N  NZ  . LYS B 1 60  ? -33.153 10.872 29.117 1.00 33.80 ? 60  LYS B NZ  1 
ATOM   2265 N  N   . THR B 1 61  ? -35.359 15.472 34.101 1.00 10.73 ? 61  THR B N   1 
ATOM   2266 C  CA  . THR B 1 61  ? -35.841 15.747 35.446 1.00 11.18 ? 61  THR B CA  1 
ATOM   2267 C  C   . THR B 1 61  ? -35.315 14.614 36.315 1.00 11.26 ? 61  THR B C   1 
ATOM   2268 O  O   . THR B 1 61  ? -35.456 13.451 35.955 1.00 11.63 ? 61  THR B O   1 
ATOM   2269 C  CB  . THR B 1 61  ? -37.382 15.729 35.500 1.00 10.67 ? 61  THR B CB  1 
ATOM   2270 O  OG1 . THR B 1 61  ? -37.897 16.735 34.624 1.00 12.72 ? 61  THR B OG1 1 
ATOM   2271 C  CG2 . THR B 1 61  ? -37.878 15.991 36.910 1.00 10.56 ? 61  THR B CG2 1 
ATOM   2272 N  N   . ASP B 1 62  ? -34.700 14.949 37.446 1.00 10.11 ? 62  ASP B N   1 
ATOM   2273 C  CA  . ASP B 1 62  ? -34.169 13.929 38.346 1.00 10.67 ? 62  ASP B CA  1 
ATOM   2274 C  C   . ASP B 1 62  ? -35.298 13.020 38.828 1.00 11.83 ? 62  ASP B C   1 
ATOM   2275 O  O   . ASP B 1 62  ? -36.224 13.468 39.504 1.00 12.18 ? 62  ASP B O   1 
ATOM   2276 C  CB  . ASP B 1 62  ? -33.492 14.584 39.549 1.00 10.16 ? 62  ASP B CB  1 
ATOM   2277 C  CG  . ASP B 1 62  ? -32.609 13.619 40.311 1.00 11.76 ? 62  ASP B CG  1 
ATOM   2278 O  OD1 . ASP B 1 62  ? -33.002 12.448 40.470 1.00 12.11 ? 62  ASP B OD1 1 
ATOM   2279 O  OD2 . ASP B 1 62  ? -31.519 14.029 40.753 1.00 13.49 ? 62  ASP B OD2 1 
ATOM   2280 N  N   . PRO B 1 63  ? -35.233 11.724 38.488 1.00 13.53 ? 63  PRO B N   1 
ATOM   2281 C  CA  . PRO B 1 63  ? -36.275 10.778 38.904 1.00 14.76 ? 63  PRO B CA  1 
ATOM   2282 C  C   . PRO B 1 63  ? -36.275 10.452 40.398 1.00 15.91 ? 63  PRO B C   1 
ATOM   2283 O  O   . PRO B 1 63  ? -37.231 9.869  40.910 1.00 16.90 ? 63  PRO B O   1 
ATOM   2284 C  CB  . PRO B 1 63  ? -35.996 9.541  38.052 1.00 13.80 ? 63  PRO B CB  1 
ATOM   2285 C  CG  . PRO B 1 63  ? -34.534 9.605  37.786 1.00 14.12 ? 63  PRO B CG  1 
ATOM   2286 C  CD  . PRO B 1 63  ? -34.184 11.071 37.686 1.00 12.45 ? 63  PRO B CD  1 
ATOM   2287 N  N   . ALA B 1 64  ? -35.208 10.830 41.095 1.00 14.40 ? 64  ALA B N   1 
ATOM   2288 C  CA  . ALA B 1 64  ? -35.102 10.557 42.522 1.00 14.89 ? 64  ALA B CA  1 
ATOM   2289 C  C   . ALA B 1 64  ? -35.799 11.611 43.376 1.00 15.50 ? 64  ALA B C   1 
ATOM   2290 O  O   . ALA B 1 64  ? -35.978 11.423 44.577 1.00 17.47 ? 64  ALA B O   1 
ATOM   2291 C  CB  . ALA B 1 64  ? -33.635 10.456 42.919 1.00 14.89 ? 64  ALA B CB  1 
ATOM   2292 N  N   . LEU B 1 65  ? -36.198 12.717 42.762 1.00 15.75 ? 65  LEU B N   1 
ATOM   2293 C  CA  . LEU B 1 65  ? -36.855 13.785 43.503 1.00 15.54 ? 65  LEU B CA  1 
ATOM   2294 C  C   . LEU B 1 65  ? -38.311 13.965 43.109 1.00 17.42 ? 65  LEU B C   1 
ATOM   2295 O  O   . LEU B 1 65  ? -38.750 13.494 42.061 1.00 18.74 ? 65  LEU B O   1 
ATOM   2296 C  CB  . LEU B 1 65  ? -36.123 15.110 43.279 1.00 13.47 ? 65  LEU B CB  1 
ATOM   2297 C  CG  . LEU B 1 65  ? -34.652 15.198 43.683 1.00 12.30 ? 65  LEU B CG  1 
ATOM   2298 C  CD1 . LEU B 1 65  ? -34.021 16.422 43.044 1.00 11.81 ? 65  LEU B CD1 1 
ATOM   2299 C  CD2 . LEU B 1 65  ? -34.549 15.279 45.195 1.00 14.38 ? 65  LEU B CD2 1 
ATOM   2300 N  N   . ASN B 1 66  ? -39.059 14.648 43.966 1.00 18.71 ? 66  ASN B N   1 
ATOM   2301 C  CA  . ASN B 1 66  ? -40.458 14.932 43.691 1.00 19.75 ? 66  ASN B CA  1 
ATOM   2302 C  C   . ASN B 1 66  ? -40.402 16.013 42.616 1.00 18.35 ? 66  ASN B C   1 
ATOM   2303 O  O   . ASN B 1 66  ? -39.697 17.007 42.771 1.00 18.32 ? 66  ASN B O   1 
ATOM   2304 C  CB  . ASN B 1 66  ? -41.149 15.467 44.946 1.00 22.56 ? 66  ASN B CB  1 
ATOM   2305 C  CG  . ASN B 1 66  ? -42.609 15.787 44.711 1.00 27.40 ? 66  ASN B CG  1 
ATOM   2306 O  OD1 . ASN B 1 66  ? -42.952 16.562 43.820 1.00 28.50 ? 66  ASN B OD1 1 
ATOM   2307 N  ND2 . ASN B 1 66  ? -43.479 15.188 45.512 1.00 32.91 ? 66  ASN B ND2 1 
ATOM   2308 N  N   . PRO B 1 67  ? -41.145 15.832 41.514 1.00 17.40 ? 67  PRO B N   1 
ATOM   2309 C  CA  . PRO B 1 67  ? -41.173 16.792 40.403 1.00 16.66 ? 67  PRO B CA  1 
ATOM   2310 C  C   . PRO B 1 67  ? -41.433 18.246 40.783 1.00 16.34 ? 67  PRO B C   1 
ATOM   2311 O  O   . PRO B 1 67  ? -41.030 19.163 40.064 1.00 17.11 ? 67  PRO B O   1 
ATOM   2312 C  CB  . PRO B 1 67  ? -42.256 16.241 39.477 1.00 17.86 ? 67  PRO B CB  1 
ATOM   2313 C  CG  . PRO B 1 67  ? -42.330 14.789 39.803 1.00 17.63 ? 67  PRO B CG  1 
ATOM   2314 C  CD  . PRO B 1 67  ? -42.029 14.679 41.268 1.00 16.91 ? 67  PRO B CD  1 
ATOM   2315 N  N   . ALA B 1 68  ? -42.100 18.463 41.912 1.00 15.00 ? 68  ALA B N   1 
ATOM   2316 C  CA  . ALA B 1 68  ? -42.408 19.819 42.358 1.00 14.80 ? 68  ALA B CA  1 
ATOM   2317 C  C   . ALA B 1 68  ? -41.237 20.505 43.070 1.00 15.02 ? 68  ALA B C   1 
ATOM   2318 O  O   . ALA B 1 68  ? -41.240 21.725 43.240 1.00 15.72 ? 68  ALA B O   1 
ATOM   2319 C  CB  . ALA B 1 68  ? -43.631 19.793 43.275 1.00 15.43 ? 68  ALA B CB  1 
ATOM   2320 N  N   . ASP B 1 69  ? -40.238 19.723 43.474 1.00 14.38 ? 69  ASP B N   1 
ATOM   2321 C  CA  . ASP B 1 69  ? -39.078 20.253 44.188 1.00 14.15 ? 69  ASP B CA  1 
ATOM   2322 C  C   . ASP B 1 69  ? -37.838 20.444 43.322 1.00 13.71 ? 69  ASP B C   1 
ATOM   2323 O  O   . ASP B 1 69  ? -36.768 20.777 43.829 1.00 13.35 ? 69  ASP B O   1 
ATOM   2324 C  CB  . ASP B 1 69  ? -38.724 19.335 45.360 1.00 17.66 ? 69  ASP B CB  1 
ATOM   2325 C  CG  . ASP B 1 69  ? -39.928 18.999 46.214 1.00 19.74 ? 69  ASP B CG  1 
ATOM   2326 O  OD1 . ASP B 1 69  ? -40.746 19.907 46.466 1.00 21.51 ? 69  ASP B OD1 1 
ATOM   2327 O  OD2 . ASP B 1 69  ? -40.057 17.828 46.627 1.00 22.85 ? 69  ASP B OD2 1 
ATOM   2328 N  N   . THR B 1 70  ? -37.980 20.232 42.021 1.00 12.82 ? 70  THR B N   1 
ATOM   2329 C  CA  . THR B 1 70  ? -36.860 20.382 41.105 1.00 12.40 ? 70  THR B CA  1 
ATOM   2330 C  C   . THR B 1 70  ? -37.391 20.903 39.773 1.00 13.39 ? 70  THR B C   1 
ATOM   2331 O  O   . THR B 1 70  ? -38.600 21.056 39.607 1.00 14.55 ? 70  THR B O   1 
ATOM   2332 C  CB  . THR B 1 70  ? -36.136 19.027 40.906 1.00 11.65 ? 70  THR B CB  1 
ATOM   2333 O  OG1 . THR B 1 70  ? -34.892 19.236 40.227 1.00 11.31 ? 70  THR B OG1 1 
ATOM   2334 C  CG2 . THR B 1 70  ? -37.005 18.067 40.109 1.00 11.62 ? 70  THR B CG2 1 
ATOM   2335 N  N   . LEU B 1 71  ? -36.497 21.192 38.832 1.00 12.55 ? 71  LEU B N   1 
ATOM   2336 C  CA  . LEU B 1 71  ? -36.923 21.696 37.528 1.00 12.09 ? 71  LEU B CA  1 
ATOM   2337 C  C   . LEU B 1 71  ? -36.959 20.597 36.466 1.00 11.56 ? 71  LEU B C   1 
ATOM   2338 O  O   . LEU B 1 71  ? -36.328 19.548 36.616 1.00 11.43 ? 71  LEU B O   1 
ATOM   2339 C  CB  . LEU B 1 71  ? -35.993 22.824 37.058 1.00 12.30 ? 71  LEU B CB  1 
ATOM   2340 C  CG  . LEU B 1 71  ? -35.926 24.111 37.888 1.00 11.73 ? 71  LEU B CG  1 
ATOM   2341 C  CD1 . LEU B 1 71  ? -35.125 25.158 37.131 1.00 9.76  ? 71  LEU B CD1 1 
ATOM   2342 C  CD2 . LEU B 1 71  ? -37.331 24.620 38.185 1.00 10.37 ? 71  LEU B CD2 1 
ATOM   2343 N  N   . ALA B 1 72  ? -37.716 20.853 35.401 1.00 10.77 ? 72  ALA B N   1 
ATOM   2344 C  CA  . ALA B 1 72  ? -37.849 19.932 34.273 1.00 10.45 ? 72  ALA B CA  1 
ATOM   2345 C  C   . ALA B 1 72  ? -37.266 20.648 33.044 1.00 10.28 ? 72  ALA B C   1 
ATOM   2346 O  O   . ALA B 1 72  ? -37.188 21.880 33.016 1.00 10.66 ? 72  ALA B O   1 
ATOM   2347 C  CB  . ALA B 1 72  ? -39.325 19.583 34.047 1.00 8.38  ? 72  ALA B CB  1 
ATOM   2348 N  N   . PRO B 1 73  ? -36.841 19.889 32.017 1.00 10.19 ? 73  PRO B N   1 
ATOM   2349 C  CA  . PRO B 1 73  ? -36.269 20.518 30.819 1.00 9.96  ? 73  PRO B CA  1 
ATOM   2350 C  C   . PRO B 1 73  ? -37.102 21.653 30.226 1.00 10.65 ? 73  PRO B C   1 
ATOM   2351 O  O   . PRO B 1 73  ? -36.556 22.643 29.739 1.00 10.86 ? 73  PRO B O   1 
ATOM   2352 C  CB  . PRO B 1 73  ? -36.099 19.350 29.849 1.00 9.89  ? 73  PRO B CB  1 
ATOM   2353 C  CG  . PRO B 1 73  ? -35.946 18.156 30.741 1.00 9.41  ? 73  PRO B CG  1 
ATOM   2354 C  CD  . PRO B 1 73  ? -36.850 18.419 31.912 1.00 8.61  ? 73  PRO B CD  1 
ATOM   2355 N  N   . ALA B 1 74  ? -38.422 21.512 30.275 1.00 11.31 ? 74  ALA B N   1 
ATOM   2356 C  CA  . ALA B 1 74  ? -39.311 22.526 29.727 1.00 12.10 ? 74  ALA B CA  1 
ATOM   2357 C  C   . ALA B 1 74  ? -39.156 23.886 30.418 1.00 12.59 ? 74  ALA B C   1 
ATOM   2358 O  O   . ALA B 1 74  ? -39.388 24.929 29.802 1.00 13.03 ? 74  ALA B O   1 
ATOM   2359 C  CB  . ALA B 1 74  ? -40.769 22.048 29.823 1.00 12.23 ? 74  ALA B CB  1 
ATOM   2360 N  N   . ASP B 1 75  ? -38.751 23.871 31.686 1.00 11.00 ? 75  ASP B N   1 
ATOM   2361 C  CA  . ASP B 1 75  ? -38.590 25.102 32.465 1.00 10.61 ? 75  ASP B CA  1 
ATOM   2362 C  C   . ASP B 1 75  ? -37.499 26.047 31.973 1.00 10.43 ? 75  ASP B C   1 
ATOM   2363 O  O   . ASP B 1 75  ? -37.483 27.217 32.350 1.00 11.24 ? 75  ASP B O   1 
ATOM   2364 C  CB  . ASP B 1 75  ? -38.322 24.764 33.937 1.00 12.92 ? 75  ASP B CB  1 
ATOM   2365 C  CG  . ASP B 1 75  ? -39.497 24.065 34.601 1.00 17.34 ? 75  ASP B CG  1 
ATOM   2366 O  OD1 . ASP B 1 75  ? -40.655 24.425 34.295 1.00 17.73 ? 75  ASP B OD1 1 
ATOM   2367 O  OD2 . ASP B 1 75  ? -39.263 23.157 35.429 1.00 14.76 ? 75  ASP B OD2 1 
ATOM   2368 N  N   . TYR B 1 76  ? -36.590 25.548 31.139 1.00 12.32 ? 76  TYR B N   1 
ATOM   2369 C  CA  . TYR B 1 76  ? -35.494 26.370 30.627 1.00 12.30 ? 76  TYR B CA  1 
ATOM   2370 C  C   . TYR B 1 76  ? -35.795 27.042 29.290 1.00 13.77 ? 76  TYR B C   1 
ATOM   2371 O  O   . TYR B 1 76  ? -34.956 27.758 28.745 1.00 14.15 ? 76  TYR B O   1 
ATOM   2372 C  CB  . TYR B 1 76  ? -34.221 25.527 30.502 1.00 13.42 ? 76  TYR B CB  1 
ATOM   2373 C  CG  . TYR B 1 76  ? -33.440 25.433 31.794 1.00 12.15 ? 76  TYR B CG  1 
ATOM   2374 C  CD1 . TYR B 1 76  ? -33.694 24.412 32.710 1.00 12.52 ? 76  TYR B CD1 1 
ATOM   2375 C  CD2 . TYR B 1 76  ? -32.486 26.397 32.125 1.00 12.16 ? 76  TYR B CD2 1 
ATOM   2376 C  CE1 . TYR B 1 76  ? -33.021 24.355 33.930 1.00 14.16 ? 76  TYR B CE1 1 
ATOM   2377 C  CE2 . TYR B 1 76  ? -31.807 26.352 33.341 1.00 12.21 ? 76  TYR B CE2 1 
ATOM   2378 C  CZ  . TYR B 1 76  ? -32.080 25.331 34.241 1.00 14.51 ? 76  TYR B CZ  1 
ATOM   2379 O  OH  . TYR B 1 76  ? -31.435 25.300 35.457 1.00 13.90 ? 76  TYR B OH  1 
ATOM   2380 N  N   . THR B 1 77  ? -36.995 26.822 28.767 1.00 14.84 ? 77  THR B N   1 
ATOM   2381 C  CA  . THR B 1 77  ? -37.387 27.412 27.491 1.00 15.47 ? 77  THR B CA  1 
ATOM   2382 C  C   . THR B 1 77  ? -37.283 28.937 27.508 1.00 14.27 ? 77  THR B C   1 
ATOM   2383 O  O   . THR B 1 77  ? -37.872 29.596 28.363 1.00 13.30 ? 77  THR B O   1 
ATOM   2384 C  CB  . THR B 1 77  ? -38.834 27.024 27.129 1.00 16.47 ? 77  THR B CB  1 
ATOM   2385 O  OG1 . THR B 1 77  ? -38.927 25.600 27.014 1.00 17.03 ? 77  THR B OG1 1 
ATOM   2386 C  CG2 . THR B 1 77  ? -39.249 27.672 25.814 1.00 15.64 ? 77  THR B CG2 1 
ATOM   2387 N  N   . GLY B 1 78  ? -36.534 29.485 26.555 1.00 14.90 ? 78  GLY B N   1 
ATOM   2388 C  CA  . GLY B 1 78  ? -36.366 30.926 26.464 1.00 15.39 ? 78  GLY B CA  1 
ATOM   2389 C  C   . GLY B 1 78  ? -35.415 31.541 27.478 1.00 16.19 ? 78  GLY B C   1 
ATOM   2390 O  O   . GLY B 1 78  ? -35.241 32.760 27.506 1.00 17.05 ? 78  GLY B O   1 
ATOM   2391 N  N   . ALA B 1 79  ? -34.782 30.711 28.301 1.00 13.61 ? 79  ALA B N   1 
ATOM   2392 C  CA  . ALA B 1 79  ? -33.871 31.210 29.323 1.00 14.16 ? 79  ALA B CA  1 
ATOM   2393 C  C   . ALA B 1 79  ? -32.621 31.888 28.767 1.00 14.36 ? 79  ALA B C   1 
ATOM   2394 O  O   . ALA B 1 79  ? -32.230 32.958 29.238 1.00 13.60 ? 79  ALA B O   1 
ATOM   2395 C  CB  . ALA B 1 79  ? -33.473 30.079 30.263 1.00 12.50 ? 79  ALA B CB  1 
ATOM   2396 N  N   . ASN B 1 80  ? -31.990 31.275 27.772 1.00 14.76 ? 80  ASN B N   1 
ATOM   2397 C  CA  . ASN B 1 80  ? -30.781 31.852 27.195 1.00 16.52 ? 80  ASN B CA  1 
ATOM   2398 C  C   . ASN B 1 80  ? -31.012 33.211 26.532 1.00 17.60 ? 80  ASN B C   1 
ATOM   2399 O  O   . ASN B 1 80  ? -30.199 34.125 26.672 1.00 17.53 ? 80  ASN B O   1 
ATOM   2400 C  CB  . ASN B 1 80  ? -30.162 30.893 26.179 1.00 19.67 ? 80  ASN B CB  1 
ATOM   2401 C  CG  . ASN B 1 80  ? -28.879 31.441 25.575 1.00 24.95 ? 80  ASN B CG  1 
ATOM   2402 O  OD1 . ASN B 1 80  ? -28.875 31.938 24.449 1.00 26.51 ? 80  ASN B OD1 1 
ATOM   2403 N  ND2 . ASN B 1 80  ? -27.784 31.358 26.325 1.00 26.85 ? 80  ASN B ND2 1 
ATOM   2404 N  N   . ALA B 1 81  ? -32.118 33.347 25.812 1.00 18.24 ? 81  ALA B N   1 
ATOM   2405 C  CA  . ALA B 1 81  ? -32.422 34.600 25.130 1.00 19.40 ? 81  ALA B CA  1 
ATOM   2406 C  C   . ALA B 1 81  ? -32.767 35.728 26.098 1.00 19.79 ? 81  ALA B C   1 
ATOM   2407 O  O   . ALA B 1 81  ? -32.421 36.887 25.865 1.00 21.83 ? 81  ALA B O   1 
ATOM   2408 C  CB  . ALA B 1 81  ? -33.572 34.389 24.148 1.00 18.93 ? 81  ALA B CB  1 
ATOM   2409 N  N   . ALA B 1 82  ? -33.441 35.386 27.189 1.00 17.81 ? 82  ALA B N   1 
ATOM   2410 C  CA  . ALA B 1 82  ? -33.845 36.386 28.165 1.00 18.14 ? 82  ALA B CA  1 
ATOM   2411 C  C   . ALA B 1 82  ? -32.788 36.774 29.199 1.00 18.00 ? 82  ALA B C   1 
ATOM   2412 O  O   . ALA B 1 82  ? -32.580 37.960 29.457 1.00 18.19 ? 82  ALA B O   1 
ATOM   2413 C  CB  . ALA B 1 82  ? -35.114 35.921 28.880 1.00 17.13 ? 82  ALA B CB  1 
ATOM   2414 N  N   . LEU B 1 83  ? -32.123 35.782 29.786 1.00 17.77 ? 83  LEU B N   1 
ATOM   2415 C  CA  . LEU B 1 83  ? -31.129 36.043 30.828 1.00 16.63 ? 83  LEU B CA  1 
ATOM   2416 C  C   . LEU B 1 83  ? -29.685 35.740 30.456 1.00 16.04 ? 83  LEU B C   1 
ATOM   2417 O  O   . LEU B 1 83  ? -28.777 35.965 31.256 1.00 16.29 ? 83  LEU B O   1 
ATOM   2418 C  CB  . LEU B 1 83  ? -31.489 35.248 32.084 1.00 16.25 ? 83  LEU B CB  1 
ATOM   2419 C  CG  . LEU B 1 83  ? -32.966 35.264 32.473 1.00 17.61 ? 83  LEU B CG  1 
ATOM   2420 C  CD1 . LEU B 1 83  ? -33.344 33.953 33.139 1.00 19.66 ? 83  LEU B CD1 1 
ATOM   2421 C  CD2 . LEU B 1 83  ? -33.225 36.427 33.407 1.00 19.66 ? 83  LEU B CD2 1 
ATOM   2422 N  N   . LYS B 1 84  ? -29.474 35.229 29.251 1.00 14.89 ? 84  LYS B N   1 
ATOM   2423 C  CA  . LYS B 1 84  ? -28.135 34.885 28.797 1.00 16.41 ? 84  LYS B CA  1 
ATOM   2424 C  C   . LYS B 1 84  ? -27.494 33.869 29.737 1.00 16.43 ? 84  LYS B C   1 
ATOM   2425 O  O   . LYS B 1 84  ? -26.329 34.009 30.128 1.00 16.32 ? 84  LYS B O   1 
ATOM   2426 C  CB  . LYS B 1 84  ? -27.258 36.136 28.709 1.00 24.91 ? 84  LYS B CB  1 
ATOM   2427 C  CG  . LYS B 1 84  ? -26.347 36.158 27.492 1.00 30.90 ? 84  LYS B CG  1 
ATOM   2428 C  CD  . LYS B 1 84  ? -27.005 36.881 26.323 1.00 36.69 ? 84  LYS B CD  1 
ATOM   2429 C  CE  . LYS B 1 84  ? -27.762 35.911 25.419 1.00 38.40 ? 84  LYS B CE  1 
ATOM   2430 N  NZ  . LYS B 1 84  ? -28.782 36.604 24.573 1.00 38.74 ? 84  LYS B NZ  1 
ATOM   2431 N  N   . VAL B 1 85  ? -28.265 32.852 30.105 1.00 13.56 ? 85  VAL B N   1 
ATOM   2432 C  CA  . VAL B 1 85  ? -27.771 31.801 30.983 1.00 13.65 ? 85  VAL B CA  1 
ATOM   2433 C  C   . VAL B 1 85  ? -27.721 30.483 30.223 1.00 14.05 ? 85  VAL B C   1 
ATOM   2434 O  O   . VAL B 1 85  ? -28.415 30.308 29.219 1.00 14.36 ? 85  VAL B O   1 
ATOM   2435 C  CB  . VAL B 1 85  ? -28.679 31.617 32.222 1.00 13.25 ? 85  VAL B CB  1 
ATOM   2436 C  CG1 . VAL B 1 85  ? -28.698 32.889 33.044 1.00 10.87 ? 85  VAL B CG1 1 
ATOM   2437 C  CG2 . VAL B 1 85  ? -30.088 31.236 31.786 1.00 13.89 ? 85  VAL B CG2 1 
ATOM   2438 N  N   . ASP B 1 86  ? -26.887 29.566 30.703 1.00 13.63 ? 86  ASP B N   1 
ATOM   2439 C  CA  . ASP B 1 86  ? -26.742 28.245 30.100 1.00 13.50 ? 86  ASP B CA  1 
ATOM   2440 C  C   . ASP B 1 86  ? -27.224 27.241 31.129 1.00 13.09 ? 86  ASP B C   1 
ATOM   2441 O  O   . ASP B 1 86  ? -27.458 27.593 32.285 1.00 13.76 ? 86  ASP B O   1 
ATOM   2442 C  CB  . ASP B 1 86  ? -25.270 27.923 29.824 1.00 15.14 ? 86  ASP B CB  1 
ATOM   2443 C  CG  . ASP B 1 86  ? -24.711 28.662 28.631 1.00 16.99 ? 86  ASP B CG  1 
ATOM   2444 O  OD1 . ASP B 1 86  ? -25.499 29.196 27.826 1.00 18.94 ? 86  ASP B OD1 1 
ATOM   2445 O  OD2 . ASP B 1 86  ? -23.467 28.699 28.504 1.00 15.10 ? 86  ASP B OD2 1 
ATOM   2446 N  N   . ARG B 1 87  ? -27.377 25.991 30.714 1.00 12.08 ? 87  ARG B N   1 
ATOM   2447 C  CA  . ARG B 1 87  ? -27.748 24.952 31.659 1.00 12.83 ? 87  ARG B CA  1 
ATOM   2448 C  C   . ARG B 1 87  ? -26.379 24.578 32.235 1.00 12.47 ? 87  ARG B C   1 
ATOM   2449 O  O   . ARG B 1 87  ? -25.667 23.751 31.670 1.00 12.60 ? 87  ARG B O   1 
ATOM   2450 C  CB  . ARG B 1 87  ? -28.379 23.761 30.936 1.00 12.06 ? 87  ARG B CB  1 
ATOM   2451 C  CG  . ARG B 1 87  ? -29.798 24.026 30.442 1.00 13.99 ? 87  ARG B CG  1 
ATOM   2452 C  CD  . ARG B 1 87  ? -30.179 23.071 29.321 1.00 16.86 ? 87  ARG B CD  1 
ATOM   2453 N  NE  . ARG B 1 87  ? -31.471 23.398 28.722 1.00 16.41 ? 87  ARG B NE  1 
ATOM   2454 C  CZ  . ARG B 1 87  ? -31.636 24.226 27.692 1.00 19.41 ? 87  ARG B CZ  1 
ATOM   2455 N  NH1 . ARG B 1 87  ? -30.588 24.823 27.139 1.00 16.95 ? 87  ARG B NH1 1 
ATOM   2456 N  NH2 . ARG B 1 87  ? -32.850 24.453 27.209 1.00 16.57 ? 87  ARG B NH2 1 
ATOM   2457 N  N   . GLY B 1 88  ? -26.009 25.214 33.344 1.00 11.27 ? 88  GLY B N   1 
ATOM   2458 C  CA  . GLY B 1 88  ? -24.707 24.968 33.946 1.00 11.07 ? 88  GLY B CA  1 
ATOM   2459 C  C   . GLY B 1 88  ? -24.579 23.831 34.942 1.00 9.99  ? 88  GLY B C   1 
ATOM   2460 O  O   . GLY B 1 88  ? -25.267 23.798 35.962 1.00 11.03 ? 88  GLY B O   1 
ATOM   2461 N  N   . HIS B 1 89  ? -23.680 22.900 34.644 1.00 9.10  ? 89  HIS B N   1 
ATOM   2462 C  CA  . HIS B 1 89  ? -23.435 21.756 35.515 1.00 10.18 ? 89  HIS B CA  1 
ATOM   2463 C  C   . HIS B 1 89  ? -22.781 22.210 36.817 1.00 10.24 ? 89  HIS B C   1 
ATOM   2464 O  O   . HIS B 1 89  ? -21.978 23.147 36.821 1.00 9.31  ? 89  HIS B O   1 
ATOM   2465 C  CB  . HIS B 1 89  ? -22.468 20.762 34.859 1.00 11.43 ? 89  HIS B CB  1 
ATOM   2466 C  CG  . HIS B 1 89  ? -23.040 20.012 33.696 1.00 12.34 ? 89  HIS B CG  1 
ATOM   2467 N  ND1 . HIS B 1 89  ? -22.960 20.477 32.401 1.00 13.90 ? 89  HIS B ND1 1 
ATOM   2468 C  CD2 . HIS B 1 89  ? -23.652 18.806 33.626 1.00 12.88 ? 89  HIS B CD2 1 
ATOM   2469 C  CE1 . HIS B 1 89  ? -23.499 19.590 31.583 1.00 12.69 ? 89  HIS B CE1 1 
ATOM   2470 N  NE2 . HIS B 1 89  ? -23.926 18.567 32.301 1.00 13.21 ? 89  HIS B NE2 1 
ATOM   2471 N  N   . GLN B 1 90  ? -23.128 21.547 37.917 1.00 9.31  ? 90  GLN B N   1 
ATOM   2472 C  CA  . GLN B 1 90  ? -22.498 21.834 39.202 1.00 10.20 ? 90  GLN B CA  1 
ATOM   2473 C  C   . GLN B 1 90  ? -21.336 20.833 39.204 1.00 10.25 ? 90  GLN B C   1 
ATOM   2474 O  O   . GLN B 1 90  ? -20.171 21.225 39.209 1.00 11.82 ? 90  GLN B O   1 
ATOM   2475 C  CB  . GLN B 1 90  ? -23.470 21.584 40.359 1.00 9.35  ? 90  GLN B CB  1 
ATOM   2476 C  CG  . GLN B 1 90  ? -24.654 22.554 40.364 1.00 8.80  ? 90  GLN B CG  1 
ATOM   2477 C  CD  . GLN B 1 90  ? -24.884 23.230 41.710 1.00 10.62 ? 90  GLN B CD  1 
ATOM   2478 O  OE1 . GLN B 1 90  ? -23.944 23.682 42.363 1.00 10.16 ? 90  GLN B OE1 1 
ATOM   2479 N  NE2 . GLN B 1 90  ? -26.145 23.308 42.124 1.00 7.87  ? 90  GLN B NE2 1 
ATOM   2480 N  N   . ALA B 1 91  ? -21.654 19.541 39.176 1.00 8.84  ? 91  ALA B N   1 
ATOM   2481 C  CA  . ALA B 1 91  ? -20.621 18.510 39.094 1.00 8.91  ? 91  ALA B CA  1 
ATOM   2482 C  C   . ALA B 1 91  ? -20.327 18.456 37.593 1.00 8.98  ? 91  ALA B C   1 
ATOM   2483 O  O   . ALA B 1 91  ? -21.233 18.241 36.789 1.00 9.39  ? 91  ALA B O   1 
ATOM   2484 C  CB  . ALA B 1 91  ? -21.157 17.169 39.581 1.00 7.20  ? 91  ALA B CB  1 
ATOM   2485 N  N   . PRO B 1 92  ? -19.056 18.641 37.197 1.00 10.93 ? 92  PRO B N   1 
ATOM   2486 C  CA  . PRO B 1 92  ? -18.669 18.626 35.779 1.00 11.31 ? 92  PRO B CA  1 
ATOM   2487 C  C   . PRO B 1 92  ? -18.830 17.304 35.031 1.00 11.82 ? 92  PRO B C   1 
ATOM   2488 O  O   . PRO B 1 92  ? -18.392 16.249 35.489 1.00 12.38 ? 92  PRO B O   1 
ATOM   2489 C  CB  . PRO B 1 92  ? -17.223 19.119 35.796 1.00 10.95 ? 92  PRO B CB  1 
ATOM   2490 C  CG  . PRO B 1 92  ? -16.726 18.771 37.158 1.00 12.12 ? 92  PRO B CG  1 
ATOM   2491 C  CD  . PRO B 1 92  ? -17.899 18.848 38.086 1.00 9.85  ? 92  PRO B CD  1 
ATOM   2492 N  N   . LEU B 1 93  ? -19.456 17.383 33.862 1.00 11.02 ? 93  LEU B N   1 
ATOM   2493 C  CA  . LEU B 1 93  ? -19.699 16.209 33.032 1.00 12.37 ? 93  LEU B CA  1 
ATOM   2494 C  C   . LEU B 1 93  ? -18.418 15.496 32.609 1.00 12.20 ? 93  LEU B C   1 
ATOM   2495 O  O   . LEU B 1 93  ? -18.242 14.312 32.882 1.00 13.33 ? 93  LEU B O   1 
ATOM   2496 C  CB  . LEU B 1 93  ? -20.500 16.610 31.786 1.00 12.32 ? 93  LEU B CB  1 
ATOM   2497 C  CG  . LEU B 1 93  ? -20.934 15.504 30.816 1.00 11.78 ? 93  LEU B CG  1 
ATOM   2498 C  CD1 . LEU B 1 93  ? -21.794 14.479 31.532 1.00 11.56 ? 93  LEU B CD1 1 
ATOM   2499 C  CD2 . LEU B 1 93  ? -21.701 16.127 29.667 1.00 11.81 ? 93  LEU B CD2 1 
ATOM   2500 N  N   . ALA B 1 94  ? -17.524 16.227 31.953 1.00 14.09 ? 94  ALA B N   1 
ATOM   2501 C  CA  . ALA B 1 94  ? -16.266 15.664 31.460 1.00 15.20 ? 94  ALA B CA  1 
ATOM   2502 C  C   . ALA B 1 94  ? -15.368 15.003 32.513 1.00 15.47 ? 94  ALA B C   1 
ATOM   2503 O  O   . ALA B 1 94  ? -14.673 14.029 32.218 1.00 16.19 ? 94  ALA B O   1 
ATOM   2504 C  CB  . ALA B 1 94  ? -15.480 16.745 30.722 1.00 11.61 ? 94  ALA B CB  1 
ATOM   2505 N  N   . SER B 1 95  ? -15.378 15.527 33.734 1.00 13.68 ? 95  SER B N   1 
ATOM   2506 C  CA  . SER B 1 95  ? -14.540 14.983 34.799 1.00 12.64 ? 95  SER B CA  1 
ATOM   2507 C  C   . SER B 1 95  ? -15.081 13.716 35.447 1.00 11.10 ? 95  SER B C   1 
ATOM   2508 O  O   . SER B 1 95  ? -14.327 12.966 36.066 1.00 11.07 ? 95  SER B O   1 
ATOM   2509 C  CB  . SER B 1 95  ? -14.328 16.036 35.887 1.00 9.31  ? 95  SER B CB  1 
ATOM   2510 O  OG  . SER B 1 95  ? -13.988 17.284 35.317 1.00 12.87 ? 95  SER B OG  1 
ATOM   2511 N  N   . LEU B 1 96  ? -16.377 13.469 35.298 1.00 10.53 ? 96  LEU B N   1 
ATOM   2512 C  CA  . LEU B 1 96  ? -16.985 12.302 35.928 1.00 11.51 ? 96  LEU B CA  1 
ATOM   2513 C  C   . LEU B 1 96  ? -17.823 11.400 35.027 1.00 11.91 ? 96  LEU B C   1 
ATOM   2514 O  O   . LEU B 1 96  ? -18.390 10.415 35.504 1.00 12.11 ? 96  LEU B O   1 
ATOM   2515 C  CB  . LEU B 1 96  ? -17.859 12.759 37.101 1.00 12.25 ? 96  LEU B CB  1 
ATOM   2516 C  CG  . LEU B 1 96  ? -17.208 13.696 38.119 1.00 12.77 ? 96  LEU B CG  1 
ATOM   2517 C  CD1 . LEU B 1 96  ? -18.216 14.738 38.593 1.00 10.99 ? 96  LEU B CD1 1 
ATOM   2518 C  CD2 . LEU B 1 96  ? -16.684 12.869 39.287 1.00 12.44 ? 96  LEU B CD2 1 
ATOM   2519 N  N   . ALA B 1 97  ? -17.901 11.720 33.738 1.00 12.44 ? 97  ALA B N   1 
ATOM   2520 C  CA  . ALA B 1 97  ? -18.717 10.937 32.810 1.00 14.55 ? 97  ALA B CA  1 
ATOM   2521 C  C   . ALA B 1 97  ? -18.319 9.465  32.684 1.00 16.48 ? 97  ALA B C   1 
ATOM   2522 O  O   . ALA B 1 97  ? -18.990 8.695  31.993 1.00 16.60 ? 97  ALA B O   1 
ATOM   2523 C  CB  . ALA B 1 97  ? -18.717 11.598 31.436 1.00 14.77 ? 97  ALA B CB  1 
ATOM   2524 N  N   . GLY B 1 98  ? -17.240 9.073  33.353 1.00 16.21 ? 98  GLY B N   1 
ATOM   2525 C  CA  . GLY B 1 98  ? -16.800 7.690  33.289 1.00 15.82 ? 98  GLY B CA  1 
ATOM   2526 C  C   . GLY B 1 98  ? -17.488 6.760  34.274 1.00 15.54 ? 98  GLY B C   1 
ATOM   2527 O  O   . GLY B 1 98  ? -17.401 5.544  34.137 1.00 17.20 ? 98  GLY B O   1 
ATOM   2528 N  N   . VAL B 1 99  ? -18.170 7.315  35.270 1.00 14.64 ? 99  VAL B N   1 
ATOM   2529 C  CA  . VAL B 1 99  ? -18.860 6.497  36.267 1.00 14.00 ? 99  VAL B CA  1 
ATOM   2530 C  C   . VAL B 1 99  ? -20.070 5.788  35.660 1.00 14.36 ? 99  VAL B C   1 
ATOM   2531 O  O   . VAL B 1 99  ? -20.574 6.194  34.613 1.00 14.16 ? 99  VAL B O   1 
ATOM   2532 C  CB  . VAL B 1 99  ? -19.311 7.350  37.475 1.00 14.09 ? 99  VAL B CB  1 
ATOM   2533 C  CG1 . VAL B 1 99  ? -18.091 7.955  38.154 1.00 14.92 ? 99  VAL B CG1 1 
ATOM   2534 C  CG2 . VAL B 1 99  ? -20.267 8.454  37.023 1.00 13.48 ? 99  VAL B CG2 1 
ATOM   2535 N  N   . SER B 1 100 ? -20.537 4.739  36.331 1.00 13.71 ? 100 SER B N   1 
ATOM   2536 C  CA  . SER B 1 100 ? -21.661 3.945  35.846 1.00 15.37 ? 100 SER B CA  1 
ATOM   2537 C  C   . SER B 1 100 ? -23.007 4.660  35.715 1.00 16.31 ? 100 SER B C   1 
ATOM   2538 O  O   . SER B 1 100 ? -23.825 4.282  34.880 1.00 18.43 ? 100 SER B O   1 
ATOM   2539 C  CB  . SER B 1 100 ? -21.832 2.696  36.717 1.00 17.41 ? 100 SER B CB  1 
ATOM   2540 O  OG  . SER B 1 100 ? -22.242 3.037  38.028 1.00 22.42 ? 100 SER B OG  1 
ATOM   2541 N  N   . ASP B 1 101 ? -23.253 5.678  36.531 1.00 14.68 ? 101 ASP B N   1 
ATOM   2542 C  CA  . ASP B 1 101 ? -24.521 6.400  36.441 1.00 13.47 ? 101 ASP B CA  1 
ATOM   2543 C  C   . ASP B 1 101 ? -24.283 7.807  35.915 1.00 12.50 ? 101 ASP B C   1 
ATOM   2544 O  O   . ASP B 1 101 ? -24.943 8.758  36.336 1.00 11.97 ? 101 ASP B O   1 
ATOM   2545 C  CB  . ASP B 1 101 ? -25.211 6.459  37.813 1.00 14.92 ? 101 ASP B CB  1 
ATOM   2546 C  CG  . ASP B 1 101 ? -24.264 6.868  38.941 1.00 17.07 ? 101 ASP B CG  1 
ATOM   2547 O  OD1 . ASP B 1 101 ? -23.218 7.493  38.661 1.00 16.43 ? 101 ASP B OD1 1 
ATOM   2548 O  OD2 . ASP B 1 101 ? -24.572 6.562  40.115 1.00 16.96 ? 101 ASP B OD2 1 
ATOM   2549 N  N   . TRP B 1 102 ? -23.347 7.925  34.978 1.00 11.51 ? 102 TRP B N   1 
ATOM   2550 C  CA  . TRP B 1 102 ? -22.983 9.218  34.403 1.00 12.47 ? 102 TRP B CA  1 
ATOM   2551 C  C   . TRP B 1 102 ? -24.141 10.063 33.854 1.00 12.34 ? 102 TRP B C   1 
ATOM   2552 O  O   . TRP B 1 102 ? -24.054 11.288 33.848 1.00 12.22 ? 102 TRP B O   1 
ATOM   2553 C  CB  . TRP B 1 102 ? -21.922 9.021  33.313 1.00 13.24 ? 102 TRP B CB  1 
ATOM   2554 C  CG  . TRP B 1 102 ? -22.461 8.417  32.067 1.00 14.86 ? 102 TRP B CG  1 
ATOM   2555 C  CD1 . TRP B 1 102 ? -22.545 7.087  31.771 1.00 15.77 ? 102 TRP B CD1 1 
ATOM   2556 C  CD2 . TRP B 1 102 ? -23.039 9.113  30.960 1.00 16.06 ? 102 TRP B CD2 1 
ATOM   2557 N  NE1 . TRP B 1 102 ? -23.145 6.911  30.546 1.00 16.86 ? 102 TRP B NE1 1 
ATOM   2558 C  CE2 . TRP B 1 102 ? -23.458 8.140  30.027 1.00 17.99 ? 102 TRP B CE2 1 
ATOM   2559 C  CE3 . TRP B 1 102 ? -23.246 10.467 30.664 1.00 16.56 ? 102 TRP B CE3 1 
ATOM   2560 C  CZ2 . TRP B 1 102 ? -24.074 8.479  28.816 1.00 18.48 ? 102 TRP B CZ2 1 
ATOM   2561 C  CZ3 . TRP B 1 102 ? -23.859 10.804 29.459 1.00 17.49 ? 102 TRP B CZ3 1 
ATOM   2562 C  CH2 . TRP B 1 102 ? -24.266 9.812  28.552 1.00 16.41 ? 102 TRP B CH2 1 
ATOM   2563 N  N   . GLU B 1 103 ? -25.216 9.423  33.399 1.00 12.15 ? 103 GLU B N   1 
ATOM   2564 C  CA  . GLU B 1 103 ? -26.361 10.160 32.854 1.00 13.39 ? 103 GLU B CA  1 
ATOM   2565 C  C   . GLU B 1 103 ? -26.967 11.113 33.880 1.00 11.29 ? 103 GLU B C   1 
ATOM   2566 O  O   . GLU B 1 103 ? -27.588 12.113 33.519 1.00 10.01 ? 103 GLU B O   1 
ATOM   2567 C  CB  . GLU B 1 103 ? -27.449 9.195  32.370 1.00 19.90 ? 103 GLU B CB  1 
ATOM   2568 C  CG  . GLU B 1 103 ? -27.012 8.269  31.252 1.00 27.91 ? 103 GLU B CG  1 
ATOM   2569 C  CD  . GLU B 1 103 ? -26.852 6.828  31.720 1.00 34.72 ? 103 GLU B CD  1 
ATOM   2570 O  OE1 . GLU B 1 103 ? -26.280 6.616  32.817 1.00 34.58 ? 103 GLU B OE1 1 
ATOM   2571 O  OE2 . GLU B 1 103 ? -27.300 5.911  30.990 1.00 35.86 ? 103 GLU B OE2 1 
ATOM   2572 N  N   . SER B 1 104 ? -26.789 10.795 35.160 1.00 11.64 ? 104 SER B N   1 
ATOM   2573 C  CA  . SER B 1 104 ? -27.321 11.624 36.240 1.00 11.07 ? 104 SER B CA  1 
ATOM   2574 C  C   . SER B 1 104 ? -26.629 12.989 36.307 1.00 9.79  ? 104 SER B C   1 
ATOM   2575 O  O   . SER B 1 104 ? -27.108 13.904 36.976 1.00 9.34  ? 104 SER B O   1 
ATOM   2576 C  CB  . SER B 1 104 ? -27.174 10.897 37.581 1.00 11.38 ? 104 SER B CB  1 
ATOM   2577 O  OG  . SER B 1 104 ? -25.812 10.794 37.961 1.00 13.09 ? 104 SER B OG  1 
ATOM   2578 N  N   . LEU B 1 105 ? -25.499 13.125 35.617 1.00 7.20  ? 105 LEU B N   1 
ATOM   2579 C  CA  . LEU B 1 105 ? -24.781 14.393 35.600 1.00 7.16  ? 105 LEU B CA  1 
ATOM   2580 C  C   . LEU B 1 105 ? -25.600 15.407 34.813 1.00 8.02  ? 105 LEU B C   1 
ATOM   2581 O  O   . LEU B 1 105 ? -25.412 16.621 34.941 1.00 7.92  ? 105 LEU B O   1 
ATOM   2582 C  CB  . LEU B 1 105 ? -23.407 14.221 34.950 1.00 9.02  ? 105 LEU B CB  1 
ATOM   2583 C  CG  . LEU B 1 105 ? -22.375 13.440 35.767 1.00 9.54  ? 105 LEU B CG  1 
ATOM   2584 C  CD1 . LEU B 1 105 ? -21.265 12.945 34.849 1.00 8.90  ? 105 LEU B CD1 1 
ATOM   2585 C  CD2 . LEU B 1 105 ? -21.819 14.336 36.869 1.00 10.98 ? 105 LEU B CD2 1 
ATOM   2586 N  N   . ASN B 1 106 ? -26.522 14.899 34.001 1.00 10.24 ? 106 ASN B N   1 
ATOM   2587 C  CA  . ASN B 1 106 ? -27.368 15.759 33.186 1.00 10.01 ? 106 ASN B CA  1 
ATOM   2588 C  C   . ASN B 1 106 ? -28.794 15.869 33.724 1.00 10.54 ? 106 ASN B C   1 
ATOM   2589 O  O   . ASN B 1 106 ? -29.684 16.383 33.044 1.00 11.26 ? 106 ASN B O   1 
ATOM   2590 C  CB  . ASN B 1 106 ? -27.362 15.272 31.737 1.00 10.11 ? 106 ASN B CB  1 
ATOM   2591 C  CG  . ASN B 1 106 ? -25.989 15.397 31.091 1.00 10.83 ? 106 ASN B CG  1 
ATOM   2592 O  OD1 . ASN B 1 106 ? -25.334 16.431 31.202 1.00 11.76 ? 106 ASN B OD1 1 
ATOM   2593 N  ND2 . ASN B 1 106 ? -25.547 14.341 30.419 1.00 12.12 ? 106 ASN B ND2 1 
ATOM   2594 N  N   . TYR B 1 107 ? -29.012 15.374 34.941 1.00 9.53  ? 107 TYR B N   1 
ATOM   2595 C  CA  . TYR B 1 107 ? -30.321 15.498 35.576 1.00 10.01 ? 107 TYR B CA  1 
ATOM   2596 C  C   . TYR B 1 107 ? -30.338 16.965 35.988 1.00 10.09 ? 107 TYR B C   1 
ATOM   2597 O  O   . TYR B 1 107 ? -29.300 17.507 36.372 1.00 9.79  ? 107 TYR B O   1 
ATOM   2598 C  CB  . TYR B 1 107 ? -30.417 14.604 36.816 1.00 11.14 ? 107 TYR B CB  1 
ATOM   2599 C  CG  . TYR B 1 107 ? -30.621 13.139 36.503 1.00 12.20 ? 107 TYR B CG  1 
ATOM   2600 C  CD1 . TYR B 1 107 ? -30.839 12.706 35.192 1.00 12.16 ? 107 TYR B CD1 1 
ATOM   2601 C  CD2 . TYR B 1 107 ? -30.572 12.181 37.515 1.00 12.21 ? 107 TYR B CD2 1 
ATOM   2602 C  CE1 . TYR B 1 107 ? -31.001 11.352 34.898 1.00 14.65 ? 107 TYR B CE1 1 
ATOM   2603 C  CE2 . TYR B 1 107 ? -30.732 10.824 37.234 1.00 13.54 ? 107 TYR B CE2 1 
ATOM   2604 C  CZ  . TYR B 1 107 ? -30.945 10.417 35.923 1.00 14.92 ? 107 TYR B CZ  1 
ATOM   2605 O  OH  . TYR B 1 107 ? -31.088 9.078  35.637 1.00 15.92 ? 107 TYR B OH  1 
ATOM   2606 N  N   . LEU B 1 108 ? -31.494 17.616 35.920 1.00 9.25  ? 108 LEU B N   1 
ATOM   2607 C  CA  . LEU B 1 108 ? -31.548 19.033 36.252 1.00 9.27  ? 108 LEU B CA  1 
ATOM   2608 C  C   . LEU B 1 108 ? -31.262 19.392 37.709 1.00 8.92  ? 108 LEU B C   1 
ATOM   2609 O  O   . LEU B 1 108 ? -31.148 20.562 38.044 1.00 10.40 ? 108 LEU B O   1 
ATOM   2610 C  CB  . LEU B 1 108 ? -32.886 19.628 35.793 1.00 10.24 ? 108 LEU B CB  1 
ATOM   2611 C  CG  . LEU B 1 108 ? -33.044 19.665 34.263 1.00 12.46 ? 108 LEU B CG  1 
ATOM   2612 C  CD1 . LEU B 1 108 ? -34.211 20.549 33.888 1.00 13.87 ? 108 LEU B CD1 1 
ATOM   2613 C  CD2 . LEU B 1 108 ? -31.773 20.181 33.612 1.00 13.47 ? 108 LEU B CD2 1 
ATOM   2614 N  N   . SER B 1 109 ? -31.134 18.397 38.577 1.00 10.22 ? 109 SER B N   1 
ATOM   2615 C  CA  . SER B 1 109 ? -30.818 18.676 39.975 1.00 10.20 ? 109 SER B CA  1 
ATOM   2616 C  C   . SER B 1 109 ? -29.338 19.077 40.068 1.00 11.53 ? 109 SER B C   1 
ATOM   2617 O  O   . SER B 1 109 ? -28.896 19.677 41.053 1.00 11.09 ? 109 SER B O   1 
ATOM   2618 C  CB  . SER B 1 109 ? -31.068 17.436 40.827 1.00 7.97  ? 109 SER B CB  1 
ATOM   2619 O  OG  . SER B 1 109 ? -30.493 16.294 40.221 1.00 8.72  ? 109 SER B OG  1 
ATOM   2620 N  N   . ASN B 1 110 ? -28.586 18.740 39.024 1.00 9.87  ? 110 ASN B N   1 
ATOM   2621 C  CA  . ASN B 1 110 ? -27.158 19.036 38.949 1.00 8.60  ? 110 ASN B CA  1 
ATOM   2622 C  C   . ASN B 1 110 ? -26.904 20.237 38.046 1.00 9.19  ? 110 ASN B C   1 
ATOM   2623 O  O   . ASN B 1 110 ? -25.765 20.530 37.698 1.00 10.23 ? 110 ASN B O   1 
ATOM   2624 C  CB  . ASN B 1 110 ? -26.404 17.818 38.404 1.00 7.02  ? 110 ASN B CB  1 
ATOM   2625 C  CG  . ASN B 1 110 ? -24.899 18.010 38.412 1.00 10.38 ? 110 ASN B CG  1 
ATOM   2626 O  OD1 . ASN B 1 110 ? -24.331 18.486 39.395 1.00 8.53  ? 110 ASN B OD1 1 
ATOM   2627 N  ND2 . ASN B 1 110 ? -24.244 17.642 37.311 1.00 8.54  ? 110 ASN B ND2 1 
ATOM   2628 N  N   . ILE B 1 111 ? -27.976 20.932 37.682 1.00 9.92  ? 111 ILE B N   1 
ATOM   2629 C  CA  . ILE B 1 111 ? -27.897 22.093 36.806 1.00 9.28  ? 111 ILE B CA  1 
ATOM   2630 C  C   . ILE B 1 111 ? -28.545 23.326 37.444 1.00 9.53  ? 111 ILE B C   1 
ATOM   2631 O  O   . ILE B 1 111 ? -29.402 23.207 38.320 1.00 9.77  ? 111 ILE B O   1 
ATOM   2632 C  CB  . ILE B 1 111 ? -28.630 21.804 35.470 1.00 10.81 ? 111 ILE B CB  1 
ATOM   2633 C  CG1 . ILE B 1 111 ? -28.084 20.520 34.841 1.00 11.91 ? 111 ILE B CG1 1 
ATOM   2634 C  CG2 . ILE B 1 111 ? -28.502 22.992 34.516 1.00 12.17 ? 111 ILE B CG2 1 
ATOM   2635 C  CD1 . ILE B 1 111 ? -26.680 20.638 34.316 1.00 13.81 ? 111 ILE B CD1 1 
ATOM   2636 N  N   . THR B 1 112 ? -28.113 24.506 37.007 1.00 8.59  ? 112 THR B N   1 
ATOM   2637 C  CA  . THR B 1 112 ? -28.672 25.776 37.466 1.00 8.19  ? 112 THR B CA  1 
ATOM   2638 C  C   . THR B 1 112 ? -28.522 26.753 36.306 1.00 9.38  ? 112 THR B C   1 
ATOM   2639 O  O   . THR B 1 112 ? -27.731 26.513 35.390 1.00 9.14  ? 112 THR B O   1 
ATOM   2640 C  CB  . THR B 1 112 ? -27.913 26.386 38.684 1.00 9.30  ? 112 THR B CB  1 
ATOM   2641 O  OG1 . THR B 1 112 ? -26.724 27.041 38.224 1.00 9.20  ? 112 THR B OG1 1 
ATOM   2642 C  CG2 . THR B 1 112 ? -27.556 25.320 39.706 1.00 8.34  ? 112 THR B CG2 1 
ATOM   2643 N  N   . PRO B 1 113 ? -29.308 27.847 36.305 1.00 10.43 ? 113 PRO B N   1 
ATOM   2644 C  CA  . PRO B 1 113 ? -29.207 28.836 35.226 1.00 10.34 ? 113 PRO B CA  1 
ATOM   2645 C  C   . PRO B 1 113 ? -27.944 29.660 35.471 1.00 10.65 ? 113 PRO B C   1 
ATOM   2646 O  O   . PRO B 1 113 ? -27.960 30.636 36.219 1.00 11.72 ? 113 PRO B O   1 
ATOM   2647 C  CB  . PRO B 1 113 ? -30.485 29.671 35.371 1.00 11.20 ? 113 PRO B CB  1 
ATOM   2648 C  CG  . PRO B 1 113 ? -31.322 28.959 36.430 1.00 11.03 ? 113 PRO B CG  1 
ATOM   2649 C  CD  . PRO B 1 113 ? -30.358 28.206 37.271 1.00 9.86  ? 113 PRO B CD  1 
ATOM   2650 N  N   . GLN B 1 114 ? -26.849 29.245 34.846 1.00 10.66 ? 114 GLN B N   1 
ATOM   2651 C  CA  . GLN B 1 114 ? -25.561 29.904 35.008 1.00 10.74 ? 114 GLN B CA  1 
ATOM   2652 C  C   . GLN B 1 114 ? -25.225 30.806 33.820 1.00 12.06 ? 114 GLN B C   1 
ATOM   2653 O  O   . GLN B 1 114 ? -25.319 30.380 32.670 1.00 12.70 ? 114 GLN B O   1 
ATOM   2654 C  CB  . GLN B 1 114 ? -24.482 28.833 35.171 1.00 10.19 ? 114 GLN B CB  1 
ATOM   2655 C  CG  . GLN B 1 114 ? -23.138 29.346 35.635 1.00 12.02 ? 114 GLN B CG  1 
ATOM   2656 C  CD  . GLN B 1 114 ? -22.194 28.212 35.968 1.00 12.78 ? 114 GLN B CD  1 
ATOM   2657 O  OE1 . GLN B 1 114 ? -21.641 28.149 37.063 1.00 15.15 ? 114 GLN B OE1 1 
ATOM   2658 N  NE2 . GLN B 1 114 ? -22.012 27.303 35.023 1.00 10.38 ? 114 GLN B NE2 1 
ATOM   2659 N  N   . LYS B 1 115 ? -24.832 32.048 34.095 1.00 13.17 ? 115 LYS B N   1 
ATOM   2660 C  CA  . LYS B 1 115 ? -24.486 32.984 33.026 1.00 13.92 ? 115 LYS B CA  1 
ATOM   2661 C  C   . LYS B 1 115 ? -23.491 32.339 32.068 1.00 15.06 ? 115 LYS B C   1 
ATOM   2662 O  O   . LYS B 1 115 ? -22.501 31.736 32.494 1.00 15.32 ? 115 LYS B O   1 
ATOM   2663 C  CB  . LYS B 1 115 ? -23.894 34.270 33.606 1.00 13.45 ? 115 LYS B CB  1 
ATOM   2664 C  CG  . LYS B 1 115 ? -24.901 35.125 34.360 1.00 14.81 ? 115 LYS B CG  1 
ATOM   2665 C  CD  . LYS B 1 115 ? -25.910 35.785 33.423 1.00 14.72 ? 115 LYS B CD  1 
ATOM   2666 C  CE  . LYS B 1 115 ? -26.807 36.749 34.193 1.00 16.91 ? 115 LYS B CE  1 
ATOM   2667 N  NZ  . LYS B 1 115 ? -27.898 37.314 33.353 1.00 19.65 ? 115 LYS B NZ  1 
ATOM   2668 N  N   . SER B 1 116 ? -23.767 32.461 30.773 1.00 15.24 ? 116 SER B N   1 
ATOM   2669 C  CA  . SER B 1 116 ? -22.919 31.872 29.737 1.00 15.63 ? 116 SER B CA  1 
ATOM   2670 C  C   . SER B 1 116 ? -21.460 32.296 29.830 1.00 14.30 ? 116 SER B C   1 
ATOM   2671 O  O   . SER B 1 116 ? -20.562 31.492 29.593 1.00 14.90 ? 116 SER B O   1 
ATOM   2672 C  CB  . SER B 1 116 ? -23.460 32.233 28.352 1.00 17.15 ? 116 SER B CB  1 
ATOM   2673 O  OG  . SER B 1 116 ? -24.869 32.101 28.318 1.00 22.10 ? 116 SER B OG  1 
ATOM   2674 N  N   . ASP B 1 117 ? -21.228 33.558 30.168 1.00 13.26 ? 117 ASP B N   1 
ATOM   2675 C  CA  . ASP B 1 117 ? -19.869 34.078 30.272 1.00 13.77 ? 117 ASP B CA  1 
ATOM   2676 C  C   . ASP B 1 117 ? -19.094 33.443 31.414 1.00 12.68 ? 117 ASP B C   1 
ATOM   2677 O  O   . ASP B 1 117 ? -17.874 33.321 31.349 1.00 13.61 ? 117 ASP B O   1 
ATOM   2678 C  CB  . ASP B 1 117 ? -19.899 35.599 30.433 1.00 16.38 ? 117 ASP B CB  1 
ATOM   2679 C  CG  . ASP B 1 117 ? -20.307 36.305 29.154 1.00 19.93 ? 117 ASP B CG  1 
ATOM   2680 O  OD1 . ASP B 1 117 ? -20.130 35.711 28.067 1.00 18.79 ? 117 ASP B OD1 1 
ATOM   2681 O  OD2 . ASP B 1 117 ? -20.808 37.447 29.237 1.00 23.63 ? 117 ASP B OD2 1 
ATOM   2682 N  N   . LEU B 1 118 ? -19.800 33.046 32.465 1.00 11.85 ? 118 LEU B N   1 
ATOM   2683 C  CA  . LEU B 1 118 ? -19.151 32.393 33.593 1.00 12.31 ? 118 LEU B CA  1 
ATOM   2684 C  C   . LEU B 1 118 ? -18.974 30.917 33.234 1.00 11.96 ? 118 LEU B C   1 
ATOM   2685 O  O   . LEU B 1 118 ? -17.865 30.382 33.287 1.00 12.21 ? 118 LEU B O   1 
ATOM   2686 C  CB  . LEU B 1 118 ? -20.003 32.536 34.861 1.00 11.44 ? 118 LEU B CB  1 
ATOM   2687 C  CG  . LEU B 1 118 ? -19.507 31.791 36.106 1.00 11.31 ? 118 LEU B CG  1 
ATOM   2688 C  CD1 . LEU B 1 118 ? -18.133 32.306 36.513 1.00 10.57 ? 118 LEU B CD1 1 
ATOM   2689 C  CD2 . LEU B 1 118 ? -20.507 31.971 37.238 1.00 10.26 ? 118 LEU B CD2 1 
ATOM   2690 N  N   . ASN B 1 119 ? -20.075 30.274 32.849 1.00 12.27 ? 119 ASN B N   1 
ATOM   2691 C  CA  . ASN B 1 119 ? -20.076 28.859 32.469 1.00 14.75 ? 119 ASN B CA  1 
ATOM   2692 C  C   . ASN B 1 119 ? -19.004 28.512 31.436 1.00 15.49 ? 119 ASN B C   1 
ATOM   2693 O  O   . ASN B 1 119 ? -18.314 27.499 31.560 1.00 15.40 ? 119 ASN B O   1 
ATOM   2694 C  CB  . ASN B 1 119 ? -21.455 28.469 31.913 1.00 15.11 ? 119 ASN B CB  1 
ATOM   2695 C  CG  . ASN B 1 119 ? -21.499 27.040 31.397 1.00 16.20 ? 119 ASN B CG  1 
ATOM   2696 O  OD1 . ASN B 1 119 ? -20.878 26.143 31.966 1.00 17.94 ? 119 ASN B OD1 1 
ATOM   2697 N  ND2 . ASN B 1 119 ? -22.241 26.820 30.318 1.00 16.13 ? 119 ASN B ND2 1 
ATOM   2698 N  N   . GLN B 1 120 ? -18.872 29.352 30.416 1.00 16.47 ? 120 GLN B N   1 
ATOM   2699 C  CA  . GLN B 1 120 ? -17.896 29.112 29.359 1.00 18.29 ? 120 GLN B CA  1 
ATOM   2700 C  C   . GLN B 1 120 ? -16.595 29.882 29.563 1.00 17.87 ? 120 GLN B C   1 
ATOM   2701 O  O   . GLN B 1 120 ? -15.692 29.816 28.731 1.00 20.07 ? 120 GLN B O   1 
ATOM   2702 C  CB  . GLN B 1 120 ? -18.505 29.472 28.001 1.00 20.54 ? 120 GLN B CB  1 
ATOM   2703 C  CG  . GLN B 1 120 ? -19.731 28.644 27.646 1.00 23.95 ? 120 GLN B CG  1 
ATOM   2704 C  CD  . GLN B 1 120 ? -20.507 29.218 26.479 1.00 30.15 ? 120 GLN B CD  1 
ATOM   2705 O  OE1 . GLN B 1 120 ? -19.924 29.719 25.520 1.00 32.65 ? 120 GLN B OE1 1 
ATOM   2706 N  NE2 . GLN B 1 120 ? -21.830 29.147 26.555 1.00 31.10 ? 120 GLN B NE2 1 
ATOM   2707 N  N   . GLY B 1 121 ? -16.497 30.598 30.678 1.00 15.42 ? 121 GLY B N   1 
ATOM   2708 C  CA  . GLY B 1 121 ? -15.300 31.369 30.956 1.00 14.03 ? 121 GLY B CA  1 
ATOM   2709 C  C   . GLY B 1 121 ? -14.454 30.834 32.094 1.00 12.30 ? 121 GLY B C   1 
ATOM   2710 O  O   . GLY B 1 121 ? -13.940 29.719 32.030 1.00 13.16 ? 121 GLY B O   1 
ATOM   2711 N  N   . ALA B 1 122 ? -14.314 31.637 33.143 1.00 12.16 ? 122 ALA B N   1 
ATOM   2712 C  CA  . ALA B 1 122 ? -13.509 31.273 34.303 1.00 12.38 ? 122 ALA B CA  1 
ATOM   2713 C  C   . ALA B 1 122 ? -13.918 29.948 34.942 1.00 13.42 ? 122 ALA B C   1 
ATOM   2714 O  O   . ALA B 1 122 ? -13.065 29.187 35.408 1.00 13.79 ? 122 ALA B O   1 
ATOM   2715 C  CB  . ALA B 1 122 ? -13.566 32.391 35.341 1.00 11.38 ? 122 ALA B CB  1 
ATOM   2716 N  N   . TRP B 1 123 ? -15.218 29.672 34.968 1.00 12.04 ? 123 TRP B N   1 
ATOM   2717 C  CA  . TRP B 1 123 ? -15.707 28.437 35.564 1.00 11.52 ? 123 TRP B CA  1 
ATOM   2718 C  C   . TRP B 1 123 ? -15.198 27.216 34.797 1.00 11.81 ? 123 TRP B C   1 
ATOM   2719 O  O   . TRP B 1 123 ? -14.791 26.223 35.402 1.00 12.08 ? 123 TRP B O   1 
ATOM   2720 C  CB  . TRP B 1 123 ? -17.244 28.436 35.613 1.00 9.57  ? 123 TRP B CB  1 
ATOM   2721 C  CG  . TRP B 1 123 ? -17.816 27.345 36.483 1.00 10.03 ? 123 TRP B CG  1 
ATOM   2722 C  CD1 . TRP B 1 123 ? -18.350 26.160 36.065 1.00 9.67  ? 123 TRP B CD1 1 
ATOM   2723 C  CD2 . TRP B 1 123 ? -17.877 27.327 37.916 1.00 10.61 ? 123 TRP B CD2 1 
ATOM   2724 N  NE1 . TRP B 1 123 ? -18.738 25.406 37.145 1.00 10.67 ? 123 TRP B NE1 1 
ATOM   2725 C  CE2 . TRP B 1 123 ? -18.458 26.098 38.294 1.00 10.59 ? 123 TRP B CE2 1 
ATOM   2726 C  CE3 . TRP B 1 123 ? -17.494 28.232 38.917 1.00 10.54 ? 123 TRP B CE3 1 
ATOM   2727 C  CZ2 . TRP B 1 123 ? -18.668 25.747 39.635 1.00 10.45 ? 123 TRP B CZ2 1 
ATOM   2728 C  CZ3 . TRP B 1 123 ? -17.704 27.881 40.251 1.00 9.88  ? 123 TRP B CZ3 1 
ATOM   2729 C  CH2 . TRP B 1 123 ? -18.286 26.648 40.594 1.00 10.00 ? 123 TRP B CH2 1 
ATOM   2730 N  N   . ALA B 1 124 ? -15.222 27.293 33.469 1.00 11.03 ? 124 ALA B N   1 
ATOM   2731 C  CA  . ALA B 1 124 ? -14.754 26.197 32.621 1.00 10.71 ? 124 ALA B CA  1 
ATOM   2732 C  C   . ALA B 1 124 ? -13.238 26.037 32.729 1.00 11.69 ? 124 ALA B C   1 
ATOM   2733 O  O   . ALA B 1 124 ? -12.710 24.926 32.657 1.00 12.05 ? 124 ALA B O   1 
ATOM   2734 C  CB  . ALA B 1 124 ? -15.143 26.456 31.169 1.00 9.98  ? 124 ALA B CB  1 
ATOM   2735 N  N   . ARG B 1 125 ? -12.536 27.153 32.890 1.00 11.66 ? 125 ARG B N   1 
ATOM   2736 C  CA  . ARG B 1 125 ? -11.087 27.110 33.011 1.00 12.75 ? 125 ARG B CA  1 
ATOM   2737 C  C   . ARG B 1 125 ? -10.691 26.438 34.326 1.00 12.84 ? 125 ARG B C   1 
ATOM   2738 O  O   . ARG B 1 125 ? -9.719  25.684 34.379 1.00 13.44 ? 125 ARG B O   1 
ATOM   2739 C  CB  . ARG B 1 125 ? -10.512 28.524 32.934 1.00 17.67 ? 125 ARG B CB  1 
ATOM   2740 C  CG  . ARG B 1 125 ? -9.809  28.824 31.619 1.00 25.06 ? 125 ARG B CG  1 
ATOM   2741 C  CD  . ARG B 1 125 ? -10.655 29.709 30.723 1.00 30.97 ? 125 ARG B CD  1 
ATOM   2742 N  NE  . ARG B 1 125 ? -10.930 31.016 31.321 1.00 32.80 ? 125 ARG B NE  1 
ATOM   2743 C  CZ  . ARG B 1 125 ? -11.586 31.999 30.705 1.00 32.48 ? 125 ARG B CZ  1 
ATOM   2744 N  NH1 . ARG B 1 125 ? -12.037 31.826 29.469 1.00 32.61 ? 125 ARG B NH1 1 
ATOM   2745 N  NH2 . ARG B 1 125 ? -11.804 33.150 31.328 1.00 27.56 ? 125 ARG B NH2 1 
ATOM   2746 N  N   . LEU B 1 126 ? -11.449 26.704 35.386 1.00 11.23 ? 126 LEU B N   1 
ATOM   2747 C  CA  . LEU B 1 126 ? -11.166 26.088 36.679 1.00 10.55 ? 126 LEU B CA  1 
ATOM   2748 C  C   . LEU B 1 126 ? -11.444 24.592 36.567 1.00 10.85 ? 126 LEU B C   1 
ATOM   2749 O  O   . LEU B 1 126 ? -10.673 23.767 37.060 1.00 11.50 ? 126 LEU B O   1 
ATOM   2750 C  CB  . LEU B 1 126 ? -12.040 26.712 37.777 1.00 10.88 ? 126 LEU B CB  1 
ATOM   2751 C  CG  . LEU B 1 126 ? -11.983 26.106 39.186 1.00 10.78 ? 126 LEU B CG  1 
ATOM   2752 C  CD1 . LEU B 1 126 ? -10.550 25.828 39.601 1.00 9.96  ? 126 LEU B CD1 1 
ATOM   2753 C  CD2 . LEU B 1 126 ? -12.631 27.067 40.165 1.00 11.56 ? 126 LEU B CD2 1 
ATOM   2754 N  N   . GLU B 1 127 ? -12.545 24.240 35.908 1.00 10.33 ? 127 GLU B N   1 
ATOM   2755 C  CA  . GLU B 1 127 ? -12.898 22.837 35.727 1.00 10.04 ? 127 GLU B CA  1 
ATOM   2756 C  C   . GLU B 1 127 ? -11.769 22.095 35.007 1.00 10.46 ? 127 GLU B C   1 
ATOM   2757 O  O   . GLU B 1 127 ? -11.462 20.947 35.331 1.00 10.92 ? 127 GLU B O   1 
ATOM   2758 C  CB  . GLU B 1 127 ? -14.198 22.717 34.925 1.00 10.53 ? 127 GLU B CB  1 
ATOM   2759 C  CG  . GLU B 1 127 ? -15.463 22.828 35.773 1.00 10.37 ? 127 GLU B CG  1 
ATOM   2760 C  CD  . GLU B 1 127 ? -16.722 23.004 34.939 1.00 14.42 ? 127 GLU B CD  1 
ATOM   2761 O  OE1 . GLU B 1 127 ? -16.614 23.401 33.758 1.00 16.07 ? 127 GLU B OE1 1 
ATOM   2762 O  OE2 . GLU B 1 127 ? -17.823 22.749 35.467 1.00 14.93 ? 127 GLU B OE2 1 
ATOM   2763 N  N   . ASP B 1 128 ? -11.151 22.753 34.030 1.00 11.70 ? 128 ASP B N   1 
ATOM   2764 C  CA  . ASP B 1 128 ? -10.051 22.146 33.279 1.00 13.37 ? 128 ASP B CA  1 
ATOM   2765 C  C   . ASP B 1 128 ? -8.868  21.847 34.196 1.00 12.10 ? 128 ASP B C   1 
ATOM   2766 O  O   . ASP B 1 128 ? -8.358  20.729 34.219 1.00 12.47 ? 128 ASP B O   1 
ATOM   2767 C  CB  . ASP B 1 128 ? -9.577  23.077 32.156 1.00 22.87 ? 128 ASP B CB  1 
ATOM   2768 C  CG  . ASP B 1 128 ? -10.547 23.139 30.992 1.00 30.36 ? 128 ASP B CG  1 
ATOM   2769 O  OD1 . ASP B 1 128 ? -11.421 22.251 30.883 1.00 35.87 ? 128 ASP B OD1 1 
ATOM   2770 O  OD2 . ASP B 1 128 ? -10.434 24.084 30.181 1.00 36.30 ? 128 ASP B OD2 1 
ATOM   2771 N  N   . GLN B 1 129 ? -8.437  22.853 34.950 1.00 13.02 ? 129 GLN B N   1 
ATOM   2772 C  CA  . GLN B 1 129 ? -7.306  22.698 35.862 1.00 13.75 ? 129 GLN B CA  1 
ATOM   2773 C  C   . GLN B 1 129 ? -7.603  21.672 36.947 1.00 14.60 ? 129 GLN B C   1 
ATOM   2774 O  O   . GLN B 1 129 ? -6.725  20.910 37.356 1.00 14.26 ? 129 GLN B O   1 
ATOM   2775 C  CB  . GLN B 1 129 ? -6.954  24.047 36.497 1.00 15.27 ? 129 GLN B CB  1 
ATOM   2776 C  CG  . GLN B 1 129 ? -6.188  24.974 35.566 1.00 17.08 ? 129 GLN B CG  1 
ATOM   2777 C  CD  . GLN B 1 129 ? -5.178  24.229 34.708 1.00 21.23 ? 129 GLN B CD  1 
ATOM   2778 O  OE1 . GLN B 1 129 ? -4.324  23.504 35.221 1.00 21.75 ? 129 GLN B OE1 1 
ATOM   2779 N  NE2 . GLN B 1 129 ? -5.274  24.402 33.395 1.00 22.87 ? 129 GLN B NE2 1 
ATOM   2780 N  N   . GLU B 1 130 ? -8.849  21.660 37.408 1.00 14.21 ? 130 GLU B N   1 
ATOM   2781 C  CA  . GLU B 1 130 ? -9.291  20.722 38.435 1.00 13.70 ? 130 GLU B CA  1 
ATOM   2782 C  C   . GLU B 1 130 ? -9.139  19.301 37.899 1.00 14.09 ? 130 GLU B C   1 
ATOM   2783 O  O   . GLU B 1 130 ? -8.653  18.403 38.591 1.00 14.86 ? 130 GLU B O   1 
ATOM   2784 C  CB  . GLU B 1 130 ? -10.756 21.009 38.782 1.00 12.14 ? 130 GLU B CB  1 
ATOM   2785 C  CG  . GLU B 1 130 ? -11.411 20.027 39.725 1.00 11.20 ? 130 GLU B CG  1 
ATOM   2786 C  CD  . GLU B 1 130 ? -12.877 20.355 39.961 1.00 12.45 ? 130 GLU B CD  1 
ATOM   2787 O  OE1 . GLU B 1 130 ? -13.488 21.032 39.106 1.00 11.13 ? 130 GLU B OE1 1 
ATOM   2788 O  OE2 . GLU B 1 130 ? -13.420 19.936 41.002 1.00 12.19 ? 130 GLU B OE2 1 
ATOM   2789 N  N   . ARG B 1 131 ? -9.548  19.113 36.650 1.00 15.12 ? 131 ARG B N   1 
ATOM   2790 C  CA  . ARG B 1 131 ? -9.471  17.816 35.993 1.00 17.19 ? 131 ARG B CA  1 
ATOM   2791 C  C   . ARG B 1 131 ? -8.025  17.406 35.712 1.00 18.09 ? 131 ARG B C   1 
ATOM   2792 O  O   . ARG B 1 131 ? -7.666  16.236 35.850 1.00 19.68 ? 131 ARG B O   1 
ATOM   2793 C  CB  . ARG B 1 131 ? -10.255 17.861 34.680 1.00 20.20 ? 131 ARG B CB  1 
ATOM   2794 C  CG  . ARG B 1 131 ? -10.521 16.506 34.059 1.00 24.71 ? 131 ARG B CG  1 
ATOM   2795 C  CD  . ARG B 1 131 ? -11.576 16.614 32.977 1.00 28.62 ? 131 ARG B CD  1 
ATOM   2796 N  NE  . ARG B 1 131 ? -11.524 17.905 32.293 1.00 33.88 ? 131 ARG B NE  1 
ATOM   2797 C  CZ  . ARG B 1 131 ? -12.527 18.782 32.259 1.00 35.12 ? 131 ARG B CZ  1 
ATOM   2798 N  NH1 . ARG B 1 131 ? -13.676 18.518 32.871 1.00 34.25 ? 131 ARG B NH1 1 
ATOM   2799 N  NH2 . ARG B 1 131 ? -12.381 19.928 31.607 1.00 34.62 ? 131 ARG B NH2 1 
ATOM   2800 N  N   . LYS B 1 132 ? -7.197  18.372 35.323 1.00 15.54 ? 132 LYS B N   1 
ATOM   2801 C  CA  . LYS B 1 132 ? -5.802  18.088 35.011 1.00 15.54 ? 132 LYS B CA  1 
ATOM   2802 C  C   . LYS B 1 132 ? -4.986  17.655 36.224 1.00 15.25 ? 132 LYS B C   1 
ATOM   2803 O  O   . LYS B 1 132 ? -3.953  17.006 36.077 1.00 15.39 ? 132 LYS B O   1 
ATOM   2804 C  CB  . LYS B 1 132 ? -5.154  19.305 34.350 1.00 16.83 ? 132 LYS B CB  1 
ATOM   2805 C  CG  . LYS B 1 132 ? -5.525  19.456 32.884 1.00 24.80 ? 132 LYS B CG  1 
ATOM   2806 C  CD  . LYS B 1 132 ? -4.969  20.738 32.284 1.00 31.74 ? 132 LYS B CD  1 
ATOM   2807 C  CE  . LYS B 1 132 ? -5.627  21.048 30.941 1.00 33.37 ? 132 LYS B CE  1 
ATOM   2808 N  NZ  . LYS B 1 132 ? -5.097  22.299 30.323 1.00 34.41 ? 132 LYS B NZ  1 
ATOM   2809 N  N   . LEU B 1 133 ? -5.446  18.007 37.421 1.00 14.54 ? 133 LEU B N   1 
ATOM   2810 C  CA  . LEU B 1 133 ? -4.738  17.630 38.644 1.00 14.05 ? 133 LEU B CA  1 
ATOM   2811 C  C   . LEU B 1 133 ? -4.615  16.116 38.730 1.00 14.26 ? 133 LEU B C   1 
ATOM   2812 O  O   . LEU B 1 133 ? -3.606  15.589 39.193 1.00 13.75 ? 133 LEU B O   1 
ATOM   2813 C  CB  . LEU B 1 133 ? -5.490  18.131 39.882 1.00 12.51 ? 133 LEU B CB  1 
ATOM   2814 C  CG  . LEU B 1 133 ? -5.336  19.594 40.289 1.00 12.69 ? 133 LEU B CG  1 
ATOM   2815 C  CD1 . LEU B 1 133 ? -6.290  19.892 41.435 1.00 12.56 ? 133 LEU B CD1 1 
ATOM   2816 C  CD2 . LEU B 1 133 ? -3.900  19.872 40.704 1.00 12.33 ? 133 LEU B CD2 1 
ATOM   2817 N  N   . ILE B 1 134 ? -5.655  15.423 38.278 1.00 15.76 ? 134 ILE B N   1 
ATOM   2818 C  CA  . ILE B 1 134 ? -5.693  13.966 38.320 1.00 17.40 ? 134 ILE B CA  1 
ATOM   2819 C  C   . ILE B 1 134 ? -4.676  13.304 37.390 1.00 19.19 ? 134 ILE B C   1 
ATOM   2820 O  O   . ILE B 1 134 ? -4.434  12.098 37.481 1.00 18.98 ? 134 ILE B O   1 
ATOM   2821 C  CB  . ILE B 1 134 ? -7.121  13.444 37.991 1.00 16.70 ? 134 ILE B CB  1 
ATOM   2822 C  CG1 . ILE B 1 134 ? -7.353  12.103 38.686 1.00 16.86 ? 134 ILE B CG1 1 
ATOM   2823 C  CG2 . ILE B 1 134 ? -7.309  13.312 36.486 1.00 17.16 ? 134 ILE B CG2 1 
ATOM   2824 C  CD1 . ILE B 1 134 ? -7.398  12.199 40.190 1.00 16.88 ? 134 ILE B CD1 1 
ATOM   2825 N  N   . ASP B 1 135 ? -4.081  14.097 36.502 1.00 20.84 ? 135 ASP B N   1 
ATOM   2826 C  CA  . ASP B 1 135 ? -3.088  13.585 35.565 1.00 22.51 ? 135 ASP B CA  1 
ATOM   2827 C  C   . ASP B 1 135 ? -1.710  13.508 36.215 1.00 22.91 ? 135 ASP B C   1 
ATOM   2828 O  O   . ASP B 1 135 ? -0.784  12.935 35.649 1.00 23.71 ? 135 ASP B O   1 
ATOM   2829 C  CB  . ASP B 1 135 ? -3.020  14.474 34.322 1.00 24.78 ? 135 ASP B CB  1 
ATOM   2830 C  CG  . ASP B 1 135 ? -4.191  14.251 33.382 1.00 26.83 ? 135 ASP B CG  1 
ATOM   2831 O  OD1 . ASP B 1 135 ? -4.904  13.241 33.547 1.00 30.36 ? 135 ASP B OD1 1 
ATOM   2832 O  OD2 . ASP B 1 135 ? -4.398  15.086 32.479 1.00 31.18 ? 135 ASP B OD2 1 
ATOM   2833 N  N   . ARG B 1 136 ? -1.573  14.094 37.400 1.00 22.01 ? 136 ARG B N   1 
ATOM   2834 C  CA  . ARG B 1 136 ? -0.302  14.061 38.116 1.00 20.91 ? 136 ARG B CA  1 
ATOM   2835 C  C   . ARG B 1 136 ? -0.129  12.664 38.695 1.00 21.18 ? 136 ARG B C   1 
ATOM   2836 O  O   . ARG B 1 136 ? -1.092  12.052 39.157 1.00 20.40 ? 136 ARG B O   1 
ATOM   2837 C  CB  . ARG B 1 136 ? -0.293  15.093 39.241 1.00 22.00 ? 136 ARG B CB  1 
ATOM   2838 C  CG  . ARG B 1 136 ? -0.294  16.523 38.758 1.00 23.19 ? 136 ARG B CG  1 
ATOM   2839 C  CD  . ARG B 1 136 ? 0.171   17.463 39.846 1.00 25.36 ? 136 ARG B CD  1 
ATOM   2840 N  NE  . ARG B 1 136 ? 0.086   18.856 39.419 1.00 32.38 ? 136 ARG B NE  1 
ATOM   2841 C  CZ  . ARG B 1 136 ? 1.132   19.589 39.047 1.00 33.27 ? 136 ARG B CZ  1 
ATOM   2842 N  NH1 . ARG B 1 136 ? 2.352   19.063 39.047 1.00 32.85 ? 136 ARG B NH1 1 
ATOM   2843 N  NH2 . ARG B 1 136 ? 0.956   20.849 38.672 1.00 33.38 ? 136 ARG B NH2 1 
ATOM   2844 N  N   . ALA B 1 137 ? 1.100   12.164 38.676 1.00 21.48 ? 137 ALA B N   1 
ATOM   2845 C  CA  . ALA B 1 137 ? 1.385   10.825 39.175 1.00 22.23 ? 137 ALA B CA  1 
ATOM   2846 C  C   . ALA B 1 137 ? 1.102   10.658 40.664 1.00 21.87 ? 137 ALA B C   1 
ATOM   2847 O  O   . ALA B 1 137 ? 0.595   9.619  41.091 1.00 22.90 ? 137 ALA B O   1 
ATOM   2848 C  CB  . ALA B 1 137 ? 2.841   10.459 38.876 1.00 24.13 ? 137 ALA B CB  1 
ATOM   2849 N  N   . ASP B 1 138 ? 1.421   11.684 41.447 1.00 19.72 ? 138 ASP B N   1 
ATOM   2850 C  CA  . ASP B 1 138 ? 1.222   11.629 42.889 1.00 18.91 ? 138 ASP B CA  1 
ATOM   2851 C  C   . ASP B 1 138 ? -0.169  12.034 43.374 1.00 16.69 ? 138 ASP B C   1 
ATOM   2852 O  O   . ASP B 1 138 ? -0.427  12.044 44.574 1.00 15.26 ? 138 ASP B O   1 
ATOM   2853 C  CB  . ASP B 1 138 ? 2.278   12.489 43.588 1.00 22.11 ? 138 ASP B CB  1 
ATOM   2854 C  CG  . ASP B 1 138 ? 2.483   13.823 42.911 1.00 23.85 ? 138 ASP B CG  1 
ATOM   2855 O  OD1 . ASP B 1 138 ? 1.739   14.127 41.956 1.00 25.45 ? 138 ASP B OD1 1 
ATOM   2856 O  OD2 . ASP B 1 138 ? 3.389   14.567 43.335 1.00 26.06 ? 138 ASP B OD2 1 
ATOM   2857 N  N   . ILE B 1 139 ? -1.065  12.374 42.455 1.00 15.73 ? 139 ILE B N   1 
ATOM   2858 C  CA  . ILE B 1 139 ? -2.417  12.755 42.847 1.00 14.48 ? 139 ILE B CA  1 
ATOM   2859 C  C   . ILE B 1 139 ? -3.380  11.668 42.395 1.00 14.25 ? 139 ILE B C   1 
ATOM   2860 O  O   . ILE B 1 139 ? -3.559  11.443 41.200 1.00 15.15 ? 139 ILE B O   1 
ATOM   2861 C  CB  . ILE B 1 139 ? -2.822  14.109 42.231 1.00 14.14 ? 139 ILE B CB  1 
ATOM   2862 C  CG1 . ILE B 1 139 ? -1.934  15.216 42.801 1.00 10.71 ? 139 ILE B CG1 1 
ATOM   2863 C  CG2 . ILE B 1 139 ? -4.293  14.408 42.537 1.00 12.76 ? 139 ILE B CG2 1 
ATOM   2864 C  CD1 . ILE B 1 139 ? -2.272  16.596 42.280 1.00 15.22 ? 139 ILE B CD1 1 
ATOM   2865 N  N   . SER B 1 140 ? -3.994  10.992 43.361 1.00 12.73 ? 140 SER B N   1 
ATOM   2866 C  CA  . SER B 1 140 ? -4.913  9.903  43.067 1.00 13.22 ? 140 SER B CA  1 
ATOM   2867 C  C   . SER B 1 140 ? -6.382  10.274 43.227 1.00 13.13 ? 140 SER B C   1 
ATOM   2868 O  O   . SER B 1 140 ? -7.262  9.575  42.722 1.00 13.32 ? 140 SER B O   1 
ATOM   2869 C  CB  . SER B 1 140 ? -4.593  8.710  43.966 1.00 16.10 ? 140 SER B CB  1 
ATOM   2870 O  OG  . SER B 1 140 ? -4.780  9.052  45.327 1.00 22.15 ? 140 SER B OG  1 
ATOM   2871 N  N   . SER B 1 141 ? -6.648  11.369 43.930 1.00 11.19 ? 141 SER B N   1 
ATOM   2872 C  CA  . SER B 1 141 ? -8.021  11.803 44.141 1.00 10.78 ? 141 SER B CA  1 
ATOM   2873 C  C   . SER B 1 141 ? -8.156  13.310 44.239 1.00 10.65 ? 141 SER B C   1 
ATOM   2874 O  O   . SER B 1 141 ? -7.254  14.006 44.701 1.00 9.99  ? 141 SER B O   1 
ATOM   2875 C  CB  . SER B 1 141 ? -8.586  11.200 45.433 1.00 9.15  ? 141 SER B CB  1 
ATOM   2876 O  OG  . SER B 1 141 ? -9.023  9.869  45.249 1.00 12.21 ? 141 SER B OG  1 
ATOM   2877 N  N   . VAL B 1 142 ? -9.302  13.798 43.786 1.00 10.64 ? 142 VAL B N   1 
ATOM   2878 C  CA  . VAL B 1 142 ? -9.639  15.204 43.871 1.00 9.43  ? 142 VAL B CA  1 
ATOM   2879 C  C   . VAL B 1 142 ? -11.044 15.175 44.459 1.00 9.23  ? 142 VAL B C   1 
ATOM   2880 O  O   . VAL B 1 142 ? -11.955 14.569 43.884 1.00 9.52  ? 142 VAL B O   1 
ATOM   2881 C  CB  . VAL B 1 142 ? -9.672  15.892 42.491 1.00 9.72  ? 142 VAL B CB  1 
ATOM   2882 C  CG1 . VAL B 1 142 ? -10.176 17.319 42.644 1.00 8.81  ? 142 VAL B CG1 1 
ATOM   2883 C  CG2 . VAL B 1 142 ? -8.276  15.896 41.875 1.00 10.02 ? 142 VAL B CG2 1 
ATOM   2884 N  N   . TYR B 1 143 ? -11.207 15.778 45.630 1.00 8.42  ? 143 TYR B N   1 
ATOM   2885 C  CA  . TYR B 1 143 ? -12.510 15.820 46.276 1.00 7.31  ? 143 TYR B CA  1 
ATOM   2886 C  C   . TYR B 1 143 ? -12.981 17.248 46.202 1.00 7.62  ? 143 TYR B C   1 
ATOM   2887 O  O   . TYR B 1 143 ? -12.306 18.161 46.676 1.00 8.31  ? 143 TYR B O   1 
ATOM   2888 C  CB  . TYR B 1 143 ? -12.414 15.387 47.734 1.00 8.16  ? 143 TYR B CB  1 
ATOM   2889 C  CG  . TYR B 1 143 ? -12.270 13.897 47.909 1.00 7.92  ? 143 TYR B CG  1 
ATOM   2890 C  CD1 . TYR B 1 143 ? -13.392 13.073 47.989 1.00 8.33  ? 143 TYR B CD1 1 
ATOM   2891 C  CD2 . TYR B 1 143 ? -11.011 13.311 48.008 1.00 8.43  ? 143 TYR B CD2 1 
ATOM   2892 C  CE1 . TYR B 1 143 ? -13.261 11.699 48.166 1.00 10.29 ? 143 TYR B CE1 1 
ATOM   2893 C  CE2 . TYR B 1 143 ? -10.868 11.943 48.183 1.00 9.93  ? 143 TYR B CE2 1 
ATOM   2894 C  CZ  . TYR B 1 143 ? -11.995 11.142 48.263 1.00 10.76 ? 143 TYR B CZ  1 
ATOM   2895 O  OH  . TYR B 1 143 ? -11.848 9.789  48.451 1.00 13.35 ? 143 TYR B OH  1 
ATOM   2896 N  N   . THR B 1 144 ? -14.148 17.442 45.606 1.00 6.26  ? 144 THR B N   1 
ATOM   2897 C  CA  . THR B 1 144 ? -14.681 18.776 45.460 1.00 6.20  ? 144 THR B CA  1 
ATOM   2898 C  C   . THR B 1 144 ? -16.108 18.908 45.969 1.00 6.69  ? 144 THR B C   1 
ATOM   2899 O  O   . THR B 1 144 ? -16.895 17.964 45.914 1.00 6.15  ? 144 THR B O   1 
ATOM   2900 C  CB  . THR B 1 144 ? -14.636 19.203 43.973 1.00 6.98  ? 144 THR B CB  1 
ATOM   2901 O  OG1 . THR B 1 144 ? -13.275 19.212 43.522 1.00 8.75  ? 144 THR B OG1 1 
ATOM   2902 C  CG2 . THR B 1 144 ? -15.247 20.585 43.784 1.00 5.07  ? 144 THR B CG2 1 
ATOM   2903 N  N   . VAL B 1 145 ? -16.413 20.084 46.503 1.00 8.14  ? 145 VAL B N   1 
ATOM   2904 C  CA  . VAL B 1 145 ? -17.756 20.402 46.961 1.00 7.93  ? 145 VAL B CA  1 
ATOM   2905 C  C   . VAL B 1 145 ? -18.013 21.740 46.287 1.00 6.68  ? 145 VAL B C   1 
ATOM   2906 O  O   . VAL B 1 145 ? -17.179 22.643 46.350 1.00 6.32  ? 145 VAL B O   1 
ATOM   2907 C  CB  . VAL B 1 145 ? -17.864 20.592 48.496 1.00 10.74 ? 145 VAL B CB  1 
ATOM   2908 C  CG1 . VAL B 1 145 ? -19.325 20.795 48.880 1.00 10.48 ? 145 VAL B CG1 1 
ATOM   2909 C  CG2 . VAL B 1 145 ? -17.309 19.382 49.227 1.00 11.37 ? 145 VAL B CG2 1 
ATOM   2910 N  N   . THR B 1 146 ? -19.155 21.856 45.622 1.00 6.27  ? 146 THR B N   1 
ATOM   2911 C  CA  . THR B 1 146 ? -19.505 23.086 44.928 1.00 5.60  ? 146 THR B CA  1 
ATOM   2912 C  C   . THR B 1 146 ? -20.981 23.402 45.166 1.00 5.76  ? 146 THR B C   1 
ATOM   2913 O  O   . THR B 1 146 ? -21.768 22.520 45.503 1.00 6.09  ? 146 THR B O   1 
ATOM   2914 C  CB  . THR B 1 146 ? -19.205 22.953 43.406 1.00 6.06  ? 146 THR B CB  1 
ATOM   2915 O  OG1 . THR B 1 146 ? -19.383 24.220 42.760 1.00 7.15  ? 146 THR B OG1 1 
ATOM   2916 C  CG2 . THR B 1 146 ? -20.114 21.910 42.764 1.00 5.30  ? 146 THR B CG2 1 
ATOM   2917 N  N   . GLY B 1 147 ? -21.347 24.669 45.015 1.00 6.58  ? 147 GLY B N   1 
ATOM   2918 C  CA  . GLY B 1 147 ? -22.727 25.054 45.223 1.00 6.64  ? 147 GLY B CA  1 
ATOM   2919 C  C   . GLY B 1 147 ? -22.968 26.509 44.874 1.00 7.86  ? 147 GLY B C   1 
ATOM   2920 O  O   . GLY B 1 147 ? -22.031 27.238 44.553 1.00 7.33  ? 147 GLY B O   1 
ATOM   2921 N  N   . PRO B 1 148 ? -24.229 26.961 44.923 1.00 9.62  ? 148 PRO B N   1 
ATOM   2922 C  CA  . PRO B 1 148 ? -24.575 28.346 44.606 1.00 9.72  ? 148 PRO B CA  1 
ATOM   2923 C  C   . PRO B 1 148 ? -24.715 29.225 45.839 1.00 11.06 ? 148 PRO B C   1 
ATOM   2924 O  O   . PRO B 1 148 ? -24.722 28.741 46.970 1.00 11.18 ? 148 PRO B O   1 
ATOM   2925 C  CB  . PRO B 1 148 ? -25.906 28.204 43.886 1.00 10.59 ? 148 PRO B CB  1 
ATOM   2926 C  CG  . PRO B 1 148 ? -26.554 26.991 44.577 1.00 12.03 ? 148 PRO B CG  1 
ATOM   2927 C  CD  . PRO B 1 148 ? -25.436 26.179 45.240 1.00 9.86  ? 148 PRO B CD  1 
ATOM   2928 N  N   . LEU B 1 149 ? -24.831 30.525 45.590 1.00 11.92 ? 149 LEU B N   1 
ATOM   2929 C  CA  . LEU B 1 149 ? -25.022 31.531 46.623 1.00 12.59 ? 149 LEU B CA  1 
ATOM   2930 C  C   . LEU B 1 149 ? -26.263 32.283 46.175 1.00 11.74 ? 149 LEU B C   1 
ATOM   2931 O  O   . LEU B 1 149 ? -26.517 32.396 44.981 1.00 10.36 ? 149 LEU B O   1 
ATOM   2932 C  CB  . LEU B 1 149 ? -23.834 32.493 46.675 1.00 16.08 ? 149 LEU B CB  1 
ATOM   2933 C  CG  . LEU B 1 149 ? -22.693 32.118 47.621 1.00 18.21 ? 149 LEU B CG  1 
ATOM   2934 C  CD1 . LEU B 1 149 ? -21.588 33.149 47.515 1.00 20.51 ? 149 LEU B CD1 1 
ATOM   2935 C  CD2 . LEU B 1 149 ? -23.210 32.049 49.039 1.00 22.45 ? 149 LEU B CD2 1 
ATOM   2936 N  N   . TYR B 1 150 ? -27.043 32.780 47.125 1.00 13.89 ? 150 TYR B N   1 
ATOM   2937 C  CA  . TYR B 1 150 ? -28.257 33.528 46.807 1.00 15.10 ? 150 TYR B CA  1 
ATOM   2938 C  C   . TYR B 1 150 ? -28.207 34.835 47.578 1.00 16.62 ? 150 TYR B C   1 
ATOM   2939 O  O   . TYR B 1 150 ? -28.767 34.941 48.666 1.00 19.37 ? 150 TYR B O   1 
ATOM   2940 C  CB  . TYR B 1 150 ? -29.493 32.730 47.224 1.00 12.35 ? 150 TYR B CB  1 
ATOM   2941 C  CG  . TYR B 1 150 ? -29.577 31.373 46.575 1.00 10.76 ? 150 TYR B CG  1 
ATOM   2942 C  CD1 . TYR B 1 150 ? -30.022 31.236 45.261 1.00 11.34 ? 150 TYR B CD1 1 
ATOM   2943 C  CD2 . TYR B 1 150 ? -29.194 30.224 47.265 1.00 10.10 ? 150 TYR B CD2 1 
ATOM   2944 C  CE1 . TYR B 1 150 ? -30.082 29.988 44.648 1.00 9.73  ? 150 TYR B CE1 1 
ATOM   2945 C  CE2 . TYR B 1 150 ? -29.251 28.973 46.662 1.00 9.33  ? 150 TYR B CE2 1 
ATOM   2946 C  CZ  . TYR B 1 150 ? -29.695 28.866 45.353 1.00 9.79  ? 150 TYR B CZ  1 
ATOM   2947 O  OH  . TYR B 1 150 ? -29.743 27.635 44.749 1.00 11.47 ? 150 TYR B OH  1 
ATOM   2948 N  N   . GLU B 1 151 ? -27.547 35.837 47.010 1.00 15.25 ? 151 GLU B N   1 
ATOM   2949 C  CA  . GLU B 1 151 ? -27.410 37.107 47.700 1.00 15.85 ? 151 GLU B CA  1 
ATOM   2950 C  C   . GLU B 1 151 ? -28.084 38.306 47.042 1.00 16.88 ? 151 GLU B C   1 
ATOM   2951 O  O   . GLU B 1 151 ? -28.179 39.371 47.642 1.00 18.41 ? 151 GLU B O   1 
ATOM   2952 C  CB  . GLU B 1 151 ? -25.923 37.381 47.929 1.00 14.54 ? 151 GLU B CB  1 
ATOM   2953 C  CG  . GLU B 1 151 ? -25.241 36.238 48.677 1.00 17.98 ? 151 GLU B CG  1 
ATOM   2954 C  CD  . GLU B 1 151 ? -23.757 36.453 48.862 1.00 19.42 ? 151 GLU B CD  1 
ATOM   2955 O  OE1 . GLU B 1 151 ? -23.091 36.868 47.892 1.00 21.02 ? 151 GLU B OE1 1 
ATOM   2956 O  OE2 . GLU B 1 151 ? -23.258 36.204 49.979 1.00 17.90 ? 151 GLU B OE2 1 
ATOM   2957 N  N   . ARG B 1 152 ? -28.563 38.139 45.818 1.00 20.17 ? 152 ARG B N   1 
ATOM   2958 C  CA  . ARG B 1 152 ? -29.229 39.238 45.135 1.00 20.82 ? 152 ARG B CA  1 
ATOM   2959 C  C   . ARG B 1 152 ? -30.179 38.720 44.062 1.00 21.67 ? 152 ARG B C   1 
ATOM   2960 O  O   . ARG B 1 152 ? -29.920 37.687 43.443 1.00 22.12 ? 152 ARG B O   1 
ATOM   2961 C  CB  . ARG B 1 152 ? -28.190 40.182 44.521 1.00 21.02 ? 152 ARG B CB  1 
ATOM   2962 C  CG  . ARG B 1 152 ? -27.884 39.917 43.067 1.00 20.05 ? 152 ARG B CG  1 
ATOM   2963 C  CD  . ARG B 1 152 ? -26.773 40.816 42.565 1.00 20.95 ? 152 ARG B CD  1 
ATOM   2964 N  NE  . ARG B 1 152 ? -26.190 40.273 41.341 1.00 26.45 ? 152 ARG B NE  1 
ATOM   2965 C  CZ  . ARG B 1 152 ? -24.963 39.770 41.259 1.00 24.56 ? 152 ARG B CZ  1 
ATOM   2966 N  NH1 . ARG B 1 152 ? -24.186 39.743 42.332 1.00 23.63 ? 152 ARG B NH1 1 
ATOM   2967 N  NH2 . ARG B 1 152 ? -24.520 39.276 40.109 1.00 25.81 ? 152 ARG B NH2 1 
ATOM   2968 N  N   . ASP B 1 153 ? -31.280 39.438 43.858 1.00 19.52 ? 153 ASP B N   1 
ATOM   2969 C  CA  . ASP B 1 153 ? -32.282 39.062 42.867 1.00 19.52 ? 153 ASP B CA  1 
ATOM   2970 C  C   . ASP B 1 153 ? -31.662 39.007 41.476 1.00 19.30 ? 153 ASP B C   1 
ATOM   2971 O  O   . ASP B 1 153 ? -31.063 39.977 41.017 1.00 19.95 ? 153 ASP B O   1 
ATOM   2972 C  CB  . ASP B 1 153 ? -33.436 40.068 42.886 1.00 26.27 ? 153 ASP B CB  1 
ATOM   2973 C  CG  . ASP B 1 153 ? -34.425 39.849 41.751 1.00 33.12 ? 153 ASP B CG  1 
ATOM   2974 O  OD1 . ASP B 1 153 ? -34.758 38.680 41.455 1.00 34.20 ? 153 ASP B OD1 1 
ATOM   2975 O  OD2 . ASP B 1 153 ? -34.871 40.852 41.152 1.00 35.71 ? 153 ASP B OD2 1 
ATOM   2976 N  N   . MET B 1 154 ? -31.810 37.867 40.807 1.00 19.74 ? 154 MET B N   1 
ATOM   2977 C  CA  . MET B 1 154 ? -31.255 37.685 39.470 1.00 19.88 ? 154 MET B CA  1 
ATOM   2978 C  C   . MET B 1 154 ? -32.344 37.516 38.414 1.00 20.47 ? 154 MET B C   1 
ATOM   2979 O  O   . MET B 1 154 ? -32.054 37.205 37.262 1.00 22.28 ? 154 MET B O   1 
ATOM   2980 C  CB  . MET B 1 154 ? -30.336 36.459 39.448 1.00 19.43 ? 154 MET B CB  1 
ATOM   2981 C  CG  . MET B 1 154 ? -29.059 36.624 40.250 1.00 20.35 ? 154 MET B CG  1 
ATOM   2982 S  SD  . MET B 1 154 ? -27.915 37.771 39.474 1.00 22.19 ? 154 MET B SD  1 
ATOM   2983 C  CE  . MET B 1 154 ? -27.364 36.789 38.077 1.00 21.87 ? 154 MET B CE  1 
ATOM   2984 N  N   . GLY B 1 155 ? -33.594 37.727 38.807 1.00 19.32 ? 155 GLY B N   1 
ATOM   2985 C  CA  . GLY B 1 155 ? -34.690 37.570 37.868 1.00 18.73 ? 155 GLY B CA  1 
ATOM   2986 C  C   . GLY B 1 155 ? -35.275 36.173 37.956 1.00 18.57 ? 155 GLY B C   1 
ATOM   2987 O  O   . GLY B 1 155 ? -34.981 35.435 38.899 1.00 18.16 ? 155 GLY B O   1 
ATOM   2988 N  N   . LYS B 1 156 ? -36.100 35.804 36.979 1.00 17.56 ? 156 LYS B N   1 
ATOM   2989 C  CA  . LYS B 1 156 ? -36.722 34.482 36.961 1.00 17.15 ? 156 LYS B CA  1 
ATOM   2990 C  C   . LYS B 1 156 ? -36.695 33.871 35.565 1.00 16.36 ? 156 LYS B C   1 
ATOM   2991 O  O   . LYS B 1 156 ? -36.654 34.588 34.566 1.00 16.59 ? 156 LYS B O   1 
ATOM   2992 C  CB  . LYS B 1 156 ? -38.177 34.572 37.430 1.00 23.09 ? 156 LYS B CB  1 
ATOM   2993 C  CG  . LYS B 1 156 ? -38.382 35.336 38.727 1.00 30.19 ? 156 LYS B CG  1 
ATOM   2994 C  CD  . LYS B 1 156 ? -38.182 34.437 39.946 1.00 34.69 ? 156 LYS B CD  1 
ATOM   2995 C  CE  . LYS B 1 156 ? -37.284 35.093 40.997 1.00 36.57 ? 156 LYS B CE  1 
ATOM   2996 N  NZ  . LYS B 1 156 ? -37.076 36.563 40.768 1.00 37.75 ? 156 LYS B NZ  1 
ATOM   2997 N  N   . LEU B 1 157 ? -36.713 32.544 35.499 1.00 14.96 ? 157 LEU B N   1 
ATOM   2998 C  CA  . LEU B 1 157 ? -36.732 31.856 34.213 1.00 14.48 ? 157 LEU B CA  1 
ATOM   2999 C  C   . LEU B 1 157 ? -38.073 32.214 33.565 1.00 14.89 ? 157 LEU B C   1 
ATOM   3000 O  O   . LEU B 1 157 ? -39.123 32.096 34.199 1.00 15.21 ? 157 LEU B O   1 
ATOM   3001 C  CB  . LEU B 1 157 ? -36.630 30.340 34.420 1.00 14.36 ? 157 LEU B CB  1 
ATOM   3002 C  CG  . LEU B 1 157 ? -35.298 29.840 34.986 1.00 15.74 ? 157 LEU B CG  1 
ATOM   3003 C  CD1 . LEU B 1 157 ? -35.415 28.373 35.374 1.00 14.69 ? 157 LEU B CD1 1 
ATOM   3004 C  CD2 . LEU B 1 157 ? -34.201 30.033 33.953 1.00 14.40 ? 157 LEU B CD2 1 
ATOM   3005 N  N   . PRO B 1 158 ? -38.056 32.650 32.295 1.00 15.44 ? 158 PRO B N   1 
ATOM   3006 C  CA  . PRO B 1 158 ? -39.296 33.024 31.601 1.00 16.70 ? 158 PRO B CA  1 
ATOM   3007 C  C   . PRO B 1 158 ? -40.227 31.877 31.223 1.00 17.36 ? 158 PRO B C   1 
ATOM   3008 O  O   . PRO B 1 158 ? -41.413 32.095 30.993 1.00 18.51 ? 158 PRO B O   1 
ATOM   3009 C  CB  . PRO B 1 158 ? -38.800 33.758 30.361 1.00 15.38 ? 158 PRO B CB  1 
ATOM   3010 C  CG  . PRO B 1 158 ? -37.481 33.122 30.075 1.00 14.98 ? 158 PRO B CG  1 
ATOM   3011 C  CD  . PRO B 1 158 ? -36.876 32.807 31.425 1.00 15.13 ? 158 PRO B CD  1 
ATOM   3012 N  N   . GLY B 1 159 ? -39.695 30.661 31.164 1.00 17.90 ? 159 GLY B N   1 
ATOM   3013 C  CA  . GLY B 1 159 ? -40.511 29.528 30.766 1.00 17.62 ? 159 GLY B CA  1 
ATOM   3014 C  C   . GLY B 1 159 ? -41.097 28.627 31.834 1.00 17.73 ? 159 GLY B C   1 
ATOM   3015 O  O   . GLY B 1 159 ? -41.449 27.488 31.533 1.00 18.63 ? 159 GLY B O   1 
ATOM   3016 N  N   . THR B 1 160 ? -41.213 29.111 33.069 1.00 18.51 ? 160 THR B N   1 
ATOM   3017 C  CA  . THR B 1 160 ? -41.780 28.290 34.141 1.00 18.22 ? 160 THR B CA  1 
ATOM   3018 C  C   . THR B 1 160 ? -42.635 29.076 35.128 1.00 20.39 ? 160 THR B C   1 
ATOM   3019 O  O   . THR B 1 160 ? -42.423 30.271 35.341 1.00 20.63 ? 160 THR B O   1 
ATOM   3020 C  CB  . THR B 1 160 ? -40.686 27.569 34.947 1.00 16.72 ? 160 THR B CB  1 
ATOM   3021 O  OG1 . THR B 1 160 ? -41.300 26.659 35.871 1.00 16.05 ? 160 THR B OG1 1 
ATOM   3022 C  CG2 . THR B 1 160 ? -39.845 28.572 35.722 1.00 14.08 ? 160 THR B CG2 1 
ATOM   3023 N  N   . GLN B 1 161 ? -43.600 28.383 35.728 1.00 21.75 ? 161 GLN B N   1 
ATOM   3024 C  CA  . GLN B 1 161 ? -44.503 28.975 36.708 1.00 22.39 ? 161 GLN B CA  1 
ATOM   3025 C  C   . GLN B 1 161 ? -44.064 28.532 38.100 1.00 21.90 ? 161 GLN B C   1 
ATOM   3026 O  O   . GLN B 1 161 ? -44.640 28.943 39.108 1.00 23.51 ? 161 GLN B O   1 
ATOM   3027 C  CB  . GLN B 1 161 ? -45.939 28.509 36.451 1.00 28.92 ? 161 GLN B CB  1 
ATOM   3028 C  CG  . GLN B 1 161 ? -46.896 29.615 36.034 1.00 32.65 ? 161 GLN B CG  1 
ATOM   3029 C  CD  . GLN B 1 161 ? -46.256 30.628 35.099 1.00 37.99 ? 161 GLN B CD  1 
ATOM   3030 O  OE1 . GLN B 1 161 ? -45.907 30.308 33.960 1.00 39.10 ? 161 GLN B OE1 1 
ATOM   3031 N  NE2 . GLN B 1 161 ? -46.097 31.859 35.578 1.00 38.53 ? 161 GLN B NE2 1 
ATOM   3032 N  N   . LYS B 1 162 ? -43.039 27.685 38.138 1.00 17.94 ? 162 LYS B N   1 
ATOM   3033 C  CA  . LYS B 1 162 ? -42.494 27.164 39.388 1.00 15.74 ? 162 LYS B CA  1 
ATOM   3034 C  C   . LYS B 1 162 ? -41.744 28.240 40.164 1.00 15.51 ? 162 LYS B C   1 
ATOM   3035 O  O   . LYS B 1 162 ? -41.007 29.038 39.582 1.00 15.55 ? 162 LYS B O   1 
ATOM   3036 C  CB  . LYS B 1 162 ? -41.519 26.024 39.098 1.00 16.38 ? 162 LYS B CB  1 
ATOM   3037 C  CG  . LYS B 1 162 ? -42.134 24.648 39.021 1.00 18.31 ? 162 LYS B CG  1 
ATOM   3038 C  CD  . LYS B 1 162 ? -41.042 23.599 38.933 1.00 20.23 ? 162 LYS B CD  1 
ATOM   3039 C  CE  . LYS B 1 162 ? -41.575 22.278 38.411 1.00 21.88 ? 162 LYS B CE  1 
ATOM   3040 N  NZ  . LYS B 1 162 ? -41.150 22.030 37.002 1.00 23.62 ? 162 LYS B NZ  1 
ATOM   3041 N  N   . ALA B 1 163 ? -41.929 28.260 41.479 1.00 15.70 ? 163 ALA B N   1 
ATOM   3042 C  CA  . ALA B 1 163 ? -41.219 29.218 42.316 1.00 15.77 ? 163 ALA B CA  1 
ATOM   3043 C  C   . ALA B 1 163 ? -39.777 28.717 42.380 1.00 15.35 ? 163 ALA B C   1 
ATOM   3044 O  O   . ALA B 1 163 ? -39.533 27.551 42.697 1.00 16.01 ? 163 ALA B O   1 
ATOM   3045 C  CB  . ALA B 1 163 ? -41.824 29.255 43.711 1.00 15.58 ? 163 ALA B CB  1 
ATOM   3046 N  N   . HIS B 1 164 ? -38.829 29.596 42.066 1.00 15.11 ? 164 HIS B N   1 
ATOM   3047 C  CA  . HIS B 1 164 ? -37.412 29.241 42.072 1.00 13.74 ? 164 HIS B CA  1 
ATOM   3048 C  C   . HIS B 1 164 ? -36.569 30.478 42.341 1.00 13.78 ? 164 HIS B C   1 
ATOM   3049 O  O   . HIS B 1 164 ? -37.055 31.602 42.247 1.00 13.52 ? 164 HIS B O   1 
ATOM   3050 C  CB  . HIS B 1 164 ? -37.015 28.651 40.717 1.00 13.09 ? 164 HIS B CB  1 
ATOM   3051 C  CG  . HIS B 1 164 ? -37.177 29.608 39.575 1.00 13.95 ? 164 HIS B CG  1 
ATOM   3052 N  ND1 . HIS B 1 164 ? -38.404 29.906 39.021 1.00 14.52 ? 164 HIS B ND1 1 
ATOM   3053 C  CD2 . HIS B 1 164 ? -36.270 30.356 38.903 1.00 14.37 ? 164 HIS B CD2 1 
ATOM   3054 C  CE1 . HIS B 1 164 ? -38.246 30.798 38.059 1.00 14.67 ? 164 HIS B CE1 1 
ATOM   3055 N  NE2 . HIS B 1 164 ? -36.960 31.088 37.966 1.00 14.84 ? 164 HIS B NE2 1 
ATOM   3056 N  N   . THR B 1 165 ? -35.302 30.267 42.670 1.00 12.80 ? 165 THR B N   1 
ATOM   3057 C  CA  . THR B 1 165 ? -34.395 31.375 42.934 1.00 12.81 ? 165 THR B CA  1 
ATOM   3058 C  C   . THR B 1 165 ? -33.095 31.152 42.182 1.00 11.80 ? 165 THR B C   1 
ATOM   3059 O  O   . THR B 1 165 ? -32.355 30.219 42.479 1.00 11.67 ? 165 THR B O   1 
ATOM   3060 C  CB  . THR B 1 165 ? -34.071 31.501 44.436 1.00 14.59 ? 165 THR B CB  1 
ATOM   3061 O  OG1 . THR B 1 165 ? -35.290 31.562 45.188 1.00 16.45 ? 165 THR B OG1 1 
ATOM   3062 C  CG2 . THR B 1 165 ? -33.257 32.760 44.698 1.00 14.08 ? 165 THR B CG2 1 
ATOM   3063 N  N   . ILE B 1 166 ? -32.816 32.009 41.207 1.00 11.86 ? 166 ILE B N   1 
ATOM   3064 C  CA  . ILE B 1 166 ? -31.592 31.881 40.428 1.00 11.71 ? 166 ILE B CA  1 
ATOM   3065 C  C   . ILE B 1 166 ? -30.388 32.313 41.259 1.00 11.60 ? 166 ILE B C   1 
ATOM   3066 O  O   . ILE B 1 166 ? -30.411 33.365 41.893 1.00 11.98 ? 166 ILE B O   1 
ATOM   3067 C  CB  . ILE B 1 166 ? -31.649 32.739 39.147 1.00 10.40 ? 166 ILE B CB  1 
ATOM   3068 C  CG1 . ILE B 1 166 ? -32.759 32.220 38.225 1.00 10.76 ? 166 ILE B CG1 1 
ATOM   3069 C  CG2 . ILE B 1 166 ? -30.299 32.703 38.438 1.00 9.00  ? 166 ILE B CG2 1 
ATOM   3070 C  CD1 . ILE B 1 166 ? -32.956 33.049 36.963 1.00 11.47 ? 166 ILE B CD1 1 
ATOM   3071 N  N   . PRO B 1 167 ? -29.324 31.491 41.277 1.00 11.94 ? 167 PRO B N   1 
ATOM   3072 C  CA  . PRO B 1 167 ? -28.110 31.809 42.039 1.00 11.20 ? 167 PRO B CA  1 
ATOM   3073 C  C   . PRO B 1 167 ? -27.474 33.119 41.589 1.00 10.67 ? 167 PRO B C   1 
ATOM   3074 O  O   . PRO B 1 167 ? -27.623 33.527 40.438 1.00 10.48 ? 167 PRO B O   1 
ATOM   3075 C  CB  . PRO B 1 167 ? -27.186 30.618 41.773 1.00 10.37 ? 167 PRO B CB  1 
ATOM   3076 C  CG  . PRO B 1 167 ? -28.088 29.519 41.314 1.00 10.43 ? 167 PRO B CG  1 
ATOM   3077 C  CD  . PRO B 1 167 ? -29.218 30.189 40.594 1.00 11.43 ? 167 PRO B CD  1 
ATOM   3078 N  N   . SER B 1 168 ? -26.768 33.775 42.504 1.00 8.99  ? 168 SER B N   1 
ATOM   3079 C  CA  . SER B 1 168 ? -26.094 35.026 42.193 1.00 8.73  ? 168 SER B CA  1 
ATOM   3080 C  C   . SER B 1 168 ? -24.590 34.783 42.124 1.00 9.13  ? 168 SER B C   1 
ATOM   3081 O  O   . SER B 1 168 ? -23.844 35.607 41.601 1.00 10.04 ? 168 SER B O   1 
ATOM   3082 C  CB  . SER B 1 168 ? -26.405 36.084 43.259 1.00 8.95  ? 168 SER B CB  1 
ATOM   3083 O  OG  . SER B 1 168 ? -25.928 35.693 44.533 1.00 11.50 ? 168 SER B OG  1 
ATOM   3084 N  N   . ALA B 1 169 ? -24.155 33.638 42.642 1.00 8.71  ? 169 ALA B N   1 
ATOM   3085 C  CA  . ALA B 1 169 ? -22.739 33.288 42.653 1.00 8.06  ? 169 ALA B CA  1 
ATOM   3086 C  C   . ALA B 1 169 ? -22.537 31.787 42.835 1.00 8.49  ? 169 ALA B C   1 
ATOM   3087 O  O   . ALA B 1 169 ? -23.473 31.059 43.162 1.00 8.00  ? 169 ALA B O   1 
ATOM   3088 C  CB  . ALA B 1 169 ? -22.029 34.051 43.768 1.00 7.81  ? 169 ALA B CB  1 
ATOM   3089 N  N   . TYR B 1 170 ? -21.307 31.331 42.618 1.00 8.13  ? 170 TYR B N   1 
ATOM   3090 C  CA  . TYR B 1 170 ? -20.968 29.923 42.752 1.00 8.81  ? 170 TYR B CA  1 
ATOM   3091 C  C   . TYR B 1 170 ? -19.622 29.775 43.450 1.00 9.41  ? 170 TYR B C   1 
ATOM   3092 O  O   . TYR B 1 170 ? -18.720 30.589 43.257 1.00 9.87  ? 170 TYR B O   1 
ATOM   3093 C  CB  . TYR B 1 170 ? -20.897 29.264 41.371 1.00 10.20 ? 170 TYR B CB  1 
ATOM   3094 C  CG  . TYR B 1 170 ? -22.198 29.312 40.601 1.00 9.77  ? 170 TYR B CG  1 
ATOM   3095 C  CD1 . TYR B 1 170 ? -23.130 28.281 40.709 1.00 8.71  ? 170 TYR B CD1 1 
ATOM   3096 C  CD2 . TYR B 1 170 ? -22.505 30.399 39.778 1.00 10.42 ? 170 TYR B CD2 1 
ATOM   3097 C  CE1 . TYR B 1 170 ? -24.339 28.327 40.021 1.00 10.02 ? 170 TYR B CE1 1 
ATOM   3098 C  CE2 . TYR B 1 170 ? -23.715 30.456 39.083 1.00 10.05 ? 170 TYR B CE2 1 
ATOM   3099 C  CZ  . TYR B 1 170 ? -24.626 29.416 39.212 1.00 11.54 ? 170 TYR B CZ  1 
ATOM   3100 O  OH  . TYR B 1 170 ? -25.831 29.467 38.547 1.00 14.25 ? 170 TYR B OH  1 
ATOM   3101 N  N   . TRP B 1 171 ? -19.491 28.731 44.260 1.00 9.41  ? 171 TRP B N   1 
ATOM   3102 C  CA  . TRP B 1 171 ? -18.248 28.479 44.976 1.00 8.79  ? 171 TRP B CA  1 
ATOM   3103 C  C   . TRP B 1 171 ? -17.820 27.041 44.752 1.00 8.20  ? 171 TRP B C   1 
ATOM   3104 O  O   . TRP B 1 171 ? -18.628 26.185 44.390 1.00 9.07  ? 171 TRP B O   1 
ATOM   3105 C  CB  . TRP B 1 171 ? -18.419 28.742 46.482 1.00 7.12  ? 171 TRP B CB  1 
ATOM   3106 C  CG  . TRP B 1 171 ? -19.624 28.086 47.069 1.00 6.89  ? 171 TRP B CG  1 
ATOM   3107 C  CD1 . TRP B 1 171 ? -20.883 28.611 47.150 1.00 5.86  ? 171 TRP B CD1 1 
ATOM   3108 C  CD2 . TRP B 1 171 ? -19.705 26.760 47.611 1.00 7.09  ? 171 TRP B CD2 1 
ATOM   3109 N  NE1 . TRP B 1 171 ? -21.746 27.694 47.704 1.00 7.89  ? 171 TRP B NE1 1 
ATOM   3110 C  CE2 . TRP B 1 171 ? -21.051 26.548 47.996 1.00 7.59  ? 171 TRP B CE2 1 
ATOM   3111 C  CE3 . TRP B 1 171 ? -18.775 25.729 47.807 1.00 6.69  ? 171 TRP B CE3 1 
ATOM   3112 C  CZ2 . TRP B 1 171 ? -21.489 25.344 48.565 1.00 7.14  ? 171 TRP B CZ2 1 
ATOM   3113 C  CZ3 . TRP B 1 171 ? -19.211 24.530 48.375 1.00 7.19  ? 171 TRP B CZ3 1 
ATOM   3114 C  CH2 . TRP B 1 171 ? -20.558 24.350 48.746 1.00 7.86  ? 171 TRP B CH2 1 
ATOM   3115 N  N   . LYS B 1 172 ? -16.537 26.785 44.965 1.00 7.29  ? 172 LYS B N   1 
ATOM   3116 C  CA  . LYS B 1 172 ? -15.981 25.456 44.795 1.00 8.04  ? 172 LYS B CA  1 
ATOM   3117 C  C   . LYS B 1 172 ? -14.808 25.284 45.759 1.00 8.03  ? 172 LYS B C   1 
ATOM   3118 O  O   . LYS B 1 172 ? -13.880 26.091 45.770 1.00 9.48  ? 172 LYS B O   1 
ATOM   3119 C  CB  . LYS B 1 172 ? -15.511 25.262 43.346 1.00 9.00  ? 172 LYS B CB  1 
ATOM   3120 C  CG  . LYS B 1 172 ? -15.018 23.857 43.039 1.00 11.13 ? 172 LYS B CG  1 
ATOM   3121 C  CD  . LYS B 1 172 ? -14.748 23.669 41.555 1.00 11.38 ? 172 LYS B CD  1 
ATOM   3122 C  CE  . LYS B 1 172 ? -16.012 23.238 40.815 1.00 10.32 ? 172 LYS B CE  1 
ATOM   3123 N  NZ  . LYS B 1 172 ? -15.731 22.927 39.379 1.00 9.28  ? 172 LYS B NZ  1 
ATOM   3124 N  N   . VAL B 1 173 ? -14.877 24.235 46.572 1.00 7.35  ? 173 VAL B N   1 
ATOM   3125 C  CA  . VAL B 1 173 ? -13.842 23.917 47.545 1.00 6.99  ? 173 VAL B CA  1 
ATOM   3126 C  C   . VAL B 1 173 ? -13.207 22.610 47.087 1.00 6.87  ? 173 VAL B C   1 
ATOM   3127 O  O   . VAL B 1 173 ? -13.905 21.628 46.822 1.00 6.98  ? 173 VAL B O   1 
ATOM   3128 C  CB  . VAL B 1 173 ? -14.445 23.745 48.958 1.00 6.61  ? 173 VAL B CB  1 
ATOM   3129 C  CG1 . VAL B 1 173 ? -13.371 23.351 49.935 1.00 6.90  ? 173 VAL B CG1 1 
ATOM   3130 C  CG2 . VAL B 1 173 ? -15.099 25.040 49.400 1.00 5.93  ? 173 VAL B CG2 1 
ATOM   3131 N  N   . ILE B 1 174 ? -11.882 22.599 47.000 1.00 6.54  ? 174 ILE B N   1 
ATOM   3132 C  CA  . ILE B 1 174 ? -11.158 21.428 46.518 1.00 7.01  ? 174 ILE B CA  1 
ATOM   3133 C  C   . ILE B 1 174 ? -9.956  21.042 47.368 1.00 6.52  ? 174 ILE B C   1 
ATOM   3134 O  O   . ILE B 1 174 ? -9.293  21.892 47.955 1.00 8.01  ? 174 ILE B O   1 
ATOM   3135 C  CB  . ILE B 1 174 ? -10.618 21.677 45.069 1.00 9.28  ? 174 ILE B CB  1 
ATOM   3136 C  CG1 . ILE B 1 174 ? -11.714 22.282 44.187 1.00 12.32 ? 174 ILE B CG1 1 
ATOM   3137 C  CG2 . ILE B 1 174 ? -10.092 20.383 44.464 1.00 8.81  ? 174 ILE B CG2 1 
ATOM   3138 C  CD1 . ILE B 1 174 ? -11.181 23.197 43.097 1.00 12.89 ? 174 ILE B CD1 1 
ATOM   3139 N  N   . PHE B 1 175 ? -9.696  19.744 47.443 1.00 7.62  ? 175 PHE B N   1 
ATOM   3140 C  CA  . PHE B 1 175 ? -8.519  19.241 48.131 1.00 8.52  ? 175 PHE B CA  1 
ATOM   3141 C  C   . PHE B 1 175 ? -8.137  17.942 47.437 1.00 9.16  ? 175 PHE B C   1 
ATOM   3142 O  O   . PHE B 1 175 ? -8.974  17.289 46.805 1.00 8.77  ? 175 PHE B O   1 
ATOM   3143 C  CB  . PHE B 1 175 ? -8.747  19.067 49.648 1.00 7.66  ? 175 PHE B CB  1 
ATOM   3144 C  CG  . PHE B 1 175 ? -9.538  17.856 50.031 1.00 7.79  ? 175 PHE B CG  1 
ATOM   3145 C  CD1 . PHE B 1 175 ? -8.924  16.612 50.147 1.00 8.17  ? 175 PHE B CD1 1 
ATOM   3146 C  CD2 . PHE B 1 175 ? -10.890 17.971 50.346 1.00 7.74  ? 175 PHE B CD2 1 
ATOM   3147 C  CE1 . PHE B 1 175 ? -9.647  15.496 50.578 1.00 9.33  ? 175 PHE B CE1 1 
ATOM   3148 C  CE2 . PHE B 1 175 ? -11.623 16.862 50.778 1.00 8.68  ? 175 PHE B CE2 1 
ATOM   3149 C  CZ  . PHE B 1 175 ? -11.002 15.624 50.896 1.00 8.66  ? 175 PHE B CZ  1 
ATOM   3150 N  N   . ILE B 1 176 ? -6.865  17.582 47.522 1.00 9.10  ? 176 ILE B N   1 
ATOM   3151 C  CA  . ILE B 1 176 ? -6.392  16.380 46.860 1.00 9.15  ? 176 ILE B CA  1 
ATOM   3152 C  C   . ILE B 1 176 ? -6.044  15.246 47.810 1.00 9.72  ? 176 ILE B C   1 
ATOM   3153 O  O   . ILE B 1 176 ? -5.757  15.461 48.990 1.00 8.50  ? 176 ILE B O   1 
ATOM   3154 C  CB  . ILE B 1 176 ? -5.144  16.681 46.002 1.00 8.89  ? 176 ILE B CB  1 
ATOM   3155 C  CG1 . ILE B 1 176 ? -4.089  17.400 46.854 1.00 9.95  ? 176 ILE B CG1 1 
ATOM   3156 C  CG2 . ILE B 1 176 ? -5.533  17.530 44.808 1.00 8.80  ? 176 ILE B CG2 1 
ATOM   3157 C  CD1 . ILE B 1 176 ? -2.665  17.274 46.326 1.00 9.93  ? 176 ILE B CD1 1 
ATOM   3158 N  N   . ASN B 1 177 ? -6.097  14.040 47.256 1.00 9.24  ? 177 ASN B N   1 
ATOM   3159 C  CA  . ASN B 1 177 ? -5.763  12.803 47.937 1.00 11.93 ? 177 ASN B CA  1 
ATOM   3160 C  C   . ASN B 1 177 ? -6.559  12.359 49.157 1.00 13.73 ? 177 ASN B C   1 
ATOM   3161 O  O   . ASN B 1 177 ? -7.612  11.747 49.015 1.00 17.43 ? 177 ASN B O   1 
ATOM   3162 C  CB  . ASN B 1 177 ? -4.267  12.798 48.264 1.00 9.75  ? 177 ASN B CB  1 
ATOM   3163 C  CG  . ASN B 1 177 ? -3.410  12.670 47.019 1.00 13.81 ? 177 ASN B CG  1 
ATOM   3164 O  OD1 . ASN B 1 177 ? -3.925  12.445 45.925 1.00 14.45 ? 177 ASN B OD1 1 
ATOM   3165 N  ND2 . ASN B 1 177 ? -2.100  12.815 47.177 1.00 13.07 ? 177 ASN B ND2 1 
ATOM   3166 N  N   . ASN B 1 178 ? -6.064  12.668 50.351 1.00 12.46 ? 178 ASN B N   1 
ATOM   3167 C  CA  . ASN B 1 178 ? -6.711  12.211 51.578 1.00 13.37 ? 178 ASN B CA  1 
ATOM   3168 C  C   . ASN B 1 178 ? -7.560  13.162 52.404 1.00 11.61 ? 178 ASN B C   1 
ATOM   3169 O  O   . ASN B 1 178 ? -8.716  12.860 52.711 1.00 10.14 ? 178 ASN B O   1 
ATOM   3170 C  CB  . ASN B 1 178 ? -5.653  11.606 52.495 1.00 18.16 ? 178 ASN B CB  1 
ATOM   3171 C  CG  . ASN B 1 178 ? -4.839  10.541 51.806 1.00 23.40 ? 178 ASN B CG  1 
ATOM   3172 O  OD1 . ASN B 1 178 ? -5.367  9.501  51.420 1.00 26.68 ? 178 ASN B OD1 1 
ATOM   3173 N  ND2 . ASN B 1 178 ? -3.544  10.795 51.642 1.00 29.20 ? 178 ASN B ND2 1 
ATOM   3174 N  N   . SER B 1 179 ? -6.985  14.294 52.792 1.00 10.07 ? 179 SER B N   1 
ATOM   3175 C  CA  . SER B 1 179 ? -7.712  15.239 53.625 1.00 9.72  ? 179 SER B CA  1 
ATOM   3176 C  C   . SER B 1 179 ? -7.002  16.577 53.658 1.00 9.27  ? 179 SER B C   1 
ATOM   3177 O  O   . SER B 1 179 ? -5.773  16.634 53.616 1.00 8.80  ? 179 SER B O   1 
ATOM   3178 C  CB  . SER B 1 179 ? -7.819  14.677 55.051 1.00 10.60 ? 179 SER B CB  1 
ATOM   3179 O  OG  . SER B 1 179 ? -8.145  15.685 55.991 1.00 12.59 ? 179 SER B OG  1 
ATOM   3180 N  N   . PRO B 1 180 ? -7.770  17.676 53.734 1.00 10.87 ? 180 PRO B N   1 
ATOM   3181 C  CA  . PRO B 1 180 ? -7.153  19.005 53.775 1.00 10.20 ? 180 PRO B CA  1 
ATOM   3182 C  C   . PRO B 1 180 ? -6.296  19.157 55.031 1.00 10.54 ? 180 PRO B C   1 
ATOM   3183 O  O   . PRO B 1 180 ? -5.526  20.107 55.161 1.00 10.81 ? 180 PRO B O   1 
ATOM   3184 C  CB  . PRO B 1 180 ? -8.347  19.966 53.756 1.00 7.79  ? 180 PRO B CB  1 
ATOM   3185 C  CG  . PRO B 1 180 ? -9.511  19.153 54.177 1.00 6.72  ? 180 PRO B CG  1 
ATOM   3186 C  CD  . PRO B 1 180 ? -9.242  17.740 53.785 1.00 6.35  ? 180 PRO B CD  1 
ATOM   3187 N  N   . ALA B 1 181 ? -6.435  18.210 55.956 1.00 8.57  ? 181 ALA B N   1 
ATOM   3188 C  CA  . ALA B 1 181 ? -5.660  18.234 57.190 1.00 8.99  ? 181 ALA B CA  1 
ATOM   3189 C  C   . ALA B 1 181 ? -4.175  18.028 56.893 1.00 9.74  ? 181 ALA B C   1 
ATOM   3190 O  O   . ALA B 1 181 ? -3.319  18.516 57.629 1.00 11.10 ? 181 ALA B O   1 
ATOM   3191 C  CB  . ALA B 1 181 ? -6.157  17.150 58.141 1.00 9.59  ? 181 ALA B CB  1 
ATOM   3192 N  N   . VAL B 1 182 ? -3.872  17.312 55.811 1.00 8.51  ? 182 VAL B N   1 
ATOM   3193 C  CA  . VAL B 1 182 ? -2.484  17.044 55.434 1.00 7.52  ? 182 VAL B CA  1 
ATOM   3194 C  C   . VAL B 1 182 ? -2.183  17.336 53.959 1.00 8.53  ? 182 VAL B C   1 
ATOM   3195 O  O   . VAL B 1 182 ? -1.016  17.375 53.561 1.00 8.77  ? 182 VAL B O   1 
ATOM   3196 C  CB  . VAL B 1 182 ? -2.102  15.558 55.717 1.00 9.03  ? 182 VAL B CB  1 
ATOM   3197 C  CG1 . VAL B 1 182 ? -2.254  15.247 57.199 1.00 9.68  ? 182 VAL B CG1 1 
ATOM   3198 C  CG2 . VAL B 1 182 ? -2.987  14.619 54.902 1.00 9.40  ? 182 VAL B CG2 1 
ATOM   3199 N  N   . ASN B 1 183 ? -3.230  17.545 53.158 1.00 8.08  ? 183 ASN B N   1 
ATOM   3200 C  CA  . ASN B 1 183 ? -3.085  17.794 51.717 1.00 7.25  ? 183 ASN B CA  1 
ATOM   3201 C  C   . ASN B 1 183 ? -3.488  19.187 51.258 1.00 8.49  ? 183 ASN B C   1 
ATOM   3202 O  O   . ASN B 1 183 ? -4.320  19.847 51.885 1.00 9.74  ? 183 ASN B O   1 
ATOM   3203 C  CB  . ASN B 1 183 ? -3.917  16.785 50.923 1.00 7.32  ? 183 ASN B CB  1 
ATOM   3204 C  CG  . ASN B 1 183 ? -3.433  15.363 51.097 1.00 8.72  ? 183 ASN B CG  1 
ATOM   3205 O  OD1 . ASN B 1 183 ? -4.167  14.501 51.581 1.00 7.57  ? 183 ASN B OD1 1 
ATOM   3206 N  ND2 . ASN B 1 183 ? -2.191  15.108 50.698 1.00 9.65  ? 183 ASN B ND2 1 
ATOM   3207 N  N   . HIS B 1 184 ? -2.915  19.613 50.135 1.00 7.00  ? 184 HIS B N   1 
ATOM   3208 C  CA  . HIS B 1 184 ? -3.203  20.925 49.566 1.00 6.37  ? 184 HIS B CA  1 
ATOM   3209 C  C   . HIS B 1 184 ? -4.693  21.089 49.280 1.00 6.69  ? 184 HIS B C   1 
ATOM   3210 O  O   . HIS B 1 184 ? -5.364  20.138 48.872 1.00 6.21  ? 184 HIS B O   1 
ATOM   3211 C  CB  . HIS B 1 184 ? -2.432  21.118 48.261 1.00 6.63  ? 184 HIS B CB  1 
ATOM   3212 C  CG  . HIS B 1 184 ? -0.946  21.042 48.414 1.00 8.24  ? 184 HIS B CG  1 
ATOM   3213 N  ND1 . HIS B 1 184 ? -0.284  21.526 49.522 1.00 8.78  ? 184 HIS B ND1 1 
ATOM   3214 C  CD2 . HIS B 1 184 ? 0.010   20.554 47.587 1.00 8.47  ? 184 HIS B CD2 1 
ATOM   3215 C  CE1 . HIS B 1 184 ? 1.017   21.340 49.371 1.00 9.50  ? 184 HIS B CE1 1 
ATOM   3216 N  NE2 . HIS B 1 184 ? 1.222   20.752 48.206 1.00 9.13  ? 184 HIS B NE2 1 
ATOM   3217 N  N   . TYR B 1 185 ? -5.202  22.301 49.479 1.00 6.42  ? 185 TYR B N   1 
ATOM   3218 C  CA  . TYR B 1 185 ? -6.610  22.579 49.228 1.00 6.64  ? 185 TYR B CA  1 
ATOM   3219 C  C   . TYR B 1 185 ? -6.778  23.954 48.599 1.00 7.30  ? 185 TYR B C   1 
ATOM   3220 O  O   . TYR B 1 185 ? -5.829  24.740 48.513 1.00 7.25  ? 185 TYR B O   1 
ATOM   3221 C  CB  . TYR B 1 185 ? -7.421  22.499 50.530 1.00 6.46  ? 185 TYR B CB  1 
ATOM   3222 C  CG  . TYR B 1 185 ? -6.964  23.468 51.598 1.00 7.01  ? 185 TYR B CG  1 
ATOM   3223 C  CD1 . TYR B 1 185 ? -7.468  24.771 51.650 1.00 6.63  ? 185 TYR B CD1 1 
ATOM   3224 C  CD2 . TYR B 1 185 ? -6.013  23.089 52.547 1.00 7.80  ? 185 TYR B CD2 1 
ATOM   3225 C  CE1 . TYR B 1 185 ? -7.035  25.670 52.618 1.00 7.88  ? 185 TYR B CE1 1 
ATOM   3226 C  CE2 . TYR B 1 185 ? -5.572  23.981 53.520 1.00 8.00  ? 185 TYR B CE2 1 
ATOM   3227 C  CZ  . TYR B 1 185 ? -6.085  25.267 53.550 1.00 9.19  ? 185 TYR B CZ  1 
ATOM   3228 O  OH  . TYR B 1 185 ? -5.642  26.151 54.508 1.00 9.46  ? 185 TYR B OH  1 
ATOM   3229 N  N   . ALA B 1 186 ? -7.996  24.237 48.160 1.00 6.56  ? 186 ALA B N   1 
ATOM   3230 C  CA  . ALA B 1 186 ? -8.309  25.510 47.527 1.00 7.17  ? 186 ALA B CA  1 
ATOM   3231 C  C   . ALA B 1 186 ? -9.805  25.794 47.600 1.00 6.73  ? 186 ALA B C   1 
ATOM   3232 O  O   . ALA B 1 186 ? -10.618 24.880 47.748 1.00 7.00  ? 186 ALA B O   1 
ATOM   3233 C  CB  . ALA B 1 186 ? -7.867  25.484 46.074 1.00 5.79  ? 186 ALA B CB  1 
ATOM   3234 N  N   . ALA B 1 187 ? -10.156 27.069 47.498 1.00 6.82  ? 187 ALA B N   1 
ATOM   3235 C  CA  . ALA B 1 187 ? -11.546 27.487 47.512 1.00 7.71  ? 187 ALA B CA  1 
ATOM   3236 C  C   . ALA B 1 187 ? -11.655 28.688 46.593 1.00 8.10  ? 187 ALA B C   1 
ATOM   3237 O  O   . ALA B 1 187 ? -10.804 29.576 46.618 1.00 8.87  ? 187 ALA B O   1 
ATOM   3238 C  CB  . ALA B 1 187 ? -11.985 27.853 48.924 1.00 7.18  ? 187 ALA B CB  1 
ATOM   3239 N  N   . PHE B 1 188 ? -12.694 28.698 45.767 1.00 9.17  ? 188 PHE B N   1 
ATOM   3240 C  CA  . PHE B 1 188 ? -12.928 29.789 44.830 1.00 9.36  ? 188 PHE B CA  1 
ATOM   3241 C  C   . PHE B 1 188 ? -14.381 30.221 44.946 1.00 9.45  ? 188 PHE B C   1 
ATOM   3242 O  O   . PHE B 1 188 ? -15.234 29.445 45.386 1.00 9.70  ? 188 PHE B O   1 
ATOM   3243 C  CB  . PHE B 1 188 ? -12.672 29.333 43.388 1.00 9.85  ? 188 PHE B CB  1 
ATOM   3244 C  CG  . PHE B 1 188 ? -11.272 28.854 43.132 1.00 10.70 ? 188 PHE B CG  1 
ATOM   3245 C  CD1 . PHE B 1 188 ? -10.919 27.530 43.381 1.00 10.53 ? 188 PHE B CD1 1 
ATOM   3246 C  CD2 . PHE B 1 188 ? -10.313 29.719 42.614 1.00 11.33 ? 188 PHE B CD2 1 
ATOM   3247 C  CE1 . PHE B 1 188 ? -9.629  27.071 43.119 1.00 10.81 ? 188 PHE B CE1 1 
ATOM   3248 C  CE2 . PHE B 1 188 ? -9.021  29.273 42.347 1.00 12.46 ? 188 PHE B CE2 1 
ATOM   3249 C  CZ  . PHE B 1 188 ? -8.678  27.946 42.600 1.00 11.96 ? 188 PHE B CZ  1 
ATOM   3250 N  N   . LEU B 1 189 ? -14.655 31.458 44.548 1.00 8.66  ? 189 LEU B N   1 
ATOM   3251 C  CA  . LEU B 1 189 ? -16.011 31.993 44.570 1.00 9.98  ? 189 LEU B CA  1 
ATOM   3252 C  C   . LEU B 1 189 ? -16.174 32.953 43.394 1.00 10.17 ? 189 LEU B C   1 
ATOM   3253 O  O   . LEU B 1 189 ? -15.458 33.947 43.297 1.00 11.05 ? 189 LEU B O   1 
ATOM   3254 C  CB  . LEU B 1 189 ? -16.278 32.720 45.887 1.00 10.41 ? 189 LEU B CB  1 
ATOM   3255 C  CG  . LEU B 1 189 ? -17.748 32.848 46.290 1.00 12.46 ? 189 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B 1 189 ? -17.854 33.008 47.804 1.00 13.23 ? 189 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B 1 189 ? -18.371 34.038 45.583 1.00 13.90 ? 189 LEU B CD2 1 
ATOM   3258 N  N   . PHE B 1 190 ? -17.108 32.647 42.497 1.00 10.87 ? 190 PHE B N   1 
ATOM   3259 C  CA  . PHE B 1 190 ? -17.349 33.487 41.322 1.00 11.46 ? 190 PHE B CA  1 
ATOM   3260 C  C   . PHE B 1 190 ? -18.767 34.056 41.284 1.00 12.10 ? 190 PHE B C   1 
ATOM   3261 O  O   . PHE B 1 190 ? -19.741 33.335 41.486 1.00 12.21 ? 190 PHE B O   1 
ATOM   3262 C  CB  . PHE B 1 190 ? -17.139 32.691 40.026 1.00 11.58 ? 190 PHE B CB  1 
ATOM   3263 C  CG  . PHE B 1 190 ? -15.787 32.050 39.904 1.00 12.04 ? 190 PHE B CG  1 
ATOM   3264 C  CD1 . PHE B 1 190 ? -15.534 30.816 40.490 1.00 12.60 ? 190 PHE B CD1 1 
ATOM   3265 C  CD2 . PHE B 1 190 ? -14.775 32.666 39.174 1.00 14.16 ? 190 PHE B CD2 1 
ATOM   3266 C  CE1 . PHE B 1 190 ? -14.291 30.201 40.349 1.00 12.36 ? 190 PHE B CE1 1 
ATOM   3267 C  CE2 . PHE B 1 190 ? -13.528 32.057 39.028 1.00 13.14 ? 190 PHE B CE2 1 
ATOM   3268 C  CZ  . PHE B 1 190 ? -13.290 30.824 39.617 1.00 13.00 ? 190 PHE B CZ  1 
ATOM   3269 N  N   . ASP B 1 191 ? -18.875 35.351 41.014 1.00 11.11 ? 191 ASP B N   1 
ATOM   3270 C  CA  . ASP B 1 191 ? -20.172 35.996 40.903 1.00 10.70 ? 191 ASP B CA  1 
ATOM   3271 C  C   . ASP B 1 191 ? -20.694 35.628 39.515 1.00 10.09 ? 191 ASP B C   1 
ATOM   3272 O  O   . ASP B 1 191 ? -19.911 35.401 38.591 1.00 9.19  ? 191 ASP B O   1 
ATOM   3273 C  CB  . ASP B 1 191 ? -20.024 37.517 41.019 1.00 12.87 ? 191 ASP B CB  1 
ATOM   3274 C  CG  . ASP B 1 191 ? -21.364 38.235 41.057 1.00 16.63 ? 191 ASP B CG  1 
ATOM   3275 O  OD1 . ASP B 1 191 ? -21.915 38.537 39.975 1.00 17.02 ? 191 ASP B OD1 1 
ATOM   3276 O  OD2 . ASP B 1 191 ? -21.869 38.499 42.171 1.00 20.23 ? 191 ASP B OD2 1 
ATOM   3277 N  N   . GLN B 1 192 ? -22.012 35.559 39.376 1.00 10.99 ? 192 GLN B N   1 
ATOM   3278 C  CA  . GLN B 1 192 ? -22.637 35.226 38.101 1.00 12.37 ? 192 GLN B CA  1 
ATOM   3279 C  C   . GLN B 1 192 ? -22.142 36.134 36.979 1.00 13.43 ? 192 GLN B C   1 
ATOM   3280 O  O   . GLN B 1 192 ? -21.942 35.689 35.849 1.00 14.06 ? 192 GLN B O   1 
ATOM   3281 C  CB  . GLN B 1 192 ? -24.159 35.366 38.212 1.00 11.36 ? 192 GLN B CB  1 
ATOM   3282 C  CG  . GLN B 1 192 ? -24.855 34.164 38.810 1.00 10.41 ? 192 GLN B CG  1 
ATOM   3283 C  CD  . GLN B 1 192 ? -25.340 33.187 37.755 1.00 10.02 ? 192 GLN B CD  1 
ATOM   3284 O  OE1 . GLN B 1 192 ? -24.635 32.896 36.787 1.00 9.99  ? 192 GLN B OE1 1 
ATOM   3285 N  NE2 . GLN B 1 192 ? -26.550 32.672 37.940 1.00 9.34  ? 192 GLN B NE2 1 
ATOM   3286 N  N   . ASN B 1 193 ? -21.936 37.406 37.306 1.00 14.87 ? 193 ASN B N   1 
ATOM   3287 C  CA  . ASN B 1 193 ? -21.503 38.395 36.327 1.00 18.04 ? 193 ASN B CA  1 
ATOM   3288 C  C   . ASN B 1 193 ? -20.003 38.477 36.073 1.00 18.46 ? 193 ASN B C   1 
ATOM   3289 O  O   . ASN B 1 193 ? -19.500 39.524 35.674 1.00 19.41 ? 193 ASN B O   1 
ATOM   3290 C  CB  . ASN B 1 193 ? -22.023 39.777 36.733 1.00 22.88 ? 193 ASN B CB  1 
ATOM   3291 C  CG  . ASN B 1 193 ? -23.542 39.856 36.718 1.00 30.03 ? 193 ASN B CG  1 
ATOM   3292 O  OD1 . ASN B 1 193 ? -24.139 40.694 37.395 1.00 32.10 ? 193 ASN B OD1 1 
ATOM   3293 N  ND2 . ASN B 1 193 ? -24.173 38.980 35.944 1.00 30.48 ? 193 ASN B ND2 1 
ATOM   3294 N  N   . THR B 1 194 ? -19.289 37.379 36.292 1.00 16.83 ? 194 THR B N   1 
ATOM   3295 C  CA  . THR B 1 194 ? -17.846 37.363 36.065 1.00 15.93 ? 194 THR B CA  1 
ATOM   3296 C  C   . THR B 1 194 ? -17.564 37.444 34.565 1.00 16.35 ? 194 THR B C   1 
ATOM   3297 O  O   . THR B 1 194 ? -18.070 36.639 33.788 1.00 15.52 ? 194 THR B O   1 
ATOM   3298 C  CB  . THR B 1 194 ? -17.215 36.076 36.634 1.00 17.12 ? 194 THR B CB  1 
ATOM   3299 O  OG1 . THR B 1 194 ? -17.414 36.039 38.053 1.00 15.51 ? 194 THR B OG1 1 
ATOM   3300 C  CG2 . THR B 1 194 ? -15.724 36.024 36.330 1.00 14.44 ? 194 THR B CG2 1 
ATOM   3301 N  N   . PRO B 1 195 ? -16.750 38.424 34.139 1.00 17.59 ? 195 PRO B N   1 
ATOM   3302 C  CA  . PRO B 1 195 ? -16.422 38.586 32.716 1.00 17.39 ? 195 PRO B CA  1 
ATOM   3303 C  C   . PRO B 1 195 ? -15.884 37.307 32.087 1.00 17.45 ? 195 PRO B C   1 
ATOM   3304 O  O   . PRO B 1 195 ? -15.183 36.533 32.735 1.00 16.50 ? 195 PRO B O   1 
ATOM   3305 C  CB  . PRO B 1 195 ? -15.390 39.712 32.705 1.00 18.53 ? 195 PRO B CB  1 
ATOM   3306 C  CG  . PRO B 1 195 ? -15.634 40.459 33.970 1.00 20.04 ? 195 PRO B CG  1 
ATOM   3307 C  CD  . PRO B 1 195 ? -16.084 39.436 34.975 1.00 17.87 ? 195 PRO B CD  1 
ATOM   3308 N  N   . LYS B 1 196 ? -16.208 37.098 30.816 1.00 18.22 ? 196 LYS B N   1 
ATOM   3309 C  CA  . LYS B 1 196 ? -15.783 35.906 30.093 1.00 20.41 ? 196 LYS B CA  1 
ATOM   3310 C  C   . LYS B 1 196 ? -14.277 35.629 30.136 1.00 21.23 ? 196 LYS B C   1 
ATOM   3311 O  O   . LYS B 1 196 ? -13.861 34.478 30.288 1.00 23.00 ? 196 LYS B O   1 
ATOM   3312 C  CB  . LYS B 1 196 ? -16.244 35.997 28.635 1.00 25.16 ? 196 LYS B CB  1 
ATOM   3313 C  CG  . LYS B 1 196 ? -15.800 34.831 27.769 1.00 28.73 ? 196 LYS B CG  1 
ATOM   3314 C  CD  . LYS B 1 196 ? -16.940 33.857 27.528 1.00 34.19 ? 196 LYS B CD  1 
ATOM   3315 C  CE  . LYS B 1 196 ? -17.351 33.838 26.061 1.00 35.30 ? 196 LYS B CE  1 
ATOM   3316 N  NZ  . LYS B 1 196 ? -17.403 32.452 25.507 1.00 36.09 ? 196 LYS B NZ  1 
ATOM   3317 N  N   . GLY B 1 197 ? -13.464 36.674 30.007 1.00 19.93 ? 197 GLY B N   1 
ATOM   3318 C  CA  . GLY B 1 197 ? -12.023 36.484 30.011 1.00 18.92 ? 197 GLY B CA  1 
ATOM   3319 C  C   . GLY B 1 197 ? -11.336 36.584 31.359 1.00 18.94 ? 197 GLY B C   1 
ATOM   3320 O  O   . GLY B 1 197 ? -10.124 36.797 31.425 1.00 19.25 ? 197 GLY B O   1 
ATOM   3321 N  N   . ALA B 1 198 ? -12.096 36.425 32.436 1.00 18.39 ? 198 ALA B N   1 
ATOM   3322 C  CA  . ALA B 1 198 ? -11.536 36.508 33.782 1.00 17.72 ? 198 ALA B CA  1 
ATOM   3323 C  C   . ALA B 1 198 ? -10.588 35.352 34.106 1.00 16.74 ? 198 ALA B C   1 
ATOM   3324 O  O   . ALA B 1 198 ? -10.798 34.217 33.678 1.00 16.62 ? 198 ALA B O   1 
ATOM   3325 C  CB  . ALA B 1 198 ? -12.661 36.559 34.811 1.00 16.09 ? 198 ALA B CB  1 
ATOM   3326 N  N   . ASP B 1 199 ? -9.543  35.665 34.867 1.00 15.76 ? 199 ASP B N   1 
ATOM   3327 C  CA  . ASP B 1 199 ? -8.542  34.693 35.300 1.00 14.66 ? 199 ASP B CA  1 
ATOM   3328 C  C   . ASP B 1 199 ? -9.055  34.103 36.614 1.00 14.10 ? 199 ASP B C   1 
ATOM   3329 O  O   . ASP B 1 199 ? -9.106  34.796 37.631 1.00 14.09 ? 199 ASP B O   1 
ATOM   3330 C  CB  . ASP B 1 199 ? -7.208  35.415 35.516 1.00 14.83 ? 199 ASP B CB  1 
ATOM   3331 C  CG  . ASP B 1 199 ? -6.190  34.578 36.267 1.00 18.10 ? 199 ASP B CG  1 
ATOM   3332 O  OD1 . ASP B 1 199 ? -6.342  33.342 36.338 1.00 18.31 ? 199 ASP B OD1 1 
ATOM   3333 O  OD2 . ASP B 1 199 ? -5.221  35.169 36.790 1.00 23.49 ? 199 ASP B OD2 1 
ATOM   3334 N  N   . PHE B 1 200 ? -9.439  32.829 36.593 1.00 14.21 ? 200 PHE B N   1 
ATOM   3335 C  CA  . PHE B 1 200 ? -9.977  32.184 37.790 1.00 14.93 ? 200 PHE B CA  1 
ATOM   3336 C  C   . PHE B 1 200 ? -9.090  32.305 39.027 1.00 14.57 ? 200 PHE B C   1 
ATOM   3337 O  O   . PHE B 1 200 ? -9.579  32.214 40.154 1.00 15.22 ? 200 PHE B O   1 
ATOM   3338 C  CB  . PHE B 1 200 ? -10.303 30.708 37.505 1.00 15.00 ? 200 PHE B CB  1 
ATOM   3339 C  CG  . PHE B 1 200 ? -9.102  29.804 37.458 1.00 15.87 ? 200 PHE B CG  1 
ATOM   3340 C  CD1 . PHE B 1 200 ? -8.612  29.214 38.619 1.00 14.08 ? 200 PHE B CD1 1 
ATOM   3341 C  CD2 . PHE B 1 200 ? -8.478  29.518 36.247 1.00 15.54 ? 200 PHE B CD2 1 
ATOM   3342 C  CE1 . PHE B 1 200 ? -7.521  28.352 38.575 1.00 14.78 ? 200 PHE B CE1 1 
ATOM   3343 C  CE2 . PHE B 1 200 ? -7.384  28.656 36.194 1.00 17.09 ? 200 PHE B CE2 1 
ATOM   3344 C  CZ  . PHE B 1 200 ? -6.906  28.072 37.363 1.00 15.17 ? 200 PHE B CZ  1 
ATOM   3345 N  N   . CYS B 1 201 ? -7.796  32.527 38.814 1.00 13.33 ? 201 CYS B N   1 
ATOM   3346 C  CA  . CYS B 1 201 ? -6.848  32.667 39.911 1.00 12.90 ? 201 CYS B CA  1 
ATOM   3347 C  C   . CYS B 1 201 ? -7.152  33.876 40.789 1.00 13.35 ? 201 CYS B C   1 
ATOM   3348 O  O   . CYS B 1 201 ? -6.729  33.932 41.942 1.00 14.97 ? 201 CYS B O   1 
ATOM   3349 C  CB  . CYS B 1 201 ? -5.427  32.802 39.365 1.00 13.60 ? 201 CYS B CB  1 
ATOM   3350 S  SG  . CYS B 1 201 ? -4.819  31.317 38.516 1.00 15.38 ? 201 CYS B SG  1 
ATOM   3351 N  N   . GLN B 1 202 ? -7.877  34.846 40.244 1.00 12.50 ? 202 GLN B N   1 
ATOM   3352 C  CA  . GLN B 1 202 ? -8.205  36.049 40.995 1.00 13.92 ? 202 GLN B CA  1 
ATOM   3353 C  C   . GLN B 1 202 ? -9.424  35.885 41.897 1.00 13.53 ? 202 GLN B C   1 
ATOM   3354 O  O   . GLN B 1 202 ? -9.843  36.840 42.551 1.00 14.47 ? 202 GLN B O   1 
ATOM   3355 C  CB  . GLN B 1 202 ? -8.449  37.219 40.035 1.00 21.62 ? 202 GLN B CB  1 
ATOM   3356 C  CG  . GLN B 1 202 ? -7.246  37.594 39.185 1.00 30.40 ? 202 GLN B CG  1 
ATOM   3357 C  CD  . GLN B 1 202 ? -6.023  37.939 40.020 1.00 35.63 ? 202 GLN B CD  1 
ATOM   3358 O  OE1 . GLN B 1 202 ? -6.060  38.849 40.851 1.00 37.22 ? 202 GLN B OE1 1 
ATOM   3359 N  NE2 . GLN B 1 202 ? -4.929  37.211 39.801 1.00 36.65 ? 202 GLN B NE2 1 
ATOM   3360 N  N   . PHE B 1 203 ? -9.989  34.684 41.951 1.00 13.72 ? 203 PHE B N   1 
ATOM   3361 C  CA  . PHE B 1 203 ? -11.180 34.470 42.770 1.00 12.99 ? 203 PHE B CA  1 
ATOM   3362 C  C   . PHE B 1 203 ? -10.996 33.475 43.905 1.00 11.61 ? 203 PHE B C   1 
ATOM   3363 O  O   . PHE B 1 203 ? -11.940 32.806 44.328 1.00 10.84 ? 203 PHE B O   1 
ATOM   3364 C  CB  . PHE B 1 203 ? -12.342 34.063 41.864 1.00 13.45 ? 203 PHE B CB  1 
ATOM   3365 C  CG  . PHE B 1 203 ? -12.619 35.066 40.783 1.00 14.79 ? 203 PHE B CG  1 
ATOM   3366 C  CD1 . PHE B 1 203 ? -11.923 35.021 39.578 1.00 15.30 ? 203 PHE B CD1 1 
ATOM   3367 C  CD2 . PHE B 1 203 ? -13.531 36.094 40.991 1.00 15.57 ? 203 PHE B CD2 1 
ATOM   3368 C  CE1 . PHE B 1 203 ? -12.126 35.985 38.599 1.00 16.91 ? 203 PHE B CE1 1 
ATOM   3369 C  CE2 . PHE B 1 203 ? -13.743 37.067 40.017 1.00 17.54 ? 203 PHE B CE2 1 
ATOM   3370 C  CZ  . PHE B 1 203 ? -13.037 37.011 38.818 1.00 17.07 ? 203 PHE B CZ  1 
ATOM   3371 N  N   . ARG B 1 204 ? -9.768  33.395 44.403 1.00 10.92 ? 204 ARG B N   1 
ATOM   3372 C  CA  . ARG B 1 204 ? -9.447  32.500 45.501 1.00 11.71 ? 204 ARG B CA  1 
ATOM   3373 C  C   . ARG B 1 204 ? -9.968  33.126 46.789 1.00 11.20 ? 204 ARG B C   1 
ATOM   3374 O  O   . ARG B 1 204 ? -9.780  34.319 47.024 1.00 11.00 ? 204 ARG B O   1 
ATOM   3375 C  CB  . ARG B 1 204 ? -7.931  32.303 45.593 1.00 12.57 ? 204 ARG B CB  1 
ATOM   3376 C  CG  . ARG B 1 204 ? -7.316  31.626 44.382 1.00 14.10 ? 204 ARG B CG  1 
ATOM   3377 C  CD  . ARG B 1 204 ? -5.850  31.989 44.253 1.00 15.88 ? 204 ARG B CD  1 
ATOM   3378 N  NE  . ARG B 1 204 ? -5.027  31.159 45.127 1.00 22.89 ? 204 ARG B NE  1 
ATOM   3379 C  CZ  . ARG B 1 204 ? -3.707  31.020 45.015 1.00 24.43 ? 204 ARG B CZ  1 
ATOM   3380 N  NH1 . ARG B 1 204 ? -3.050  31.662 44.056 1.00 21.24 ? 204 ARG B NH1 1 
ATOM   3381 N  NH2 . ARG B 1 204 ? -3.047  30.233 45.862 1.00 21.34 ? 204 ARG B NH2 1 
ATOM   3382 N  N   . VAL B 1 205 ? -10.634 32.325 47.614 1.00 9.70  ? 205 VAL B N   1 
ATOM   3383 C  CA  . VAL B 1 205 ? -11.176 32.805 48.883 1.00 9.12  ? 205 VAL B CA  1 
ATOM   3384 C  C   . VAL B 1 205 ? -10.884 31.764 49.960 1.00 9.04  ? 205 VAL B C   1 
ATOM   3385 O  O   . VAL B 1 205 ? -10.209 30.771 49.693 1.00 9.34  ? 205 VAL B O   1 
ATOM   3386 C  CB  . VAL B 1 205 ? -12.713 33.019 48.795 1.00 8.58  ? 205 VAL B CB  1 
ATOM   3387 C  CG1 . VAL B 1 205 ? -13.032 34.114 47.794 1.00 7.79  ? 205 VAL B CG1 1 
ATOM   3388 C  CG2 . VAL B 1 205 ? -13.400 31.719 48.398 1.00 8.67  ? 205 VAL B CG2 1 
ATOM   3389 N  N   . THR B 1 206 ? -11.377 31.990 51.176 1.00 8.68  ? 206 THR B N   1 
ATOM   3390 C  CA  . THR B 1 206 ? -11.173 31.024 52.254 1.00 9.10  ? 206 THR B CA  1 
ATOM   3391 C  C   . THR B 1 206 ? -12.438 30.184 52.375 1.00 9.59  ? 206 THR B C   1 
ATOM   3392 O  O   . THR B 1 206 ? -13.505 30.591 51.911 1.00 9.31  ? 206 THR B O   1 
ATOM   3393 C  CB  . THR B 1 206 ? -10.909 31.708 53.619 1.00 8.55  ? 206 THR B CB  1 
ATOM   3394 O  OG1 . THR B 1 206 ? -12.021 32.539 53.968 1.00 10.48 ? 206 THR B OG1 1 
ATOM   3395 C  CG2 . THR B 1 206 ? -9.650  32.554 53.558 1.00 10.27 ? 206 THR B CG2 1 
ATOM   3396 N  N   . VAL B 1 207 ? -12.320 29.011 52.989 1.00 9.29  ? 207 VAL B N   1 
ATOM   3397 C  CA  . VAL B 1 207 ? -13.475 28.146 53.167 1.00 8.64  ? 207 VAL B CA  1 
ATOM   3398 C  C   . VAL B 1 207 ? -14.435 28.823 54.142 1.00 10.00 ? 207 VAL B C   1 
ATOM   3399 O  O   . VAL B 1 207 ? -15.653 28.717 54.010 1.00 9.75  ? 207 VAL B O   1 
ATOM   3400 C  CB  . VAL B 1 207 ? -13.058 26.774 53.728 1.00 9.07  ? 207 VAL B CB  1 
ATOM   3401 C  CG1 . VAL B 1 207 ? -14.293 25.976 54.136 1.00 8.84  ? 207 VAL B CG1 1 
ATOM   3402 C  CG2 . VAL B 1 207 ? -12.258 26.016 52.683 1.00 7.86  ? 207 VAL B CG2 1 
ATOM   3403 N  N   . ASP B 1 208 ? -13.872 29.533 55.115 1.00 9.51  ? 208 ASP B N   1 
ATOM   3404 C  CA  . ASP B 1 208 ? -14.666 30.230 56.115 1.00 9.16  ? 208 ASP B CA  1 
ATOM   3405 C  C   . ASP B 1 208 ? -15.634 31.226 55.484 1.00 8.68  ? 208 ASP B C   1 
ATOM   3406 O  O   . ASP B 1 208 ? -16.797 31.302 55.871 1.00 9.28  ? 208 ASP B O   1 
ATOM   3407 C  CB  . ASP B 1 208 ? -13.752 30.965 57.094 1.00 10.93 ? 208 ASP B CB  1 
ATOM   3408 C  CG  . ASP B 1 208 ? -14.527 31.824 58.068 1.00 13.17 ? 208 ASP B CG  1 
ATOM   3409 O  OD1 . ASP B 1 208 ? -15.241 31.260 58.916 1.00 15.04 ? 208 ASP B OD1 1 
ATOM   3410 O  OD2 . ASP B 1 208 ? -14.430 33.062 57.981 1.00 18.22 ? 208 ASP B OD2 1 
ATOM   3411 N  N   . GLU B 1 209 ? -15.151 31.998 54.518 1.00 8.44  ? 209 GLU B N   1 
ATOM   3412 C  CA  . GLU B 1 209 ? -16.003 32.973 53.857 1.00 8.02  ? 209 GLU B CA  1 
ATOM   3413 C  C   . GLU B 1 209 ? -17.198 32.286 53.199 1.00 8.40  ? 209 GLU B C   1 
ATOM   3414 O  O   . GLU B 1 209 ? -18.322 32.780 53.270 1.00 8.34  ? 209 GLU B O   1 
ATOM   3415 C  CB  . GLU B 1 209 ? -15.220 33.757 52.803 1.00 7.92  ? 209 GLU B CB  1 
ATOM   3416 C  CG  . GLU B 1 209 ? -16.130 34.541 51.874 1.00 11.33 ? 209 GLU B CG  1 
ATOM   3417 C  CD  . GLU B 1 209 ? -15.400 35.548 51.021 1.00 11.81 ? 209 GLU B CD  1 
ATOM   3418 O  OE1 . GLU B 1 209 ? -14.151 35.572 51.044 1.00 13.08 ? 209 GLU B OE1 1 
ATOM   3419 O  OE2 . GLU B 1 209 ? -16.088 36.319 50.323 1.00 15.10 ? 209 GLU B OE2 1 
ATOM   3420 N  N   . ILE B 1 210 ? -16.950 31.148 52.554 1.00 8.45  ? 210 ILE B N   1 
ATOM   3421 C  CA  . ILE B 1 210 ? -18.014 30.401 51.892 1.00 7.65  ? 210 ILE B CA  1 
ATOM   3422 C  C   . ILE B 1 210 ? -19.043 29.926 52.919 1.00 8.29  ? 210 ILE B C   1 
ATOM   3423 O  O   . ILE B 1 210 ? -20.254 30.022 52.696 1.00 8.41  ? 210 ILE B O   1 
ATOM   3424 C  CB  . ILE B 1 210 ? -17.445 29.173 51.131 1.00 7.45  ? 210 ILE B CB  1 
ATOM   3425 C  CG1 . ILE B 1 210 ? -16.633 29.646 49.923 1.00 8.04  ? 210 ILE B CG1 1 
ATOM   3426 C  CG2 . ILE B 1 210 ? -18.583 28.258 50.671 1.00 6.41  ? 210 ILE B CG2 1 
ATOM   3427 C  CD1 . ILE B 1 210 ? -15.770 28.572 49.300 1.00 7.29  ? 210 ILE B CD1 1 
ATOM   3428 N  N   . GLU B 1 211 ? -18.557 29.414 54.046 1.00 8.41  ? 211 GLU B N   1 
ATOM   3429 C  CA  . GLU B 1 211 ? -19.430 28.924 55.107 1.00 8.46  ? 211 GLU B CA  1 
ATOM   3430 C  C   . GLU B 1 211 ? -20.299 30.041 55.677 1.00 9.01  ? 211 GLU B C   1 
ATOM   3431 O  O   . GLU B 1 211 ? -21.485 29.844 55.937 1.00 10.59 ? 211 GLU B O   1 
ATOM   3432 C  CB  . GLU B 1 211 ? -18.596 28.288 56.220 1.00 6.64  ? 211 GLU B CB  1 
ATOM   3433 C  CG  . GLU B 1 211 ? -18.009 26.941 55.827 1.00 7.43  ? 211 GLU B CG  1 
ATOM   3434 C  CD  . GLU B 1 211 ? -17.316 26.242 56.975 1.00 9.38  ? 211 GLU B CD  1 
ATOM   3435 O  OE1 . GLU B 1 211 ? -16.998 26.912 57.972 1.00 10.57 ? 211 GLU B OE1 1 
ATOM   3436 O  OE2 . GLU B 1 211 ? -17.088 25.021 56.880 1.00 10.41 ? 211 GLU B OE2 1 
ATOM   3437 N  N   . LYS B 1 212 ? -19.708 31.215 55.861 1.00 9.08  ? 212 LYS B N   1 
ATOM   3438 C  CA  . LYS B 1 212 ? -20.435 32.358 56.398 1.00 10.34 ? 212 LYS B CA  1 
ATOM   3439 C  C   . LYS B 1 212 ? -21.535 32.842 55.449 1.00 11.31 ? 212 LYS B C   1 
ATOM   3440 O  O   . LYS B 1 212 ? -22.591 33.308 55.887 1.00 11.57 ? 212 LYS B O   1 
ATOM   3441 C  CB  . LYS B 1 212 ? -19.463 33.509 56.671 1.00 11.93 ? 212 LYS B CB  1 
ATOM   3442 C  CG  . LYS B 1 212 ? -18.521 33.260 57.834 1.00 15.31 ? 212 LYS B CG  1 
ATOM   3443 C  CD  . LYS B 1 212 ? -19.288 33.135 59.137 1.00 18.10 ? 212 LYS B CD  1 
ATOM   3444 C  CE  . LYS B 1 212 ? -18.498 32.346 60.163 1.00 21.10 ? 212 LYS B CE  1 
ATOM   3445 N  NZ  . LYS B 1 212 ? -17.152 32.935 60.367 1.00 24.24 ? 212 LYS B NZ  1 
ATOM   3446 N  N   . ARG B 1 213 ? -21.291 32.722 54.148 1.00 11.06 ? 213 ARG B N   1 
ATOM   3447 C  CA  . ARG B 1 213 ? -22.256 33.181 53.158 1.00 11.18 ? 213 ARG B CA  1 
ATOM   3448 C  C   . ARG B 1 213 ? -23.283 32.139 52.727 1.00 11.95 ? 213 ARG B C   1 
ATOM   3449 O  O   . ARG B 1 213 ? -24.281 32.482 52.101 1.00 13.02 ? 213 ARG B O   1 
ATOM   3450 C  CB  . ARG B 1 213 ? -21.512 33.717 51.931 1.00 8.87  ? 213 ARG B CB  1 
ATOM   3451 C  CG  . ARG B 1 213 ? -20.735 35.003 52.204 1.00 8.44  ? 213 ARG B CG  1 
ATOM   3452 C  CD  . ARG B 1 213 ? -19.776 35.333 51.076 1.00 9.96  ? 213 ARG B CD  1 
ATOM   3453 N  NE  . ARG B 1 213 ? -20.472 35.916 49.933 1.00 8.66  ? 213 ARG B NE  1 
ATOM   3454 C  CZ  . ARG B 1 213 ? -19.862 36.400 48.859 1.00 9.63  ? 213 ARG B CZ  1 
ATOM   3455 N  NH1 . ARG B 1 213 ? -18.542 36.372 48.778 1.00 9.75  ? 213 ARG B NH1 1 
ATOM   3456 N  NH2 . ARG B 1 213 ? -20.570 36.917 47.868 1.00 10.19 ? 213 ARG B NH2 1 
ATOM   3457 N  N   . THR B 1 214 ? -23.047 30.873 53.065 1.00 11.17 ? 214 THR B N   1 
ATOM   3458 C  CA  . THR B 1 214 ? -23.967 29.801 52.684 1.00 10.63 ? 214 THR B CA  1 
ATOM   3459 C  C   . THR B 1 214 ? -24.714 29.157 53.851 1.00 10.89 ? 214 THR B C   1 
ATOM   3460 O  O   . THR B 1 214 ? -25.775 28.570 53.654 1.00 11.79 ? 214 THR B O   1 
ATOM   3461 C  CB  . THR B 1 214 ? -23.235 28.668 51.942 1.00 8.12  ? 214 THR B CB  1 
ATOM   3462 O  OG1 . THR B 1 214 ? -22.272 28.078 52.819 1.00 7.04  ? 214 THR B OG1 1 
ATOM   3463 C  CG2 . THR B 1 214 ? -22.539 29.195 50.706 1.00 7.88  ? 214 THR B CG2 1 
ATOM   3464 N  N   . GLY B 1 215 ? -24.157 29.248 55.055 1.00 10.63 ? 215 GLY B N   1 
ATOM   3465 C  CA  . GLY B 1 215 ? -24.804 28.648 56.210 1.00 8.30  ? 215 GLY B CA  1 
ATOM   3466 C  C   . GLY B 1 215 ? -24.430 27.184 56.360 1.00 10.18 ? 215 GLY B C   1 
ATOM   3467 O  O   . GLY B 1 215 ? -24.939 26.484 57.238 1.00 11.17 ? 215 GLY B O   1 
ATOM   3468 N  N   . LEU B 1 216 ? -23.528 26.721 55.502 1.00 9.12  ? 216 LEU B N   1 
ATOM   3469 C  CA  . LEU B 1 216 ? -23.080 25.334 55.533 1.00 9.18  ? 216 LEU B CA  1 
ATOM   3470 C  C   . LEU B 1 216 ? -21.761 25.177 56.275 1.00 9.38  ? 216 LEU B C   1 
ATOM   3471 O  O   . LEU B 1 216 ? -21.049 26.147 56.516 1.00 11.06 ? 216 LEU B O   1 
ATOM   3472 C  CB  . LEU B 1 216 ? -22.869 24.812 54.110 1.00 10.30 ? 216 LEU B CB  1 
ATOM   3473 C  CG  . LEU B 1 216 ? -24.005 24.865 53.094 1.00 11.26 ? 216 LEU B CG  1 
ATOM   3474 C  CD1 . LEU B 1 216 ? -23.439 24.590 51.706 1.00 11.32 ? 216 LEU B CD1 1 
ATOM   3475 C  CD2 . LEU B 1 216 ? -25.071 23.846 53.456 1.00 10.41 ? 216 LEU B CD2 1 
ATOM   3476 N  N   . ILE B 1 217 ? -21.445 23.940 56.634 1.00 9.07  ? 217 ILE B N   1 
ATOM   3477 C  CA  . ILE B 1 217 ? -20.175 23.637 57.273 1.00 9.30  ? 217 ILE B CA  1 
ATOM   3478 C  C   . ILE B 1 217 ? -19.548 22.594 56.356 1.00 9.07  ? 217 ILE B C   1 
ATOM   3479 O  O   . ILE B 1 217 ? -20.036 21.471 56.261 1.00 10.32 ? 217 ILE B O   1 
ATOM   3480 C  CB  . ILE B 1 217 ? -20.350 23.049 58.685 1.00 9.45  ? 217 ILE B CB  1 
ATOM   3481 C  CG1 . ILE B 1 217 ? -20.813 24.145 59.649 1.00 9.92  ? 217 ILE B CG1 1 
ATOM   3482 C  CG2 . ILE B 1 217 ? -19.022 22.485 59.179 1.00 8.34  ? 217 ILE B CG2 1 
ATOM   3483 C  CD1 . ILE B 1 217 ? -21.063 23.646 61.057 1.00 16.67 ? 217 ILE B CD1 1 
ATOM   3484 N  N   . ILE B 1 218 ? -18.487 22.986 55.658 1.00 8.70  ? 218 ILE B N   1 
ATOM   3485 C  CA  . ILE B 1 218 ? -17.788 22.096 54.733 1.00 9.13  ? 218 ILE B CA  1 
ATOM   3486 C  C   . ILE B 1 218 ? -16.799 21.231 55.511 1.00 8.32  ? 218 ILE B C   1 
ATOM   3487 O  O   . ILE B 1 218 ? -16.319 21.640 56.569 1.00 9.25  ? 218 ILE B O   1 
ATOM   3488 C  CB  . ILE B 1 218 ? -17.016 22.920 53.663 1.00 11.28 ? 218 ILE B CB  1 
ATOM   3489 C  CG1 . ILE B 1 218 ? -17.939 23.983 53.061 1.00 14.02 ? 218 ILE B CG1 1 
ATOM   3490 C  CG2 . ILE B 1 218 ? -16.473 22.009 52.576 1.00 10.73 ? 218 ILE B CG2 1 
ATOM   3491 C  CD1 . ILE B 1 218 ? -19.174 23.424 52.409 1.00 13.95 ? 218 ILE B CD1 1 
ATOM   3492 N  N   . TRP B 1 219 ? -16.494 20.044 54.989 1.00 8.12  ? 219 TRP B N   1 
ATOM   3493 C  CA  . TRP B 1 219 ? -15.554 19.132 55.649 1.00 9.84  ? 219 TRP B CA  1 
ATOM   3494 C  C   . TRP B 1 219 ? -15.970 18.983 57.108 1.00 10.25 ? 219 TRP B C   1 
ATOM   3495 O  O   . TRP B 1 219 ? -15.141 19.070 58.011 1.00 10.19 ? 219 TRP B O   1 
ATOM   3496 C  CB  . TRP B 1 219 ? -14.131 19.700 55.599 1.00 9.48  ? 219 TRP B CB  1 
ATOM   3497 C  CG  . TRP B 1 219 ? -13.626 20.078 54.225 1.00 9.76  ? 219 TRP B CG  1 
ATOM   3498 C  CD1 . TRP B 1 219 ? -14.010 19.546 53.026 1.00 9.08  ? 219 TRP B CD1 1 
ATOM   3499 C  CD2 . TRP B 1 219 ? -12.582 21.019 53.930 1.00 9.71  ? 219 TRP B CD2 1 
ATOM   3500 N  NE1 . TRP B 1 219 ? -13.265 20.092 52.002 1.00 9.57  ? 219 TRP B NE1 1 
ATOM   3501 C  CE2 . TRP B 1 219 ? -12.381 20.997 52.529 1.00 9.97  ? 219 TRP B CE2 1 
ATOM   3502 C  CE3 . TRP B 1 219 ? -11.795 21.876 54.715 1.00 10.75 ? 219 TRP B CE3 1 
ATOM   3503 C  CZ2 . TRP B 1 219 ? -11.422 21.800 51.895 1.00 9.63  ? 219 TRP B CZ2 1 
ATOM   3504 C  CZ3 . TRP B 1 219 ? -10.837 22.679 54.082 1.00 11.12 ? 219 TRP B CZ3 1 
ATOM   3505 C  CH2 . TRP B 1 219 ? -10.662 22.631 52.684 1.00 10.37 ? 219 TRP B CH2 1 
ATOM   3506 N  N   . ALA B 1 220 ? -17.259 18.748 57.323 1.00 11.74 ? 220 ALA B N   1 
ATOM   3507 C  CA  . ALA B 1 220 ? -17.833 18.638 58.661 1.00 11.40 ? 220 ALA B CA  1 
ATOM   3508 C  C   . ALA B 1 220 ? -17.359 17.500 59.562 1.00 12.11 ? 220 ALA B C   1 
ATOM   3509 O  O   . ALA B 1 220 ? -17.754 17.439 60.725 1.00 12.76 ? 220 ALA B O   1 
ATOM   3510 C  CB  . ALA B 1 220 ? -19.351 18.603 58.550 1.00 10.64 ? 220 ALA B CB  1 
ATOM   3511 N  N   . GLY B 1 221 ? -16.526 16.602 59.043 1.00 10.12 ? 221 GLY B N   1 
ATOM   3512 C  CA  . GLY B 1 221 ? -16.046 15.498 59.859 1.00 9.97  ? 221 GLY B CA  1 
ATOM   3513 C  C   . GLY B 1 221 ? -14.638 15.705 60.397 1.00 11.00 ? 221 GLY B C   1 
ATOM   3514 O  O   . GLY B 1 221 ? -14.115 14.865 61.123 1.00 11.13 ? 221 GLY B O   1 
ATOM   3515 N  N   . LEU B 1 222 ? -14.021 16.827 60.044 1.00 10.89 ? 222 LEU B N   1 
ATOM   3516 C  CA  . LEU B 1 222 ? -12.664 17.127 60.494 1.00 11.70 ? 222 LEU B CA  1 
ATOM   3517 C  C   . LEU B 1 222 ? -12.617 17.522 61.971 1.00 11.89 ? 222 LEU B C   1 
ATOM   3518 O  O   . LEU B 1 222 ? -13.568 18.105 62.500 1.00 10.99 ? 222 LEU B O   1 
ATOM   3519 C  CB  . LEU B 1 222 ? -12.077 18.281 59.675 1.00 11.14 ? 222 LEU B CB  1 
ATOM   3520 C  CG  . LEU B 1 222 ? -11.679 18.070 58.214 1.00 11.88 ? 222 LEU B CG  1 
ATOM   3521 C  CD1 . LEU B 1 222 ? -11.178 19.396 57.654 1.00 11.89 ? 222 LEU B CD1 1 
ATOM   3522 C  CD2 . LEU B 1 222 ? -10.609 16.993 58.103 1.00 10.57 ? 222 LEU B CD2 1 
ATOM   3523 N  N   . PRO B 1 223 ? -11.510 17.191 62.660 1.00 12.04 ? 223 PRO B N   1 
ATOM   3524 C  CA  . PRO B 1 223 ? -11.391 17.554 64.077 1.00 12.51 ? 223 PRO B CA  1 
ATOM   3525 C  C   . PRO B 1 223 ? -11.531 19.073 64.199 1.00 11.93 ? 223 PRO B C   1 
ATOM   3526 O  O   . PRO B 1 223 ? -11.168 19.807 63.280 1.00 11.63 ? 223 PRO B O   1 
ATOM   3527 C  CB  . PRO B 1 223 ? -9.991  17.071 64.458 1.00 10.58 ? 223 PRO B CB  1 
ATOM   3528 C  CG  . PRO B 1 223 ? -9.689  15.993 63.465 1.00 10.91 ? 223 PRO B CG  1 
ATOM   3529 C  CD  . PRO B 1 223 ? -10.337 16.438 62.185 1.00 10.82 ? 223 PRO B CD  1 
ATOM   3530 N  N   . ASP B 1 224 ? -12.056 19.535 65.328 1.00 12.20 ? 224 ASP B N   1 
ATOM   3531 C  CA  . ASP B 1 224 ? -12.272 20.960 65.563 1.00 11.51 ? 224 ASP B CA  1 
ATOM   3532 C  C   . ASP B 1 224 ? -11.052 21.853 65.343 1.00 13.22 ? 224 ASP B C   1 
ATOM   3533 O  O   . ASP B 1 224 ? -11.149 22.899 64.698 1.00 12.48 ? 224 ASP B O   1 
ATOM   3534 C  CB  . ASP B 1 224 ? -12.791 21.178 66.982 1.00 12.35 ? 224 ASP B CB  1 
ATOM   3535 C  CG  . ASP B 1 224 ? -14.254 20.826 67.128 1.00 14.79 ? 224 ASP B CG  1 
ATOM   3536 O  OD1 . ASP B 1 224 ? -14.888 20.450 66.120 1.00 13.79 ? 224 ASP B OD1 1 
ATOM   3537 O  OD2 . ASP B 1 224 ? -14.771 20.926 68.258 1.00 15.37 ? 224 ASP B OD2 1 
ATOM   3538 N  N   . ASP B 1 225 ? -9.906  21.454 65.886 1.00 13.61 ? 225 ASP B N   1 
ATOM   3539 C  CA  . ASP B 1 225 ? -8.701  22.266 65.743 1.00 15.10 ? 225 ASP B CA  1 
ATOM   3540 C  C   . ASP B 1 225 ? -8.293  22.439 64.281 1.00 13.74 ? 225 ASP B C   1 
ATOM   3541 O  O   . ASP B 1 225 ? -7.850  23.513 63.879 1.00 14.11 ? 225 ASP B O   1 
ATOM   3542 C  CB  . ASP B 1 225 ? -7.548  21.655 66.547 1.00 16.92 ? 225 ASP B CB  1 
ATOM   3543 C  CG  . ASP B 1 225 ? -7.158  20.280 66.057 1.00 21.92 ? 225 ASP B CG  1 
ATOM   3544 O  OD1 . ASP B 1 225 ? -8.053  19.433 65.861 1.00 30.21 ? 225 ASP B OD1 1 
ATOM   3545 O  OD2 . ASP B 1 225 ? -5.950  20.041 65.867 1.00 30.70 ? 225 ASP B OD2 1 
ATOM   3546 N  N   . VAL B 1 226 ? -8.454  21.382 63.490 1.00 14.12 ? 226 VAL B N   1 
ATOM   3547 C  CA  . VAL B 1 226 ? -8.103  21.423 62.075 1.00 13.56 ? 226 VAL B CA  1 
ATOM   3548 C  C   . VAL B 1 226 ? -9.014  22.388 61.333 1.00 13.25 ? 226 VAL B C   1 
ATOM   3549 O  O   . VAL B 1 226 ? -8.563  23.152 60.480 1.00 13.77 ? 226 VAL B O   1 
ATOM   3550 C  CB  . VAL B 1 226 ? -8.226  20.024 61.433 1.00 13.21 ? 226 VAL B CB  1 
ATOM   3551 C  CG1 . VAL B 1 226 ? -8.060  20.120 59.923 1.00 12.94 ? 226 VAL B CG1 1 
ATOM   3552 C  CG2 . VAL B 1 226 ? -7.179  19.100 62.021 1.00 13.09 ? 226 VAL B CG2 1 
ATOM   3553 N  N   . GLN B 1 227 ? -10.300 22.349 61.665 1.00 12.31 ? 227 GLN B N   1 
ATOM   3554 C  CA  . GLN B 1 227 ? -11.276 23.224 61.031 1.00 12.42 ? 227 GLN B CA  1 
ATOM   3555 C  C   . GLN B 1 227 ? -10.979 24.686 61.339 1.00 13.14 ? 227 GLN B C   1 
ATOM   3556 O  O   . GLN B 1 227 ? -10.890 25.517 60.436 1.00 15.56 ? 227 GLN B O   1 
ATOM   3557 C  CB  . GLN B 1 227 ? -12.684 22.874 61.514 1.00 11.63 ? 227 GLN B CB  1 
ATOM   3558 C  CG  . GLN B 1 227 ? -13.215 21.566 60.952 1.00 11.90 ? 227 GLN B CG  1 
ATOM   3559 C  CD  . GLN B 1 227 ? -14.707 21.402 61.169 1.00 13.14 ? 227 GLN B CD  1 
ATOM   3560 O  OE1 . GLN B 1 227 ? -15.175 20.341 61.584 1.00 14.04 ? 227 GLN B OE1 1 
ATOM   3561 N  NE2 . GLN B 1 227 ? -15.464 22.454 60.888 1.00 11.27 ? 227 GLN B NE2 1 
ATOM   3562 N  N   . ALA B 1 228 ? -10.818 24.996 62.618 1.00 12.96 ? 228 ALA B N   1 
ATOM   3563 C  CA  . ALA B 1 228 ? -10.546 26.363 63.030 1.00 14.98 ? 228 ALA B CA  1 
ATOM   3564 C  C   . ALA B 1 228 ? -9.265  26.889 62.399 1.00 16.78 ? 228 ALA B C   1 
ATOM   3565 O  O   . ALA B 1 228 ? -9.198  28.041 61.974 1.00 20.46 ? 228 ALA B O   1 
ATOM   3566 C  CB  . ALA B 1 228 ? -10.446 26.437 64.546 1.00 14.81 ? 228 ALA B CB  1 
ATOM   3567 N  N   . SER B 1 229 ? -8.256  26.032 62.321 1.00 15.85 ? 229 SER B N   1 
ATOM   3568 C  CA  . SER B 1 229 ? -6.964  26.416 61.774 1.00 17.32 ? 229 SER B CA  1 
ATOM   3569 C  C   . SER B 1 229 ? -6.885  26.664 60.276 1.00 16.77 ? 229 SER B C   1 
ATOM   3570 O  O   . SER B 1 229 ? -6.375  27.694 59.842 1.00 19.36 ? 229 SER B O   1 
ATOM   3571 C  CB  . SER B 1 229 ? -5.922  25.365 62.144 1.00 19.61 ? 229 SER B CB  1 
ATOM   3572 O  OG  . SER B 1 229 ? -5.123  25.821 63.215 1.00 26.86 ? 229 SER B OG  1 
ATOM   3573 N  N   . LEU B 1 230 ? -7.394  25.730 59.484 1.00 13.51 ? 230 LEU B N   1 
ATOM   3574 C  CA  . LEU B 1 230 ? -7.297  25.848 58.035 1.00 12.19 ? 230 LEU B CA  1 
ATOM   3575 C  C   . LEU B 1 230 ? -8.402  26.560 57.267 1.00 12.49 ? 230 LEU B C   1 
ATOM   3576 O  O   . LEU B 1 230 ? -8.152  27.095 56.192 1.00 12.02 ? 230 LEU B O   1 
ATOM   3577 C  CB  . LEU B 1 230 ? -7.099  24.456 57.435 1.00 12.71 ? 230 LEU B CB  1 
ATOM   3578 C  CG  . LEU B 1 230 ? -5.938  23.651 58.028 1.00 12.98 ? 230 LEU B CG  1 
ATOM   3579 C  CD1 . LEU B 1 230 ? -5.857  22.295 57.361 1.00 14.17 ? 230 LEU B CD1 1 
ATOM   3580 C  CD2 . LEU B 1 230 ? -4.640  24.418 57.839 1.00 13.13 ? 230 LEU B CD2 1 
ATOM   3581 N  N   . LYS B 1 231 ? -9.617  26.579 57.799 1.00 12.07 ? 231 LYS B N   1 
ATOM   3582 C  CA  . LYS B 1 231 ? -10.717 27.207 57.082 1.00 12.00 ? 231 LYS B CA  1 
ATOM   3583 C  C   . LYS B 1 231 ? -10.559 28.706 56.872 1.00 12.24 ? 231 LYS B C   1 
ATOM   3584 O  O   . LYS B 1 231 ? -11.221 29.290 56.011 1.00 12.56 ? 231 LYS B O   1 
ATOM   3585 C  CB  . LYS B 1 231 ? -12.041 26.891 57.782 1.00 6.94  ? 231 LYS B CB  1 
ATOM   3586 C  CG  . LYS B 1 231 ? -12.383 25.407 57.716 1.00 7.22  ? 231 LYS B CG  1 
ATOM   3587 C  CD  . LYS B 1 231 ? -13.869 25.158 57.785 1.00 8.23  ? 231 LYS B CD  1 
ATOM   3588 C  CE  . LYS B 1 231 ? -14.168 23.672 57.806 1.00 6.76  ? 231 LYS B CE  1 
ATOM   3589 N  NZ  . LYS B 1 231 ? -15.535 23.406 58.338 1.00 6.32  ? 231 LYS B NZ  1 
ATOM   3590 N  N   . SER B 1 232 ? -9.674  29.330 57.641 1.00 12.04 ? 232 SER B N   1 
ATOM   3591 C  CA  . SER B 1 232 ? -9.450  30.765 57.502 1.00 12.62 ? 232 SER B CA  1 
ATOM   3592 C  C   . SER B 1 232 ? -8.151  31.079 56.768 1.00 12.29 ? 232 SER B C   1 
ATOM   3593 O  O   . SER B 1 232 ? -7.753  32.235 56.666 1.00 13.41 ? 232 SER B O   1 
ATOM   3594 C  CB  . SER B 1 232 ? -9.439  31.429 58.873 1.00 15.37 ? 232 SER B CB  1 
ATOM   3595 O  OG  . SER B 1 232 ? -10.767 31.641 59.321 1.00 21.97 ? 232 SER B OG  1 
ATOM   3596 N  N   . LYS B 1 233 ? -7.501  30.043 56.252 1.00 11.36 ? 233 LYS B N   1 
ATOM   3597 C  CA  . LYS B 1 233 ? -6.245  30.207 55.532 1.00 11.13 ? 233 LYS B CA  1 
ATOM   3598 C  C   . LYS B 1 233 ? -6.391  29.755 54.084 1.00 11.22 ? 233 LYS B C   1 
ATOM   3599 O  O   . LYS B 1 233 ? -6.695  28.593 53.817 1.00 11.13 ? 233 LYS B O   1 
ATOM   3600 C  CB  . LYS B 1 233 ? -5.143  29.384 56.211 1.00 11.63 ? 233 LYS B CB  1 
ATOM   3601 C  CG  . LYS B 1 233 ? -3.727  29.746 55.782 1.00 12.62 ? 233 LYS B CG  1 
ATOM   3602 C  CD  . LYS B 1 233 ? -3.439  31.223 56.024 1.00 16.42 ? 233 LYS B CD  1 
ATOM   3603 C  CE  . LYS B 1 233 ? -1.989  31.568 55.725 1.00 20.29 ? 233 LYS B CE  1 
ATOM   3604 N  NZ  . LYS B 1 233 ? -1.417  30.683 54.680 1.00 23.70 ? 233 LYS B NZ  1 
ATOM   3605 N  N   . PRO B 1 234 ? -6.196  30.675 53.129 1.00 11.82 ? 234 PRO B N   1 
ATOM   3606 C  CA  . PRO B 1 234 ? -6.321  30.275 51.723 1.00 12.07 ? 234 PRO B CA  1 
ATOM   3607 C  C   . PRO B 1 234 ? -5.279  29.195 51.440 1.00 10.78 ? 234 PRO B C   1 
ATOM   3608 O  O   . PRO B 1 234 ? -4.152  29.276 51.929 1.00 12.04 ? 234 PRO B O   1 
ATOM   3609 C  CB  . PRO B 1 234 ? -6.050  31.565 50.947 1.00 12.90 ? 234 PRO B CB  1 
ATOM   3610 C  CG  . PRO B 1 234 ? -6.270  32.671 51.945 1.00 14.26 ? 234 PRO B CG  1 
ATOM   3611 C  CD  . PRO B 1 234 ? -5.870  32.104 53.274 1.00 13.43 ? 234 PRO B CD  1 
ATOM   3612 N  N   . GLY B 1 235 ? -5.661  28.186 50.666 1.00 7.84  ? 235 GLY B N   1 
ATOM   3613 C  CA  . GLY B 1 235 ? -4.748  27.098 50.363 1.00 8.97  ? 235 GLY B CA  1 
ATOM   3614 C  C   . GLY B 1 235 ? -3.751  27.382 49.255 1.00 9.86  ? 235 GLY B C   1 
ATOM   3615 O  O   . GLY B 1 235 ? -3.817  28.419 48.597 1.00 10.95 ? 235 GLY B O   1 
ATOM   3616 N  N   . VAL B 1 236 ? -2.827  26.451 49.040 1.00 9.87  ? 236 VAL B N   1 
ATOM   3617 C  CA  . VAL B 1 236 ? -1.820  26.624 48.003 1.00 10.52 ? 236 VAL B CA  1 
ATOM   3618 C  C   . VAL B 1 236 ? -2.028  25.716 46.797 1.00 10.27 ? 236 VAL B C   1 
ATOM   3619 O  O   . VAL B 1 236 ? -1.197  25.690 45.891 1.00 10.92 ? 236 VAL B O   1 
ATOM   3620 C  CB  . VAL B 1 236 ? -0.400  26.392 48.562 1.00 10.87 ? 236 VAL B CB  1 
ATOM   3621 C  CG1 . VAL B 1 236 ? -0.196  27.241 49.808 1.00 11.91 ? 236 VAL B CG1 1 
ATOM   3622 C  CG2 . VAL B 1 236 ? -0.189  24.925 48.865 1.00 9.48  ? 236 VAL B CG2 1 
ATOM   3623 N  N   . LEU B 1 237 ? -3.130  24.972 46.781 1.00 9.59  ? 237 LEU B N   1 
ATOM   3624 C  CA  . LEU B 1 237 ? -3.414  24.088 45.653 1.00 9.67  ? 237 LEU B CA  1 
ATOM   3625 C  C   . LEU B 1 237 ? -3.472  24.851 44.317 1.00 9.48  ? 237 LEU B C   1 
ATOM   3626 O  O   . LEU B 1 237 ? -3.040  24.333 43.289 1.00 10.54 ? 237 LEU B O   1 
ATOM   3627 C  CB  . LEU B 1 237 ? -4.728  23.334 45.872 1.00 8.30  ? 237 LEU B CB  1 
ATOM   3628 C  CG  . LEU B 1 237 ? -5.072  22.312 44.779 1.00 9.74  ? 237 LEU B CG  1 
ATOM   3629 C  CD1 . LEU B 1 237 ? -4.009  21.200 44.748 1.00 10.40 ? 237 LEU B CD1 1 
ATOM   3630 C  CD2 . LEU B 1 237 ? -6.455  21.729 45.037 1.00 8.85  ? 237 LEU B CD2 1 
ATOM   3631 N  N   . PRO B 1 238 ? -4.019  26.082 44.310 1.00 8.37  ? 238 PRO B N   1 
ATOM   3632 C  CA  . PRO B 1 238 ? -4.076  26.824 43.041 1.00 9.32  ? 238 PRO B CA  1 
ATOM   3633 C  C   . PRO B 1 238 ? -2.709  27.019 42.370 1.00 9.81  ? 238 PRO B C   1 
ATOM   3634 O  O   . PRO B 1 238 ? -2.629  27.200 41.153 1.00 8.49  ? 238 PRO B O   1 
ATOM   3635 C  CB  . PRO B 1 238 ? -4.733  28.152 43.426 1.00 8.51  ? 238 PRO B CB  1 
ATOM   3636 C  CG  . PRO B 1 238 ? -5.511  27.834 44.679 1.00 7.56  ? 238 PRO B CG  1 
ATOM   3637 C  CD  . PRO B 1 238 ? -4.647  26.839 45.408 1.00 7.52  ? 238 PRO B CD  1 
ATOM   3638 N  N   . GLU B 1 239 ? -1.641  26.985 43.163 1.00 11.10 ? 239 GLU B N   1 
ATOM   3639 C  CA  . GLU B 1 239 ? -0.296  27.142 42.623 1.00 12.92 ? 239 GLU B CA  1 
ATOM   3640 C  C   . GLU B 1 239 ? 0.029   25.968 41.698 1.00 14.21 ? 239 GLU B C   1 
ATOM   3641 O  O   . GLU B 1 239 ? 0.804   26.102 40.749 1.00 14.90 ? 239 GLU B O   1 
ATOM   3642 C  CB  . GLU B 1 239 ? 0.727   27.214 43.756 1.00 13.91 ? 239 GLU B CB  1 
ATOM   3643 C  CG  . GLU B 1 239 ? 1.299   28.604 43.969 1.00 16.09 ? 239 GLU B CG  1 
ATOM   3644 C  CD  . GLU B 1 239 ? 0.247   29.602 44.411 1.00 20.66 ? 239 GLU B CD  1 
ATOM   3645 O  OE1 . GLU B 1 239 ? -0.725  29.186 45.078 1.00 21.09 ? 239 GLU B OE1 1 
ATOM   3646 O  OE2 . GLU B 1 239 ? 0.392   30.802 44.093 1.00 23.22 ? 239 GLU B OE2 1 
ATOM   3647 N  N   . LEU B 1 240 ? -0.569  24.814 41.976 1.00 13.38 ? 240 LEU B N   1 
ATOM   3648 C  CA  . LEU B 1 240 ? -0.353  23.640 41.144 1.00 14.73 ? 240 LEU B CA  1 
ATOM   3649 C  C   . LEU B 1 240 ? -1.286  23.700 39.937 1.00 16.16 ? 240 LEU B C   1 
ATOM   3650 O  O   . LEU B 1 240 ? -1.210  22.863 39.041 1.00 16.92 ? 240 LEU B O   1 
ATOM   3651 C  CB  . LEU B 1 240 ? -0.632  22.364 41.937 1.00 15.62 ? 240 LEU B CB  1 
ATOM   3652 C  CG  . LEU B 1 240 ? 0.438   21.920 42.933 1.00 17.69 ? 240 LEU B CG  1 
ATOM   3653 C  CD1 . LEU B 1 240 ? 0.120   20.510 43.406 1.00 17.59 ? 240 LEU B CD1 1 
ATOM   3654 C  CD2 . LEU B 1 240 ? 1.818   21.972 42.278 1.00 19.04 ? 240 LEU B CD2 1 
ATOM   3655 N  N   . MET B 1 241 ? -2.167  24.696 39.925 1.00 15.62 ? 241 MET B N   1 
ATOM   3656 C  CA  . MET B 1 241 ? -3.119  24.867 38.835 1.00 17.72 ? 241 MET B CA  1 
ATOM   3657 C  C   . MET B 1 241 ? -2.734  26.040 37.934 1.00 18.49 ? 241 MET B C   1 
ATOM   3658 O  O   . MET B 1 241 ? -3.534  26.495 37.114 1.00 19.20 ? 241 MET B O   1 
ATOM   3659 C  CB  . MET B 1 241 ? -4.529  25.085 39.394 1.00 18.23 ? 241 MET B CB  1 
ATOM   3660 C  CG  . MET B 1 241 ? -5.018  23.977 40.316 1.00 18.68 ? 241 MET B CG  1 
ATOM   3661 S  SD  . MET B 1 241 ? -6.605  24.380 41.102 1.00 23.01 ? 241 MET B SD  1 
ATOM   3662 C  CE  . MET B 1 241 ? -7.738  23.448 40.080 1.00 22.40 ? 241 MET B CE  1 
ATOM   3663 N  N   . GLY B 1 242 ? -1.512  26.537 38.103 1.00 20.12 ? 242 GLY B N   1 
ATOM   3664 C  CA  . GLY B 1 242 ? -1.040  27.632 37.275 1.00 20.94 ? 242 GLY B CA  1 
ATOM   3665 C  C   . GLY B 1 242 ? -1.186  29.040 37.819 1.00 22.08 ? 242 GLY B C   1 
ATOM   3666 O  O   . GLY B 1 242 ? -0.914  30.004 37.103 1.00 24.46 ? 242 GLY B O   1 
ATOM   3667 N  N   . CYS B 1 243 ? -1.610  29.180 39.070 1.00 19.44 ? 243 CYS B N   1 
ATOM   3668 C  CA  . CYS B 1 243 ? -1.765  30.508 39.656 1.00 18.78 ? 243 CYS B CA  1 
ATOM   3669 C  C   . CYS B 1 243 ? -0.462  30.959 40.305 1.00 20.89 ? 243 CYS B C   1 
ATOM   3670 O  O   . CYS B 1 243 ? 0.330   30.135 40.765 1.00 20.95 ? 243 CYS B O   1 
ATOM   3671 C  CB  . CYS B 1 243 ? -2.887  30.505 40.697 1.00 16.38 ? 243 CYS B CB  1 
ATOM   3672 S  SG  . CYS B 1 243 ? -4.506  30.005 40.032 1.00 14.63 ? 243 CYS B SG  1 
ATOM   3673 N  N   . LYS B 1 244 ? -0.243  32.269 40.335 1.00 25.09 ? 244 LYS B N   1 
ATOM   3674 C  CA  . LYS B 1 244 ? 0.963   32.831 40.934 1.00 29.50 ? 244 LYS B CA  1 
ATOM   3675 C  C   . LYS B 1 244 ? 0.606   33.678 42.150 1.00 33.10 ? 244 LYS B C   1 
ATOM   3676 O  O   . LYS B 1 244 ? -0.427  34.351 42.170 1.00 33.27 ? 244 LYS B O   1 
ATOM   3677 C  CB  . LYS B 1 244 ? 1.715   33.687 39.914 1.00 35.22 ? 244 LYS B CB  1 
ATOM   3678 C  CG  . LYS B 1 244 ? 1.720   33.113 38.509 1.00 37.36 ? 244 LYS B CG  1 
ATOM   3679 C  CD  . LYS B 1 244 ? 2.850   32.113 38.323 1.00 38.96 ? 244 LYS B CD  1 
ATOM   3680 C  CE  . LYS B 1 244 ? 2.945   31.652 36.873 1.00 40.35 ? 244 LYS B CE  1 
ATOM   3681 N  NZ  . LYS B 1 244 ? 4.357   31.396 36.465 1.00 41.27 ? 244 LYS B NZ  1 
ATOM   3682 N  N   . ASN B 1 245 ? 1.467   33.634 43.163 1.00 39.60 ? 245 ASN B N   1 
ATOM   3683 C  CA  . ASN B 1 245 ? 1.253   34.388 44.396 1.00 40.53 ? 245 ASN B CA  1 
ATOM   3684 C  C   . ASN B 1 245 ? -0.171  34.185 44.922 1.00 40.56 ? 245 ASN B C   1 
ATOM   3685 O  O   . ASN B 1 245 ? -0.947  35.166 44.946 1.00 40.90 ? 245 ASN B O   1 
ATOM   3686 C  CB  . ASN B 1 245 ? 1.521   35.880 44.154 1.00 39.87 ? 245 ASN B CB  1 
ATOM   3687 C  CG  . ASN B 1 245 ? 2.998   36.183 43.933 1.00 41.22 ? 245 ASN B CG  1 
ATOM   3688 O  OD1 . ASN B 1 245 ? 3.658   35.555 43.100 1.00 42.36 ? 245 ASN B OD1 1 
ATOM   3689 N  ND2 . ASN B 1 245 ? 3.523   37.151 44.682 1.00 41.18 ? 245 ASN B ND2 1 
ATOM   3690 O  OXT . ASN B 1 245 ? -0.495  33.038 45.300 1.00 38.59 ? 245 ASN B OXT 1 
HETATM 3691 MG MG  . MG  C 2 .   ? 18.807  24.309 70.653 1.00 16.85 ? 251 MG  A MG  1 
HETATM 3692 MG MG  . MG  D 2 .   ? -20.339 24.215 32.819 1.00 17.72 ? 251 MG  B MG  1 
HETATM 3693 O  O   . HOH E 3 .   ? 20.616  23.309 71.521 1.00 18.25 ? 252 HOH A O   1 
HETATM 3694 O  O   . HOH E 3 .   ? 19.529  24.996 68.656 1.00 14.99 ? 253 HOH A O   1 
HETATM 3695 O  O   . HOH E 3 .   ? 16.776  25.195 70.619 1.00 12.07 ? 254 HOH A O   1 
HETATM 3696 O  O   . HOH E 3 .   ? 18.068  23.897 72.781 1.00 16.12 ? 255 HOH A O   1 
HETATM 3697 O  O   . HOH E 3 .   ? 18.095  22.463 69.777 1.00 12.86 ? 256 HOH A O   1 
HETATM 3698 O  O   . HOH E 3 .   ? 1.490   24.222 52.323 1.00 6.33  ? 257 HOH A O   1 
HETATM 3699 O  O   . HOH E 3 .   ? 20.196  25.627 64.788 1.00 5.44  ? 258 HOH A O   1 
HETATM 3700 O  O   . HOH E 3 .   ? 31.779  22.518 64.257 1.00 5.83  ? 259 HOH A O   1 
HETATM 3701 O  O   . HOH E 3 .   ? 20.037  25.102 62.142 1.00 6.94  ? 260 HOH A O   1 
HETATM 3702 O  O   . HOH E 3 .   ? 15.827  18.567 50.659 1.00 7.71  ? 261 HOH A O   1 
HETATM 3703 O  O   . HOH E 3 .   ? 14.513  16.255 55.231 1.00 8.17  ? 262 HOH A O   1 
HETATM 3704 O  O   . HOH E 3 .   ? 16.330  22.641 65.417 1.00 7.67  ? 263 HOH A O   1 
HETATM 3705 O  O   . HOH E 3 .   ? 13.507  25.640 65.333 1.00 8.64  ? 264 HOH A O   1 
HETATM 3706 O  O   . HOH E 3 .   ? 11.800  19.751 54.419 1.00 8.69  ? 265 HOH A O   1 
HETATM 3707 O  O   . HOH E 3 .   ? 31.528  20.970 61.460 1.00 9.18  ? 266 HOH A O   1 
HETATM 3708 O  O   . HOH E 3 .   ? 27.145  22.741 62.455 1.00 8.90  ? 267 HOH A O   1 
HETATM 3709 O  O   . HOH E 3 .   ? 30.320  23.588 66.441 1.00 9.61  ? 268 HOH A O   1 
HETATM 3710 O  O   . HOH E 3 .   ? 19.888  10.778 53.582 1.00 10.39 ? 269 HOH A O   1 
HETATM 3711 O  O   . HOH E 3 .   ? 16.805  11.794 60.565 1.00 10.00 ? 270 HOH A O   1 
HETATM 3712 O  O   . HOH E 3 .   ? 32.961  18.279 65.321 1.00 10.29 ? 271 HOH A O   1 
HETATM 3713 O  O   . HOH E 3 .   ? 24.514  19.750 49.047 1.00 11.56 ? 272 HOH A O   1 
HETATM 3714 O  O   . HOH E 3 .   ? 11.745  19.568 66.809 1.00 11.75 ? 273 HOH A O   1 
HETATM 3715 O  O   . HOH E 3 .   ? 15.481  11.781 48.938 1.00 11.81 ? 274 HOH A O   1 
HETATM 3716 O  O   . HOH E 3 .   ? 25.888  25.605 75.635 1.00 11.88 ? 275 HOH A O   1 
HETATM 3717 O  O   . HOH E 3 .   ? 13.508  18.426 38.518 1.00 12.22 ? 276 HOH A O   1 
HETATM 3718 O  O   . HOH E 3 .   ? 35.426  29.903 72.397 1.00 11.78 ? 277 HOH A O   1 
HETATM 3719 O  O   . HOH E 3 .   ? 14.072  17.140 52.633 1.00 12.19 ? 278 HOH A O   1 
HETATM 3720 O  O   . HOH E 3 .   ? 28.417  26.105 56.856 1.00 12.79 ? 279 HOH A O   1 
HETATM 3721 O  O   . HOH E 3 .   ? 32.055  17.335 76.268 1.00 13.35 ? 280 HOH A O   1 
HETATM 3722 O  O   . HOH E 3 .   ? -0.473  12.296 53.013 1.00 13.39 ? 281 HOH A O   1 
HETATM 3723 O  O   . HOH E 3 .   ? 13.989  33.981 70.382 1.00 13.13 ? 282 HOH A O   1 
HETATM 3724 O  O   . HOH E 3 .   ? 16.704  20.397 41.445 1.00 13.22 ? 283 HOH A O   1 
HETATM 3725 O  O   . HOH E 3 .   ? 21.510  37.295 57.993 1.00 12.85 ? 284 HOH A O   1 
HETATM 3726 O  O   . HOH E 3 .   ? 7.688   28.295 49.977 1.00 14.01 ? 285 HOH A O   1 
HETATM 3727 O  O   . HOH E 3 .   ? 23.020  25.815 65.574 1.00 13.87 ? 286 HOH A O   1 
HETATM 3728 O  O   . HOH E 3 .   ? 18.109  20.186 70.998 1.00 13.63 ? 287 HOH A O   1 
HETATM 3729 O  O   . HOH E 3 .   ? 29.894  16.671 54.569 1.00 14.91 ? 288 HOH A O   1 
HETATM 3730 O  O   . HOH E 3 .   ? 9.888   35.055 51.471 1.00 15.77 ? 289 HOH A O   1 
HETATM 3731 O  O   . HOH E 3 .   ? 19.005  36.541 70.090 1.00 15.63 ? 290 HOH A O   1 
HETATM 3732 O  O   . HOH E 3 .   ? 2.514   21.448 66.246 1.00 16.26 ? 291 HOH A O   1 
HETATM 3733 O  O   . HOH E 3 .   ? 32.471  22.396 74.400 1.00 16.16 ? 292 HOH A O   1 
HETATM 3734 O  O   . HOH E 3 .   ? 25.746  12.945 74.363 1.00 16.70 ? 293 HOH A O   1 
HETATM 3735 O  O   . HOH E 3 .   ? 15.953  22.477 37.053 1.00 17.28 ? 294 HOH A O   1 
HETATM 3736 O  O   . HOH E 3 .   ? 28.270  12.762 71.848 1.00 17.55 ? 295 HOH A O   1 
HETATM 3737 O  O   . HOH E 3 .   ? 27.895  35.358 59.145 1.00 17.09 ? 296 HOH A O   1 
HETATM 3738 O  O   . HOH E 3 .   ? 5.596   7.846  62.602 1.00 17.76 ? 297 HOH A O   1 
HETATM 3739 O  O   . HOH E 3 .   ? 10.839  18.124 35.774 1.00 18.30 ? 298 HOH A O   1 
HETATM 3740 O  O   . HOH E 3 .   ? 6.966   14.172 45.224 1.00 18.92 ? 299 HOH A O   1 
HETATM 3741 O  O   . HOH E 3 .   ? 30.974  28.672 76.226 1.00 19.74 ? 300 HOH A O   1 
HETATM 3742 O  O   . HOH E 3 .   ? 26.172  18.384 79.458 1.00 19.69 ? 301 HOH A O   1 
HETATM 3743 O  O   . HOH E 3 .   ? 23.554  27.073 54.464 1.00 20.55 ? 302 HOH A O   1 
HETATM 3744 O  O   . HOH E 3 .   ? 27.584  21.073 45.555 1.00 21.07 ? 303 HOH A O   1 
HETATM 3745 O  O   . HOH E 3 .   ? 3.957   30.318 55.898 1.00 20.23 ? 304 HOH A O   1 
HETATM 3746 O  O   . HOH E 3 .   ? 33.379  22.137 52.756 1.00 21.09 ? 305 HOH A O   1 
HETATM 3747 O  O   . HOH E 3 .   ? 7.473   31.797 69.818 1.00 21.12 ? 306 HOH A O   1 
HETATM 3748 O  O   . HOH E 3 .   ? 22.818  35.936 51.368 1.00 20.35 ? 307 HOH A O   1 
HETATM 3749 O  O   . HOH E 3 .   ? 22.729  16.414 48.141 1.00 21.69 ? 308 HOH A O   1 
HETATM 3750 O  O   . HOH E 3 .   ? 16.597  13.874 75.106 1.00 21.85 ? 309 HOH A O   1 
HETATM 3751 O  O   . HOH E 3 .   ? 21.845  35.893 73.658 1.00 21.36 ? 310 HOH A O   1 
HETATM 3752 O  O   . HOH E 3 .   ? 26.546  18.394 48.122 1.00 21.42 ? 311 HOH A O   1 
HETATM 3753 O  O   . HOH E 3 .   ? 34.361  18.785 55.784 1.00 22.49 ? 312 HOH A O   1 
HETATM 3754 O  O   . HOH E 3 .   ? 16.552  8.117  59.823 1.00 22.06 ? 313 HOH A O   1 
HETATM 3755 O  O   . HOH E 3 .   ? 3.404   33.105 55.676 1.00 22.62 ? 314 HOH A O   1 
HETATM 3756 O  O   . HOH E 3 .   ? 5.751   9.221  56.090 1.00 22.81 ? 315 HOH A O   1 
HETATM 3757 O  O   . HOH E 3 .   ? 24.591  32.515 53.707 1.00 23.03 ? 316 HOH A O   1 
HETATM 3758 O  O   . HOH E 3 .   ? 14.789  8.235  57.376 1.00 23.94 ? 317 HOH A O   1 
HETATM 3759 O  O   . HOH E 3 .   ? 36.557  16.402 56.921 1.00 24.19 ? 318 HOH A O   1 
HETATM 3760 O  O   . HOH E 3 .   ? 19.548  15.780 45.532 1.00 26.28 ? 319 HOH A O   1 
HETATM 3761 O  O   . HOH E 3 .   ? -3.744  28.292 63.794 1.00 26.53 ? 320 HOH A O   1 
HETATM 3762 O  O   . HOH E 3 .   ? 37.392  14.512 63.792 1.00 26.63 ? 321 HOH A O   1 
HETATM 3763 O  O   . HOH E 3 .   ? 10.498  34.186 47.350 1.00 26.75 ? 322 HOH A O   1 
HETATM 3764 O  O   . HOH E 3 .   ? 12.581  36.369 58.332 1.00 27.29 ? 323 HOH A O   1 
HETATM 3765 O  O   . HOH E 3 .   ? 32.465  20.471 76.631 1.00 27.71 ? 324 HOH A O   1 
HETATM 3766 O  O   . HOH E 3 .   ? 19.868  28.544 44.800 1.00 27.22 ? 325 HOH A O   1 
HETATM 3767 O  O   . HOH E 3 .   ? 40.817  25.369 71.172 1.00 28.11 ? 326 HOH A O   1 
HETATM 3768 O  O   . HOH E 3 .   ? 29.659  42.066 58.100 1.00 27.24 ? 327 HOH A O   1 
HETATM 3769 O  O   . HOH E 3 .   ? 36.036  30.764 57.755 1.00 28.63 ? 328 HOH A O   1 
HETATM 3770 O  O   . HOH E 3 .   ? 15.073  24.709 36.372 1.00 28.01 ? 329 HOH A O   1 
HETATM 3771 O  O   . HOH E 3 .   ? 0.212   20.159 65.912 1.00 30.01 ? 330 HOH A O   1 
HETATM 3772 O  O   . HOH E 3 .   ? 11.676  20.251 33.178 1.00 29.71 ? 331 HOH A O   1 
HETATM 3773 O  O   . HOH E 3 .   ? 28.570  28.246 74.275 1.00 30.44 ? 332 HOH A O   1 
HETATM 3774 O  O   . HOH E 3 .   ? 41.578  24.275 60.822 1.00 30.83 ? 333 HOH A O   1 
HETATM 3775 O  O   . HOH E 3 .   ? 12.643  8.528  54.383 1.00 30.51 ? 334 HOH A O   1 
HETATM 3776 O  O   . HOH E 3 .   ? 31.768  31.189 78.732 1.00 31.00 ? 335 HOH A O   1 
HETATM 3777 O  O   . HOH E 3 .   ? 8.374   19.499 35.328 1.00 30.72 ? 336 HOH A O   1 
HETATM 3778 O  O   . HOH E 3 .   ? 11.006  14.534 73.498 1.00 31.06 ? 337 HOH A O   1 
HETATM 3779 O  O   . HOH E 3 .   ? 5.962   25.943 71.413 1.00 31.63 ? 338 HOH A O   1 
HETATM 3780 O  O   . HOH E 3 .   ? -3.520  16.968 60.849 1.00 32.48 ? 339 HOH A O   1 
HETATM 3781 O  O   . HOH E 3 .   ? 17.255  4.308  64.857 1.00 31.86 ? 340 HOH A O   1 
HETATM 3782 O  O   . HOH E 3 .   ? 3.279   31.427 68.688 1.00 32.49 ? 341 HOH A O   1 
HETATM 3783 O  O   . HOH E 3 .   ? 38.391  19.334 65.769 1.00 32.59 ? 342 HOH A O   1 
HETATM 3784 O  O   . HOH E 3 .   ? 34.855  39.071 68.276 1.00 33.72 ? 343 HOH A O   1 
HETATM 3785 O  O   . HOH E 3 .   ? 27.611  21.974 78.635 1.00 32.95 ? 344 HOH A O   1 
HETATM 3786 O  O   . HOH E 3 .   ? 35.284  12.120 68.619 1.00 33.44 ? 345 HOH A O   1 
HETATM 3787 O  O   . HOH E 3 .   ? 25.125  27.802 51.999 1.00 34.98 ? 346 HOH A O   1 
HETATM 3788 O  O   . HOH E 3 .   ? 38.555  31.778 75.988 1.00 35.68 ? 347 HOH A O   1 
HETATM 3789 O  O   . HOH E 3 .   ? 9.485   29.404 42.973 1.00 36.85 ? 348 HOH A O   1 
HETATM 3790 O  O   . HOH E 3 .   ? 16.972  5.299  59.540 1.00 36.31 ? 349 HOH A O   1 
HETATM 3791 O  O   . HOH E 3 .   ? 27.635  25.570 50.734 1.00 36.33 ? 350 HOH A O   1 
HETATM 3792 O  O   . HOH E 3 .   ? 19.172  37.663 59.221 1.00 9.34  ? 351 HOH A O   1 
HETATM 3793 O  O   . HOH E 3 .   ? 22.716  39.795 58.309 1.00 12.69 ? 352 HOH A O   1 
HETATM 3794 O  O   . HOH E 3 .   ? 30.577  35.762 61.264 1.00 15.81 ? 353 HOH A O   1 
HETATM 3795 O  O   . HOH E 3 .   ? 13.367  37.402 55.772 1.00 18.08 ? 354 HOH A O   1 
HETATM 3796 O  O   . HOH E 3 .   ? 6.225   29.318 55.121 1.00 18.28 ? 355 HOH A O   1 
HETATM 3797 O  O   . HOH E 3 .   ? 1.261   30.134 57.412 1.00 21.26 ? 356 HOH A O   1 
HETATM 3798 O  O   . HOH E 3 .   ? 25.440  6.041  62.407 1.00 25.35 ? 357 HOH A O   1 
HETATM 3799 O  O   . HOH E 3 .   ? 5.512   34.914 54.620 1.00 29.77 ? 358 HOH A O   1 
HETATM 3800 O  O   . HOH E 3 .   ? 0.357   30.799 52.140 1.00 29.83 ? 359 HOH A O   1 
HETATM 3801 O  O   . HOH E 3 .   ? 39.863  23.376 57.021 1.00 29.74 ? 360 HOH A O   1 
HETATM 3802 O  O   . HOH E 3 .   ? 6.970   35.600 52.450 1.00 29.91 ? 361 HOH A O   1 
HETATM 3803 O  O   . HOH E 3 .   ? 16.783  22.566 39.660 1.00 30.21 ? 362 HOH A O   1 
HETATM 3804 O  O   . HOH E 3 .   ? 34.798  24.422 76.089 1.00 31.28 ? 363 HOH A O   1 
HETATM 3805 O  O   . HOH E 3 .   ? 16.218  19.192 72.445 1.00 31.67 ? 364 HOH A O   1 
HETATM 3806 O  O   . HOH E 3 .   ? 29.945  36.099 57.525 1.00 31.79 ? 365 HOH A O   1 
HETATM 3807 O  O   . HOH E 3 .   ? 26.046  26.925 45.636 1.00 32.99 ? 366 HOH A O   1 
HETATM 3808 O  O   . HOH E 3 .   ? -5.994  13.284 57.951 1.00 33.56 ? 367 HOH A O   1 
HETATM 3809 O  O   . HOH E 3 .   ? 33.439  28.392 78.738 1.00 33.64 ? 368 HOH A O   1 
HETATM 3810 O  O   . HOH E 3 .   ? 20.472  38.192 71.306 1.00 34.22 ? 369 HOH A O   1 
HETATM 3811 O  O   . HOH E 3 .   ? 17.521  13.829 44.193 1.00 34.69 ? 370 HOH A O   1 
HETATM 3812 O  O   . HOH E 3 .   ? 30.398  8.228  62.180 1.00 35.86 ? 371 HOH A O   1 
HETATM 3813 O  O   . HOH E 3 .   ? 13.868  5.328  66.289 1.00 36.34 ? 372 HOH A O   1 
HETATM 3814 O  O   . HOH E 3 .   ? 25.925  27.037 48.618 1.00 37.17 ? 373 HOH A O   1 
HETATM 3815 O  O   . HOH E 3 .   ? 4.741   28.387 71.102 1.00 38.40 ? 374 HOH A O   1 
HETATM 3816 O  O   . HOH E 3 .   ? 24.359  2.252  61.335 1.00 38.92 ? 375 HOH A O   1 
HETATM 3817 O  O   . HOH F 3 .   ? -22.034 23.066 32.035 1.00 16.71 ? 252 HOH B O   1 
HETATM 3818 O  O   . HOH F 3 .   ? -21.221 24.789 34.749 1.00 15.99 ? 253 HOH B O   1 
HETATM 3819 O  O   . HOH F 3 .   ? -18.358 25.072 32.903 1.00 12.65 ? 254 HOH B O   1 
HETATM 3820 O  O   . HOH F 3 .   ? -19.726 23.709 30.756 1.00 17.51 ? 255 HOH B O   1 
HETATM 3821 O  O   . HOH F 3 .   ? -19.708 22.331 33.688 1.00 13.36 ? 256 HOH B O   1 
HETATM 3822 O  O   . HOH F 3 .   ? -0.770  22.951 51.701 1.00 5.32  ? 257 HOH B O   1 
HETATM 3823 O  O   . HOH F 3 .   ? -3.260  24.277 51.132 1.00 6.03  ? 258 HOH B O   1 
HETATM 3824 O  O   . HOH F 3 .   ? -21.967 25.344 38.643 1.00 5.57  ? 259 HOH B O   1 
HETATM 3825 O  O   . HOH F 3 .   ? -33.378 22.021 39.053 1.00 5.65  ? 260 HOH B O   1 
HETATM 3826 O  O   . HOH F 3 .   ? -21.769 24.701 41.293 1.00 6.86  ? 261 HOH B O   1 
HETATM 3827 O  O   . HOH F 3 .   ? -17.468 18.202 52.731 1.00 7.47  ? 262 HOH B O   1 
HETATM 3828 O  O   . HOH F 3 .   ? -16.087 16.074 48.154 1.00 7.75  ? 263 HOH B O   1 
HETATM 3829 O  O   . HOH F 3 .   ? -18.103 22.433 38.044 1.00 7.24  ? 264 HOH B O   1 
HETATM 3830 O  O   . HOH F 3 .   ? -15.178 25.603 38.138 1.00 8.57  ? 265 HOH B O   1 
HETATM 3831 O  O   . HOH F 3 .   ? -13.418 19.472 49.104 1.00 9.08  ? 266 HOH B O   1 
HETATM 3832 O  O   . HOH F 3 .   ? -33.209 20.539 41.822 1.00 8.81  ? 267 HOH B O   1 
HETATM 3833 O  O   . HOH F 3 .   ? -28.753 22.268 40.997 1.00 9.05  ? 268 HOH B O   1 
HETATM 3834 O  O   . HOH F 3 .   ? -32.032 23.122 36.788 1.00 9.82  ? 269 HOH B O   1 
HETATM 3835 O  O   . HOH F 3 .   ? -21.255 10.441 49.629 1.00 10.24 ? 270 HOH B O   1 
HETATM 3836 O  O   . HOH F 3 .   ? -18.184 11.565 42.756 1.00 10.64 ? 271 HOH B O   1 
HETATM 3837 O  O   . HOH F 3 .   ? -34.535 17.721 37.934 1.00 11.40 ? 272 HOH B O   1 
HETATM 3838 O  O   . HOH F 3 .   ? -26.158 19.171 54.348 1.00 11.20 ? 273 HOH B O   1 
HETATM 3839 O  O   . HOH F 3 .   ? -13.436 19.586 36.515 1.00 11.91 ? 274 HOH B O   1 
HETATM 3840 O  O   . HOH F 3 .   ? -17.119 11.502 54.400 1.00 11.85 ? 275 HOH B O   1 
HETATM 3841 O  O   . HOH F 3 .   ? -27.575 25.389 27.710 1.00 12.18 ? 276 HOH B O   1 
HETATM 3842 O  O   . HOH F 3 .   ? -15.143 17.865 64.806 1.00 11.90 ? 277 HOH B O   1 
HETATM 3843 O  O   . HOH F 3 .   ? -37.136 29.591 30.982 1.00 12.19 ? 278 HOH B O   1 
HETATM 3844 O  O   . HOH F 3 .   ? -15.703 16.992 50.819 1.00 11.70 ? 279 HOH B O   1 
HETATM 3845 O  O   . HOH F 3 .   ? -30.053 25.686 46.547 1.00 12.43 ? 280 HOH B O   1 
HETATM 3846 O  O   . HOH F 3 .   ? -33.804 16.902 27.105 1.00 12.79 ? 281 HOH B O   1 
HETATM 3847 O  O   . HOH F 3 .   ? -0.919  12.304 50.152 1.00 13.35 ? 282 HOH B O   1 
HETATM 3848 O  O   . HOH F 3 .   ? -15.884 33.877 33.326 1.00 13.22 ? 283 HOH B O   1 
HETATM 3849 O  O   . HOH F 3 .   ? -18.282 19.931 61.966 1.00 13.35 ? 284 HOH B O   1 
HETATM 3850 O  O   . HOH F 3 .   ? -23.585 36.702 45.228 1.00 14.59 ? 285 HOH B O   1 
HETATM 3851 O  O   . HOH F 3 .   ? -9.443  28.204 53.476 1.00 14.13 ? 286 HOH B O   1 
HETATM 3852 O  O   . HOH F 3 .   ? -24.705 25.460 37.924 1.00 14.23 ? 287 HOH B O   1 
HETATM 3853 O  O   . HOH F 3 .   ? -19.815 20.056 32.514 1.00 13.80 ? 288 HOH B O   1 
HETATM 3854 O  O   . HOH F 3 .   ? -31.525 15.983 48.656 1.00 14.12 ? 289 HOH B O   1 
HETATM 3855 O  O   . HOH F 3 .   ? -12.031 34.700 52.251 1.00 15.24 ? 290 HOH B O   1 
HETATM 3856 O  O   . HOH F 3 .   ? -20.894 36.291 33.406 1.00 16.33 ? 291 HOH B O   1 
HETATM 3857 O  O   . HOH F 3 .   ? -4.090  21.573 37.137 1.00 16.69 ? 292 HOH B O   1 
HETATM 3858 O  O   . HOH F 3 .   ? -33.994 22.029 28.946 1.00 16.54 ? 293 HOH B O   1 
HETATM 3859 O  O   . HOH F 3 .   ? -27.291 12.560 29.308 1.00 16.51 ? 294 HOH B O   1 
HETATM 3860 O  O   . HOH F 3 .   ? -17.511 21.933 66.454 1.00 17.54 ? 295 HOH B O   1 
HETATM 3861 O  O   . HOH F 3 .   ? -29.565 12.459 31.398 1.00 17.35 ? 296 HOH B O   1 
HETATM 3862 O  O   . HOH F 3 .   ? -29.883 34.820 44.280 1.00 17.44 ? 297 HOH B O   1 
HETATM 3863 O  O   . HOH F 3 .   ? -6.916  7.875  40.663 1.00 18.12 ? 298 HOH B O   1 
HETATM 3864 O  O   . HOH F 3 .   ? -12.288 17.808 67.624 1.00 18.08 ? 299 HOH B O   1 
HETATM 3865 O  O   . HOH F 3 .   ? -8.440  14.235 58.229 1.00 19.52 ? 300 HOH B O   1 
HETATM 3866 O  O   . HOH F 3 .   ? -32.662 28.436 27.183 1.00 19.70 ? 301 HOH B O   1 
HETATM 3867 O  O   . HOH F 3 .   ? -27.922 17.747 23.811 1.00 19.89 ? 302 HOH B O   1 
HETATM 3868 O  O   . HOH F 3 .   ? -25.633 26.649 48.733 1.00 20.28 ? 303 HOH B O   1 
HETATM 3869 O  O   . HOH F 3 .   ? -28.998 20.635 57.893 1.00 20.61 ? 304 HOH B O   1 
HETATM 3870 O  O   . HOH F 3 .   ? -5.836  30.330 47.609 1.00 21.08 ? 305 HOH B O   1 
HETATM 3871 O  O   . HOH F 3 .   ? -35.189 21.632 50.708 1.00 20.47 ? 306 HOH B O   1 
HETATM 3872 O  O   . HOH F 3 .   ? -9.351  31.681 33.747 1.00 21.61 ? 307 HOH B O   1 
HETATM 3873 O  O   . HOH F 3 .   ? -24.693 35.084 51.798 1.00 22.08 ? 308 HOH B O   1 
HETATM 3874 O  O   . HOH F 3 .   ? -24.397 15.989 55.300 1.00 21.44 ? 309 HOH B O   1 
HETATM 3875 O  O   . HOH F 3 .   ? -18.168 13.921 28.221 1.00 22.01 ? 310 HOH B O   1 
HETATM 3876 O  O   . HOH F 3 .   ? -23.556 35.484 30.085 1.00 22.22 ? 311 HOH B O   1 
HETATM 3877 O  O   . HOH F 3 .   ? -28.376 17.968 55.341 1.00 22.25 ? 312 HOH B O   1 
HETATM 3878 O  O   . HOH F 3 .   ? -35.891 18.215 47.616 1.00 22.37 ? 313 HOH B O   1 
HETATM 3879 O  O   . HOH F 3 .   ? -17.915 7.763  43.419 1.00 22.68 ? 314 HOH B O   1 
HETATM 3880 O  O   . HOH F 3 .   ? -5.125  32.965 47.897 1.00 22.91 ? 315 HOH B O   1 
HETATM 3881 O  O   . HOH F 3 .   ? -7.322  9.014  47.292 1.00 23.46 ? 316 HOH B O   1 
HETATM 3882 O  O   . HOH F 3 .   ? -26.617 32.092 49.787 1.00 22.64 ? 317 HOH B O   1 
HETATM 3883 O  O   . HOH F 3 .   ? -16.278 8.007  45.782 1.00 23.80 ? 318 HOH B O   1 
HETATM 3884 O  O   . HOH F 3 .   ? -38.159 16.010 46.349 1.00 23.18 ? 319 HOH B O   1 
HETATM 3885 O  O   . HOH F 3 .   ? -21.049 15.295 57.799 1.00 25.68 ? 320 HOH B O   1 
HETATM 3886 O  O   . HOH F 3 .   ? 1.802   28.238 39.555 1.00 26.91 ? 321 HOH B O   1 
HETATM 3887 O  O   . HOH F 3 .   ? -39.125 13.580 39.020 1.00 28.50 ? 322 HOH B O   1 
HETATM 3888 O  O   . HOH F 3 .   ? -12.166 34.034 56.316 1.00 27.00 ? 323 HOH B O   1 
HETATM 3889 O  O   . HOH F 3 .   ? -14.713 36.215 44.963 1.00 27.16 ? 324 HOH B O   1 
HETATM 3890 O  O   . HOH F 3 .   ? -34.118 20.284 26.674 1.00 27.16 ? 325 HOH B O   1 
HETATM 3891 O  O   . HOH F 3 .   ? -21.733 28.078 58.374 1.00 26.73 ? 326 HOH B O   1 
HETATM 3892 O  O   . HOH F 3 .   ? -42.521 24.740 32.280 1.00 28.46 ? 327 HOH B O   1 
HETATM 3893 O  O   . HOH F 3 .   ? -31.207 42.082 44.981 1.00 27.79 ? 328 HOH B O   1 
HETATM 3894 O  O   . HOH F 3 .   ? -37.662 29.994 45.551 1.00 27.59 ? 329 HOH B O   1 
HETATM 3895 O  O   . HOH F 3 .   ? -16.543 24.357 67.061 1.00 28.42 ? 330 HOH B O   1 
HETATM 3896 O  O   . HOH F 3 .   ? -1.795  20.302 37.145 1.00 30.98 ? 331 HOH B O   1 
HETATM 3897 O  O   . HOH F 3 .   ? -13.287 19.138 70.147 1.00 29.77 ? 332 HOH B O   1 
HETATM 3898 O  O   . HOH F 3 .   ? -30.246 27.856 28.868 1.00 30.35 ? 333 HOH B O   1 
HETATM 3899 O  O   . HOH F 3 .   ? -43.356 23.300 42.595 1.00 30.85 ? 334 HOH B O   1 
HETATM 3900 O  O   . HOH F 3 .   ? -14.047 8.446  49.114 1.00 30.59 ? 335 HOH B O   1 
HETATM 3901 O  O   . HOH F 3 .   ? -33.430 30.818 24.690 1.00 30.61 ? 336 HOH B O   1 
HETATM 3902 O  O   . HOH F 3 .   ? -9.891  19.279 68.149 1.00 30.85 ? 337 HOH B O   1 
HETATM 3903 O  O   . HOH F 3 .   ? -12.605 14.475 29.849 1.00 31.25 ? 338 HOH B O   1 
HETATM 3904 O  O   . HOH F 3 .   ? -7.673  26.133 32.059 1.00 31.50 ? 339 HOH B O   1 
HETATM 3905 O  O   . HOH F 3 .   ? 1.667   17.170 42.577 1.00 32.64 ? 340 HOH B O   1 
HETATM 3906 O  O   . HOH F 3 .   ? -19.186 3.594  38.564 1.00 32.19 ? 341 HOH B O   1 
HETATM 3907 O  O   . HOH F 3 .   ? 5.915   15.667 42.440 1.00 32.46 ? 342 HOH B O   1 
HETATM 3908 O  O   . HOH F 3 .   ? -40.017 18.935 37.628 1.00 32.66 ? 343 HOH B O   1 
HETATM 3909 O  O   . HOH F 3 .   ? -36.704 38.190 35.338 1.00 32.61 ? 344 HOH B O   1 
HETATM 3910 O  O   . HOH F 3 .   ? -29.225 21.706 24.802 1.00 32.76 ? 345 HOH B O   1 
HETATM 3911 O  O   . HOH F 3 .   ? -36.966 11.766 34.785 1.00 33.51 ? 346 HOH B O   1 
HETATM 3912 O  O   . HOH F 3 .   ? -26.879 27.110 51.156 1.00 35.07 ? 347 HOH B O   1 
HETATM 3913 O  O   . HOH F 3 .   ? -40.397 31.799 27.365 1.00 36.27 ? 348 HOH B O   1 
HETATM 3914 O  O   . HOH F 3 .   ? -11.111 29.337 60.614 1.00 35.85 ? 349 HOH B O   1 
HETATM 3915 O  O   . HOH F 3 .   ? -17.930 4.937  43.368 1.00 36.41 ? 350 HOH B O   1 
HETATM 3916 O  O   . HOH F 3 .   ? -28.798 24.813 52.636 1.00 36.95 ? 351 HOH B O   1 
HETATM 3917 O  O   . HOH F 3 .   ? -17.618 24.092 62.474 1.00 25.28 ? 352 HOH B O   1 
HETATM 3918 O  O   . HOH F 3 .   ? -20.426 12.365 55.261 1.00 29.64 ? 353 HOH B O   1 
HETATM 3919 O  O   . HOH F 3 .   ? -41.920 26.127 29.340 1.00 29.50 ? 354 HOH B O   1 
HETATM 3920 O  O   . HOH F 3 .   ? -3.510  34.082 42.788 1.00 29.81 ? 355 HOH B O   1 
HETATM 3921 O  O   . HOH F 3 .   ? -17.691 29.204 59.768 1.00 30.44 ? 356 HOH B O   1 
HETATM 3922 O  O   . HOH F 3 .   ? -27.107 10.886 27.150 1.00 31.93 ? 357 HOH B O   1 
HETATM 3923 O  O   . HOH F 3 .   ? -2.605  33.273 36.308 1.00 32.00 ? 358 HOH B O   1 
HETATM 3924 O  O   . HOH F 3 .   ? -18.384 37.406 45.645 1.00 31.97 ? 359 HOH B O   1 
HETATM 3925 O  O   . HOH F 3 .   ? -22.883 9.637  25.092 1.00 32.33 ? 360 HOH B O   1 
HETATM 3926 O  O   . HOH F 3 .   ? -25.298 14.364 53.398 1.00 32.84 ? 361 HOH B O   1 
HETATM 3927 O  O   . HOH F 3 .   ? -7.034  35.741 44.323 1.00 32.83 ? 362 HOH B O   1 
HETATM 3928 O  O   . HOH F 3 .   ? -30.819 9.949  30.578 1.00 33.19 ? 363 HOH B O   1 
HETATM 3929 O  O   . HOH F 3 .   ? -12.509 28.150 28.649 1.00 33.71 ? 364 HOH B O   1 
HETATM 3930 O  O   . HOH F 3 .   ? -20.342 33.687 26.501 1.00 33.51 ? 365 HOH B O   1 
HETATM 3931 O  O   . HOH F 3 .   ? -3.746  28.325 34.617 1.00 33.77 ? 366 HOH B O   1 
HETATM 3932 O  O   . HOH F 3 .   ? -42.397 25.726 45.133 1.00 33.78 ? 367 HOH B O   1 
HETATM 3933 O  O   . HOH F 3 .   ? -29.916 38.105 35.249 1.00 34.36 ? 368 HOH B O   1 
HETATM 3934 O  O   . HOH F 3 .   ? 2.685   22.990 39.002 1.00 34.50 ? 369 HOH B O   1 
HETATM 3935 O  O   . HOH F 3 .   ? -28.249 11.302 53.308 1.00 34.73 ? 370 HOH B O   1 
HETATM 3936 O  O   . HOH F 3 .   ? -13.769 24.633 65.243 1.00 35.51 ? 371 HOH B O   1 
HETATM 3937 O  O   . HOH F 3 .   ? -34.301 15.799 48.947 1.00 35.51 ? 372 HOH B O   1 
HETATM 3938 O  O   . HOH F 3 .   ? -23.360 36.170 26.679 1.00 36.12 ? 373 HOH B O   1 
HETATM 3939 O  O   . HOH F 3 .   ? -2.232  34.177 39.093 1.00 36.30 ? 374 HOH B O   1 
HETATM 3940 O  O   . HOH F 3 .   ? -16.699 5.668  47.326 1.00 36.51 ? 375 HOH B O   1 
HETATM 3941 O  O   . HOH F 3 .   ? -34.088 27.495 51.733 1.00 36.40 ? 376 HOH B O   1 
HETATM 3942 O  O   . HOH F 3 .   ? -28.584 26.773 48.784 1.00 36.91 ? 377 HOH B O   1 
HETATM 3943 O  O   . HOH F 3 .   ? -27.914 6.213  34.995 1.00 37.83 ? 378 HOH B O   1 
# 
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   ASP 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   GLU 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   CYS 9   9   9   CYS CYS A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  PRO 51  51  51  PRO PRO 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  GLY 54  54  54  GLY GLY A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  GLN 90  90  90  GLN GLN A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  PRO 92  92  92  PRO PRO 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  SER 95  95  95  SER SER A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 SER 109 109 109 SER SER A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 TYR 143 143 143 TYR TYR A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LYS 156 156 156 LYS LYS 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 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ASN 183 183 183 ASN ASN A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 TYR 185 185 185 TYR TYR A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 PHE 188 188 188 PHE PHE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 CYS 201 201 201 CYS CYS A . n 
A 1 202 GLN 202 202 202 GLN GLN A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 GLU 209 209 209 GLU GLU A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 GLU 211 211 211 GLU GLU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 TRP 219 219 219 TRP TRP A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LYS 231 231 231 LYS LYS A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 CYS 243 243 243 CYS CYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
B 1 1   ASP 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   GLU 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   ?   ?   ?   B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   ASP 7   7   7   ASP ASP B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   CYS 9   9   9   CYS CYS B . n 
B 1 10  ALA 10  10  10  ALA ALA B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  CYS 13  13  13  CYS CYS B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  VAL 21  21  21  VAL VAL B . n 
B 1 22  SER 22  22  22  SER SER B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  HIS 26  26  26  HIS HIS B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  TYR 28  28  28  TYR TYR B . n 
B 1 29  THR 29  29  29  THR THR B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ASN 31  31  31  ASN ASN B . n 
B 1 32  ASN 32  32  32  ASN ASN B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  LYS 37  37  37  LYS LYS B . n 
B 1 38  PHE 38  38  38  PHE PHE B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  TRP 41  41  41  TRP TRP B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  THR 47  47  47  THR THR B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  ASP 49  49  49  ASP ASP B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  PRO 51  51  51  PRO PRO 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  GLY 54  54  54  GLY GLY B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  THR 56  56  56  THR THR B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  TRP 59  59  59  TRP TRP B . n 
B 1 60  LYS 60  60  60  LYS LYS B . n 
B 1 61  THR 61  61  61  THR THR B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  PRO 67  67  67  PRO PRO B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  THR 70  70  70  THR THR B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  THR 77  77  77  THR THR B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  LYS 84  84  84  LYS LYS B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  HIS 89  89  89  HIS HIS B . n 
B 1 90  GLN 90  90  90  GLN GLN B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  PRO 92  92  92  PRO PRO 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  SER 95  95  95  SER SER B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 TRP 102 102 102 TRP TRP B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 ASN 106 106 106 ASN ASN B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 SER 109 109 109 SER SER B . n 
B 1 110 ASN 110 110 110 ASN ASN B . n 
B 1 111 ILE 111 111 111 ILE ILE B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 GLN 114 114 114 GLN GLN B . n 
B 1 115 LYS 115 115 115 LYS LYS B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 ASP 117 117 117 ASP ASP B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLN 120 120 120 GLN GLN B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 ARG 125 125 125 ARG ARG B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 LYS 132 132 132 LYS LYS B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 SER 140 140 140 SER SER B . n 
B 1 141 SER 141 141 141 SER SER B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 TYR 143 143 143 TYR TYR B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 PRO 148 148 148 PRO PRO B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 GLU 151 151 151 GLU GLU B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 MET 154 154 154 MET MET B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 LYS 156 156 156 LYS LYS 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 GLY 159 159 159 GLY GLY B . n 
B 1 160 THR 160 160 160 THR THR B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 THR 165 165 165 THR THR B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 PRO 167 167 167 PRO PRO B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 TYR 170 170 170 TYR TYR B . n 
B 1 171 TRP 171 171 171 TRP TRP B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 ILE 176 176 176 ILE ILE B . n 
B 1 177 ASN 177 177 177 ASN ASN B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 SER 179 179 179 SER SER B . n 
B 1 180 PRO 180 180 180 PRO PRO B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 ASN 183 183 183 ASN ASN B . n 
B 1 184 HIS 184 184 184 HIS HIS B . n 
B 1 185 TYR 185 185 185 TYR TYR B . n 
B 1 186 ALA 186 186 186 ALA ALA B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 PHE 188 188 188 PHE PHE B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 PHE 190 190 190 PHE PHE B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ASN 193 193 193 ASN ASN B . n 
B 1 194 THR 194 194 194 THR THR B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 CYS 201 201 201 CYS CYS B . n 
B 1 202 GLN 202 202 202 GLN GLN B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 VAL 205 205 205 VAL VAL B . n 
B 1 206 THR 206 206 206 THR THR B . n 
B 1 207 VAL 207 207 207 VAL VAL B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 GLU 209 209 209 GLU GLU B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 GLU 211 211 211 GLU GLU B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 TRP 219 219 219 TRP TRP B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 GLY 221 221 221 GLY GLY B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 PRO 223 223 223 PRO PRO B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 ASP 225 225 225 ASP ASP B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 LYS 231 231 231 LYS LYS B . n 
B 1 232 SER 232 232 232 SER SER B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 GLY 235 235 235 GLY GLY B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 PRO 238 238 238 PRO PRO B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 MET 241 241 241 MET MET B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 CYS 243 243 243 CYS CYS B . n 
B 1 244 LYS 244 244 244 LYS LYS B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
# 
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 MG  1   251 1   MG  MG  A . 
D 2 MG  1   251 1   MG  MG  B . 
E 3 HOH 1   252 2   HOH HOH A . 
E 3 HOH 2   253 3   HOH HOH A . 
E 3 HOH 3   254 4   HOH HOH A . 
E 3 HOH 4   255 5   HOH HOH A . 
E 3 HOH 5   256 6   HOH HOH A . 
E 3 HOH 6   257 2   HOH HOH A . 
E 3 HOH 7   258 4   HOH HOH A . 
E 3 HOH 8   259 6   HOH HOH A . 
E 3 HOH 9   260 8   HOH HOH A . 
E 3 HOH 10  261 10  HOH HOH A . 
E 3 HOH 11  262 12  HOH HOH A . 
E 3 HOH 12  263 14  HOH HOH A . 
E 3 HOH 13  264 16  HOH HOH A . 
E 3 HOH 14  265 18  HOH HOH A . 
E 3 HOH 15  266 20  HOH HOH A . 
E 3 HOH 16  267 22  HOH HOH A . 
E 3 HOH 17  268 24  HOH HOH A . 
E 3 HOH 18  269 26  HOH HOH A . 
E 3 HOH 19  270 28  HOH HOH A . 
E 3 HOH 20  271 30  HOH HOH A . 
E 3 HOH 21  272 32  HOH HOH A . 
E 3 HOH 22  273 34  HOH HOH A . 
E 3 HOH 23  274 36  HOH HOH A . 
E 3 HOH 24  275 38  HOH HOH A . 
E 3 HOH 25  276 40  HOH HOH A . 
E 3 HOH 26  277 42  HOH HOH A . 
E 3 HOH 27  278 44  HOH HOH A . 
E 3 HOH 28  279 46  HOH HOH A . 
E 3 HOH 29  280 48  HOH HOH A . 
E 3 HOH 30  281 50  HOH HOH A . 
E 3 HOH 31  282 52  HOH HOH A . 
E 3 HOH 32  283 54  HOH HOH A . 
E 3 HOH 33  284 56  HOH HOH A . 
E 3 HOH 34  285 58  HOH HOH A . 
E 3 HOH 35  286 60  HOH HOH A . 
E 3 HOH 36  287 62  HOH HOH A . 
E 3 HOH 37  288 64  HOH HOH A . 
E 3 HOH 38  289 66  HOH HOH A . 
E 3 HOH 39  290 68  HOH HOH A . 
E 3 HOH 40  291 70  HOH HOH A . 
E 3 HOH 41  292 72  HOH HOH A . 
E 3 HOH 42  293 74  HOH HOH A . 
E 3 HOH 43  294 76  HOH HOH A . 
E 3 HOH 44  295 78  HOH HOH A . 
E 3 HOH 45  296 80  HOH HOH A . 
E 3 HOH 46  297 82  HOH HOH A . 
E 3 HOH 47  298 84  HOH HOH A . 
E 3 HOH 48  299 86  HOH HOH A . 
E 3 HOH 49  300 88  HOH HOH A . 
E 3 HOH 50  301 90  HOH HOH A . 
E 3 HOH 51  302 92  HOH HOH A . 
E 3 HOH 52  303 94  HOH HOH A . 
E 3 HOH 53  304 96  HOH HOH A . 
E 3 HOH 54  305 98  HOH HOH A . 
E 3 HOH 55  306 100 HOH HOH A . 
E 3 HOH 56  307 102 HOH HOH A . 
E 3 HOH 57  308 104 HOH HOH A . 
E 3 HOH 58  309 106 HOH HOH A . 
E 3 HOH 59  310 108 HOH HOH A . 
E 3 HOH 60  311 110 HOH HOH A . 
E 3 HOH 61  312 112 HOH HOH A . 
E 3 HOH 62  313 114 HOH HOH A . 
E 3 HOH 63  314 116 HOH HOH A . 
E 3 HOH 64  315 118 HOH HOH A . 
E 3 HOH 65  316 120 HOH HOH A . 
E 3 HOH 66  317 122 HOH HOH A . 
E 3 HOH 67  318 124 HOH HOH A . 
E 3 HOH 68  319 126 HOH HOH A . 
E 3 HOH 69  320 129 HOH HOH A . 
E 3 HOH 70  321 130 HOH HOH A . 
E 3 HOH 71  322 132 HOH HOH A . 
E 3 HOH 72  323 134 HOH HOH A . 
E 3 HOH 73  324 136 HOH HOH A . 
E 3 HOH 74  325 138 HOH HOH A . 
E 3 HOH 75  326 140 HOH HOH A . 
E 3 HOH 76  327 142 HOH HOH A . 
E 3 HOH 77  328 144 HOH HOH A . 
E 3 HOH 78  329 146 HOH HOH A . 
E 3 HOH 79  330 148 HOH HOH A . 
E 3 HOH 80  331 150 HOH HOH A . 
E 3 HOH 81  332 152 HOH HOH A . 
E 3 HOH 82  333 154 HOH HOH A . 
E 3 HOH 83  334 156 HOH HOH A . 
E 3 HOH 84  335 158 HOH HOH A . 
E 3 HOH 85  336 160 HOH HOH A . 
E 3 HOH 86  337 162 HOH HOH A . 
E 3 HOH 87  338 164 HOH HOH A . 
E 3 HOH 88  339 167 HOH HOH A . 
E 3 HOH 89  340 168 HOH HOH A . 
E 3 HOH 90  341 171 HOH HOH A . 
E 3 HOH 91  342 172 HOH HOH A . 
E 3 HOH 92  343 174 HOH HOH A . 
E 3 HOH 93  344 176 HOH HOH A . 
E 3 HOH 94  345 178 HOH HOH A . 
E 3 HOH 95  346 180 HOH HOH A . 
E 3 HOH 96  347 182 HOH HOH A . 
E 3 HOH 97  348 184 HOH HOH A . 
E 3 HOH 98  349 186 HOH HOH A . 
E 3 HOH 99  350 188 HOH HOH A . 
E 3 HOH 100 351 190 HOH HOH A . 
E 3 HOH 101 352 191 HOH HOH A . 
E 3 HOH 102 353 192 HOH HOH A . 
E 3 HOH 103 354 193 HOH HOH A . 
E 3 HOH 104 355 194 HOH HOH A . 
E 3 HOH 105 356 195 HOH HOH A . 
E 3 HOH 106 357 196 HOH HOH A . 
E 3 HOH 107 358 199 HOH HOH A . 
E 3 HOH 108 359 200 HOH HOH A . 
E 3 HOH 109 360 202 HOH HOH A . 
E 3 HOH 110 361 204 HOH HOH A . 
E 3 HOH 111 362 205 HOH HOH A . 
E 3 HOH 112 363 207 HOH HOH A . 
E 3 HOH 113 364 208 HOH HOH A . 
E 3 HOH 114 365 212 HOH HOH A . 
E 3 HOH 115 366 214 HOH HOH A . 
E 3 HOH 116 367 219 HOH HOH A . 
E 3 HOH 117 368 220 HOH HOH A . 
E 3 HOH 118 369 223 HOH HOH A . 
E 3 HOH 119 370 227 HOH HOH A . 
E 3 HOH 120 371 232 HOH HOH A . 
E 3 HOH 121 372 233 HOH HOH A . 
E 3 HOH 122 373 238 HOH HOH A . 
E 3 HOH 123 374 240 HOH HOH A . 
E 3 HOH 124 375 241 HOH HOH A . 
F 3 HOH 1   252 2   HOH HOH B . 
F 3 HOH 2   253 3   HOH HOH B . 
F 3 HOH 3   254 4   HOH HOH B . 
F 3 HOH 4   255 5   HOH HOH B . 
F 3 HOH 5   256 6   HOH HOH B . 
F 3 HOH 6   257 1   HOH HOH B . 
F 3 HOH 7   258 3   HOH HOH B . 
F 3 HOH 8   259 5   HOH HOH B . 
F 3 HOH 9   260 7   HOH HOH B . 
F 3 HOH 10  261 9   HOH HOH B . 
F 3 HOH 11  262 11  HOH HOH B . 
F 3 HOH 12  263 13  HOH HOH B . 
F 3 HOH 13  264 15  HOH HOH B . 
F 3 HOH 14  265 17  HOH HOH B . 
F 3 HOH 15  266 19  HOH HOH B . 
F 3 HOH 16  267 21  HOH HOH B . 
F 3 HOH 17  268 23  HOH HOH B . 
F 3 HOH 18  269 25  HOH HOH B . 
F 3 HOH 19  270 27  HOH HOH B . 
F 3 HOH 20  271 29  HOH HOH B . 
F 3 HOH 21  272 31  HOH HOH B . 
F 3 HOH 22  273 33  HOH HOH B . 
F 3 HOH 23  274 35  HOH HOH B . 
F 3 HOH 24  275 37  HOH HOH B . 
F 3 HOH 25  276 39  HOH HOH B . 
F 3 HOH 26  277 41  HOH HOH B . 
F 3 HOH 27  278 43  HOH HOH B . 
F 3 HOH 28  279 45  HOH HOH B . 
F 3 HOH 29  280 47  HOH HOH B . 
F 3 HOH 30  281 49  HOH HOH B . 
F 3 HOH 31  282 51  HOH HOH B . 
F 3 HOH 32  283 53  HOH HOH B . 
F 3 HOH 33  284 55  HOH HOH B . 
F 3 HOH 34  285 57  HOH HOH B . 
F 3 HOH 35  286 59  HOH HOH B . 
F 3 HOH 36  287 61  HOH HOH B . 
F 3 HOH 37  288 63  HOH HOH B . 
F 3 HOH 38  289 65  HOH HOH B . 
F 3 HOH 39  290 67  HOH HOH B . 
F 3 HOH 40  291 69  HOH HOH B . 
F 3 HOH 41  292 71  HOH HOH B . 
F 3 HOH 42  293 73  HOH HOH B . 
F 3 HOH 43  294 75  HOH HOH B . 
F 3 HOH 44  295 77  HOH HOH B . 
F 3 HOH 45  296 79  HOH HOH B . 
F 3 HOH 46  297 81  HOH HOH B . 
F 3 HOH 47  298 83  HOH HOH B . 
F 3 HOH 48  299 85  HOH HOH B . 
F 3 HOH 49  300 87  HOH HOH B . 
F 3 HOH 50  301 89  HOH HOH B . 
F 3 HOH 51  302 91  HOH HOH B . 
F 3 HOH 52  303 93  HOH HOH B . 
F 3 HOH 53  304 95  HOH HOH B . 
F 3 HOH 54  305 97  HOH HOH B . 
F 3 HOH 55  306 99  HOH HOH B . 
F 3 HOH 56  307 101 HOH HOH B . 
F 3 HOH 57  308 103 HOH HOH B . 
F 3 HOH 58  309 105 HOH HOH B . 
F 3 HOH 59  310 107 HOH HOH B . 
F 3 HOH 60  311 109 HOH HOH B . 
F 3 HOH 61  312 111 HOH HOH B . 
F 3 HOH 62  313 113 HOH HOH B . 
F 3 HOH 63  314 115 HOH HOH B . 
F 3 HOH 64  315 117 HOH HOH B . 
F 3 HOH 65  316 119 HOH HOH B . 
F 3 HOH 66  317 121 HOH HOH B . 
F 3 HOH 67  318 123 HOH HOH B . 
F 3 HOH 68  319 125 HOH HOH B . 
F 3 HOH 69  320 127 HOH HOH B . 
F 3 HOH 70  321 128 HOH HOH B . 
F 3 HOH 71  322 131 HOH HOH B . 
F 3 HOH 72  323 133 HOH HOH B . 
F 3 HOH 73  324 135 HOH HOH B . 
F 3 HOH 74  325 137 HOH HOH B . 
F 3 HOH 75  326 139 HOH HOH B . 
F 3 HOH 76  327 141 HOH HOH B . 
F 3 HOH 77  328 143 HOH HOH B . 
F 3 HOH 78  329 145 HOH HOH B . 
F 3 HOH 79  330 147 HOH HOH B . 
F 3 HOH 80  331 149 HOH HOH B . 
F 3 HOH 81  332 151 HOH HOH B . 
F 3 HOH 82  333 153 HOH HOH B . 
F 3 HOH 83  334 155 HOH HOH B . 
F 3 HOH 84  335 157 HOH HOH B . 
F 3 HOH 85  336 159 HOH HOH B . 
F 3 HOH 86  337 161 HOH HOH B . 
F 3 HOH 87  338 163 HOH HOH B . 
F 3 HOH 88  339 165 HOH HOH B . 
F 3 HOH 89  340 166 HOH HOH B . 
F 3 HOH 90  341 169 HOH HOH B . 
F 3 HOH 91  342 170 HOH HOH B . 
F 3 HOH 92  343 173 HOH HOH B . 
F 3 HOH 93  344 175 HOH HOH B . 
F 3 HOH 94  345 177 HOH HOH B . 
F 3 HOH 95  346 179 HOH HOH B . 
F 3 HOH 96  347 181 HOH HOH B . 
F 3 HOH 97  348 183 HOH HOH B . 
F 3 HOH 98  349 185 HOH HOH B . 
F 3 HOH 99  350 187 HOH HOH B . 
F 3 HOH 100 351 189 HOH HOH B . 
F 3 HOH 101 352 197 HOH HOH B . 
F 3 HOH 102 353 198 HOH HOH B . 
F 3 HOH 103 354 201 HOH HOH B . 
F 3 HOH 104 355 203 HOH HOH B . 
F 3 HOH 105 356 206 HOH HOH B . 
F 3 HOH 106 357 209 HOH HOH B . 
F 3 HOH 107 358 210 HOH HOH B . 
F 3 HOH 108 359 211 HOH HOH B . 
F 3 HOH 109 360 213 HOH HOH B . 
F 3 HOH 110 361 215 HOH HOH B . 
F 3 HOH 111 362 216 HOH HOH B . 
F 3 HOH 112 363 217 HOH HOH B . 
F 3 HOH 113 364 218 HOH HOH B . 
F 3 HOH 114 365 221 HOH HOH B . 
F 3 HOH 115 366 222 HOH HOH B . 
F 3 HOH 116 367 224 HOH HOH B . 
F 3 HOH 117 368 225 HOH HOH B . 
F 3 HOH 118 369 226 HOH HOH B . 
F 3 HOH 119 370 228 HOH HOH B . 
F 3 HOH 120 371 229 HOH HOH B . 
F 3 HOH 121 372 230 HOH HOH B . 
F 3 HOH 122 373 231 HOH HOH B . 
F 3 HOH 123 374 234 HOH HOH B . 
F 3 HOH 124 375 235 HOH HOH B . 
F 3 HOH 125 376 236 HOH HOH B . 
F 3 HOH 126 377 237 HOH HOH B . 
F 3 HOH 127 378 239 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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  OD1 ? A ASN 119 ? A ASN 119 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 253 ? 1_555 87.2  ? 
2  OD1 ? A ASN 119 ? A ASN 119 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 256 ? 1_555 171.4 ? 
3  O   ? E HOH .   ? A HOH 253 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 256 ? 1_555 90.4  ? 
4  OD1 ? A ASN 119 ? A ASN 119 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 254 ? 1_555 80.4  ? 
5  O   ? E HOH .   ? A HOH 253 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 254 ? 1_555 99.2  ? 
6  O   ? E HOH .   ? A HOH 256 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 254 ? 1_555 91.9  ? 
7  OD1 ? A ASN 119 ? A ASN 119 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 252 ? 1_555 96.2  ? 
8  O   ? E HOH .   ? A HOH 253 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 252 ? 1_555 102.9 ? 
9  O   ? E HOH .   ? A HOH 256 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 252 ? 1_555 92.4  ? 
10 O   ? E HOH .   ? A HOH 254 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 252 ? 1_555 157.5 ? 
11 OD1 ? A ASN 119 ? A ASN 119 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 255 ? 1_555 85.4  ? 
12 O   ? E HOH .   ? A HOH 253 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 255 ? 1_555 172.4 ? 
13 O   ? E HOH .   ? A HOH 256 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 255 ? 1_555 96.7  ? 
14 O   ? E HOH .   ? A HOH 254 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 255 ? 1_555 77.9  ? 
15 O   ? E HOH .   ? A HOH 252 ? 1_555 MG ? C MG . ? A MG 251 ? 1_555 O ? E HOH . ? A HOH 255 ? 1_555 79.7  ? 
16 OD1 ? B ASN 119 ? B ASN 119 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 255 ? 1_555 84.6  ? 
17 OD1 ? B ASN 119 ? B ASN 119 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 256 ? 1_555 177.3 ? 
18 O   ? F HOH .   ? B HOH 255 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 256 ? 1_555 95.4  ? 
19 OD1 ? B ASN 119 ? B ASN 119 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 252 ? 1_555 97.6  ? 
20 O   ? F HOH .   ? B HOH 255 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 252 ? 1_555 76.2  ? 
21 O   ? F HOH .   ? B HOH 256 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 252 ? 1_555 85.0  ? 
22 OD1 ? B ASN 119 ? B ASN 119 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 254 ? 1_555 83.7  ? 
23 O   ? F HOH .   ? B HOH 255 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 254 ? 1_555 82.7  ? 
24 O   ? F HOH .   ? B HOH 256 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 254 ? 1_555 93.6  ? 
25 O   ? F HOH .   ? B HOH 252 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 254 ? 1_555 158.6 ? 
26 OD1 ? B ASN 119 ? B ASN 119 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 253 ? 1_555 90.8  ? 
27 O   ? F HOH .   ? B HOH 255 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 253 ? 1_555 172.0 ? 
28 O   ? F HOH .   ? B HOH 256 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 253 ? 1_555 89.5  ? 
29 O   ? F HOH .   ? B HOH 252 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 253 ? 1_555 98.1  ? 
30 O   ? F HOH .   ? B HOH 254 ? 1_555 MG ? D MG . ? B MG 251 ? 1_555 O ? F HOH . ? B HOH 253 ? 1_555 103.3 ? 
# 
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 1999-05-18 
2 'Structure model' 1 1 2007-10-16 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-04 
# 
_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' 
3 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MADNESS  'data collection' .     ? 1 
PROCOR   'data scaling'    .     ? 2 
PROCOR   'data reduction'  .     ? 3 
XSCALE   'data scaling'    .     ? 4 
ARP/wARP 'model building'  .     ? 5 
X-PLOR   'model building'  3.851 ? 6 
X-PLOR   refinement        3.851 ? 7 
MADNESS  'data reduction'  .     ? 8 
X-PLOR   phasing           3.851 ? 9 
# 
_pdbx_entry_details.entry_id             1QAE 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;REFERENCE
  DATABASE: GENBANK
  ENTRY_NAME: SMANUCES
;
# 
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 ALA A 10  ? ? 68.14   -51.38 
2  1 LYS A 37  ? ? 83.81   6.74   
3  1 GLN A 90  ? ? -92.61  -63.22 
4  1 ALA A 97  ? ? -56.74  -2.38  
5  1 ASN A 177 ? ? 63.12   -99.62 
6  1 ALA B 10  ? ? 65.48   -47.09 
7  1 LYS B 37  ? ? 83.08   6.79   
8  1 ALA B 52  ? ? -170.52 134.28 
9  1 GLN B 90  ? ? -91.73  -62.54 
10 1 ASN B 177 ? ? 61.80   -95.88 
# 
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 ASP 1 ? A ASP 1 
2  1 Y 1 A THR 2 ? A THR 2 
3  1 Y 1 A LEU 3 ? A LEU 3 
4  1 Y 1 A GLU 4 ? A GLU 4 
5  1 Y 1 A SER 5 ? A SER 5 
6  1 Y 1 B ASP 1 ? B ASP 1 
7  1 Y 1 B THR 2 ? B THR 2 
8  1 Y 1 B LEU 3 ? B LEU 3 
9  1 Y 1 B GLU 4 ? B GLU 4 
10 1 Y 1 B SER 5 ? B SER 5 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION' MG  
3 water           HOH 
# 
