data_102L
# 
_entry.id   102L 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   102L         
WWPDB D_1000170005 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        102L 
_pdbx_database_status.recvd_initial_deposition_date   1992-09-29 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Heinz, D.W.'    1 
'Matthews, B.W.' 2 
# 
_citation.id                        primary 
_citation.title                     'How amino-acid insertions are allowed in an alpha-helix of T4 lysozyme.' 
_citation.journal_abbrev            Nature 
_citation.journal_volume            361 
_citation.page_first                561 
_citation.page_last                 564 
_citation.year                      1993 
_citation.journal_id_ASTM           NATUAS 
_citation.country                   UK 
_citation.journal_id_ISSN           0028-0836 
_citation.journal_id_CSD            0006 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   8429913 
_citation.pdbx_database_id_DOI      10.1038/361561a0 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Heinz, D.W.'     1 
primary 'Baase, W.A.'     2 
primary 'Dahlquist, F.W.' 3 
primary 'Matthews, B.W.'  4 
# 
_cell.entry_id           102L 
_cell.length_a           60.900 
_cell.length_b           60.900 
_cell.length_c           96.100 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_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                         102L 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_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 'T4 LYSOZYME'        18699.441 1   ? ? ? ? 
2 non-polymer syn 'CHLORIDE ION'       35.453    2   ? ? ? ? 
3 non-polymer syn BETA-MERCAPTOETHANOL 78.133    2   ? ? ? ? 
4 water       nat water                18.015    132 ? ? ? ? 
# 
_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       
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGIL
RNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWD
AYKNL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGIL
RNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWD
AYKNL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   ILE n 
1 4   PHE n 
1 5   GLU n 
1 6   MET n 
1 7   LEU n 
1 8   ARG n 
1 9   ILE n 
1 10  ASP n 
1 11  GLU n 
1 12  GLY n 
1 13  LEU n 
1 14  ARG n 
1 15  LEU n 
1 16  LYS n 
1 17  ILE n 
1 18  TYR n 
1 19  LYS n 
1 20  ASP n 
1 21  THR n 
1 22  GLU n 
1 23  GLY n 
1 24  TYR n 
1 25  TYR n 
1 26  THR n 
1 27  ILE n 
1 28  GLY n 
1 29  ILE n 
1 30  GLY n 
1 31  HIS n 
1 32  LEU n 
1 33  LEU n 
1 34  THR n 
1 35  LYS n 
1 36  SER n 
1 37  PRO n 
1 38  SER n 
1 39  LEU n 
1 40  ASN n 
1 41  ALA n 
1 42  ALA n 
1 43  ALA n 
1 44  LYS n 
1 45  SER n 
1 46  GLU n 
1 47  LEU n 
1 48  ASP n 
1 49  LYS n 
1 50  ALA n 
1 51  ILE n 
1 52  GLY n 
1 53  ARG n 
1 54  ASN n 
1 55  THR n 
1 56  ASN n 
1 57  GLY n 
1 58  VAL n 
1 59  ILE n 
1 60  THR n 
1 61  LYS n 
1 62  ASP n 
1 63  GLU n 
1 64  ALA n 
1 65  GLU n 
1 66  LYS n 
1 67  LEU n 
1 68  PHE n 
1 69  ASN n 
1 70  GLN n 
1 71  ASP n 
1 72  VAL n 
1 73  ASP n 
1 74  ALA n 
1 75  ALA n 
1 76  VAL n 
1 77  ARG n 
1 78  GLY n 
1 79  ILE n 
1 80  LEU n 
1 81  ARG n 
1 82  ASN n 
1 83  ALA n 
1 84  LYS n 
1 85  LEU n 
1 86  LYS n 
1 87  PRO n 
1 88  VAL n 
1 89  TYR n 
1 90  ASP n 
1 91  SER n 
1 92  LEU n 
1 93  ASP n 
1 94  ALA n 
1 95  VAL n 
1 96  ARG n 
1 97  ARG n 
1 98  ALA n 
1 99  ALA n 
1 100 LEU n 
1 101 ILE n 
1 102 ASN n 
1 103 MET n 
1 104 VAL n 
1 105 PHE n 
1 106 GLN n 
1 107 MET n 
1 108 GLY n 
1 109 GLU n 
1 110 THR n 
1 111 GLY n 
1 112 VAL n 
1 113 ALA n 
1 114 GLY n 
1 115 PHE n 
1 116 THR n 
1 117 ASN n 
1 118 SER n 
1 119 LEU n 
1 120 ARG n 
1 121 MET n 
1 122 LEU n 
1 123 GLN n 
1 124 GLN n 
1 125 LYS n 
1 126 ARG n 
1 127 TRP n 
1 128 ASP n 
1 129 GLU n 
1 130 ALA n 
1 131 ALA n 
1 132 VAL n 
1 133 ASN n 
1 134 LEU n 
1 135 ALA n 
1 136 LYS n 
1 137 SER n 
1 138 ARG n 
1 139 TRP n 
1 140 TYR n 
1 141 ASN n 
1 142 GLN n 
1 143 THR n 
1 144 PRO n 
1 145 ASN n 
1 146 ARG n 
1 147 ALA n 
1 148 LYS n 
1 149 ARG n 
1 150 VAL n 
1 151 ILE n 
1 152 THR n 
1 153 THR n 
1 154 PHE n 
1 155 ARG n 
1 156 THR n 
1 157 GLY n 
1 158 THR n 
1 159 TRP n 
1 160 ASP n 
1 161 ALA n 
1 162 TYR n 
1 163 LYS n 
1 164 ASN n 
1 165 LEU 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                     'T4-like viruses' 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   'Enterobacteria phage T4 sensu lato' 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Enterobacteria phage T4' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10665 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      ? 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       M13 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LYS_BPT4 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00720 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              102L 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 165 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00720 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  164 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       164 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 102L ALA A 41 A UNP P00720 ?   ?  INSERTION 40 1 
1 102L THR A 55 ? UNP P00720 CYS 54 CONFLICT  54 2 
1 102L ALA A 98 ? UNP P00720 CYS 97 CONFLICT  97 3 
# 
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 
BME non-polymer         . BETA-MERCAPTOETHANOL ? 'C2 H6 O S'      78.133  
CL  non-polymer         . 'CHLORIDE ION'       ? 'Cl -1'          35.453  
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 
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          102L 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.75 
_exptl_crystal.density_percent_sol   55.28 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 102L 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            1.74 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.174 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  
;RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES
ARE EXTREMELY MOBILE.  THUS THE COORDINATES FOR THESE
RESIDUES ARE VERY UNRELIABLE.  THIS ENTRY DOES NOT INCLUDE
RESIDUES 163 AND 164.
;
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_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.pdbx_overall_phase_error                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1297 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             132 
_refine_hist.number_atoms_total               1439 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        . 
# 
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 
t_bond_d           0.014 ? ? ? 'X-RAY DIFFRACTION' ? 
t_angle_deg        2.0   ? ? ? 'X-RAY DIFFRACTION' ? 
t_dihedral_angle_d ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_incorr_chiral_ct ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_pseud_angle      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_trig_c_planes    ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_gen_planes       ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_it               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
t_nbd              ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  102L 
_struct.title                     'HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME' 
_struct.pdbx_descriptor           
'LYSOZYME INSERTION MUTANT WITH ALA INSERTED AFTER ASN 40, CYS 54 REPLACED BY THR, CYS 97 REPLACED BY ALA (INS(N40-A), C54T,C97A)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        102L 
_struct_keywords.pdbx_keywords   'HYDROLASE(O-GLYCOSYL)' 
_struct_keywords.text            'HYDROLASE(O-GLYCOSYL)' 
# 
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 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  ASN A 2   ? GLY A 12  ? ASN A 2   GLY A 12  1 ? 11 
HELX_P HELX_P2  2  ALA A 41  A GLY A 52  ? ALA A 40  GLY A 51  1 ? 12 
HELX_P HELX_P3  3  THR A 60  ? ASN A 82  ? THR A 59  ASN A 81  1 ? 23 
HELX_P HELX_P4  4  LYS A 84  ? LEU A 92  ? LYS A 83  LEU A 91  1 ? 9  
HELX_P HELX_P5  5  ASP A 93  ? GLY A 108 ? ASP A 92  GLY A 107 1 ? 16 
HELX_P HELX_P6  6  MET A 107 ? GLY A 114 ? MET A 106 GLY A 113 1 ? 8  
HELX_P HELX_P7  7  PHE A 115 ? GLN A 124 ? PHE A 114 GLN A 123 1 ? 10 
HELX_P HELX_P8  8  ARG A 126 ? LYS A 136 ? ARG A 125 LYS A 135 1 ? 11 
HELX_P HELX_P9  9  SER A 137 ? THR A 143 ? SER A 136 THR A 142 1 ? 7  
HELX_P HELX_P10 10 THR A 143 ? GLY A 157 ? THR A 142 GLY A 156 1 ? 15 
HELX_P HELX_P11 11 TRP A 159 ? LYS A 163 ? TRP A 158 LYS A 162 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           D 
_struct_conn.ptnr1_label_comp_id           BME 
_struct_conn.ptnr1_label_seq_id            . 
_struct_conn.ptnr1_label_atom_id           S2 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           E 
_struct_conn.ptnr2_label_comp_id           BME 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           S2 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            BME 
_struct_conn.ptnr1_auth_seq_id             901 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            BME 
_struct_conn.ptnr2_auth_seq_id             902 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.988 
_struct_conn.pdbx_value_order              ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   3 
_struct_sheet.details          ? 
# 
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 
# 
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 ARG A 14 ? LYS A 19 ? ARG A 14 LYS A 19 
A 2 TYR A 25 ? GLY A 28 ? TYR A 25 GLY A 28 
A 3 HIS A 31 ? THR A 34 ? HIS A 31 THR A 34 
# 
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 O TYR A 18 ? O TYR A 18 N THR A 26 ? N THR A 26 
A 2 3 O ILE A 27 ? O ILE A 27 N HIS A 31 ? N HIS A 31 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CL A 173'  
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE CL A 178'  
AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE BME A 901' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE BME A 902' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5 THR A 143 ? THR A 142 . ? 1_555 ? 
2  AC1 5 ASN A 145 ? ASN A 144 . ? 1_555 ? 
3  AC1 5 ARG A 146 ? ARG A 145 . ? 1_555 ? 
4  AC1 5 HOH F .   ? HOH A 209 . ? 1_555 ? 
5  AC1 5 HOH F .   ? HOH A 291 . ? 4_655 ? 
6  AC2 3 LYS A 136 ? LYS A 135 . ? 3_665 ? 
7  AC2 3 HOH F .   ? HOH A 215 . ? 1_555 ? 
8  AC2 3 HOH F .   ? HOH A 220 . ? 3_665 ? 
9  AC3 2 ASP A 73  ? ASP A 72  . ? 5_555 ? 
10 AC3 2 BME E .   ? BME A 902 . ? 1_555 ? 
11 AC4 4 ASN A 69  ? ASN A 68  . ? 5_555 ? 
12 AC4 4 ALA A 94  ? ALA A 93  . ? 1_555 ? 
13 AC4 4 ILE A 101 ? ILE A 100 . ? 1_555 ? 
14 AC4 4 BME D .   ? BME A 901 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          102L 
_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                    102L 
_atom_sites.fract_transf_matrix[1][1]   0.016420 
_atom_sites.fract_transf_matrix[1][2]   0.009480 
_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]   0.018961 
_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]   0.010406 
_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_sites_footnote.id 
_atom_sites_footnote.text 
1 
;RESIDUES 162 - 164 IN WILD-TYPE AND ALL MUTANT LYSOZYMES ARE EXTREMELY MOBILE.  THUS THE COORDINATES FOR THESE RESIDUES ARE VERY UNRELIABLE.  THIS ENTRY DOES NOT INCLUDE RESIDUES 163 AND 164.
;
2 'SEO 901 FORMS AN S-S LINKAGE TO SEO 902.' 
# 
loop_
_atom_type.symbol 
C  
CL 
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   . MET A 1 1   ? 44.061 -3.277 8.755   1.00 22.03  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 43.619 -1.924 8.869   1.00 14.21  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 42.195 -1.991 9.394   1.00 18.00  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 41.523 -2.983 9.193   1.00 16.68  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 43.727 -1.353 7.458   1.00 17.98  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 42.994 -0.069 7.291   1.00 31.76  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 44.005 1.333  7.794   1.00 35.36  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 45.515 0.985  6.912   1.00 39.74  ? 1   MET A CE  1 
ATOM   9    N  N   . ASN A 1 2   ? 41.782 -0.980 10.131  1.00 11.26  ? 2   ASN A N   1 
ATOM   10   C  CA  . ASN A 1 2   ? 40.445 -0.876 10.670  1.00 9.77   ? 2   ASN A CA  1 
ATOM   11   C  C   . ASN A 1 2   ? 40.049 0.598  10.743  1.00 12.27  ? 2   ASN A C   1 
ATOM   12   O  O   . ASN A 1 2   ? 40.888 1.470  10.488  1.00 12.69  ? 2   ASN A O   1 
ATOM   13   C  CB  . ASN A 1 2   ? 40.325 -1.552 12.050  1.00 9.48   ? 2   ASN A CB  1 
ATOM   14   C  CG  . ASN A 1 2   ? 41.252 -0.970 13.055  1.00 15.18  ? 2   ASN A CG  1 
ATOM   15   O  OD1 . ASN A 1 2   ? 41.201 0.238  13.326  1.00 14.85  ? 2   ASN A OD1 1 
ATOM   16   N  ND2 . ASN A 1 2   ? 42.096 -1.839 13.600  1.00 12.08  ? 2   ASN A ND2 1 
ATOM   17   N  N   . ILE A 1 3   ? 38.797 0.867  11.127  1.00 10.41  ? 3   ILE A N   1 
ATOM   18   C  CA  . ILE A 1 3   ? 38.254 2.240  11.220  1.00 12.34  ? 3   ILE A CA  1 
ATOM   19   C  C   . ILE A 1 3   ? 39.087 3.218  12.033  1.00 11.77  ? 3   ILE A C   1 
ATOM   20   O  O   . ILE A 1 3   ? 39.242 4.402  11.649  1.00 11.80  ? 3   ILE A O   1 
ATOM   21   C  CB  . ILE A 1 3   ? 36.728 2.309  11.544  1.00 7.73   ? 3   ILE A CB  1 
ATOM   22   C  CG1 . ILE A 1 3   ? 36.147 3.735  11.342  1.00 10.50  ? 3   ILE A CG1 1 
ATOM   23   C  CG2 . ILE A 1 3   ? 36.422 1.775  12.964  1.00 7.84   ? 3   ILE A CG2 1 
ATOM   24   C  CD1 . ILE A 1 3   ? 36.389 4.347  9.944   1.00 6.51   ? 3   ILE A CD1 1 
ATOM   25   N  N   . PHE A 1 4   ? 39.579 2.751  13.181  1.00 7.52   ? 4   PHE A N   1 
ATOM   26   C  CA  . PHE A 1 4   ? 40.340 3.621  14.036  1.00 12.31  ? 4   PHE A CA  1 
ATOM   27   C  C   . PHE A 1 4   ? 41.630 4.016  13.379  1.00 15.51  ? 4   PHE A C   1 
ATOM   28   O  O   . PHE A 1 4   ? 42.032 5.160  13.445  1.00 14.87  ? 4   PHE A O   1 
ATOM   29   C  CB  . PHE A 1 4   ? 40.621 2.933  15.371  1.00 8.96   ? 4   PHE A CB  1 
ATOM   30   C  CG  . PHE A 1 4   ? 39.379 2.855  16.227  1.00 9.96   ? 4   PHE A CG  1 
ATOM   31   C  CD1 . PHE A 1 4   ? 39.073 3.907  17.101  1.00 15.69  ? 4   PHE A CD1 1 
ATOM   32   C  CD2 . PHE A 1 4   ? 38.518 1.751  16.206  1.00 12.68  ? 4   PHE A CD2 1 
ATOM   33   C  CE1 . PHE A 1 4   ? 37.914 3.872  17.879  1.00 10.88  ? 4   PHE A CE1 1 
ATOM   34   C  CE2 . PHE A 1 4   ? 37.354 1.718  16.979  1.00 14.17  ? 4   PHE A CE2 1 
ATOM   35   C  CZ  . PHE A 1 4   ? 37.059 2.771  17.845  1.00 13.15  ? 4   PHE A CZ  1 
ATOM   36   N  N   . GLU A 1 5   ? 42.313 3.039  12.797  1.00 10.64  ? 5   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 5   ? 43.586 3.293  12.110  1.00 13.83  ? 5   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 5   ? 43.359 4.133  10.909  1.00 16.78  ? 5   GLU A C   1 
ATOM   39   O  O   . GLU A 1 5   ? 44.141 4.992  10.620  1.00 15.29  ? 5   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 5   ? 44.253 1.987  11.668  1.00 12.62  ? 5   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 5   ? 44.624 1.030  12.827  1.00 20.04  ? 5   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 5   ? 45.297 -0.300 12.431  1.00 37.71  ? 5   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 5   ? 45.500 -0.641 11.262  1.00 42.95  ? 5   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 5   ? 45.773 -0.974 13.473  1.00 49.47  ? 5   GLU A OE2 1 
ATOM   45   N  N   . MET A 1 6   ? 42.271 3.898  10.223  1.00 11.52  ? 6   MET A N   1 
ATOM   46   C  CA  . MET A 1 6   ? 41.968 4.686  9.048   1.00 6.95   ? 6   MET A CA  1 
ATOM   47   C  C   . MET A 1 6   ? 41.759 6.148  9.439   1.00 19.45  ? 6   MET A C   1 
ATOM   48   O  O   . MET A 1 6   ? 42.311 7.077  8.827   1.00 13.48  ? 6   MET A O   1 
ATOM   49   C  CB  . MET A 1 6   ? 40.635 4.224  8.503   1.00 7.79   ? 6   MET A CB  1 
ATOM   50   C  CG  . MET A 1 6   ? 40.324 4.716  7.108   1.00 7.00   ? 6   MET A CG  1 
ATOM   51   S  SD  . MET A 1 6   ? 38.533 4.536  6.837   1.00 11.73  ? 6   MET A SD  1 
ATOM   52   C  CE  . MET A 1 6   ? 38.411 4.480  5.006   1.00 16.93  ? 6   MET A CE  1 
ATOM   53   N  N   . LEU A 1 7   ? 40.901 6.361  10.423  1.00 14.66  ? 7   LEU A N   1 
ATOM   54   C  CA  . LEU A 1 7   ? 40.631 7.752  10.830  1.00 13.95  ? 7   LEU A CA  1 
ATOM   55   C  C   . LEU A 1 7   ? 41.841 8.428  11.477  1.00 11.28  ? 7   LEU A C   1 
ATOM   56   O  O   . LEU A 1 7   ? 42.015 9.638  11.421  1.00 16.66  ? 7   LEU A O   1 
ATOM   57   C  CB  . LEU A 1 7   ? 39.432 7.834  11.746  1.00 8.48   ? 7   LEU A CB  1 
ATOM   58   C  CG  . LEU A 1 7   ? 38.123 7.896  10.989  1.00 9.83   ? 7   LEU A CG  1 
ATOM   59   C  CD1 . LEU A 1 7   ? 37.036 7.572  11.985  1.00 13.24  ? 7   LEU A CD1 1 
ATOM   60   C  CD2 . LEU A 1 7   ? 37.917 9.302  10.431  1.00 8.80   ? 7   LEU A CD2 1 
ATOM   61   N  N   . ARG A 1 8   ? 42.711 7.650  12.102  1.00 12.11  ? 8   ARG A N   1 
ATOM   62   C  CA  . ARG A 1 8   ? 43.896 8.220  12.718  1.00 10.01  ? 8   ARG A CA  1 
ATOM   63   C  C   . ARG A 1 8   ? 44.851 8.775  11.671  1.00 20.54  ? 8   ARG A C   1 
ATOM   64   O  O   . ARG A 1 8   ? 45.453 9.802  11.898  1.00 14.32  ? 8   ARG A O   1 
ATOM   65   C  CB  . ARG A 1 8   ? 44.536 7.355  13.764  1.00 16.50  ? 8   ARG A CB  1 
ATOM   66   C  CG  . ARG A 1 8   ? 45.960 7.773  14.115  1.00 23.96  ? 8   ARG A CG  1 
ATOM   67   C  CD  . ARG A 1 8   ? 46.080 8.683  15.336  1.00 40.52  ? 8   ARG A CD  1 
ATOM   68   N  NE  . ARG A 1 8   ? 47.473 8.999  15.693  1.00 58.50  ? 8   ARG A NE  1 
ATOM   69   C  CZ  . ARG A 1 8   ? 48.312 9.683  14.897  1.00 59.15  ? 8   ARG A CZ  1 
ATOM   70   N  NH1 . ARG A 1 8   ? 47.950 10.125 13.681  1.00 35.67  ? 8   ARG A NH1 1 
ATOM   71   N  NH2 . ARG A 1 8   ? 49.551 9.918  15.329  1.00 100.00 ? 8   ARG A NH2 1 
ATOM   72   N  N   . ILE A 1 9   ? 44.882 8.144  10.504  1.00 12.16  ? 9   ILE A N   1 
ATOM   73   C  CA  . ILE A 1 9   ? 45.665 8.595  9.364   1.00 11.08  ? 9   ILE A CA  1 
ATOM   74   C  C   . ILE A 1 9   ? 45.034 9.856  8.758   1.00 22.81  ? 9   ILE A C   1 
ATOM   75   O  O   . ILE A 1 9   ? 45.707 10.815 8.449   1.00 16.55  ? 9   ILE A O   1 
ATOM   76   C  CB  . ILE A 1 9   ? 45.770 7.486  8.314   1.00 13.53  ? 9   ILE A CB  1 
ATOM   77   C  CG1 . ILE A 1 9   ? 46.780 6.430  8.797   1.00 14.69  ? 9   ILE A CG1 1 
ATOM   78   C  CG2 . ILE A 1 9   ? 46.196 8.090  6.974   1.00 11.41  ? 9   ILE A CG2 1 
ATOM   79   C  CD1 . ILE A 1 9   ? 46.593 5.086  8.102   1.00 15.90  ? 9   ILE A CD1 1 
ATOM   80   N  N   . ASP A 1 10  ? 43.716 9.893  8.630   1.00 10.87  ? 10  ASP A N   1 
ATOM   81   C  CA  . ASP A 1 10  ? 43.019 11.005 8.031   1.00 10.92  ? 10  ASP A CA  1 
ATOM   82   C  C   . ASP A 1 10  ? 42.991 12.293 8.849   1.00 13.58  ? 10  ASP A C   1 
ATOM   83   O  O   . ASP A 1 10  ? 43.058 13.386 8.327   1.00 16.13  ? 10  ASP A O   1 
ATOM   84   C  CB  . ASP A 1 10  ? 41.618 10.612 7.575   1.00 12.37  ? 10  ASP A CB  1 
ATOM   85   C  CG  . ASP A 1 10  ? 41.678 9.831  6.281   1.00 14.52  ? 10  ASP A CG  1 
ATOM   86   O  OD1 . ASP A 1 10  ? 42.584 9.953  5.475   1.00 15.75  ? 10  ASP A OD1 1 
ATOM   87   O  OD2 . ASP A 1 10  ? 40.668 9.030  6.097   1.00 16.98  ? 10  ASP A OD2 1 
ATOM   88   N  N   . GLU A 1 11  ? 42.896 12.141 10.143  1.00 12.00  ? 11  GLU A N   1 
ATOM   89   C  CA  . GLU A 1 11  ? 42.781 13.282 11.034  1.00 19.67  ? 11  GLU A CA  1 
ATOM   90   C  C   . GLU A 1 11  ? 44.046 13.712 11.758  1.00 19.51  ? 11  GLU A C   1 
ATOM   91   O  O   . GLU A 1 11  ? 44.106 14.857 12.188  1.00 18.69  ? 11  GLU A O   1 
ATOM   92   C  CB  . GLU A 1 11  ? 41.739 12.927 12.097  1.00 10.12  ? 11  GLU A CB  1 
ATOM   93   C  CG  . GLU A 1 11  ? 40.404 12.639 11.422  1.00 13.57  ? 11  GLU A CG  1 
ATOM   94   C  CD  . GLU A 1 11  ? 39.651 13.846 10.902  1.00 25.40  ? 11  GLU A CD  1 
ATOM   95   O  OE1 . GLU A 1 11  ? 40.224 14.997 11.170  1.00 26.26  ? 11  GLU A OE1 1 
ATOM   96   O  OE2 . GLU A 1 11  ? 38.594 13.734 10.303  1.00 22.37  ? 11  GLU A OE2 1 
ATOM   97   N  N   . GLY A 1 12  ? 44.981 12.764 11.978  1.00 14.65  ? 12  GLY A N   1 
ATOM   98   C  CA  . GLY A 1 12  ? 46.223 12.976 12.716  1.00 13.81  ? 12  GLY A CA  1 
ATOM   99   C  C   . GLY A 1 12  ? 45.927 13.089 14.206  1.00 21.33  ? 12  GLY A C   1 
ATOM   100  O  O   . GLY A 1 12  ? 44.819 12.814 14.633  1.00 18.51  ? 12  GLY A O   1 
ATOM   101  N  N   . LEU A 1 13  ? 46.908 13.466 15.020  1.00 16.15  ? 13  LEU A N   1 
ATOM   102  C  CA  . LEU A 1 13  ? 46.704 13.623 16.478  1.00 12.68  ? 13  LEU A CA  1 
ATOM   103  C  C   . LEU A 1 13  ? 47.348 14.915 16.937  1.00 28.41  ? 13  LEU A C   1 
ATOM   104  O  O   . LEU A 1 13  ? 48.555 15.086 16.766  1.00 32.04  ? 13  LEU A O   1 
ATOM   105  C  CB  . LEU A 1 13  ? 47.430 12.502 17.209  1.00 24.50  ? 13  LEU A CB  1 
ATOM   106  C  CG  . LEU A 1 13  ? 47.503 12.663 18.717  1.00 31.12  ? 13  LEU A CG  1 
ATOM   107  C  CD1 . LEU A 1 13  ? 46.084 12.751 19.249  1.00 33.16  ? 13  LEU A CD1 1 
ATOM   108  C  CD2 . LEU A 1 13  ? 48.128 11.380 19.256  1.00 45.36  ? 13  LEU A CD2 1 
ATOM   109  N  N   . ARG A 1 14  ? 46.579 15.802 17.550  1.00 26.84  ? 14  ARG A N   1 
ATOM   110  C  CA  . ARG A 1 14  ? 47.115 17.067 18.073  1.00 23.06  ? 14  ARG A CA  1 
ATOM   111  C  C   . ARG A 1 14  ? 46.685 17.208 19.483  1.00 21.62  ? 14  ARG A C   1 
ATOM   112  O  O   . ARG A 1 14  ? 45.523 17.030 19.772  1.00 19.06  ? 14  ARG A O   1 
ATOM   113  C  CB  . ARG A 1 14  ? 46.725 18.264 17.238  1.00 21.69  ? 14  ARG A CB  1 
ATOM   114  C  CG  . ARG A 1 14  ? 47.322 17.982 15.877  1.00 24.04  ? 14  ARG A CG  1 
ATOM   115  C  CD  . ARG A 1 14  ? 47.571 19.169 14.983  1.00 36.55  ? 14  ARG A CD  1 
ATOM   116  N  NE  . ARG A 1 14  ? 48.487 20.157 15.532  1.00 48.24  ? 14  ARG A NE  1 
ATOM   117  C  CZ  . ARG A 1 14  ? 48.493 21.393 15.035  1.00 100.00 ? 14  ARG A CZ  1 
ATOM   118  N  NH1 . ARG A 1 14  ? 47.668 21.734 14.027  1.00 38.57  ? 14  ARG A NH1 1 
ATOM   119  N  NH2 . ARG A 1 14  ? 49.332 22.302 15.539  1.00 100.00 ? 14  ARG A NH2 1 
ATOM   120  N  N   . LEU A 1 15  ? 47.645 17.453 20.351  1.00 17.62  ? 15  LEU A N   1 
ATOM   121  C  CA  . LEU A 1 15  ? 47.385 17.573 21.767  1.00 22.79  ? 15  LEU A CA  1 
ATOM   122  C  C   . LEU A 1 15  ? 47.102 19.000 22.245  1.00 32.69  ? 15  LEU A C   1 
ATOM   123  O  O   . LEU A 1 15  ? 46.841 19.224 23.434  1.00 28.86  ? 15  LEU A O   1 
ATOM   124  C  CB  . LEU A 1 15  ? 48.486 16.923 22.603  1.00 19.64  ? 15  LEU A CB  1 
ATOM   125  C  CG  . LEU A 1 15  ? 48.644 15.425 22.358  1.00 26.11  ? 15  LEU A CG  1 
ATOM   126  C  CD1 . LEU A 1 15  ? 49.676 14.882 23.315  1.00 30.63  ? 15  LEU A CD1 1 
ATOM   127  C  CD2 . LEU A 1 15  ? 47.326 14.688 22.579  1.00 23.42  ? 15  LEU A CD2 1 
ATOM   128  N  N   . LYS A 1 16  ? 47.147 19.961 21.338  1.00 16.18  ? 16  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 16  ? 46.886 21.354 21.690  1.00 26.29  ? 16  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 16  ? 45.745 21.807 20.834  1.00 18.81  ? 16  LYS A C   1 
ATOM   131  O  O   . LYS A 1 16  ? 45.561 21.212 19.759  1.00 32.69  ? 16  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 16  ? 48.141 22.221 21.488  1.00 27.01  ? 16  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 16  ? 47.929 23.708 21.708  1.00 52.28  ? 16  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 16  ? 48.169 24.162 23.149  1.00 100.00 ? 16  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 16  ? 46.903 24.656 23.872  1.00 100.00 ? 16  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 16  ? 46.855 26.123 24.145  1.00 100.00 ? 16  LYS A NZ  1 
ATOM   137  N  N   . ILE A 1 17  ? 44.928 22.778 21.299  1.00 20.42  ? 17  ILE A N   1 
ATOM   138  C  CA  . ILE A 1 17  ? 43.804 23.226 20.475  1.00 13.98  ? 17  ILE A CA  1 
ATOM   139  C  C   . ILE A 1 17  ? 44.345 23.696 19.135  1.00 38.21  ? 17  ILE A C   1 
ATOM   140  O  O   . ILE A 1 17  ? 45.371 24.393 19.132  1.00 21.64  ? 17  ILE A O   1 
ATOM   141  C  CB  . ILE A 1 17  ? 42.958 24.331 21.146  1.00 20.71  ? 17  ILE A CB  1 
ATOM   142  C  CG1 . ILE A 1 17  ? 42.258 23.734 22.379  1.00 28.04  ? 17  ILE A CG1 1 
ATOM   143  C  CG2 . ILE A 1 17  ? 41.910 24.958 20.195  1.00 19.24  ? 17  ILE A CG2 1 
ATOM   144  C  CD1 . ILE A 1 17  ? 41.342 24.732 23.071  1.00 26.92  ? 17  ILE A CD1 1 
ATOM   145  N  N   . TYR A 1 18  ? 43.687 23.335 18.033  1.00 19.70  ? 18  TYR A N   1 
ATOM   146  C  CA  . TYR A 1 18  ? 44.164 23.752 16.739  1.00 15.71  ? 18  TYR A CA  1 
ATOM   147  C  C   . TYR A 1 18  ? 42.987 24.124 15.865  1.00 17.89  ? 18  TYR A C   1 
ATOM   148  O  O   . TYR A 1 18  ? 41.838 23.868 16.226  1.00 24.51  ? 18  TYR A O   1 
ATOM   149  C  CB  . TYR A 1 18  ? 45.073 22.698 16.091  1.00 20.98  ? 18  TYR A CB  1 
ATOM   150  C  CG  . TYR A 1 18  ? 44.351 21.434 15.660  1.00 40.94  ? 18  TYR A CG  1 
ATOM   151  C  CD1 . TYR A 1 18  ? 44.200 20.358 16.543  1.00 17.72  ? 18  TYR A CD1 1 
ATOM   152  C  CD2 . TYR A 1 18  ? 43.861 21.294 14.356  1.00 34.27  ? 18  TYR A CD2 1 
ATOM   153  C  CE1 . TYR A 1 18  ? 43.558 19.185 16.132  1.00 36.09  ? 18  TYR A CE1 1 
ATOM   154  C  CE2 . TYR A 1 18  ? 43.246 20.114 13.916  1.00 27.96  ? 18  TYR A CE2 1 
ATOM   155  C  CZ  . TYR A 1 18  ? 43.054 19.081 14.830  1.00 24.67  ? 18  TYR A CZ  1 
ATOM   156  O  OH  . TYR A 1 18  ? 42.452 17.938 14.408  1.00 35.50  ? 18  TYR A OH  1 
ATOM   157  N  N   . LYS A 1 19  ? 43.244 24.712 14.715  1.00 18.57  ? 19  LYS A N   1 
ATOM   158  C  CA  . LYS A 1 19  ? 42.151 25.009 13.828  1.00 18.39  ? 19  LYS A CA  1 
ATOM   159  C  C   . LYS A 1 19  ? 42.113 23.991 12.712  1.00 42.60  ? 19  LYS A C   1 
ATOM   160  O  O   . LYS A 1 19  ? 43.152 23.687 12.122  1.00 22.60  ? 19  LYS A O   1 
ATOM   161  C  CB  . LYS A 1 19  ? 42.309 26.331 13.191  1.00 32.22  ? 19  LYS A CB  1 
ATOM   162  C  CG  . LYS A 1 19  ? 42.133 27.447 14.162  1.00 23.27  ? 19  LYS A CG  1 
ATOM   163  C  CD  . LYS A 1 19  ? 41.653 28.683 13.441  1.00 56.93  ? 19  LYS A CD  1 
ATOM   164  C  CE  . LYS A 1 19  ? 42.199 29.982 14.019  1.00 35.81  ? 19  LYS A CE  1 
ATOM   165  N  NZ  . LYS A 1 19  ? 41.540 31.177 13.457  1.00 100.00 ? 19  LYS A NZ  1 
ATOM   166  N  N   . ASP A 1 20  ? 40.908 23.490 12.396  1.00 26.75  ? 20  ASP A N   1 
ATOM   167  C  CA  . ASP A 1 20  ? 40.819 22.532 11.321  1.00 21.10  ? 20  ASP A CA  1 
ATOM   168  C  C   . ASP A 1 20  ? 40.935 23.185 9.922   1.00 29.11  ? 20  ASP A C   1 
ATOM   169  O  O   . ASP A 1 20  ? 41.140 24.381 9.818   1.00 28.77  ? 20  ASP A O   1 
ATOM   170  C  CB  . ASP A 1 20  ? 39.698 21.530 11.528  1.00 16.04  ? 20  ASP A CB  1 
ATOM   171  C  CG  . ASP A 1 20  ? 38.340 22.048 11.206  1.00 21.96  ? 20  ASP A CG  1 
ATOM   172  O  OD1 . ASP A 1 20  ? 38.305 23.268 10.836  1.00 22.80  ? 20  ASP A OD1 1 
ATOM   173  O  OD2 . ASP A 1 20  ? 37.355 21.394 11.310  1.00 30.14  ? 20  ASP A OD2 1 
ATOM   174  N  N   . THR A 1 21  ? 40.813 22.409 8.859   1.00 25.15  ? 21  THR A N   1 
ATOM   175  C  CA  . THR A 1 21  ? 40.919 22.897 7.481   1.00 25.90  ? 21  THR A CA  1 
ATOM   176  C  C   . THR A 1 21  ? 39.936 23.993 7.146   1.00 50.89  ? 21  THR A C   1 
ATOM   177  O  O   . THR A 1 21  ? 40.126 24.696 6.129   1.00 44.17  ? 21  THR A O   1 
ATOM   178  C  CB  . THR A 1 21  ? 40.733 21.750 6.458   1.00 37.26  ? 21  THR A CB  1 
ATOM   179  O  OG1 . THR A 1 21  ? 39.363 21.578 6.215   1.00 49.93  ? 21  THR A OG1 1 
ATOM   180  C  CG2 . THR A 1 21  ? 41.304 20.423 7.009   1.00 47.37  ? 21  THR A CG2 1 
ATOM   181  N  N   . GLU A 1 22  ? 38.873 24.073 7.985   1.00 28.42  ? 22  GLU A N   1 
ATOM   182  C  CA  . GLU A 1 22  ? 37.772 25.046 7.840   1.00 26.89  ? 22  GLU A CA  1 
ATOM   183  C  C   . GLU A 1 22  ? 37.895 26.196 8.815   1.00 31.73  ? 22  GLU A C   1 
ATOM   184  O  O   . GLU A 1 22  ? 36.988 27.006 8.871   1.00 33.99  ? 22  GLU A O   1 
ATOM   185  C  CB  . GLU A 1 22  ? 36.401 24.450 8.091   1.00 21.74  ? 22  GLU A CB  1 
ATOM   186  C  CG  . GLU A 1 22  ? 36.046 23.272 7.172   1.00 52.16  ? 22  GLU A CG  1 
ATOM   187  C  CD  . GLU A 1 22  ? 35.630 23.705 5.801   1.00 57.07  ? 22  GLU A CD  1 
ATOM   188  O  OE1 . GLU A 1 22  ? 35.024 24.866 5.825   1.00 54.28  ? 22  GLU A OE1 1 
ATOM   189  O  OE2 . GLU A 1 22  ? 35.845 23.040 4.793   1.00 69.63  ? 22  GLU A OE2 1 
ATOM   190  N  N   . GLY A 1 23  ? 39.004 26.187 9.603   1.00 24.52  ? 23  GLY A N   1 
ATOM   191  C  CA  . GLY A 1 23  ? 39.361 27.176 10.603  1.00 18.51  ? 23  GLY A CA  1 
ATOM   192  C  C   . GLY A 1 23  ? 38.657 27.000 11.940  1.00 46.51  ? 23  GLY A C   1 
ATOM   193  O  O   . GLY A 1 23  ? 38.613 27.946 12.722  1.00 30.99  ? 23  GLY A O   1 
ATOM   194  N  N   . TYR A 1 24  ? 38.099 25.809 12.208  1.00 27.73  ? 24  TYR A N   1 
ATOM   195  C  CA  . TYR A 1 24  ? 37.450 25.619 13.492  1.00 16.73  ? 24  TYR A CA  1 
ATOM   196  C  C   . TYR A 1 24  ? 38.357 24.994 14.477  1.00 27.94  ? 24  TYR A C   1 
ATOM   197  O  O   . TYR A 1 24  ? 39.261 24.200 14.161  1.00 19.90  ? 24  TYR A O   1 
ATOM   198  C  CB  . TYR A 1 24  ? 36.223 24.752 13.483  1.00 18.23  ? 24  TYR A CB  1 
ATOM   199  C  CG  . TYR A 1 24  ? 35.246 25.262 12.506  1.00 51.24  ? 24  TYR A CG  1 
ATOM   200  C  CD1 . TYR A 1 24  ? 34.925 26.617 12.473  1.00 36.28  ? 24  TYR A CD1 1 
ATOM   201  C  CD2 . TYR A 1 24  ? 34.625 24.374 11.629  1.00 25.92  ? 24  TYR A CD2 1 
ATOM   202  C  CE1 . TYR A 1 24  ? 33.980 27.084 11.555  1.00 100.00 ? 24  TYR A CE1 1 
ATOM   203  C  CE2 . TYR A 1 24  ? 33.698 24.838 10.695  1.00 35.38  ? 24  TYR A CE2 1 
ATOM   204  C  CZ  . TYR A 1 24  ? 33.377 26.197 10.661  1.00 62.34  ? 24  TYR A CZ  1 
ATOM   205  O  OH  . TYR A 1 24  ? 32.457 26.659 9.740   1.00 65.81  ? 24  TYR A OH  1 
ATOM   206  N  N   . TYR A 1 25  ? 38.023 25.322 15.694  1.00 17.66  ? 25  TYR A N   1 
ATOM   207  C  CA  . TYR A 1 25  ? 38.755 24.848 16.827  1.00 18.84  ? 25  TYR A CA  1 
ATOM   208  C  C   . TYR A 1 25  ? 38.447 23.381 17.067  1.00 17.86  ? 25  TYR A C   1 
ATOM   209  O  O   . TYR A 1 25  ? 37.269 22.991 17.244  1.00 17.69  ? 25  TYR A O   1 
ATOM   210  C  CB  . TYR A 1 25  ? 38.347 25.722 17.996  1.00 32.98  ? 25  TYR A CB  1 
ATOM   211  C  CG  . TYR A 1 25  ? 39.027 27.054 17.899  1.00 56.48  ? 25  TYR A CG  1 
ATOM   212  C  CD1 . TYR A 1 25  ? 40.419 27.148 17.777  1.00 32.62  ? 25  TYR A CD1 1 
ATOM   213  C  CD2 . TYR A 1 25  ? 38.274 28.229 17.919  1.00 35.75  ? 25  TYR A CD2 1 
ATOM   214  C  CE1 . TYR A 1 25  ? 41.050 28.390 17.642  1.00 68.36  ? 25  TYR A CE1 1 
ATOM   215  C  CE2 . TYR A 1 25  ? 38.889 29.482 17.871  1.00 29.80  ? 25  TYR A CE2 1 
ATOM   216  C  CZ  . TYR A 1 25  ? 40.281 29.560 17.731  1.00 40.93  ? 25  TYR A CZ  1 
ATOM   217  O  OH  . TYR A 1 25  ? 40.870 30.813 17.730  1.00 38.41  ? 25  TYR A OH  1 
ATOM   218  N  N   . THR A 1 26  ? 39.544 22.623 17.066  1.00 16.68  ? 26  THR A N   1 
ATOM   219  C  CA  . THR A 1 26  ? 39.562 21.186 17.188  1.00 20.26  ? 26  THR A CA  1 
ATOM   220  C  C   . THR A 1 26  ? 40.676 20.812 18.127  1.00 22.77  ? 26  THR A C   1 
ATOM   221  O  O   . THR A 1 26  ? 41.578 21.597 18.433  1.00 16.17  ? 26  THR A O   1 
ATOM   222  C  CB  . THR A 1 26  ? 39.845 20.670 15.734  1.00 17.99  ? 26  THR A CB  1 
ATOM   223  O  OG1 . THR A 1 26  ? 38.853 21.192 14.871  1.00 20.26  ? 26  THR A OG1 1 
ATOM   224  C  CG2 . THR A 1 26  ? 39.883 19.158 15.549  1.00 12.09  ? 26  THR A CG2 1 
ATOM   225  N  N   . ILE A 1 27  ? 40.653 19.572 18.551  1.00 15.85  ? 27  ILE A N   1 
ATOM   226  C  CA  . ILE A 1 27  ? 41.730 19.014 19.350  1.00 23.82  ? 27  ILE A CA  1 
ATOM   227  C  C   . ILE A 1 27  ? 41.729 17.489 19.107  1.00 17.09  ? 27  ILE A C   1 
ATOM   228  O  O   . ILE A 1 27  ? 40.796 16.971 18.532  1.00 17.56  ? 27  ILE A O   1 
ATOM   229  C  CB  . ILE A 1 27  ? 41.677 19.397 20.855  1.00 26.09  ? 27  ILE A CB  1 
ATOM   230  C  CG1 . ILE A 1 27  ? 43.025 19.251 21.604  1.00 20.12  ? 27  ILE A CG1 1 
ATOM   231  C  CG2 . ILE A 1 27  ? 40.566 18.565 21.484  1.00 23.11  ? 27  ILE A CG2 1 
ATOM   232  C  CD1 . ILE A 1 27  ? 43.111 20.016 22.912  1.00 28.34  ? 27  ILE A CD1 1 
ATOM   233  N  N   . GLY A 1 28  ? 42.802 16.834 19.498  1.00 16.93  ? 28  GLY A N   1 
ATOM   234  C  CA  . GLY A 1 28  ? 42.992 15.394 19.468  1.00 15.97  ? 28  GLY A CA  1 
ATOM   235  C  C   . GLY A 1 28  ? 42.965 14.815 18.104  1.00 21.48  ? 28  GLY A C   1 
ATOM   236  O  O   . GLY A 1 28  ? 43.757 15.202 17.265  1.00 15.60  ? 28  GLY A O   1 
ATOM   237  N  N   . ILE A 1 29  ? 42.085 13.857 17.930  1.00 15.02  ? 29  ILE A N   1 
ATOM   238  C  CA  . ILE A 1 29  ? 41.983 13.190 16.647  1.00 11.34  ? 29  ILE A CA  1 
ATOM   239  C  C   . ILE A 1 29  ? 40.732 13.617 15.912  1.00 12.88  ? 29  ILE A C   1 
ATOM   240  O  O   . ILE A 1 29  ? 39.738 12.896 15.784  1.00 16.81  ? 29  ILE A O   1 
ATOM   241  C  CB  . ILE A 1 29  ? 42.061 11.683 16.808  1.00 16.78  ? 29  ILE A CB  1 
ATOM   242  C  CG1 . ILE A 1 29  ? 43.440 11.325 17.392  1.00 23.39  ? 29  ILE A CG1 1 
ATOM   243  C  CG2 . ILE A 1 29  ? 41.859 11.056 15.420  1.00 13.32  ? 29  ILE A CG2 1 
ATOM   244  C  CD1 . ILE A 1 29  ? 43.432 10.032 18.203  1.00 21.19  ? 29  ILE A CD1 1 
ATOM   245  N  N   . GLY A 1 30  ? 40.755 14.845 15.441  1.00 13.62  ? 30  GLY A N   1 
ATOM   246  C  CA  . GLY A 1 30  ? 39.630 15.363 14.702  1.00 10.89  ? 30  GLY A CA  1 
ATOM   247  C  C   . GLY A 1 30  ? 38.420 15.665 15.571  1.00 19.05  ? 30  GLY A C   1 
ATOM   248  O  O   . GLY A 1 30  ? 37.325 15.715 15.060  1.00 19.04  ? 30  GLY A O   1 
ATOM   249  N  N   . HIS A 1 31  ? 38.582 15.943 16.864  1.00 13.56  ? 31  HIS A N   1 
ATOM   250  C  CA  . HIS A 1 31  ? 37.412 16.245 17.671  1.00 11.73  ? 31  HIS A CA  1 
ATOM   251  C  C   . HIS A 1 31  ? 37.012 17.733 17.566  1.00 13.00  ? 31  HIS A C   1 
ATOM   252  O  O   . HIS A 1 31  ? 37.664 18.566 18.200  1.00 15.78  ? 31  HIS A O   1 
ATOM   253  C  CB  . HIS A 1 31  ? 37.686 15.918 19.172  1.00 8.42   ? 31  HIS A CB  1 
ATOM   254  C  CG  . HIS A 1 31  ? 36.418 16.124 19.997  1.00 14.31  ? 31  HIS A CG  1 
ATOM   255  N  ND1 . HIS A 1 31  ? 35.339 15.217 19.985  1.00 16.57  ? 31  HIS A ND1 1 
ATOM   256  C  CD2 . HIS A 1 31  ? 36.067 17.149 20.834  1.00 19.90  ? 31  HIS A CD2 1 
ATOM   257  C  CE1 . HIS A 1 31  ? 34.411 15.691 20.790  1.00 12.02  ? 31  HIS A CE1 1 
ATOM   258  N  NE2 . HIS A 1 31  ? 34.817 16.842 21.335  1.00 13.20  ? 31  HIS A NE2 1 
ATOM   259  N  N   . LEU A 1 32  ? 35.944 18.072 16.853  1.00 14.70  ? 32  LEU A N   1 
ATOM   260  C  CA  . LEU A 1 32  ? 35.576 19.474 16.738  1.00 21.27  ? 32  LEU A CA  1 
ATOM   261  C  C   . LEU A 1 32  ? 35.110 20.070 18.055  1.00 17.96  ? 32  LEU A C   1 
ATOM   262  O  O   . LEU A 1 32  ? 34.293 19.484 18.768  1.00 23.59  ? 32  LEU A O   1 
ATOM   263  C  CB  . LEU A 1 32  ? 34.483 19.655 15.709  1.00 24.96  ? 32  LEU A CB  1 
ATOM   264  C  CG  . LEU A 1 32  ? 33.809 21.021 15.883  1.00 37.08  ? 32  LEU A CG  1 
ATOM   265  C  CD1 . LEU A 1 32  ? 34.716 22.128 15.321  1.00 29.79  ? 32  LEU A CD1 1 
ATOM   266  C  CD2 . LEU A 1 32  ? 32.493 21.024 15.144  1.00 32.18  ? 32  LEU A CD2 1 
ATOM   267  N  N   . LEU A 1 33  ? 35.614 21.219 18.415  1.00 18.72  ? 33  LEU A N   1 
ATOM   268  C  CA  . LEU A 1 33  ? 35.164 21.764 19.676  1.00 20.97  ? 33  LEU A CA  1 
ATOM   269  C  C   . LEU A 1 33  ? 34.032 22.737 19.503  1.00 41.75  ? 33  LEU A C   1 
ATOM   270  O  O   . LEU A 1 33  ? 32.991 22.672 20.171  1.00 27.34  ? 33  LEU A O   1 
ATOM   271  C  CB  . LEU A 1 33  ? 36.311 22.445 20.429  1.00 13.76  ? 33  LEU A CB  1 
ATOM   272  C  CG  . LEU A 1 33  ? 37.266 21.410 20.982  1.00 19.34  ? 33  LEU A CG  1 
ATOM   273  C  CD1 . LEU A 1 33  ? 38.555 22.130 21.302  1.00 19.06  ? 33  LEU A CD1 1 
ATOM   274  C  CD2 . LEU A 1 33  ? 36.698 20.851 22.272  1.00 15.40  ? 33  LEU A CD2 1 
ATOM   275  N  N   . THR A 1 34  ? 34.266 23.645 18.590  1.00 22.36  ? 34  THR A N   1 
ATOM   276  C  CA  . THR A 1 34  ? 33.301 24.679 18.367  1.00 44.00  ? 34  THR A CA  1 
ATOM   277  C  C   . THR A 1 34  ? 33.559 25.307 17.052  1.00 45.76  ? 34  THR A C   1 
ATOM   278  O  O   . THR A 1 34  ? 34.697 25.346 16.597  1.00 31.22  ? 34  THR A O   1 
ATOM   279  C  CB  . THR A 1 34  ? 33.444 25.783 19.483  1.00 35.75  ? 34  THR A CB  1 
ATOM   280  O  OG1 . THR A 1 34  ? 32.376 26.698 19.491  1.00 32.90  ? 34  THR A OG1 1 
ATOM   281  C  CG2 . THR A 1 34  ? 34.762 26.563 19.415  1.00 20.37  ? 34  THR A CG2 1 
ATOM   282  N  N   . LYS A 1 35  ? 32.501 25.849 16.494  1.00 24.25  ? 35  LYS A N   1 
ATOM   283  C  CA  . LYS A 1 35  ? 32.574 26.565 15.243  1.00 42.63  ? 35  LYS A CA  1 
ATOM   284  C  C   . LYS A 1 35  ? 32.811 28.058 15.481  1.00 64.06  ? 35  LYS A C   1 
ATOM   285  O  O   . LYS A 1 35  ? 33.171 28.779 14.559  1.00 57.09  ? 35  LYS A O   1 
ATOM   286  C  CB  . LYS A 1 35  ? 31.353 26.311 14.391  1.00 34.49  ? 35  LYS A CB  1 
ATOM   287  C  CG  . LYS A 1 35  ? 31.160 24.811 14.132  1.00 39.32  ? 35  LYS A CG  1 
ATOM   288  C  CD  . LYS A 1 35  ? 30.230 24.508 12.965  1.00 39.85  ? 35  LYS A CD  1 
ATOM   289  C  CE  . LYS A 1 35  ? 30.173 23.040 12.532  1.00 100.00 ? 35  LYS A CE  1 
ATOM   290  N  NZ  . LYS A 1 35  ? 28.965 22.679 11.760  1.00 100.00 ? 35  LYS A NZ  1 
ATOM   291  N  N   . SER A 1 36  ? 32.647 28.482 16.750  1.00 48.05  ? 36  SER A N   1 
ATOM   292  C  CA  . SER A 1 36  ? 32.831 29.863 17.244  1.00 100.00 ? 36  SER A CA  1 
ATOM   293  C  C   . SER A 1 36  ? 34.270 30.363 17.150  1.00 51.92  ? 36  SER A C   1 
ATOM   294  O  O   . SER A 1 36  ? 35.239 29.634 17.356  1.00 34.57  ? 36  SER A O   1 
ATOM   295  C  CB  . SER A 1 36  ? 32.263 30.099 18.656  1.00 53.85  ? 36  SER A CB  1 
ATOM   296  O  OG  . SER A 1 36  ? 33.084 30.962 19.427  1.00 86.01  ? 36  SER A OG  1 
ATOM   297  N  N   . PRO A 1 37  ? 34.411 31.645 16.853  1.00 100.00 ? 37  PRO A N   1 
ATOM   298  C  CA  . PRO A 1 37  ? 35.715 32.247 16.702  1.00 88.71  ? 37  PRO A CA  1 
ATOM   299  C  C   . PRO A 1 37  ? 36.445 32.546 18.008  1.00 82.14  ? 37  PRO A C   1 
ATOM   300  O  O   . PRO A 1 37  ? 37.608 32.955 18.010  1.00 89.87  ? 37  PRO A O   1 
ATOM   301  C  CB  . PRO A 1 37  ? 35.496 33.521 15.905  1.00 54.39  ? 37  PRO A CB  1 
ATOM   302  C  CG  . PRO A 1 37  ? 34.026 33.611 15.550  1.00 84.05  ? 37  PRO A CG  1 
ATOM   303  C  CD  . PRO A 1 37  ? 33.343 32.420 16.171  1.00 52.62  ? 37  PRO A CD  1 
ATOM   304  N  N   . SER A 1 38  ? 35.757 32.342 19.122  1.00 71.36  ? 38  SER A N   1 
ATOM   305  C  CA  . SER A 1 38  ? 36.379 32.588 20.402  1.00 51.34  ? 38  SER A CA  1 
ATOM   306  C  C   . SER A 1 38  ? 37.170 31.381 20.937  1.00 52.97  ? 38  SER A C   1 
ATOM   307  O  O   . SER A 1 38  ? 36.646 30.307 21.261  1.00 44.90  ? 38  SER A O   1 
ATOM   308  C  CB  . SER A 1 38  ? 35.428 33.211 21.431  1.00 100.00 ? 38  SER A CB  1 
ATOM   309  O  OG  . SER A 1 38  ? 36.119 33.409 22.663  1.00 98.19  ? 38  SER A OG  1 
ATOM   310  N  N   . LEU A 1 39  ? 38.472 31.582 21.057  1.00 41.59  ? 39  LEU A N   1 
ATOM   311  C  CA  . LEU A 1 39  ? 39.388 30.558 21.549  1.00 28.63  ? 39  LEU A CA  1 
ATOM   312  C  C   . LEU A 1 39  ? 39.387 30.417 23.055  1.00 43.98  ? 39  LEU A C   1 
ATOM   313  O  O   . LEU A 1 39  ? 39.138 29.356 23.656  1.00 40.86  ? 39  LEU A O   1 
ATOM   314  C  CB  . LEU A 1 39  ? 40.865 30.883 21.166  1.00 51.77  ? 39  LEU A CB  1 
ATOM   315  C  CG  . LEU A 1 39  ? 41.867 30.049 21.986  1.00 44.11  ? 39  LEU A CG  1 
ATOM   316  C  CD1 . LEU A 1 39  ? 42.133 28.717 21.319  1.00 53.35  ? 39  LEU A CD1 1 
ATOM   317  C  CD2 . LEU A 1 39  ? 43.181 30.782 22.224  1.00 51.54  ? 39  LEU A CD2 1 
ATOM   318  N  N   . ASN A 1 40  ? 39.818 31.534 23.630  1.00 71.83  ? 40  ASN A N   1 
ATOM   319  C  CA  . ASN A 1 40  ? 40.066 31.715 25.041  1.00 48.90  ? 40  ASN A CA  1 
ATOM   320  C  C   . ASN A 1 40  ? 38.939 31.498 26.000  1.00 63.59  ? 40  ASN A C   1 
ATOM   321  O  O   . ASN A 1 40  ? 39.157 31.303 27.210  1.00 100.00 ? 40  ASN A O   1 
ATOM   322  C  CB  . ASN A 1 40  ? 41.001 32.867 25.413  1.00 100.00 ? 40  ASN A CB  1 
ATOM   323  C  CG  . ASN A 1 40  ? 42.336 32.324 25.893  1.00 100.00 ? 40  ASN A CG  1 
ATOM   324  O  OD1 . ASN A 1 40  ? 43.415 32.767 25.435  1.00 100.00 ? 40  ASN A OD1 1 
ATOM   325  N  ND2 . ASN A 1 40  ? 42.269 31.340 26.802  1.00 100.00 ? 40  ASN A ND2 1 
ATOM   326  N  N   . ALA A 1 41  A 37.787 31.453 25.447  1.00 43.92  ? 40  ALA A N   1 
ATOM   327  C  CA  . ALA A 1 41  A 36.675 31.171 26.270  1.00 100.00 ? 40  ALA A CA  1 
ATOM   328  C  C   . ALA A 1 41  A 36.020 29.971 25.676  1.00 71.47  ? 40  ALA A C   1 
ATOM   329  O  O   . ALA A 1 41  A 36.257 28.839 26.083  1.00 76.87  ? 40  ALA A O   1 
ATOM   330  C  CB  . ALA A 1 41  A 35.727 32.351 26.359  1.00 98.13  ? 40  ALA A CB  1 
ATOM   331  N  N   . ALA A 1 42  ? 35.288 30.257 24.615  1.00 35.10  ? 41  ALA A N   1 
ATOM   332  C  CA  . ALA A 1 42  ? 34.472 29.292 23.912  1.00 35.81  ? 41  ALA A CA  1 
ATOM   333  C  C   . ALA A 1 42  ? 35.127 27.965 23.689  1.00 38.31  ? 41  ALA A C   1 
ATOM   334  O  O   . ALA A 1 42  ? 34.663 26.939 24.153  1.00 37.71  ? 41  ALA A O   1 
ATOM   335  C  CB  . ALA A 1 42  ? 33.760 29.813 22.676  1.00 27.38  ? 41  ALA A CB  1 
ATOM   336  N  N   . ALA A 1 43  ? 36.228 27.971 22.983  1.00 32.48  ? 42  ALA A N   1 
ATOM   337  C  CA  . ALA A 1 43  ? 36.872 26.701 22.726  1.00 31.86  ? 42  ALA A CA  1 
ATOM   338  C  C   . ALA A 1 43  ? 37.431 26.052 23.970  1.00 27.02  ? 42  ALA A C   1 
ATOM   339  O  O   . ALA A 1 43  ? 37.346 24.837 24.174  1.00 24.88  ? 42  ALA A O   1 
ATOM   340  C  CB  . ALA A 1 43  ? 38.018 26.854 21.743  1.00 32.17  ? 42  ALA A CB  1 
ATOM   341  N  N   . LYS A 1 44  ? 38.089 26.850 24.780  1.00 25.88  ? 43  LYS A N   1 
ATOM   342  C  CA  . LYS A 1 44  ? 38.683 26.280 25.960  1.00 30.75  ? 43  LYS A CA  1 
ATOM   343  C  C   . LYS A 1 44  ? 37.624 25.781 26.942  1.00 12.82  ? 43  LYS A C   1 
ATOM   344  O  O   . LYS A 1 44  ? 37.780 24.779 27.629  1.00 28.89  ? 43  LYS A O   1 
ATOM   345  C  CB  . LYS A 1 44  ? 39.583 27.272 26.600  1.00 23.60  ? 43  LYS A CB  1 
ATOM   346  C  CG  . LYS A 1 44  ? 40.944 27.265 25.975  1.00 41.34  ? 43  LYS A CG  1 
ATOM   347  C  CD  . LYS A 1 44  ? 41.700 28.478 26.428  1.00 64.02  ? 43  LYS A CD  1 
ATOM   348  C  CE  . LYS A 1 44  ? 43.191 28.429 26.169  1.00 100.00 ? 43  LYS A CE  1 
ATOM   349  N  NZ  . LYS A 1 44  ? 43.990 29.087 27.218  1.00 62.38  ? 43  LYS A NZ  1 
ATOM   350  N  N   . SER A 1 45  ? 36.501 26.455 26.891  1.00 15.50  ? 44  SER A N   1 
ATOM   351  C  CA  . SER A 1 45  ? 35.355 26.129 27.710  1.00 39.96  ? 44  SER A CA  1 
ATOM   352  C  C   . SER A 1 45  ? 34.784 24.766 27.289  1.00 24.46  ? 44  SER A C   1 
ATOM   353  O  O   . SER A 1 45  ? 34.574 23.887 28.118  1.00 23.38  ? 44  SER A O   1 
ATOM   354  C  CB  . SER A 1 45  ? 34.339 27.285 27.581  1.00 24.45  ? 44  SER A CB  1 
ATOM   355  O  OG  . SER A 1 45  ? 33.113 27.025 28.211  1.00 44.80  ? 44  SER A OG  1 
ATOM   356  N  N   . GLU A 1 46  ? 34.615 24.613 25.980  1.00 22.09  ? 45  GLU A N   1 
ATOM   357  C  CA  . GLU A 1 46  ? 34.119 23.396 25.425  1.00 14.38  ? 45  GLU A CA  1 
ATOM   358  C  C   . GLU A 1 46  ? 35.094 22.299 25.708  1.00 21.28  ? 45  GLU A C   1 
ATOM   359  O  O   . GLU A 1 46  ? 34.709 21.212 26.099  1.00 17.95  ? 45  GLU A O   1 
ATOM   360  C  CB  . GLU A 1 46  ? 33.990 23.539 23.936  1.00 13.45  ? 45  GLU A CB  1 
ATOM   361  C  CG  . GLU A 1 46  ? 32.765 24.391 23.575  1.00 18.14  ? 45  GLU A CG  1 
ATOM   362  C  CD  . GLU A 1 46  ? 31.465 23.733 23.926  1.00 27.85  ? 45  GLU A CD  1 
ATOM   363  O  OE1 . GLU A 1 46  ? 31.253 22.554 23.804  1.00 27.27  ? 45  GLU A OE1 1 
ATOM   364  O  OE2 . GLU A 1 46  ? 30.564 24.588 24.307  1.00 32.33  ? 45  GLU A OE2 1 
ATOM   365  N  N   . LEU A 1 47  ? 36.351 22.605 25.565  1.00 17.42  ? 46  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 47  ? 37.309 21.565 25.846  1.00 16.82  ? 46  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 47  ? 37.236 21.053 27.295  1.00 28.48  ? 46  LEU A C   1 
ATOM   368  O  O   . LEU A 1 47  ? 37.266 19.854 27.569  1.00 23.01  ? 46  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 47  ? 38.740 22.042 25.544  1.00 17.60  ? 46  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 47  ? 39.831 20.993 25.864  1.00 13.82  ? 46  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 47  ? 39.610 19.749 25.008  1.00 13.31  ? 46  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 47  ? 41.187 21.622 25.487  1.00 15.53  ? 46  LEU A CD2 1 
ATOM   373  N  N   . ASP A 1 48  ? 37.167 21.986 28.248  1.00 18.89  ? 47  ASP A N   1 
ATOM   374  C  CA  . ASP A 1 48  ? 37.157 21.599 29.633  1.00 21.53  ? 47  ASP A CA  1 
ATOM   375  C  C   . ASP A 1 48  ? 35.950 20.824 29.998  1.00 13.39  ? 47  ASP A C   1 
ATOM   376  O  O   . ASP A 1 48  ? 36.045 19.949 30.830  1.00 15.61  ? 47  ASP A O   1 
ATOM   377  C  CB  . ASP A 1 48  ? 37.345 22.762 30.603  1.00 32.42  ? 47  ASP A CB  1 
ATOM   378  C  CG  . ASP A 1 48  ? 38.685 23.464 30.503  1.00 28.33  ? 47  ASP A CG  1 
ATOM   379  O  OD1 . ASP A 1 48  ? 39.732 23.005 30.021  1.00 27.12  ? 47  ASP A OD1 1 
ATOM   380  O  OD2 . ASP A 1 48  ? 38.603 24.631 31.030  1.00 37.87  ? 47  ASP A OD2 1 
ATOM   381  N  N   . LYS A 1 49  ? 34.844 21.190 29.372  1.00 13.81  ? 48  LYS A N   1 
ATOM   382  C  CA  . LYS A 1 49  ? 33.597 20.481 29.596  1.00 15.80  ? 48  LYS A CA  1 
ATOM   383  C  C   . LYS A 1 49  ? 33.679 19.063 28.986  1.00 12.54  ? 48  LYS A C   1 
ATOM   384  O  O   . LYS A 1 49  ? 33.154 18.087 29.527  1.00 14.11  ? 48  LYS A O   1 
ATOM   385  C  CB  . LYS A 1 49  ? 32.577 21.331 28.878  1.00 18.93  ? 48  LYS A CB  1 
ATOM   386  C  CG  . LYS A 1 49  ? 31.254 20.697 28.605  1.00 17.49  ? 48  LYS A CG  1 
ATOM   387  C  CD  . LYS A 1 49  ? 30.221 21.778 28.424  1.00 21.88  ? 48  LYS A CD  1 
ATOM   388  C  CE  . LYS A 1 49  ? 30.194 22.314 27.016  1.00 33.44  ? 48  LYS A CE  1 
ATOM   389  N  NZ  . LYS A 1 49  ? 29.549 21.358 26.087  1.00 23.65  ? 48  LYS A NZ  1 
ATOM   390  N  N   . ALA A 1 50  ? 34.350 18.941 27.842  1.00 15.04  ? 49  ALA A N   1 
ATOM   391  C  CA  . ALA A 1 50  ? 34.458 17.624 27.186  1.00 19.71  ? 49  ALA A CA  1 
ATOM   392  C  C   . ALA A 1 50  ? 35.327 16.655 27.977  1.00 16.75  ? 49  ALA A C   1 
ATOM   393  O  O   . ALA A 1 50  ? 35.060 15.457 28.113  1.00 19.16  ? 49  ALA A O   1 
ATOM   394  C  CB  . ALA A 1 50  ? 34.921 17.767 25.740  1.00 17.74  ? 49  ALA A CB  1 
ATOM   395  N  N   . ILE A 1 51  ? 36.375 17.203 28.557  1.00 12.62  ? 50  ILE A N   1 
ATOM   396  C  CA  . ILE A 1 51  ? 37.352 16.436 29.328  1.00 16.81  ? 50  ILE A CA  1 
ATOM   397  C  C   . ILE A 1 51  ? 37.040 16.275 30.804  1.00 27.80  ? 50  ILE A C   1 
ATOM   398  O  O   . ILE A 1 51  ? 37.451 15.311 31.456  1.00 24.90  ? 50  ILE A O   1 
ATOM   399  C  CB  . ILE A 1 51  ? 38.768 17.066 29.162  1.00 13.88  ? 50  ILE A CB  1 
ATOM   400  C  CG1 . ILE A 1 51  ? 39.234 17.043 27.705  1.00 33.66  ? 50  ILE A CG1 1 
ATOM   401  C  CG2 . ILE A 1 51  ? 39.798 16.397 30.036  1.00 15.04  ? 50  ILE A CG2 1 
ATOM   402  C  CD1 . ILE A 1 51  ? 39.201 15.651 27.056  1.00 25.54  ? 50  ILE A CD1 1 
ATOM   403  N  N   . GLY A 1 52  ? 36.367 17.243 31.355  1.00 18.61  ? 51  GLY A N   1 
ATOM   404  C  CA  . GLY A 1 52  ? 36.064 17.136 32.749  1.00 24.27  ? 51  GLY A CA  1 
ATOM   405  C  C   . GLY A 1 52  ? 37.132 17.713 33.646  1.00 26.79  ? 51  GLY A C   1 
ATOM   406  O  O   . GLY A 1 52  ? 37.233 17.344 34.806  1.00 27.91  ? 51  GLY A O   1 
ATOM   407  N  N   . ARG A 1 53  ? 37.933 18.622 33.131  1.00 27.86  ? 52  ARG A N   1 
ATOM   408  C  CA  . ARG A 1 53  ? 38.943 19.226 33.976  1.00 20.39  ? 52  ARG A CA  1 
ATOM   409  C  C   . ARG A 1 53  ? 39.394 20.522 33.413  1.00 32.81  ? 52  ARG A C   1 
ATOM   410  O  O   . ARG A 1 53  ? 39.056 20.800 32.259  1.00 23.27  ? 52  ARG A O   1 
ATOM   411  C  CB  . ARG A 1 53  ? 40.114 18.297 34.269  1.00 29.48  ? 52  ARG A CB  1 
ATOM   412  C  CG  . ARG A 1 53  ? 41.179 18.266 33.183  1.00 26.18  ? 52  ARG A CG  1 
ATOM   413  C  CD  . ARG A 1 53  ? 42.135 17.122 33.453  1.00 22.11  ? 52  ARG A CD  1 
ATOM   414  N  NE  . ARG A 1 53  ? 43.067 16.875 32.353  1.00 33.93  ? 52  ARG A NE  1 
ATOM   415  C  CZ  . ARG A 1 53  ? 43.830 17.823 31.777  1.00 36.63  ? 52  ARG A CZ  1 
ATOM   416  N  NH1 . ARG A 1 53  ? 43.747 19.106 32.155  1.00 53.95  ? 52  ARG A NH1 1 
ATOM   417  N  NH2 . ARG A 1 53  ? 44.669 17.490 30.780  1.00 25.65  ? 52  ARG A NH2 1 
ATOM   418  N  N   . ASN A 1 54  ? 40.136 21.298 34.218  1.00 34.56  ? 53  ASN A N   1 
ATOM   419  C  CA  . ASN A 1 54  ? 40.650 22.557 33.734  1.00 22.44  ? 53  ASN A CA  1 
ATOM   420  C  C   . ASN A 1 54  ? 41.866 22.250 32.887  1.00 28.30  ? 53  ASN A C   1 
ATOM   421  O  O   . ASN A 1 54  ? 42.911 21.898 33.410  1.00 35.72  ? 53  ASN A O   1 
ATOM   422  C  CB  . ASN A 1 54  ? 40.984 23.546 34.852  1.00 28.73  ? 53  ASN A CB  1 
ATOM   423  C  CG  . ASN A 1 54  ? 40.182 24.812 34.632  1.00 100.00 ? 53  ASN A CG  1 
ATOM   424  O  OD1 . ASN A 1 54  ? 39.016 24.891 35.050  1.00 100.00 ? 53  ASN A OD1 1 
ATOM   425  N  ND2 . ASN A 1 54  ? 40.763 25.755 33.877  1.00 40.00  ? 53  ASN A ND2 1 
ATOM   426  N  N   . THR A 1 55  ? 41.701 22.335 31.578  1.00 30.85  ? 54  THR A N   1 
ATOM   427  C  CA  . THR A 1 55  ? 42.765 21.938 30.683  1.00 31.85  ? 54  THR A CA  1 
ATOM   428  C  C   . THR A 1 55  ? 43.764 22.961 30.252  1.00 34.54  ? 54  THR A C   1 
ATOM   429  O  O   . THR A 1 55  ? 44.880 22.585 29.941  1.00 43.42  ? 54  THR A O   1 
ATOM   430  C  CB  . THR A 1 55  ? 42.264 21.279 29.375  1.00 26.20  ? 54  THR A CB  1 
ATOM   431  O  OG1 . THR A 1 55  ? 41.666 22.249 28.495  1.00 25.39  ? 54  THR A OG1 1 
ATOM   432  C  CG2 . THR A 1 55  ? 41.377 20.064 29.687  1.00 24.92  ? 54  THR A CG2 1 
ATOM   433  N  N   . ASN A 1 56  ? 43.380 24.203 30.088  1.00 45.44  ? 55  ASN A N   1 
ATOM   434  C  CA  . ASN A 1 56  ? 44.324 25.139 29.519  1.00 93.69  ? 55  ASN A CA  1 
ATOM   435  C  C   . ASN A 1 56  ? 44.695 24.780 28.077  1.00 60.47  ? 55  ASN A C   1 
ATOM   436  O  O   . ASN A 1 56  ? 45.888 24.905 27.659  1.00 55.88  ? 55  ASN A O   1 
ATOM   437  C  CB  . ASN A 1 56  ? 45.518 25.611 30.407  1.00 40.63  ? 55  ASN A CB  1 
ATOM   438  C  CG  . ASN A 1 56  ? 45.909 27.111 30.238  1.00 45.86  ? 55  ASN A CG  1 
ATOM   439  O  OD1 . ASN A 1 56  ? 45.097 28.010 29.899  1.00 57.43  ? 55  ASN A OD1 1 
ATOM   440  N  ND2 . ASN A 1 56  ? 47.192 27.382 30.474  1.00 100.00 ? 55  ASN A ND2 1 
ATOM   441  N  N   . GLY A 1 57  ? 43.710 24.284 27.287  1.00 30.09  ? 56  GLY A N   1 
ATOM   442  C  CA  . GLY A 1 57  ? 43.810 23.964 25.851  1.00 24.84  ? 56  GLY A CA  1 
ATOM   443  C  C   . GLY A 1 57  ? 44.769 22.834 25.463  1.00 22.73  ? 56  GLY A C   1 
ATOM   444  O  O   . GLY A 1 57  ? 45.073 22.567 24.303  1.00 29.35  ? 56  GLY A O   1 
ATOM   445  N  N   . VAL A 1 58  ? 45.243 22.120 26.443  1.00 21.99  ? 57  VAL A N   1 
ATOM   446  C  CA  . VAL A 1 58  ? 46.136 20.988 26.160  1.00 20.74  ? 57  VAL A CA  1 
ATOM   447  C  C   . VAL A 1 58  ? 45.654 19.677 26.835  1.00 33.25  ? 57  VAL A C   1 
ATOM   448  O  O   . VAL A 1 58  ? 45.295 19.637 28.020  1.00 26.29  ? 57  VAL A O   1 
ATOM   449  C  CB  . VAL A 1 58  ? 47.559 21.311 26.624  1.00 36.72  ? 57  VAL A CB  1 
ATOM   450  C  CG1 . VAL A 1 58  ? 48.414 20.057 26.561  1.00 24.01  ? 57  VAL A CG1 1 
ATOM   451  C  CG2 . VAL A 1 58  ? 48.146 22.379 25.720  1.00 57.89  ? 57  VAL A CG2 1 
ATOM   452  N  N   . ILE A 1 59  ? 45.670 18.571 26.095  1.00 19.98  ? 58  ILE A N   1 
ATOM   453  C  CA  . ILE A 1 59  ? 45.198 17.301 26.630  1.00 24.84  ? 58  ILE A CA  1 
ATOM   454  C  C   . ILE A 1 59  ? 46.294 16.287 26.447  1.00 21.26  ? 58  ILE A C   1 
ATOM   455  O  O   . ILE A 1 59  ? 47.276 16.573 25.754  1.00 26.23  ? 58  ILE A O   1 
ATOM   456  C  CB  . ILE A 1 59  ? 43.858 16.876 25.969  1.00 29.15  ? 58  ILE A CB  1 
ATOM   457  C  CG1 . ILE A 1 59  ? 44.014 16.658 24.426  1.00 17.88  ? 58  ILE A CG1 1 
ATOM   458  C  CG2 . ILE A 1 59  ? 42.737 17.891 26.320  1.00 17.46  ? 58  ILE A CG2 1 
ATOM   459  C  CD1 . ILE A 1 59  ? 42.835 15.945 23.771  1.00 16.30  ? 58  ILE A CD1 1 
ATOM   460  N  N   . THR A 1 60  ? 46.136 15.134 27.088  1.00 18.62  ? 59  THR A N   1 
ATOM   461  C  CA  . THR A 1 60  ? 47.082 14.037 27.006  1.00 20.06  ? 59  THR A CA  1 
ATOM   462  C  C   . THR A 1 60  ? 46.627 13.090 25.913  1.00 23.26  ? 59  THR A C   1 
ATOM   463  O  O   . THR A 1 60  ? 45.501 13.174 25.420  1.00 19.61  ? 59  THR A O   1 
ATOM   464  C  CB  . THR A 1 60  ? 47.257 13.297 28.368  1.00 26.47  ? 59  THR A CB  1 
ATOM   465  O  OG1 . THR A 1 60  ? 46.088 12.532 28.670  1.00 22.79  ? 59  THR A OG1 1 
ATOM   466  C  CG2 . THR A 1 60  ? 47.511 14.306 29.480  1.00 27.85  ? 59  THR A CG2 1 
ATOM   467  N  N   . LYS A 1 61  ? 47.497 12.171 25.555  1.00 27.30  ? 60  LYS A N   1 
ATOM   468  C  CA  . LYS A 1 61  ? 47.236 11.200 24.517  1.00 16.07  ? 60  LYS A CA  1 
ATOM   469  C  C   . LYS A 1 61  ? 46.034 10.326 24.878  1.00 14.87  ? 60  LYS A C   1 
ATOM   470  O  O   . LYS A 1 61  ? 45.115 10.113 24.066  1.00 17.89  ? 60  LYS A O   1 
ATOM   471  C  CB  . LYS A 1 61  ? 48.493 10.373 24.205  1.00 27.89  ? 60  LYS A CB  1 
ATOM   472  C  CG  . LYS A 1 61  ? 48.388 9.456  22.973  1.00 49.44  ? 60  LYS A CG  1 
ATOM   473  C  CD  . LYS A 1 61  ? 49.662 8.648  22.703  1.00 48.25  ? 60  LYS A CD  1 
ATOM   474  C  CE  . LYS A 1 61  ? 49.524 7.667  21.546  1.00 78.26  ? 60  LYS A CE  1 
ATOM   475  N  NZ  . LYS A 1 61  ? 49.840 8.270  20.236  1.00 100.00 ? 60  LYS A NZ  1 
ATOM   476  N  N   . ASP A 1 62  ? 45.990 9.880  26.145  1.00 21.96  ? 61  ASP A N   1 
ATOM   477  C  CA  . ASP A 1 62  ? 44.878 9.061  26.617  1.00 13.53  ? 61  ASP A CA  1 
ATOM   478  C  C   . ASP A 1 62  ? 43.541 9.794  26.457  1.00 17.92  ? 61  ASP A C   1 
ATOM   479  O  O   . ASP A 1 62  ? 42.534 9.175  26.104  1.00 23.32  ? 61  ASP A O   1 
ATOM   480  C  CB  . ASP A 1 62  ? 45.039 8.694  28.080  1.00 18.40  ? 61  ASP A CB  1 
ATOM   481  C  CG  . ASP A 1 62  ? 46.104 7.702  28.349  1.00 100.00 ? 61  ASP A CG  1 
ATOM   482  O  OD1 . ASP A 1 62  ? 46.710 7.255  27.263  1.00 59.96  ? 61  ASP A OD1 1 
ATOM   483  O  OD2 . ASP A 1 62  ? 46.363 7.332  29.480  1.00 100.00 ? 61  ASP A OD2 1 
ATOM   484  N  N   . GLU A 1 63  ? 43.565 11.119 26.786  1.00 20.84  ? 62  GLU A N   1 
ATOM   485  C  CA  . GLU A 1 63  ? 42.406 12.024 26.690  1.00 9.83   ? 62  GLU A CA  1 
ATOM   486  C  C   . GLU A 1 63  ? 41.937 12.114 25.244  1.00 14.72  ? 62  GLU A C   1 
ATOM   487  O  O   . GLU A 1 63  ? 40.749 11.984 24.975  1.00 18.60  ? 62  GLU A O   1 
ATOM   488  C  CB  . GLU A 1 63  ? 42.680 13.400 27.273  1.00 13.54  ? 62  GLU A CB  1 
ATOM   489  C  CG  . GLU A 1 63  ? 42.682 13.304 28.810  1.00 17.40  ? 62  GLU A CG  1 
ATOM   490  C  CD  . GLU A 1 63  ? 43.173 14.547 29.487  1.00 26.39  ? 62  GLU A CD  1 
ATOM   491  O  OE1 . GLU A 1 63  ? 43.738 15.453 28.876  1.00 25.27  ? 62  GLU A OE1 1 
ATOM   492  O  OE2 . GLU A 1 63  ? 42.859 14.558 30.767  1.00 22.98  ? 62  GLU A OE2 1 
ATOM   493  N  N   . ALA A 1 64  ? 42.901 12.266 24.319  1.00 16.42  ? 63  ALA A N   1 
ATOM   494  C  CA  . ALA A 1 64  ? 42.587 12.328 22.895  1.00 16.70  ? 63  ALA A CA  1 
ATOM   495  C  C   . ALA A 1 64  ? 41.895 11.058 22.393  1.00 17.07  ? 63  ALA A C   1 
ATOM   496  O  O   . ALA A 1 64  ? 40.983 11.104 21.567  1.00 16.00  ? 63  ALA A O   1 
ATOM   497  C  CB  . ALA A 1 64  ? 43.845 12.628 22.075  1.00 11.69  ? 63  ALA A CB  1 
ATOM   498  N  N   . GLU A 1 65  ? 42.409 9.914  22.876  1.00 15.62  ? 64  GLU A N   1 
ATOM   499  C  CA  . GLU A 1 65  ? 41.920 8.599  22.511  1.00 10.83  ? 64  GLU A CA  1 
ATOM   500  C  C   . GLU A 1 65  ? 40.578 8.339  23.120  1.00 11.46  ? 64  GLU A C   1 
ATOM   501  O  O   . GLU A 1 65  ? 39.726 7.690  22.532  1.00 14.58  ? 64  GLU A O   1 
ATOM   502  C  CB  . GLU A 1 65  ? 42.922 7.503  22.918  1.00 20.73  ? 64  GLU A CB  1 
ATOM   503  C  CG  . GLU A 1 65  ? 44.140 7.515  21.957  1.00 21.54  ? 64  GLU A CG  1 
ATOM   504  C  CD  . GLU A 1 65  ? 45.278 6.645  22.417  1.00 37.07  ? 64  GLU A CD  1 
ATOM   505  O  OE1 . GLU A 1 65  ? 45.311 6.093  23.525  1.00 33.16  ? 64  GLU A OE1 1 
ATOM   506  O  OE2 . GLU A 1 65  ? 46.209 6.574  21.508  1.00 35.12  ? 64  GLU A OE2 1 
ATOM   507  N  N   . LYS A 1 66  ? 40.366 8.886  24.290  1.00 11.75  ? 65  LYS A N   1 
ATOM   508  C  CA  . LYS A 1 66  ? 39.060 8.731  24.905  1.00 8.98   ? 65  LYS A CA  1 
ATOM   509  C  C   . LYS A 1 66  ? 38.039 9.485  24.056  1.00 20.77  ? 65  LYS A C   1 
ATOM   510  O  O   . LYS A 1 66  ? 36.993 8.946  23.692  1.00 17.76  ? 65  LYS A O   1 
ATOM   511  C  CB  . LYS A 1 66  ? 39.053 9.279  26.307  1.00 13.75  ? 65  LYS A CB  1 
ATOM   512  C  CG  . LYS A 1 66  ? 37.667 9.110  26.929  1.00 29.01  ? 65  LYS A CG  1 
ATOM   513  C  CD  . LYS A 1 66  ? 37.673 8.827  28.425  1.00 79.03  ? 65  LYS A CD  1 
ATOM   514  C  CE  . LYS A 1 66  ? 36.496 7.966  28.860  1.00 68.86  ? 65  LYS A CE  1 
ATOM   515  N  NZ  . LYS A 1 66  ? 36.156 8.171  30.272  1.00 76.11  ? 65  LYS A NZ  1 
ATOM   516  N  N   . LEU A 1 67  ? 38.356 10.733 23.640  1.00 11.76  ? 66  LEU A N   1 
ATOM   517  C  CA  . LEU A 1 67  ? 37.419 11.498 22.757  1.00 4.31   ? 66  LEU A CA  1 
ATOM   518  C  C   . LEU A 1 67  ? 37.176 10.754 21.442  1.00 12.37  ? 66  LEU A C   1 
ATOM   519  O  O   . LEU A 1 67  ? 36.052 10.712 20.941  1.00 11.62  ? 66  LEU A O   1 
ATOM   520  C  CB  . LEU A 1 67  ? 37.962 12.913 22.364  1.00 10.45  ? 66  LEU A CB  1 
ATOM   521  C  CG  . LEU A 1 67  ? 38.080 13.843 23.584  1.00 17.68  ? 66  LEU A CG  1 
ATOM   522  C  CD1 . LEU A 1 67  ? 38.694 15.194 23.213  1.00 17.97  ? 66  LEU A CD1 1 
ATOM   523  C  CD2 . LEU A 1 67  ? 36.718 14.083 24.167  1.00 23.17  ? 66  LEU A CD2 1 
ATOM   524  N  N   . PHE A 1 68  ? 38.243 10.189 20.896  1.00 14.89  ? 67  PHE A N   1 
ATOM   525  C  CA  . PHE A 1 68  ? 38.198 9.464  19.626  1.00 10.25  ? 67  PHE A CA  1 
ATOM   526  C  C   . PHE A 1 68  ? 37.283 8.259  19.734  1.00 8.66   ? 67  PHE A C   1 
ATOM   527  O  O   . PHE A 1 68  ? 36.384 8.089  18.908  1.00 14.98  ? 67  PHE A O   1 
ATOM   528  C  CB  . PHE A 1 68  ? 39.618 9.073  19.260  1.00 11.58  ? 67  PHE A CB  1 
ATOM   529  C  CG  . PHE A 1 68  ? 39.779 8.485  17.877  1.00 14.25  ? 67  PHE A CG  1 
ATOM   530  C  CD1 . PHE A 1 68  ? 38.969 8.851  16.801  1.00 17.92  ? 67  PHE A CD1 1 
ATOM   531  C  CD2 . PHE A 1 68  ? 40.784 7.547  17.651  1.00 13.66  ? 67  PHE A CD2 1 
ATOM   532  C  CE1 . PHE A 1 68  ? 39.182 8.320  15.526  1.00 13.79  ? 67  PHE A CE1 1 
ATOM   533  C  CE2 . PHE A 1 68  ? 41.036 7.028  16.382  1.00 10.69  ? 67  PHE A CE2 1 
ATOM   534  C  CZ  . PHE A 1 68  ? 40.207 7.400  15.325  1.00 12.55  ? 67  PHE A CZ  1 
ATOM   535  N  N   . ASN A 1 69  ? 37.432 7.447  20.791  1.00 12.97  ? 68  ASN A N   1 
ATOM   536  C  CA  . ASN A 1 69  ? 36.494 6.329  20.993  1.00 9.27   ? 68  ASN A CA  1 
ATOM   537  C  C   . ASN A 1 69  ? 35.020 6.763  21.051  1.00 10.39  ? 68  ASN A C   1 
ATOM   538  O  O   . ASN A 1 69  ? 34.086 6.141  20.518  1.00 16.16  ? 68  ASN A O   1 
ATOM   539  C  CB  . ASN A 1 69  ? 36.831 5.539  22.271  1.00 11.62  ? 68  ASN A CB  1 
ATOM   540  C  CG  . ASN A 1 69  ? 38.092 4.693  22.121  1.00 21.76  ? 68  ASN A CG  1 
ATOM   541  O  OD1 . ASN A 1 69  ? 38.278 4.075  21.092  1.00 23.49  ? 68  ASN A OD1 1 
ATOM   542  N  ND2 . ASN A 1 69  ? 38.958 4.628  23.144  1.00 20.74  ? 68  ASN A ND2 1 
ATOM   543  N  N   . GLN A 1 70  ? 34.783 7.822  21.765  1.00 9.48   ? 69  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 70  ? 33.417 8.322  21.844  1.00 8.74   ? 69  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 70  ? 32.895 8.756  20.496  1.00 5.11   ? 69  GLN A C   1 
ATOM   546  O  O   . GLN A 1 70  ? 31.728 8.549  20.161  1.00 14.54  ? 69  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 70  ? 33.313 9.548  22.827  1.00 8.47   ? 69  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 70  ? 33.649 9.099  24.266  1.00 9.94   ? 69  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 70  ? 33.780 10.255 25.239  1.00 21.42  ? 69  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 70  ? 33.916 10.029 26.430  1.00 19.51  ? 69  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 70  ? 33.767 11.478 24.738  1.00 14.94  ? 69  GLN A NE2 1 
ATOM   552  N  N   . ASP A 1 71  ? 33.746 9.459  19.734  1.00 11.12  ? 70  ASP A N   1 
ATOM   553  C  CA  . ASP A 1 71  ? 33.304 9.980  18.465  1.00 9.69   ? 70  ASP A CA  1 
ATOM   554  C  C   . ASP A 1 71  ? 33.065 8.894  17.438  1.00 12.82  ? 70  ASP A C   1 
ATOM   555  O  O   . ASP A 1 71  ? 32.169 9.042  16.604  1.00 16.59  ? 70  ASP A O   1 
ATOM   556  C  CB  . ASP A 1 71  ? 34.279 11.030 17.910  1.00 11.84  ? 70  ASP A CB  1 
ATOM   557  C  CG  . ASP A 1 71  ? 34.362 12.290 18.748  1.00 19.73  ? 70  ASP A CG  1 
ATOM   558  O  OD1 . ASP A 1 71  ? 33.539 12.655 19.525  1.00 18.18  ? 70  ASP A OD1 1 
ATOM   559  O  OD2 . ASP A 1 71  ? 35.435 12.954 18.570  1.00 14.64  ? 70  ASP A OD2 1 
ATOM   560  N  N   . VAL A 1 72  ? 33.844 7.786  17.481  1.00 13.17  ? 71  VAL A N   1 
ATOM   561  C  CA  . VAL A 1 72  ? 33.650 6.709  16.508  1.00 13.15  ? 71  VAL A CA  1 
ATOM   562  C  C   . VAL A 1 72  ? 32.336 6.007  16.870  1.00 10.31  ? 71  VAL A C   1 
ATOM   563  O  O   . VAL A 1 72  ? 31.508 5.698  16.021  1.00 12.65  ? 71  VAL A O   1 
ATOM   564  C  CB  . VAL A 1 72  ? 34.854 5.729  16.434  1.00 12.87  ? 71  VAL A CB  1 
ATOM   565  C  CG1 . VAL A 1 72  ? 34.538 4.464  15.613  1.00 7.84   ? 71  VAL A CG1 1 
ATOM   566  C  CG2 . VAL A 1 72  ? 36.072 6.426  15.835  1.00 12.09  ? 71  VAL A CG2 1 
ATOM   567  N  N   . ASP A 1 73  ? 32.152 5.809  18.154  1.00 11.97  ? 72  ASP A N   1 
ATOM   568  C  CA  . ASP A 1 73  ? 30.937 5.156  18.630  1.00 7.98   ? 72  ASP A CA  1 
ATOM   569  C  C   . ASP A 1 73  ? 29.724 5.942  18.217  1.00 10.29  ? 72  ASP A C   1 
ATOM   570  O  O   . ASP A 1 73  ? 28.720 5.406  17.739  1.00 11.86  ? 72  ASP A O   1 
ATOM   571  C  CB  . ASP A 1 73  ? 31.056 4.961  20.160  1.00 9.25   ? 72  ASP A CB  1 
ATOM   572  C  CG  . ASP A 1 73  ? 29.915 4.158  20.760  1.00 14.36  ? 72  ASP A CG  1 
ATOM   573  O  OD1 . ASP A 1 73  ? 29.701 2.994  20.210  1.00 23.67  ? 72  ASP A OD1 1 
ATOM   574  O  OD2 . ASP A 1 73  ? 29.336 4.518  21.747  1.00 27.12  ? 72  ASP A OD2 1 
ATOM   575  N  N   . ALA A 1 74  ? 29.786 7.263  18.409  1.00 14.04  ? 73  ALA A N   1 
ATOM   576  C  CA  . ALA A 1 74  ? 28.678 8.139  18.052  1.00 14.94  ? 73  ALA A CA  1 
ATOM   577  C  C   . ALA A 1 74  ? 28.335 8.093  16.579  1.00 19.38  ? 73  ALA A C   1 
ATOM   578  O  O   . ALA A 1 74  ? 27.156 8.126  16.194  1.00 13.84  ? 73  ALA A O   1 
ATOM   579  C  CB  . ALA A 1 74  ? 28.992 9.588  18.433  1.00 14.56  ? 73  ALA A CB  1 
ATOM   580  N  N   . ALA A 1 75  ? 29.386 8.020  15.773  1.00 14.43  ? 74  ALA A N   1 
ATOM   581  C  CA  . ALA A 1 75  ? 29.272 8.002  14.314  1.00 17.25  ? 74  ALA A CA  1 
ATOM   582  C  C   . ALA A 1 75  ? 28.521 6.736  13.912  1.00 14.45  ? 74  ALA A C   1 
ATOM   583  O  O   . ALA A 1 75  ? 27.480 6.805  13.259  1.00 14.89  ? 74  ALA A O   1 
ATOM   584  C  CB  . ALA A 1 75  ? 30.638 8.148  13.607  1.00 9.08   ? 74  ALA A CB  1 
ATOM   585  N  N   . VAL A 1 76  ? 29.033 5.579  14.376  1.00 11.87  ? 75  VAL A N   1 
ATOM   586  C  CA  . VAL A 1 76  ? 28.342 4.348  14.077  1.00 17.71  ? 75  VAL A CA  1 
ATOM   587  C  C   . VAL A 1 76  ? 26.875 4.389  14.508  1.00 30.00  ? 75  VAL A C   1 
ATOM   588  O  O   . VAL A 1 76  ? 25.988 3.994  13.766  1.00 19.87  ? 75  VAL A O   1 
ATOM   589  C  CB  . VAL A 1 76  ? 28.993 3.159  14.786  1.00 23.35  ? 75  VAL A CB  1 
ATOM   590  C  CG1 . VAL A 1 76  ? 28.206 1.863  14.455  1.00 15.27  ? 75  VAL A CG1 1 
ATOM   591  C  CG2 . VAL A 1 76  ? 30.419 3.050  14.261  1.00 16.50  ? 75  VAL A CG2 1 
ATOM   592  N  N   . ARG A 1 77  ? 26.627 4.822  15.740  1.00 17.77  ? 76  ARG A N   1 
ATOM   593  C  CA  . ARG A 1 77  ? 25.273 4.799  16.244  1.00 14.52  ? 76  ARG A CA  1 
ATOM   594  C  C   . ARG A 1 77  ? 24.394 5.768  15.477  1.00 24.38  ? 76  ARG A C   1 
ATOM   595  O  O   . ARG A 1 77  ? 23.208 5.535  15.213  1.00 25.54  ? 76  ARG A O   1 
ATOM   596  C  CB  . ARG A 1 77  ? 25.219 4.972  17.771  1.00 14.34  ? 76  ARG A CB  1 
ATOM   597  C  CG  . ARG A 1 77  ? 25.385 3.625  18.544  1.00 29.54  ? 76  ARG A CG  1 
ATOM   598  C  CD  . ARG A 1 77  ? 25.451 3.698  20.104  1.00 61.03  ? 76  ARG A CD  1 
ATOM   599  N  NE  . ARG A 1 77  ? 26.480 4.662  20.566  1.00 42.52  ? 76  ARG A NE  1 
ATOM   600  C  CZ  . ARG A 1 77  ? 26.240 5.916  20.839  1.00 100.00 ? 76  ARG A CZ  1 
ATOM   601  N  NH1 . ARG A 1 77  ? 25.021 6.448  21.020  1.00 100.00 ? 76  ARG A NH1 1 
ATOM   602  N  NH2 . ARG A 1 77  ? 27.274 6.722  21.193  1.00 25.73  ? 76  ARG A NH2 1 
ATOM   603  N  N   . GLY A 1 78  ? 24.997 6.847  15.051  1.00 16.19  ? 77  GLY A N   1 
ATOM   604  C  CA  . GLY A 1 78  ? 24.247 7.838  14.274  1.00 11.86  ? 77  GLY A CA  1 
ATOM   605  C  C   . GLY A 1 78  ? 23.808 7.273  12.947  1.00 20.83  ? 77  GLY A C   1 
ATOM   606  O  O   . GLY A 1 78  ? 22.691 7.478  12.523  1.00 20.29  ? 77  GLY A O   1 
ATOM   607  N  N   . ILE A 1 79  ? 24.711 6.561  12.286  1.00 17.48  ? 78  ILE A N   1 
ATOM   608  C  CA  . ILE A 1 79  ? 24.411 5.899  11.016  1.00 17.82  ? 78  ILE A CA  1 
ATOM   609  C  C   . ILE A 1 79  ? 23.221 4.935  11.212  1.00 26.56  ? 78  ILE A C   1 
ATOM   610  O  O   . ILE A 1 79  ? 22.294 4.841  10.394  1.00 19.86  ? 78  ILE A O   1 
ATOM   611  C  CB  . ILE A 1 79  ? 25.610 5.104  10.465  1.00 15.30  ? 78  ILE A CB  1 
ATOM   612  C  CG1 . ILE A 1 79  ? 26.648 6.035  9.817   1.00 10.06  ? 78  ILE A CG1 1 
ATOM   613  C  CG2 . ILE A 1 79  ? 25.177 4.056  9.446   1.00 9.68   ? 78  ILE A CG2 1 
ATOM   614  C  CD1 . ILE A 1 79  ? 28.050 5.410  9.765   1.00 12.00  ? 78  ILE A CD1 1 
ATOM   615  N  N   . LEU A 1 80  ? 23.253 4.182  12.311  1.00 18.36  ? 79  LEU A N   1 
ATOM   616  C  CA  . LEU A 1 80  ? 22.243 3.164  12.564  1.00 20.92  ? 79  LEU A CA  1 
ATOM   617  C  C   . LEU A 1 80  ? 20.887 3.662  12.916  1.00 23.74  ? 79  LEU A C   1 
ATOM   618  O  O   . LEU A 1 80  ? 19.954 2.889  12.818  1.00 32.95  ? 79  LEU A O   1 
ATOM   619  C  CB  . LEU A 1 80  ? 22.692 1.988  13.450  1.00 22.28  ? 79  LEU A CB  1 
ATOM   620  C  CG  . LEU A 1 80  ? 24.007 1.355  12.972  1.00 32.86  ? 79  LEU A CG  1 
ATOM   621  C  CD1 . LEU A 1 80  ? 24.617 0.563  14.106  1.00 29.85  ? 79  LEU A CD1 1 
ATOM   622  C  CD2 . LEU A 1 80  ? 23.819 0.437  11.765  1.00 20.77  ? 79  LEU A CD2 1 
ATOM   623  N  N   . ARG A 1 81  ? 20.817 4.929  13.343  1.00 25.27  ? 80  ARG A N   1 
ATOM   624  C  CA  . ARG A 1 81  ? 19.592 5.582  13.726  1.00 21.23  ? 80  ARG A CA  1 
ATOM   625  C  C   . ARG A 1 81  ? 19.054 6.404  12.563  1.00 35.49  ? 80  ARG A C   1 
ATOM   626  O  O   . ARG A 1 81  ? 17.942 6.904  12.599  1.00 43.37  ? 80  ARG A O   1 
ATOM   627  C  CB  . ARG A 1 81  ? 19.953 6.588  14.827  1.00 34.23  ? 80  ARG A CB  1 
ATOM   628  C  CG  . ARG A 1 81  ? 19.716 6.170  16.275  1.00 95.42  ? 80  ARG A CG  1 
ATOM   629  C  CD  . ARG A 1 81  ? 19.612 7.396  17.200  1.00 100.00 ? 80  ARG A CD  1 
ATOM   630  N  NE  . ARG A 1 81  ? 20.912 7.874  17.687  1.00 100.00 ? 80  ARG A NE  1 
ATOM   631  C  CZ  . ARG A 1 81  ? 21.534 9.016  17.335  1.00 100.00 ? 80  ARG A CZ  1 
ATOM   632  N  NH1 . ARG A 1 81  ? 21.026 9.910  16.463  1.00 68.38  ? 80  ARG A NH1 1 
ATOM   633  N  NH2 . ARG A 1 81  ? 22.717 9.263  17.892  1.00 72.87  ? 80  ARG A NH2 1 
ATOM   634  N  N   . ASN A 1 82  ? 19.887 6.621  11.545  1.00 19.23  ? 81  ASN A N   1 
ATOM   635  C  CA  . ASN A 1 82  ? 19.497 7.445  10.458  1.00 18.92  ? 81  ASN A CA  1 
ATOM   636  C  C   . ASN A 1 82  ? 18.738 6.655  9.391   1.00 37.00  ? 81  ASN A C   1 
ATOM   637  O  O   . ASN A 1 82  ? 19.255 5.649  8.895   1.00 23.14  ? 81  ASN A O   1 
ATOM   638  C  CB  . ASN A 1 82  ? 20.729 8.119  9.869   1.00 18.81  ? 81  ASN A CB  1 
ATOM   639  C  CG  . ASN A 1 82  ? 20.280 9.153  8.876   1.00 34.66  ? 81  ASN A CG  1 
ATOM   640  O  OD1 . ASN A 1 82  ? 19.729 8.810  7.841   1.00 32.07  ? 81  ASN A OD1 1 
ATOM   641  N  ND2 . ASN A 1 82  ? 20.422 10.414 9.249   1.00 24.89  ? 81  ASN A ND2 1 
ATOM   642  N  N   . ALA A 1 83  ? 17.506 7.086  9.067   1.00 36.90  ? 82  ALA A N   1 
ATOM   643  C  CA  . ALA A 1 83  ? 16.668 6.384  8.099   1.00 23.62  ? 82  ALA A CA  1 
ATOM   644  C  C   . ALA A 1 83  ? 17.304 6.302  6.760   1.00 23.44  ? 82  ALA A C   1 
ATOM   645  O  O   . ALA A 1 83  ? 17.073 5.378  6.016   1.00 26.65  ? 82  ALA A O   1 
ATOM   646  C  CB  . ALA A 1 83  ? 15.346 7.092  7.913   1.00 31.06  ? 82  ALA A CB  1 
ATOM   647  N  N   . LYS A 1 84  ? 18.051 7.313  6.445   1.00 23.23  ? 83  LYS A N   1 
ATOM   648  C  CA  . LYS A 1 84  ? 18.723 7.358  5.184   1.00 20.56  ? 83  LYS A CA  1 
ATOM   649  C  C   . LYS A 1 84  ? 20.047 6.607  5.181   1.00 17.43  ? 83  LYS A C   1 
ATOM   650  O  O   . LYS A 1 84  ? 20.445 6.056  4.169   1.00 24.39  ? 83  LYS A O   1 
ATOM   651  C  CB  . LYS A 1 84  ? 19.011 8.791  4.797   1.00 37.54  ? 83  LYS A CB  1 
ATOM   652  C  CG  . LYS A 1 84  ? 17.832 9.482  4.153   1.00 56.41  ? 83  LYS A CG  1 
ATOM   653  C  CD  . LYS A 1 84  ? 17.059 10.324 5.158   1.00 100.00 ? 83  LYS A CD  1 
ATOM   654  C  CE  . LYS A 1 84  ? 16.230 11.420 4.494   1.00 100.00 ? 83  LYS A CE  1 
ATOM   655  N  NZ  . LYS A 1 84  ? 16.988 12.250 3.539   1.00 100.00 ? 83  LYS A NZ  1 
ATOM   656  N  N   . LEU A 1 85  ? 20.758 6.628  6.288   1.00 22.02  ? 84  LEU A N   1 
ATOM   657  C  CA  . LEU A 1 85  ? 22.056 5.991  6.277   1.00 21.01  ? 84  LEU A CA  1 
ATOM   658  C  C   . LEU A 1 85  ? 22.052 4.512  6.549   1.00 18.28  ? 84  LEU A C   1 
ATOM   659  O  O   . LEU A 1 85  ? 22.826 3.759  6.003   1.00 17.24  ? 84  LEU A O   1 
ATOM   660  C  CB  . LEU A 1 85  ? 23.084 6.740  7.141   1.00 14.43  ? 84  LEU A CB  1 
ATOM   661  C  CG  . LEU A 1 85  ? 23.203 8.228  6.781   1.00 22.52  ? 84  LEU A CG  1 
ATOM   662  C  CD1 . LEU A 1 85  ? 24.073 8.951  7.804   1.00 14.86  ? 84  LEU A CD1 1 
ATOM   663  C  CD2 . LEU A 1 85  ? 23.747 8.461  5.364   1.00 17.15  ? 84  LEU A CD2 1 
ATOM   664  N  N   . LYS A 1 86  ? 21.192 4.092  7.425   1.00 12.28  ? 85  LYS A N   1 
ATOM   665  C  CA  . LYS A 1 86  ? 21.147 2.720  7.826   1.00 19.73  ? 85  LYS A CA  1 
ATOM   666  C  C   . LYS A 1 86  ? 21.079 1.702  6.720   1.00 20.38  ? 85  LYS A C   1 
ATOM   667  O  O   . LYS A 1 86  ? 21.777 0.716  6.741   1.00 13.55  ? 85  LYS A O   1 
ATOM   668  C  CB  . LYS A 1 86  ? 19.991 2.535  8.779   1.00 18.24  ? 85  LYS A CB  1 
ATOM   669  C  CG  . LYS A 1 86  ? 20.012 1.152  9.398   1.00 20.15  ? 85  LYS A CG  1 
ATOM   670  C  CD  . LYS A 1 86  ? 19.053 1.037  10.564  1.00 30.04  ? 85  LYS A CD  1 
ATOM   671  C  CE  . LYS A 1 86  ? 19.242 -0.249 11.331  1.00 57.19  ? 85  LYS A CE  1 
ATOM   672  N  NZ  . LYS A 1 86  ? 19.297 -1.395 10.428  1.00 34.35  ? 85  LYS A NZ  1 
ATOM   673  N  N   . PRO A 1 87  ? 20.172 1.894  5.781   1.00 14.39  ? 86  PRO A N   1 
ATOM   674  C  CA  . PRO A 1 87  ? 20.022 0.935  4.715   1.00 23.80  ? 86  PRO A CA  1 
ATOM   675  C  C   . PRO A 1 87  ? 21.257 0.868  3.873   1.00 16.45  ? 86  PRO A C   1 
ATOM   676  O  O   . PRO A 1 87  ? 21.596 -0.186 3.406   1.00 12.25  ? 86  PRO A O   1 
ATOM   677  C  CB  . PRO A 1 87  ? 18.819 1.365  3.854   1.00 16.51  ? 86  PRO A CB  1 
ATOM   678  C  CG  . PRO A 1 87  ? 18.240 2.597  4.520   1.00 31.84  ? 86  PRO A CG  1 
ATOM   679  C  CD  . PRO A 1 87  ? 19.143 2.959  5.700   1.00 15.89  ? 86  PRO A CD  1 
ATOM   680  N  N   . VAL A 1 88  ? 21.944 1.978  3.673   1.00 8.94   ? 87  VAL A N   1 
ATOM   681  C  CA  . VAL A 1 88  ? 23.173 1.908  2.871   1.00 15.00  ? 87  VAL A CA  1 
ATOM   682  C  C   . VAL A 1 88  ? 24.248 1.085  3.610   1.00 9.44   ? 87  VAL A C   1 
ATOM   683  O  O   . VAL A 1 88  ? 24.904 0.229  3.051   1.00 15.90  ? 87  VAL A O   1 
ATOM   684  C  CB  . VAL A 1 88  ? 23.670 3.319  2.562   1.00 16.47  ? 87  VAL A CB  1 
ATOM   685  C  CG1 . VAL A 1 88  ? 24.965 3.273  1.731   1.00 15.77  ? 87  VAL A CG1 1 
ATOM   686  C  CG2 . VAL A 1 88  ? 22.537 4.054  1.822   1.00 22.97  ? 87  VAL A CG2 1 
ATOM   687  N  N   . TYR A 1 89  ? 24.437 1.389  4.881   1.00 11.39  ? 88  TYR A N   1 
ATOM   688  C  CA  . TYR A 1 89  ? 25.382 0.713  5.730   1.00 10.39  ? 88  TYR A CA  1 
ATOM   689  C  C   . TYR A 1 89  ? 25.086 -0.765 5.725   1.00 17.58  ? 88  TYR A C   1 
ATOM   690  O  O   . TYR A 1 89  ? 25.946 -1.593 5.526   1.00 11.66  ? 88  TYR A O   1 
ATOM   691  C  CB  . TYR A 1 89  ? 25.276 1.289  7.168   1.00 13.22  ? 88  TYR A CB  1 
ATOM   692  C  CG  . TYR A 1 89  ? 26.347 0.813  8.108   1.00 13.98  ? 88  TYR A CG  1 
ATOM   693  C  CD1 . TYR A 1 89  ? 27.567 1.492  8.202   1.00 12.88  ? 88  TYR A CD1 1 
ATOM   694  C  CD2 . TYR A 1 89  ? 26.122 -0.340 8.860   1.00 18.49  ? 88  TYR A CD2 1 
ATOM   695  C  CE1 . TYR A 1 89  ? 28.539 1.015  9.077   1.00 11.29  ? 88  TYR A CE1 1 
ATOM   696  C  CE2 . TYR A 1 89  ? 27.092 -0.824 9.742   1.00 21.65  ? 88  TYR A CE2 1 
ATOM   697  C  CZ  . TYR A 1 89  ? 28.296 -0.118 9.854   1.00 27.56  ? 88  TYR A CZ  1 
ATOM   698  O  OH  . TYR A 1 89  ? 29.293 -0.539 10.690  1.00 19.14  ? 88  TYR A OH  1 
ATOM   699  N  N   . ASP A 1 90  ? 23.832 -1.124 5.919   1.00 17.02  ? 89  ASP A N   1 
ATOM   700  C  CA  . ASP A 1 90  ? 23.523 -2.557 5.942   1.00 12.53  ? 89  ASP A CA  1 
ATOM   701  C  C   . ASP A 1 90  ? 23.835 -3.246 4.644   1.00 19.78  ? 89  ASP A C   1 
ATOM   702  O  O   . ASP A 1 90  ? 24.130 -4.440 4.597   1.00 19.70  ? 89  ASP A O   1 
ATOM   703  C  CB  . ASP A 1 90  ? 22.025 -2.762 6.239   1.00 13.98  ? 89  ASP A CB  1 
ATOM   704  C  CG  . ASP A 1 90  ? 21.623 -2.512 7.688   1.00 18.35  ? 89  ASP A CG  1 
ATOM   705  O  OD1 . ASP A 1 90  ? 22.625 -2.513 8.544   1.00 21.36  ? 89  ASP A OD1 1 
ATOM   706  O  OD2 . ASP A 1 90  ? 20.472 -2.208 7.981   1.00 26.04  ? 89  ASP A OD2 1 
ATOM   707  N  N   . SER A 1 91  ? 23.706 -2.548 3.547   1.00 14.57  ? 90  SER A N   1 
ATOM   708  C  CA  . SER A 1 91  ? 23.954 -3.194 2.308   1.00 8.87   ? 90  SER A CA  1 
ATOM   709  C  C   . SER A 1 91  ? 25.417 -3.393 2.009   1.00 14.58  ? 90  SER A C   1 
ATOM   710  O  O   . SER A 1 91  ? 25.759 -4.110 1.111   1.00 13.83  ? 90  SER A O   1 
ATOM   711  C  CB  . SER A 1 91  ? 23.360 -2.367 1.172   1.00 11.36  ? 90  SER A CB  1 
ATOM   712  O  OG  . SER A 1 91  ? 24.184 -1.188 0.936   1.00 10.22  ? 90  SER A OG  1 
ATOM   713  N  N   . LEU A 1 92  ? 26.319 -2.721 2.679   1.00 9.02   ? 91  LEU A N   1 
ATOM   714  C  CA  . LEU A 1 92  ? 27.732 -2.802 2.300   1.00 11.78  ? 91  LEU A CA  1 
ATOM   715  C  C   . LEU A 1 92  ? 28.587 -3.873 2.969   1.00 13.30  ? 91  LEU A C   1 
ATOM   716  O  O   . LEU A 1 92  ? 28.267 -4.312 4.084   1.00 13.45  ? 91  LEU A O   1 
ATOM   717  C  CB  . LEU A 1 92  ? 28.411 -1.449 2.721   1.00 13.41  ? 91  LEU A CB  1 
ATOM   718  C  CG  . LEU A 1 92  ? 27.846 -0.179 2.025   1.00 21.01  ? 91  LEU A CG  1 
ATOM   719  C  CD1 . LEU A 1 92  ? 28.274 1.109  2.730   1.00 20.41  ? 91  LEU A CD1 1 
ATOM   720  C  CD2 . LEU A 1 92  ? 28.340 -0.137 0.573   1.00 12.12  ? 91  LEU A CD2 1 
ATOM   721  N  N   . ASP A 1 93  ? 29.760 -4.129 2.373   1.00 13.62  ? 92  ASP A N   1 
ATOM   722  C  CA  . ASP A 1 93  ? 30.778 -5.008 2.979   1.00 8.68   ? 92  ASP A CA  1 
ATOM   723  C  C   . ASP A 1 93  ? 31.551 -4.287 4.101   1.00 11.62  ? 92  ASP A C   1 
ATOM   724  O  O   . ASP A 1 93  ? 31.421 -3.067 4.283   1.00 13.09  ? 92  ASP A O   1 
ATOM   725  C  CB  . ASP A 1 93  ? 31.754 -5.499 1.911   1.00 15.01  ? 92  ASP A CB  1 
ATOM   726  C  CG  . ASP A 1 93  ? 32.453 -4.336 1.245   1.00 17.31  ? 92  ASP A CG  1 
ATOM   727  O  OD1 . ASP A 1 93  ? 31.687 -3.841 0.316   1.00 19.88  ? 92  ASP A OD1 1 
ATOM   728  O  OD2 . ASP A 1 93  ? 33.551 -3.863 1.606   1.00 17.12  ? 92  ASP A OD2 1 
ATOM   729  N  N   . ALA A 1 94  ? 32.420 -5.011 4.878   1.00 13.64  ? 93  ALA A N   1 
ATOM   730  C  CA  . ALA A 1 94  ? 33.120 -4.407 5.979   1.00 12.75  ? 93  ALA A CA  1 
ATOM   731  C  C   . ALA A 1 94  ? 34.013 -3.209 5.631   1.00 13.28  ? 93  ALA A C   1 
ATOM   732  O  O   . ALA A 1 94  ? 34.044 -2.225 6.401   1.00 17.02  ? 93  ALA A O   1 
ATOM   733  C  CB  . ALA A 1 94  ? 33.784 -5.429 6.943   1.00 14.03  ? 93  ALA A CB  1 
ATOM   734  N  N   . VAL A 1 95  ? 34.716 -3.276 4.497   1.00 11.99  ? 94  VAL A N   1 
ATOM   735  C  CA  . VAL A 1 95  ? 35.593 -2.186 4.133   1.00 12.23  ? 94  VAL A CA  1 
ATOM   736  C  C   . VAL A 1 95  ? 34.828 -0.921 3.787   1.00 14.90  ? 94  VAL A C   1 
ATOM   737  O  O   . VAL A 1 95  ? 35.066 0.158  4.293   1.00 15.44  ? 94  VAL A O   1 
ATOM   738  C  CB  . VAL A 1 95  ? 36.542 -2.648 3.063   1.00 17.84  ? 94  VAL A CB  1 
ATOM   739  C  CG1 . VAL A 1 95  ? 37.534 -1.541 2.775   1.00 13.16  ? 94  VAL A CG1 1 
ATOM   740  C  CG2 . VAL A 1 95  ? 37.310 -3.751 3.719   1.00 16.03  ? 94  VAL A CG2 1 
ATOM   741  N  N   . ARG A 1 96  ? 33.855 -1.074 2.938   1.00 15.37  ? 95  ARG A N   1 
ATOM   742  C  CA  . ARG A 1 96  ? 33.083 0.083  2.584   1.00 11.67  ? 95  ARG A CA  1 
ATOM   743  C  C   . ARG A 1 96  ? 32.337 0.677  3.750   1.00 14.05  ? 95  ARG A C   1 
ATOM   744  O  O   . ARG A 1 96  ? 32.135 1.882  3.779   1.00 13.31  ? 95  ARG A O   1 
ATOM   745  C  CB  . ARG A 1 96  ? 32.214 -0.255 1.396   1.00 12.67  ? 95  ARG A CB  1 
ATOM   746  C  CG  . ARG A 1 96  ? 33.035 -0.628 0.191   1.00 8.67   ? 95  ARG A CG  1 
ATOM   747  C  CD  . ARG A 1 96  ? 32.089 -0.848 -0.997  1.00 15.53  ? 95  ARG A CD  1 
ATOM   748  N  NE  . ARG A 1 96  ? 32.759 -0.970 -2.267  1.00 12.99  ? 95  ARG A NE  1 
ATOM   749  C  CZ  . ARG A 1 96  ? 33.154 -2.145 -2.806  1.00 16.72  ? 95  ARG A CZ  1 
ATOM   750  N  NH1 . ARG A 1 96  ? 33.019 -3.302 -2.167  1.00 17.07  ? 95  ARG A NH1 1 
ATOM   751  N  NH2 . ARG A 1 96  ? 33.754 -2.136 -4.013  1.00 13.47  ? 95  ARG A NH2 1 
ATOM   752  N  N   . ARG A 1 97  ? 31.900 -0.150 4.735   1.00 10.69  ? 96  ARG A N   1 
ATOM   753  C  CA  . ARG A 1 97  ? 31.200 0.392  5.926   1.00 13.73  ? 96  ARG A CA  1 
ATOM   754  C  C   . ARG A 1 97  ? 32.117 1.370  6.626   1.00 13.84  ? 96  ARG A C   1 
ATOM   755  O  O   . ARG A 1 97  ? 31.696 2.416  7.051   1.00 12.80  ? 96  ARG A O   1 
ATOM   756  C  CB  . ARG A 1 97  ? 30.720 -0.637 6.952   1.00 9.35   ? 96  ARG A CB  1 
ATOM   757  C  CG  . ARG A 1 97  ? 29.629 -1.487 6.382   1.00 11.15  ? 96  ARG A CG  1 
ATOM   758  C  CD  . ARG A 1 97  ? 29.204 -2.600 7.326   1.00 24.71  ? 96  ARG A CD  1 
ATOM   759  N  NE  . ARG A 1 97  ? 28.000 -3.264 6.835   1.00 17.50  ? 96  ARG A NE  1 
ATOM   760  C  CZ  . ARG A 1 97  ? 27.458 -4.352 7.321   1.00 29.09  ? 96  ARG A CZ  1 
ATOM   761  N  NH1 . ARG A 1 97  ? 27.995 -4.977 8.365   1.00 27.01  ? 96  ARG A NH1 1 
ATOM   762  N  NH2 . ARG A 1 97  ? 26.373 -4.851 6.708   1.00 11.86  ? 96  ARG A NH2 1 
ATOM   763  N  N   . ALA A 1 98  ? 33.383 1.004  6.679   1.00 11.36  ? 97  ALA A N   1 
ATOM   764  C  CA  . ALA A 1 98  ? 34.385 1.872  7.222   1.00 13.36  ? 97  ALA A CA  1 
ATOM   765  C  C   . ALA A 1 98  ? 34.465 3.206  6.445   1.00 9.93   ? 97  ALA A C   1 
ATOM   766  O  O   . ALA A 1 98  ? 34.585 4.274  7.053   1.00 11.94  ? 97  ALA A O   1 
ATOM   767  C  CB  . ALA A 1 98  ? 35.739 1.161  7.218   1.00 12.64  ? 97  ALA A CB  1 
ATOM   768  N  N   . ALA A 1 99  ? 34.387 3.193  5.108   1.00 16.06  ? 98  ALA A N   1 
ATOM   769  C  CA  . ALA A 1 99  ? 34.444 4.442  4.388   1.00 16.82  ? 98  ALA A CA  1 
ATOM   770  C  C   . ALA A 1 99  ? 33.259 5.333  4.717   1.00 12.30  ? 98  ALA A C   1 
ATOM   771  O  O   . ALA A 1 99  ? 33.369 6.560  4.763   1.00 12.15  ? 98  ALA A O   1 
ATOM   772  C  CB  . ALA A 1 99  ? 34.538 4.221  2.889   1.00 14.10  ? 98  ALA A CB  1 
ATOM   773  N  N   . LEU A 1 100 ? 32.095 4.713  4.968   1.00 8.00   ? 99  LEU A N   1 
ATOM   774  C  CA  . LEU A 1 100 ? 30.927 5.509  5.308   1.00 5.74   ? 99  LEU A CA  1 
ATOM   775  C  C   . LEU A 1 100 ? 31.057 6.074  6.700   1.00 11.93  ? 99  LEU A C   1 
ATOM   776  O  O   . LEU A 1 100 ? 30.649 7.200  6.951   1.00 10.04  ? 99  LEU A O   1 
ATOM   777  C  CB  . LEU A 1 100 ? 29.614 4.661  5.197   1.00 9.92   ? 99  LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 100 ? 28.307 5.438  5.355   1.00 8.37   ? 99  LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 100 ? 28.051 6.270  4.146   1.00 17.73  ? 99  LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 100 ? 27.159 4.416  5.465   1.00 16.88  ? 99  LEU A CD2 1 
ATOM   781  N  N   . ILE A 1 101 ? 31.634 5.312  7.621   1.00 7.36   ? 100 ILE A N   1 
ATOM   782  C  CA  . ILE A 1 101 ? 31.822 5.825  8.930   1.00 9.58   ? 100 ILE A CA  1 
ATOM   783  C  C   . ILE A 1 101 ? 32.777 7.033  8.858   1.00 14.81  ? 100 ILE A C   1 
ATOM   784  O  O   . ILE A 1 101 ? 32.631 8.064  9.528   1.00 11.71  ? 100 ILE A O   1 
ATOM   785  C  CB  . ILE A 1 101 ? 32.350 4.750  9.854   1.00 10.49  ? 100 ILE A CB  1 
ATOM   786  C  CG1 . ILE A 1 101 ? 31.331 3.584  10.022  1.00 8.75   ? 100 ILE A CG1 1 
ATOM   787  C  CG2 . ILE A 1 101 ? 32.757 5.388  11.195  1.00 10.22  ? 100 ILE A CG2 1 
ATOM   788  C  CD1 . ILE A 1 101 ? 31.942 2.398  10.770  1.00 6.42   ? 100 ILE A CD1 1 
ATOM   789  N  N   . ASN A 1 102 ? 33.773 6.944  7.998   1.00 12.01  ? 101 ASN A N   1 
ATOM   790  C  CA  . ASN A 1 102 ? 34.706 8.049  7.890   1.00 11.92  ? 101 ASN A CA  1 
ATOM   791  C  C   . ASN A 1 102 ? 34.024 9.317  7.447   1.00 12.11  ? 101 ASN A C   1 
ATOM   792  O  O   . ASN A 1 102 ? 34.228 10.382 8.059   1.00 11.85  ? 101 ASN A O   1 
ATOM   793  C  CB  . ASN A 1 102 ? 35.782 7.646  6.894   1.00 9.73   ? 101 ASN A CB  1 
ATOM   794  C  CG  . ASN A 1 102 ? 36.993 8.567  6.814   1.00 15.46  ? 101 ASN A CG  1 
ATOM   795  O  OD1 . ASN A 1 102 ? 36.848 9.768  6.620   1.00 15.84  ? 101 ASN A OD1 1 
ATOM   796  N  ND2 . ASN A 1 102 ? 38.177 7.983  6.918   1.00 9.11   ? 101 ASN A ND2 1 
ATOM   797  N  N   . MET A 1 103 ? 33.244 9.217  6.364   1.00 8.87   ? 102 MET A N   1 
ATOM   798  C  CA  . MET A 1 103 ? 32.574 10.407 5.911   1.00 17.96  ? 102 MET A CA  1 
ATOM   799  C  C   . MET A 1 103 ? 31.703 10.988 7.041   1.00 25.03  ? 102 MET A C   1 
ATOM   800  O  O   . MET A 1 103 ? 31.605 12.212 7.209   1.00 12.85  ? 102 MET A O   1 
ATOM   801  C  CB  . MET A 1 103 ? 31.642 10.128 4.714   1.00 16.90  ? 102 MET A CB  1 
ATOM   802  C  CG  . MET A 1 103 ? 32.348 9.824  3.412   1.00 17.35  ? 102 MET A CG  1 
ATOM   803  S  SD  . MET A 1 103 ? 31.151 9.640  2.048   1.00 20.22  ? 102 MET A SD  1 
ATOM   804  C  CE  . MET A 1 103 ? 30.637 11.361 1.847   1.00 16.02  ? 102 MET A CE  1 
ATOM   805  N  N   . VAL A 1 104 ? 30.991 10.082 7.770   1.00 12.09  ? 103 VAL A N   1 
ATOM   806  C  CA  . VAL A 1 104 ? 30.129 10.528 8.849   1.00 12.44  ? 103 VAL A CA  1 
ATOM   807  C  C   . VAL A 1 104 ? 30.908 11.220 9.945   1.00 15.71  ? 103 VAL A C   1 
ATOM   808  O  O   . VAL A 1 104 ? 30.468 12.229 10.480  1.00 17.43  ? 103 VAL A O   1 
ATOM   809  C  CB  . VAL A 1 104 ? 29.184 9.457  9.379   1.00 14.83  ? 103 VAL A CB  1 
ATOM   810  C  CG1 . VAL A 1 104 ? 28.396 10.024 10.565  1.00 15.30  ? 103 VAL A CG1 1 
ATOM   811  C  CG2 . VAL A 1 104 ? 28.191 9.051  8.295   1.00 11.85  ? 103 VAL A CG2 1 
ATOM   812  N  N   . PHE A 1 105 ? 32.076 10.692 10.263  1.00 14.64  ? 104 PHE A N   1 
ATOM   813  C  CA  . PHE A 1 105 ? 32.869 11.292 11.298  1.00 10.30  ? 104 PHE A CA  1 
ATOM   814  C  C   . PHE A 1 105 ? 33.294 12.708 10.897  1.00 11.21  ? 104 PHE A C   1 
ATOM   815  O  O   . PHE A 1 105 ? 33.273 13.662 11.652  1.00 15.44  ? 104 PHE A O   1 
ATOM   816  C  CB  . PHE A 1 105 ? 34.087 10.388 11.429  1.00 13.82  ? 104 PHE A CB  1 
ATOM   817  C  CG  . PHE A 1 105 ? 35.010 10.789 12.543  1.00 11.55  ? 104 PHE A CG  1 
ATOM   818  C  CD1 . PHE A 1 105 ? 35.981 11.761 12.332  1.00 12.22  ? 104 PHE A CD1 1 
ATOM   819  C  CD2 . PHE A 1 105 ? 34.985 10.127 13.771  1.00 12.10  ? 104 PHE A CD2 1 
ATOM   820  C  CE1 . PHE A 1 105 ? 36.864 12.117 13.352  1.00 14.96  ? 104 PHE A CE1 1 
ATOM   821  C  CE2 . PHE A 1 105 ? 35.868 10.455 14.796  1.00 12.74  ? 104 PHE A CE2 1 
ATOM   822  C  CZ  . PHE A 1 105 ? 36.828 11.447 14.576  1.00 12.94  ? 104 PHE A CZ  1 
ATOM   823  N  N   . GLN A 1 106 ? 33.682 12.867 9.657   1.00 12.76  ? 105 GLN A N   1 
ATOM   824  C  CA  . GLN A 1 106 ? 34.145 14.172 9.178   1.00 16.70  ? 105 GLN A CA  1 
ATOM   825  C  C   . GLN A 1 106 ? 33.050 15.220 9.003   1.00 18.05  ? 105 GLN A C   1 
ATOM   826  O  O   . GLN A 1 106 ? 33.212 16.375 9.341   1.00 20.67  ? 105 GLN A O   1 
ATOM   827  C  CB  . GLN A 1 106 ? 34.815 13.967 7.785   1.00 16.02  ? 105 GLN A CB  1 
ATOM   828  C  CG  . GLN A 1 106 ? 35.385 15.280 7.171   1.00 20.22  ? 105 GLN A CG  1 
ATOM   829  C  CD  . GLN A 1 106 ? 36.108 15.140 5.843   1.00 16.12  ? 105 GLN A CD  1 
ATOM   830  O  OE1 . GLN A 1 106 ? 36.130 14.060 5.241   1.00 17.14  ? 105 GLN A OE1 1 
ATOM   831  N  NE2 . GLN A 1 106 ? 36.743 16.236 5.393   1.00 15.60  ? 105 GLN A NE2 1 
ATOM   832  N  N   . MET A 1 107 ? 31.964 14.801 8.383   1.00 18.48  ? 106 MET A N   1 
ATOM   833  C  CA  . MET A 1 107 ? 30.906 15.688 7.982   1.00 26.87  ? 106 MET A CA  1 
ATOM   834  C  C   . MET A 1 107 ? 29.572 15.635 8.692   1.00 25.37  ? 106 MET A C   1 
ATOM   835  O  O   . MET A 1 107 ? 28.690 16.461 8.487   1.00 26.73  ? 106 MET A O   1 
ATOM   836  C  CB  . MET A 1 107 ? 30.859 15.890 6.450   1.00 25.90  ? 106 MET A CB  1 
ATOM   837  C  CG  . MET A 1 107 ? 30.205 14.862 5.571   1.00 33.88  ? 106 MET A CG  1 
ATOM   838  S  SD  . MET A 1 107 ? 30.686 15.219 3.855   1.00 37.47  ? 106 MET A SD  1 
ATOM   839  C  CE  . MET A 1 107 ? 32.164 14.199 3.743   1.00 40.94  ? 106 MET A CE  1 
ATOM   840  N  N   . GLY A 1 108 ? 29.380 14.666 9.523   1.00 14.16  ? 107 GLY A N   1 
ATOM   841  C  CA  . GLY A 1 108 ? 28.118 14.665 10.161  1.00 13.18  ? 107 GLY A CA  1 
ATOM   842  C  C   . GLY A 1 108 ? 27.101 13.889 9.384   1.00 13.65  ? 107 GLY A C   1 
ATOM   843  O  O   . GLY A 1 108 ? 27.106 13.779 8.176   1.00 17.43  ? 107 GLY A O   1 
ATOM   844  N  N   . GLU A 1 109 ? 26.241 13.308 10.140  1.00 19.07  ? 108 GLU A N   1 
ATOM   845  C  CA  . GLU A 1 109 ? 25.215 12.468 9.632   1.00 21.13  ? 108 GLU A CA  1 
ATOM   846  C  C   . GLU A 1 109 ? 24.322 13.227 8.672   1.00 26.92  ? 108 GLU A C   1 
ATOM   847  O  O   . GLU A 1 109 ? 23.877 12.766 7.611   1.00 21.11  ? 108 GLU A O   1 
ATOM   848  C  CB  . GLU A 1 109 ? 24.514 11.911 10.905  1.00 21.79  ? 108 GLU A CB  1 
ATOM   849  C  CG  . GLU A 1 109 ? 23.260 11.097 10.674  1.00 59.51  ? 108 GLU A CG  1 
ATOM   850  C  CD  . GLU A 1 109 ? 22.507 11.033 11.949  1.00 94.11  ? 108 GLU A CD  1 
ATOM   851  O  OE1 . GLU A 1 109 ? 23.314 11.064 12.979  1.00 69.99  ? 108 GLU A OE1 1 
ATOM   852  O  OE2 . GLU A 1 109 ? 21.284 10.972 12.007  1.00 66.47  ? 108 GLU A OE2 1 
ATOM   853  N  N   . THR A 1 110 ? 24.055 14.456 9.036   1.00 35.78  ? 109 THR A N   1 
ATOM   854  C  CA  . THR A 1 110 ? 23.219 15.238 8.185   1.00 22.12  ? 109 THR A CA  1 
ATOM   855  C  C   . THR A 1 110 ? 23.902 15.521 6.870   1.00 43.21  ? 109 THR A C   1 
ATOM   856  O  O   . THR A 1 110 ? 23.257 15.498 5.817   1.00 28.10  ? 109 THR A O   1 
ATOM   857  C  CB  . THR A 1 110 ? 22.763 16.547 8.873   1.00 31.22  ? 109 THR A CB  1 
ATOM   858  O  OG1 . THR A 1 110 ? 21.968 16.193 9.976   1.00 44.82  ? 109 THR A OG1 1 
ATOM   859  C  CG2 . THR A 1 110 ? 21.933 17.367 7.890   1.00 40.05  ? 109 THR A CG2 1 
ATOM   860  N  N   . GLY A 1 111 ? 25.203 15.813 6.949   1.00 24.96  ? 110 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 111 ? 25.949 16.111 5.748   1.00 20.79  ? 110 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 111 ? 25.970 14.917 4.814   1.00 28.72  ? 110 GLY A C   1 
ATOM   863  O  O   . GLY A 1 111 ? 25.692 15.084 3.622   1.00 24.83  ? 110 GLY A O   1 
ATOM   864  N  N   . VAL A 1 112 ? 26.301 13.718 5.367   1.00 19.44  ? 111 VAL A N   1 
ATOM   865  C  CA  . VAL A 1 112 ? 26.375 12.555 4.490   1.00 17.92  ? 111 VAL A CA  1 
ATOM   866  C  C   . VAL A 1 112 ? 25.033 12.186 3.872   1.00 22.93  ? 111 VAL A C   1 
ATOM   867  O  O   . VAL A 1 112 ? 24.919 11.796 2.707   1.00 15.51  ? 111 VAL A O   1 
ATOM   868  C  CB  . VAL A 1 112 ? 27.000 11.400 5.197   1.00 18.25  ? 111 VAL A CB  1 
ATOM   869  C  CG1 . VAL A 1 112 ? 27.018 10.268 4.179   1.00 11.22  ? 111 VAL A CG1 1 
ATOM   870  C  CG2 . VAL A 1 112 ? 28.414 11.849 5.559   1.00 16.14  ? 111 VAL A CG2 1 
ATOM   871  N  N   . ALA A 1 113 ? 24.004 12.308 4.693   1.00 21.49  ? 112 ALA A N   1 
ATOM   872  C  CA  . ALA A 1 113 ? 22.643 12.004 4.286   1.00 18.29  ? 112 ALA A CA  1 
ATOM   873  C  C   . ALA A 1 113 ? 22.212 12.781 3.021   1.00 44.74  ? 112 ALA A C   1 
ATOM   874  O  O   . ALA A 1 113 ? 21.336 12.340 2.252   1.00 29.99  ? 112 ALA A O   1 
ATOM   875  C  CB  . ALA A 1 113 ? 21.654 12.122 5.471   1.00 22.93  ? 112 ALA A CB  1 
ATOM   876  N  N   . GLY A 1 114 ? 22.882 13.917 2.761   1.00 25.37  ? 113 GLY A N   1 
ATOM   877  C  CA  . GLY A 1 114 ? 22.600 14.746 1.574   1.00 38.37  ? 113 GLY A CA  1 
ATOM   878  C  C   . GLY A 1 114 ? 23.208 14.284 0.243   1.00 46.09  ? 113 GLY A C   1 
ATOM   879  O  O   . GLY A 1 114 ? 22.964 14.846 -0.838  1.00 41.77  ? 113 GLY A O   1 
ATOM   880  N  N   . PHE A 1 115 ? 24.051 13.273 0.296   1.00 20.66  ? 114 PHE A N   1 
ATOM   881  C  CA  . PHE A 1 115 ? 24.644 12.773 -0.918  1.00 14.78  ? 114 PHE A CA  1 
ATOM   882  C  C   . PHE A 1 115 ? 23.682 11.725 -1.412  1.00 19.78  ? 114 PHE A C   1 
ATOM   883  O  O   . PHE A 1 115 ? 23.978 10.576 -1.601  1.00 16.19  ? 114 PHE A O   1 
ATOM   884  C  CB  . PHE A 1 115 ? 26.041 12.192 -0.633  1.00 19.30  ? 114 PHE A CB  1 
ATOM   885  C  CG  . PHE A 1 115 ? 27.195 13.184 -0.386  1.00 24.87  ? 114 PHE A CG  1 
ATOM   886  C  CD1 . PHE A 1 115 ? 27.206 14.092 0.666   1.00 31.09  ? 114 PHE A CD1 1 
ATOM   887  C  CD2 . PHE A 1 115 ? 28.301 13.208 -1.244  1.00 27.92  ? 114 PHE A CD2 1 
ATOM   888  C  CE1 . PHE A 1 115 ? 28.265 14.987 0.865   1.00 24.83  ? 114 PHE A CE1 1 
ATOM   889  C  CE2 . PHE A 1 115 ? 29.377 14.089 -1.070  1.00 26.33  ? 114 PHE A CE2 1 
ATOM   890  C  CZ  . PHE A 1 115 ? 29.343 15.002 -0.023  1.00 27.41  ? 114 PHE A CZ  1 
ATOM   891  N  N   . THR A 1 116 ? 22.483 12.154 -1.573  1.00 16.64  ? 115 THR A N   1 
ATOM   892  C  CA  . THR A 1 116 ? 21.414 11.290 -1.971  1.00 14.45  ? 115 THR A CA  1 
ATOM   893  C  C   . THR A 1 116 ? 21.773 10.395 -3.122  1.00 23.36  ? 115 THR A C   1 
ATOM   894  O  O   . THR A 1 116 ? 21.541 9.185  -3.135  1.00 17.73  ? 115 THR A O   1 
ATOM   895  C  CB  . THR A 1 116 ? 20.200 12.141 -2.449  1.00 29.15  ? 115 THR A CB  1 
ATOM   896  O  OG1 . THR A 1 116 ? 19.778 13.001 -1.431  1.00 41.72  ? 115 THR A OG1 1 
ATOM   897  C  CG2 . THR A 1 116 ? 19.046 11.247 -2.864  1.00 44.66  ? 115 THR A CG2 1 
ATOM   898  N  N   . ASN A 1 117 ? 22.253 11.025 -4.159  1.00 17.58  ? 116 ASN A N   1 
ATOM   899  C  CA  . ASN A 1 117 ? 22.564 10.272 -5.359  1.00 20.45  ? 116 ASN A CA  1 
ATOM   900  C  C   . ASN A 1 117 ? 23.683 9.256  -5.168  1.00 18.67  ? 116 ASN A C   1 
ATOM   901  O  O   . ASN A 1 117 ? 23.583 8.133  -5.662  1.00 17.59  ? 116 ASN A O   1 
ATOM   902  C  CB  . ASN A 1 117 ? 22.781 11.143 -6.638  1.00 35.70  ? 116 ASN A CB  1 
ATOM   903  C  CG  . ASN A 1 117 ? 21.584 12.010 -7.008  1.00 39.35  ? 116 ASN A CG  1 
ATOM   904  O  OD1 . ASN A 1 117 ? 20.443 11.578 -6.884  1.00 34.72  ? 116 ASN A OD1 1 
ATOM   905  N  ND2 . ASN A 1 117 ? 21.817 13.247 -7.422  1.00 30.21  ? 116 ASN A ND2 1 
ATOM   906  N  N   . SER A 1 118 ? 24.745 9.673  -4.489  1.00 17.34  ? 117 SER A N   1 
ATOM   907  C  CA  . SER A 1 118 ? 25.837 8.759  -4.263  1.00 12.93  ? 117 SER A CA  1 
ATOM   908  C  C   . SER A 1 118 ? 25.362 7.585  -3.442  1.00 16.14  ? 117 SER A C   1 
ATOM   909  O  O   . SER A 1 118 ? 25.728 6.487  -3.724  1.00 18.38  ? 117 SER A O   1 
ATOM   910  C  CB  . SER A 1 118 ? 26.938 9.410  -3.485  1.00 14.14  ? 117 SER A CB  1 
ATOM   911  O  OG  . SER A 1 118 ? 27.296 10.585 -4.151  1.00 24.02  ? 117 SER A OG  1 
ATOM   912  N  N   . LEU A 1 119 ? 24.584 7.869  -2.409  1.00 17.06  ? 118 LEU A N   1 
ATOM   913  C  CA  . LEU A 1 119 ? 24.033 6.857  -1.523  1.00 16.03  ? 118 LEU A CA  1 
ATOM   914  C  C   . LEU A 1 119 ? 23.255 5.800  -2.277  1.00 19.61  ? 118 LEU A C   1 
ATOM   915  O  O   . LEU A 1 119 ? 23.322 4.606  -1.992  1.00 16.36  ? 118 LEU A O   1 
ATOM   916  C  CB  . LEU A 1 119 ? 23.191 7.450  -0.361  1.00 24.00  ? 118 LEU A CB  1 
ATOM   917  C  CG  . LEU A 1 119 ? 23.976 8.392  0.599   1.00 20.41  ? 118 LEU A CG  1 
ATOM   918  C  CD1 . LEU A 1 119 ? 23.046 8.998  1.620   1.00 12.47  ? 118 LEU A CD1 1 
ATOM   919  C  CD2 . LEU A 1 119 ? 25.064 7.646  1.367   1.00 18.60  ? 118 LEU A CD2 1 
ATOM   920  N  N   . ARG A 1 120 ? 22.473 6.250  -3.222  1.00 15.66  ? 119 ARG A N   1 
ATOM   921  C  CA  . ARG A 1 120 ? 21.680 5.292  -3.965  1.00 17.62  ? 119 ARG A CA  1 
ATOM   922  C  C   . ARG A 1 120 ? 22.574 4.438  -4.831  1.00 16.45  ? 119 ARG A C   1 
ATOM   923  O  O   . ARG A 1 120 ? 22.337 3.249  -5.007  1.00 20.45  ? 119 ARG A O   1 
ATOM   924  C  CB  . ARG A 1 120 ? 20.634 6.045  -4.756  1.00 24.49  ? 119 ARG A CB  1 
ATOM   925  C  CG  . ARG A 1 120 ? 19.862 5.229  -5.775  1.00 40.26  ? 119 ARG A CG  1 
ATOM   926  C  CD  . ARG A 1 120 ? 19.112 6.108  -6.790  1.00 94.67  ? 119 ARG A CD  1 
ATOM   927  N  NE  . ARG A 1 120 ? 19.802 6.260  -8.085  1.00 100.00 ? 119 ARG A NE  1 
ATOM   928  C  CZ  . ARG A 1 120 ? 20.369 7.401  -8.528  1.00 100.00 ? 119 ARG A CZ  1 
ATOM   929  N  NH1 . ARG A 1 120 ? 20.340 8.541  -7.819  1.00 100.00 ? 119 ARG A NH1 1 
ATOM   930  N  NH2 . ARG A 1 120 ? 20.967 7.387  -9.733  1.00 100.00 ? 119 ARG A NH2 1 
ATOM   931  N  N   . MET A 1 121 ? 23.653 5.056  -5.371  1.00 11.89  ? 120 MET A N   1 
ATOM   932  C  CA  . MET A 1 121 ? 24.529 4.265  -6.182  1.00 14.24  ? 120 MET A CA  1 
ATOM   933  C  C   . MET A 1 121 ? 25.309 3.297  -5.329  1.00 19.32  ? 120 MET A C   1 
ATOM   934  O  O   . MET A 1 121 ? 25.660 2.222  -5.777  1.00 20.66  ? 120 MET A O   1 
ATOM   935  C  CB  . MET A 1 121 ? 25.518 5.098  -7.021  1.00 13.26  ? 120 MET A CB  1 
ATOM   936  C  CG  . MET A 1 121 ? 24.812 5.882  -8.121  1.00 34.94  ? 120 MET A CG  1 
ATOM   937  S  SD  . MET A 1 121 ? 25.950 7.124  -8.703  1.00 34.29  ? 120 MET A SD  1 
ATOM   938  C  CE  . MET A 1 121 ? 24.874 8.369  -9.454  1.00 36.65  ? 120 MET A CE  1 
ATOM   939  N  N   . LEU A 1 122 ? 25.624 3.680  -4.114  1.00 17.21  ? 121 LEU A N   1 
ATOM   940  C  CA  . LEU A 1 122 ? 26.392 2.742  -3.281  1.00 10.30  ? 121 LEU A CA  1 
ATOM   941  C  C   . LEU A 1 122 ? 25.490 1.536  -2.941  1.00 19.89  ? 121 LEU A C   1 
ATOM   942  O  O   . LEU A 1 122 ? 25.887 0.385  -2.982  1.00 16.16  ? 121 LEU A O   1 
ATOM   943  C  CB  . LEU A 1 122 ? 26.871 3.449  -2.014  1.00 10.87  ? 121 LEU A CB  1 
ATOM   944  C  CG  . LEU A 1 122 ? 28.041 4.413  -2.267  1.00 19.30  ? 121 LEU A CG  1 
ATOM   945  C  CD1 . LEU A 1 122 ? 28.314 5.225  -0.999  1.00 17.94  ? 121 LEU A CD1 1 
ATOM   946  C  CD2 . LEU A 1 122 ? 29.281 3.645  -2.616  1.00 14.40  ? 121 LEU A CD2 1 
ATOM   947  N  N   . GLN A 1 123 ? 24.241 1.824  -2.648  1.00 10.10  ? 122 GLN A N   1 
ATOM   948  C  CA  . GLN A 1 123 ? 23.352 0.790  -2.330  1.00 12.38  ? 122 GLN A CA  1 
ATOM   949  C  C   . GLN A 1 123 ? 23.198 -0.204 -3.496  1.00 23.58  ? 122 GLN A C   1 
ATOM   950  O  O   . GLN A 1 123 ? 23.120 -1.442 -3.308  1.00 26.28  ? 122 GLN A O   1 
ATOM   951  C  CB  . GLN A 1 123 ? 22.023 1.431  -1.891  1.00 14.12  ? 122 GLN A CB  1 
ATOM   952  C  CG  . GLN A 1 123 ? 21.160 0.304  -1.332  1.00 29.28  ? 122 GLN A CG  1 
ATOM   953  C  CD  . GLN A 1 123 ? 19.989 0.761  -0.526  1.00 100.00 ? 122 GLN A CD  1 
ATOM   954  O  OE1 . GLN A 1 123 ? 19.867 1.956  -0.252  1.00 37.82  ? 122 GLN A OE1 1 
ATOM   955  N  NE2 . GLN A 1 123 ? 19.145 -0.199 -0.139  1.00 100.00 ? 122 GLN A NE2 1 
ATOM   956  N  N   . GLN A 1 124 ? 23.192 0.327  -4.733  1.00 20.89  ? 123 GLN A N   1 
ATOM   957  C  CA  . GLN A 1 124 ? 23.066 -0.504 -5.939  1.00 16.26  ? 123 GLN A CA  1 
ATOM   958  C  C   . GLN A 1 124 ? 24.363 -1.180 -6.368  1.00 27.11  ? 123 GLN A C   1 
ATOM   959  O  O   . GLN A 1 124 ? 24.359 -1.896 -7.349  1.00 28.81  ? 123 GLN A O   1 
ATOM   960  C  CB  . GLN A 1 124 ? 22.528 0.281  -7.153  1.00 18.19  ? 123 GLN A CB  1 
ATOM   961  C  CG  . GLN A 1 124 ? 21.185 0.966  -6.871  1.00 19.93  ? 123 GLN A CG  1 
ATOM   962  C  CD  . GLN A 1 124 ? 20.699 1.713  -8.087  1.00 31.47  ? 123 GLN A CD  1 
ATOM   963  O  OE1 . GLN A 1 124 ? 20.212 1.113  -9.052  1.00 97.91  ? 123 GLN A OE1 1 
ATOM   964  N  NE2 . GLN A 1 124 ? 20.921 3.020  -8.098  1.00 56.01  ? 123 GLN A NE2 1 
ATOM   965  N  N   . LYS A 1 125 ? 25.472 -0.909 -5.661  1.00 14.58  ? 124 LYS A N   1 
ATOM   966  C  CA  . LYS A 1 125 ? 26.775 -1.493 -5.940  1.00 9.37   ? 124 LYS A CA  1 
ATOM   967  C  C   . LYS A 1 125 ? 27.362 -1.029 -7.254  1.00 22.17  ? 124 LYS A C   1 
ATOM   968  O  O   . LYS A 1 125 ? 28.074 -1.755 -7.955  1.00 19.80  ? 124 LYS A O   1 
ATOM   969  C  CB  . LYS A 1 125 ? 26.896 -3.010 -5.711  1.00 18.90  ? 124 LYS A CB  1 
ATOM   970  C  CG  . LYS A 1 125 ? 26.415 -3.386 -4.304  1.00 18.86  ? 124 LYS A CG  1 
ATOM   971  C  CD  . LYS A 1 125 ? 26.832 -4.768 -3.864  1.00 14.29  ? 124 LYS A CD  1 
ATOM   972  C  CE  . LYS A 1 125 ? 26.306 -5.138 -2.486  1.00 12.62  ? 124 LYS A CE  1 
ATOM   973  N  NZ  . LYS A 1 125 ? 26.782 -4.236 -1.454  1.00 24.52  ? 124 LYS A NZ  1 
ATOM   974  N  N   . ARG A 1 126 ? 27.063 0.215  -7.602  1.00 17.51  ? 125 ARG A N   1 
ATOM   975  C  CA  . ARG A 1 126 ? 27.599 0.775  -8.842  1.00 14.87  ? 125 ARG A CA  1 
ATOM   976  C  C   . ARG A 1 126 ? 28.811 1.588  -8.434  1.00 16.40  ? 125 ARG A C   1 
ATOM   977  O  O   . ARG A 1 126 ? 28.718 2.813  -8.275  1.00 19.06  ? 125 ARG A O   1 
ATOM   978  C  CB  . ARG A 1 126 ? 26.532 1.682  -9.431  1.00 13.92  ? 125 ARG A CB  1 
ATOM   979  C  CG  . ARG A 1 126 ? 25.350 0.910  -10.061 1.00 24.71  ? 125 ARG A CG  1 
ATOM   980  C  CD  . ARG A 1 126 ? 24.245 1.897  -10.494 1.00 22.73  ? 125 ARG A CD  1 
ATOM   981  N  NE  . ARG A 1 126 ? 23.437 1.592  -11.682 1.00 77.13  ? 125 ARG A NE  1 
ATOM   982  C  CZ  . ARG A 1 126 ? 22.440 0.688  -11.749 1.00 100.00 ? 125 ARG A CZ  1 
ATOM   983  N  NH1 . ARG A 1 126 ? 22.132 -0.095 -10.716 1.00 100.00 ? 125 ARG A NH1 1 
ATOM   984  N  NH2 . ARG A 1 126 ? 21.749 0.562  -12.893 1.00 59.78  ? 125 ARG A NH2 1 
ATOM   985  N  N   . TRP A 1 127 ? 29.901 0.882  -8.184  1.00 21.10  ? 126 TRP A N   1 
ATOM   986  C  CA  . TRP A 1 127 ? 31.105 1.441  -7.625  1.00 17.57  ? 126 TRP A CA  1 
ATOM   987  C  C   . TRP A 1 127 ? 31.758 2.603  -8.370  1.00 23.23  ? 126 TRP A C   1 
ATOM   988  O  O   . TRP A 1 127 ? 32.055 3.641  -7.792  1.00 18.03  ? 126 TRP A O   1 
ATOM   989  C  CB  . TRP A 1 127 ? 32.120 0.397  -7.070  1.00 14.90  ? 126 TRP A CB  1 
ATOM   990  C  CG  . TRP A 1 127 ? 31.500 -0.753 -6.323  1.00 18.83  ? 126 TRP A CG  1 
ATOM   991  C  CD1 . TRP A 1 127 ? 31.612 -2.067 -6.671  1.00 12.53  ? 126 TRP A CD1 1 
ATOM   992  C  CD2 . TRP A 1 127 ? 30.679 -0.730 -5.161  1.00 18.44  ? 126 TRP A CD2 1 
ATOM   993  N  NE1 . TRP A 1 127 ? 30.960 -2.850 -5.813  1.00 13.77  ? 126 TRP A NE1 1 
ATOM   994  C  CE2 . TRP A 1 127 ? 30.378 -2.072 -4.844  1.00 15.79  ? 126 TRP A CE2 1 
ATOM   995  C  CE3 . TRP A 1 127 ? 30.203 0.277  -4.324  1.00 14.67  ? 126 TRP A CE3 1 
ATOM   996  C  CZ2 . TRP A 1 127 ? 29.600 -2.424 -3.732  1.00 19.40  ? 126 TRP A CZ2 1 
ATOM   997  C  CZ3 . TRP A 1 127 ? 29.411 -0.075 -3.231  1.00 12.24  ? 126 TRP A CZ3 1 
ATOM   998  C  CH2 . TRP A 1 127 ? 29.115 -1.418 -2.939  1.00 15.01  ? 126 TRP A CH2 1 
ATOM   999  N  N   . ASP A 1 128 ? 32.014 2.410  -9.633  1.00 18.14  ? 127 ASP A N   1 
ATOM   1000 C  CA  . ASP A 1 128 ? 32.632 3.444  -10.422 1.00 20.66  ? 127 ASP A CA  1 
ATOM   1001 C  C   . ASP A 1 128 ? 31.713 4.664  -10.542 1.00 29.84  ? 127 ASP A C   1 
ATOM   1002 O  O   . ASP A 1 128 ? 32.145 5.802  -10.477 1.00 20.25  ? 127 ASP A O   1 
ATOM   1003 C  CB  . ASP A 1 128 ? 33.187 2.865  -11.746 1.00 17.25  ? 127 ASP A CB  1 
ATOM   1004 C  CG  . ASP A 1 128 ? 34.401 1.895  -11.550 1.00 23.66  ? 127 ASP A CG  1 
ATOM   1005 O  OD1 . ASP A 1 128 ? 34.516 1.097  -10.626 1.00 67.58  ? 127 ASP A OD1 1 
ATOM   1006 O  OD2 . ASP A 1 128 ? 35.355 2.073  -12.414 1.00 61.70  ? 127 ASP A OD2 1 
ATOM   1007 N  N   . GLU A 1 129 ? 30.402 4.455  -10.616 1.00 16.70  ? 128 GLU A N   1 
ATOM   1008 C  CA  . GLU A 1 129 ? 29.573 5.614  -10.745 1.00 14.66  ? 128 GLU A CA  1 
ATOM   1009 C  C   . GLU A 1 129 ? 29.464 6.397  -9.473  1.00 21.23  ? 128 GLU A C   1 
ATOM   1010 O  O   . GLU A 1 129 ? 29.400 7.606  -9.514  1.00 19.56  ? 128 GLU A O   1 
ATOM   1011 C  CB  . GLU A 1 129 ? 28.220 5.268  -11.332 1.00 23.78  ? 128 GLU A CB  1 
ATOM   1012 C  CG  . GLU A 1 129 ? 28.463 4.212  -12.432 1.00 31.56  ? 128 GLU A CG  1 
ATOM   1013 C  CD  . GLU A 1 129 ? 27.219 3.561  -12.949 1.00 100.00 ? 128 GLU A CD  1 
ATOM   1014 O  OE1 . GLU A 1 129 ? 26.155 4.319  -12.842 1.00 65.42  ? 128 GLU A OE1 1 
ATOM   1015 O  OE2 . GLU A 1 129 ? 27.213 2.458  -13.453 1.00 100.00 ? 128 GLU A OE2 1 
ATOM   1016 N  N   . ALA A 1 130 ? 29.395 5.704  -8.362  1.00 18.40  ? 129 ALA A N   1 
ATOM   1017 C  CA  . ALA A 1 130 ? 29.309 6.390  -7.091  1.00 12.89  ? 129 ALA A CA  1 
ATOM   1018 C  C   . ALA A 1 130 ? 30.573 7.216  -6.882  1.00 10.59  ? 129 ALA A C   1 
ATOM   1019 O  O   . ALA A 1 130 ? 30.516 8.330  -6.365  1.00 18.27  ? 129 ALA A O   1 
ATOM   1020 C  CB  . ALA A 1 130 ? 29.137 5.381  -5.966  1.00 12.26  ? 129 ALA A CB  1 
ATOM   1021 N  N   . ALA A 1 131 ? 31.701 6.700  -7.295  1.00 14.41  ? 130 ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 131 ? 32.962 7.433  -7.106  1.00 12.85  ? 130 ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 131 ? 33.012 8.741  -7.860  1.00 25.16  ? 130 ALA A C   1 
ATOM   1024 O  O   . ALA A 1 131 ? 33.538 9.755  -7.402  1.00 20.28  ? 130 ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 131 ? 34.139 6.578  -7.501  1.00 10.82  ? 130 ALA A CB  1 
ATOM   1026 N  N   . VAL A 1 132 ? 32.464 8.694  -9.051  1.00 16.01  ? 131 VAL A N   1 
ATOM   1027 C  CA  . VAL A 1 132 ? 32.414 9.849  -9.890  1.00 18.35  ? 131 VAL A CA  1 
ATOM   1028 C  C   . VAL A 1 132 ? 31.524 10.898 -9.262  1.00 17.31  ? 131 VAL A C   1 
ATOM   1029 O  O   . VAL A 1 132 ? 31.920 12.055 -9.141  1.00 21.64  ? 131 VAL A O   1 
ATOM   1030 C  CB  . VAL A 1 132 ? 31.982 9.554  -11.331 1.00 24.98  ? 131 VAL A CB  1 
ATOM   1031 C  CG1 . VAL A 1 132 ? 31.570 10.859 -11.981 1.00 29.68  ? 131 VAL A CG1 1 
ATOM   1032 C  CG2 . VAL A 1 132 ? 33.144 8.964  -12.121 1.00 19.51  ? 131 VAL A CG2 1 
ATOM   1033 N  N   . ASN A 1 133 ? 30.336 10.472 -8.805  1.00 14.41  ? 132 ASN A N   1 
ATOM   1034 C  CA  . ASN A 1 133 ? 29.401 11.347 -8.135  1.00 10.59  ? 132 ASN A CA  1 
ATOM   1035 C  C   . ASN A 1 133 ? 29.955 11.906 -6.839  1.00 16.17  ? 132 ASN A C   1 
ATOM   1036 O  O   . ASN A 1 133 ? 29.759 13.059 -6.485  1.00 15.37  ? 132 ASN A O   1 
ATOM   1037 C  CB  . ASN A 1 133 ? 28.089 10.584 -7.807  1.00 15.01  ? 132 ASN A CB  1 
ATOM   1038 C  CG  . ASN A 1 133 ? 26.967 11.504 -7.401  1.00 15.62  ? 132 ASN A CG  1 
ATOM   1039 O  OD1 . ASN A 1 133 ? 26.652 11.691 -6.212  1.00 18.03  ? 132 ASN A OD1 1 
ATOM   1040 N  ND2 . ASN A 1 133 ? 26.377 12.149 -8.415  1.00 20.90  ? 132 ASN A ND2 1 
ATOM   1041 N  N   . LEU A 1 134 ? 30.617 11.068 -6.062  1.00 11.52  ? 133 LEU A N   1 
ATOM   1042 C  CA  . LEU A 1 134 ? 31.116 11.577 -4.795  1.00 9.35   ? 133 LEU A CA  1 
ATOM   1043 C  C   . LEU A 1 134 ? 32.084 12.746 -5.009  1.00 19.45  ? 133 LEU A C   1 
ATOM   1044 O  O   . LEU A 1 134 ? 32.139 13.670 -4.214  1.00 18.90  ? 133 LEU A O   1 
ATOM   1045 C  CB  . LEU A 1 134 ? 31.819 10.441 -4.033  1.00 9.94   ? 133 LEU A CB  1 
ATOM   1046 C  CG  . LEU A 1 134 ? 30.869 9.457  -3.271  1.00 14.67  ? 133 LEU A CG  1 
ATOM   1047 C  CD1 . LEU A 1 134 ? 31.622 8.143  -2.952  1.00 15.38  ? 133 LEU A CD1 1 
ATOM   1048 C  CD2 . LEU A 1 134 ? 30.316 10.112 -2.003  1.00 15.19  ? 133 LEU A CD2 1 
ATOM   1049 N  N   . ALA A 1 135 ? 32.839 12.681 -6.114  1.00 15.42  ? 134 ALA A N   1 
ATOM   1050 C  CA  . ALA A 1 135 ? 33.860 13.714 -6.421  1.00 12.43  ? 134 ALA A CA  1 
ATOM   1051 C  C   . ALA A 1 135 ? 33.276 15.077 -6.758  1.00 17.49  ? 134 ALA A C   1 
ATOM   1052 O  O   . ALA A 1 135 ? 33.960 16.072 -6.684  1.00 17.09  ? 134 ALA A O   1 
ATOM   1053 C  CB  . ALA A 1 135 ? 34.822 13.191 -7.502  1.00 12.50  ? 134 ALA A CB  1 
ATOM   1054 N  N   . LYS A 1 136 ? 32.017 15.134 -7.131  1.00 19.37  ? 135 LYS A N   1 
ATOM   1055 C  CA  . LYS A 1 136 ? 31.395 16.432 -7.464  1.00 15.19  ? 135 LYS A CA  1 
ATOM   1056 C  C   . LYS A 1 136 ? 30.767 17.037 -6.240  1.00 16.43  ? 135 LYS A C   1 
ATOM   1057 O  O   . LYS A 1 136 ? 29.546 17.073 -6.063  1.00 20.65  ? 135 LYS A O   1 
ATOM   1058 C  CB  . LYS A 1 136 ? 30.310 16.220 -8.482  1.00 14.75  ? 135 LYS A CB  1 
ATOM   1059 C  CG  . LYS A 1 136 ? 30.849 15.506 -9.695  1.00 16.00  ? 135 LYS A CG  1 
ATOM   1060 C  CD  . LYS A 1 136 ? 29.732 15.312 -10.698 1.00 34.63  ? 135 LYS A CD  1 
ATOM   1061 C  CE  . LYS A 1 136 ? 30.257 14.888 -12.053 1.00 43.31  ? 135 LYS A CE  1 
ATOM   1062 N  NZ  . LYS A 1 136 ? 29.387 13.885 -12.677 1.00 100.00 ? 135 LYS A NZ  1 
ATOM   1063 N  N   . SER A 1 137 ? 31.614 17.460 -5.344  1.00 11.10  ? 136 SER A N   1 
ATOM   1064 C  CA  . SER A 1 137 ? 31.134 17.955 -4.098  1.00 14.26  ? 136 SER A CA  1 
ATOM   1065 C  C   . SER A 1 137 ? 32.145 18.956 -3.574  1.00 15.64  ? 136 SER A C   1 
ATOM   1066 O  O   . SER A 1 137 ? 33.329 18.936 -3.926  1.00 18.86  ? 136 SER A O   1 
ATOM   1067 C  CB  . SER A 1 137 ? 31.047 16.771 -3.114  1.00 11.35  ? 136 SER A CB  1 
ATOM   1068 O  OG  . SER A 1 137 ? 32.338 16.138 -2.989  1.00 15.17  ? 136 SER A OG  1 
ATOM   1069 N  N   . ARG A 1 138 ? 31.691 19.788 -2.697  1.00 10.94  ? 137 ARG A N   1 
ATOM   1070 C  CA  . ARG A 1 138 ? 32.576 20.706 -2.054  1.00 16.44  ? 137 ARG A CA  1 
ATOM   1071 C  C   . ARG A 1 138 ? 33.617 19.935 -1.247  1.00 15.90  ? 137 ARG A C   1 
ATOM   1072 O  O   . ARG A 1 138 ? 34.799 20.305 -1.153  1.00 16.98  ? 137 ARG A O   1 
ATOM   1073 C  CB  . ARG A 1 138 ? 31.722 21.524 -1.087  1.00 21.65  ? 137 ARG A CB  1 
ATOM   1074 C  CG  . ARG A 1 138 ? 32.601 22.509 -0.296  1.00 18.44  ? 137 ARG A CG  1 
ATOM   1075 C  CD  . ARG A 1 138 ? 31.855 23.328 0.758   1.00 22.70  ? 137 ARG A CD  1 
ATOM   1076 N  NE  . ARG A 1 138 ? 32.596 24.499 1.225   1.00 37.28  ? 137 ARG A NE  1 
ATOM   1077 C  CZ  . ARG A 1 138 ? 33.426 24.481 2.270   1.00 51.87  ? 137 ARG A CZ  1 
ATOM   1078 N  NH1 . ARG A 1 138 ? 33.641 23.375 2.989   1.00 34.71  ? 137 ARG A NH1 1 
ATOM   1079 N  NH2 . ARG A 1 138 ? 34.060 25.609 2.596   1.00 76.46  ? 137 ARG A NH2 1 
ATOM   1080 N  N   . TRP A 1 139 ? 33.137 18.841 -0.620  1.00 14.49  ? 138 TRP A N   1 
ATOM   1081 C  CA  . TRP A 1 139 ? 33.923 17.930 0.182   1.00 9.50   ? 138 TRP A CA  1 
ATOM   1082 C  C   . TRP A 1 139 ? 35.192 17.529 -0.565  1.00 13.37  ? 138 TRP A C   1 
ATOM   1083 O  O   . TRP A 1 139 ? 36.289 17.683 -0.084  1.00 13.99  ? 138 TRP A O   1 
ATOM   1084 C  CB  . TRP A 1 139 ? 33.102 16.662 0.520   1.00 16.91  ? 138 TRP A CB  1 
ATOM   1085 C  CG  . TRP A 1 139 ? 33.903 15.523 1.072   1.00 17.14  ? 138 TRP A CG  1 
ATOM   1086 C  CD1 . TRP A 1 139 ? 34.607 15.542 2.238   1.00 14.15  ? 138 TRP A CD1 1 
ATOM   1087 C  CD2 . TRP A 1 139 ? 33.991 14.169 0.566   1.00 8.04   ? 138 TRP A CD2 1 
ATOM   1088 N  NE1 . TRP A 1 139 ? 35.159 14.305 2.502   1.00 18.16  ? 138 TRP A NE1 1 
ATOM   1089 C  CE2 . TRP A 1 139 ? 34.779 13.422 1.497   1.00 13.32  ? 138 TRP A CE2 1 
ATOM   1090 C  CE3 . TRP A 1 139 ? 33.459 13.548 -0.549  1.00 8.90   ? 138 TRP A CE3 1 
ATOM   1091 C  CZ2 . TRP A 1 139 ? 35.090 12.066 1.309   1.00 13.57  ? 138 TRP A CZ2 1 
ATOM   1092 C  CZ3 . TRP A 1 139 ? 33.778 12.204 -0.723  1.00 12.28  ? 138 TRP A CZ3 1 
ATOM   1093 C  CH2 . TRP A 1 139 ? 34.542 11.463 0.210   1.00 11.90  ? 138 TRP A CH2 1 
ATOM   1094 N  N   . TYR A 1 140 ? 35.048 17.046 -1.789  1.00 10.08  ? 139 TYR A N   1 
ATOM   1095 C  CA  . TYR A 1 140 ? 36.211 16.646 -2.548  1.00 10.34  ? 139 TYR A CA  1 
ATOM   1096 C  C   . TYR A 1 140 ? 37.101 17.836 -2.907  1.00 28.02  ? 139 TYR A C   1 
ATOM   1097 O  O   . TYR A 1 140 ? 38.334 17.742 -2.924  1.00 15.40  ? 139 TYR A O   1 
ATOM   1098 C  CB  . TYR A 1 140 ? 35.713 16.042 -3.849  1.00 14.15  ? 139 TYR A CB  1 
ATOM   1099 C  CG  . TYR A 1 140 ? 36.793 15.608 -4.770  1.00 19.26  ? 139 TYR A CG  1 
ATOM   1100 C  CD1 . TYR A 1 140 ? 37.315 14.330 -4.602  1.00 18.41  ? 139 TYR A CD1 1 
ATOM   1101 C  CD2 . TYR A 1 140 ? 37.197 16.380 -5.863  1.00 19.66  ? 139 TYR A CD2 1 
ATOM   1102 C  CE1 . TYR A 1 140 ? 38.252 13.812 -5.487  1.00 23.76  ? 139 TYR A CE1 1 
ATOM   1103 C  CE2 . TYR A 1 140 ? 38.149 15.880 -6.753  1.00 37.63  ? 139 TYR A CE2 1 
ATOM   1104 C  CZ  . TYR A 1 140 ? 38.674 14.597 -6.560  1.00 49.53  ? 139 TYR A CZ  1 
ATOM   1105 O  OH  . TYR A 1 140 ? 39.608 14.083 -7.427  1.00 60.38  ? 139 TYR A OH  1 
ATOM   1106 N  N   . ASN A 1 141 ? 36.453 18.958 -3.233  1.00 15.32  ? 140 ASN A N   1 
ATOM   1107 C  CA  . ASN A 1 141 ? 37.229 20.153 -3.620  1.00 20.08  ? 140 ASN A CA  1 
ATOM   1108 C  C   . ASN A 1 141 ? 38.038 20.776 -2.479  1.00 15.74  ? 140 ASN A C   1 
ATOM   1109 O  O   . ASN A 1 141 ? 39.159 21.296 -2.642  1.00 18.67  ? 140 ASN A O   1 
ATOM   1110 C  CB  . ASN A 1 141 ? 36.369 21.177 -4.381  1.00 31.81  ? 140 ASN A CB  1 
ATOM   1111 C  CG  . ASN A 1 141 ? 36.067 20.679 -5.770  1.00 23.26  ? 140 ASN A CG  1 
ATOM   1112 O  OD1 . ASN A 1 141 ? 34.955 20.198 -6.052  1.00 26.56  ? 140 ASN A OD1 1 
ATOM   1113 N  ND2 . ASN A 1 141 ? 37.094 20.698 -6.606  1.00 28.31  ? 140 ASN A ND2 1 
ATOM   1114 N  N   . GLN A 1 142 ? 37.496 20.708 -1.300  1.00 10.93  ? 141 GLN A N   1 
ATOM   1115 C  CA  . GLN A 1 142 ? 38.179 21.274 -0.138  1.00 16.38  ? 141 GLN A CA  1 
ATOM   1116 C  C   . GLN A 1 142 ? 39.240 20.383 0.477   1.00 29.20  ? 141 GLN A C   1 
ATOM   1117 O  O   . GLN A 1 142 ? 40.240 20.900 0.941   1.00 22.26  ? 141 GLN A O   1 
ATOM   1118 C  CB  . GLN A 1 142 ? 37.203 21.731 0.968   1.00 13.27  ? 141 GLN A CB  1 
ATOM   1119 C  CG  . GLN A 1 142 ? 36.210 22.754 0.390   1.00 30.18  ? 141 GLN A CG  1 
ATOM   1120 C  CD  . GLN A 1 142 ? 36.862 24.003 -0.182  1.00 52.04  ? 141 GLN A CD  1 
ATOM   1121 O  OE1 . GLN A 1 142 ? 36.634 24.385 -1.359  1.00 31.51  ? 141 GLN A OE1 1 
ATOM   1122 N  NE2 . GLN A 1 142 ? 37.654 24.649 0.661   1.00 24.15  ? 141 GLN A NE2 1 
ATOM   1123 N  N   . THR A 1 143 ? 38.998 19.057 0.552   1.00 17.32  ? 142 THR A N   1 
ATOM   1124 C  CA  . THR A 1 143 ? 39.966 18.113 1.134   1.00 9.26   ? 142 THR A CA  1 
ATOM   1125 C  C   . THR A 1 143 ? 40.116 16.958 0.166   1.00 14.56  ? 142 THR A C   1 
ATOM   1126 O  O   . THR A 1 143 ? 39.756 15.813 0.438   1.00 15.55  ? 142 THR A O   1 
ATOM   1127 C  CB  . THR A 1 143 ? 39.512 17.574 2.507   1.00 22.35  ? 142 THR A CB  1 
ATOM   1128 O  OG1 . THR A 1 143 ? 38.182 17.061 2.386   1.00 16.87  ? 142 THR A OG1 1 
ATOM   1129 C  CG2 . THR A 1 143 ? 39.507 18.718 3.501   1.00 14.10  ? 142 THR A CG2 1 
ATOM   1130 N  N   . PRO A 1 144 ? 40.674 17.281 -0.981  1.00 14.37  ? 143 PRO A N   1 
ATOM   1131 C  CA  . PRO A 1 144 ? 40.844 16.300 -2.071  1.00 13.63  ? 143 PRO A CA  1 
ATOM   1132 C  C   . PRO A 1 144 ? 41.681 15.008 -1.757  1.00 13.98  ? 143 PRO A C   1 
ATOM   1133 O  O   . PRO A 1 144 ? 41.370 13.901 -2.230  1.00 14.27  ? 143 PRO A O   1 
ATOM   1134 C  CB  . PRO A 1 144 ? 41.422 17.119 -3.256  1.00 13.83  ? 143 PRO A CB  1 
ATOM   1135 C  CG  . PRO A 1 144 ? 42.096 18.351 -2.618  1.00 16.65  ? 143 PRO A CG  1 
ATOM   1136 C  CD  . PRO A 1 144 ? 41.435 18.538 -1.229  1.00 13.92  ? 143 PRO A CD  1 
ATOM   1137 N  N   . ASN A 1 145 ? 42.785 15.132 -1.027  1.00 7.45   ? 144 ASN A N   1 
ATOM   1138 C  CA  . ASN A 1 145 ? 43.586 13.967 -0.766  1.00 10.82  ? 144 ASN A CA  1 
ATOM   1139 C  C   . ASN A 1 145 ? 42.828 12.926 0.089   1.00 17.97  ? 144 ASN A C   1 
ATOM   1140 O  O   . ASN A 1 145 ? 42.868 11.720 -0.192  1.00 18.24  ? 144 ASN A O   1 
ATOM   1141 C  CB  . ASN A 1 145 ? 44.969 14.324 -0.148  1.00 13.04  ? 144 ASN A CB  1 
ATOM   1142 C  CG  . ASN A 1 145 ? 45.959 15.039 -1.071  1.00 21.99  ? 144 ASN A CG  1 
ATOM   1143 O  OD1 . ASN A 1 145 ? 46.011 14.804 -2.265  1.00 27.64  ? 144 ASN A OD1 1 
ATOM   1144 N  ND2 . ASN A 1 145 ? 46.791 15.876 -0.499  1.00 30.24  ? 144 ASN A ND2 1 
ATOM   1145 N  N   . ARG A 1 146 ? 42.213 13.422 1.155   1.00 13.19  ? 145 ARG A N   1 
ATOM   1146 C  CA  . ARG A 1 146 ? 41.418 12.608 2.037   1.00 16.28  ? 145 ARG A CA  1 
ATOM   1147 C  C   . ARG A 1 146 ? 40.188 12.095 1.269   1.00 12.23  ? 145 ARG A C   1 
ATOM   1148 O  O   . ARG A 1 146 ? 39.852 10.891 1.266   1.00 18.05  ? 145 ARG A O   1 
ATOM   1149 C  CB  . ARG A 1 146 ? 40.942 13.384 3.245   1.00 8.06   ? 145 ARG A CB  1 
ATOM   1150 C  CG  . ARG A 1 146 ? 39.815 12.621 3.974   1.00 17.52  ? 145 ARG A CG  1 
ATOM   1151 C  CD  . ARG A 1 146 ? 39.604 13.120 5.359   1.00 33.39  ? 145 ARG A CD  1 
ATOM   1152 N  NE  . ARG A 1 146 ? 38.745 12.253 6.137   1.00 18.59  ? 145 ARG A NE  1 
ATOM   1153 C  CZ  . ARG A 1 146 ? 38.556 12.656 7.346   1.00 19.12  ? 145 ARG A CZ  1 
ATOM   1154 N  NH1 . ARG A 1 146 ? 39.164 13.782 7.693   1.00 12.88  ? 145 ARG A NH1 1 
ATOM   1155 N  NH2 . ARG A 1 146 ? 37.775 11.968 8.173   1.00 8.96   ? 145 ARG A NH2 1 
ATOM   1156 N  N   . ALA A 1 147 ? 39.493 13.030 0.596   1.00 11.42  ? 146 ALA A N   1 
ATOM   1157 C  CA  . ALA A 1 147 ? 38.362 12.574 -0.174  1.00 10.15  ? 146 ALA A CA  1 
ATOM   1158 C  C   . ALA A 1 147 ? 38.776 11.435 -1.145  1.00 18.67  ? 146 ALA A C   1 
ATOM   1159 O  O   . ALA A 1 147 ? 38.112 10.409 -1.213  1.00 12.53  ? 146 ALA A O   1 
ATOM   1160 C  CB  . ALA A 1 147 ? 37.655 13.735 -0.885  1.00 18.09  ? 146 ALA A CB  1 
ATOM   1161 N  N   . LYS A 1 148 ? 39.870 11.572 -1.893  1.00 15.01  ? 147 LYS A N   1 
ATOM   1162 C  CA  . LYS A 1 148 ? 40.297 10.518 -2.834  1.00 11.85  ? 147 LYS A CA  1 
ATOM   1163 C  C   . LYS A 1 148 ? 40.518 9.178  -2.170  1.00 16.29  ? 147 LYS A C   1 
ATOM   1164 O  O   . LYS A 1 148 ? 40.216 8.116  -2.764  1.00 12.24  ? 147 LYS A O   1 
ATOM   1165 C  CB  . LYS A 1 148 ? 41.573 10.906 -3.518  1.00 15.43  ? 147 LYS A CB  1 
ATOM   1166 C  CG  . LYS A 1 148 ? 41.297 11.766 -4.697  1.00 37.91  ? 147 LYS A CG  1 
ATOM   1167 C  CD  . LYS A 1 148 ? 42.577 12.306 -5.261  1.00 32.50  ? 147 LYS A CD  1 
ATOM   1168 C  CE  . LYS A 1 148 ? 42.330 13.604 -5.995  1.00 37.27  ? 147 LYS A CE  1 
ATOM   1169 N  NZ  . LYS A 1 148 ? 43.506 14.484 -6.020  1.00 100.00 ? 147 LYS A NZ  1 
ATOM   1170 N  N   . ARG A 1 149 ? 41.079 9.217  -0.956  1.00 10.94  ? 148 ARG A N   1 
ATOM   1171 C  CA  . ARG A 1 149 ? 41.300 8.010  -0.195  1.00 16.36  ? 148 ARG A CA  1 
ATOM   1172 C  C   . ARG A 1 149 ? 39.974 7.328  0.129   1.00 19.07  ? 148 ARG A C   1 
ATOM   1173 O  O   . ARG A 1 149 ? 39.835 6.129  -0.100  1.00 15.89  ? 148 ARG A O   1 
ATOM   1174 C  CB  . ARG A 1 149 ? 42.064 8.251  1.107   1.00 14.88  ? 148 ARG A CB  1 
ATOM   1175 C  CG  . ARG A 1 149 ? 43.533 8.589  0.906   1.00 10.54  ? 148 ARG A CG  1 
ATOM   1176 C  CD  . ARG A 1 149 ? 44.330 8.400  2.160   1.00 15.81  ? 148 ARG A CD  1 
ATOM   1177 N  NE  . ARG A 1 149 ? 44.068 9.477  3.112   1.00 19.77  ? 148 ARG A NE  1 
ATOM   1178 C  CZ  . ARG A 1 149 ? 44.655 10.691 3.131   1.00 16.47  ? 148 ARG A CZ  1 
ATOM   1179 N  NH1 . ARG A 1 149 ? 45.594 11.035 2.212   1.00 15.75  ? 148 ARG A NH1 1 
ATOM   1180 N  NH2 . ARG A 1 149 ? 44.274 11.569 4.038   1.00 11.79  ? 148 ARG A NH2 1 
ATOM   1181 N  N   . VAL A 1 150 ? 38.990 8.102  0.648   1.00 14.85  ? 149 VAL A N   1 
ATOM   1182 C  CA  . VAL A 1 150 ? 37.689 7.507  1.003   1.00 9.24   ? 149 VAL A CA  1 
ATOM   1183 C  C   . VAL A 1 150 ? 36.969 6.937  -0.218  1.00 11.72  ? 149 VAL A C   1 
ATOM   1184 O  O   . VAL A 1 150 ? 36.379 5.838  -0.206  1.00 15.58  ? 149 VAL A O   1 
ATOM   1185 C  CB  . VAL A 1 150 ? 36.859 8.490  1.774   1.00 12.97  ? 149 VAL A CB  1 
ATOM   1186 C  CG1 . VAL A 1 150 ? 35.444 7.989  1.953   1.00 12.65  ? 149 VAL A CG1 1 
ATOM   1187 C  CG2 . VAL A 1 150 ? 37.553 8.735  3.110   1.00 11.80  ? 149 VAL A CG2 1 
ATOM   1188 N  N   . ILE A 1 151 ? 37.062 7.710  -1.307  1.00 12.19  ? 150 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 151 ? 36.474 7.376  -2.606  1.00 13.74  ? 150 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 151 ? 37.068 6.123  -3.210  1.00 12.78  ? 150 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 151 ? 36.315 5.351  -3.777  1.00 16.48  ? 150 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 151 ? 36.402 8.543  -3.655  1.00 11.55  ? 150 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 151 ? 35.458 9.686  -3.211  1.00 11.86  ? 150 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 151 ? 36.001 7.959  -5.027  1.00 18.72  ? 150 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 151 ? 35.673 11.009 -3.917  1.00 10.71  ? 150 ILE A CD1 1 
ATOM   1196 N  N   . THR A 1 152 ? 38.392 5.927  -3.080  1.00 15.30  ? 151 THR A N   1 
ATOM   1197 C  CA  . THR A 1 152 ? 39.075 4.738  -3.566  1.00 18.50  ? 151 THR A CA  1 
ATOM   1198 C  C   . THR A 1 152 ? 38.626 3.529  -2.787  1.00 10.11  ? 151 THR A C   1 
ATOM   1199 O  O   . THR A 1 152 ? 38.473 2.466  -3.357  1.00 14.40  ? 151 THR A O   1 
ATOM   1200 C  CB  . THR A 1 152 ? 40.602 4.872  -3.564  1.00 16.03  ? 151 THR A CB  1 
ATOM   1201 O  OG1 . THR A 1 152 ? 40.929 5.779  -4.579  1.00 26.25  ? 151 THR A OG1 1 
ATOM   1202 C  CG2 . THR A 1 152 ? 41.226 3.508  -3.880  1.00 19.01  ? 151 THR A CG2 1 
ATOM   1203 N  N   . THR A 1 153 ? 38.401 3.738  -1.495  1.00 11.07  ? 152 THR A N   1 
ATOM   1204 C  CA  . THR A 1 153 ? 37.907 2.726  -0.598  1.00 13.20  ? 152 THR A CA  1 
ATOM   1205 C  C   . THR A 1 153 ? 36.515 2.201  -1.039  1.00 18.15  ? 152 THR A C   1 
ATOM   1206 O  O   . THR A 1 153 ? 36.254 0.964  -1.096  1.00 12.17  ? 152 THR A O   1 
ATOM   1207 C  CB  . THR A 1 153 ? 37.960 3.231  0.864   1.00 11.39  ? 152 THR A CB  1 
ATOM   1208 O  OG1 . THR A 1 153 ? 39.289 3.620  1.123   1.00 13.47  ? 152 THR A OG1 1 
ATOM   1209 C  CG2 . THR A 1 153 ? 37.654 2.094  1.805   1.00 10.85  ? 152 THR A CG2 1 
ATOM   1210 N  N   . PHE A 1 154 ? 35.628 3.145  -1.393  1.00 12.34  ? 153 PHE A N   1 
ATOM   1211 C  CA  . PHE A 1 154 ? 34.306 2.824  -1.876  1.00 11.77  ? 153 PHE A CA  1 
ATOM   1212 C  C   . PHE A 1 154 ? 34.413 2.143  -3.233  1.00 16.24  ? 153 PHE A C   1 
ATOM   1213 O  O   . PHE A 1 154 ? 33.717 1.160  -3.536  1.00 20.62  ? 153 PHE A O   1 
ATOM   1214 C  CB  . PHE A 1 154 ? 33.475 4.131  -2.001  1.00 10.58  ? 153 PHE A CB  1 
ATOM   1215 C  CG  . PHE A 1 154 ? 32.790 4.605  -0.731  1.00 16.14  ? 153 PHE A CG  1 
ATOM   1216 C  CD1 . PHE A 1 154 ? 31.960 3.762  0.003   1.00 20.24  ? 153 PHE A CD1 1 
ATOM   1217 C  CD2 . PHE A 1 154 ? 32.882 5.927  -0.304  1.00 16.60  ? 153 PHE A CD2 1 
ATOM   1218 C  CE1 . PHE A 1 154 ? 31.280 4.202  1.130   1.00 12.32  ? 153 PHE A CE1 1 
ATOM   1219 C  CE2 . PHE A 1 154 ? 32.241 6.389  0.845   1.00 17.09  ? 153 PHE A CE2 1 
ATOM   1220 C  CZ  . PHE A 1 154 ? 31.411 5.522  1.547   1.00 13.50  ? 153 PHE A CZ  1 
ATOM   1221 N  N   . ARG A 1 155 ? 35.320 2.661  -4.087  1.00 16.49  ? 154 ARG A N   1 
ATOM   1222 C  CA  . ARG A 1 155 ? 35.488 2.125  -5.426  1.00 11.85  ? 154 ARG A CA  1 
ATOM   1223 C  C   . ARG A 1 155 ? 35.955 0.687  -5.442  1.00 22.54  ? 154 ARG A C   1 
ATOM   1224 O  O   . ARG A 1 155 ? 35.327 -0.136 -6.087  1.00 25.41  ? 154 ARG A O   1 
ATOM   1225 C  CB  . ARG A 1 155 ? 36.364 2.958  -6.327  1.00 16.55  ? 154 ARG A CB  1 
ATOM   1226 C  CG  . ARG A 1 155 ? 35.890 2.997  -7.774  1.00 20.89  ? 154 ARG A CG  1 
ATOM   1227 C  CD  . ARG A 1 155 ? 36.984 3.413  -8.751  1.00 19.45  ? 154 ARG A CD  1 
ATOM   1228 N  NE  . ARG A 1 155 ? 38.275 3.610  -8.078  1.00 100.00 ? 154 ARG A NE  1 
ATOM   1229 C  CZ  . ARG A 1 155 ? 39.342 2.815  -8.217  1.00 100.00 ? 154 ARG A CZ  1 
ATOM   1230 N  NH1 . ARG A 1 155 ? 39.303 1.752  -9.021  1.00 62.48  ? 154 ARG A NH1 1 
ATOM   1231 N  NH2 . ARG A 1 155 ? 40.468 3.091  -7.534  1.00 63.99  ? 154 ARG A NH2 1 
ATOM   1232 N  N   . THR A 1 156 ? 37.032 0.429  -4.704  1.00 21.28  ? 155 THR A N   1 
ATOM   1233 C  CA  . THR A 1 156 ? 37.684 -0.866 -4.631  1.00 20.58  ? 155 THR A CA  1 
ATOM   1234 C  C   . THR A 1 156 ? 37.236 -1.826 -3.568  1.00 29.07  ? 155 THR A C   1 
ATOM   1235 O  O   . THR A 1 156 ? 37.421 -3.022 -3.762  1.00 24.58  ? 155 THR A O   1 
ATOM   1236 C  CB  . THR A 1 156 ? 39.214 -0.697 -4.511  1.00 16.66  ? 155 THR A CB  1 
ATOM   1237 O  OG1 . THR A 1 156 ? 39.558 -0.099 -3.276  1.00 20.23  ? 155 THR A OG1 1 
ATOM   1238 C  CG2 . THR A 1 156 ? 39.673 0.174  -5.661  1.00 22.52  ? 155 THR A CG2 1 
ATOM   1239 N  N   . GLY A 1 157 ? 36.755 -1.336 -2.438  1.00 20.53  ? 156 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 157 ? 36.402 -2.210 -1.346  1.00 14.28  ? 156 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 157 ? 37.653 -2.798 -0.724  1.00 18.32  ? 156 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 157 ? 37.624 -3.817 -0.047  1.00 17.82  ? 156 GLY A O   1 
ATOM   1243 N  N   . THR A 1 158 ? 38.801 -2.146 -0.943  1.00 17.75  ? 157 THR A N   1 
ATOM   1244 C  CA  . THR A 1 158 ? 40.032 -2.607 -0.320  1.00 13.71  ? 157 THR A CA  1 
ATOM   1245 C  C   . THR A 1 158 ? 40.653 -1.450 0.446   1.00 20.80  ? 157 THR A C   1 
ATOM   1246 O  O   . THR A 1 158 ? 40.233 -0.351 0.260   1.00 14.06  ? 157 THR A O   1 
ATOM   1247 C  CB  . THR A 1 158 ? 41.089 -2.938 -1.356  1.00 30.84  ? 157 THR A CB  1 
ATOM   1248 O  OG1 . THR A 1 158 ? 41.594 -1.708 -1.857  1.00 18.26  ? 157 THR A OG1 1 
ATOM   1249 C  CG2 . THR A 1 158 ? 40.510 -3.803 -2.461  1.00 24.84  ? 157 THR A CG2 1 
ATOM   1250 N  N   . TRP A 1 159 ? 41.708 -1.678 1.214   1.00 15.08  ? 158 TRP A N   1 
ATOM   1251 C  CA  . TRP A 1 159 ? 42.337 -0.615 1.978   1.00 13.20  ? 158 TRP A CA  1 
ATOM   1252 C  C   . TRP A 1 159 ? 43.539 -0.052 1.226   1.00 20.84  ? 158 TRP A C   1 
ATOM   1253 O  O   . TRP A 1 159 ? 44.370 0.632  1.777   1.00 20.59  ? 158 TRP A O   1 
ATOM   1254 C  CB  . TRP A 1 159 ? 42.865 -1.191 3.287   1.00 11.79  ? 158 TRP A CB  1 
ATOM   1255 C  CG  . TRP A 1 159 ? 41.827 -1.635 4.273   1.00 14.12  ? 158 TRP A CG  1 
ATOM   1256 C  CD1 . TRP A 1 159 ? 41.552 -2.920 4.588   1.00 13.32  ? 158 TRP A CD1 1 
ATOM   1257 C  CD2 . TRP A 1 159 ? 40.939 -0.809 5.035   1.00 20.46  ? 158 TRP A CD2 1 
ATOM   1258 N  NE1 . TRP A 1 159 ? 40.568 -2.963 5.540   1.00 19.41  ? 158 TRP A NE1 1 
ATOM   1259 C  CE2 . TRP A 1 159 ? 40.172 -1.685 5.852   1.00 17.96  ? 158 TRP A CE2 1 
ATOM   1260 C  CE3 . TRP A 1 159 ? 40.768 0.566  5.152   1.00 18.05  ? 158 TRP A CE3 1 
ATOM   1261 C  CZ2 . TRP A 1 159 ? 39.211 -1.241 6.746   1.00 17.77  ? 158 TRP A CZ2 1 
ATOM   1262 C  CZ3 . TRP A 1 159 ? 39.855 0.989  6.078   1.00 19.13  ? 158 TRP A CZ3 1 
ATOM   1263 C  CH2 . TRP A 1 159 ? 39.069 0.103  6.843   1.00 17.07  ? 158 TRP A CH2 1 
ATOM   1264 N  N   . ASP A 1 160 ? 43.639 -0.338 -0.040  1.00 17.01  ? 159 ASP A N   1 
ATOM   1265 C  CA  . ASP A 1 160 ? 44.815 0.154  -0.763  1.00 16.67  ? 159 ASP A CA  1 
ATOM   1266 C  C   . ASP A 1 160 ? 45.215 1.622  -0.580  1.00 25.23  ? 159 ASP A C   1 
ATOM   1267 O  O   . ASP A 1 160 ? 46.397 1.912  -0.536  1.00 27.38  ? 159 ASP A O   1 
ATOM   1268 C  CB  . ASP A 1 160 ? 44.773 -0.215 -2.252  1.00 24.42  ? 159 ASP A CB  1 
ATOM   1269 C  CG  . ASP A 1 160 ? 44.680 -1.713 -2.512  1.00 48.23  ? 159 ASP A CG  1 
ATOM   1270 O  OD1 . ASP A 1 160 ? 45.018 -2.464 -1.479  1.00 41.28  ? 159 ASP A OD1 1 
ATOM   1271 O  OD2 . ASP A 1 160 ? 44.380 -2.178 -3.591  1.00 44.64  ? 159 ASP A OD2 1 
ATOM   1272 N  N   . ALA A 1 161 ? 44.239 2.533  -0.548  1.00 24.34  ? 160 ALA A N   1 
ATOM   1273 C  CA  . ALA A 1 161 ? 44.515 3.969  -0.451  1.00 15.36  ? 160 ALA A CA  1 
ATOM   1274 C  C   . ALA A 1 161 ? 45.235 4.303  0.834   1.00 20.55  ? 160 ALA A C   1 
ATOM   1275 O  O   . ALA A 1 161 ? 45.885 5.321  0.980   1.00 20.15  ? 160 ALA A O   1 
ATOM   1276 C  CB  . ALA A 1 161 ? 43.227 4.790  -0.632  1.00 16.32  ? 160 ALA A CB  1 
ATOM   1277 N  N   . TYR A 1 162 ? 45.132 3.432  1.780   1.00 17.00  ? 161 TYR A N   1 
ATOM   1278 C  CA  . TYR A 1 162 ? 45.720 3.704  3.032   1.00 16.51  ? 161 TYR A CA  1 
ATOM   1279 C  C   . TYR A 1 162 ? 46.983 2.944  3.272   1.00 26.21  ? 161 TYR A C   1 
ATOM   1280 O  O   . TYR A 1 162 ? 47.564 3.096  4.338   1.00 30.12  ? 161 TYR A O   1 
ATOM   1281 C  CB  . TYR A 1 162 ? 44.689 3.402  4.146   1.00 18.77  ? 161 TYR A CB  1 
ATOM   1282 C  CG  . TYR A 1 162 ? 43.589 4.410  4.214   1.00 17.18  ? 161 TYR A CG  1 
ATOM   1283 C  CD1 . TYR A 1 162 ? 43.752 5.575  4.973   1.00 9.51   ? 161 TYR A CD1 1 
ATOM   1284 C  CD2 . TYR A 1 162 ? 42.457 4.206  3.424   1.00 13.93  ? 161 TYR A CD2 1 
ATOM   1285 C  CE1 . TYR A 1 162 ? 42.727 6.519  5.017   1.00 10.62  ? 161 TYR A CE1 1 
ATOM   1286 C  CE2 . TYR A 1 162 ? 41.446 5.163  3.428   1.00 15.90  ? 161 TYR A CE2 1 
ATOM   1287 C  CZ  . TYR A 1 162 ? 41.593 6.296  4.230   1.00 11.60  ? 161 TYR A CZ  1 
ATOM   1288 O  OH  . TYR A 1 162 ? 40.554 7.202  4.273   1.00 12.91  ? 161 TYR A OH  1 
ATOM   1289 N  N   . LYS A 1 163 ? 47.340 2.095  2.404   1.00 52.34  ? 162 LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 163 ? 48.558 1.279  2.555   1.00 100.00 ? 162 LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 163 ? 49.765 1.809  1.757   1.00 53.99  ? 162 LYS A C   1 
ATOM   1292 O  O   . LYS A 1 163 ? 50.824 2.091  2.326   1.00 40.69  ? 162 LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 163 ? 48.399 -0.233 2.395   1.00 86.39  ? 162 LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 163 ? 47.487 -0.828 3.442   1.00 54.55  ? 162 LYS A CG  1 
ATOM   1295 C  CD  . LYS A 1 163 ? 47.042 -2.267 3.144   1.00 100.00 ? 162 LYS A CD  1 
ATOM   1296 C  CE  . LYS A 1 163 ? 47.048 -2.611 1.653   1.00 99.84  ? 162 LYS A CE  1 
ATOM   1297 N  NZ  . LYS A 1 163 ? 45.951 -3.517 1.236   1.00 61.13  ? 162 LYS A NZ  1 
HETATM 1298 CL CL  . CL  B 2 .   ? 42.929 16.535 2.063   1.00 3.86   ? 173 CL  A CL  1 
HETATM 1299 CL CL  . CL  C 2 .   ? 32.067 15.336 23.954  0.50 2.26   ? 178 CL  A CL  1 
HETATM 1300 C  C1  . BME D 3 .   ? 31.965 -0.933 15.030  1.00 33.04  ? 901 BME A C1  1 
HETATM 1301 C  C2  . BME D 3 .   ? 31.963 -1.528 13.675  1.00 34.06  ? 901 BME A C2  1 
HETATM 1302 O  O1  . BME D 3 .   ? 33.365 -0.851 15.514  1.00 38.25  ? 901 BME A O1  1 
HETATM 1303 S  S2  . BME D 3 .   ? 33.648 -1.772 13.157  1.00 28.66  ? 901 BME A S2  1 
HETATM 1304 C  C1  . BME E 3 .   ? 34.138 -2.257 9.175   1.00 37.55  ? 902 BME A C1  1 
HETATM 1305 C  C2  . BME E 3 .   ? 33.301 -2.197 10.499  1.00 45.81  ? 902 BME A C2  1 
HETATM 1306 O  O1  . BME E 3 .   ? 34.873 -3.387 9.105   1.00 52.06  ? 902 BME A O1  1 
HETATM 1307 S  S2  . BME E 3 .   ? 33.692 -0.686 11.493  1.00 47.60  ? 902 BME A S2  1 
HETATM 1308 O  O   . HOH F 4 .   ? 38.096 12.403 18.145  1.00 13.29  ? 171 HOH A O   1 
HETATM 1309 O  O   . HOH F 4 .   ? 35.798 18.883 3.172   1.00 28.26  ? 172 HOH A O   1 
HETATM 1310 O  O   . HOH F 4 .   ? 41.760 23.289 1.355   1.00 22.98  ? 174 HOH A O   1 
HETATM 1311 O  O   . HOH F 4 .   ? 41.405 2.139  0.050   1.00 20.64  ? 175 HOH A O   1 
HETATM 1312 O  O   . HOH F 4 .   ? 41.546 26.175 28.863  1.00 83.67  ? 176 HOH A O   1 
HETATM 1313 O  O   . HOH F 4 .   ? 33.112 -7.870 4.081   1.00 19.02  ? 177 HOH A O   1 
HETATM 1314 O  O   . HOH F 4 .   ? 40.318 12.967 19.810  1.00 17.65  ? 179 HOH A O   1 
HETATM 1315 O  O   . HOH F 4 .   ? 44.691 10.848 -1.785  1.00 21.86  ? 180 HOH A O   1 
HETATM 1316 O  O   . HOH F 4 .   ? 28.350 -6.907 4.876   1.00 22.98  ? 181 HOH A O   1 
HETATM 1317 O  O   . HOH F 4 .   ? 33.184 12.730 22.367  1.00 26.31  ? 182 HOH A O   1 
HETATM 1318 O  O   . HOH F 4 .   ? 34.192 11.289 28.922  1.00 39.30  ? 183 HOH A O   1 
HETATM 1319 O  O   . HOH F 4 .   ? 48.531 9.908  28.532  1.00 69.93  ? 184 HOH A O   1 
HETATM 1320 O  O   . HOH F 4 .   ? 31.118 5.925  23.394  1.00 30.98  ? 185 HOH A O   1 
HETATM 1321 O  O   . HOH F 4 .   ? 40.670 5.447  20.531  1.00 26.46  ? 186 HOH A O   1 
HETATM 1322 O  O   . HOH F 4 .   ? 44.851 -3.689 11.364  1.00 44.47  ? 187 HOH A O   1 
HETATM 1323 O  O   . HOH F 4 .   ? 39.211 22.653 -6.614  1.00 28.22  ? 188 HOH A O   1 
HETATM 1324 O  O   . HOH F 4 .   ? 50.725 17.496 19.609  1.00 39.08  ? 189 HOH A O   1 
HETATM 1325 O  O   . HOH F 4 .   ? 36.286 27.659 16.011  1.00 43.54  ? 190 HOH A O   1 
HETATM 1326 O  O   . HOH F 4 .   ? 37.325 29.870 14.316  1.00 54.86  ? 191 HOH A O   1 
HETATM 1327 O  O   . HOH F 4 .   ? 44.145 25.354 9.871   1.00 29.12  ? 192 HOH A O   1 
HETATM 1328 O  O   . HOH F 4 .   ? 19.914 -2.351 2.972   1.00 25.96  ? 193 HOH A O   1 
HETATM 1329 O  O   . HOH F 4 .   ? 35.024 5.367  -10.938 1.00 52.83  ? 194 HOH A O   1 
HETATM 1330 O  O   . HOH F 4 .   ? 36.970 -1.366 10.719  1.00 14.46  ? 195 HOH A O   1 
HETATM 1331 O  O   . HOH F 4 .   ? 46.254 20.177 30.445  1.00 38.09  ? 196 HOH A O   1 
HETATM 1332 O  O   . HOH F 4 .   ? 24.906 12.490 -4.355  1.00 31.44  ? 197 HOH A O   1 
HETATM 1333 O  O   . HOH F 4 .   ? 31.003 25.725 27.630  1.00 35.97  ? 198 HOH A O   1 
HETATM 1334 O  O   . HOH F 4 .   ? 33.053 18.349 22.286  1.00 23.79  ? 200 HOH A O   1 
HETATM 1335 O  O   . HOH F 4 .   ? 29.906 7.926  22.130  1.00 27.03  ? 201 HOH A O   1 
HETATM 1336 O  O   . HOH F 4 .   ? 30.816 12.254 20.570  1.00 52.47  ? 202 HOH A O   1 
HETATM 1337 O  O   . HOH F 4 .   ? 37.437 19.518 13.151  1.00 31.11  ? 203 HOH A O   1 
HETATM 1338 O  O   . HOH F 4 .   ? 39.166 17.819 11.596  1.00 36.09  ? 204 HOH A O   1 
HETATM 1339 O  O   . HOH F 4 .   ? 25.857 17.244 9.151   1.00 34.11  ? 206 HOH A O   1 
HETATM 1340 O  O   . HOH F 4 .   ? 41.734 15.909 8.730   1.00 42.70  ? 207 HOH A O   1 
HETATM 1341 O  O   . HOH F 4 .   ? 35.521 11.602 4.867   1.00 13.10  ? 208 HOH A O   1 
HETATM 1342 O  O   . HOH F 4 .   ? 42.648 16.745 4.820   1.00 33.52  ? 209 HOH A O   1 
HETATM 1343 O  O   . HOH F 4 .   ? 35.364 -5.423 0.458   1.00 33.55  ? 210 HOH A O   1 
HETATM 1344 O  O   . HOH F 4 .   ? 46.823 9.941  -0.263  1.00 26.68  ? 211 HOH A O   1 
HETATM 1345 O  O   . HOH F 4 .   ? 23.034 17.372 -1.523  1.00 54.08  ? 212 HOH A O   1 
HETATM 1346 O  O   . HOH F 4 .   ? 25.878 -1.906 -1.282  1.00 17.69  ? 213 HOH A O   1 
HETATM 1347 O  O   . HOH F 4 .   ? 22.101 -3.839 -2.071  1.00 36.41  ? 214 HOH A O   1 
HETATM 1348 O  O   . HOH F 4 .   ? 33.200 14.066 26.295  1.00 20.90  ? 215 HOH A O   1 
HETATM 1349 O  O   . HOH F 4 .   ? 36.306 10.068 -8.358  1.00 32.95  ? 216 HOH A O   1 
HETATM 1350 O  O   . HOH F 4 .   ? 34.183 -1.226 -9.731  1.00 44.54  ? 217 HOH A O   1 
HETATM 1351 O  O   . HOH F 4 .   ? 28.142 9.138  -11.756 1.00 31.53  ? 218 HOH A O   1 
HETATM 1352 O  O   . HOH F 4 .   ? 27.371 11.830 -11.295 1.00 29.61  ? 219 HOH A O   1 
HETATM 1353 O  O   . HOH F 4 .   ? 34.195 18.746 -8.611  1.00 42.28  ? 220 HOH A O   1 
HETATM 1354 O  O   . HOH F 4 .   ? 44.210 5.721  17.095  1.00 41.26  ? 221 HOH A O   1 
HETATM 1355 O  O   . HOH F 4 .   ? 29.780 24.425 17.619  1.00 49.06  ? 222 HOH A O   1 
HETATM 1356 O  O   . HOH F 4 .   ? 42.608 -4.620 12.725  1.00 28.41  ? 223 HOH A O   1 
HETATM 1357 O  O   . HOH F 4 .   ? 36.348 17.366 12.868  1.00 50.00  ? 224 HOH A O   1 
HETATM 1358 O  O   . HOH F 4 .   ? 33.991 17.051 12.427  1.00 58.54  ? 225 HOH A O   1 
HETATM 1359 O  O   . HOH F 4 .   ? 22.121 -3.263 11.351  1.00 43.15  ? 226 HOH A O   1 
HETATM 1360 O  O   . HOH F 4 .   ? 48.868 6.787  11.796  1.00 43.31  ? 227 HOH A O   1 
HETATM 1361 O  O   . HOH F 4 .   ? 48.126 11.083 10.805  1.00 54.30  ? 228 HOH A O   1 
HETATM 1362 O  O   . HOH F 4 .   ? 41.811 16.815 12.172  1.00 34.02  ? 229 HOH A O   1 
HETATM 1363 O  O   . HOH F 4 .   ? 43.542 14.182 6.056   1.00 34.74  ? 230 HOH A O   1 
HETATM 1364 O  O   . HOH F 4 .   ? 42.509 -4.675 1.537   1.00 34.83  ? 231 HOH A O   1 
HETATM 1365 O  O   . HOH F 4 .   ? 46.694 7.191  -0.979  1.00 30.18  ? 232 HOH A O   1 
HETATM 1366 O  O   . HOH F 4 .   ? 44.683 8.016  -2.932  1.00 57.08  ? 233 HOH A O   1 
HETATM 1367 O  O   . HOH F 4 .   ? 40.403 18.925 -6.576  1.00 60.62  ? 234 HOH A O   1 
HETATM 1368 O  O   . HOH F 4 .   ? 31.239 -0.146 -11.070 1.00 30.45  ? 235 HOH A O   1 
HETATM 1369 O  O   . HOH F 4 .   ? 46.624 20.068 12.175  1.00 46.72  ? 236 HOH A O   1 
HETATM 1370 O  O   . HOH F 4 .   ? 40.340 16.308 6.565   1.00 43.62  ? 237 HOH A O   1 
HETATM 1371 O  O   . HOH F 4 .   ? 35.251 -2.460 -7.791  1.00 31.67  ? 238 HOH A O   1 
HETATM 1372 O  O   . HOH F 4 .   ? 36.144 12.727 28.321  1.00 30.48  ? 239 HOH A O   1 
HETATM 1373 O  O   . HOH F 4 .   ? 43.786 5.137  25.143  1.00 34.19  ? 240 HOH A O   1 
HETATM 1374 O  O   . HOH F 4 .   ? 25.330 9.438  17.681  1.00 41.35  ? 242 HOH A O   1 
HETATM 1375 O  O   . HOH F 4 .   ? 46.886 4.606  11.725  1.00 29.48  ? 244 HOH A O   1 
HETATM 1376 O  O   . HOH F 4 .   ? 47.530 13.510 3.173   1.00 51.83  ? 245 HOH A O   1 
HETATM 1377 O  O   . HOH F 4 .   ? 30.660 15.821 20.737  1.00 53.44  ? 246 HOH A O   1 
HETATM 1378 O  O   . HOH F 4 .   ? 46.483 26.587 14.929  1.00 63.08  ? 247 HOH A O   1 
HETATM 1379 O  O   . HOH F 4 .   ? 39.375 -5.712 6.020   1.00 28.28  ? 248 HOH A O   1 
HETATM 1380 O  O   . HOH F 4 .   ? 38.632 10.465 -7.046  1.00 41.05  ? 249 HOH A O   1 
HETATM 1381 O  O   . HOH F 4 .   ? 36.509 11.688 -10.563 1.00 49.80  ? 250 HOH A O   1 
HETATM 1382 O  O   . HOH F 4 .   ? 33.959 13.372 -10.940 1.00 32.55  ? 251 HOH A O   1 
HETATM 1383 O  O   . HOH F 4 .   ? 18.823 5.971  1.452   1.00 43.13  ? 253 HOH A O   1 
HETATM 1384 O  O   . HOH F 4 .   ? 25.427 16.611 11.810  1.00 55.54  ? 254 HOH A O   1 
HETATM 1385 O  O   . HOH F 4 .   ? 37.048 15.866 10.437  1.00 42.74  ? 256 HOH A O   1 
HETATM 1386 O  O   . HOH F 4 .   ? 46.280 6.969  18.650  1.00 68.24  ? 257 HOH A O   1 
HETATM 1387 O  O   . HOH F 4 .   ? 45.872 26.615 21.420  1.00 81.81  ? 258 HOH A O   1 
HETATM 1388 O  O   . HOH F 4 .   ? 41.016 12.992 32.125  1.00 38.67  ? 259 HOH A O   1 
HETATM 1389 O  O   . HOH F 4 .   ? 44.958 11.009 31.106  1.00 66.03  ? 260 HOH A O   1 
HETATM 1390 O  O   . HOH F 4 .   ? 39.281 6.196  -7.075  1.00 55.14  ? 261 HOH A O   1 
HETATM 1391 O  O   . HOH F 4 .   ? 34.544 14.036 15.944  1.00 48.51  ? 265 HOH A O   1 
HETATM 1392 O  O   . HOH F 4 .   ? 34.254 16.253 16.408  1.00 73.87  ? 266 HOH A O   1 
HETATM 1393 O  O   . HOH F 4 .   ? 34.880 15.148 13.577  1.00 34.84  ? 267 HOH A O   1 
HETATM 1394 O  O   . HOH F 4 .   ? 16.220 9.252  9.605   1.00 52.37  ? 268 HOH A O   1 
HETATM 1395 O  O   . HOH F 4 .   ? 44.412 22.139 9.873   1.00 45.61  ? 269 HOH A O   1 
HETATM 1396 O  O   . HOH F 4 .   ? 30.061 18.534 -0.226  1.00 18.25  ? 270 HOH A O   1 
HETATM 1397 O  O   . HOH F 4 .   ? 36.987 7.323  -9.714  1.00 51.67  ? 271 HOH A O   1 
HETATM 1398 O  O   . HOH F 4 .   ? 17.564 13.497 -5.856  1.00 56.04  ? 272 HOH A O   1 
HETATM 1399 O  O   . HOH F 4 .   ? 38.917 -6.321 0.815   1.00 32.76  ? 273 HOH A O   1 
HETATM 1400 O  O   . HOH F 4 .   ? 31.336 11.619 15.581  1.00 26.91  ? 274 HOH A O   1 
HETATM 1401 O  O   . HOH F 4 .   ? 28.801 19.172 7.163   1.00 65.05  ? 275 HOH A O   1 
HETATM 1402 O  O   . HOH F 4 .   ? 19.061 11.089 0.874   1.00 51.52  ? 276 HOH A O   1 
HETATM 1403 O  O   . HOH F 4 .   ? 34.443 -4.499 -5.906  1.00 33.94  ? 277 HOH A O   1 
HETATM 1404 O  O   . HOH F 4 .   ? 41.176 25.917 31.281  1.00 41.18  ? 278 HOH A O   1 
HETATM 1405 O  O   . HOH F 4 .   ? 19.166 16.384 0.237   1.00 64.27  ? 279 HOH A O   1 
HETATM 1406 O  O   . HOH F 4 .   ? 32.948 17.487 18.525  1.00 57.74  ? 280 HOH A O   1 
HETATM 1407 O  O   . HOH F 4 .   ? 31.867 21.028 21.598  1.00 34.21  ? 281 HOH A O   1 
HETATM 1408 O  O   . HOH F 4 .   ? 32.630 19.898 24.297  1.00 46.41  ? 282 HOH A O   1 
HETATM 1409 O  O   . HOH F 4 .   ? 44.561 3.854  15.665  1.00 48.43  ? 283 HOH A O   1 
HETATM 1410 O  O   . HOH F 4 .   ? 50.251 12.775 26.467  1.00 54.22  ? 284 HOH A O   1 
HETATM 1411 O  O   . HOH F 4 .   ? 43.239 15.940 15.205  1.00 49.70  ? 285 HOH A O   1 
HETATM 1412 O  O   . HOH F 4 .   ? 50.184 16.658 26.748  1.00 50.47  ? 286 HOH A O   1 
HETATM 1413 O  O   . HOH F 4 .   ? 44.275 -1.192 15.565  1.00 29.35  ? 288 HOH A O   1 
HETATM 1414 O  O   . HOH F 4 .   ? 20.673 9.527  13.716  1.00 48.08  ? 289 HOH A O   1 
HETATM 1415 O  O   . HOH F 4 .   ? 21.224 -6.188 4.291   1.00 55.38  ? 290 HOH A O   1 
HETATM 1416 O  O   . HOH F 4 .   ? 23.462 -6.131 -0.931  1.00 42.67  ? 291 HOH A O   1 
HETATM 1417 O  O   . HOH F 4 .   ? 19.598 7.883  -1.753  1.00 54.61  ? 292 HOH A O   1 
HETATM 1418 O  O   . HOH F 4 .   ? 28.493 -0.451 -12.055 1.00 50.64  ? 293 HOH A O   1 
HETATM 1419 O  O   . HOH F 4 .   ? 47.877 2.126  10.111  1.00 74.51  ? 294 HOH A O   1 
HETATM 1420 O  O   . HOH F 4 .   ? 46.951 3.901  14.761  1.00 37.70  ? 295 HOH A O   1 
HETATM 1421 O  O   . HOH F 4 .   ? 41.818 -6.740 5.894   1.00 55.95  ? 296 HOH A O   1 
HETATM 1422 O  O   . HOH F 4 .   ? 45.348 16.158 14.386  1.00 58.67  ? 298 HOH A O   1 
HETATM 1423 O  O   . HOH F 4 .   ? 32.910 13.202 14.575  1.00 32.80  ? 299 HOH A O   1 
HETATM 1424 O  O   . HOH F 4 .   ? 37.174 19.979 -9.339  1.00 56.51  ? 300 HOH A O   1 
HETATM 1425 O  O   . HOH F 4 .   ? 19.966 4.789  -1.594  1.00 64.09  ? 301 HOH A O   1 
HETATM 1426 O  O   . HOH F 4 .   ? 18.043 -1.988 6.226   1.00 47.25  ? 302 HOH A O   1 
HETATM 1427 O  O   . HOH F 4 .   ? 33.385 18.940 3.855   1.00 39.24  ? 303 HOH A O   1 
HETATM 1428 O  O   . HOH F 4 .   ? 42.147 19.045 10.097  1.00 46.07  ? 304 HOH A O   1 
HETATM 1429 O  O   . HOH F 4 .   ? 34.873 21.175 10.274  1.00 51.47  ? 306 HOH A O   1 
HETATM 1430 O  O   . HOH F 4 .   ? 31.864 19.402 19.901  1.00 47.35  ? 307 HOH A O   1 
HETATM 1431 O  O   . HOH F 4 .   ? 39.169 14.702 34.071  1.00 53.43  ? 308 HOH A O   1 
HETATM 1432 O  O   . HOH F 4 .   ? 29.564 1.695  -11.709 1.00 29.28  ? 311 HOH A O   1 
HETATM 1433 O  O   . HOH F 4 .   ? 39.890 11.752 -8.559  1.00 39.59  ? 312 HOH A O   1 
HETATM 1434 O  O   . HOH F 4 .   ? 41.357 8.351  -6.452  1.00 64.12  ? 313 HOH A O   1 
HETATM 1435 O  O   . HOH F 4 .   ? 49.886 12.264 12.561  1.00 56.84  ? 315 HOH A O   1 
HETATM 1436 O  O   . HOH F 4 .   ? 42.814 17.351 -7.638  1.00 74.10  ? 316 HOH A O   1 
HETATM 1437 O  O   . HOH F 4 .   ? 47.953 24.348 17.699  1.00 56.40  ? 319 HOH A O   1 
HETATM 1438 O  O   . HOH F 4 .   ? 38.347 18.616 7.395   1.00 60.22  ? 321 HOH A O   1 
HETATM 1439 O  O   . HOH F 4 .   ? 49.091 21.550 18.562  1.00 68.84  ? 322 HOH A 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   MET 1   1   1   MET MET A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   ILE 3   3   3   ILE ILE A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  TYR 18  18  18  TYR TYR A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  ALA 41  40  40  ALA ALA A A n 
A 1 42  ALA 42  41  41  ALA ALA A . n 
A 1 43  ALA 43  42  42  ALA ALA A . n 
A 1 44  LYS 44  43  43  LYS LYS A . n 
A 1 45  SER 45  44  44  SER SER A . n 
A 1 46  GLU 46  45  45  GLU GLU A . n 
A 1 47  LEU 47  46  46  LEU LEU A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  LYS 49  48  48  LYS LYS A . n 
A 1 50  ALA 50  49  49  ALA ALA A . n 
A 1 51  ILE 51  50  50  ILE ILE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ARG 53  52  52  ARG ARG A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ASN 56  55  55  ASN ASN A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  VAL 58  57  57  VAL VAL A . n 
A 1 59  ILE 59  58  58  ILE ILE A . n 
A 1 60  THR 60  59  59  THR THR A . n 
A 1 61  LYS 61  60  60  LYS LYS A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  ALA 64  63  63  ALA ALA A . n 
A 1 65  GLU 65  64  64  GLU GLU A . n 
A 1 66  LYS 66  65  65  LYS LYS A . n 
A 1 67  LEU 67  66  66  LEU LEU A . n 
A 1 68  PHE 68  67  67  PHE PHE A . n 
A 1 69  ASN 69  68  68  ASN ASN A . n 
A 1 70  GLN 70  69  69  GLN GLN A . n 
A 1 71  ASP 71  70  70  ASP ASP A . n 
A 1 72  VAL 72  71  71  VAL VAL A . n 
A 1 73  ASP 73  72  72  ASP ASP A . n 
A 1 74  ALA 74  73  73  ALA ALA A . n 
A 1 75  ALA 75  74  74  ALA ALA A . n 
A 1 76  VAL 76  75  75  VAL VAL A . n 
A 1 77  ARG 77  76  76  ARG ARG A . n 
A 1 78  GLY 78  77  77  GLY GLY A . n 
A 1 79  ILE 79  78  78  ILE ILE A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  ARG 81  80  80  ARG ARG A . n 
A 1 82  ASN 82  81  81  ASN ASN A . n 
A 1 83  ALA 83  82  82  ALA ALA A . n 
A 1 84  LYS 84  83  83  LYS LYS A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  LYS 86  85  85  LYS LYS A . n 
A 1 87  PRO 87  86  86  PRO PRO A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  TYR 89  88  88  TYR TYR A . n 
A 1 90  ASP 90  89  89  ASP ASP A . n 
A 1 91  SER 91  90  90  SER SER A . n 
A 1 92  LEU 92  91  91  LEU LEU A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  ALA 94  93  93  ALA ALA A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ARG 96  95  95  ARG ARG A . n 
A 1 97  ARG 97  96  96  ARG ARG A . n 
A 1 98  ALA 98  97  97  ALA ALA A . n 
A 1 99  ALA 99  98  98  ALA ALA A . n 
A 1 100 LEU 100 99  99  LEU LEU A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 ASN 102 101 101 ASN ASN A . n 
A 1 103 MET 103 102 102 MET MET A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 PHE 105 104 104 PHE PHE A . n 
A 1 106 GLN 106 105 105 GLN GLN A . n 
A 1 107 MET 107 106 106 MET MET A . n 
A 1 108 GLY 108 107 107 GLY GLY A . n 
A 1 109 GLU 109 108 108 GLU GLU A . n 
A 1 110 THR 110 109 109 THR THR A . n 
A 1 111 GLY 111 110 110 GLY GLY A . n 
A 1 112 VAL 112 111 111 VAL VAL A . n 
A 1 113 ALA 113 112 112 ALA ALA A . n 
A 1 114 GLY 114 113 113 GLY GLY A . n 
A 1 115 PHE 115 114 114 PHE PHE A . n 
A 1 116 THR 116 115 115 THR THR A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 SER 118 117 117 SER SER A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 ARG 120 119 119 ARG ARG A . n 
A 1 121 MET 121 120 120 MET MET A . n 
A 1 122 LEU 122 121 121 LEU LEU A . n 
A 1 123 GLN 123 122 122 GLN GLN A . n 
A 1 124 GLN 124 123 123 GLN GLN A . n 
A 1 125 LYS 125 124 124 LYS LYS A . n 
A 1 126 ARG 126 125 125 ARG ARG A . n 
A 1 127 TRP 127 126 126 TRP TRP A . n 
A 1 128 ASP 128 127 127 ASP ASP A . n 
A 1 129 GLU 129 128 128 GLU GLU A . n 
A 1 130 ALA 130 129 129 ALA ALA A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 VAL 132 131 131 VAL VAL A . n 
A 1 133 ASN 133 132 132 ASN ASN A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 LYS 136 135 135 LYS LYS A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 ARG 138 137 137 ARG ARG A . n 
A 1 139 TRP 139 138 138 TRP TRP A . n 
A 1 140 TYR 140 139 139 TYR TYR A . n 
A 1 141 ASN 141 140 140 ASN ASN A . n 
A 1 142 GLN 142 141 141 GLN GLN A . n 
A 1 143 THR 143 142 142 THR THR A . n 
A 1 144 PRO 144 143 143 PRO PRO A . n 
A 1 145 ASN 145 144 144 ASN ASN A . n 
A 1 146 ARG 146 145 145 ARG ARG A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 ARG 149 148 148 ARG ARG A . n 
A 1 150 VAL 150 149 149 VAL VAL A . n 
A 1 151 ILE 151 150 150 ILE ILE A . n 
A 1 152 THR 152 151 151 THR THR A . n 
A 1 153 THR 153 152 152 THR THR A . n 
A 1 154 PHE 154 153 153 PHE PHE A . n 
A 1 155 ARG 155 154 154 ARG ARG A . n 
A 1 156 THR 156 155 155 THR THR A . n 
A 1 157 GLY 157 156 156 GLY GLY A . n 
A 1 158 THR 158 157 157 THR THR A . n 
A 1 159 TRP 159 158 158 TRP TRP A . n 
A 1 160 ASP 160 159 159 ASP ASP A . n 
A 1 161 ALA 161 160 160 ALA ALA A . n 
A 1 162 TYR 162 161 161 TYR TYR A . n 
A 1 163 LYS 163 162 162 LYS LYS A . n 
A 1 164 ASN 164 163 ?   ?   ?   A . n 
A 1 165 LEU 165 164 ?   ?   ?   A . 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 
B 2 CL  1   173 173 CL  CL  A . 
C 2 CL  1   178 178 CL  CL  A . 
D 3 BME 1   901 901 BME SEO A . 
E 3 BME 1   902 902 BME SEO A . 
F 4 HOH 1   171 171 HOH HOH A . 
F 4 HOH 2   172 172 HOH HOH A . 
F 4 HOH 3   174 174 HOH HOH A . 
F 4 HOH 4   175 175 HOH HOH A . 
F 4 HOH 5   176 176 HOH HOH A . 
F 4 HOH 6   177 177 HOH HOH A . 
F 4 HOH 7   179 179 HOH HOH A . 
F 4 HOH 8   180 180 HOH HOH A . 
F 4 HOH 9   181 181 HOH HOH A . 
F 4 HOH 10  182 182 HOH HOH A . 
F 4 HOH 11  183 183 HOH HOH A . 
F 4 HOH 12  184 184 HOH HOH A . 
F 4 HOH 13  185 185 HOH HOH A . 
F 4 HOH 14  186 186 HOH HOH A . 
F 4 HOH 15  187 187 HOH HOH A . 
F 4 HOH 16  188 188 HOH HOH A . 
F 4 HOH 17  189 189 HOH HOH A . 
F 4 HOH 18  190 190 HOH HOH A . 
F 4 HOH 19  191 191 HOH HOH A . 
F 4 HOH 20  192 192 HOH HOH A . 
F 4 HOH 21  193 193 HOH HOH A . 
F 4 HOH 22  194 194 HOH HOH A . 
F 4 HOH 23  195 195 HOH HOH A . 
F 4 HOH 24  196 196 HOH HOH A . 
F 4 HOH 25  197 197 HOH HOH A . 
F 4 HOH 26  198 198 HOH HOH A . 
F 4 HOH 27  200 200 HOH HOH A . 
F 4 HOH 28  201 201 HOH HOH A . 
F 4 HOH 29  202 202 HOH HOH A . 
F 4 HOH 30  203 203 HOH HOH A . 
F 4 HOH 31  204 204 HOH HOH A . 
F 4 HOH 32  206 206 HOH HOH A . 
F 4 HOH 33  207 207 HOH HOH A . 
F 4 HOH 34  208 208 HOH HOH A . 
F 4 HOH 35  209 209 HOH HOH A . 
F 4 HOH 36  210 210 HOH HOH A . 
F 4 HOH 37  211 211 HOH HOH A . 
F 4 HOH 38  212 212 HOH HOH A . 
F 4 HOH 39  213 213 HOH HOH A . 
F 4 HOH 40  214 214 HOH HOH A . 
F 4 HOH 41  215 215 HOH HOH A . 
F 4 HOH 42  216 216 HOH HOH A . 
F 4 HOH 43  217 217 HOH HOH A . 
F 4 HOH 44  218 218 HOH HOH A . 
F 4 HOH 45  219 219 HOH HOH A . 
F 4 HOH 46  220 220 HOH HOH A . 
F 4 HOH 47  221 221 HOH HOH A . 
F 4 HOH 48  222 222 HOH HOH A . 
F 4 HOH 49  223 223 HOH HOH A . 
F 4 HOH 50  224 224 HOH HOH A . 
F 4 HOH 51  225 225 HOH HOH A . 
F 4 HOH 52  226 226 HOH HOH A . 
F 4 HOH 53  227 227 HOH HOH A . 
F 4 HOH 54  228 228 HOH HOH A . 
F 4 HOH 55  229 229 HOH HOH A . 
F 4 HOH 56  230 230 HOH HOH A . 
F 4 HOH 57  231 231 HOH HOH A . 
F 4 HOH 58  232 232 HOH HOH A . 
F 4 HOH 59  233 233 HOH HOH A . 
F 4 HOH 60  234 234 HOH HOH A . 
F 4 HOH 61  235 235 HOH HOH A . 
F 4 HOH 62  236 236 HOH HOH A . 
F 4 HOH 63  237 237 HOH HOH A . 
F 4 HOH 64  238 238 HOH HOH A . 
F 4 HOH 65  239 239 HOH HOH A . 
F 4 HOH 66  240 240 HOH HOH A . 
F 4 HOH 67  242 242 HOH HOH A . 
F 4 HOH 68  244 244 HOH HOH A . 
F 4 HOH 69  245 245 HOH HOH A . 
F 4 HOH 70  246 246 HOH HOH A . 
F 4 HOH 71  247 247 HOH HOH A . 
F 4 HOH 72  248 248 HOH HOH A . 
F 4 HOH 73  249 249 HOH HOH A . 
F 4 HOH 74  250 250 HOH HOH A . 
F 4 HOH 75  251 251 HOH HOH A . 
F 4 HOH 76  253 253 HOH HOH A . 
F 4 HOH 77  254 254 HOH HOH A . 
F 4 HOH 78  256 256 HOH HOH A . 
F 4 HOH 79  257 257 HOH HOH A . 
F 4 HOH 80  258 258 HOH HOH A . 
F 4 HOH 81  259 259 HOH HOH A . 
F 4 HOH 82  260 260 HOH HOH A . 
F 4 HOH 83  261 261 HOH HOH A . 
F 4 HOH 84  265 265 HOH HOH A . 
F 4 HOH 85  266 266 HOH HOH A . 
F 4 HOH 86  267 267 HOH HOH A . 
F 4 HOH 87  268 268 HOH HOH A . 
F 4 HOH 88  269 269 HOH HOH A . 
F 4 HOH 89  270 270 HOH HOH A . 
F 4 HOH 90  271 271 HOH HOH A . 
F 4 HOH 91  272 272 HOH HOH A . 
F 4 HOH 92  273 273 HOH HOH A . 
F 4 HOH 93  274 274 HOH HOH A . 
F 4 HOH 94  275 275 HOH HOH A . 
F 4 HOH 95  276 276 HOH HOH A . 
F 4 HOH 96  277 277 HOH HOH A . 
F 4 HOH 97  278 278 HOH HOH A . 
F 4 HOH 98  279 279 HOH HOH A . 
F 4 HOH 99  280 280 HOH HOH A . 
F 4 HOH 100 281 281 HOH HOH A . 
F 4 HOH 101 282 282 HOH HOH A . 
F 4 HOH 102 283 283 HOH HOH A . 
F 4 HOH 103 284 284 HOH HOH A . 
F 4 HOH 104 285 285 HOH HOH A . 
F 4 HOH 105 286 286 HOH HOH A . 
F 4 HOH 106 288 288 HOH HOH A . 
F 4 HOH 107 289 289 HOH HOH A . 
F 4 HOH 108 290 290 HOH HOH A . 
F 4 HOH 109 291 291 HOH HOH A . 
F 4 HOH 110 292 292 HOH HOH A . 
F 4 HOH 111 293 293 HOH HOH A . 
F 4 HOH 112 294 294 HOH HOH A . 
F 4 HOH 113 295 295 HOH HOH A . 
F 4 HOH 114 296 296 HOH HOH A . 
F 4 HOH 115 298 298 HOH HOH A . 
F 4 HOH 116 299 299 HOH HOH A . 
F 4 HOH 117 300 300 HOH HOH A . 
F 4 HOH 118 301 301 HOH HOH A . 
F 4 HOH 119 302 302 HOH HOH A . 
F 4 HOH 120 303 303 HOH HOH A . 
F 4 HOH 121 304 304 HOH HOH A . 
F 4 HOH 122 306 306 HOH HOH A . 
F 4 HOH 123 307 307 HOH HOH A . 
F 4 HOH 124 308 308 HOH HOH A . 
F 4 HOH 125 311 311 HOH HOH A . 
F 4 HOH 126 312 312 HOH HOH A . 
F 4 HOH 127 313 313 HOH HOH A . 
F 4 HOH 128 315 315 HOH HOH A . 
F 4 HOH 129 316 316 HOH HOH A . 
F 4 HOH 130 319 319 HOH HOH A . 
F 4 HOH 131 321 321 HOH HOH A . 
F 4 HOH 132 322 322 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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_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 1993-10-31 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
_software.name             TNT 
_software.classification   refinement 
_software.version          . 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
THERE ARE SEVERAL SUBTLE ASPECTS OF THE SECONDARY STRUCTURE
OF THIS MOLECULE WHICH CANNOT CONVENIENTLY BE REPRESENTED
IN THE HELIX AND SHEET RECORDS BELOW.  THESE ASPECTS
INFLUENCE THE REPRESENTATION OF HELIX 6 AND STRAND 3 OF
SHEET *S1*.  THE PAPER J.MOL.BIOL., V. 118, P. 81, 1978
SHOULD BE CONSULTED FOR THESE SUBTLETIES.
;
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 CL A CL  173 ? ? 1_555 O  A HOH 291 ? ? 4_655 1.63 
2 1 O1 A BME 901 ? ? 1_555 O1 A BME 901 ? ? 5_555 1.98 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             5 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             5 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.329 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.077 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB A ASP 47  ? ? CG A ASP 47  ? ? OD1 A ASP 47  ? ? 126.89 118.30 8.59  0.90 N 
2  1 CB A ASP 47  ? ? CG A ASP 47  ? ? OD2 A ASP 47  ? ? 109.73 118.30 -8.57 0.90 N 
3  1 CB A ASP 70  ? ? CG A ASP 70  ? ? OD1 A ASP 70  ? ? 125.35 118.30 7.05  0.90 N 
4  1 NE A ARG 76  ? ? CZ A ARG 76  ? ? NH1 A ARG 76  ? ? 125.16 120.30 4.86  0.50 N 
5  1 NE A ARG 80  ? ? CZ A ARG 80  ? ? NH1 A ARG 80  ? ? 123.86 120.30 3.56  0.50 N 
6  1 NE A ARG 80  ? ? CZ A ARG 80  ? ? NH2 A ARG 80  ? ? 117.29 120.30 -3.01 0.50 N 
7  1 CB A ASP 92  ? ? CG A ASP 92  ? ? OD1 A ASP 92  ? ? 109.56 118.30 -8.74 0.90 N 
8  1 CB A ASP 92  ? ? CG A ASP 92  ? ? OD2 A ASP 92  ? ? 124.79 118.30 6.49  0.90 N 
9  1 CB A ASP 127 ? ? CG A ASP 127 ? ? OD1 A ASP 127 ? ? 124.75 118.30 6.45  0.90 N 
10 1 CD A ARG 145 ? ? NE A ARG 145 ? ? CZ  A ARG 145 ? ? 113.84 123.60 -9.76 1.40 N 
11 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH1 A ARG 145 ? ? 116.36 120.30 -3.94 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ILE A 29 ? ? -106.80 71.71  
2 1 ALA A 40 A ? -123.42 -78.14 
# 
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 ASN 163 ? A ASN 164 
2 1 Y 1 A LEU 164 ? A LEU 165 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION'       CL  
3 BETA-MERCAPTOETHANOL BME 
4 water                HOH 
# 
