data_1GKC
# 
_entry.id   1GKC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.382 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   1GKC         pdb_00001gkc 10.2210/pdb1gkc/pdb 
PDBE  EBI-8443     ?            ?                   
WWPDB D_1290008443 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1GKC 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2001-08-10 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Rowsell, S.'   1 
'Pauptit, R.A.' 2 
# 
_citation.id                        primary 
_citation.title                     'Crystal Structure of Mmp9 in Complex with a Reverse Hydroxamate Inhibitor' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            319 
_citation.page_first                173 
_citation.page_last                 ? 
_citation.year                      2002 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12051944 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(02)00262-0' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rowsell, S.'    1  ? 
primary 'Hawtin, P.'     2  ? 
primary 'Minshull, C.A.' 3  ? 
primary 'Jepson, H.'     4  ? 
primary 'Brockbank, S.'  5  ? 
primary 'Barratt, D.'    6  ? 
primary 'Slater, A.M.'   7  ? 
primary 'Mcpheat, W.'    8  ? 
primary 'Waterson, D.'   9  ? 
primary 'Henney, A.'     10 ? 
primary 'Pauptit, R.A.'  11 ? 
# 
_cell.entry_id           1GKC 
_cell.length_a           56.005 
_cell.length_b           56.005 
_cell.length_c           262.655 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1GKC 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
# 
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 '92 KDA TYPE IV COLLAGENASE'                                                               18384.408 2   
3.4.24.35 ? 'CATALYTIC DOMAIN RESIDUES 107-215,391-443' ? 
2 non-polymer syn 'CALCIUM ION'                                                                              40.078    10  ? ? ? ? 
3 non-polymer syn 'N~2~-[(2R)-2-{[formyl(hydroxy)amino]methyl}-4-methylpentanoyl]-N,3-dimethyl-L-valinamide' 315.408   2   ? ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                                 65.409    4   ? ? ? ? 
5 water       nat water                                                                                      18.015    120 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'MMP-9,92 KDA GELATINASE, GELATINASE B, MATRIX METALLOPROTEINASE-9' 
# 
_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       
;MFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKD
GLLAHAFPPGPGIQGDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIR
HLY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKD
GLLAHAFPPGPGIQGDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIR
HLY
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PHE n 
1 3   GLN n 
1 4   THR n 
1 5   PHE n 
1 6   GLU n 
1 7   GLY n 
1 8   ASP n 
1 9   LEU n 
1 10  LYS n 
1 11  TRP n 
1 12  HIS n 
1 13  HIS n 
1 14  HIS n 
1 15  ASN n 
1 16  ILE n 
1 17  THR n 
1 18  TYR n 
1 19  TRP n 
1 20  ILE n 
1 21  GLN n 
1 22  ASN n 
1 23  TYR n 
1 24  SER n 
1 25  GLU n 
1 26  ASP n 
1 27  LEU n 
1 28  PRO n 
1 29  ARG n 
1 30  ALA n 
1 31  VAL n 
1 32  ILE n 
1 33  ASP n 
1 34  ASP n 
1 35  ALA n 
1 36  PHE n 
1 37  ALA n 
1 38  ARG n 
1 39  ALA n 
1 40  PHE n 
1 41  ALA n 
1 42  LEU n 
1 43  TRP n 
1 44  SER n 
1 45  ALA n 
1 46  VAL n 
1 47  THR n 
1 48  PRO n 
1 49  LEU n 
1 50  THR n 
1 51  PHE n 
1 52  THR n 
1 53  ARG n 
1 54  VAL n 
1 55  TYR n 
1 56  SER n 
1 57  ARG n 
1 58  ASP n 
1 59  ALA n 
1 60  ASP n 
1 61  ILE n 
1 62  VAL n 
1 63  ILE n 
1 64  GLN n 
1 65  PHE n 
1 66  GLY n 
1 67  VAL n 
1 68  ALA n 
1 69  GLU n 
1 70  HIS n 
1 71  GLY n 
1 72  ASP n 
1 73  GLY n 
1 74  TYR n 
1 75  PRO n 
1 76  PHE n 
1 77  ASP n 
1 78  GLY n 
1 79  LYS n 
1 80  ASP n 
1 81  GLY n 
1 82  LEU n 
1 83  LEU n 
1 84  ALA n 
1 85  HIS n 
1 86  ALA n 
1 87  PHE n 
1 88  PRO n 
1 89  PRO n 
1 90  GLY n 
1 91  PRO n 
1 92  GLY n 
1 93  ILE n 
1 94  GLN n 
1 95  GLY n 
1 96  ASP n 
1 97  ALA n 
1 98  HIS n 
1 99  PHE n 
1 100 ASP n 
1 101 ASP n 
1 102 ASP n 
1 103 GLU n 
1 104 LEU n 
1 105 TRP n 
1 106 SER n 
1 107 LEU n 
1 108 GLY n 
1 109 LYS n 
1 110 GLY n 
1 111 GLN n 
1 112 GLY n 
1 113 TYR n 
1 114 SER n 
1 115 LEU n 
1 116 PHE n 
1 117 LEU n 
1 118 VAL n 
1 119 ALA n 
1 120 ALA n 
1 121 HIS n 
1 122 GLU n 
1 123 PHE n 
1 124 GLY n 
1 125 HIS n 
1 126 ALA n 
1 127 LEU n 
1 128 GLY n 
1 129 LEU n 
1 130 ASP n 
1 131 HIS n 
1 132 SER n 
1 133 SER n 
1 134 VAL n 
1 135 PRO n 
1 136 GLU n 
1 137 ALA n 
1 138 LEU n 
1 139 MET n 
1 140 TYR n 
1 141 PRO n 
1 142 MET n 
1 143 TYR n 
1 144 ARG n 
1 145 PHE n 
1 146 THR n 
1 147 GLU n 
1 148 GLY n 
1 149 PRO n 
1 150 PRO n 
1 151 LEU n 
1 152 HIS n 
1 153 LYS n 
1 154 ASP n 
1 155 ASP n 
1 156 VAL n 
1 157 ASN n 
1 158 GLY n 
1 159 ILE n 
1 160 ARG n 
1 161 HIS n 
1 162 LEU n 
1 163 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 PDB 1GKC       1 ? ? 1GKC   ? 
2 UNP MM09_HUMAN 1 ? ? P14780 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1GKC A 1   ? 1   ? 1GKC   106 ? 106 ? 106 106 
2 2 1GKC A 2   ? 110 ? P14780 107 ? 215 ? 107 215 
3 2 1GKC A 111 ? 163 ? P14780 391 ? 443 ? 391 443 
4 1 1GKC B 1   ? 1   ? 1GKC   106 ? 106 ? 106 106 
5 2 1GKC B 2   ? 110 ? P14780 107 ? 215 ? 107 215 
6 2 1GKC B 111 ? 163 ? P14780 391 ? 443 ? 391 443 
# 
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 
CA  non-polymer         . 'CALCIUM ION'                                                                              ? 'Ca 2' 
40.078  
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 
NFH non-polymer         . 'N~2~-[(2R)-2-{[formyl(hydroxy)amino]methyl}-4-methylpentanoyl]-N,3-dimethyl-L-valinamide' ? 
'C15 H29 N3 O4'  315.408 
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 
ZN  non-polymer         . 'ZINC ION'                                                                                 ? 'Zn 2' 
65.409  
# 
_exptl.entry_id          1GKC 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   2 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.80 
_exptl_crystal.density_percent_sol   50.00 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.50 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;THE CRYSTALLISATION DROPS CONTAINED A 1:1 MIXTURE OF PURIFIED COMPLEX SOLUTION (0.55 MG/ML PROTEIN AND 0.5 MM INHIBITOR SOLUTION CONCENTRATED TO ~4 MG/ML IN 20 MM TRIS- HCL PH 7.5, 2 MM CACL2, 50 MM NACL) AND RESERVOIR BUFFER (3.6 M NACL, 0.1 M HEPES PH 7.5).
;
# 
_diffrn.id                     1 
_diffrn.ambient_temp           298.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC CCD' 
_diffrn_detector.pdbx_collection_date   1999-08-25 
_diffrn_detector.details                'SILICON MIRROR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI(III)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.87 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX9.6' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX9.6 
_diffrn_source.pdbx_wavelength             0.87 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1GKC 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             51.300 
_reflns.d_resolution_high            2.300 
_reflns.number_obs                   17375 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         88.0 
_reflns.pdbx_Rmerge_I_obs            0.11700 
_reflns.pdbx_Rsym_value              0.11700 
_reflns.pdbx_netI_over_sigmaI        14.4000 
_reflns.B_iso_Wilson_estimate        28.30 
_reflns.pdbx_redundancy              4.500 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.30 
_reflns_shell.d_res_low              2.44 
_reflns_shell.percent_possible_all   83.0 
_reflns_shell.Rmerge_I_obs           0.47900 
_reflns_shell.pdbx_Rsym_value        0.47900 
_reflns_shell.meanI_over_sigI_obs    4.200 
_reflns_shell.pdbx_redundancy        4.40 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1GKC 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17375 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             51.30 
_refine.ls_d_res_high                            2.30 
_refine.ls_percent_reflns_obs                    88.3 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.207 
_refine.ls_R_factor_R_free                       0.239 
_refine.ls_R_factor_R_free_error                 0.009 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.500 
_refine.ls_number_reflns_R_free                  684 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               28.00 
_refine.aniso_B[1][1]                            -5.43000 
_refine.aniso_B[2][2]                            -5.43000 
_refine.aniso_B[3][3]                            10.86000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 0.37 
_refine.solvent_model_param_bsol                 47.85 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'X-PLOR, CNS' 
_refine.pdbx_starting_model                      'PDB ENTRY 1HFS' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        1GKC 
_refine_analyze.Luzzati_coordinate_error_obs    0.28 
_refine_analyze.Luzzati_sigma_a_obs             0.28 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.32 
_refine_analyze.Luzzati_sigma_a_free            0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2512 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               2690 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        51.30 
# 
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 
c_bond_d                0.006 ?     ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.20  ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      23.40 ?     ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.77  ?     ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?     ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.710 1.500 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.710 2.000 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             2.670 2.000 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            3.860 2.500 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              1 
_refine_ls_restr_ncs.ncs_model_details   ? 
_refine_ls_restr_ncs.rms_dev_position    0.09 
_refine_ls_restr_ncs.weight_position     50 
_refine_ls_restr_ncs.rms_dev_B_iso       2.6 
_refine_ls_restr_ncs.weight_B_iso        2.0 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_type           . 
_refine_ls_restr_ncs.pdbx_auth_asym_id   . 
_refine_ls_restr_ncs.pdbx_ens_id         1 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_asym_id        ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.d_res_high                       2.30 
_refine_ls_shell.d_res_low                        2.38 
_refine_ls_shell.number_reflns_R_work             1517 
_refine_ls_shell.R_factor_R_work                  0.2770 
_refine_ls_shell.percent_reflns_obs               83.00 
_refine_ls_shell.R_factor_R_free                  0.3380 
_refine_ls_shell.R_factor_R_free_error            0.041 
_refine_ls_shell.percent_reflns_R_free            3.60 
_refine_ls_shell.number_reflns_R_free             68 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.pdbx_refine_id 
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
'X-RAY DIFFRACTION' 1 PROTEIN_REP.PARAM PROTEIN.TOP 
'X-RAY DIFFRACTION' 2 ION.PARAM         WATER.TOP   
'X-RAY DIFFRACTION' 3 WATER_REP.PARAM   ION.TOP     
'X-RAY DIFFRACTION' 4 FRA.PAR           FRA.TOP     
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   -0.228610 
_struct_ncs_oper.matrix[1][2]   -0.962500 
_struct_ncs_oper.matrix[1][3]   0.146040 
_struct_ncs_oper.matrix[2][1]   -0.957770 
_struct_ncs_oper.matrix[2][2]   0.195490 
_struct_ncs_oper.matrix[2][3]   -0.210850 
_struct_ncs_oper.matrix[3][1]   0.174400 
_struct_ncs_oper.matrix[3][2]   -0.188080 
_struct_ncs_oper.matrix[3][3]   -0.966550 
_struct_ncs_oper.vector[1]      68.09161 
_struct_ncs_oper.vector[2]      96.29951 
_struct_ncs_oper.vector[3]      249.65909 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       ? 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  1GKC 
_struct.title                     'MMP9-inhibitor complex' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1GKC 
_struct_keywords.pdbx_keywords   'HYDROLASE/HYDROLASE INHIBITOR' 
_struct_keywords.text            'MATRIX METALLOPROTEASE, HYDROLASE, GLYCOPROTEIN, HYDROLASE-HYDROLASE INHIBITOR COMPLEX' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 5 ? 
T N N 5 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 PRO A 28  ? ALA A 45  ? PRO A 133 ALA A 150 1 ? 18 
HELX_P HELX_P2 2 LEU A 115 ? LEU A 127 ? LEU A 395 LEU A 407 1 ? 13 
HELX_P HELX_P3 3 HIS A 152 ? TYR A 163 ? HIS A 432 TYR A 443 1 ? 12 
HELX_P HELX_P4 4 PRO B 28  ? ALA B 45  ? PRO B 133 ALA B 150 1 ? 18 
HELX_P HELX_P5 5 LEU B 115 ? LEU B 127 ? LEU B 395 LEU B 407 1 ? 13 
HELX_P HELX_P6 6 HIS B 152 ? TYR B 163 ? HIS B 432 TYR B 443 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 26  OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 131  A CA  1446 1_555 ? ? ? ? ? ? ? 3.141 ? ? 
metalc2  metalc ? ? A ASP 26  OD2 ? ? ? 1_555 E CA  . CA ? ? A ASP 131  A CA  1446 1_555 ? ? ? ? ? ? ? 2.603 ? ? 
metalc3  metalc ? ? A SER 44  O   ? ? ? 1_555 J CA  . CA ? ? A SER 149  A CA  1452 1_555 ? ? ? ? ? ? ? 2.972 ? ? 
metalc4  metalc ? ? A ASP 60  O   ? ? ? 1_555 D CA  . CA ? ? A ASP 165  A CA  1445 1_555 ? ? ? ? ? ? ? 2.531 ? ? 
metalc5  metalc ? ? A HIS 70  NE2 ? ? ? 1_555 I ZN  . ZN ? ? A HIS 175  A ZN  1451 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc6  metalc ? ? A ASP 72  OD2 ? ? ? 1_555 I ZN  . ZN ? ? A ASP 177  A ZN  1451 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc7  metalc ? ? A ASP 77  OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 182  A CA  1444 1_555 ? ? ? ? ? ? ? 2.650 ? ? 
metalc8  metalc ? ? A GLY 78  O   ? ? ? 1_555 C CA  . CA ? ? A GLY 183  A CA  1444 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc9  metalc ? ? A ASP 80  O   ? ? ? 1_555 C CA  . CA ? ? A ASP 185  A CA  1444 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc10 metalc ? ? A LEU 82  O   ? ? ? 1_555 C CA  . CA ? ? A LEU 187  A CA  1444 1_555 ? ? ? ? ? ? ? 2.507 ? ? 
metalc11 metalc ? ? A HIS 85  NE2 ? ? ? 1_555 I ZN  . ZN ? ? A HIS 190  A ZN  1451 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc12 metalc ? ? A GLY 92  O   ? ? ? 1_555 D CA  . CA ? ? A GLY 197  A CA  1445 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc13 metalc ? ? A GLN 94  O   ? ? ? 1_555 D CA  . CA ? ? A GLN 199  A CA  1445 1_555 ? ? ? ? ? ? ? 2.641 ? ? 
metalc14 metalc ? ? A ASP 96  OD1 ? ? ? 1_555 D CA  . CA ? ? A ASP 201  A CA  1445 1_555 ? ? ? ? ? ? ? 2.616 ? ? 
metalc15 metalc ? ? A HIS 98  ND1 ? ? ? 1_555 I ZN  . ZN ? ? A HIS 203  A ZN  1451 1_555 ? ? ? ? ? ? ? 2.225 ? ? 
metalc16 metalc ? ? A ASP 100 OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 205  A CA  1444 1_555 ? ? ? ? ? ? ? 2.543 ? ? 
metalc17 metalc ? ? A ASP 101 O   ? ? ? 1_555 E CA  . CA ? ? A ASP 206  A CA  1446 1_555 ? ? ? ? ? ? ? 2.675 ? ? 
metalc18 metalc ? ? A ASP 101 OD1 ? ? ? 1_555 E CA  . CA ? ? A ASP 206  A CA  1446 1_555 ? ? ? ? ? ? ? 2.812 ? ? 
metalc19 metalc ? ? A GLU 103 OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 208  A CA  1444 1_555 ? ? ? ? ? ? ? 2.677 ? ? 
metalc20 metalc ? ? A GLU 103 O   ? ? ? 1_555 E CA  . CA ? ? A GLU 208  A CA  1446 1_555 ? ? ? ? ? ? ? 2.694 ? ? 
metalc21 metalc ? ? A SER 106 OG  ? ? ? 1_555 F CA  . CA ? ? A SER 211  A CA  1447 1_555 ? ? ? ? ? ? ? 3.236 ? ? 
metalc22 metalc ? ? A LEU 107 O   ? ? ? 1_555 F CA  . CA ? ? A LEU 212  A CA  1447 1_555 ? ? ? ? ? ? ? 2.696 ? ? 
metalc23 metalc ? ? A GLY 108 O   ? ? ? 1_555 F CA  . CA ? ? A GLY 213  A CA  1447 1_555 ? ? ? ? ? ? ? 3.076 ? ? 
metalc24 metalc ? ? A LYS 109 O   ? ? ? 1_555 F CA  . CA ? ? A LYS 214  A CA  1447 1_555 ? ? ? ? ? ? ? 2.738 ? ? 
metalc25 metalc ? ? A HIS 121 NE2 ? ? ? 1_555 H ZN  . ZN ? ? A HIS 401  A ZN  1450 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc26 metalc ? ? A HIS 125 NE2 ? ? ? 1_555 H ZN  . ZN ? ? A HIS 405  A ZN  1450 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc27 metalc ? ? A HIS 131 NE2 ? ? ? 1_555 H ZN  . ZN ? ? A HIS 411  A ZN  1450 1_555 ? ? ? ? ? ? ? 2.223 ? ? 
metalc28 metalc ? ? D CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1445 A HOH 2028 1_555 ? ? ? ? ? ? ? 2.752 ? ? 
metalc29 metalc ? ? D CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1445 A HOH 2039 1_555 ? ? ? ? ? ? ? 2.816 ? ? 
metalc30 metalc ? ? F CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1447 A HOH 2047 1_555 ? ? ? ? ? ? ? 2.610 ? ? 
metalc31 metalc ? ? F CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1447 A HOH 2050 1_555 ? ? ? ? ? ? ? 2.699 ? ? 
metalc32 metalc ? ? G NFH .   ON  ? ? ? 1_555 H ZN  . ZN ? ? A NFH 1448 A ZN  1450 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc33 metalc ? ? G NFH .   OM  ? ? ? 1_555 H ZN  . ZN ? ? A NFH 1448 A ZN  1450 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc34 metalc ? ? J CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1452 A HOH 2021 1_555 ? ? ? ? ? ? ? 2.877 ? ? 
metalc35 metalc ? ? J CA  .   CA  ? ? ? 1_555 S HOH . O  ? ? A CA  1452 A HOH 2022 1_555 ? ? ? ? ? ? ? 3.037 ? ? 
metalc36 metalc ? ? B ASP 26  OD2 ? ? ? 1_555 M CA  . CA ? ? B ASP 131  B CA  1446 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc37 metalc ? ? B ASP 26  OD1 ? ? ? 1_555 M CA  . CA ? ? B ASP 131  B CA  1446 1_555 ? ? ? ? ? ? ? 3.224 ? ? 
metalc38 metalc ? ? B SER 44  O   ? ? ? 1_555 O CA  . CA ? ? B SER 149  B CA  1448 1_555 ? ? ? ? ? ? ? 3.187 ? ? 
metalc39 metalc ? ? B THR 47  O   ? ? ? 1_555 O CA  . CA ? ? B THR 152  B CA  1448 1_555 ? ? ? ? ? ? ? 3.185 ? ? 
metalc40 metalc ? ? B ASP 60  O   ? ? ? 1_555 L CA  . CA ? ? B ASP 165  B CA  1445 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc41 metalc ? ? B HIS 70  NE2 ? ? ? 1_555 R ZN  . ZN ? ? B HIS 175  B ZN  1452 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc42 metalc ? ? B ASP 72  OD2 ? ? ? 1_555 R ZN  . ZN ? ? B ASP 177  B ZN  1452 1_555 ? ? ? ? ? ? ? 2.184 ? ? 
metalc43 metalc ? ? B ASP 77  OD1 ? ? ? 1_555 K CA  . CA ? ? B ASP 182  B CA  1444 1_555 ? ? ? ? ? ? ? 2.605 ? ? 
metalc44 metalc ? ? B GLY 78  O   ? ? ? 1_555 K CA  . CA ? ? B GLY 183  B CA  1444 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc45 metalc ? ? B ASP 80  O   ? ? ? 1_555 K CA  . CA ? ? B ASP 185  B CA  1444 1_555 ? ? ? ? ? ? ? 2.714 ? ? 
metalc46 metalc ? ? B LEU 82  O   ? ? ? 1_555 K CA  . CA ? ? B LEU 187  B CA  1444 1_555 ? ? ? ? ? ? ? 2.376 ? ? 
metalc47 metalc ? ? B HIS 85  NE2 ? ? ? 1_555 R ZN  . ZN ? ? B HIS 190  B ZN  1452 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc48 metalc ? ? B GLY 92  O   ? ? ? 1_555 L CA  . CA ? ? B GLY 197  B CA  1445 1_555 ? ? ? ? ? ? ? 2.506 ? ? 
metalc49 metalc ? ? B GLN 94  O   ? ? ? 1_555 L CA  . CA ? ? B GLN 199  B CA  1445 1_555 ? ? ? ? ? ? ? 2.469 ? ? 
metalc50 metalc ? ? B ASP 96  OD1 ? ? ? 1_555 L CA  . CA ? ? B ASP 201  B CA  1445 1_555 ? ? ? ? ? ? ? 2.606 ? ? 
metalc51 metalc ? ? B HIS 98  ND1 ? ? ? 1_555 R ZN  . ZN ? ? B HIS 203  B ZN  1452 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc52 metalc ? ? B ASP 100 OD2 ? ? ? 1_555 K CA  . CA ? ? B ASP 205  B CA  1444 1_555 ? ? ? ? ? ? ? 2.591 ? ? 
metalc53 metalc ? ? B ASP 101 OD1 ? ? ? 1_555 M CA  . CA ? ? B ASP 206  B CA  1446 1_555 ? ? ? ? ? ? ? 2.895 ? ? 
metalc54 metalc ? ? B ASP 101 O   ? ? ? 1_555 M CA  . CA ? ? B ASP 206  B CA  1446 1_555 ? ? ? ? ? ? ? 2.690 ? ? 
metalc55 metalc ? ? B GLU 103 OE2 ? ? ? 1_555 K CA  . CA ? ? B GLU 208  B CA  1444 1_555 ? ? ? ? ? ? ? 2.733 ? ? 
metalc56 metalc ? ? B GLU 103 O   ? ? ? 1_555 M CA  . CA ? ? B GLU 208  B CA  1446 1_555 ? ? ? ? ? ? ? 2.527 ? ? 
metalc57 metalc ? ? B SER 106 OG  ? ? ? 1_555 N CA  . CA ? ? B SER 211  B CA  1447 1_555 ? ? ? ? ? ? ? 3.119 ? ? 
metalc58 metalc ? ? B LEU 107 O   ? ? ? 1_555 N CA  . CA ? ? B LEU 212  B CA  1447 1_555 ? ? ? ? ? ? ? 2.640 ? ? 
metalc59 metalc ? ? B GLY 108 O   ? ? ? 1_555 N CA  . CA ? ? B GLY 213  B CA  1447 1_555 ? ? ? ? ? ? ? 3.012 ? ? 
metalc60 metalc ? ? B LYS 109 O   ? ? ? 1_555 N CA  . CA ? ? B LYS 214  B CA  1447 1_555 ? ? ? ? ? ? ? 2.893 ? ? 
metalc61 metalc ? ? B HIS 121 NE2 ? ? ? 1_555 Q ZN  . ZN ? ? B HIS 401  B ZN  1451 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc62 metalc ? ? B HIS 125 NE2 ? ? ? 1_555 Q ZN  . ZN ? ? B HIS 405  B ZN  1451 1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc63 metalc ? ? B HIS 131 NE2 ? ? ? 1_555 Q ZN  . ZN ? ? B HIS 411  B ZN  1451 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc64 metalc ? ? L CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1445 B HOH 2030 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc65 metalc ? ? L CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1445 B HOH 2041 1_555 ? ? ? ? ? ? ? 2.751 ? ? 
metalc66 metalc ? ? M CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1446 B HOH 2011 1_555 ? ? ? ? ? ? ? 2.784 ? ? 
metalc67 metalc ? ? N CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1447 B HOH 2052 1_555 ? ? ? ? ? ? ? 2.649 ? ? 
metalc68 metalc ? ? O CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1448 B HOH 2021 1_555 ? ? ? ? ? ? ? 2.981 ? ? 
metalc69 metalc ? ? O CA  .   CA  ? ? ? 1_555 T HOH . O  ? ? B CA  1448 B HOH 2022 1_555 ? ? ? ? ? ? ? 2.890 ? ? 
metalc70 metalc ? ? P NFH .   ON  ? ? ? 1_555 Q ZN  . ZN ? ? B NFH 1449 B ZN  1451 1_555 ? ? ? ? ? ? ? 1.979 ? ? 
metalc71 metalc ? ? P NFH .   OM  ? ? ? 1_555 Q ZN  . ZN ? ? B NFH 1449 B ZN  1451 1_555 ? ? ? ? ? ? ? 2.543 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 2 ? 
BA ? 5 ? 
BB ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? parallel      
AA 2 3 ? parallel      
AA 3 4 ? parallel      
AA 4 5 ? anti-parallel 
AB 1 2 ? parallel      
BA 1 2 ? parallel      
BA 2 3 ? parallel      
BA 3 4 ? parallel      
BA 4 5 ? anti-parallel 
BB 1 2 ? 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 
AA 1 THR A 50  ? ARG A 53  ? THR A 155 ARG A 158 
AA 2 ASN A 15  ? ILE A 20  ? ASN A 120 ILE A 125 
AA 3 ILE A 61  ? GLY A 66  ? ILE A 166 GLY A 171 
AA 4 ALA A 97  ? ASP A 100 ? ALA A 202 ASP A 205 
AA 5 ALA A 84  ? ALA A 86  ? ALA A 189 ALA A 191 
AB 1 TRP A 105 ? SER A 106 ? TRP A 210 SER A 211 
AB 2 TYR A 113 ? SER A 114 ? TYR A 393 SER A 394 
BA 1 THR B 50  ? ARG B 53  ? THR B 155 ARG B 158 
BA 2 ASN B 15  ? ILE B 20  ? ASN B 120 ILE B 125 
BA 3 ILE B 61  ? GLY B 66  ? ILE B 166 GLY B 171 
BA 4 ALA B 97  ? ASP B 100 ? ALA B 202 ASP B 205 
BA 5 ALA B 84  ? ALA B 86  ? ALA B 189 ALA B 191 
BB 1 TRP B 105 ? SER B 106 ? TRP B 210 SER B 211 
BB 2 TYR B 113 ? SER B 114 ? TYR B 393 SER B 394 
# 
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 
AA 1 2 N THR A 52  ? N THR A 157 O ILE A 16  ? O ILE A 121 
AA 2 3 N TRP A 19  ? N TRP A 124 O ILE A 61  ? O ILE A 166 
AA 3 4 N GLN A 64  ? N GLN A 169 O ALA A 97  ? O ALA A 202 
AA 4 5 N HIS A 98  ? N HIS A 203 O HIS A 85  ? O HIS A 190 
AB 1 2 N SER A 106 ? N SER A 211 O TYR A 113 ? O TYR A 393 
BA 1 2 N THR B 52  ? N THR B 157 O ILE B 16  ? O ILE B 121 
BA 2 3 N TRP B 19  ? N TRP B 124 O ILE B 61  ? O ILE B 166 
BA 3 4 N GLN B 64  ? N GLN B 169 O ALA B 97  ? O ALA B 202 
BA 4 5 N HIS B 98  ? N HIS B 203 O HIS B 85  ? O HIS B 190 
BB 1 2 N SER B 106 ? N SER B 211 O TYR B 113 ? O TYR B 393 
# 
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 A CA  1444 ? 6  'BINDING SITE FOR RESIDUE CA A 1444'  
AC2 Software A CA  1445 ? 6  'BINDING SITE FOR RESIDUE CA A 1445'  
AC3 Software A CA  1446 ? 3  'BINDING SITE FOR RESIDUE CA A 1446'  
AC4 Software A CA  1447 ? 7  'BINDING SITE FOR RESIDUE CA A 1447'  
AC5 Software A NFH 1448 ? 15 'BINDING SITE FOR RESIDUE NFH A 1448' 
AC6 Software A ZN  1450 ? 4  'BINDING SITE FOR RESIDUE ZN A 1450'  
AC7 Software A ZN  1451 ? 4  'BINDING SITE FOR RESIDUE ZN A 1451'  
AC8 Software A CA  1452 ? 3  'BINDING SITE FOR RESIDUE CA A 1452'  
AC9 Software B CA  1444 ? 6  'BINDING SITE FOR RESIDUE CA B 1444'  
BC1 Software B CA  1445 ? 6  'BINDING SITE FOR RESIDUE CA B 1445'  
BC2 Software B CA  1446 ? 4  'BINDING SITE FOR RESIDUE CA B 1446'  
BC3 Software B CA  1447 ? 6  'BINDING SITE FOR RESIDUE CA B 1447'  
BC4 Software B CA  1448 ? 4  'BINDING SITE FOR RESIDUE CA B 1448'  
BC5 Software B NFH 1449 ? 14 'BINDING SITE FOR RESIDUE NFH B 1449' 
BC6 Software B ZN  1451 ? 4  'BINDING SITE FOR RESIDUE ZN B 1451'  
BC7 Software B ZN  1452 ? 4  'BINDING SITE FOR RESIDUE ZN B 1452'  
# 
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 6  ASP A 77  ? ASP A 182  . ? 1_555 ? 
2  AC1 6  GLY A 78  ? GLY A 183  . ? 1_555 ? 
3  AC1 6  ASP A 80  ? ASP A 185  . ? 1_555 ? 
4  AC1 6  LEU A 82  ? LEU A 187  . ? 1_555 ? 
5  AC1 6  ASP A 100 ? ASP A 205  . ? 1_555 ? 
6  AC1 6  GLU A 103 ? GLU A 208  . ? 1_555 ? 
7  AC2 6  ASP A 60  ? ASP A 165  . ? 1_555 ? 
8  AC2 6  GLY A 92  ? GLY A 197  . ? 1_555 ? 
9  AC2 6  GLN A 94  ? GLN A 199  . ? 1_555 ? 
10 AC2 6  ASP A 96  ? ASP A 201  . ? 1_555 ? 
11 AC2 6  HOH S .   ? HOH A 2028 . ? 1_555 ? 
12 AC2 6  HOH S .   ? HOH A 2039 . ? 1_555 ? 
13 AC3 3  ASP A 26  ? ASP A 131  . ? 1_555 ? 
14 AC3 3  ASP A 101 ? ASP A 206  . ? 1_555 ? 
15 AC3 3  GLU A 103 ? GLU A 208  . ? 1_555 ? 
16 AC4 7  SER A 106 ? SER A 211  . ? 1_555 ? 
17 AC4 7  LEU A 107 ? LEU A 212  . ? 1_555 ? 
18 AC4 7  GLY A 108 ? GLY A 213  . ? 1_555 ? 
19 AC4 7  LYS A 109 ? LYS A 214  . ? 1_555 ? 
20 AC4 7  GLY A 110 ? GLY A 215  . ? 1_555 ? 
21 AC4 7  HOH S .   ? HOH A 2047 . ? 1_555 ? 
22 AC4 7  HOH S .   ? HOH A 2050 . ? 1_555 ? 
23 AC5 15 GLY A 81  ? GLY A 186  . ? 1_555 ? 
24 AC5 15 LEU A 82  ? LEU A 187  . ? 1_555 ? 
25 AC5 15 LEU A 83  ? LEU A 188  . ? 1_555 ? 
26 AC5 15 ALA A 84  ? ALA A 189  . ? 1_555 ? 
27 AC5 15 TYR A 113 ? TYR A 393  . ? 1_555 ? 
28 AC5 15 HIS A 121 ? HIS A 401  . ? 1_555 ? 
29 AC5 15 GLU A 122 ? GLU A 402  . ? 1_555 ? 
30 AC5 15 HIS A 125 ? HIS A 405  . ? 1_555 ? 
31 AC5 15 HIS A 131 ? HIS A 411  . ? 1_555 ? 
32 AC5 15 PRO A 141 ? PRO A 421  . ? 1_555 ? 
33 AC5 15 MET A 142 ? MET A 422  . ? 1_555 ? 
34 AC5 15 TYR A 143 ? TYR A 423  . ? 1_555 ? 
35 AC5 15 ZN  H .   ? ZN  A 1450 . ? 1_555 ? 
36 AC5 15 HOH S .   ? HOH A 2038 . ? 1_555 ? 
37 AC5 15 HOH S .   ? HOH A 2056 . ? 1_555 ? 
38 AC6 4  HIS A 121 ? HIS A 401  . ? 1_555 ? 
39 AC6 4  HIS A 125 ? HIS A 405  . ? 1_555 ? 
40 AC6 4  HIS A 131 ? HIS A 411  . ? 1_555 ? 
41 AC6 4  NFH G .   ? NFH A 1448 . ? 1_555 ? 
42 AC7 4  HIS A 70  ? HIS A 175  . ? 1_555 ? 
43 AC7 4  ASP A 72  ? ASP A 177  . ? 1_555 ? 
44 AC7 4  HIS A 85  ? HIS A 190  . ? 1_555 ? 
45 AC7 4  HIS A 98  ? HIS A 203  . ? 1_555 ? 
46 AC8 3  SER A 44  ? SER A 149  . ? 1_555 ? 
47 AC8 3  HOH S .   ? HOH A 2021 . ? 1_555 ? 
48 AC8 3  HOH S .   ? HOH A 2022 . ? 1_555 ? 
49 AC9 6  ASP B 77  ? ASP B 182  . ? 1_555 ? 
50 AC9 6  GLY B 78  ? GLY B 183  . ? 1_555 ? 
51 AC9 6  ASP B 80  ? ASP B 185  . ? 1_555 ? 
52 AC9 6  LEU B 82  ? LEU B 187  . ? 1_555 ? 
53 AC9 6  ASP B 100 ? ASP B 205  . ? 1_555 ? 
54 AC9 6  GLU B 103 ? GLU B 208  . ? 1_555 ? 
55 BC1 6  ASP B 60  ? ASP B 165  . ? 1_555 ? 
56 BC1 6  GLY B 92  ? GLY B 197  . ? 1_555 ? 
57 BC1 6  GLN B 94  ? GLN B 199  . ? 1_555 ? 
58 BC1 6  ASP B 96  ? ASP B 201  . ? 1_555 ? 
59 BC1 6  HOH T .   ? HOH B 2030 . ? 1_555 ? 
60 BC1 6  HOH T .   ? HOH B 2041 . ? 1_555 ? 
61 BC2 4  ASP B 26  ? ASP B 131  . ? 1_555 ? 
62 BC2 4  ASP B 101 ? ASP B 206  . ? 1_555 ? 
63 BC2 4  GLU B 103 ? GLU B 208  . ? 1_555 ? 
64 BC2 4  HOH T .   ? HOH B 2011 . ? 1_555 ? 
65 BC3 6  SER B 106 ? SER B 211  . ? 1_555 ? 
66 BC3 6  LEU B 107 ? LEU B 212  . ? 1_555 ? 
67 BC3 6  GLY B 108 ? GLY B 213  . ? 1_555 ? 
68 BC3 6  LYS B 109 ? LYS B 214  . ? 1_555 ? 
69 BC3 6  GLN B 111 ? GLN B 391  . ? 1_555 ? 
70 BC3 6  HOH T .   ? HOH B 2052 . ? 1_555 ? 
71 BC4 4  SER B 44  ? SER B 149  . ? 1_555 ? 
72 BC4 4  THR B 47  ? THR B 152  . ? 1_555 ? 
73 BC4 4  HOH T .   ? HOH B 2021 . ? 1_555 ? 
74 BC4 4  HOH T .   ? HOH B 2022 . ? 1_555 ? 
75 BC5 14 GLY B 81  ? GLY B 186  . ? 1_555 ? 
76 BC5 14 LEU B 82  ? LEU B 187  . ? 1_555 ? 
77 BC5 14 LEU B 83  ? LEU B 188  . ? 1_555 ? 
78 BC5 14 ALA B 84  ? ALA B 189  . ? 1_555 ? 
79 BC5 14 TYR B 113 ? TYR B 393  . ? 1_555 ? 
80 BC5 14 HIS B 121 ? HIS B 401  . ? 1_555 ? 
81 BC5 14 GLU B 122 ? GLU B 402  . ? 1_555 ? 
82 BC5 14 HIS B 125 ? HIS B 405  . ? 1_555 ? 
83 BC5 14 HIS B 131 ? HIS B 411  . ? 1_555 ? 
84 BC5 14 TYR B 140 ? TYR B 420  . ? 1_555 ? 
85 BC5 14 PRO B 141 ? PRO B 421  . ? 1_555 ? 
86 BC5 14 MET B 142 ? MET B 422  . ? 1_555 ? 
87 BC5 14 TYR B 143 ? TYR B 423  . ? 1_555 ? 
88 BC5 14 ZN  Q .   ? ZN  B 1451 . ? 1_555 ? 
89 BC6 4  HIS B 121 ? HIS B 401  . ? 1_555 ? 
90 BC6 4  HIS B 125 ? HIS B 405  . ? 1_555 ? 
91 BC6 4  HIS B 131 ? HIS B 411  . ? 1_555 ? 
92 BC6 4  NFH P .   ? NFH B 1449 . ? 1_555 ? 
93 BC7 4  HIS B 70  ? HIS B 175  . ? 1_555 ? 
94 BC7 4  ASP B 72  ? ASP B 177  . ? 1_555 ? 
95 BC7 4  HIS B 85  ? HIS B 190  . ? 1_555 ? 
96 BC7 4  HIS B 98  ? HIS B 203  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1GKC 
_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                    1GKC 
_atom_sites.fract_transf_matrix[1][1]   0.017856 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017856 
_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]   0.003807 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
S  
ZN 
# 
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   . PHE A 1 5   ? 69.510 28.084 105.133 1.00 76.75 ? 110  PHE A N   1 
ATOM   2    C  CA  . PHE A 1 5   ? 68.217 27.455 105.522 1.00 76.45 ? 110  PHE A CA  1 
ATOM   3    C  C   . PHE A 1 5   ? 67.022 28.261 105.029 1.00 76.18 ? 110  PHE A C   1 
ATOM   4    O  O   . PHE A 1 5   ? 65.965 28.280 105.664 1.00 76.86 ? 110  PHE A O   1 
ATOM   5    C  CB  . PHE A 1 5   ? 68.144 27.293 107.042 1.00 76.67 ? 110  PHE A CB  1 
ATOM   6    C  CG  . PHE A 1 5   ? 69.059 26.231 107.577 1.00 76.83 ? 110  PHE A CG  1 
ATOM   7    C  CD1 . PHE A 1 5   ? 70.433 26.309 107.372 1.00 76.63 ? 110  PHE A CD1 1 
ATOM   8    C  CD2 . PHE A 1 5   ? 68.547 25.145 108.276 1.00 76.62 ? 110  PHE A CD2 1 
ATOM   9    C  CE1 . PHE A 1 5   ? 71.282 25.322 107.853 1.00 75.40 ? 110  PHE A CE1 1 
ATOM   10   C  CE2 . PHE A 1 5   ? 69.390 24.152 108.763 1.00 76.11 ? 110  PHE A CE2 1 
ATOM   11   C  CZ  . PHE A 1 5   ? 70.760 24.241 108.550 1.00 75.74 ? 110  PHE A CZ  1 
ATOM   12   N  N   . GLU A 1 6   ? 67.204 28.928 103.893 1.00 74.63 ? 111  GLU A N   1 
ATOM   13   C  CA  . GLU A 1 6   ? 66.148 29.724 103.279 1.00 73.01 ? 111  GLU A CA  1 
ATOM   14   C  C   . GLU A 1 6   ? 66.025 29.282 101.826 1.00 69.95 ? 111  GLU A C   1 
ATOM   15   O  O   . GLU A 1 6   ? 67.025 29.180 101.111 1.00 70.43 ? 111  GLU A O   1 
ATOM   16   C  CB  . GLU A 1 6   ? 66.490 31.215 103.335 1.00 75.82 ? 111  GLU A CB  1 
ATOM   17   C  CG  . GLU A 1 6   ? 66.819 31.745 104.726 1.00 80.41 ? 111  GLU A CG  1 
ATOM   18   C  CD  . GLU A 1 6   ? 65.689 31.554 105.725 1.00 83.58 ? 111  GLU A CD  1 
ATOM   19   O  OE1 . GLU A 1 6   ? 64.561 32.022 105.452 1.00 85.28 ? 111  GLU A OE1 1 
ATOM   20   O  OE2 . GLU A 1 6   ? 65.934 30.941 106.789 1.00 84.02 ? 111  GLU A OE2 1 
ATOM   21   N  N   . GLY A 1 7   ? 64.801 29.009 101.394 1.00 66.03 ? 112  GLY A N   1 
ATOM   22   C  CA  . GLY A 1 7   ? 64.587 28.577 100.027 1.00 60.34 ? 112  GLY A CA  1 
ATOM   23   C  C   . GLY A 1 7   ? 63.299 29.143 99.479  1.00 56.89 ? 112  GLY A C   1 
ATOM   24   O  O   . GLY A 1 7   ? 62.515 29.744 100.213 1.00 57.97 ? 112  GLY A O   1 
ATOM   25   N  N   . ASP A 1 8   ? 63.077 28.955 98.185  1.00 53.94 ? 113  ASP A N   1 
ATOM   26   C  CA  . ASP A 1 8   ? 61.866 29.459 97.553  1.00 50.40 ? 113  ASP A CA  1 
ATOM   27   C  C   . ASP A 1 8   ? 61.098 28.345 96.867  1.00 46.20 ? 113  ASP A C   1 
ATOM   28   O  O   . ASP A 1 8   ? 60.589 28.519 95.763  1.00 46.06 ? 113  ASP A O   1 
ATOM   29   C  CB  . ASP A 1 8   ? 62.209 30.556 96.543  1.00 52.58 ? 113  ASP A CB  1 
ATOM   30   C  CG  . ASP A 1 8   ? 62.790 31.792 97.202  1.00 53.44 ? 113  ASP A CG  1 
ATOM   31   O  OD1 . ASP A 1 8   ? 62.092 32.405 98.039  1.00 53.76 ? 113  ASP A OD1 1 
ATOM   32   O  OD2 . ASP A 1 8   ? 63.944 32.146 96.885  1.00 53.72 ? 113  ASP A OD2 1 
ATOM   33   N  N   . LEU A 1 9   ? 61.024 27.198 97.535  1.00 40.51 ? 114  LEU A N   1 
ATOM   34   C  CA  . LEU A 1 9   ? 60.309 26.043 97.018  1.00 35.29 ? 114  LEU A CA  1 
ATOM   35   C  C   . LEU A 1 9   ? 59.229 25.624 98.003  1.00 33.60 ? 114  LEU A C   1 
ATOM   36   O  O   . LEU A 1 9   ? 59.363 25.842 99.205  1.00 33.68 ? 114  LEU A O   1 
ATOM   37   C  CB  . LEU A 1 9   ? 61.265 24.870 96.812  1.00 35.18 ? 114  LEU A CB  1 
ATOM   38   C  CG  . LEU A 1 9   ? 62.424 25.022 95.829  1.00 35.74 ? 114  LEU A CG  1 
ATOM   39   C  CD1 . LEU A 1 9   ? 63.155 23.689 95.726  1.00 34.64 ? 114  LEU A CD1 1 
ATOM   40   C  CD2 . LEU A 1 9   ? 61.906 25.455 94.463  1.00 31.83 ? 114  LEU A CD2 1 
ATOM   41   N  N   . LYS A 1 10  ? 58.151 25.040 97.489  1.00 30.09 ? 115  LYS A N   1 
ATOM   42   C  CA  . LYS A 1 10  ? 57.066 24.556 98.331  1.00 28.79 ? 115  LYS A CA  1 
ATOM   43   C  C   . LYS A 1 10  ? 56.854 23.099 97.946  1.00 27.74 ? 115  LYS A C   1 
ATOM   44   O  O   . LYS A 1 10  ? 57.490 22.610 97.017  1.00 26.52 ? 115  LYS A O   1 
ATOM   45   C  CB  . LYS A 1 10  ? 55.782 25.350 98.091  1.00 27.23 ? 115  LYS A CB  1 
ATOM   46   C  CG  . LYS A 1 10  ? 55.136 25.113 96.739  1.00 30.27 ? 115  LYS A CG  1 
ATOM   47   C  CD  . LYS A 1 10  ? 53.726 25.671 96.711  1.00 31.99 ? 115  LYS A CD  1 
ATOM   48   C  CE  . LYS A 1 10  ? 53.015 25.309 95.420  1.00 33.32 ? 115  LYS A CE  1 
ATOM   49   N  NZ  . LYS A 1 10  ? 51.602 25.772 95.434  1.00 31.74 ? 115  LYS A NZ  1 
ATOM   50   N  N   . TRP A 1 11  ? 55.984 22.398 98.660  1.00 26.86 ? 116  TRP A N   1 
ATOM   51   C  CA  . TRP A 1 11  ? 55.725 21.005 98.327  1.00 26.50 ? 116  TRP A CA  1 
ATOM   52   C  C   . TRP A 1 11  ? 54.723 20.991 97.184  1.00 27.50 ? 116  TRP A C   1 
ATOM   53   O  O   . TRP A 1 11  ? 53.828 21.836 97.125  1.00 25.79 ? 116  TRP A O   1 
ATOM   54   C  CB  . TRP A 1 11  ? 55.139 20.242 99.525  1.00 24.26 ? 116  TRP A CB  1 
ATOM   55   C  CG  . TRP A 1 11  ? 56.071 20.142 100.708 1.00 26.96 ? 116  TRP A CG  1 
ATOM   56   C  CD1 . TRP A 1 11  ? 55.977 20.821 101.894 1.00 23.47 ? 116  TRP A CD1 1 
ATOM   57   C  CD2 . TRP A 1 11  ? 57.243 19.321 100.810 1.00 26.47 ? 116  TRP A CD2 1 
ATOM   58   N  NE1 . TRP A 1 11  ? 57.014 20.472 102.724 1.00 22.33 ? 116  TRP A NE1 1 
ATOM   59   C  CE2 . TRP A 1 11  ? 57.806 19.554 102.087 1.00 25.23 ? 116  TRP A CE2 1 
ATOM   60   C  CE3 . TRP A 1 11  ? 57.873 18.414 99.946  1.00 25.47 ? 116  TRP A CE3 1 
ATOM   61   C  CZ2 . TRP A 1 11  ? 58.972 18.910 102.521 1.00 24.08 ? 116  TRP A CZ2 1 
ATOM   62   C  CZ3 . TRP A 1 11  ? 59.037 17.774 100.378 1.00 24.64 ? 116  TRP A CZ3 1 
ATOM   63   C  CH2 . TRP A 1 11  ? 59.572 18.027 101.654 1.00 25.34 ? 116  TRP A CH2 1 
ATOM   64   N  N   . HIS A 1 12  ? 54.877 20.039 96.271  1.00 27.87 ? 117  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 12  ? 53.950 19.932 95.158  1.00 29.48 ? 117  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 12  ? 52.794 18.982 95.465  1.00 31.31 ? 117  HIS A C   1 
ATOM   67   O  O   . HIS A 1 12  ? 51.849 18.873 94.687  1.00 36.62 ? 117  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 12  ? 54.692 19.528 93.885  1.00 25.71 ? 117  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 12  ? 55.384 20.674 93.214  1.00 27.00 ? 117  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 12  ? 56.184 20.520 92.103  1.00 28.15 ? 117  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 12  ? 55.394 21.998 93.501  1.00 27.93 ? 117  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 12  ? 56.659 21.697 91.736  1.00 25.56 ? 117  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 12  ? 56.195 22.611 92.568  1.00 25.76 ? 117  HIS A NE2 1 
ATOM   74   N  N   . HIS A 1 13  ? 52.868 18.292 96.600  1.00 28.91 ? 118  HIS A N   1 
ATOM   75   C  CA  . HIS A 1 13  ? 51.782 17.412 97.007  1.00 27.75 ? 118  HIS A CA  1 
ATOM   76   C  C   . HIS A 1 13  ? 51.232 17.949 98.322  1.00 28.02 ? 118  HIS A C   1 
ATOM   77   O  O   . HIS A 1 13  ? 51.906 18.717 99.006  1.00 30.48 ? 118  HIS A O   1 
ATOM   78   C  CB  . HIS A 1 13  ? 52.257 15.966 97.160  1.00 26.46 ? 118  HIS A CB  1 
ATOM   79   C  CG  . HIS A 1 13  ? 53.454 15.800 98.041  1.00 28.06 ? 118  HIS A CG  1 
ATOM   80   N  ND1 . HIS A 1 13  ? 54.715 16.213 97.672  1.00 27.31 ? 118  HIS A ND1 1 
ATOM   81   C  CD2 . HIS A 1 13  ? 53.587 15.230 99.262  1.00 26.27 ? 118  HIS A CD2 1 
ATOM   82   C  CE1 . HIS A 1 13  ? 55.575 15.901 98.625  1.00 25.21 ? 118  HIS A CE1 1 
ATOM   83   N  NE2 . HIS A 1 13  ? 54.916 15.304 99.600  1.00 25.44 ? 118  HIS A NE2 1 
ATOM   84   N  N   . HIS A 1 14  ? 50.008 17.566 98.670  1.00 28.21 ? 119  HIS A N   1 
ATOM   85   C  CA  . HIS A 1 14  ? 49.394 18.049 99.900  1.00 28.31 ? 119  HIS A CA  1 
ATOM   86   C  C   . HIS A 1 14  ? 49.318 17.040 101.034 1.00 28.11 ? 119  HIS A C   1 
ATOM   87   O  O   . HIS A 1 14  ? 49.120 17.424 102.184 1.00 28.79 ? 119  HIS A O   1 
ATOM   88   C  CB  . HIS A 1 14  ? 48.001 18.597 99.607  1.00 27.88 ? 119  HIS A CB  1 
ATOM   89   C  CG  . HIS A 1 14  ? 48.015 19.881 98.843  1.00 30.03 ? 119  HIS A CG  1 
ATOM   90   N  ND1 . HIS A 1 14  ? 46.862 20.530 98.452  1.00 32.34 ? 119  HIS A ND1 1 
ATOM   91   C  CD2 . HIS A 1 14  ? 49.045 20.642 98.402  1.00 28.56 ? 119  HIS A CD2 1 
ATOM   92   C  CE1 . HIS A 1 14  ? 47.182 21.636 97.804  1.00 30.91 ? 119  HIS A CE1 1 
ATOM   93   N  NE2 . HIS A 1 14  ? 48.500 21.728 97.760  1.00 30.11 ? 119  HIS A NE2 1 
ATOM   94   N  N   . ASN A 1 15  ? 49.447 15.757 100.715 1.00 28.28 ? 120  ASN A N   1 
ATOM   95   C  CA  . ASN A 1 15  ? 49.418 14.724 101.742 1.00 30.67 ? 120  ASN A CA  1 
ATOM   96   C  C   . ASN A 1 15  ? 50.873 14.489 102.141 1.00 29.30 ? 120  ASN A C   1 
ATOM   97   O  O   . ASN A 1 15  ? 51.564 13.634 101.585 1.00 29.67 ? 120  ASN A O   1 
ATOM   98   C  CB  . ASN A 1 15  ? 48.753 13.442 101.206 1.00 35.59 ? 120  ASN A CB  1 
ATOM   99   C  CG  . ASN A 1 15  ? 49.339 12.970 99.874  1.00 40.97 ? 120  ASN A CG  1 
ATOM   100  O  OD1 . ASN A 1 15  ? 49.628 13.776 98.982  1.00 42.91 ? 120  ASN A OD1 1 
ATOM   101  N  ND2 . ASN A 1 15  ? 49.494 11.652 99.728  1.00 42.68 ? 120  ASN A ND2 1 
ATOM   102  N  N   . ILE A 1 16  ? 51.330 15.287 103.103 1.00 26.98 ? 121  ILE A N   1 
ATOM   103  C  CA  . ILE A 1 16  ? 52.710 15.233 103.577 1.00 26.04 ? 121  ILE A CA  1 
ATOM   104  C  C   . ILE A 1 16  ? 52.945 14.179 104.650 1.00 23.95 ? 121  ILE A C   1 
ATOM   105  O  O   . ILE A 1 16  ? 52.081 13.928 105.484 1.00 24.37 ? 121  ILE A O   1 
ATOM   106  C  CB  . ILE A 1 16  ? 53.138 16.617 104.109 1.00 26.73 ? 121  ILE A CB  1 
ATOM   107  C  CG1 . ILE A 1 16  ? 52.997 17.650 102.987 1.00 29.00 ? 121  ILE A CG1 1 
ATOM   108  C  CG2 . ILE A 1 16  ? 54.574 16.568 104.626 1.00 26.58 ? 121  ILE A CG2 1 
ATOM   109  C  CD1 . ILE A 1 16  ? 53.451 19.037 103.357 1.00 32.81 ? 121  ILE A CD1 1 
ATOM   110  N  N   . THR A 1 17  ? 54.119 13.560 104.621 1.00 20.08 ? 122  THR A N   1 
ATOM   111  C  CA  . THR A 1 17  ? 54.441 12.534 105.598 1.00 21.17 ? 122  THR A CA  1 
ATOM   112  C  C   . THR A 1 17  ? 55.624 12.925 106.481 1.00 20.68 ? 122  THR A C   1 
ATOM   113  O  O   . THR A 1 17  ? 56.502 13.706 106.081 1.00 18.28 ? 122  THR A O   1 
ATOM   114  C  CB  . THR A 1 17  ? 54.763 11.172 104.914 1.00 22.42 ? 122  THR A CB  1 
ATOM   115  O  OG1 . THR A 1 17  ? 55.948 11.294 104.115 1.00 20.53 ? 122  THR A OG1 1 
ATOM   116  C  CG2 . THR A 1 17  ? 53.592 10.722 104.042 1.00 21.00 ? 122  THR A CG2 1 
ATOM   117  N  N   . TYR A 1 18  ? 55.640 12.382 107.693 1.00 18.69 ? 123  TYR A N   1 
ATOM   118  C  CA  . TYR A 1 18  ? 56.728 12.671 108.612 1.00 17.02 ? 123  TYR A CA  1 
ATOM   119  C  C   . TYR A 1 18  ? 57.109 11.446 109.419 1.00 15.63 ? 123  TYR A C   1 
ATOM   120  O  O   . TYR A 1 18  ? 56.277 10.594 109.735 1.00 14.88 ? 123  TYR A O   1 
ATOM   121  C  CB  . TYR A 1 18  ? 56.374 13.828 109.561 1.00 12.64 ? 123  TYR A CB  1 
ATOM   122  C  CG  . TYR A 1 18  ? 55.291 13.533 110.579 1.00 14.99 ? 123  TYR A CG  1 
ATOM   123  C  CD1 . TYR A 1 18  ? 53.949 13.737 110.277 1.00 15.83 ? 123  TYR A CD1 1 
ATOM   124  C  CD2 . TYR A 1 18  ? 55.613 13.088 111.867 1.00 15.15 ? 123  TYR A CD2 1 
ATOM   125  C  CE1 . TYR A 1 18  ? 52.953 13.517 111.228 1.00 14.44 ? 123  TYR A CE1 1 
ATOM   126  C  CE2 . TYR A 1 18  ? 54.623 12.866 112.821 1.00 13.15 ? 123  TYR A CE2 1 
ATOM   127  C  CZ  . TYR A 1 18  ? 53.296 13.087 112.495 1.00 14.54 ? 123  TYR A CZ  1 
ATOM   128  O  OH  . TYR A 1 18  ? 52.305 12.912 113.439 1.00 17.15 ? 123  TYR A OH  1 
ATOM   129  N  N   . TRP A 1 19  ? 58.387 11.380 109.745 1.00 14.30 ? 124  TRP A N   1 
ATOM   130  C  CA  . TRP A 1 19  ? 58.933 10.288 110.504 1.00 15.16 ? 124  TRP A CA  1 
ATOM   131  C  C   . TRP A 1 19  ? 59.679 10.821 111.720 1.00 15.01 ? 124  TRP A C   1 
ATOM   132  O  O   . TRP A 1 19  ? 60.575 11.645 111.590 1.00 15.43 ? 124  TRP A O   1 
ATOM   133  C  CB  . TRP A 1 19  ? 59.876 9.486  109.603 1.00 17.22 ? 124  TRP A CB  1 
ATOM   134  C  CG  . TRP A 1 19  ? 60.649 8.390  110.274 1.00 14.19 ? 124  TRP A CG  1 
ATOM   135  C  CD1 . TRP A 1 19  ? 60.186 7.506  111.204 1.00 15.79 ? 124  TRP A CD1 1 
ATOM   136  C  CD2 . TRP A 1 19  ? 62.005 8.019  110.004 1.00 17.22 ? 124  TRP A CD2 1 
ATOM   137  N  NE1 . TRP A 1 19  ? 61.172 6.599  111.530 1.00 17.60 ? 124  TRP A NE1 1 
ATOM   138  C  CE2 . TRP A 1 19  ? 62.299 6.892  110.807 1.00 18.18 ? 124  TRP A CE2 1 
ATOM   139  C  CE3 . TRP A 1 19  ? 63.002 8.525  109.157 1.00 17.93 ? 124  TRP A CE3 1 
ATOM   140  C  CZ2 . TRP A 1 19  ? 63.548 6.262  110.788 1.00 17.69 ? 124  TRP A CZ2 1 
ATOM   141  C  CZ3 . TRP A 1 19  ? 64.244 7.899  109.139 1.00 22.22 ? 124  TRP A CZ3 1 
ATOM   142  C  CH2 . TRP A 1 19  ? 64.505 6.776  109.951 1.00 19.94 ? 124  TRP A CH2 1 
ATOM   143  N  N   . ILE A 1 20  ? 59.283 10.365 112.903 1.00 13.81 ? 125  ILE A N   1 
ATOM   144  C  CA  . ILE A 1 20  ? 59.960 10.754 114.127 1.00 14.20 ? 125  ILE A CA  1 
ATOM   145  C  C   . ILE A 1 20  ? 61.038 9.685  114.249 1.00 14.73 ? 125  ILE A C   1 
ATOM   146  O  O   . ILE A 1 20  ? 60.763 8.564  114.660 1.00 17.21 ? 125  ILE A O   1 
ATOM   147  C  CB  . ILE A 1 20  ? 59.009 10.697 115.341 1.00 14.44 ? 125  ILE A CB  1 
ATOM   148  C  CG1 . ILE A 1 20  ? 57.833 11.649 115.110 1.00 14.53 ? 125  ILE A CG1 1 
ATOM   149  C  CG2 . ILE A 1 20  ? 59.758 11.087 116.609 1.00 10.86 ? 125  ILE A CG2 1 
ATOM   150  C  CD1 . ILE A 1 20  ? 56.721 11.500 116.106 1.00 16.01 ? 125  ILE A CD1 1 
ATOM   151  N  N   . GLN A 1 21  ? 62.259 10.036 113.863 1.00 15.17 ? 126  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 21  ? 63.374 9.102  113.877 1.00 17.19 ? 126  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 21  ? 63.858 8.702  115.270 1.00 18.20 ? 126  GLN A C   1 
ATOM   154  O  O   . GLN A 1 21  ? 64.062 7.519  115.536 1.00 18.29 ? 126  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 21  ? 64.540 9.679  113.065 1.00 15.71 ? 126  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 21  ? 65.810 8.849  113.134 1.00 19.08 ? 126  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 21  ? 67.006 9.537  112.492 1.00 21.76 ? 126  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 21  ? 68.141 9.434  112.978 1.00 21.48 ? 126  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 21  ? 66.762 10.235 111.395 1.00 21.97 ? 126  GLN A NE2 1 
ATOM   160  N  N   . ASN A 1 22  ? 64.066 9.681  116.145 1.00 19.88 ? 127  ASN A N   1 
ATOM   161  C  CA  . ASN A 1 22  ? 64.515 9.397  117.504 1.00 18.22 ? 127  ASN A CA  1 
ATOM   162  C  C   . ASN A 1 22  ? 63.900 10.386 118.483 1.00 19.18 ? 127  ASN A C   1 
ATOM   163  O  O   . ASN A 1 22  ? 63.238 11.341 118.068 1.00 18.72 ? 127  ASN A O   1 
ATOM   164  C  CB  . ASN A 1 22  ? 66.042 9.423  117.594 1.00 19.01 ? 127  ASN A CB  1 
ATOM   165  C  CG  . ASN A 1 22  ? 66.631 10.770 117.242 1.00 21.39 ? 127  ASN A CG  1 
ATOM   166  O  OD1 . ASN A 1 22  ? 65.957 11.798 117.310 1.00 25.90 ? 127  ASN A OD1 1 
ATOM   167  N  ND2 . ASN A 1 22  ? 67.909 10.774 116.880 1.00 20.17 ? 127  ASN A ND2 1 
ATOM   168  N  N   . TYR A 1 23  ? 64.128 10.163 119.779 1.00 17.90 ? 128  TYR A N   1 
ATOM   169  C  CA  . TYR A 1 23  ? 63.539 11.006 120.822 1.00 15.61 ? 128  TYR A CA  1 
ATOM   170  C  C   . TYR A 1 23  ? 64.501 11.716 121.746 1.00 14.76 ? 128  TYR A C   1 
ATOM   171  O  O   . TYR A 1 23  ? 65.681 11.396 121.808 1.00 15.87 ? 128  TYR A O   1 
ATOM   172  C  CB  . TYR A 1 23  ? 62.592 10.166 121.693 1.00 15.35 ? 128  TYR A CB  1 
ATOM   173  C  CG  . TYR A 1 23  ? 61.389 9.623  120.957 1.00 14.14 ? 128  TYR A CG  1 
ATOM   174  C  CD1 . TYR A 1 23  ? 61.476 8.467  120.178 1.00 12.53 ? 128  TYR A CD1 1 
ATOM   175  C  CD2 . TYR A 1 23  ? 60.172 10.293 121.008 1.00 12.14 ? 128  TYR A CD2 1 
ATOM   176  C  CE1 . TYR A 1 23  ? 60.374 8.000  119.469 1.00 12.28 ? 128  TYR A CE1 1 
ATOM   177  C  CE2 . TYR A 1 23  ? 59.078 9.839  120.306 1.00 14.27 ? 128  TYR A CE2 1 
ATOM   178  C  CZ  . TYR A 1 23  ? 59.182 8.698  119.539 1.00 13.46 ? 128  TYR A CZ  1 
ATOM   179  O  OH  . TYR A 1 23  ? 58.084 8.292  118.837 1.00 12.04 ? 128  TYR A OH  1 
ATOM   180  N  N   . SER A 1 24  ? 63.969 12.693 122.471 1.00 17.19 ? 129  SER A N   1 
ATOM   181  C  CA  . SER A 1 24  ? 64.742 13.430 123.460 1.00 19.66 ? 129  SER A CA  1 
ATOM   182  C  C   . SER A 1 24  ? 64.600 12.640 124.753 1.00 22.10 ? 129  SER A C   1 
ATOM   183  O  O   . SER A 1 24  ? 63.646 11.882 124.920 1.00 21.65 ? 129  SER A O   1 
ATOM   184  C  CB  . SER A 1 24  ? 64.173 14.826 123.675 1.00 17.51 ? 129  SER A CB  1 
ATOM   185  O  OG  . SER A 1 24  ? 64.731 15.394 124.844 1.00 16.48 ? 129  SER A OG  1 
ATOM   186  N  N   . GLU A 1 25  ? 65.529 12.821 125.677 1.00 24.54 ? 130  GLU A N   1 
ATOM   187  C  CA  . GLU A 1 25  ? 65.459 12.085 126.925 1.00 28.04 ? 130  GLU A CA  1 
ATOM   188  C  C   . GLU A 1 25  ? 64.587 12.788 127.971 1.00 27.09 ? 130  GLU A C   1 
ATOM   189  O  O   . GLU A 1 25  ? 64.154 12.167 128.939 1.00 29.20 ? 130  GLU A O   1 
ATOM   190  C  CB  . GLU A 1 25  ? 66.884 11.859 127.459 1.00 31.45 ? 130  GLU A CB  1 
ATOM   191  C  CG  . GLU A 1 25  ? 67.799 11.117 126.464 1.00 36.20 ? 130  GLU A CG  1 
ATOM   192  C  CD  . GLU A 1 25  ? 69.207 10.871 126.996 1.00 37.68 ? 130  GLU A CD  1 
ATOM   193  O  OE1 . GLU A 1 25  ? 69.330 10.501 128.182 1.00 43.10 ? 130  GLU A OE1 1 
ATOM   194  O  OE2 . GLU A 1 25  ? 70.189 11.031 126.237 1.00 32.89 ? 130  GLU A OE2 1 
ATOM   195  N  N   . ASP A 1 26  ? 64.301 14.069 127.751 1.00 23.80 ? 131  ASP A N   1 
ATOM   196  C  CA  . ASP A 1 26  ? 63.519 14.870 128.693 1.00 21.55 ? 131  ASP A CA  1 
ATOM   197  C  C   . ASP A 1 26  ? 62.029 14.589 128.821 1.00 22.60 ? 131  ASP A C   1 
ATOM   198  O  O   . ASP A 1 26  ? 61.417 14.946 129.826 1.00 22.01 ? 131  ASP A O   1 
ATOM   199  C  CB  . ASP A 1 26  ? 63.657 16.355 128.367 1.00 20.53 ? 131  ASP A CB  1 
ATOM   200  C  CG  . ASP A 1 26  ? 65.084 16.774 128.149 1.00 21.96 ? 131  ASP A CG  1 
ATOM   201  O  OD1 . ASP A 1 26  ? 65.993 16.132 128.718 1.00 23.79 ? 131  ASP A OD1 1 
ATOM   202  O  OD2 . ASP A 1 26  ? 65.291 17.760 127.417 1.00 19.14 ? 131  ASP A OD2 1 
ATOM   203  N  N   . LEU A 1 27  ? 61.426 13.985 127.808 1.00 21.60 ? 132  LEU A N   1 
ATOM   204  C  CA  . LEU A 1 27  ? 59.996 13.736 127.862 1.00 17.46 ? 132  LEU A CA  1 
ATOM   205  C  C   . LEU A 1 27  ? 59.625 12.322 127.447 1.00 17.91 ? 132  LEU A C   1 
ATOM   206  O  O   . LEU A 1 27  ? 60.350 11.668 126.703 1.00 20.57 ? 132  LEU A O   1 
ATOM   207  C  CB  . LEU A 1 27  ? 59.274 14.744 126.964 1.00 18.77 ? 132  LEU A CB  1 
ATOM   208  C  CG  . LEU A 1 27  ? 59.410 16.228 127.329 1.00 16.38 ? 132  LEU A CG  1 
ATOM   209  C  CD1 . LEU A 1 27  ? 58.952 17.103 126.185 1.00 16.14 ? 132  LEU A CD1 1 
ATOM   210  C  CD2 . LEU A 1 27  ? 58.584 16.513 128.574 1.00 17.73 ? 132  LEU A CD2 1 
ATOM   211  N  N   . PRO A 1 28  ? 58.493 11.818 127.952 1.00 18.54 ? 133  PRO A N   1 
ATOM   212  C  CA  . PRO A 1 28  ? 58.070 10.464 127.588 1.00 18.30 ? 133  PRO A CA  1 
ATOM   213  C  C   . PRO A 1 28  ? 57.739 10.482 126.092 1.00 18.28 ? 133  PRO A C   1 
ATOM   214  O  O   . PRO A 1 28  ? 57.305 11.511 125.566 1.00 15.16 ? 133  PRO A O   1 
ATOM   215  C  CB  . PRO A 1 28  ? 56.828 10.250 128.448 1.00 16.44 ? 133  PRO A CB  1 
ATOM   216  C  CG  . PRO A 1 28  ? 57.029 11.174 129.599 1.00 13.96 ? 133  PRO A CG  1 
ATOM   217  C  CD  . PRO A 1 28  ? 57.590 12.397 128.962 1.00 16.46 ? 133  PRO A CD  1 
ATOM   218  N  N   . ARG A 1 29  ? 57.931 9.358  125.412 1.00 18.49 ? 134  ARG A N   1 
ATOM   219  C  CA  . ARG A 1 29  ? 57.661 9.313  123.978 1.00 20.66 ? 134  ARG A CA  1 
ATOM   220  C  C   . ARG A 1 29  ? 56.217 9.633  123.615 1.00 20.30 ? 134  ARG A C   1 
ATOM   221  O  O   . ARG A 1 29  ? 55.961 10.226 122.575 1.00 19.91 ? 134  ARG A O   1 
ATOM   222  C  CB  . ARG A 1 29  ? 58.084 7.961  123.411 1.00 20.98 ? 134  ARG A CB  1 
ATOM   223  C  CG  . ARG A 1 29  ? 59.563 7.723  123.628 1.00 21.85 ? 134  ARG A CG  1 
ATOM   224  C  CD  . ARG A 1 29  ? 60.064 6.476  122.953 1.00 25.93 ? 134  ARG A CD  1 
ATOM   225  N  NE  . ARG A 1 29  ? 61.506 6.346  123.137 1.00 29.18 ? 134  ARG A NE  1 
ATOM   226  C  CZ  . ARG A 1 29  ? 62.234 5.347  122.652 1.00 32.95 ? 134  ARG A CZ  1 
ATOM   227  N  NH1 . ARG A 1 29  ? 61.649 4.384  121.949 1.00 31.93 ? 134  ARG A NH1 1 
ATOM   228  N  NH2 . ARG A 1 29  ? 63.544 5.314  122.867 1.00 31.66 ? 134  ARG A NH2 1 
ATOM   229  N  N   . ALA A 1 30  ? 55.274 9.256  124.470 1.00 19.00 ? 135  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 30  ? 53.871 9.552  124.201 1.00 20.03 ? 135  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 30  ? 53.642 11.073 124.226 1.00 19.99 ? 135  ALA A C   1 
ATOM   232  O  O   . ALA A 1 30  ? 52.814 11.601 123.489 1.00 19.37 ? 135  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 30  ? 52.980 8.861  125.237 1.00 18.70 ? 135  ALA A CB  1 
ATOM   234  N  N   . VAL A 1 31  ? 54.378 11.774 125.082 1.00 18.65 ? 136  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? 54.245 13.227 125.175 1.00 18.87 ? 136  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? 54.838 13.900 123.930 1.00 17.85 ? 136  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? 54.277 14.870 123.400 1.00 16.07 ? 136  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? 54.950 13.777 126.459 1.00 18.18 ? 136  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? 54.999 15.309 126.443 1.00 16.50 ? 136  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? 54.204 13.303 127.688 1.00 13.02 ? 136  VAL A CG2 1 
ATOM   241  N  N   . ILE A 1 32  ? 55.969 13.374 123.469 1.00 14.93 ? 137  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 32  ? 56.630 13.916 122.295 1.00 13.94 ? 137  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 32  ? 55.781 13.689 121.044 1.00 13.89 ? 137  ILE A C   1 
ATOM   244  O  O   . ILE A 1 32  ? 55.557 14.616 120.270 1.00 13.43 ? 137  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 32  ? 58.035 13.292 122.121 1.00 13.55 ? 137  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 32  ? 58.917 13.705 123.307 1.00 11.84 ? 137  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 32  ? 58.657 13.730 120.789 1.00 10.34 ? 137  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 32  ? 60.329 13.165 123.274 1.00 8.78  ? 137  ILE A CD1 1 
ATOM   249  N  N   . ASP A 1 33  ? 55.298 12.465 120.850 1.00 14.79 ? 138  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 33  ? 54.469 12.168 119.685 1.00 16.05 ? 138  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 33  ? 53.317 13.170 119.602 1.00 16.70 ? 138  ASP A C   1 
ATOM   252  O  O   . ASP A 1 33  ? 53.086 13.784 118.564 1.00 19.57 ? 138  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 33  ? 53.891 10.748 119.764 1.00 14.50 ? 138  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 33  ? 54.946 9.662  119.593 1.00 16.77 ? 138  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 33  ? 56.089 9.967  119.188 1.00 18.40 ? 138  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 33  ? 54.619 8.484  119.853 1.00 20.23 ? 138  ASP A OD2 1 
ATOM   257  N  N   . ASP A 1 34  ? 52.612 13.337 120.716 1.00 16.62 ? 139  ASP A N   1 
ATOM   258  C  CA  . ASP A 1 34  ? 51.460 14.232 120.801 1.00 15.09 ? 139  ASP A CA  1 
ATOM   259  C  C   . ASP A 1 34  ? 51.785 15.693 120.526 1.00 15.75 ? 139  ASP A C   1 
ATOM   260  O  O   . ASP A 1 34  ? 51.004 16.396 119.894 1.00 17.52 ? 139  ASP A O   1 
ATOM   261  C  CB  . ASP A 1 34  ? 50.812 14.099 122.181 1.00 14.62 ? 139  ASP A CB  1 
ATOM   262  C  CG  . ASP A 1 34  ? 49.611 15.003 122.354 1.00 16.52 ? 139  ASP A CG  1 
ATOM   263  O  OD1 . ASP A 1 34  ? 48.584 14.769 121.692 1.00 19.96 ? 139  ASP A OD1 1 
ATOM   264  O  OD2 . ASP A 1 34  ? 49.688 15.953 123.152 1.00 12.35 ? 139  ASP A OD2 1 
ATOM   265  N  N   . ALA A 1 35  ? 52.935 16.152 121.008 1.00 16.49 ? 140  ALA A N   1 
ATOM   266  C  CA  . ALA A 1 35  ? 53.356 17.536 120.805 1.00 14.14 ? 140  ALA A CA  1 
ATOM   267  C  C   . ALA A 1 35  ? 53.576 17.805 119.319 1.00 13.23 ? 140  ALA A C   1 
ATOM   268  O  O   . ALA A 1 35  ? 53.156 18.838 118.797 1.00 13.50 ? 140  ALA A O   1 
ATOM   269  C  CB  . ALA A 1 35  ? 54.648 17.819 121.586 1.00 10.53 ? 140  ALA A CB  1 
ATOM   270  N  N   . PHE A 1 36  ? 54.249 16.877 118.645 1.00 12.36 ? 141  PHE A N   1 
ATOM   271  C  CA  . PHE A 1 36  ? 54.501 17.017 117.216 1.00 15.20 ? 141  PHE A CA  1 
ATOM   272  C  C   . PHE A 1 36  ? 53.183 16.988 116.433 1.00 15.88 ? 141  PHE A C   1 
ATOM   273  O  O   . PHE A 1 36  ? 52.980 17.783 115.516 1.00 18.45 ? 141  PHE A O   1 
ATOM   274  C  CB  . PHE A 1 36  ? 55.431 15.901 116.722 1.00 13.79 ? 141  PHE A CB  1 
ATOM   275  C  CG  . PHE A 1 36  ? 56.867 16.073 117.146 1.00 11.40 ? 141  PHE A CG  1 
ATOM   276  C  CD1 . PHE A 1 36  ? 57.408 17.340 117.318 1.00 12.07 ? 141  PHE A CD1 1 
ATOM   277  C  CD2 . PHE A 1 36  ? 57.685 14.973 117.341 1.00 11.50 ? 141  PHE A CD2 1 
ATOM   278  C  CE1 . PHE A 1 36  ? 58.752 17.507 117.678 1.00 15.23 ? 141  PHE A CE1 1 
ATOM   279  C  CE2 . PHE A 1 36  ? 59.032 15.133 117.701 1.00 10.84 ? 141  PHE A CE2 1 
ATOM   280  C  CZ  . PHE A 1 36  ? 59.564 16.396 117.868 1.00 9.69  ? 141  PHE A CZ  1 
ATOM   281  N  N   . ALA A 1 37  ? 52.289 16.080 116.815 1.00 15.46 ? 142  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 37  ? 50.997 15.940 116.156 1.00 16.51 ? 142  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 37  ? 50.175 17.217 116.281 1.00 17.88 ? 142  ALA A C   1 
ATOM   284  O  O   . ALA A 1 37  ? 49.519 17.642 115.327 1.00 14.95 ? 142  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 37  ? 50.235 14.769 116.751 1.00 16.42 ? 142  ALA A CB  1 
ATOM   286  N  N   . ARG A 1 38  ? 50.207 17.826 117.464 1.00 17.58 ? 143  ARG A N   1 
ATOM   287  C  CA  . ARG A 1 38  ? 49.465 19.055 117.687 1.00 16.25 ? 143  ARG A CA  1 
ATOM   288  C  C   . ARG A 1 38  ? 50.139 20.214 116.952 1.00 16.25 ? 143  ARG A C   1 
ATOM   289  O  O   . ARG A 1 38  ? 49.478 21.162 116.535 1.00 18.41 ? 143  ARG A O   1 
ATOM   290  C  CB  . ARG A 1 38  ? 49.349 19.353 119.191 1.00 13.94 ? 143  ARG A CB  1 
ATOM   291  C  CG  . ARG A 1 38  ? 48.421 18.387 119.930 1.00 13.87 ? 143  ARG A CG  1 
ATOM   292  C  CD  . ARG A 1 38  ? 48.231 18.747 121.404 1.00 13.42 ? 143  ARG A CD  1 
ATOM   293  N  NE  . ARG A 1 38  ? 49.470 18.634 122.168 1.00 12.17 ? 143  ARG A NE  1 
ATOM   294  C  CZ  . ARG A 1 38  ? 50.164 19.671 122.631 1.00 14.73 ? 143  ARG A CZ  1 
ATOM   295  N  NH1 . ARG A 1 38  ? 49.732 20.910 122.416 1.00 12.72 ? 143  ARG A NH1 1 
ATOM   296  N  NH2 . ARG A 1 38  ? 51.305 19.471 123.287 1.00 14.62 ? 143  ARG A NH2 1 
ATOM   297  N  N   . ALA A 1 39  ? 51.453 20.140 116.787 1.00 14.76 ? 144  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 39  ? 52.165 21.199 116.079 1.00 14.81 ? 144  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 39  ? 51.763 21.169 114.592 1.00 15.68 ? 144  ALA A C   1 
ATOM   300  O  O   . ALA A 1 39  ? 51.588 22.214 113.970 1.00 14.69 ? 144  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 39  ? 53.687 21.021 116.247 1.00 9.68  ? 144  ALA A CB  1 
ATOM   302  N  N   . PHE A 1 40  ? 51.605 19.968 114.033 1.00 16.80 ? 145  PHE A N   1 
ATOM   303  C  CA  . PHE A 1 40  ? 51.193 19.815 112.632 1.00 17.22 ? 145  PHE A CA  1 
ATOM   304  C  C   . PHE A 1 40  ? 49.729 20.209 112.438 1.00 19.32 ? 145  PHE A C   1 
ATOM   305  O  O   . PHE A 1 40  ? 49.366 20.790 111.414 1.00 20.25 ? 145  PHE A O   1 
ATOM   306  C  CB  . PHE A 1 40  ? 51.386 18.367 112.154 1.00 14.07 ? 145  PHE A CB  1 
ATOM   307  C  CG  . PHE A 1 40  ? 52.791 18.045 111.744 1.00 9.59  ? 145  PHE A CG  1 
ATOM   308  C  CD1 . PHE A 1 40  ? 53.433 18.797 110.767 1.00 10.98 ? 145  PHE A CD1 1 
ATOM   309  C  CD2 . PHE A 1 40  ? 53.472 16.990 112.326 1.00 9.63  ? 145  PHE A CD2 1 
ATOM   310  C  CE1 . PHE A 1 40  ? 54.739 18.503 110.373 1.00 10.38 ? 145  PHE A CE1 1 
ATOM   311  C  CE2 . PHE A 1 40  ? 54.781 16.687 111.939 1.00 11.84 ? 145  PHE A CE2 1 
ATOM   312  C  CZ  . PHE A 1 40  ? 55.414 17.448 110.958 1.00 9.71  ? 145  PHE A CZ  1 
ATOM   313  N  N   . ALA A 1 41  ? 48.889 19.891 113.420 1.00 18.99 ? 146  ALA A N   1 
ATOM   314  C  CA  . ALA A 1 41  ? 47.471 20.224 113.330 1.00 20.15 ? 146  ALA A CA  1 
ATOM   315  C  C   . ALA A 1 41  ? 47.246 21.727 113.195 1.00 21.23 ? 146  ALA A C   1 
ATOM   316  O  O   . ALA A 1 41  ? 46.272 22.153 112.592 1.00 24.43 ? 146  ALA A O   1 
ATOM   317  C  CB  . ALA A 1 41  ? 46.730 19.695 114.542 1.00 16.75 ? 146  ALA A CB  1 
ATOM   318  N  N   . LEU A 1 42  ? 48.137 22.533 113.764 1.00 23.09 ? 147  LEU A N   1 
ATOM   319  C  CA  . LEU A 1 42  ? 47.996 23.983 113.668 1.00 21.92 ? 147  LEU A CA  1 
ATOM   320  C  C   . LEU A 1 42  ? 47.984 24.422 112.206 1.00 22.21 ? 147  LEU A C   1 
ATOM   321  O  O   . LEU A 1 42  ? 47.188 25.265 111.797 1.00 22.01 ? 147  LEU A O   1 
ATOM   322  C  CB  . LEU A 1 42  ? 49.155 24.698 114.367 1.00 20.86 ? 147  LEU A CB  1 
ATOM   323  C  CG  . LEU A 1 42  ? 49.260 24.748 115.894 1.00 24.92 ? 147  LEU A CG  1 
ATOM   324  C  CD1 . LEU A 1 42  ? 50.469 25.598 116.255 1.00 22.84 ? 147  LEU A CD1 1 
ATOM   325  C  CD2 . LEU A 1 42  ? 48.001 25.342 116.513 1.00 22.59 ? 147  LEU A CD2 1 
ATOM   326  N  N   . TRP A 1 43  ? 48.884 23.842 111.425 1.00 21.86 ? 148  TRP A N   1 
ATOM   327  C  CA  . TRP A 1 43  ? 49.013 24.196 110.026 1.00 23.11 ? 148  TRP A CA  1 
ATOM   328  C  C   . TRP A 1 43  ? 47.955 23.571 109.126 1.00 23.44 ? 148  TRP A C   1 
ATOM   329  O  O   . TRP A 1 43  ? 47.419 24.237 108.244 1.00 21.73 ? 148  TRP A O   1 
ATOM   330  C  CB  . TRP A 1 43  ? 50.413 23.831 109.534 1.00 19.89 ? 148  TRP A CB  1 
ATOM   331  C  CG  . TRP A 1 43  ? 51.513 24.569 110.249 1.00 21.33 ? 148  TRP A CG  1 
ATOM   332  C  CD1 . TRP A 1 43  ? 52.445 24.037 111.100 1.00 20.02 ? 148  TRP A CD1 1 
ATOM   333  C  CD2 . TRP A 1 43  ? 51.827 25.964 110.138 1.00 21.93 ? 148  TRP A CD2 1 
ATOM   334  N  NE1 . TRP A 1 43  ? 53.320 25.012 111.517 1.00 17.63 ? 148  TRP A NE1 1 
ATOM   335  C  CE2 . TRP A 1 43  ? 52.965 26.203 110.942 1.00 20.27 ? 148  TRP A CE2 1 
ATOM   336  C  CE3 . TRP A 1 43  ? 51.259 27.036 109.435 1.00 18.40 ? 148  TRP A CE3 1 
ATOM   337  C  CZ2 . TRP A 1 43  ? 53.548 27.472 111.059 1.00 19.95 ? 148  TRP A CZ2 1 
ATOM   338  C  CZ3 . TRP A 1 43  ? 51.838 28.297 109.553 1.00 19.74 ? 148  TRP A CZ3 1 
ATOM   339  C  CH2 . TRP A 1 43  ? 52.972 28.503 110.359 1.00 18.39 ? 148  TRP A CH2 1 
ATOM   340  N  N   . SER A 1 44  ? 47.645 22.300 109.351 1.00 25.55 ? 149  SER A N   1 
ATOM   341  C  CA  . SER A 1 44  ? 46.648 21.630 108.531 1.00 27.95 ? 149  SER A CA  1 
ATOM   342  C  C   . SER A 1 44  ? 45.274 22.220 108.782 1.00 28.65 ? 149  SER A C   1 
ATOM   343  O  O   . SER A 1 44  ? 44.340 21.959 108.031 1.00 30.51 ? 149  SER A O   1 
ATOM   344  C  CB  . SER A 1 44  ? 46.618 20.127 108.823 1.00 28.12 ? 149  SER A CB  1 
ATOM   345  O  OG  . SER A 1 44  ? 46.132 19.877 110.124 1.00 27.95 ? 149  SER A OG  1 
ATOM   346  N  N   . ALA A 1 45  ? 45.148 23.022 109.833 1.00 27.46 ? 150  ALA A N   1 
ATOM   347  C  CA  . ALA A 1 45  ? 43.864 23.627 110.151 1.00 27.51 ? 150  ALA A CA  1 
ATOM   348  C  C   . ALA A 1 45  ? 43.552 24.843 109.280 1.00 28.60 ? 150  ALA A C   1 
ATOM   349  O  O   . ALA A 1 45  ? 42.393 25.187 109.091 1.00 28.82 ? 150  ALA A O   1 
ATOM   350  C  CB  . ALA A 1 45  ? 43.817 24.013 111.620 1.00 24.47 ? 150  ALA A CB  1 
ATOM   351  N  N   . VAL A 1 46  ? 44.579 25.492 108.745 1.00 30.95 ? 151  VAL A N   1 
ATOM   352  C  CA  . VAL A 1 46  ? 44.366 26.670 107.909 1.00 30.77 ? 151  VAL A CA  1 
ATOM   353  C  C   . VAL A 1 46  ? 44.765 26.451 106.455 1.00 30.85 ? 151  VAL A C   1 
ATOM   354  O  O   . VAL A 1 46  ? 44.898 27.405 105.691 1.00 31.86 ? 151  VAL A O   1 
ATOM   355  C  CB  . VAL A 1 46  ? 45.144 27.891 108.456 1.00 30.72 ? 151  VAL A CB  1 
ATOM   356  C  CG1 . VAL A 1 46  ? 44.557 28.320 109.784 1.00 32.55 ? 151  VAL A CG1 1 
ATOM   357  C  CG2 . VAL A 1 46  ? 46.617 27.546 108.623 1.00 27.92 ? 151  VAL A CG2 1 
ATOM   358  N  N   . THR A 1 47  ? 44.958 25.195 106.072 1.00 30.06 ? 152  THR A N   1 
ATOM   359  C  CA  . THR A 1 47  ? 45.339 24.879 104.703 1.00 30.51 ? 152  THR A CA  1 
ATOM   360  C  C   . THR A 1 47  ? 44.760 23.530 104.301 1.00 30.44 ? 152  THR A C   1 
ATOM   361  O  O   . THR A 1 47  ? 44.171 22.831 105.125 1.00 29.70 ? 152  THR A O   1 
ATOM   362  C  CB  . THR A 1 47  ? 46.879 24.805 104.536 1.00 29.92 ? 152  THR A CB  1 
ATOM   363  O  OG1 . THR A 1 47  ? 47.390 23.686 105.273 1.00 28.72 ? 152  THR A OG1 1 
ATOM   364  C  CG2 . THR A 1 47  ? 47.538 26.087 105.021 1.00 30.53 ? 152  THR A CG2 1 
ATOM   365  N  N   . PRO A 1 48  ? 44.904 23.157 103.017 1.00 30.47 ? 153  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 48  ? 44.392 21.875 102.527 1.00 30.14 ? 153  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 48  ? 45.400 20.750 102.768 1.00 29.51 ? 153  PRO A C   1 
ATOM   368  O  O   . PRO A 1 48  ? 45.190 19.619 102.336 1.00 30.25 ? 153  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 48  ? 44.174 22.145 101.042 1.00 30.77 ? 153  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 48  ? 45.304 23.059 100.717 1.00 32.01 ? 153  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 48  ? 45.298 24.023 101.887 1.00 30.45 ? 153  PRO A CD  1 
ATOM   372  N  N   . LEU A 1 49  ? 46.496 21.075 103.451 1.00 27.86 ? 154  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 49  ? 47.539 20.100 103.753 1.00 26.19 ? 154  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 49  ? 47.104 19.116 104.832 1.00 25.56 ? 154  LEU A C   1 
ATOM   375  O  O   . LEU A 1 49  ? 46.290 19.440 105.693 1.00 26.20 ? 154  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 49  ? 48.808 20.805 104.233 1.00 26.31 ? 154  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 49  ? 49.491 21.847 103.342 1.00 25.08 ? 154  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 49  ? 50.606 22.524 104.124 1.00 23.11 ? 154  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 49  ? 50.043 21.196 102.097 1.00 26.17 ? 154  LEU A CD2 1 
ATOM   380  N  N   . THR A 1 50  ? 47.646 17.908 104.764 1.00 24.90 ? 155  THR A N   1 
ATOM   381  C  CA  . THR A 1 50  ? 47.363 16.875 105.752 1.00 26.31 ? 155  THR A CA  1 
ATOM   382  C  C   . THR A 1 50  ? 48.711 16.294 106.134 1.00 25.34 ? 155  THR A C   1 
ATOM   383  O  O   . THR A 1 50  ? 49.670 16.379 105.360 1.00 23.30 ? 155  THR A O   1 
ATOM   384  C  CB  . THR A 1 50  ? 46.481 15.746 105.190 1.00 27.72 ? 155  THR A CB  1 
ATOM   385  O  OG1 . THR A 1 50  ? 47.094 15.203 104.014 1.00 32.34 ? 155  THR A OG1 1 
ATOM   386  C  CG2 . THR A 1 50  ? 45.088 16.267 104.862 1.00 27.86 ? 155  THR A CG2 1 
ATOM   387  N  N   . PHE A 1 51  ? 48.790 15.707 107.323 1.00 23.87 ? 156  PHE A N   1 
ATOM   388  C  CA  . PHE A 1 51  ? 50.044 15.139 107.787 1.00 22.82 ? 156  PHE A CA  1 
ATOM   389  C  C   . PHE A 1 51  ? 49.864 13.718 108.286 1.00 24.14 ? 156  PHE A C   1 
ATOM   390  O  O   . PHE A 1 51  ? 49.026 13.441 109.145 1.00 26.34 ? 156  PHE A O   1 
ATOM   391  C  CB  . PHE A 1 51  ? 50.630 16.046 108.870 1.00 19.73 ? 156  PHE A CB  1 
ATOM   392  C  CG  . PHE A 1 51  ? 50.935 17.434 108.375 1.00 15.72 ? 156  PHE A CG  1 
ATOM   393  C  CD1 . PHE A 1 51  ? 52.108 17.693 107.676 1.00 15.50 ? 156  PHE A CD1 1 
ATOM   394  C  CD2 . PHE A 1 51  ? 50.011 18.461 108.536 1.00 16.19 ? 156  PHE A CD2 1 
ATOM   395  C  CE1 . PHE A 1 51  ? 52.357 18.952 107.139 1.00 14.40 ? 156  PHE A CE1 1 
ATOM   396  C  CE2 . PHE A 1 51  ? 50.249 19.725 108.004 1.00 15.79 ? 156  PHE A CE2 1 
ATOM   397  C  CZ  . PHE A 1 51  ? 51.423 19.972 107.304 1.00 15.01 ? 156  PHE A CZ  1 
ATOM   398  N  N   . THR A 1 52  ? 50.660 12.819 107.726 1.00 24.42 ? 157  THR A N   1 
ATOM   399  C  CA  . THR A 1 52  ? 50.595 11.410 108.070 1.00 23.69 ? 157  THR A CA  1 
ATOM   400  C  C   . THR A 1 52  ? 51.915 10.939 108.638 1.00 22.11 ? 157  THR A C   1 
ATOM   401  O  O   . THR A 1 52  ? 52.984 11.228 108.090 1.00 21.92 ? 157  THR A O   1 
ATOM   402  C  CB  . THR A 1 52  ? 50.245 10.569 106.822 1.00 23.41 ? 157  THR A CB  1 
ATOM   403  O  OG1 . THR A 1 52  ? 48.935 10.931 106.373 1.00 25.91 ? 157  THR A OG1 1 
ATOM   404  C  CG2 . THR A 1 52  ? 50.277 9.081  107.135 1.00 21.00 ? 157  THR A CG2 1 
ATOM   405  N  N   . ARG A 1 53  ? 51.830 10.214 109.745 1.00 22.59 ? 158  ARG A N   1 
ATOM   406  C  CA  . ARG A 1 53  ? 53.015 9.679  110.394 1.00 22.35 ? 158  ARG A CA  1 
ATOM   407  C  C   . ARG A 1 53  ? 53.362 8.320  109.802 1.00 21.92 ? 158  ARG A C   1 
ATOM   408  O  O   . ARG A 1 53  ? 52.508 7.442  109.710 1.00 21.61 ? 158  ARG A O   1 
ATOM   409  C  CB  . ARG A 1 53  ? 52.780 9.534  111.899 1.00 21.18 ? 158  ARG A CB  1 
ATOM   410  C  CG  . ARG A 1 53  ? 53.998 9.010  112.630 1.00 21.22 ? 158  ARG A CG  1 
ATOM   411  C  CD  . ARG A 1 53  ? 53.758 8.843  114.113 1.00 20.30 ? 158  ARG A CD  1 
ATOM   412  N  NE  . ARG A 1 53  ? 54.959 8.340  114.776 1.00 20.99 ? 158  ARG A NE  1 
ATOM   413  C  CZ  . ARG A 1 53  ? 55.013 7.974  116.051 1.00 20.64 ? 158  ARG A CZ  1 
ATOM   414  N  NH1 . ARG A 1 53  ? 53.931 8.058  116.811 1.00 19.84 ? 158  ARG A NH1 1 
ATOM   415  N  NH2 . ARG A 1 53  ? 56.147 7.506  116.560 1.00 20.74 ? 158  ARG A NH2 1 
ATOM   416  N  N   . VAL A 1 54  ? 54.618 8.156  109.399 1.00 24.22 ? 159  VAL A N   1 
ATOM   417  C  CA  . VAL A 1 54  ? 55.092 6.901  108.823 1.00 25.52 ? 159  VAL A CA  1 
ATOM   418  C  C   . VAL A 1 54  ? 56.344 6.469  109.579 1.00 28.57 ? 159  VAL A C   1 
ATOM   419  O  O   . VAL A 1 54  ? 56.842 7.212  110.424 1.00 29.72 ? 159  VAL A O   1 
ATOM   420  C  CB  . VAL A 1 54  ? 55.403 7.059  107.311 1.00 23.23 ? 159  VAL A CB  1 
ATOM   421  C  CG1 . VAL A 1 54  ? 54.147 7.523  106.573 1.00 19.77 ? 159  VAL A CG1 1 
ATOM   422  C  CG2 . VAL A 1 54  ? 56.539 8.045  107.109 1.00 21.91 ? 159  VAL A CG2 1 
ATOM   423  N  N   . TYR A 1 55  ? 56.859 5.278  109.282 1.00 31.79 ? 160  TYR A N   1 
ATOM   424  C  CA  . TYR A 1 55  ? 58.033 4.791  109.995 1.00 33.61 ? 160  TYR A CA  1 
ATOM   425  C  C   . TYR A 1 55  ? 59.270 4.449  109.170 1.00 36.31 ? 160  TYR A C   1 
ATOM   426  O  O   . TYR A 1 55  ? 60.097 3.640  109.591 1.00 39.18 ? 160  TYR A O   1 
ATOM   427  C  CB  . TYR A 1 55  ? 57.634 3.596  110.863 1.00 29.27 ? 160  TYR A CB  1 
ATOM   428  C  CG  . TYR A 1 55  ? 56.570 3.952  111.873 1.00 28.93 ? 160  TYR A CG  1 
ATOM   429  C  CD1 . TYR A 1 55  ? 55.230 4.056  111.498 1.00 28.23 ? 160  TYR A CD1 1 
ATOM   430  C  CD2 . TYR A 1 55  ? 56.912 4.261  113.191 1.00 28.64 ? 160  TYR A CD2 1 
ATOM   431  C  CE1 . TYR A 1 55  ? 54.256 4.465  112.410 1.00 29.32 ? 160  TYR A CE1 1 
ATOM   432  C  CE2 . TYR A 1 55  ? 55.949 4.670  114.108 1.00 29.60 ? 160  TYR A CE2 1 
ATOM   433  C  CZ  . TYR A 1 55  ? 54.626 4.772  113.712 1.00 30.04 ? 160  TYR A CZ  1 
ATOM   434  O  OH  . TYR A 1 55  ? 53.680 5.193  114.616 1.00 32.56 ? 160  TYR A OH  1 
ATOM   435  N  N   . SER A 1 56  ? 59.414 5.075  108.010 1.00 37.86 ? 161  SER A N   1 
ATOM   436  C  CA  . SER A 1 56  ? 60.574 4.816  107.174 1.00 39.80 ? 161  SER A CA  1 
ATOM   437  C  C   . SER A 1 56  ? 61.231 6.128  106.766 1.00 41.58 ? 161  SER A C   1 
ATOM   438  O  O   . SER A 1 56  ? 60.664 7.200  106.972 1.00 41.79 ? 161  SER A O   1 
ATOM   439  C  CB  . SER A 1 56  ? 60.166 4.018  105.933 1.00 38.63 ? 161  SER A CB  1 
ATOM   440  O  OG  . SER A 1 56  ? 59.238 4.737  105.143 1.00 39.02 ? 161  SER A OG  1 
ATOM   441  N  N   . ARG A 1 57  ? 62.426 6.033  106.187 1.00 44.11 ? 162  ARG A N   1 
ATOM   442  C  CA  . ARG A 1 57  ? 63.188 7.198  105.739 1.00 46.57 ? 162  ARG A CA  1 
ATOM   443  C  C   . ARG A 1 57  ? 62.537 7.862  104.529 1.00 47.42 ? 162  ARG A C   1 
ATOM   444  O  O   . ARG A 1 57  ? 63.027 8.879  104.040 1.00 48.56 ? 162  ARG A O   1 
ATOM   445  C  CB  . ARG A 1 57  ? 64.613 6.790  105.350 1.00 48.67 ? 162  ARG A CB  1 
ATOM   446  C  CG  . ARG A 1 57  ? 65.408 6.045  106.418 1.00 53.36 ? 162  ARG A CG  1 
ATOM   447  C  CD  . ARG A 1 57  ? 64.757 4.721  106.797 1.00 57.23 ? 162  ARG A CD  1 
ATOM   448  N  NE  . ARG A 1 57  ? 65.661 3.839  107.528 1.00 60.31 ? 162  ARG A NE  1 
ATOM   449  C  CZ  . ARG A 1 57  ? 65.274 2.728  108.145 1.00 62.63 ? 162  ARG A CZ  1 
ATOM   450  N  NH1 . ARG A 1 57  ? 63.997 2.372  108.120 1.00 63.79 ? 162  ARG A NH1 1 
ATOM   451  N  NH2 . ARG A 1 57  ? 66.161 1.965  108.777 1.00 62.58 ? 162  ARG A NH2 1 
ATOM   452  N  N   . ASP A 1 58  ? 61.441 7.282  104.048 1.00 48.01 ? 163  ASP A N   1 
ATOM   453  C  CA  . ASP A 1 58  ? 60.739 7.804  102.876 1.00 46.94 ? 163  ASP A CA  1 
ATOM   454  C  C   . ASP A 1 58  ? 59.838 9.008  103.127 1.00 42.48 ? 163  ASP A C   1 
ATOM   455  O  O   . ASP A 1 58  ? 59.350 9.627  102.181 1.00 43.42 ? 163  ASP A O   1 
ATOM   456  C  CB  . ASP A 1 58  ? 59.909 6.695  102.227 1.00 52.93 ? 163  ASP A CB  1 
ATOM   457  C  CG  . ASP A 1 58  ? 60.766 5.584  101.665 1.00 56.71 ? 163  ASP A CG  1 
ATOM   458  O  OD1 . ASP A 1 58  ? 61.681 5.891  100.871 1.00 59.29 ? 163  ASP A OD1 1 
ATOM   459  O  OD2 . ASP A 1 58  ? 60.525 4.409  102.013 1.00 61.03 ? 163  ASP A OD2 1 
ATOM   460  N  N   . ALA A 1 59  ? 59.612 9.337  104.392 1.00 35.33 ? 164  ALA A N   1 
ATOM   461  C  CA  . ALA A 1 59  ? 58.768 10.476 104.738 1.00 28.19 ? 164  ALA A CA  1 
ATOM   462  C  C   . ALA A 1 59  ? 59.332 11.776 104.159 1.00 24.32 ? 164  ALA A C   1 
ATOM   463  O  O   . ALA A 1 59  ? 60.528 11.868 103.859 1.00 18.94 ? 164  ALA A O   1 
ATOM   464  C  CB  . ALA A 1 59  ? 58.656 10.591 106.254 1.00 28.52 ? 164  ALA A CB  1 
ATOM   465  N  N   . ASP A 1 60  ? 58.468 12.776 103.996 1.00 20.55 ? 165  ASP A N   1 
ATOM   466  C  CA  . ASP A 1 60  ? 58.910 14.070 103.491 1.00 19.96 ? 165  ASP A CA  1 
ATOM   467  C  C   . ASP A 1 60  ? 59.619 14.808 104.609 1.00 19.50 ? 165  ASP A C   1 
ATOM   468  O  O   . ASP A 1 60  ? 60.669 15.387 104.403 1.00 20.89 ? 165  ASP A O   1 
ATOM   469  C  CB  . ASP A 1 60  ? 57.732 14.931 103.033 1.00 20.58 ? 165  ASP A CB  1 
ATOM   470  C  CG  . ASP A 1 60  ? 56.953 14.302 101.918 1.00 19.34 ? 165  ASP A CG  1 
ATOM   471  O  OD1 . ASP A 1 60  ? 57.577 13.931 100.907 1.00 22.92 ? 165  ASP A OD1 1 
ATOM   472  O  OD2 . ASP A 1 60  ? 55.720 14.185 102.053 1.00 20.26 ? 165  ASP A OD2 1 
ATOM   473  N  N   . ILE A 1 61  ? 59.031 14.798 105.798 1.00 18.88 ? 166  ILE A N   1 
ATOM   474  C  CA  . ILE A 1 61  ? 59.638 15.496 106.923 1.00 18.31 ? 166  ILE A CA  1 
ATOM   475  C  C   . ILE A 1 61  ? 60.198 14.523 107.950 1.00 18.31 ? 166  ILE A C   1 
ATOM   476  O  O   . ILE A 1 61  ? 59.448 13.831 108.635 1.00 19.42 ? 166  ILE A O   1 
ATOM   477  C  CB  . ILE A 1 61  ? 58.612 16.435 107.598 1.00 16.76 ? 166  ILE A CB  1 
ATOM   478  C  CG1 . ILE A 1 61  ? 58.129 17.477 106.581 1.00 16.47 ? 166  ILE A CG1 1 
ATOM   479  C  CG2 . ILE A 1 61  ? 59.241 17.114 108.817 1.00 15.02 ? 166  ILE A CG2 1 
ATOM   480  C  CD1 . ILE A 1 61  ? 57.004 18.367 107.073 1.00 12.28 ? 166  ILE A CD1 1 
ATOM   481  N  N   . VAL A 1 62  ? 61.522 14.453 108.032 1.00 16.42 ? 167  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 62  ? 62.172 13.577 108.992 1.00 14.89 ? 167  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 62  ? 62.581 14.415 110.200 1.00 17.08 ? 167  VAL A C   1 
ATOM   484  O  O   . VAL A 1 62  ? 63.232 15.456 110.064 1.00 13.46 ? 167  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 62  ? 63.410 12.891 108.391 1.00 16.42 ? 167  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 62  ? 64.133 12.076 109.464 1.00 14.30 ? 167  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 62  ? 62.984 11.982 107.243 1.00 18.08 ? 167  VAL A CG2 1 
ATOM   488  N  N   . ILE A 1 63  ? 62.183 13.943 111.378 1.00 15.49 ? 168  ILE A N   1 
ATOM   489  C  CA  . ILE A 1 63  ? 62.445 14.624 112.633 1.00 16.01 ? 168  ILE A CA  1 
ATOM   490  C  C   . ILE A 1 63  ? 63.482 13.906 113.486 1.00 16.29 ? 168  ILE A C   1 
ATOM   491  O  O   . ILE A 1 63  ? 63.442 12.693 113.648 1.00 18.46 ? 168  ILE A O   1 
ATOM   492  C  CB  . ILE A 1 63  ? 61.145 14.735 113.448 1.00 13.64 ? 168  ILE A CB  1 
ATOM   493  C  CG1 . ILE A 1 63  ? 60.077 15.427 112.603 1.00 12.69 ? 168  ILE A CG1 1 
ATOM   494  C  CG2 . ILE A 1 63  ? 61.406 15.473 114.755 1.00 14.98 ? 168  ILE A CG2 1 
ATOM   495  C  CD1 . ILE A 1 63  ? 58.685 15.344 113.170 1.00 10.54 ? 168  ILE A CD1 1 
ATOM   496  N  N   . GLN A 1 64  ? 64.414 14.656 114.045 1.00 19.10 ? 169  GLN A N   1 
ATOM   497  C  CA  . GLN A 1 64  ? 65.407 14.028 114.890 1.00 20.39 ? 169  GLN A CA  1 
ATOM   498  C  C   . GLN A 1 64  ? 65.998 14.991 115.905 1.00 19.32 ? 169  GLN A C   1 
ATOM   499  O  O   . GLN A 1 64  ? 66.009 16.206 115.694 1.00 17.87 ? 169  GLN A O   1 
ATOM   500  C  CB  . GLN A 1 64  ? 66.536 13.443 114.043 1.00 23.58 ? 169  GLN A CB  1 
ATOM   501  C  CG  . GLN A 1 64  ? 67.428 14.481 113.409 1.00 28.43 ? 169  GLN A CG  1 
ATOM   502  C  CD  . GLN A 1 64  ? 68.723 13.890 112.901 1.00 32.40 ? 169  GLN A CD  1 
ATOM   503  O  OE1 . GLN A 1 64  ? 69.551 13.411 113.678 1.00 36.26 ? 169  GLN A OE1 1 
ATOM   504  N  NE2 . GLN A 1 64  ? 68.908 13.917 111.591 1.00 33.78 ? 169  GLN A NE2 1 
ATOM   505  N  N   . PHE A 1 65  ? 66.482 14.423 117.005 1.00 15.27 ? 170  PHE A N   1 
ATOM   506  C  CA  . PHE A 1 65  ? 67.124 15.180 118.062 1.00 16.05 ? 170  PHE A CA  1 
ATOM   507  C  C   . PHE A 1 65  ? 68.611 14.873 117.953 1.00 17.13 ? 170  PHE A C   1 
ATOM   508  O  O   . PHE A 1 65  ? 68.998 13.728 117.747 1.00 18.15 ? 170  PHE A O   1 
ATOM   509  C  CB  . PHE A 1 65  ? 66.613 14.740 119.444 1.00 13.11 ? 170  PHE A CB  1 
ATOM   510  C  CG  . PHE A 1 65  ? 65.164 15.056 119.690 1.00 11.58 ? 170  PHE A CG  1 
ATOM   511  C  CD1 . PHE A 1 65  ? 64.157 14.272 119.131 1.00 9.60  ? 170  PHE A CD1 1 
ATOM   512  C  CD2 . PHE A 1 65  ? 64.807 16.148 120.475 1.00 11.94 ? 170  PHE A CD2 1 
ATOM   513  C  CE1 . PHE A 1 65  ? 62.817 14.572 119.352 1.00 10.10 ? 170  PHE A CE1 1 
ATOM   514  C  CE2 . PHE A 1 65  ? 63.466 16.458 120.701 1.00 11.51 ? 170  PHE A CE2 1 
ATOM   515  C  CZ  . PHE A 1 65  ? 62.471 15.671 120.141 1.00 11.15 ? 170  PHE A CZ  1 
ATOM   516  N  N   . GLY A 1 66  ? 69.450 15.889 118.082 1.00 17.88 ? 171  GLY A N   1 
ATOM   517  C  CA  . GLY A 1 66  ? 70.879 15.655 118.006 1.00 19.53 ? 171  GLY A CA  1 
ATOM   518  C  C   . GLY A 1 66  ? 71.642 16.630 118.878 1.00 21.64 ? 171  GLY A C   1 
ATOM   519  O  O   . GLY A 1 66  ? 71.083 17.631 119.324 1.00 22.76 ? 171  GLY A O   1 
ATOM   520  N  N   . VAL A 1 67  ? 72.912 16.332 119.138 1.00 23.09 ? 172  VAL A N   1 
ATOM   521  C  CA  . VAL A 1 67  ? 73.756 17.205 119.950 1.00 25.50 ? 172  VAL A CA  1 
ATOM   522  C  C   . VAL A 1 67  ? 75.038 17.489 119.174 1.00 26.07 ? 172  VAL A C   1 
ATOM   523  O  O   . VAL A 1 67  ? 75.653 16.574 118.615 1.00 24.44 ? 172  VAL A O   1 
ATOM   524  C  CB  . VAL A 1 67  ? 74.109 16.560 121.326 1.00 26.03 ? 172  VAL A CB  1 
ATOM   525  C  CG1 . VAL A 1 67  ? 72.844 16.252 122.083 1.00 26.98 ? 172  VAL A CG1 1 
ATOM   526  C  CG2 . VAL A 1 67  ? 74.918 15.292 121.134 1.00 25.99 ? 172  VAL A CG2 1 
ATOM   527  N  N   . ALA A 1 68  ? 75.427 18.760 119.139 1.00 27.68 ? 173  ALA A N   1 
ATOM   528  C  CA  . ALA A 1 68  ? 76.618 19.184 118.411 1.00 28.80 ? 173  ALA A CA  1 
ATOM   529  C  C   . ALA A 1 68  ? 76.548 18.659 116.974 1.00 29.57 ? 173  ALA A C   1 
ATOM   530  O  O   . ALA A 1 68  ? 75.538 18.843 116.289 1.00 27.64 ? 173  ALA A O   1 
ATOM   531  C  CB  . ALA A 1 68  ? 77.868 18.664 119.111 1.00 29.58 ? 173  ALA A CB  1 
ATOM   532  N  N   . GLU A 1 69  ? 77.619 18.006 116.530 1.00 29.27 ? 174  GLU A N   1 
ATOM   533  C  CA  . GLU A 1 69  ? 77.699 17.437 115.189 1.00 32.29 ? 174  GLU A CA  1 
ATOM   534  C  C   . GLU A 1 69  ? 76.657 16.340 115.076 1.00 30.20 ? 174  GLU A C   1 
ATOM   535  O  O   . GLU A 1 69  ? 76.668 15.409 115.874 1.00 31.68 ? 174  GLU A O   1 
ATOM   536  C  CB  . GLU A 1 69  ? 79.078 16.815 114.972 1.00 41.88 ? 174  GLU A CB  1 
ATOM   537  C  CG  . GLU A 1 69  ? 80.209 17.511 115.722 1.00 51.63 ? 174  GLU A CG  1 
ATOM   538  C  CD  . GLU A 1 69  ? 80.512 18.892 115.178 1.00 57.77 ? 174  GLU A CD  1 
ATOM   539  O  OE1 . GLU A 1 69  ? 81.379 19.584 115.757 1.00 58.88 ? 174  GLU A OE1 1 
ATOM   540  O  OE2 . GLU A 1 69  ? 79.888 19.284 114.167 1.00 62.24 ? 174  GLU A OE2 1 
ATOM   541  N  N   . HIS A 1 70  ? 75.768 16.418 114.092 1.00 27.49 ? 175  HIS A N   1 
ATOM   542  C  CA  . HIS A 1 70  ? 74.748 15.385 113.979 1.00 27.72 ? 175  HIS A CA  1 
ATOM   543  C  C   . HIS A 1 70  ? 74.392 14.949 112.571 1.00 30.79 ? 175  HIS A C   1 
ATOM   544  O  O   . HIS A 1 70  ? 73.257 14.536 112.317 1.00 32.24 ? 175  HIS A O   1 
ATOM   545  C  CB  . HIS A 1 70  ? 73.473 15.827 114.688 1.00 24.97 ? 175  HIS A CB  1 
ATOM   546  C  CG  . HIS A 1 70  ? 72.928 17.118 114.175 1.00 20.26 ? 175  HIS A CG  1 
ATOM   547  N  ND1 . HIS A 1 70  ? 73.354 18.341 114.644 1.00 20.15 ? 175  HIS A ND1 1 
ATOM   548  C  CD2 . HIS A 1 70  ? 72.023 17.379 113.203 1.00 17.16 ? 175  HIS A CD2 1 
ATOM   549  C  CE1 . HIS A 1 70  ? 72.734 19.302 113.982 1.00 18.26 ? 175  HIS A CE1 1 
ATOM   550  N  NE2 . HIS A 1 70  ? 71.922 18.744 113.102 1.00 15.77 ? 175  HIS A NE2 1 
ATOM   551  N  N   . GLY A 1 71  ? 75.341 15.042 111.647 1.00 32.67 ? 176  GLY A N   1 
ATOM   552  C  CA  . GLY A 1 71  ? 75.048 14.601 110.297 1.00 34.93 ? 176  GLY A CA  1 
ATOM   553  C  C   . GLY A 1 71  ? 75.221 15.634 109.213 1.00 36.14 ? 176  GLY A C   1 
ATOM   554  O  O   . GLY A 1 71  ? 76.066 15.481 108.340 1.00 37.19 ? 176  GLY A O   1 
ATOM   555  N  N   . ASP A 1 72  ? 74.399 16.674 109.240 1.00 37.27 ? 177  ASP A N   1 
ATOM   556  C  CA  . ASP A 1 72  ? 74.512 17.721 108.242 1.00 35.71 ? 177  ASP A CA  1 
ATOM   557  C  C   . ASP A 1 72  ? 75.734 18.551 108.587 1.00 36.61 ? 177  ASP A C   1 
ATOM   558  O  O   . ASP A 1 72  ? 76.570 18.132 109.389 1.00 40.71 ? 177  ASP A O   1 
ATOM   559  C  CB  . ASP A 1 72  ? 73.267 18.600 108.231 1.00 34.06 ? 177  ASP A CB  1 
ATOM   560  C  CG  . ASP A 1 72  ? 72.828 19.006 109.617 1.00 32.01 ? 177  ASP A CG  1 
ATOM   561  O  OD1 . ASP A 1 72  ? 73.684 19.394 110.439 1.00 28.22 ? 177  ASP A OD1 1 
ATOM   562  O  OD2 . ASP A 1 72  ? 71.613 18.942 109.872 1.00 33.33 ? 177  ASP A OD2 1 
ATOM   563  N  N   . GLY A 1 73  ? 75.845 19.730 107.996 1.00 34.57 ? 178  GLY A N   1 
ATOM   564  C  CA  . GLY A 1 73  ? 77.008 20.546 108.278 1.00 36.70 ? 178  GLY A CA  1 
ATOM   565  C  C   . GLY A 1 73  ? 76.753 21.721 109.194 1.00 36.80 ? 178  GLY A C   1 
ATOM   566  O  O   . GLY A 1 73  ? 77.520 22.684 109.184 1.00 37.18 ? 178  GLY A O   1 
ATOM   567  N  N   . TYR A 1 74  ? 75.688 21.649 109.991 1.00 37.02 ? 179  TYR A N   1 
ATOM   568  C  CA  . TYR A 1 74  ? 75.344 22.731 110.908 1.00 34.28 ? 179  TYR A CA  1 
ATOM   569  C  C   . TYR A 1 74  ? 75.153 22.235 112.335 1.00 31.65 ? 179  TYR A C   1 
ATOM   570  O  O   . TYR A 1 74  ? 74.033 22.165 112.838 1.00 29.30 ? 179  TYR A O   1 
ATOM   571  C  CB  . TYR A 1 74  ? 74.078 23.436 110.425 1.00 36.20 ? 179  TYR A CB  1 
ATOM   572  C  CG  . TYR A 1 74  ? 74.181 23.932 109.003 1.00 42.47 ? 179  TYR A CG  1 
ATOM   573  C  CD1 . TYR A 1 74  ? 73.949 23.076 107.927 1.00 45.68 ? 179  TYR A CD1 1 
ATOM   574  C  CD2 . TYR A 1 74  ? 74.536 25.253 108.728 1.00 44.79 ? 179  TYR A CD2 1 
ATOM   575  C  CE1 . TYR A 1 74  ? 74.065 23.524 106.609 1.00 46.33 ? 179  TYR A CE1 1 
ATOM   576  C  CE2 . TYR A 1 74  ? 74.658 25.712 107.415 1.00 45.00 ? 179  TYR A CE2 1 
ATOM   577  C  CZ  . TYR A 1 74  ? 74.420 24.843 106.362 1.00 47.34 ? 179  TYR A CZ  1 
ATOM   578  O  OH  . TYR A 1 74  ? 74.528 25.293 105.062 1.00 48.94 ? 179  TYR A OH  1 
ATOM   579  N  N   . PRO A 1 75  ? 76.260 21.895 113.014 1.00 31.79 ? 180  PRO A N   1 
ATOM   580  C  CA  . PRO A 1 75  ? 76.212 21.401 114.394 1.00 30.83 ? 180  PRO A CA  1 
ATOM   581  C  C   . PRO A 1 75  ? 75.532 22.381 115.335 1.00 28.21 ? 180  PRO A C   1 
ATOM   582  O  O   . PRO A 1 75  ? 75.505 23.579 115.073 1.00 28.60 ? 180  PRO A O   1 
ATOM   583  C  CB  . PRO A 1 75  ? 77.685 21.194 114.739 1.00 31.29 ? 180  PRO A CB  1 
ATOM   584  C  CG  . PRO A 1 75  ? 78.370 22.238 113.916 1.00 31.47 ? 180  PRO A CG  1 
ATOM   585  C  CD  . PRO A 1 75  ? 77.653 22.113 112.589 1.00 30.47 ? 180  PRO A CD  1 
ATOM   586  N  N   . PHE A 1 76  ? 74.971 21.866 116.422 1.00 25.93 ? 181  PHE A N   1 
ATOM   587  C  CA  . PHE A 1 76  ? 74.306 22.721 117.388 1.00 26.27 ? 181  PHE A CA  1 
ATOM   588  C  C   . PHE A 1 76  ? 75.351 23.306 118.335 1.00 28.41 ? 181  PHE A C   1 
ATOM   589  O  O   . PHE A 1 76  ? 76.498 22.863 118.354 1.00 27.60 ? 181  PHE A O   1 
ATOM   590  C  CB  . PHE A 1 76  ? 73.238 21.937 118.158 1.00 23.67 ? 181  PHE A CB  1 
ATOM   591  C  CG  . PHE A 1 76  ? 72.012 21.625 117.346 1.00 21.97 ? 181  PHE A CG  1 
ATOM   592  C  CD1 . PHE A 1 76  ? 71.262 22.649 116.778 1.00 22.39 ? 181  PHE A CD1 1 
ATOM   593  C  CD2 . PHE A 1 76  ? 71.590 20.309 117.165 1.00 21.41 ? 181  PHE A CD2 1 
ATOM   594  C  CE1 . PHE A 1 76  ? 70.102 22.369 116.040 1.00 22.23 ? 181  PHE A CE1 1 
ATOM   595  C  CE2 . PHE A 1 76  ? 70.432 20.019 116.430 1.00 20.84 ? 181  PHE A CE2 1 
ATOM   596  C  CZ  . PHE A 1 76  ? 69.688 21.052 115.868 1.00 19.15 ? 181  PHE A CZ  1 
ATOM   597  N  N   . ASP A 1 77  ? 74.943 24.290 119.127 1.00 28.53 ? 182  ASP A N   1 
ATOM   598  C  CA  . ASP A 1 77  ? 75.848 24.979 120.031 1.00 29.79 ? 182  ASP A CA  1 
ATOM   599  C  C   . ASP A 1 77  ? 75.677 24.718 121.535 1.00 31.81 ? 182  ASP A C   1 
ATOM   600  O  O   . ASP A 1 77  ? 75.941 25.608 122.346 1.00 34.01 ? 182  ASP A O   1 
ATOM   601  C  CB  . ASP A 1 77  ? 75.723 26.478 119.769 1.00 28.81 ? 182  ASP A CB  1 
ATOM   602  C  CG  . ASP A 1 77  ? 74.284 26.937 119.799 1.00 29.97 ? 182  ASP A CG  1 
ATOM   603  O  OD1 . ASP A 1 77  ? 73.464 26.193 120.358 1.00 30.97 ? 182  ASP A OD1 1 
ATOM   604  O  OD2 . ASP A 1 77  ? 73.962 28.025 119.284 1.00 31.92 ? 182  ASP A OD2 1 
ATOM   605  N  N   . GLY A 1 78  ? 75.249 23.520 121.921 1.00 31.93 ? 183  GLY A N   1 
ATOM   606  C  CA  . GLY A 1 78  ? 75.085 23.236 123.341 1.00 31.05 ? 183  GLY A CA  1 
ATOM   607  C  C   . GLY A 1 78  ? 73.943 24.014 123.976 1.00 32.23 ? 183  GLY A C   1 
ATOM   608  O  O   . GLY A 1 78  ? 73.094 24.524 123.276 1.00 32.15 ? 183  GLY A O   1 
ATOM   609  N  N   . LYS A 1 79  ? 73.923 24.122 125.299 1.00 32.11 ? 184  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 79  ? 72.851 24.832 126.002 1.00 33.02 ? 184  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 79  ? 72.539 26.207 125.424 1.00 31.99 ? 184  LYS A C   1 
ATOM   612  O  O   . LYS A 1 79  ? 73.445 26.975 125.118 1.00 34.08 ? 184  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 79  ? 73.209 24.984 127.484 1.00 37.17 ? 184  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 79  ? 72.020 25.232 128.396 1.00 41.04 ? 184  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 79  ? 71.101 24.017 128.419 1.00 44.80 ? 184  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 79  ? 69.925 24.219 129.353 1.00 45.32 ? 184  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 79  ? 70.371 24.435 130.752 1.00 48.28 ? 184  LYS A NZ  1 
ATOM   618  N  N   . ASP A 1 80  ? 71.250 26.504 125.278 1.00 30.60 ? 185  ASP A N   1 
ATOM   619  C  CA  . ASP A 1 80  ? 70.777 27.787 124.756 1.00 29.01 ? 185  ASP A CA  1 
ATOM   620  C  C   . ASP A 1 80  ? 71.311 28.198 123.394 1.00 26.92 ? 185  ASP A C   1 
ATOM   621  O  O   . ASP A 1 80  ? 71.999 27.438 122.727 1.00 25.74 ? 185  ASP A O   1 
ATOM   622  C  CB  . ASP A 1 80  ? 71.068 28.895 125.763 1.00 33.03 ? 185  ASP A CB  1 
ATOM   623  C  CG  . ASP A 1 80  ? 70.304 28.712 127.046 1.00 36.57 ? 185  ASP A CG  1 
ATOM   624  O  OD1 . ASP A 1 80  ? 69.058 28.796 127.011 1.00 39.21 ? 185  ASP A OD1 1 
ATOM   625  O  OD2 . ASP A 1 80  ? 70.947 28.470 128.090 1.00 40.55 ? 185  ASP A OD2 1 
ATOM   626  N  N   . GLY A 1 81  ? 70.992 29.422 122.990 1.00 24.58 ? 186  GLY A N   1 
ATOM   627  C  CA  . GLY A 1 81  ? 71.431 29.904 121.695 1.00 26.41 ? 186  GLY A CA  1 
ATOM   628  C  C   . GLY A 1 81  ? 70.472 29.395 120.637 1.00 26.21 ? 186  GLY A C   1 
ATOM   629  O  O   . GLY A 1 81  ? 69.280 29.693 120.691 1.00 27.15 ? 186  GLY A O   1 
ATOM   630  N  N   . LEU A 1 82  ? 70.987 28.625 119.684 1.00 26.00 ? 187  LEU A N   1 
ATOM   631  C  CA  . LEU A 1 82  ? 70.166 28.058 118.622 1.00 25.00 ? 187  LEU A CA  1 
ATOM   632  C  C   . LEU A 1 82  ? 69.394 26.885 119.220 1.00 24.47 ? 187  LEU A C   1 
ATOM   633  O  O   . LEU A 1 82  ? 69.996 25.979 119.775 1.00 23.75 ? 187  LEU A O   1 
ATOM   634  C  CB  . LEU A 1 82  ? 71.057 27.560 117.483 1.00 25.51 ? 187  LEU A CB  1 
ATOM   635  C  CG  . LEU A 1 82  ? 70.323 27.068 116.233 1.00 31.44 ? 187  LEU A CG  1 
ATOM   636  C  CD1 . LEU A 1 82  ? 69.618 28.248 115.564 1.00 27.44 ? 187  LEU A CD1 1 
ATOM   637  C  CD2 . LEU A 1 82  ? 71.313 26.409 115.271 1.00 32.87 ? 187  LEU A CD2 1 
ATOM   638  N  N   . LEU A 1 83  ? 68.071 26.881 119.097 1.00 22.38 ? 188  LEU A N   1 
ATOM   639  C  CA  . LEU A 1 83  ? 67.272 25.800 119.673 1.00 20.10 ? 188  LEU A CA  1 
ATOM   640  C  C   . LEU A 1 83  ? 67.026 24.638 118.712 1.00 21.08 ? 188  LEU A C   1 
ATOM   641  O  O   . LEU A 1 83  ? 66.907 23.477 119.129 1.00 18.95 ? 188  LEU A O   1 
ATOM   642  C  CB  . LEU A 1 83  ? 65.930 26.349 120.158 1.00 17.21 ? 188  LEU A CB  1 
ATOM   643  C  CG  . LEU A 1 83  ? 65.981 27.580 121.077 1.00 19.72 ? 188  LEU A CG  1 
ATOM   644  C  CD1 . LEU A 1 83  ? 64.565 27.997 121.447 1.00 14.44 ? 188  LEU A CD1 1 
ATOM   645  C  CD2 . LEU A 1 83  ? 66.791 27.275 122.329 1.00 16.62 ? 188  LEU A CD2 1 
ATOM   646  N  N   . ALA A 1 84  ? 66.956 24.958 117.426 1.00 19.08 ? 189  ALA A N   1 
ATOM   647  C  CA  . ALA A 1 84  ? 66.703 23.963 116.400 1.00 16.54 ? 189  ALA A CA  1 
ATOM   648  C  C   . ALA A 1 84  ? 66.824 24.626 115.039 1.00 17.08 ? 189  ALA A C   1 
ATOM   649  O  O   . ALA A 1 84  ? 67.110 25.815 114.943 1.00 16.33 ? 189  ALA A O   1 
ATOM   650  C  CB  . ALA A 1 84  ? 65.297 23.398 116.575 1.00 16.25 ? 189  ALA A CB  1 
ATOM   651  N  N   . HIS A 1 85  ? 66.627 23.842 113.988 1.00 16.66 ? 190  HIS A N   1 
ATOM   652  C  CA  . HIS A 1 85  ? 66.656 24.361 112.636 1.00 18.31 ? 190  HIS A CA  1 
ATOM   653  C  C   . HIS A 1 85  ? 65.982 23.372 111.699 1.00 18.42 ? 190  HIS A C   1 
ATOM   654  O  O   . HIS A 1 85  ? 65.985 22.168 111.956 1.00 18.06 ? 190  HIS A O   1 
ATOM   655  C  CB  . HIS A 1 85  ? 68.099 24.705 112.191 1.00 18.50 ? 190  HIS A CB  1 
ATOM   656  C  CG  . HIS A 1 85  ? 69.055 23.550 112.164 1.00 17.26 ? 190  HIS A CG  1 
ATOM   657  N  ND1 . HIS A 1 85  ? 70.369 23.671 112.567 1.00 18.18 ? 190  HIS A ND1 1 
ATOM   658  C  CD2 . HIS A 1 85  ? 68.920 22.281 111.712 1.00 20.42 ? 190  HIS A CD2 1 
ATOM   659  C  CE1 . HIS A 1 85  ? 71.002 22.531 112.365 1.00 17.27 ? 190  HIS A CE1 1 
ATOM   660  N  NE2 . HIS A 1 85  ? 70.145 21.671 111.846 1.00 18.89 ? 190  HIS A NE2 1 
ATOM   661  N  N   . ALA A 1 86  ? 65.367 23.887 110.637 1.00 19.52 ? 191  ALA A N   1 
ATOM   662  C  CA  . ALA A 1 86  ? 64.672 23.049 109.659 1.00 20.18 ? 191  ALA A CA  1 
ATOM   663  C  C   . ALA A 1 86  ? 65.052 23.460 108.242 1.00 22.20 ? 191  ALA A C   1 
ATOM   664  O  O   . ALA A 1 86  ? 65.547 24.563 108.026 1.00 22.82 ? 191  ALA A O   1 
ATOM   665  C  CB  . ALA A 1 86  ? 63.163 23.158 109.853 1.00 17.02 ? 191  ALA A CB  1 
ATOM   666  N  N   . PHE A 1 87  ? 64.822 22.569 107.279 1.00 24.96 ? 192  PHE A N   1 
ATOM   667  C  CA  . PHE A 1 87  ? 65.156 22.847 105.884 1.00 24.10 ? 192  PHE A CA  1 
ATOM   668  C  C   . PHE A 1 87  ? 63.906 23.012 105.033 1.00 25.05 ? 192  PHE A C   1 
ATOM   669  O  O   . PHE A 1 87  ? 62.891 22.346 105.270 1.00 24.67 ? 192  PHE A O   1 
ATOM   670  C  CB  . PHE A 1 87  ? 66.013 21.724 105.303 1.00 24.41 ? 192  PHE A CB  1 
ATOM   671  C  CG  . PHE A 1 87  ? 67.299 21.491 106.042 1.00 25.34 ? 192  PHE A CG  1 
ATOM   672  C  CD1 . PHE A 1 87  ? 67.328 20.696 107.184 1.00 27.98 ? 192  PHE A CD1 1 
ATOM   673  C  CD2 . PHE A 1 87  ? 68.483 22.059 105.594 1.00 26.82 ? 192  PHE A CD2 1 
ATOM   674  C  CE1 . PHE A 1 87  ? 68.524 20.466 107.870 1.00 27.32 ? 192  PHE A CE1 1 
ATOM   675  C  CE2 . PHE A 1 87  ? 69.682 21.839 106.267 1.00 27.38 ? 192  PHE A CE2 1 
ATOM   676  C  CZ  . PHE A 1 87  ? 69.703 21.039 107.410 1.00 28.50 ? 192  PHE A CZ  1 
ATOM   677  N  N   . PRO A 1 88  ? 63.967 23.908 104.027 1.00 25.22 ? 193  PRO A N   1 
ATOM   678  C  CA  . PRO A 1 88  ? 62.861 24.203 103.103 1.00 24.58 ? 193  PRO A CA  1 
ATOM   679  C  C   . PRO A 1 88  ? 62.454 22.970 102.299 1.00 24.59 ? 193  PRO A C   1 
ATOM   680  O  O   . PRO A 1 88  ? 63.231 22.018 102.164 1.00 23.68 ? 193  PRO A O   1 
ATOM   681  C  CB  . PRO A 1 88  ? 63.434 25.292 102.195 1.00 22.65 ? 193  PRO A CB  1 
ATOM   682  C  CG  . PRO A 1 88  ? 64.542 25.894 102.997 1.00 26.18 ? 193  PRO A CG  1 
ATOM   683  C  CD  . PRO A 1 88  ? 65.156 24.708 103.684 1.00 25.93 ? 193  PRO A CD  1 
ATOM   684  N  N   . PRO A 1 89  ? 61.233 22.981 101.745 1.00 23.30 ? 194  PRO A N   1 
ATOM   685  C  CA  . PRO A 1 89  ? 60.718 21.861 100.949 1.00 24.06 ? 194  PRO A CA  1 
ATOM   686  C  C   . PRO A 1 89  ? 61.710 21.371 99.891  1.00 23.68 ? 194  PRO A C   1 
ATOM   687  O  O   . PRO A 1 89  ? 62.473 22.147 99.325  1.00 21.32 ? 194  PRO A O   1 
ATOM   688  C  CB  . PRO A 1 89  ? 59.445 22.441 100.334 1.00 22.11 ? 194  PRO A CB  1 
ATOM   689  C  CG  . PRO A 1 89  ? 58.968 23.371 101.408 1.00 21.80 ? 194  PRO A CG  1 
ATOM   690  C  CD  . PRO A 1 89  ? 60.243 24.072 101.820 1.00 20.97 ? 194  PRO A CD  1 
ATOM   691  N  N   . GLY A 1 90  ? 61.688 20.071 99.631  1.00 26.27 ? 195  GLY A N   1 
ATOM   692  C  CA  . GLY A 1 90  ? 62.584 19.500 98.645  1.00 26.15 ? 195  GLY A CA  1 
ATOM   693  C  C   . GLY A 1 90  ? 62.908 18.059 98.978  1.00 28.20 ? 195  GLY A C   1 
ATOM   694  O  O   . GLY A 1 90  ? 62.355 17.505 99.926  1.00 29.23 ? 195  GLY A O   1 
ATOM   695  N  N   . PRO A 1 91  ? 63.801 17.420 98.211  1.00 28.08 ? 196  PRO A N   1 
ATOM   696  C  CA  . PRO A 1 91  ? 64.188 16.025 98.445  1.00 28.94 ? 196  PRO A CA  1 
ATOM   697  C  C   . PRO A 1 91  ? 65.320 15.876 99.472  1.00 29.39 ? 196  PRO A C   1 
ATOM   698  O  O   . PRO A 1 91  ? 65.972 16.855 99.837  1.00 31.26 ? 196  PRO A O   1 
ATOM   699  C  CB  . PRO A 1 91  ? 64.613 15.563 97.057  1.00 27.73 ? 196  PRO A CB  1 
ATOM   700  C  CG  . PRO A 1 91  ? 65.288 16.788 96.526  1.00 26.49 ? 196  PRO A CG  1 
ATOM   701  C  CD  . PRO A 1 91  ? 64.340 17.902 96.926  1.00 26.14 ? 196  PRO A CD  1 
ATOM   702  N  N   . GLY A 1 92  ? 65.542 14.646 99.930  1.00 28.16 ? 197  GLY A N   1 
ATOM   703  C  CA  . GLY A 1 92  ? 66.605 14.374 100.884 1.00 26.43 ? 197  GLY A CA  1 
ATOM   704  C  C   . GLY A 1 92  ? 66.466 15.066 102.223 1.00 25.89 ? 197  GLY A C   1 
ATOM   705  O  O   . GLY A 1 92  ? 65.399 15.077 102.803 1.00 26.43 ? 197  GLY A O   1 
ATOM   706  N  N   . ILE A 1 93  ? 67.548 15.648 102.719 1.00 24.59 ? 198  ILE A N   1 
ATOM   707  C  CA  . ILE A 1 93  ? 67.515 16.336 104.000 1.00 27.36 ? 198  ILE A CA  1 
ATOM   708  C  C   . ILE A 1 93  ? 66.558 17.537 103.966 1.00 29.10 ? 198  ILE A C   1 
ATOM   709  O  O   . ILE A 1 93  ? 66.139 18.048 105.009 1.00 28.33 ? 198  ILE A O   1 
ATOM   710  C  CB  . ILE A 1 93  ? 68.929 16.809 104.385 1.00 29.59 ? 198  ILE A CB  1 
ATOM   711  C  CG1 . ILE A 1 93  ? 68.946 17.268 105.840 1.00 30.60 ? 198  ILE A CG1 1 
ATOM   712  C  CG2 . ILE A 1 93  ? 69.376 17.929 103.447 1.00 29.40 ? 198  ILE A CG2 1 
ATOM   713  C  CD1 . ILE A 1 93  ? 70.323 17.634 106.334 1.00 33.20 ? 198  ILE A CD1 1 
ATOM   714  N  N   . GLN A 1 94  ? 66.212 17.975 102.760 1.00 27.92 ? 199  GLN A N   1 
ATOM   715  C  CA  . GLN A 1 94  ? 65.304 19.100 102.578 1.00 28.08 ? 199  GLN A CA  1 
ATOM   716  C  C   . GLN A 1 94  ? 63.967 18.794 103.241 1.00 23.32 ? 199  GLN A C   1 
ATOM   717  O  O   . GLN A 1 94  ? 63.442 17.705 103.097 1.00 20.60 ? 199  GLN A O   1 
ATOM   718  C  CB  . GLN A 1 94  ? 65.103 19.366 101.081 1.00 31.22 ? 199  GLN A CB  1 
ATOM   719  C  CG  . GLN A 1 94  ? 65.534 20.754 100.637 1.00 40.25 ? 199  GLN A CG  1 
ATOM   720  C  CD  . GLN A 1 94  ? 66.996 21.044 100.939 1.00 42.74 ? 199  GLN A CD  1 
ATOM   721  O  OE1 . GLN A 1 94  ? 67.459 22.173 100.787 1.00 45.88 ? 199  GLN A OE1 1 
ATOM   722  N  NE2 . GLN A 1 94  ? 67.730 20.022 101.362 1.00 44.96 ? 199  GLN A NE2 1 
ATOM   723  N  N   . GLY A 1 95  ? 63.416 19.759 103.967 1.00 23.07 ? 200  GLY A N   1 
ATOM   724  C  CA  . GLY A 1 95  ? 62.147 19.537 104.637 1.00 19.23 ? 200  GLY A CA  1 
ATOM   725  C  C   . GLY A 1 95  ? 62.279 18.891 106.009 1.00 18.68 ? 200  GLY A C   1 
ATOM   726  O  O   . GLY A 1 95  ? 61.283 18.719 106.708 1.00 22.62 ? 200  GLY A O   1 
ATOM   727  N  N   . ASP A 1 96  ? 63.496 18.532 106.405 1.00 17.22 ? 201  ASP A N   1 
ATOM   728  C  CA  . ASP A 1 96  ? 63.712 17.903 107.711 1.00 18.97 ? 201  ASP A CA  1 
ATOM   729  C  C   . ASP A 1 96  ? 63.813 18.920 108.844 1.00 19.43 ? 201  ASP A C   1 
ATOM   730  O  O   . ASP A 1 96  ? 64.156 20.076 108.621 1.00 21.36 ? 201  ASP A O   1 
ATOM   731  C  CB  . ASP A 1 96  ? 64.974 17.038 107.687 1.00 16.29 ? 201  ASP A CB  1 
ATOM   732  C  CG  . ASP A 1 96  ? 64.834 15.835 106.774 1.00 18.51 ? 201  ASP A CG  1 
ATOM   733  O  OD1 . ASP A 1 96  ? 63.724 15.612 106.260 1.00 15.25 ? 201  ASP A OD1 1 
ATOM   734  O  OD2 . ASP A 1 96  ? 65.824 15.104 106.576 1.00 19.34 ? 201  ASP A OD2 1 
ATOM   735  N  N   . ALA A 1 97  ? 63.513 18.476 110.062 1.00 19.70 ? 202  ALA A N   1 
ATOM   736  C  CA  . ALA A 1 97  ? 63.559 19.341 111.239 1.00 18.01 ? 202  ALA A CA  1 
ATOM   737  C  C   . ALA A 1 97  ? 64.389 18.706 112.350 1.00 18.31 ? 202  ALA A C   1 
ATOM   738  O  O   . ALA A 1 97  ? 64.107 17.588 112.790 1.00 17.93 ? 202  ALA A O   1 
ATOM   739  C  CB  . ALA A 1 97  ? 62.142 19.616 111.729 1.00 17.65 ? 202  ALA A CB  1 
ATOM   740  N  N   . HIS A 1 98  ? 65.407 19.431 112.805 1.00 17.90 ? 203  HIS A N   1 
ATOM   741  C  CA  . HIS A 1 98  ? 66.304 18.945 113.847 1.00 17.65 ? 203  HIS A CA  1 
ATOM   742  C  C   . HIS A 1 98  ? 66.241 19.782 115.123 1.00 17.94 ? 203  HIS A C   1 
ATOM   743  O  O   . HIS A 1 98  ? 66.248 21.008 115.063 1.00 17.49 ? 203  HIS A O   1 
ATOM   744  C  CB  . HIS A 1 98  ? 67.736 18.938 113.313 1.00 15.54 ? 203  HIS A CB  1 
ATOM   745  C  CG  . HIS A 1 98  ? 67.906 18.147 112.053 1.00 16.78 ? 203  HIS A CG  1 
ATOM   746  N  ND1 . HIS A 1 98  ? 69.025 18.248 111.258 1.00 15.86 ? 203  HIS A ND1 1 
ATOM   747  C  CD2 . HIS A 1 98  ? 67.100 17.239 111.453 1.00 14.93 ? 203  HIS A CD2 1 
ATOM   748  C  CE1 . HIS A 1 98  ? 68.902 17.439 110.221 1.00 16.22 ? 203  HIS A CE1 1 
ATOM   749  N  NE2 . HIS A 1 98  ? 67.742 16.816 110.316 1.00 14.71 ? 203  HIS A NE2 1 
ATOM   750  N  N   . PHE A 1 99  ? 66.193 19.115 116.275 1.00 17.60 ? 204  PHE A N   1 
ATOM   751  C  CA  . PHE A 1 99  ? 66.133 19.814 117.559 1.00 17.27 ? 204  PHE A CA  1 
ATOM   752  C  C   . PHE A 1 99  ? 67.378 19.555 118.402 1.00 17.45 ? 204  PHE A C   1 
ATOM   753  O  O   . PHE A 1 99  ? 67.834 18.414 118.510 1.00 15.59 ? 204  PHE A O   1 
ATOM   754  C  CB  . PHE A 1 99  ? 64.884 19.389 118.342 1.00 15.27 ? 204  PHE A CB  1 
ATOM   755  C  CG  . PHE A 1 99  ? 63.602 19.576 117.579 1.00 15.59 ? 204  PHE A CG  1 
ATOM   756  C  CD1 . PHE A 1 99  ? 63.234 18.678 116.581 1.00 15.30 ? 204  PHE A CD1 1 
ATOM   757  C  CD2 . PHE A 1 99  ? 62.790 20.683 117.816 1.00 15.08 ? 204  PHE A CD2 1 
ATOM   758  C  CE1 . PHE A 1 99  ? 62.075 18.882 115.826 1.00 17.01 ? 204  PHE A CE1 1 
ATOM   759  C  CE2 . PHE A 1 99  ? 61.636 20.899 117.071 1.00 14.70 ? 204  PHE A CE2 1 
ATOM   760  C  CZ  . PHE A 1 99  ? 61.275 19.998 116.073 1.00 16.71 ? 204  PHE A CZ  1 
ATOM   761  N  N   . ASP A 1 100 ? 67.928 20.619 118.987 1.00 16.31 ? 205  ASP A N   1 
ATOM   762  C  CA  . ASP A 1 100 ? 69.109 20.503 119.837 1.00 16.90 ? 205  ASP A CA  1 
ATOM   763  C  C   . ASP A 1 100 ? 68.730 19.883 121.185 1.00 17.81 ? 205  ASP A C   1 
ATOM   764  O  O   . ASP A 1 100 ? 68.024 20.498 121.988 1.00 18.19 ? 205  ASP A O   1 
ATOM   765  C  CB  . ASP A 1 100 ? 69.729 21.876 120.082 1.00 17.51 ? 205  ASP A CB  1 
ATOM   766  C  CG  . ASP A 1 100 ? 71.037 21.788 120.840 1.00 18.97 ? 205  ASP A CG  1 
ATOM   767  O  OD1 . ASP A 1 100 ? 71.305 20.732 121.441 1.00 18.91 ? 205  ASP A OD1 1 
ATOM   768  O  OD2 . ASP A 1 100 ? 71.798 22.767 120.836 1.00 18.05 ? 205  ASP A OD2 1 
ATOM   769  N  N   . ASP A 1 101 ? 69.208 18.670 121.436 1.00 19.02 ? 206  ASP A N   1 
ATOM   770  C  CA  . ASP A 1 101 ? 68.880 17.994 122.676 1.00 20.78 ? 206  ASP A CA  1 
ATOM   771  C  C   . ASP A 1 101 ? 69.781 18.386 123.847 1.00 21.59 ? 206  ASP A C   1 
ATOM   772  O  O   . ASP A 1 101 ? 69.827 17.692 124.849 1.00 23.96 ? 206  ASP A O   1 
ATOM   773  C  CB  . ASP A 1 101 ? 68.881 16.473 122.468 1.00 22.45 ? 206  ASP A CB  1 
ATOM   774  C  CG  . ASP A 1 101 ? 68.015 15.737 123.497 1.00 25.21 ? 206  ASP A CG  1 
ATOM   775  O  OD1 . ASP A 1 101 ? 67.013 16.317 123.968 1.00 26.38 ? 206  ASP A OD1 1 
ATOM   776  O  OD2 . ASP A 1 101 ? 68.321 14.574 123.822 1.00 24.25 ? 206  ASP A OD2 1 
ATOM   777  N  N   . ASP A 1 102 ? 70.513 19.488 123.715 1.00 23.27 ? 207  ASP A N   1 
ATOM   778  C  CA  . ASP A 1 102 ? 71.331 19.969 124.823 1.00 22.12 ? 207  ASP A CA  1 
ATOM   779  C  C   . ASP A 1 102 ? 70.458 20.966 125.570 1.00 21.36 ? 207  ASP A C   1 
ATOM   780  O  O   . ASP A 1 102 ? 70.817 21.459 126.634 1.00 22.22 ? 207  ASP A O   1 
ATOM   781  C  CB  . ASP A 1 102 ? 72.605 20.664 124.342 1.00 23.08 ? 207  ASP A CB  1 
ATOM   782  C  CG  . ASP A 1 102 ? 73.809 19.738 124.348 1.00 24.02 ? 207  ASP A CG  1 
ATOM   783  O  OD1 . ASP A 1 102 ? 73.806 18.762 125.124 1.00 26.09 ? 207  ASP A OD1 1 
ATOM   784  O  OD2 . ASP A 1 102 ? 74.766 19.989 123.591 1.00 23.97 ? 207  ASP A OD2 1 
ATOM   785  N  N   . GLU A 1 103 ? 69.303 21.255 124.982 1.00 20.40 ? 208  GLU A N   1 
ATOM   786  C  CA  . GLU A 1 103 ? 68.341 22.172 125.567 1.00 21.00 ? 208  GLU A CA  1 
ATOM   787  C  C   . GLU A 1 103 ? 67.446 21.345 126.464 1.00 19.62 ? 208  GLU A C   1 
ATOM   788  O  O   . GLU A 1 103 ? 67.323 20.140 126.271 1.00 18.21 ? 208  GLU A O   1 
ATOM   789  C  CB  . GLU A 1 103 ? 67.477 22.810 124.475 1.00 22.83 ? 208  GLU A CB  1 
ATOM   790  C  CG  . GLU A 1 103 ? 68.262 23.464 123.363 1.00 27.27 ? 208  GLU A CG  1 
ATOM   791  C  CD  . GLU A 1 103 ? 68.931 24.732 123.805 1.00 29.69 ? 208  GLU A CD  1 
ATOM   792  O  OE1 . GLU A 1 103 ? 69.277 24.846 124.996 1.00 36.53 ? 208  GLU A OE1 1 
ATOM   793  O  OE2 . GLU A 1 103 ? 69.119 25.620 122.959 1.00 34.99 ? 208  GLU A OE2 1 
ATOM   794  N  N   . LEU A 1 104 ? 66.831 21.990 127.447 1.00 18.09 ? 209  LEU A N   1 
ATOM   795  C  CA  . LEU A 1 104 ? 65.898 21.311 128.331 1.00 17.54 ? 209  LEU A CA  1 
ATOM   796  C  C   . LEU A 1 104 ? 64.529 21.445 127.653 1.00 16.85 ? 209  LEU A C   1 
ATOM   797  O  O   . LEU A 1 104 ? 64.001 22.549 127.519 1.00 18.96 ? 209  LEU A O   1 
ATOM   798  C  CB  . LEU A 1 104 ? 65.887 21.982 129.710 1.00 15.57 ? 209  LEU A CB  1 
ATOM   799  C  CG  . LEU A 1 104 ? 64.850 21.473 130.714 1.00 19.72 ? 209  LEU A CG  1 
ATOM   800  C  CD1 . LEU A 1 104 ? 65.072 20.004 130.986 1.00 18.15 ? 209  LEU A CD1 1 
ATOM   801  C  CD2 . LEU A 1 104 ? 64.947 22.273 132.008 1.00 18.92 ? 209  LEU A CD2 1 
ATOM   802  N  N   . TRP A 1 105 ? 63.974 20.328 127.197 1.00 15.69 ? 210  TRP A N   1 
ATOM   803  C  CA  . TRP A 1 105 ? 62.678 20.347 126.531 1.00 14.68 ? 210  TRP A CA  1 
ATOM   804  C  C   . TRP A 1 105 ? 61.549 20.080 127.503 1.00 14.10 ? 210  TRP A C   1 
ATOM   805  O  O   . TRP A 1 105 ? 61.614 19.147 128.301 1.00 12.40 ? 210  TRP A O   1 
ATOM   806  C  CB  . TRP A 1 105 ? 62.628 19.319 125.384 1.00 12.69 ? 210  TRP A CB  1 
ATOM   807  C  CG  . TRP A 1 105 ? 63.520 19.686 124.252 1.00 14.19 ? 210  TRP A CG  1 
ATOM   808  C  CD1 . TRP A 1 105 ? 64.688 19.072 123.893 1.00 15.08 ? 210  TRP A CD1 1 
ATOM   809  C  CD2 . TRP A 1 105 ? 63.396 20.834 123.402 1.00 14.74 ? 210  TRP A CD2 1 
ATOM   810  N  NE1 . TRP A 1 105 ? 65.302 19.770 122.885 1.00 15.30 ? 210  TRP A NE1 1 
ATOM   811  C  CE2 . TRP A 1 105 ? 64.531 20.855 122.562 1.00 13.82 ? 210  TRP A CE2 1 
ATOM   812  C  CE3 . TRP A 1 105 ? 62.438 21.850 123.273 1.00 13.00 ? 210  TRP A CE3 1 
ATOM   813  C  CZ2 . TRP A 1 105 ? 64.736 21.854 121.605 1.00 12.58 ? 210  TRP A CZ2 1 
ATOM   814  C  CZ3 . TRP A 1 105 ? 62.646 22.845 122.319 1.00 11.89 ? 210  TRP A CZ3 1 
ATOM   815  C  CH2 . TRP A 1 105 ? 63.787 22.837 121.499 1.00 10.54 ? 210  TRP A CH2 1 
ATOM   816  N  N   . SER A 1 106 ? 60.504 20.897 127.406 1.00 13.94 ? 211  SER A N   1 
ATOM   817  C  CA  . SER A 1 106 ? 59.347 20.791 128.272 1.00 13.15 ? 211  SER A CA  1 
ATOM   818  C  C   . SER A 1 106 ? 58.102 21.243 127.505 1.00 15.84 ? 211  SER A C   1 
ATOM   819  O  O   . SER A 1 106 ? 58.080 21.195 126.280 1.00 17.08 ? 211  SER A O   1 
ATOM   820  C  CB  . SER A 1 106 ? 59.568 21.682 129.492 1.00 14.15 ? 211  SER A CB  1 
ATOM   821  O  OG  . SER A 1 106 ? 58.635 21.392 130.505 1.00 17.46 ? 211  SER A OG  1 
ATOM   822  N  N   . LEU A 1 107 ? 57.068 21.667 128.233 1.00 15.21 ? 212  LEU A N   1 
ATOM   823  C  CA  . LEU A 1 107 ? 55.819 22.160 127.645 1.00 13.96 ? 212  LEU A CA  1 
ATOM   824  C  C   . LEU A 1 107 ? 55.180 23.125 128.635 1.00 17.00 ? 212  LEU A C   1 
ATOM   825  O  O   . LEU A 1 107 ? 55.367 22.992 129.837 1.00 19.75 ? 212  LEU A O   1 
ATOM   826  C  CB  . LEU A 1 107 ? 54.836 21.018 127.391 1.00 10.99 ? 212  LEU A CB  1 
ATOM   827  C  CG  . LEU A 1 107 ? 55.168 19.921 126.378 1.00 11.66 ? 212  LEU A CG  1 
ATOM   828  C  CD1 . LEU A 1 107 ? 54.139 18.817 126.510 1.00 8.67  ? 212  LEU A CD1 1 
ATOM   829  C  CD2 . LEU A 1 107 ? 55.202 20.494 124.967 1.00 7.27  ? 212  LEU A CD2 1 
ATOM   830  N  N   . GLY A 1 108 ? 54.421 24.088 128.132 1.00 19.26 ? 213  GLY A N   1 
ATOM   831  C  CA  . GLY A 1 108 ? 53.748 25.037 129.003 1.00 20.32 ? 213  GLY A CA  1 
ATOM   832  C  C   . GLY A 1 108 ? 54.639 26.040 129.713 1.00 19.73 ? 213  GLY A C   1 
ATOM   833  O  O   . GLY A 1 108 ? 55.759 26.294 129.285 1.00 20.34 ? 213  GLY A O   1 
ATOM   834  N  N   . LYS A 1 109 ? 54.123 26.618 130.795 1.00 20.81 ? 214  LYS A N   1 
ATOM   835  C  CA  . LYS A 1 109 ? 54.861 27.597 131.588 1.00 21.44 ? 214  LYS A CA  1 
ATOM   836  C  C   . LYS A 1 109 ? 55.917 26.863 132.398 1.00 21.38 ? 214  LYS A C   1 
ATOM   837  O  O   . LYS A 1 109 ? 55.743 25.688 132.729 1.00 22.09 ? 214  LYS A O   1 
ATOM   838  C  CB  . LYS A 1 109 ? 53.909 28.339 132.537 1.00 23.26 ? 214  LYS A CB  1 
ATOM   839  C  CG  . LYS A 1 109 ? 52.925 29.266 131.838 1.00 25.72 ? 214  LYS A CG  1 
ATOM   840  C  CD  . LYS A 1 109 ? 51.935 29.898 132.805 1.00 27.35 ? 214  LYS A CD  1 
ATOM   841  C  CE  . LYS A 1 109 ? 51.002 28.859 133.402 1.00 30.75 ? 214  LYS A CE  1 
ATOM   842  N  NZ  . LYS A 1 109 ? 49.866 29.485 134.138 1.00 35.19 ? 214  LYS A NZ  1 
ATOM   843  N  N   . GLY A 1 110 ? 57.008 27.548 132.721 1.00 19.58 ? 215  GLY A N   1 
ATOM   844  C  CA  . GLY A 1 110 ? 58.061 26.911 133.491 1.00 20.65 ? 215  GLY A CA  1 
ATOM   845  C  C   . GLY A 1 110 ? 59.403 27.007 132.798 1.00 20.80 ? 215  GLY A C   1 
ATOM   846  O  O   . GLY A 1 110 ? 59.496 27.528 131.689 1.00 20.47 ? 215  GLY A O   1 
ATOM   847  N  N   . GLN A 1 111 ? 60.449 26.500 133.439 1.00 21.31 ? 391  GLN A N   1 
ATOM   848  C  CA  . GLN A 1 111 ? 61.779 26.564 132.848 1.00 22.25 ? 391  GLN A CA  1 
ATOM   849  C  C   . GLN A 1 111 ? 61.886 25.585 131.676 1.00 20.85 ? 391  GLN A C   1 
ATOM   850  O  O   . GLN A 1 111 ? 61.097 24.654 131.561 1.00 20.10 ? 391  GLN A O   1 
ATOM   851  C  CB  . GLN A 1 111 ? 62.851 26.279 133.917 1.00 26.72 ? 391  GLN A CB  1 
ATOM   852  C  CG  . GLN A 1 111 ? 63.213 24.832 134.110 1.00 34.22 ? 391  GLN A CG  1 
ATOM   853  C  CD  . GLN A 1 111 ? 62.000 23.953 134.238 1.00 41.18 ? 391  GLN A CD  1 
ATOM   854  O  OE1 . GLN A 1 111 ? 61.117 24.211 135.054 1.00 48.75 ? 391  GLN A OE1 1 
ATOM   855  N  NE2 . GLN A 1 111 ? 61.944 22.903 133.427 1.00 46.74 ? 391  GLN A NE2 1 
ATOM   856  N  N   . GLY A 1 112 ? 62.866 25.794 130.808 1.00 19.12 ? 392  GLY A N   1 
ATOM   857  C  CA  . GLY A 1 112 ? 63.005 24.931 129.653 1.00 20.95 ? 392  GLY A CA  1 
ATOM   858  C  C   . GLY A 1 112 ? 62.266 25.565 128.487 1.00 19.62 ? 392  GLY A C   1 
ATOM   859  O  O   . GLY A 1 112 ? 61.669 26.627 128.637 1.00 17.25 ? 392  GLY A O   1 
ATOM   860  N  N   . TYR A 1 113 ? 62.301 24.921 127.328 1.00 19.08 ? 393  TYR A N   1 
ATOM   861  C  CA  . TYR A 1 113 ? 61.637 25.454 126.141 1.00 17.64 ? 393  TYR A CA  1 
ATOM   862  C  C   . TYR A 1 113 ? 60.474 24.563 125.714 1.00 16.46 ? 393  TYR A C   1 
ATOM   863  O  O   . TYR A 1 113 ? 60.552 23.343 125.812 1.00 18.48 ? 393  TYR A O   1 
ATOM   864  C  CB  . TYR A 1 113 ? 62.646 25.560 125.000 1.00 18.65 ? 393  TYR A CB  1 
ATOM   865  C  CG  . TYR A 1 113 ? 63.773 26.534 125.256 1.00 18.22 ? 393  TYR A CG  1 
ATOM   866  C  CD1 . TYR A 1 113 ? 63.586 27.905 125.079 1.00 19.12 ? 393  TYR A CD1 1 
ATOM   867  C  CD2 . TYR A 1 113 ? 65.036 26.084 125.660 1.00 18.43 ? 393  TYR A CD2 1 
ATOM   868  C  CE1 . TYR A 1 113 ? 64.626 28.807 125.291 1.00 20.27 ? 393  TYR A CE1 1 
ATOM   869  C  CE2 . TYR A 1 113 ? 66.091 26.980 125.878 1.00 18.43 ? 393  TYR A CE2 1 
ATOM   870  C  CZ  . TYR A 1 113 ? 65.879 28.339 125.691 1.00 20.99 ? 393  TYR A CZ  1 
ATOM   871  O  OH  . TYR A 1 113 ? 66.911 29.229 125.892 1.00 18.81 ? 393  TYR A OH  1 
ATOM   872  N  N   . SER A 1 114 ? 59.393 25.165 125.238 1.00 16.19 ? 394  SER A N   1 
ATOM   873  C  CA  . SER A 1 114 ? 58.248 24.376 124.799 1.00 16.88 ? 394  SER A CA  1 
ATOM   874  C  C   . SER A 1 114 ? 58.555 23.638 123.501 1.00 16.05 ? 394  SER A C   1 
ATOM   875  O  O   . SER A 1 114 ? 58.781 24.262 122.468 1.00 17.59 ? 394  SER A O   1 
ATOM   876  C  CB  . SER A 1 114 ? 57.026 25.268 124.581 1.00 15.95 ? 394  SER A CB  1 
ATOM   877  O  OG  . SER A 1 114 ? 55.900 24.491 124.195 1.00 16.81 ? 394  SER A OG  1 
ATOM   878  N  N   . LEU A 1 115 ? 58.563 22.311 123.557 1.00 13.28 ? 395  LEU A N   1 
ATOM   879  C  CA  . LEU A 1 115 ? 58.825 21.508 122.373 1.00 13.52 ? 395  LEU A CA  1 
ATOM   880  C  C   . LEU A 1 115 ? 57.720 21.758 121.345 1.00 13.87 ? 395  LEU A C   1 
ATOM   881  O  O   . LEU A 1 115 ? 57.979 21.792 120.149 1.00 15.88 ? 395  LEU A O   1 
ATOM   882  C  CB  . LEU A 1 115 ? 58.874 20.022 122.734 1.00 9.81  ? 395  LEU A CB  1 
ATOM   883  C  CG  . LEU A 1 115 ? 59.158 19.078 121.559 1.00 10.42 ? 395  LEU A CG  1 
ATOM   884  C  CD1 . LEU A 1 115 ? 60.518 19.417 120.974 1.00 8.66  ? 395  LEU A CD1 1 
ATOM   885  C  CD2 . LEU A 1 115 ? 59.117 17.618 122.012 1.00 7.01  ? 395  LEU A CD2 1 
ATOM   886  N  N   . PHE A 1 116 ? 56.495 21.936 121.836 1.00 13.30 ? 396  PHE A N   1 
ATOM   887  C  CA  . PHE A 1 116 ? 55.319 22.195 121.010 1.00 13.78 ? 396  PHE A CA  1 
ATOM   888  C  C   . PHE A 1 116 ? 55.440 23.476 120.178 1.00 15.62 ? 396  PHE A C   1 
ATOM   889  O  O   . PHE A 1 116 ? 55.242 23.455 118.958 1.00 15.38 ? 396  PHE A O   1 
ATOM   890  C  CB  . PHE A 1 116 ? 54.069 22.270 121.907 1.00 14.03 ? 396  PHE A CB  1 
ATOM   891  C  CG  . PHE A 1 116 ? 52.850 22.840 121.225 1.00 15.47 ? 396  PHE A CG  1 
ATOM   892  C  CD1 . PHE A 1 116 ? 52.243 22.168 120.167 1.00 16.74 ? 396  PHE A CD1 1 
ATOM   893  C  CD2 . PHE A 1 116 ? 52.322 24.064 121.632 1.00 16.39 ? 396  PHE A CD2 1 
ATOM   894  C  CE1 . PHE A 1 116 ? 51.128 22.706 119.518 1.00 15.98 ? 396  PHE A CE1 1 
ATOM   895  C  CE2 . PHE A 1 116 ? 51.211 24.611 120.993 1.00 17.97 ? 396  PHE A CE2 1 
ATOM   896  C  CZ  . PHE A 1 116 ? 50.611 23.929 119.929 1.00 16.67 ? 396  PHE A CZ  1 
ATOM   897  N  N   . LEU A 1 117 ? 55.756 24.587 120.837 1.00 14.66 ? 397  LEU A N   1 
ATOM   898  C  CA  . LEU A 1 117 ? 55.892 25.861 120.148 1.00 14.57 ? 397  LEU A CA  1 
ATOM   899  C  C   . LEU A 1 117 ? 57.084 25.912 119.202 1.00 16.31 ? 397  LEU A C   1 
ATOM   900  O  O   . LEU A 1 117 ? 57.002 26.511 118.132 1.00 18.67 ? 397  LEU A O   1 
ATOM   901  C  CB  . LEU A 1 117 ? 55.998 27.009 121.155 1.00 16.23 ? 397  LEU A CB  1 
ATOM   902  C  CG  . LEU A 1 117 ? 54.739 27.366 121.951 1.00 19.61 ? 397  LEU A CG  1 
ATOM   903  C  CD1 . LEU A 1 117 ? 55.033 28.532 122.908 1.00 17.04 ? 397  LEU A CD1 1 
ATOM   904  C  CD2 . LEU A 1 117 ? 53.615 27.734 120.982 1.00 18.70 ? 397  LEU A CD2 1 
ATOM   905  N  N   . VAL A 1 118 ? 58.198 25.299 119.591 1.00 17.18 ? 398  VAL A N   1 
ATOM   906  C  CA  . VAL A 1 118 ? 59.379 25.309 118.738 1.00 16.87 ? 398  VAL A CA  1 
ATOM   907  C  C   . VAL A 1 118 ? 59.157 24.410 117.524 1.00 17.35 ? 398  VAL A C   1 
ATOM   908  O  O   . VAL A 1 118 ? 59.610 24.715 116.427 1.00 16.12 ? 398  VAL A O   1 
ATOM   909  C  CB  . VAL A 1 118 ? 60.643 24.855 119.513 1.00 15.03 ? 398  VAL A CB  1 
ATOM   910  C  CG1 . VAL A 1 118 ? 61.838 24.750 118.562 1.00 7.55  ? 398  VAL A CG1 1 
ATOM   911  C  CG2 . VAL A 1 118 ? 60.953 25.867 120.636 1.00 13.62 ? 398  VAL A CG2 1 
ATOM   912  N  N   . ALA A 1 119 ? 58.446 23.307 117.725 1.00 17.18 ? 399  ALA A N   1 
ATOM   913  C  CA  . ALA A 1 119 ? 58.159 22.386 116.629 1.00 18.10 ? 399  ALA A CA  1 
ATOM   914  C  C   . ALA A 1 119 ? 57.296 23.084 115.583 1.00 16.31 ? 399  ALA A C   1 
ATOM   915  O  O   . ALA A 1 119 ? 57.540 22.962 114.387 1.00 17.90 ? 399  ALA A O   1 
ATOM   916  C  CB  . ALA A 1 119 ? 57.440 21.146 117.155 1.00 17.14 ? 399  ALA A CB  1 
ATOM   917  N  N   . ALA A 1 120 ? 56.288 23.814 116.048 1.00 16.32 ? 400  ALA A N   1 
ATOM   918  C  CA  . ALA A 1 120 ? 55.385 24.531 115.161 1.00 16.53 ? 400  ALA A CA  1 
ATOM   919  C  C   . ALA A 1 120 ? 56.162 25.495 114.278 1.00 17.89 ? 400  ALA A C   1 
ATOM   920  O  O   . ALA A 1 120 ? 55.859 25.640 113.101 1.00 18.21 ? 400  ALA A O   1 
ATOM   921  C  CB  . ALA A 1 120 ? 54.340 25.283 115.970 1.00 11.88 ? 400  ALA A CB  1 
ATOM   922  N  N   . HIS A 1 121 ? 57.169 26.142 114.858 1.00 18.94 ? 401  HIS A N   1 
ATOM   923  C  CA  . HIS A 1 121 ? 58.009 27.094 114.140 1.00 16.00 ? 401  HIS A CA  1 
ATOM   924  C  C   . HIS A 1 121 ? 58.849 26.371 113.091 1.00 17.48 ? 401  HIS A C   1 
ATOM   925  O  O   . HIS A 1 121 ? 58.899 26.785 111.939 1.00 17.04 ? 401  HIS A O   1 
ATOM   926  C  CB  . HIS A 1 121 ? 58.934 27.812 115.123 1.00 15.08 ? 401  HIS A CB  1 
ATOM   927  C  CG  . HIS A 1 121 ? 59.800 28.858 114.490 1.00 16.72 ? 401  HIS A CG  1 
ATOM   928  N  ND1 . HIS A 1 121 ? 59.400 30.169 114.344 1.00 16.08 ? 401  HIS A ND1 1 
ATOM   929  C  CD2 . HIS A 1 121 ? 61.049 28.788 113.972 1.00 11.82 ? 401  HIS A CD2 1 
ATOM   930  C  CE1 . HIS A 1 121 ? 60.367 30.860 113.767 1.00 16.27 ? 401  HIS A CE1 1 
ATOM   931  N  NE2 . HIS A 1 121 ? 61.377 30.045 113.531 1.00 10.47 ? 401  HIS A NE2 1 
ATOM   932  N  N   . GLU A 1 122 ? 59.512 25.292 113.497 1.00 16.98 ? 402  GLU A N   1 
ATOM   933  C  CA  . GLU A 1 122 ? 60.346 24.523 112.583 1.00 19.94 ? 402  GLU A CA  1 
ATOM   934  C  C   . GLU A 1 122 ? 59.522 23.952 111.432 1.00 20.70 ? 402  GLU A C   1 
ATOM   935  O  O   . GLU A 1 122 ? 59.961 23.972 110.285 1.00 20.70 ? 402  GLU A O   1 
ATOM   936  C  CB  . GLU A 1 122 ? 61.058 23.374 113.311 1.00 20.34 ? 402  GLU A CB  1 
ATOM   937  C  CG  . GLU A 1 122 ? 62.029 23.804 114.410 1.00 20.68 ? 402  GLU A CG  1 
ATOM   938  C  CD  . GLU A 1 122 ? 62.758 25.100 114.095 1.00 17.45 ? 402  GLU A CD  1 
ATOM   939  O  OE1 . GLU A 1 122 ? 63.300 25.234 112.987 1.00 18.70 ? 402  GLU A OE1 1 
ATOM   940  O  OE2 . GLU A 1 122 ? 62.793 25.984 114.967 1.00 17.38 ? 402  GLU A OE2 1 
ATOM   941  N  N   . PHE A 1 123 ? 58.336 23.437 111.735 1.00 20.02 ? 403  PHE A N   1 
ATOM   942  C  CA  . PHE A 1 123 ? 57.482 22.889 110.691 1.00 20.64 ? 403  PHE A CA  1 
ATOM   943  C  C   . PHE A 1 123 ? 57.040 23.998 109.732 1.00 20.93 ? 403  PHE A C   1 
ATOM   944  O  O   . PHE A 1 123 ? 56.699 23.728 108.587 1.00 20.08 ? 403  PHE A O   1 
ATOM   945  C  CB  . PHE A 1 123 ? 56.262 22.184 111.293 1.00 20.51 ? 403  PHE A CB  1 
ATOM   946  C  CG  . PHE A 1 123 ? 56.608 21.005 112.173 1.00 20.43 ? 403  PHE A CG  1 
ATOM   947  C  CD1 . PHE A 1 123 ? 57.865 20.398 112.094 1.00 17.64 ? 403  PHE A CD1 1 
ATOM   948  C  CD2 . PHE A 1 123 ? 55.678 20.509 113.087 1.00 14.31 ? 403  PHE A CD2 1 
ATOM   949  C  CE1 . PHE A 1 123 ? 58.192 19.319 112.916 1.00 18.71 ? 403  PHE A CE1 1 
ATOM   950  C  CE2 . PHE A 1 123 ? 55.988 19.424 113.918 1.00 12.75 ? 403  PHE A CE2 1 
ATOM   951  C  CZ  . PHE A 1 123 ? 57.243 18.826 113.838 1.00 15.90 ? 403  PHE A CZ  1 
ATOM   952  N  N   . GLY A 1 124 ? 57.041 25.241 110.208 1.00 20.24 ? 404  GLY A N   1 
ATOM   953  C  CA  . GLY A 1 124 ? 56.685 26.355 109.352 1.00 18.45 ? 404  GLY A CA  1 
ATOM   954  C  C   . GLY A 1 124 ? 57.748 26.442 108.263 1.00 19.06 ? 404  GLY A C   1 
ATOM   955  O  O   . GLY A 1 124 ? 57.438 26.584 107.082 1.00 18.85 ? 404  GLY A O   1 
ATOM   956  N  N   . HIS A 1 125 ? 59.011 26.353 108.666 1.00 17.32 ? 405  HIS A N   1 
ATOM   957  C  CA  . HIS A 1 125 ? 60.119 26.382 107.718 1.00 18.09 ? 405  HIS A CA  1 
ATOM   958  C  C   . HIS A 1 125 ? 60.040 25.195 106.761 1.00 18.79 ? 405  HIS A C   1 
ATOM   959  O  O   . HIS A 1 125 ? 60.171 25.352 105.554 1.00 22.20 ? 405  HIS A O   1 
ATOM   960  C  CB  . HIS A 1 125 ? 61.460 26.317 108.446 1.00 15.13 ? 405  HIS A CB  1 
ATOM   961  C  CG  . HIS A 1 125 ? 61.859 27.600 109.095 1.00 19.30 ? 405  HIS A CG  1 
ATOM   962  N  ND1 . HIS A 1 125 ? 61.769 28.816 108.452 1.00 18.08 ? 405  HIS A ND1 1 
ATOM   963  C  CD2 . HIS A 1 125 ? 62.362 27.859 110.323 1.00 15.40 ? 405  HIS A CD2 1 
ATOM   964  C  CE1 . HIS A 1 125 ? 62.197 29.769 109.258 1.00 17.34 ? 405  HIS A CE1 1 
ATOM   965  N  NE2 . HIS A 1 125 ? 62.563 29.214 110.399 1.00 18.40 ? 405  HIS A NE2 1 
ATOM   966  N  N   . ALA A 1 126 ? 59.838 24.007 107.320 1.00 18.37 ? 406  ALA A N   1 
ATOM   967  C  CA  . ALA A 1 126 ? 59.754 22.780 106.545 1.00 17.99 ? 406  ALA A CA  1 
ATOM   968  C  C   . ALA A 1 126 ? 58.665 22.838 105.468 1.00 17.88 ? 406  ALA A C   1 
ATOM   969  O  O   . ALA A 1 126 ? 58.673 22.045 104.535 1.00 15.94 ? 406  ALA A O   1 
ATOM   970  C  CB  . ALA A 1 126 ? 59.511 21.606 107.484 1.00 15.77 ? 406  ALA A CB  1 
ATOM   971  N  N   . LEU A 1 127 ? 57.730 23.773 105.612 1.00 20.32 ? 407  LEU A N   1 
ATOM   972  C  CA  . LEU A 1 127 ? 56.646 23.935 104.647 1.00 22.45 ? 407  LEU A CA  1 
ATOM   973  C  C   . LEU A 1 127 ? 56.921 25.103 103.694 1.00 23.47 ? 407  LEU A C   1 
ATOM   974  O  O   . LEU A 1 127 ? 56.093 25.422 102.844 1.00 23.57 ? 407  LEU A O   1 
ATOM   975  C  CB  . LEU A 1 127 ? 55.307 24.158 105.367 1.00 21.52 ? 407  LEU A CB  1 
ATOM   976  C  CG  . LEU A 1 127 ? 54.789 23.030 106.266 1.00 22.77 ? 407  LEU A CG  1 
ATOM   977  C  CD1 . LEU A 1 127 ? 53.461 23.421 106.888 1.00 19.54 ? 407  LEU A CD1 1 
ATOM   978  C  CD2 . LEU A 1 127 ? 54.629 21.766 105.447 1.00 25.90 ? 407  LEU A CD2 1 
ATOM   979  N  N   . GLY A 1 128 ? 58.077 25.743 103.852 1.00 22.90 ? 408  GLY A N   1 
ATOM   980  C  CA  . GLY A 1 128 ? 58.444 26.847 102.983 1.00 23.36 ? 408  GLY A CA  1 
ATOM   981  C  C   . GLY A 1 128 ? 58.411 28.268 103.528 1.00 24.25 ? 408  GLY A C   1 
ATOM   982  O  O   . GLY A 1 128 ? 58.891 29.190 102.868 1.00 22.84 ? 408  GLY A O   1 
ATOM   983  N  N   . LEU A 1 129 ? 57.855 28.463 104.719 1.00 25.11 ? 409  LEU A N   1 
ATOM   984  C  CA  . LEU A 1 129 ? 57.777 29.804 105.290 1.00 24.70 ? 409  LEU A CA  1 
ATOM   985  C  C   . LEU A 1 129 ? 59.123 30.347 105.711 1.00 25.87 ? 409  LEU A C   1 
ATOM   986  O  O   . LEU A 1 129 ? 59.989 29.598 106.156 1.00 26.76 ? 409  LEU A O   1 
ATOM   987  C  CB  . LEU A 1 129 ? 56.853 29.828 106.508 1.00 22.64 ? 409  LEU A CB  1 
ATOM   988  C  CG  . LEU A 1 129 ? 55.352 29.682 106.281 1.00 25.21 ? 409  LEU A CG  1 
ATOM   989  C  CD1 . LEU A 1 129 ? 54.639 29.943 107.588 1.00 21.69 ? 409  LEU A CD1 1 
ATOM   990  C  CD2 . LEU A 1 129 ? 54.880 30.664 105.212 1.00 24.00 ? 409  LEU A CD2 1 
ATOM   991  N  N   . ASP A 1 130 ? 59.294 31.656 105.558 1.00 27.29 ? 410  ASP A N   1 
ATOM   992  C  CA  . ASP A 1 130 ? 60.517 32.323 105.980 1.00 29.12 ? 410  ASP A CA  1 
ATOM   993  C  C   . ASP A 1 130 ? 60.188 33.050 107.289 1.00 27.33 ? 410  ASP A C   1 
ATOM   994  O  O   . ASP A 1 130 ? 59.046 33.026 107.751 1.00 19.85 ? 410  ASP A O   1 
ATOM   995  C  CB  . ASP A 1 130 ? 60.990 33.338 104.933 1.00 34.79 ? 410  ASP A CB  1 
ATOM   996  C  CG  . ASP A 1 130 ? 61.553 32.678 103.687 1.00 42.97 ? 410  ASP A CG  1 
ATOM   997  O  OD1 . ASP A 1 130 ? 62.184 31.602 103.799 1.00 48.11 ? 410  ASP A OD1 1 
ATOM   998  O  OD2 . ASP A 1 130 ? 61.381 33.247 102.590 1.00 47.38 ? 410  ASP A OD2 1 
ATOM   999  N  N   . HIS A 1 131 ? 61.190 33.687 107.883 1.00 25.92 ? 411  HIS A N   1 
ATOM   1000 C  CA  . HIS A 1 131 ? 60.995 34.418 109.128 1.00 27.93 ? 411  HIS A CA  1 
ATOM   1001 C  C   . HIS A 1 131 ? 60.103 35.634 108.947 1.00 28.39 ? 411  HIS A C   1 
ATOM   1002 O  O   . HIS A 1 131 ? 60.096 36.257 107.890 1.00 27.54 ? 411  HIS A O   1 
ATOM   1003 C  CB  . HIS A 1 131 ? 62.345 34.843 109.699 1.00 25.18 ? 411  HIS A CB  1 
ATOM   1004 C  CG  . HIS A 1 131 ? 63.056 33.747 110.430 1.00 25.67 ? 411  HIS A CG  1 
ATOM   1005 N  ND1 . HIS A 1 131 ? 64.429 33.660 110.493 1.00 24.52 ? 411  HIS A ND1 1 
ATOM   1006 C  CD2 . HIS A 1 131 ? 62.579 32.692 111.134 1.00 22.64 ? 411  HIS A CD2 1 
ATOM   1007 C  CE1 . HIS A 1 131 ? 64.768 32.596 111.199 1.00 24.55 ? 411  HIS A CE1 1 
ATOM   1008 N  NE2 . HIS A 1 131 ? 63.664 31.992 111.598 1.00 21.02 ? 411  HIS A NE2 1 
ATOM   1009 N  N   . SER A 1 132 ? 59.348 35.953 109.992 1.00 28.70 ? 412  SER A N   1 
ATOM   1010 C  CA  . SER A 1 132 ? 58.441 37.090 109.989 1.00 28.94 ? 412  SER A CA  1 
ATOM   1011 C  C   . SER A 1 132 ? 59.090 38.264 110.708 1.00 30.69 ? 412  SER A C   1 
ATOM   1012 O  O   . SER A 1 132 ? 60.020 38.081 111.489 1.00 31.96 ? 412  SER A O   1 
ATOM   1013 C  CB  . SER A 1 132 ? 57.139 36.716 110.696 1.00 27.79 ? 412  SER A CB  1 
ATOM   1014 O  OG  . SER A 1 132 ? 56.288 37.836 110.831 1.00 28.82 ? 412  SER A OG  1 
ATOM   1015 N  N   . SER A 1 133 ? 58.601 39.468 110.437 1.00 30.98 ? 413  SER A N   1 
ATOM   1016 C  CA  . SER A 1 133 ? 59.132 40.664 111.075 1.00 33.39 ? 413  SER A CA  1 
ATOM   1017 C  C   . SER A 1 133 ? 58.175 41.125 112.166 1.00 32.91 ? 413  SER A C   1 
ATOM   1018 O  O   . SER A 1 133 ? 58.454 42.076 112.893 1.00 35.58 ? 413  SER A O   1 
ATOM   1019 C  CB  . SER A 1 133 ? 59.334 41.775 110.039 1.00 34.31 ? 413  SER A CB  1 
ATOM   1020 O  OG  . SER A 1 133 ? 58.154 42.003 109.294 1.00 35.39 ? 413  SER A OG  1 
ATOM   1021 N  N   . VAL A 1 134 ? 57.043 40.436 112.264 1.00 31.58 ? 414  VAL A N   1 
ATOM   1022 C  CA  . VAL A 1 134 ? 56.023 40.725 113.264 1.00 31.56 ? 414  VAL A CA  1 
ATOM   1023 C  C   . VAL A 1 134 ? 56.399 40.007 114.564 1.00 31.65 ? 414  VAL A C   1 
ATOM   1024 O  O   . VAL A 1 134 ? 56.415 38.778 114.630 1.00 30.34 ? 414  VAL A O   1 
ATOM   1025 C  CB  . VAL A 1 134 ? 54.637 40.234 112.792 1.00 31.76 ? 414  VAL A CB  1 
ATOM   1026 C  CG1 . VAL A 1 134 ? 53.578 40.582 113.816 1.00 31.52 ? 414  VAL A CG1 1 
ATOM   1027 C  CG2 . VAL A 1 134 ? 54.304 40.849 111.455 1.00 30.36 ? 414  VAL A CG2 1 
ATOM   1028 N  N   . PRO A 1 135 ? 56.696 40.775 115.620 1.00 31.44 ? 415  PRO A N   1 
ATOM   1029 C  CA  . PRO A 1 135 ? 57.080 40.220 116.920 1.00 28.81 ? 415  PRO A CA  1 
ATOM   1030 C  C   . PRO A 1 135 ? 56.156 39.157 117.503 1.00 26.99 ? 415  PRO A C   1 
ATOM   1031 O  O   . PRO A 1 135 ? 56.626 38.199 118.098 1.00 26.82 ? 415  PRO A O   1 
ATOM   1032 C  CB  . PRO A 1 135 ? 57.176 41.461 117.802 1.00 29.00 ? 415  PRO A CB  1 
ATOM   1033 C  CG  . PRO A 1 135 ? 57.628 42.513 116.837 1.00 27.34 ? 415  PRO A CG  1 
ATOM   1034 C  CD  . PRO A 1 135 ? 56.730 42.248 115.656 1.00 29.01 ? 415  PRO A CD  1 
ATOM   1035 N  N   . GLU A 1 136 ? 54.849 39.316 117.336 1.00 28.55 ? 416  GLU A N   1 
ATOM   1036 C  CA  . GLU A 1 136 ? 53.907 38.343 117.881 1.00 29.16 ? 416  GLU A CA  1 
ATOM   1037 C  C   . GLU A 1 136 ? 53.612 37.163 116.957 1.00 28.85 ? 416  GLU A C   1 
ATOM   1038 O  O   . GLU A 1 136 ? 52.820 36.289 117.297 1.00 30.41 ? 416  GLU A O   1 
ATOM   1039 C  CB  . GLU A 1 136 ? 52.597 39.029 118.276 1.00 33.01 ? 416  GLU A CB  1 
ATOM   1040 C  CG  . GLU A 1 136 ? 52.180 40.147 117.341 1.00 42.66 ? 416  GLU A CG  1 
ATOM   1041 C  CD  . GLU A 1 136 ? 52.947 41.437 117.590 1.00 43.72 ? 416  GLU A CD  1 
ATOM   1042 O  OE1 . GLU A 1 136 ? 53.148 42.204 116.626 1.00 43.99 ? 416  GLU A OE1 1 
ATOM   1043 O  OE2 . GLU A 1 136 ? 53.336 41.690 118.752 1.00 46.02 ? 416  GLU A OE2 1 
ATOM   1044 N  N   . ALA A 1 137 ? 54.257 37.125 115.798 1.00 26.45 ? 417  ALA A N   1 
ATOM   1045 C  CA  . ALA A 1 137 ? 54.037 36.029 114.867 1.00 24.95 ? 417  ALA A CA  1 
ATOM   1046 C  C   . ALA A 1 137 ? 54.868 34.826 115.303 1.00 24.52 ? 417  ALA A C   1 
ATOM   1047 O  O   . ALA A 1 137 ? 55.952 34.986 115.861 1.00 23.59 ? 417  ALA A O   1 
ATOM   1048 C  CB  . ALA A 1 137 ? 54.429 36.452 113.456 1.00 23.05 ? 417  ALA A CB  1 
ATOM   1049 N  N   . LEU A 1 138 ? 54.354 33.625 115.049 1.00 22.60 ? 418  LEU A N   1 
ATOM   1050 C  CA  . LEU A 1 138 ? 55.060 32.399 115.396 1.00 21.25 ? 418  LEU A CA  1 
ATOM   1051 C  C   . LEU A 1 138 ? 56.378 32.281 114.639 1.00 20.33 ? 418  LEU A C   1 
ATOM   1052 O  O   . LEU A 1 138 ? 57.336 31.699 115.139 1.00 17.86 ? 418  LEU A O   1 
ATOM   1053 C  CB  . LEU A 1 138 ? 54.186 31.183 115.084 1.00 24.09 ? 418  LEU A CB  1 
ATOM   1054 C  CG  . LEU A 1 138 ? 54.819 29.794 115.255 1.00 25.61 ? 418  LEU A CG  1 
ATOM   1055 C  CD1 . LEU A 1 138 ? 55.205 29.584 116.704 1.00 24.01 ? 418  LEU A CD1 1 
ATOM   1056 C  CD2 . LEU A 1 138 ? 53.851 28.711 114.802 1.00 24.22 ? 418  LEU A CD2 1 
ATOM   1057 N  N   . MET A 1 139 ? 56.425 32.836 113.431 1.00 20.15 ? 419  MET A N   1 
ATOM   1058 C  CA  . MET A 1 139 ? 57.632 32.763 112.620 1.00 20.11 ? 419  MET A CA  1 
ATOM   1059 C  C   . MET A 1 139 ? 58.678 33.816 112.953 1.00 20.18 ? 419  MET A C   1 
ATOM   1060 O  O   . MET A 1 139 ? 59.679 33.946 112.256 1.00 20.02 ? 419  MET A O   1 
ATOM   1061 C  CB  . MET A 1 139 ? 57.286 32.817 111.130 1.00 19.41 ? 419  MET A CB  1 
ATOM   1062 C  CG  . MET A 1 139 ? 56.562 31.575 110.616 1.00 18.20 ? 419  MET A CG  1 
ATOM   1063 S  SD  . MET A 1 139 ? 57.267 29.973 111.160 1.00 18.41 ? 419  MET A SD  1 
ATOM   1064 C  CE  . MET A 1 139 ? 58.852 29.969 110.370 1.00 13.77 ? 419  MET A CE  1 
ATOM   1065 N  N   . TYR A 1 140 ? 58.450 34.571 114.022 1.00 22.13 ? 420  TYR A N   1 
ATOM   1066 C  CA  . TYR A 1 140 ? 59.433 35.561 114.443 1.00 23.96 ? 420  TYR A CA  1 
ATOM   1067 C  C   . TYR A 1 140 ? 60.679 34.746 114.812 1.00 22.16 ? 420  TYR A C   1 
ATOM   1068 O  O   . TYR A 1 140 ? 60.583 33.744 115.515 1.00 20.07 ? 420  TYR A O   1 
ATOM   1069 C  CB  . TYR A 1 140 ? 58.921 36.336 115.653 1.00 28.74 ? 420  TYR A CB  1 
ATOM   1070 C  CG  . TYR A 1 140 ? 59.721 37.578 115.957 1.00 33.66 ? 420  TYR A CG  1 
ATOM   1071 C  CD1 . TYR A 1 140 ? 59.747 38.654 115.064 1.00 35.38 ? 420  TYR A CD1 1 
ATOM   1072 C  CD2 . TYR A 1 140 ? 60.464 37.674 117.128 1.00 35.51 ? 420  TYR A CD2 1 
ATOM   1073 C  CE1 . TYR A 1 140 ? 60.495 39.791 115.334 1.00 36.85 ? 420  TYR A CE1 1 
ATOM   1074 C  CE2 . TYR A 1 140 ? 61.215 38.804 117.409 1.00 38.35 ? 420  TYR A CE2 1 
ATOM   1075 C  CZ  . TYR A 1 140 ? 61.228 39.858 116.512 1.00 40.13 ? 420  TYR A CZ  1 
ATOM   1076 O  OH  . TYR A 1 140 ? 61.973 40.976 116.801 1.00 41.02 ? 420  TYR A OH  1 
ATOM   1077 N  N   . PRO A 1 141 ? 61.863 35.172 114.347 1.00 23.33 ? 421  PRO A N   1 
ATOM   1078 C  CA  . PRO A 1 141 ? 63.148 34.501 114.591 1.00 24.11 ? 421  PRO A CA  1 
ATOM   1079 C  C   . PRO A 1 141 ? 63.624 34.301 116.028 1.00 24.67 ? 421  PRO A C   1 
ATOM   1080 O  O   . PRO A 1 141 ? 64.649 33.659 116.258 1.00 23.19 ? 421  PRO A O   1 
ATOM   1081 C  CB  . PRO A 1 141 ? 64.129 35.342 113.773 1.00 24.83 ? 421  PRO A CB  1 
ATOM   1082 C  CG  . PRO A 1 141 ? 63.542 36.703 113.850 1.00 23.46 ? 421  PRO A CG  1 
ATOM   1083 C  CD  . PRO A 1 141 ? 62.072 36.447 113.634 1.00 24.71 ? 421  PRO A CD  1 
ATOM   1084 N  N   . MET A 1 142 ? 62.870 34.827 116.986 1.00 23.77 ? 422  MET A N   1 
ATOM   1085 C  CA  . MET A 1 142 ? 63.228 34.732 118.393 1.00 24.04 ? 422  MET A CA  1 
ATOM   1086 C  C   . MET A 1 142 ? 62.181 33.938 119.171 1.00 22.85 ? 422  MET A C   1 
ATOM   1087 O  O   . MET A 1 142 ? 60.983 34.062 118.915 1.00 21.77 ? 422  MET A O   1 
ATOM   1088 C  CB  . MET A 1 142 ? 63.351 36.148 118.961 1.00 29.95 ? 422  MET A CB  1 
ATOM   1089 C  CG  . MET A 1 142 ? 63.671 36.231 120.433 1.00 39.49 ? 422  MET A CG  1 
ATOM   1090 S  SD  . MET A 1 142 ? 63.479 37.927 121.034 1.00 49.06 ? 422  MET A SD  1 
ATOM   1091 C  CE  . MET A 1 142 ? 61.893 37.842 121.866 1.00 39.08 ? 422  MET A CE  1 
ATOM   1092 N  N   . TYR A 1 143 ? 62.626 33.117 120.114 1.00 19.77 ? 423  TYR A N   1 
ATOM   1093 C  CA  . TYR A 1 143 ? 61.699 32.324 120.913 1.00 21.78 ? 423  TYR A CA  1 
ATOM   1094 C  C   . TYR A 1 143 ? 60.964 33.168 121.950 1.00 23.28 ? 423  TYR A C   1 
ATOM   1095 O  O   . TYR A 1 143 ? 61.568 34.001 122.616 1.00 23.95 ? 423  TYR A O   1 
ATOM   1096 C  CB  . TYR A 1 143 ? 62.441 31.214 121.659 1.00 19.09 ? 423  TYR A CB  1 
ATOM   1097 C  CG  . TYR A 1 143 ? 61.551 30.425 122.599 1.00 18.13 ? 423  TYR A CG  1 
ATOM   1098 C  CD1 . TYR A 1 143 ? 60.797 29.344 122.139 1.00 18.66 ? 423  TYR A CD1 1 
ATOM   1099 C  CD2 . TYR A 1 143 ? 61.445 30.769 123.946 1.00 17.67 ? 423  TYR A CD2 1 
ATOM   1100 C  CE1 . TYR A 1 143 ? 59.962 28.623 122.996 1.00 16.35 ? 423  TYR A CE1 1 
ATOM   1101 C  CE2 . TYR A 1 143 ? 60.612 30.059 124.811 1.00 17.18 ? 423  TYR A CE2 1 
ATOM   1102 C  CZ  . TYR A 1 143 ? 59.874 28.987 124.330 1.00 19.92 ? 423  TYR A CZ  1 
ATOM   1103 O  OH  . TYR A 1 143 ? 59.053 28.278 125.182 1.00 18.58 ? 423  TYR A OH  1 
ATOM   1104 N  N   . ARG A 1 144 ? 59.662 32.942 122.087 1.00 25.46 ? 424  ARG A N   1 
ATOM   1105 C  CA  . ARG A 1 144 ? 58.869 33.651 123.084 1.00 31.01 ? 424  ARG A CA  1 
ATOM   1106 C  C   . ARG A 1 144 ? 57.690 32.777 123.499 1.00 29.80 ? 424  ARG A C   1 
ATOM   1107 O  O   . ARG A 1 144 ? 56.830 32.450 122.691 1.00 29.90 ? 424  ARG A O   1 
ATOM   1108 C  CB  . ARG A 1 144 ? 58.376 35.005 122.550 1.00 35.79 ? 424  ARG A CB  1 
ATOM   1109 C  CG  . ARG A 1 144 ? 57.230 34.932 121.573 1.00 43.60 ? 424  ARG A CG  1 
ATOM   1110 C  CD  . ARG A 1 144 ? 56.693 36.313 121.235 1.00 50.63 ? 424  ARG A CD  1 
ATOM   1111 N  NE  . ARG A 1 144 ? 55.481 36.228 120.420 1.00 58.11 ? 424  ARG A NE  1 
ATOM   1112 C  CZ  . ARG A 1 144 ? 54.340 35.676 120.828 1.00 62.35 ? 424  ARG A CZ  1 
ATOM   1113 N  NH1 . ARG A 1 144 ? 54.247 35.158 122.049 1.00 65.08 ? 424  ARG A NH1 1 
ATOM   1114 N  NH2 . ARG A 1 144 ? 53.291 35.634 120.015 1.00 62.97 ? 424  ARG A NH2 1 
ATOM   1115 N  N   . PHE A 1 145 ? 57.654 32.374 124.762 1.00 29.63 ? 425  PHE A N   1 
ATOM   1116 C  CA  . PHE A 1 145 ? 56.555 31.534 125.203 1.00 28.26 ? 425  PHE A CA  1 
ATOM   1117 C  C   . PHE A 1 145 ? 55.236 32.287 125.205 1.00 29.92 ? 425  PHE A C   1 
ATOM   1118 O  O   . PHE A 1 145 ? 55.177 33.475 125.525 1.00 32.27 ? 425  PHE A O   1 
ATOM   1119 C  CB  . PHE A 1 145 ? 56.807 30.963 126.596 1.00 24.65 ? 425  PHE A CB  1 
ATOM   1120 C  CG  . PHE A 1 145 ? 55.660 30.152 127.112 1.00 23.69 ? 425  PHE A CG  1 
ATOM   1121 C  CD1 . PHE A 1 145 ? 54.673 30.740 127.898 1.00 22.35 ? 425  PHE A CD1 1 
ATOM   1122 C  CD2 . PHE A 1 145 ? 55.506 28.820 126.729 1.00 21.86 ? 425  PHE A CD2 1 
ATOM   1123 C  CE1 . PHE A 1 145 ? 53.542 30.016 128.288 1.00 23.01 ? 425  PHE A CE1 1 
ATOM   1124 C  CE2 . PHE A 1 145 ? 54.379 28.086 127.113 1.00 21.25 ? 425  PHE A CE2 1 
ATOM   1125 C  CZ  . PHE A 1 145 ? 53.395 28.684 127.892 1.00 21.91 ? 425  PHE A CZ  1 
ATOM   1126 N  N   . THR A 1 146 ? 54.172 31.586 124.843 1.00 28.15 ? 426  THR A N   1 
ATOM   1127 C  CA  . THR A 1 146 ? 52.858 32.195 124.817 1.00 28.89 ? 426  THR A CA  1 
ATOM   1128 C  C   . THR A 1 146 ? 51.771 31.168 125.054 1.00 28.39 ? 426  THR A C   1 
ATOM   1129 O  O   . THR A 1 146 ? 51.936 29.991 124.763 1.00 27.43 ? 426  THR A O   1 
ATOM   1130 C  CB  . THR A 1 146 ? 52.581 32.896 123.463 1.00 30.65 ? 426  THR A CB  1 
ATOM   1131 O  OG1 . THR A 1 146 ? 51.258 33.445 123.476 1.00 30.50 ? 426  THR A OG1 1 
ATOM   1132 C  CG2 . THR A 1 146 ? 52.692 31.913 122.309 1.00 27.51 ? 426  THR A CG2 1 
ATOM   1133 N  N   . GLU A 1 147 ? 50.662 31.627 125.615 1.00 31.92 ? 427  GLU A N   1 
ATOM   1134 C  CA  . GLU A 1 147 ? 49.515 30.767 125.864 1.00 33.81 ? 427  GLU A CA  1 
ATOM   1135 C  C   . GLU A 1 147 ? 48.501 31.133 124.785 1.00 33.55 ? 427  GLU A C   1 
ATOM   1136 O  O   . GLU A 1 147 ? 48.634 32.165 124.127 1.00 32.48 ? 427  GLU A O   1 
ATOM   1137 C  CB  . GLU A 1 147 ? 48.931 31.032 127.252 1.00 35.60 ? 427  GLU A CB  1 
ATOM   1138 C  CG  . GLU A 1 147 ? 49.820 30.574 128.402 1.00 41.56 ? 427  GLU A CG  1 
ATOM   1139 C  CD  . GLU A 1 147 ? 49.178 30.786 129.765 1.00 43.70 ? 427  GLU A CD  1 
ATOM   1140 O  OE1 . GLU A 1 147 ? 48.985 31.959 130.162 1.00 45.79 ? 427  GLU A OE1 1 
ATOM   1141 O  OE2 . GLU A 1 147 ? 48.865 29.779 130.437 1.00 43.08 ? 427  GLU A OE2 1 
ATOM   1142 N  N   . GLY A 1 148 ? 47.492 30.297 124.596 1.00 32.38 ? 428  GLY A N   1 
ATOM   1143 C  CA  . GLY A 1 148 ? 46.509 30.596 123.575 1.00 34.96 ? 428  GLY A CA  1 
ATOM   1144 C  C   . GLY A 1 148 ? 47.015 30.234 122.189 1.00 35.38 ? 428  GLY A C   1 
ATOM   1145 O  O   . GLY A 1 148 ? 48.137 29.740 122.050 1.00 34.55 ? 428  GLY A O   1 
ATOM   1146 N  N   . PRO A 1 149 ? 46.210 30.482 121.139 1.00 35.27 ? 429  PRO A N   1 
ATOM   1147 C  CA  . PRO A 1 149 ? 46.555 30.185 119.744 1.00 32.90 ? 429  PRO A CA  1 
ATOM   1148 C  C   . PRO A 1 149 ? 47.913 30.740 119.329 1.00 30.15 ? 429  PRO A C   1 
ATOM   1149 O  O   . PRO A 1 149 ? 48.156 31.939 119.403 1.00 32.20 ? 429  PRO A O   1 
ATOM   1150 C  CB  . PRO A 1 149 ? 45.396 30.803 118.966 1.00 33.89 ? 429  PRO A CB  1 
ATOM   1151 C  CG  . PRO A 1 149 ? 44.964 31.931 119.848 1.00 34.64 ? 429  PRO A CG  1 
ATOM   1152 C  CD  . PRO A 1 149 ? 44.979 31.286 121.203 1.00 35.48 ? 429  PRO A CD  1 
ATOM   1153 N  N   . PRO A 1 150 ? 48.817 29.858 118.886 1.00 27.85 ? 430  PRO A N   1 
ATOM   1154 C  CA  . PRO A 1 150 ? 50.173 30.211 118.450 1.00 27.78 ? 430  PRO A CA  1 
ATOM   1155 C  C   . PRO A 1 150 ? 50.260 30.989 117.135 1.00 27.63 ? 430  PRO A C   1 
ATOM   1156 O  O   . PRO A 1 150 ? 51.068 31.909 117.000 1.00 26.32 ? 430  PRO A O   1 
ATOM   1157 C  CB  . PRO A 1 150 ? 50.869 28.849 118.335 1.00 28.30 ? 430  PRO A CB  1 
ATOM   1158 C  CG  . PRO A 1 150 ? 50.029 27.927 119.193 1.00 29.20 ? 430  PRO A CG  1 
ATOM   1159 C  CD  . PRO A 1 150 ? 48.637 28.397 118.903 1.00 26.06 ? 430  PRO A CD  1 
ATOM   1160 N  N   . LEU A 1 151 ? 49.437 30.611 116.164 1.00 26.85 ? 431  LEU A N   1 
ATOM   1161 C  CA  . LEU A 1 151 ? 49.470 31.257 114.858 1.00 28.30 ? 431  LEU A CA  1 
ATOM   1162 C  C   . LEU A 1 151 ? 48.897 32.658 114.815 1.00 26.95 ? 431  LEU A C   1 
ATOM   1163 O  O   . LEU A 1 151 ? 47.776 32.891 115.248 1.00 27.17 ? 431  LEU A O   1 
ATOM   1164 C  CB  . LEU A 1 151 ? 48.752 30.395 113.815 1.00 26.29 ? 431  LEU A CB  1 
ATOM   1165 C  CG  . LEU A 1 151 ? 49.353 29.024 113.507 1.00 26.78 ? 431  LEU A CG  1 
ATOM   1166 C  CD1 . LEU A 1 151 ? 48.615 28.430 112.326 1.00 27.79 ? 431  LEU A CD1 1 
ATOM   1167 C  CD2 . LEU A 1 151 ? 50.827 29.144 113.188 1.00 25.85 ? 431  LEU A CD2 1 
ATOM   1168 N  N   . HIS A 1 152 ? 49.681 33.585 114.279 1.00 27.31 ? 432  HIS A N   1 
ATOM   1169 C  CA  . HIS A 1 152 ? 49.262 34.971 114.144 1.00 29.66 ? 432  HIS A CA  1 
ATOM   1170 C  C   . HIS A 1 152 ? 48.688 35.148 112.729 1.00 31.08 ? 432  HIS A C   1 
ATOM   1171 O  O   . HIS A 1 152 ? 48.989 34.353 111.843 1.00 31.29 ? 432  HIS A O   1 
ATOM   1172 C  CB  . HIS A 1 152 ? 50.469 35.883 114.367 1.00 30.80 ? 432  HIS A CB  1 
ATOM   1173 C  CG  . HIS A 1 152 ? 50.157 37.342 114.263 1.00 35.25 ? 432  HIS A CG  1 
ATOM   1174 N  ND1 . HIS A 1 152 ? 49.973 37.980 113.056 1.00 35.61 ? 432  HIS A ND1 1 
ATOM   1175 C  CD2 . HIS A 1 152 ? 50.006 38.291 115.216 1.00 36.05 ? 432  HIS A CD2 1 
ATOM   1176 C  CE1 . HIS A 1 152 ? 49.724 39.260 113.269 1.00 35.01 ? 432  HIS A CE1 1 
ATOM   1177 N  NE2 . HIS A 1 152 ? 49.739 39.474 114.571 1.00 37.63 ? 432  HIS A NE2 1 
ATOM   1178 N  N   . LYS A 1 153 ? 47.855 36.169 112.525 1.00 30.77 ? 433  LYS A N   1 
ATOM   1179 C  CA  . LYS A 1 153 ? 47.252 36.437 111.214 1.00 31.04 ? 433  LYS A CA  1 
ATOM   1180 C  C   . LYS A 1 153 ? 48.328 36.411 110.148 1.00 30.86 ? 433  LYS A C   1 
ATOM   1181 O  O   . LYS A 1 153 ? 48.111 35.954 109.025 1.00 28.27 ? 433  LYS A O   1 
ATOM   1182 C  CB  . LYS A 1 153 ? 46.590 37.817 111.186 1.00 36.69 ? 433  LYS A CB  1 
ATOM   1183 C  CG  . LYS A 1 153 ? 45.486 38.010 112.205 1.00 46.32 ? 433  LYS A CG  1 
ATOM   1184 C  CD  . LYS A 1 153 ? 45.180 39.489 112.428 1.00 52.39 ? 433  LYS A CD  1 
ATOM   1185 C  CE  . LYS A 1 153 ? 44.194 39.680 113.585 1.00 57.26 ? 433  LYS A CE  1 
ATOM   1186 N  NZ  . LYS A 1 153 ? 43.913 41.116 113.889 1.00 59.05 ? 433  LYS A NZ  1 
ATOM   1187 N  N   . ASP A 1 154 ? 49.496 36.919 110.511 1.00 29.06 ? 434  ASP A N   1 
ATOM   1188 C  CA  . ASP A 1 154 ? 50.609 36.960 109.591 1.00 26.69 ? 434  ASP A CA  1 
ATOM   1189 C  C   . ASP A 1 154 ? 51.052 35.557 109.202 1.00 27.04 ? 434  ASP A C   1 
ATOM   1190 O  O   . ASP A 1 154 ? 51.350 35.300 108.039 1.00 26.95 ? 434  ASP A O   1 
ATOM   1191 C  CB  . ASP A 1 154 ? 51.766 37.732 110.213 1.00 26.22 ? 434  ASP A CB  1 
ATOM   1192 C  CG  . ASP A 1 154 ? 52.923 37.905 109.258 1.00 27.32 ? 434  ASP A CG  1 
ATOM   1193 O  OD1 . ASP A 1 154 ? 53.916 37.168 109.388 1.00 27.96 ? 434  ASP A OD1 1 
ATOM   1194 O  OD2 . ASP A 1 154 ? 52.837 38.774 108.366 1.00 29.60 ? 434  ASP A OD2 1 
ATOM   1195 N  N   . ASP A 1 155 ? 51.086 34.644 110.169 1.00 26.04 ? 435  ASP A N   1 
ATOM   1196 C  CA  . ASP A 1 155 ? 51.496 33.270 109.890 1.00 26.18 ? 435  ASP A CA  1 
ATOM   1197 C  C   . ASP A 1 155 ? 50.483 32.586 108.979 1.00 26.53 ? 435  ASP A C   1 
ATOM   1198 O  O   . ASP A 1 155 ? 50.857 31.854 108.065 1.00 27.59 ? 435  ASP A O   1 
ATOM   1199 C  CB  . ASP A 1 155 ? 51.629 32.453 111.186 1.00 25.76 ? 435  ASP A CB  1 
ATOM   1200 C  CG  . ASP A 1 155 ? 52.659 33.026 112.159 1.00 23.37 ? 435  ASP A CG  1 
ATOM   1201 O  OD1 . ASP A 1 155 ? 53.833 33.231 111.778 1.00 17.56 ? 435  ASP A OD1 1 
ATOM   1202 O  OD2 . ASP A 1 155 ? 52.281 33.257 113.319 1.00 21.37 ? 435  ASP A OD2 1 
ATOM   1203 N  N   . VAL A 1 156 ? 49.202 32.824 109.243 1.00 26.10 ? 436  VAL A N   1 
ATOM   1204 C  CA  . VAL A 1 156 ? 48.123 32.238 108.461 1.00 27.17 ? 436  VAL A CA  1 
ATOM   1205 C  C   . VAL A 1 156 ? 48.105 32.755 107.021 1.00 28.36 ? 436  VAL A C   1 
ATOM   1206 O  O   . VAL A 1 156 ? 47.814 32.006 106.096 1.00 28.48 ? 436  VAL A O   1 
ATOM   1207 C  CB  . VAL A 1 156 ? 46.758 32.516 109.116 1.00 28.67 ? 436  VAL A CB  1 
ATOM   1208 C  CG1 . VAL A 1 156 ? 45.651 31.841 108.322 1.00 28.01 ? 436  VAL A CG1 1 
ATOM   1209 C  CG2 . VAL A 1 156 ? 46.760 32.012 110.546 1.00 27.09 ? 436  VAL A CG2 1 
ATOM   1210 N  N   . ASN A 1 157 ? 48.411 34.034 106.832 1.00 30.05 ? 437  ASN A N   1 
ATOM   1211 C  CA  . ASN A 1 157 ? 48.449 34.604 105.488 1.00 32.08 ? 437  ASN A CA  1 
ATOM   1212 C  C   . ASN A 1 157 ? 49.589 33.983 104.701 1.00 30.92 ? 437  ASN A C   1 
ATOM   1213 O  O   . ASN A 1 157 ? 49.406 33.559 103.565 1.00 31.67 ? 437  ASN A O   1 
ATOM   1214 C  CB  . ASN A 1 157 ? 48.670 36.121 105.525 1.00 36.19 ? 437  ASN A CB  1 
ATOM   1215 C  CG  . ASN A 1 157 ? 47.464 36.875 106.018 1.00 40.19 ? 437  ASN A CG  1 
ATOM   1216 O  OD1 . ASN A 1 157 ? 46.328 36.484 105.759 1.00 44.41 ? 437  ASN A OD1 1 
ATOM   1217 N  ND2 . ASN A 1 157 ? 47.701 37.978 106.719 1.00 44.69 ? 437  ASN A ND2 1 
ATOM   1218 N  N   . GLY A 1 158 ? 50.768 33.946 105.315 1.00 27.54 ? 438  GLY A N   1 
ATOM   1219 C  CA  . GLY A 1 158 ? 51.931 33.385 104.659 1.00 25.40 ? 438  GLY A CA  1 
ATOM   1220 C  C   . GLY A 1 158 ? 51.755 31.952 104.205 1.00 24.52 ? 438  GLY A C   1 
ATOM   1221 O  O   . GLY A 1 158 ? 52.171 31.593 103.110 1.00 26.30 ? 438  GLY A O   1 
ATOM   1222 N  N   . ILE A 1 159 ? 51.137 31.125 105.039 1.00 23.54 ? 439  ILE A N   1 
ATOM   1223 C  CA  . ILE A 1 159 ? 50.943 29.732 104.681 1.00 23.31 ? 439  ILE A CA  1 
ATOM   1224 C  C   . ILE A 1 159 ? 49.867 29.547 103.593 1.00 24.64 ? 439  ILE A C   1 
ATOM   1225 O  O   . ILE A 1 159 ? 50.017 28.712 102.705 1.00 25.35 ? 439  ILE A O   1 
ATOM   1226 C  CB  . ILE A 1 159 ? 50.619 28.871 105.944 1.00 20.22 ? 439  ILE A CB  1 
ATOM   1227 C  CG1 . ILE A 1 159 ? 50.814 27.393 105.614 1.00 21.12 ? 439  ILE A CG1 1 
ATOM   1228 C  CG2 . ILE A 1 159 ? 49.210 29.136 106.450 1.00 18.09 ? 439  ILE A CG2 1 
ATOM   1229 C  CD1 . ILE A 1 159 ? 52.238 27.048 105.201 1.00 14.56 ? 439  ILE A CD1 1 
ATOM   1230 N  N   . ARG A 1 160 ? 48.793 30.324 103.649 1.00 23.43 ? 440  ARG A N   1 
ATOM   1231 C  CA  . ARG A 1 160 ? 47.751 30.217 102.638 1.00 24.74 ? 440  ARG A CA  1 
ATOM   1232 C  C   . ARG A 1 160 ? 48.217 30.806 101.312 1.00 26.05 ? 440  ARG A C   1 
ATOM   1233 O  O   . ARG A 1 160 ? 47.691 30.466 100.257 1.00 29.07 ? 440  ARG A O   1 
ATOM   1234 C  CB  . ARG A 1 160 ? 46.481 30.932 103.091 1.00 25.89 ? 440  ARG A CB  1 
ATOM   1235 C  CG  . ARG A 1 160 ? 45.673 30.154 104.093 1.00 28.05 ? 440  ARG A CG  1 
ATOM   1236 C  CD  . ARG A 1 160 ? 44.453 30.927 104.518 1.00 33.06 ? 440  ARG A CD  1 
ATOM   1237 N  NE  . ARG A 1 160 ? 43.678 30.183 105.502 1.00 40.49 ? 440  ARG A NE  1 
ATOM   1238 C  CZ  . ARG A 1 160 ? 42.752 30.722 106.286 1.00 43.77 ? 440  ARG A CZ  1 
ATOM   1239 N  NH1 . ARG A 1 160 ? 42.485 32.020 106.205 1.00 45.47 ? 440  ARG A NH1 1 
ATOM   1240 N  NH2 . ARG A 1 160 ? 42.089 29.964 107.150 1.00 43.22 ? 440  ARG A NH2 1 
ATOM   1241 N  N   . HIS A 1 161 ? 49.201 31.694 101.360 1.00 24.35 ? 441  HIS A N   1 
ATOM   1242 C  CA  . HIS A 1 161 ? 49.707 32.290 100.139 1.00 24.72 ? 441  HIS A CA  1 
ATOM   1243 C  C   . HIS A 1 161 ? 50.463 31.238 99.332  1.00 26.24 ? 441  HIS A C   1 
ATOM   1244 O  O   . HIS A 1 161 ? 50.531 31.313 98.104  1.00 26.96 ? 441  HIS A O   1 
ATOM   1245 C  CB  . HIS A 1 161 ? 50.628 33.465 100.450 1.00 21.94 ? 441  HIS A CB  1 
ATOM   1246 C  CG  . HIS A 1 161 ? 50.942 34.308 99.255  1.00 21.49 ? 441  HIS A CG  1 
ATOM   1247 N  ND1 . HIS A 1 161 ? 50.018 35.152 98.679  1.00 23.21 ? 441  HIS A ND1 1 
ATOM   1248 C  CD2 . HIS A 1 161 ? 52.068 34.421 98.513  1.00 23.26 ? 441  HIS A CD2 1 
ATOM   1249 C  CE1 . HIS A 1 161 ? 50.561 35.748 97.634  1.00 21.93 ? 441  HIS A CE1 1 
ATOM   1250 N  NE2 . HIS A 1 161 ? 51.804 35.322 97.512  1.00 24.09 ? 441  HIS A NE2 1 
ATOM   1251 N  N   . LEU A 1 162 ? 51.028 30.260 100.032 1.00 27.09 ? 442  LEU A N   1 
ATOM   1252 C  CA  . LEU A 1 162 ? 51.770 29.178 99.394  1.00 27.80 ? 442  LEU A CA  1 
ATOM   1253 C  C   . LEU A 1 162 ? 50.877 28.009 98.984  1.00 28.59 ? 442  LEU A C   1 
ATOM   1254 O  O   . LEU A 1 162 ? 51.084 27.420 97.929  1.00 28.30 ? 442  LEU A O   1 
ATOM   1255 C  CB  . LEU A 1 162 ? 52.861 28.648 100.329 1.00 28.49 ? 442  LEU A CB  1 
ATOM   1256 C  CG  . LEU A 1 162 ? 54.042 29.552 100.679 1.00 30.92 ? 442  LEU A CG  1 
ATOM   1257 C  CD1 . LEU A 1 162 ? 54.898 28.875 101.737 1.00 31.60 ? 442  LEU A CD1 1 
ATOM   1258 C  CD2 . LEU A 1 162 ? 54.863 29.836 99.434  1.00 31.89 ? 442  LEU A CD2 1 
ATOM   1259 N  N   . TYR A 1 163 ? 49.896 27.674 99.821  1.00 30.49 ? 443  TYR A N   1 
ATOM   1260 C  CA  . TYR A 1 163 ? 48.993 26.553 99.548  1.00 31.37 ? 443  TYR A CA  1 
ATOM   1261 C  C   . TYR A 1 163 ? 47.518 26.945 99.497  1.00 31.76 ? 443  TYR A C   1 
ATOM   1262 O  O   . TYR A 1 163 ? 46.719 26.112 99.036  1.00 33.61 ? 443  TYR A O   1 
ATOM   1263 C  CB  . TYR A 1 163 ? 49.181 25.450 100.601 1.00 30.85 ? 443  TYR A CB  1 
ATOM   1264 C  CG  . TYR A 1 163 ? 50.611 24.990 100.753 1.00 28.19 ? 443  TYR A CG  1 
ATOM   1265 C  CD1 . TYR A 1 163 ? 51.462 25.575 101.697 1.00 25.52 ? 443  TYR A CD1 1 
ATOM   1266 C  CD2 . TYR A 1 163 ? 51.133 24.007 99.913  1.00 27.48 ? 443  TYR A CD2 1 
ATOM   1267 C  CE1 . TYR A 1 163 ? 52.805 25.190 101.793 1.00 23.19 ? 443  TYR A CE1 1 
ATOM   1268 C  CE2 . TYR A 1 163 ? 52.469 23.617 100.000 1.00 26.82 ? 443  TYR A CE2 1 
ATOM   1269 C  CZ  . TYR A 1 163 ? 53.298 24.213 100.937 1.00 24.13 ? 443  TYR A CZ  1 
ATOM   1270 O  OH  . TYR A 1 163 ? 54.618 23.837 100.986 1.00 24.42 ? 443  TYR A OH  1 
ATOM   1271 O  OXT . TYR A 1 163 ? 47.163 28.054 99.935  1.00 33.91 ? 443  TYR A OXT 1 
ATOM   1272 N  N   . ASP B 1 8   ? 38.439 24.617 161.434 1.00 58.69 ? 113  ASP B N   1 
ATOM   1273 C  CA  . ASP B 1 8   ? 39.418 24.920 160.351 1.00 58.71 ? 113  ASP B CA  1 
ATOM   1274 C  C   . ASP B 1 8   ? 40.865 24.867 160.849 1.00 56.49 ? 113  ASP B C   1 
ATOM   1275 O  O   . ASP B 1 8   ? 41.355 25.782 161.519 1.00 56.57 ? 113  ASP B O   1 
ATOM   1276 C  CB  . ASP B 1 8   ? 39.115 26.293 159.737 1.00 61.05 ? 113  ASP B CB  1 
ATOM   1277 C  CG  . ASP B 1 8   ? 39.042 27.399 160.776 1.00 62.86 ? 113  ASP B CG  1 
ATOM   1278 O  OD1 . ASP B 1 8   ? 40.101 27.786 161.322 1.00 62.33 ? 113  ASP B OD1 1 
ATOM   1279 O  OD2 . ASP B 1 8   ? 37.917 27.876 161.046 1.00 63.37 ? 113  ASP B OD2 1 
ATOM   1280 N  N   . LEU B 1 9   ? 41.541 23.778 160.512 1.00 52.64 ? 114  LEU B N   1 
ATOM   1281 C  CA  . LEU B 1 9   ? 42.921 23.579 160.910 1.00 48.28 ? 114  LEU B CA  1 
ATOM   1282 C  C   . LEU B 1 9   ? 43.846 24.419 160.029 1.00 43.58 ? 114  LEU B C   1 
ATOM   1283 O  O   . LEU B 1 9   ? 43.584 24.607 158.838 1.00 42.86 ? 114  LEU B O   1 
ATOM   1284 C  CB  . LEU B 1 9   ? 43.265 22.094 160.794 1.00 48.88 ? 114  LEU B CB  1 
ATOM   1285 C  CG  . LEU B 1 9   ? 44.509 21.605 161.528 1.00 50.33 ? 114  LEU B CG  1 
ATOM   1286 C  CD1 . LEU B 1 9   ? 44.535 22.156 162.948 1.00 50.73 ? 114  LEU B CD1 1 
ATOM   1287 C  CD2 . LEU B 1 9   ? 44.500 20.088 161.540 1.00 51.89 ? 114  LEU B CD2 1 
ATOM   1288 N  N   . LYS B 1 10  ? 44.917 24.942 160.615 1.00 37.78 ? 115  LYS B N   1 
ATOM   1289 C  CA  . LYS B 1 10  ? 45.858 25.745 159.846 1.00 34.84 ? 115  LYS B CA  1 
ATOM   1290 C  C   . LYS B 1 10  ? 47.233 25.767 160.498 1.00 32.44 ? 115  LYS B C   1 
ATOM   1291 O  O   . LYS B 1 10  ? 47.395 25.317 161.628 1.00 31.94 ? 115  LYS B O   1 
ATOM   1292 C  CB  . LYS B 1 10  ? 45.341 27.176 159.702 1.00 35.26 ? 115  LYS B CB  1 
ATOM   1293 C  CG  . LYS B 1 10  ? 45.439 28.007 160.972 1.00 39.03 ? 115  LYS B CG  1 
ATOM   1294 C  CD  . LYS B 1 10  ? 45.160 29.466 160.674 1.00 38.56 ? 115  LYS B CD  1 
ATOM   1295 C  CE  . LYS B 1 10  ? 45.529 30.353 161.845 1.00 41.04 ? 115  LYS B CE  1 
ATOM   1296 N  NZ  . LYS B 1 10  ? 45.396 31.790 161.475 1.00 41.35 ? 115  LYS B NZ  1 
ATOM   1297 N  N   . TRP B 1 11  ? 48.225 26.284 159.779 1.00 30.35 ? 116  TRP B N   1 
ATOM   1298 C  CA  . TRP B 1 11  ? 49.571 26.359 160.320 1.00 30.31 ? 116  TRP B CA  1 
ATOM   1299 C  C   . TRP B 1 11  ? 49.645 27.558 161.252 1.00 31.82 ? 116  TRP B C   1 
ATOM   1300 O  O   . TRP B 1 11  ? 49.024 28.589 160.996 1.00 32.51 ? 116  TRP B O   1 
ATOM   1301 C  CB  . TRP B 1 11  ? 50.613 26.516 159.204 1.00 27.93 ? 116  TRP B CB  1 
ATOM   1302 C  CG  . TRP B 1 11  ? 50.690 25.351 158.258 1.00 27.86 ? 116  TRP B CG  1 
ATOM   1303 C  CD1 . TRP B 1 11  ? 50.266 25.321 156.958 1.00 26.75 ? 116  TRP B CD1 1 
ATOM   1304 C  CD2 . TRP B 1 11  ? 51.204 24.040 158.541 1.00 26.96 ? 116  TRP B CD2 1 
ATOM   1305 N  NE1 . TRP B 1 11  ? 50.483 24.078 156.415 1.00 23.61 ? 116  TRP B NE1 1 
ATOM   1306 C  CE2 . TRP B 1 11  ? 51.058 23.271 157.363 1.00 27.29 ? 116  TRP B CE2 1 
ATOM   1307 C  CE3 . TRP B 1 11  ? 51.773 23.441 159.674 1.00 23.04 ? 116  TRP B CE3 1 
ATOM   1308 C  CZ2 . TRP B 1 11  ? 51.460 21.930 157.287 1.00 24.46 ? 116  TRP B CZ2 1 
ATOM   1309 C  CZ3 . TRP B 1 11  ? 52.171 22.108 159.597 1.00 23.32 ? 116  TRP B CZ3 1 
ATOM   1310 C  CH2 . TRP B 1 11  ? 52.012 21.369 158.410 1.00 23.78 ? 116  TRP B CH2 1 
ATOM   1311 N  N   . HIS B 1 12  ? 50.400 27.419 162.335 1.00 31.20 ? 117  HIS B N   1 
ATOM   1312 C  CA  . HIS B 1 12  ? 50.549 28.507 163.285 1.00 31.82 ? 117  HIS B CA  1 
ATOM   1313 C  C   . HIS B 1 12  ? 51.774 29.357 163.006 1.00 30.66 ? 117  HIS B C   1 
ATOM   1314 O  O   . HIS B 1 12  ? 51.997 30.358 163.679 1.00 34.99 ? 117  HIS B O   1 
ATOM   1315 C  CB  . HIS B 1 12  ? 50.577 27.963 164.711 1.00 31.55 ? 117  HIS B CB  1 
ATOM   1316 C  CG  . HIS B 1 12  ? 49.237 27.513 165.193 1.00 32.54 ? 117  HIS B CG  1 
ATOM   1317 N  ND1 . HIS B 1 12  ? 49.064 26.767 166.337 1.00 33.18 ? 117  HIS B ND1 1 
ATOM   1318 C  CD2 . HIS B 1 12  ? 47.999 27.711 164.681 1.00 32.52 ? 117  HIS B CD2 1 
ATOM   1319 C  CE1 . HIS B 1 12  ? 47.777 26.523 166.510 1.00 32.64 ? 117  HIS B CE1 1 
ATOM   1320 N  NE2 . HIS B 1 12  ? 47.110 27.085 165.518 1.00 34.29 ? 117  HIS B NE2 1 
ATOM   1321 N  N   . HIS B 1 13  ? 52.572 28.950 162.022 1.00 28.55 ? 118  HIS B N   1 
ATOM   1322 C  CA  . HIS B 1 13  ? 53.745 29.722 161.617 1.00 25.56 ? 118  HIS B CA  1 
ATOM   1323 C  C   . HIS B 1 13  ? 53.553 30.058 160.144 1.00 25.78 ? 118  HIS B C   1 
ATOM   1324 O  O   . HIS B 1 13  ? 52.775 29.406 159.456 1.00 26.11 ? 118  HIS B O   1 
ATOM   1325 C  CB  . HIS B 1 13  ? 55.044 28.934 161.824 1.00 25.76 ? 118  HIS B CB  1 
ATOM   1326 C  CG  . HIS B 1 13  ? 55.057 27.591 161.164 1.00 25.72 ? 118  HIS B CG  1 
ATOM   1327 N  ND1 . HIS B 1 13  ? 54.198 26.576 161.526 1.00 24.79 ? 118  HIS B ND1 1 
ATOM   1328 C  CD2 . HIS B 1 13  ? 55.839 27.090 160.180 1.00 24.52 ? 118  HIS B CD2 1 
ATOM   1329 C  CE1 . HIS B 1 13  ? 54.453 25.506 160.796 1.00 22.93 ? 118  HIS B CE1 1 
ATOM   1330 N  NE2 . HIS B 1 13  ? 55.445 25.791 159.971 1.00 23.07 ? 118  HIS B NE2 1 
ATOM   1331 N  N   . HIS B 1 14  ? 54.261 31.072 159.666 1.00 25.82 ? 119  HIS B N   1 
ATOM   1332 C  CA  . HIS B 1 14  ? 54.133 31.514 158.286 1.00 25.15 ? 119  HIS B CA  1 
ATOM   1333 C  C   . HIS B 1 14  ? 55.290 31.152 157.372 1.00 24.84 ? 119  HIS B C   1 
ATOM   1334 O  O   . HIS B 1 14  ? 55.163 31.228 156.155 1.00 24.51 ? 119  HIS B O   1 
ATOM   1335 C  CB  . HIS B 1 14  ? 53.911 33.030 158.253 1.00 25.12 ? 119  HIS B CB  1 
ATOM   1336 C  CG  . HIS B 1 14  ? 52.559 33.446 158.740 1.00 26.86 ? 119  HIS B CG  1 
ATOM   1337 N  ND1 . HIS B 1 14  ? 52.177 34.766 158.840 1.00 26.98 ? 119  HIS B ND1 1 
ATOM   1338 C  CD2 . HIS B 1 14  ? 51.495 32.712 159.144 1.00 25.46 ? 119  HIS B CD2 1 
ATOM   1339 C  CE1 . HIS B 1 14  ? 50.934 34.826 159.285 1.00 29.50 ? 119  HIS B CE1 1 
ATOM   1340 N  NE2 . HIS B 1 14  ? 50.498 33.594 159.477 1.00 28.22 ? 119  HIS B NE2 1 
ATOM   1341 N  N   . ASN B 1 15  ? 56.421 30.779 157.955 1.00 23.92 ? 120  ASN B N   1 
ATOM   1342 C  CA  . ASN B 1 15  ? 57.581 30.395 157.166 1.00 23.42 ? 120  ASN B CA  1 
ATOM   1343 C  C   . ASN B 1 15  ? 57.568 28.878 157.046 1.00 23.79 ? 120  ASN B C   1 
ATOM   1344 O  O   . ASN B 1 15  ? 58.249 28.160 157.779 1.00 22.99 ? 120  ASN B O   1 
ATOM   1345 C  CB  . ASN B 1 15  ? 58.868 30.914 157.824 1.00 24.61 ? 120  ASN B CB  1 
ATOM   1346 C  CG  . ASN B 1 15  ? 59.019 30.486 159.285 1.00 27.08 ? 120  ASN B CG  1 
ATOM   1347 O  OD1 . ASN B 1 15  ? 58.047 30.395 160.041 1.00 28.75 ? 120  ASN B OD1 1 
ATOM   1348 N  ND2 . ASN B 1 15  ? 60.259 30.244 159.689 1.00 24.54 ? 120  ASN B ND2 1 
ATOM   1349 N  N   . ILE B 1 16  ? 56.760 28.401 156.107 1.00 23.12 ? 121  ILE B N   1 
ATOM   1350 C  CA  . ILE B 1 16  ? 56.585 26.979 155.876 1.00 24.05 ? 121  ILE B CA  1 
ATOM   1351 C  C   . ILE B 1 16  ? 57.722 26.340 155.097 1.00 23.08 ? 121  ILE B C   1 
ATOM   1352 O  O   . ILE B 1 16  ? 58.319 26.962 154.223 1.00 25.00 ? 121  ILE B O   1 
ATOM   1353 C  CB  . ILE B 1 16  ? 55.245 26.734 155.156 1.00 25.87 ? 121  ILE B CB  1 
ATOM   1354 C  CG1 . ILE B 1 16  ? 54.104 27.259 156.039 1.00 26.83 ? 121  ILE B CG1 1 
ATOM   1355 C  CG2 . ILE B 1 16  ? 55.066 25.256 154.855 1.00 25.54 ? 121  ILE B CG2 1 
ATOM   1356 C  CD1 . ILE B 1 16  ? 52.721 27.053 155.465 1.00 31.75 ? 121  ILE B CD1 1 
ATOM   1357 N  N   . THR B 1 17  ? 58.029 25.094 155.429 1.00 21.12 ? 122  THR B N   1 
ATOM   1358 C  CA  . THR B 1 17  ? 59.096 24.382 154.744 1.00 19.30 ? 122  THR B CA  1 
ATOM   1359 C  C   . THR B 1 17  ? 58.564 23.156 154.026 1.00 18.87 ? 122  THR B C   1 
ATOM   1360 O  O   . THR B 1 17  ? 57.539 22.586 154.415 1.00 17.08 ? 122  THR B O   1 
ATOM   1361 C  CB  . THR B 1 17  ? 60.203 23.938 155.721 1.00 18.41 ? 122  THR B CB  1 
ATOM   1362 O  OG1 . THR B 1 17  ? 59.640 23.097 156.732 1.00 18.81 ? 122  THR B OG1 1 
ATOM   1363 C  CG2 . THR B 1 17  ? 60.861 25.147 156.359 1.00 14.91 ? 122  THR B CG2 1 
ATOM   1364 N  N   . TYR B 1 18  ? 59.260 22.756 152.966 1.00 18.82 ? 123  TYR B N   1 
ATOM   1365 C  CA  . TYR B 1 18  ? 58.848 21.584 152.207 1.00 17.71 ? 123  TYR B CA  1 
ATOM   1366 C  C   . TYR B 1 18  ? 60.048 20.798 151.726 1.00 14.81 ? 123  TYR B C   1 
ATOM   1367 O  O   . TYR B 1 18  ? 61.116 21.353 151.497 1.00 14.65 ? 123  TYR B O   1 
ATOM   1368 C  CB  . TYR B 1 18  ? 57.966 21.973 151.004 1.00 14.12 ? 123  TYR B CB  1 
ATOM   1369 C  CG  . TYR B 1 18  ? 58.671 22.725 149.891 1.00 14.85 ? 123  TYR B CG  1 
ATOM   1370 C  CD1 . TYR B 1 18  ? 58.811 24.113 149.936 1.00 15.43 ? 123  TYR B CD1 1 
ATOM   1371 C  CD2 . TYR B 1 18  ? 59.144 22.052 148.761 1.00 15.15 ? 123  TYR B CD2 1 
ATOM   1372 C  CE1 . TYR B 1 18  ? 59.392 24.817 148.882 1.00 12.87 ? 123  TYR B CE1 1 
ATOM   1373 C  CE2 . TYR B 1 18  ? 59.725 22.746 147.702 1.00 15.56 ? 123  TYR B CE2 1 
ATOM   1374 C  CZ  . TYR B 1 18  ? 59.842 24.126 147.766 1.00 17.67 ? 123  TYR B CZ  1 
ATOM   1375 O  OH  . TYR B 1 18  ? 60.378 24.816 146.702 1.00 20.47 ? 123  TYR B OH  1 
ATOM   1376 N  N   . TRP B 1 19  ? 59.840 19.499 151.567 1.00 12.91 ? 124  TRP B N   1 
ATOM   1377 C  CA  . TRP B 1 19  ? 60.867 18.587 151.121 1.00 14.27 ? 124  TRP B CA  1 
ATOM   1378 C  C   . TRP B 1 19  ? 60.355 17.741 149.955 1.00 15.49 ? 124  TRP B C   1 
ATOM   1379 O  O   . TRP B 1 19  ? 59.312 17.093 150.061 1.00 13.62 ? 124  TRP B O   1 
ATOM   1380 C  CB  . TRP B 1 19  ? 61.271 17.677 152.295 1.00 16.23 ? 124  TRP B CB  1 
ATOM   1381 C  CG  . TRP B 1 19  ? 62.237 16.559 151.970 1.00 16.27 ? 124  TRP B CG  1 
ATOM   1382 C  CD1 . TRP B 1 19  ? 63.303 16.613 151.117 1.00 17.04 ? 124  TRP B CD1 1 
ATOM   1383 C  CD2 . TRP B 1 19  ? 62.292 15.266 152.595 1.00 17.47 ? 124  TRP B CD2 1 
ATOM   1384 N  NE1 . TRP B 1 19  ? 64.021 15.442 151.179 1.00 16.74 ? 124  TRP B NE1 1 
ATOM   1385 C  CE2 . TRP B 1 19  ? 63.424 14.600 152.078 1.00 17.45 ? 124  TRP B CE2 1 
ATOM   1386 C  CE3 . TRP B 1 19  ? 61.496 14.610 153.548 1.00 17.63 ? 124  TRP B CE3 1 
ATOM   1387 C  CZ2 . TRP B 1 19  ? 63.783 13.307 152.484 1.00 18.60 ? 124  TRP B CZ2 1 
ATOM   1388 C  CZ3 . TRP B 1 19  ? 61.853 13.327 153.952 1.00 18.18 ? 124  TRP B CZ3 1 
ATOM   1389 C  CH2 . TRP B 1 19  ? 62.988 12.691 153.420 1.00 18.22 ? 124  TRP B CH2 1 
ATOM   1390 N  N   . ILE B 1 20  ? 61.080 17.770 148.841 1.00 12.10 ? 125  ILE B N   1 
ATOM   1391 C  CA  . ILE B 1 20  ? 60.729 16.956 147.696 1.00 13.59 ? 125  ILE B CA  1 
ATOM   1392 C  C   . ILE B 1 20  ? 61.514 15.672 147.918 1.00 13.64 ? 125  ILE B C   1 
ATOM   1393 O  O   . ILE B 1 20  ? 62.694 15.588 147.592 1.00 14.54 ? 125  ILE B O   1 
ATOM   1394 C  CB  . ILE B 1 20  ? 61.167 17.608 146.381 1.00 14.78 ? 125  ILE B CB  1 
ATOM   1395 C  CG1 . ILE B 1 20  ? 60.520 18.991 146.254 1.00 13.64 ? 125  ILE B CG1 1 
ATOM   1396 C  CG2 . ILE B 1 20  ? 60.773 16.715 145.214 1.00 10.29 ? 125  ILE B CG2 1 
ATOM   1397 C  CD1 . ILE B 1 20  ? 61.024 19.811 145.080 1.00 12.29 ? 125  ILE B CD1 1 
ATOM   1398 N  N   . GLN B 1 21  ? 60.855 14.679 148.496 1.00 13.68 ? 126  GLN B N   1 
ATOM   1399 C  CA  . GLN B 1 21  ? 61.496 13.413 148.802 1.00 15.77 ? 126  GLN B CA  1 
ATOM   1400 C  C   . GLN B 1 21  ? 61.971 12.587 147.604 1.00 18.55 ? 126  GLN B C   1 
ATOM   1401 O  O   . GLN B 1 21  ? 63.086 12.069 147.611 1.00 18.76 ? 126  GLN B O   1 
ATOM   1402 C  CB  . GLN B 1 21  ? 60.564 12.573 149.662 1.00 14.28 ? 126  GLN B CB  1 
ATOM   1403 C  CG  . GLN B 1 21  ? 61.092 11.200 149.957 1.00 19.68 ? 126  GLN B CG  1 
ATOM   1404 C  CD  . GLN B 1 21  ? 60.133 10.402 150.794 1.00 22.52 ? 126  GLN B CD  1 
ATOM   1405 O  OE1 . GLN B 1 21  ? 59.933 9.211  150.560 1.00 28.95 ? 126  GLN B OE1 1 
ATOM   1406 N  NE2 . GLN B 1 21  ? 59.534 11.048 151.782 1.00 19.79 ? 126  GLN B NE2 1 
ATOM   1407 N  N   . ASN B 1 22  ? 61.118 12.428 146.596 1.00 19.57 ? 127  ASN B N   1 
ATOM   1408 C  CA  . ASN B 1 22  ? 61.492 11.664 145.412 1.00 17.91 ? 127  ASN B CA  1 
ATOM   1409 C  C   . ASN B 1 22  ? 60.868 12.265 144.165 1.00 19.24 ? 127  ASN B C   1 
ATOM   1410 O  O   . ASN B 1 22  ? 60.138 13.261 144.239 1.00 19.36 ? 127  ASN B O   1 
ATOM   1411 C  CB  . ASN B 1 22  ? 61.111 10.184 145.549 1.00 17.29 ? 127  ASN B CB  1 
ATOM   1412 C  CG  . ASN B 1 22  ? 59.628 9.965  145.734 1.00 18.23 ? 127  ASN B CG  1 
ATOM   1413 O  OD1 . ASN B 1 22  ? 58.830 10.882 145.602 1.00 20.83 ? 127  ASN B OD1 1 
ATOM   1414 N  ND2 . ASN B 1 22  ? 59.254 8.735  146.035 1.00 18.51 ? 127  ASN B ND2 1 
ATOM   1415 N  N   . TYR B 1 23  ? 61.164 11.666 143.016 1.00 18.73 ? 128  TYR B N   1 
ATOM   1416 C  CA  . TYR B 1 23  ? 60.670 12.187 141.749 1.00 14.58 ? 128  TYR B CA  1 
ATOM   1417 C  C   . TYR B 1 23  ? 59.890 11.203 140.899 1.00 14.07 ? 128  TYR B C   1 
ATOM   1418 O  O   . TYR B 1 23  ? 59.880 10.005 141.158 1.00 12.64 ? 128  TYR B O   1 
ATOM   1419 C  CB  . TYR B 1 23  ? 61.844 12.731 140.921 1.00 15.39 ? 128  TYR B CB  1 
ATOM   1420 C  CG  . TYR B 1 23  ? 62.538 13.932 141.536 1.00 13.70 ? 128  TYR B CG  1 
ATOM   1421 C  CD1 . TYR B 1 23  ? 63.526 13.777 142.510 1.00 12.60 ? 128  TYR B CD1 1 
ATOM   1422 C  CD2 . TYR B 1 23  ? 62.156 15.229 141.187 1.00 15.12 ? 128  TYR B CD2 1 
ATOM   1423 C  CE1 . TYR B 1 23  ? 64.113 14.889 143.124 1.00 11.44 ? 128  TYR B CE1 1 
ATOM   1424 C  CE2 . TYR B 1 23  ? 62.731 16.341 141.793 1.00 11.78 ? 128  TYR B CE2 1 
ATOM   1425 C  CZ  . TYR B 1 23  ? 63.706 16.164 142.760 1.00 13.63 ? 128  TYR B CZ  1 
ATOM   1426 O  OH  . TYR B 1 23  ? 64.257 17.270 143.365 1.00 11.62 ? 128  TYR B OH  1 
ATOM   1427 N  N   . SER B 1 24  ? 59.230 11.737 139.877 1.00 15.52 ? 129  SER B N   1 
ATOM   1428 C  CA  . SER B 1 24  ? 58.461 10.929 138.936 1.00 17.11 ? 129  SER B CA  1 
ATOM   1429 C  C   . SER B 1 24  ? 59.374 10.596 137.766 1.00 20.19 ? 129  SER B C   1 
ATOM   1430 O  O   . SER B 1 24  ? 60.298 11.345 137.452 1.00 19.00 ? 129  SER B O   1 
ATOM   1431 C  CB  . SER B 1 24  ? 57.246 11.705 138.419 1.00 17.11 ? 129  SER B CB  1 
ATOM   1432 O  OG  . SER B 1 24  ? 56.716 11.100 137.252 1.00 14.91 ? 129  SER B OG  1 
ATOM   1433 N  N   . GLU B 1 25  ? 59.109 9.480  137.108 1.00 23.95 ? 130  GLU B N   1 
ATOM   1434 C  CA  . GLU B 1 25  ? 59.937 9.079  135.982 1.00 27.98 ? 130  GLU B CA  1 
ATOM   1435 C  C   . GLU B 1 25  ? 59.585 9.825  134.700 1.00 26.19 ? 130  GLU B C   1 
ATOM   1436 O  O   . GLU B 1 25  ? 60.331 9.763  133.732 1.00 27.48 ? 130  GLU B O   1 
ATOM   1437 C  CB  . GLU B 1 25  ? 59.795 7.575  135.743 1.00 33.47 ? 130  GLU B CB  1 
ATOM   1438 C  CG  . GLU B 1 25  ? 59.913 6.740  137.004 1.00 40.62 ? 130  GLU B CG  1 
ATOM   1439 C  CD  . GLU B 1 25  ? 60.077 5.255  136.718 1.00 45.97 ? 130  GLU B CD  1 
ATOM   1440 O  OE1 . GLU B 1 25  ? 61.082 4.880  136.068 1.00 47.09 ? 130  GLU B OE1 1 
ATOM   1441 O  OE2 . GLU B 1 25  ? 59.204 4.466  137.148 1.00 47.02 ? 130  GLU B OE2 1 
ATOM   1442 N  N   . ASP B 1 26  ? 58.464 10.543 134.702 1.00 23.99 ? 131  ASP B N   1 
ATOM   1443 C  CA  . ASP B 1 26  ? 58.008 11.256 133.511 1.00 21.74 ? 131  ASP B CA  1 
ATOM   1444 C  C   . ASP B 1 26  ? 58.637 12.606 133.194 1.00 22.03 ? 131  ASP B C   1 
ATOM   1445 O  O   . ASP B 1 26  ? 58.578 13.052 132.051 1.00 21.61 ? 131  ASP B O   1 
ATOM   1446 C  CB  . ASP B 1 26  ? 56.496 11.480 133.557 1.00 22.01 ? 131  ASP B CB  1 
ATOM   1447 C  CG  . ASP B 1 26  ? 55.717 10.228 133.884 1.00 18.40 ? 131  ASP B CG  1 
ATOM   1448 O  OD1 . ASP B 1 26  ? 56.138 9.119  133.514 1.00 21.04 ? 131  ASP B OD1 1 
ATOM   1449 O  OD2 . ASP B 1 26  ? 54.652 10.371 134.504 1.00 17.97 ? 131  ASP B OD2 1 
ATOM   1450 N  N   . LEU B 1 27  ? 59.207 13.273 134.189 1.00 19.22 ? 132  LEU B N   1 
ATOM   1451 C  CA  . LEU B 1 27  ? 59.797 14.582 133.953 1.00 17.22 ? 132  LEU B CA  1 
ATOM   1452 C  C   . LEU B 1 27  ? 61.179 14.713 134.566 1.00 17.81 ? 132  LEU B C   1 
ATOM   1453 O  O   . LEU B 1 27  ? 61.515 14.000 135.511 1.00 20.83 ? 132  LEU B O   1 
ATOM   1454 C  CB  . LEU B 1 27  ? 58.887 15.664 134.528 1.00 16.52 ? 132  LEU B CB  1 
ATOM   1455 C  CG  . LEU B 1 27  ? 57.497 15.796 133.901 1.00 20.26 ? 132  LEU B CG  1 
ATOM   1456 C  CD1 . LEU B 1 27  ? 56.642 16.745 134.732 1.00 18.39 ? 132  LEU B CD1 1 
ATOM   1457 C  CD2 . LEU B 1 27  ? 57.629 16.303 132.471 1.00 19.31 ? 132  LEU B CD2 1 
ATOM   1458 N  N   . PRO B 1 28  ? 62.014 15.617 134.021 1.00 17.25 ? 133  PRO B N   1 
ATOM   1459 C  CA  . PRO B 1 28  ? 63.371 15.820 134.557 1.00 17.25 ? 133  PRO B CA  1 
ATOM   1460 C  C   . PRO B 1 28  ? 63.250 16.450 135.954 1.00 15.64 ? 133  PRO B C   1 
ATOM   1461 O  O   . PRO B 1 28  ? 62.245 17.096 136.250 1.00 15.44 ? 133  PRO B O   1 
ATOM   1462 C  CB  . PRO B 1 28  ? 64.002 16.790 133.554 1.00 14.93 ? 133  PRO B CB  1 
ATOM   1463 C  CG  . PRO B 1 28  ? 63.214 16.559 132.292 1.00 15.96 ? 133  PRO B CG  1 
ATOM   1464 C  CD  . PRO B 1 28  ? 61.811 16.408 132.796 1.00 15.36 ? 133  PRO B CD  1 
ATOM   1465 N  N   . ARG B 1 29  ? 64.259 16.265 136.805 1.00 16.42 ? 134  ARG B N   1 
ATOM   1466 C  CA  . ARG B 1 29  ? 64.237 16.840 138.159 1.00 16.86 ? 134  ARG B CA  1 
ATOM   1467 C  C   . ARG B 1 29  ? 64.022 18.338 138.138 1.00 16.07 ? 134  ARG B C   1 
ATOM   1468 O  O   . ARG B 1 29  ? 63.219 18.869 138.899 1.00 15.45 ? 134  ARG B O   1 
ATOM   1469 C  CB  . ARG B 1 29  ? 65.551 16.591 138.906 1.00 18.20 ? 134  ARG B CB  1 
ATOM   1470 C  CG  . ARG B 1 29  ? 65.708 15.207 139.469 1.00 22.57 ? 134  ARG B CG  1 
ATOM   1471 C  CD  . ARG B 1 29  ? 66.845 15.143 140.470 1.00 21.69 ? 134  ARG B CD  1 
ATOM   1472 N  NE  . ARG B 1 29  ? 67.022 13.771 140.932 1.00 26.97 ? 134  ARG B NE  1 
ATOM   1473 C  CZ  . ARG B 1 29  ? 67.541 13.427 142.107 1.00 28.81 ? 134  ARG B CZ  1 
ATOM   1474 N  NH1 . ARG B 1 29  ? 67.945 14.360 142.966 1.00 24.33 ? 134  ARG B NH1 1 
ATOM   1475 N  NH2 . ARG B 1 29  ? 67.641 12.143 142.424 1.00 28.78 ? 134  ARG B NH2 1 
ATOM   1476 N  N   . ALA B 1 30  ? 64.764 19.013 137.268 1.00 14.39 ? 135  ALA B N   1 
ATOM   1477 C  CA  . ALA B 1 30  ? 64.685 20.461 137.163 1.00 16.40 ? 135  ALA B CA  1 
ATOM   1478 C  C   . ALA B 1 30  ? 63.278 20.946 136.837 1.00 16.67 ? 135  ALA B C   1 
ATOM   1479 O  O   . ALA B 1 30  ? 62.844 21.984 137.326 1.00 18.93 ? 135  ALA B O   1 
ATOM   1480 C  CB  . ALA B 1 30  ? 65.677 20.959 136.106 1.00 17.38 ? 135  ALA B CB  1 
ATOM   1481 N  N   . VAL B 1 31  ? 62.566 20.192 136.008 1.00 15.47 ? 136  VAL B N   1 
ATOM   1482 C  CA  . VAL B 1 31  ? 61.213 20.562 135.626 1.00 13.65 ? 136  VAL B CA  1 
ATOM   1483 C  C   . VAL B 1 31  ? 60.259 20.394 136.803 1.00 14.22 ? 136  VAL B C   1 
ATOM   1484 O  O   . VAL B 1 31  ? 59.362 21.211 137.016 1.00 13.15 ? 136  VAL B O   1 
ATOM   1485 C  CB  . VAL B 1 31  ? 60.721 19.694 134.433 1.00 14.12 ? 136  VAL B CB  1 
ATOM   1486 C  CG1 . VAL B 1 31  ? 59.229 19.926 134.177 1.00 9.73  ? 136  VAL B CG1 1 
ATOM   1487 C  CG2 . VAL B 1 31  ? 61.530 20.037 133.190 1.00 12.36 ? 136  VAL B CG2 1 
ATOM   1488 N  N   . ILE B 1 32  ? 60.460 19.323 137.563 1.00 15.06 ? 137  ILE B N   1 
ATOM   1489 C  CA  . ILE B 1 32  ? 59.617 19.029 138.709 1.00 13.17 ? 137  ILE B CA  1 
ATOM   1490 C  C   . ILE B 1 32  ? 59.862 20.025 139.830 1.00 15.99 ? 137  ILE B C   1 
ATOM   1491 O  O   . ILE B 1 32  ? 58.908 20.543 140.404 1.00 16.24 ? 137  ILE B O   1 
ATOM   1492 C  CB  . ILE B 1 32  ? 59.855 17.580 139.200 1.00 14.87 ? 137  ILE B CB  1 
ATOM   1493 C  CG1 . ILE B 1 32  ? 59.287 16.597 138.166 1.00 11.36 ? 137  ILE B CG1 1 
ATOM   1494 C  CG2 . ILE B 1 32  ? 59.229 17.371 140.571 1.00 14.89 ? 137  ILE B CG2 1 
ATOM   1495 C  CD1 . ILE B 1 32  ? 59.476 15.131 138.521 1.00 11.57 ? 137  ILE B CD1 1 
ATOM   1496 N  N   . ASP B 1 33  ? 61.132 20.308 140.134 1.00 15.66 ? 138  ASP B N   1 
ATOM   1497 C  CA  . ASP B 1 33  ? 61.447 21.279 141.184 1.00 15.15 ? 138  ASP B CA  1 
ATOM   1498 C  C   . ASP B 1 33  ? 60.752 22.603 140.871 1.00 15.48 ? 138  ASP B C   1 
ATOM   1499 O  O   . ASP B 1 33  ? 60.095 23.187 141.732 1.00 20.45 ? 138  ASP B O   1 
ATOM   1500 C  CB  . ASP B 1 33  ? 62.959 21.544 141.288 1.00 12.56 ? 138  ASP B CB  1 
ATOM   1501 C  CG  . ASP B 1 33  ? 63.746 20.351 141.803 1.00 10.35 ? 138  ASP B CG  1 
ATOM   1502 O  OD1 . ASP B 1 33  ? 63.156 19.399 142.353 1.00 11.63 ? 138  ASP B OD1 1 
ATOM   1503 O  OD2 . ASP B 1 33  ? 64.983 20.371 141.664 1.00 17.25 ? 138  ASP B OD2 1 
ATOM   1504 N  N   . ASP B 1 34  ? 60.902 23.069 139.635 1.00 14.76 ? 139  ASP B N   1 
ATOM   1505 C  CA  . ASP B 1 34  ? 60.313 24.328 139.189 1.00 13.88 ? 139  ASP B CA  1 
ATOM   1506 C  C   . ASP B 1 34  ? 58.785 24.354 139.267 1.00 13.68 ? 139  ASP B C   1 
ATOM   1507 O  O   . ASP B 1 34  ? 58.200 25.343 139.697 1.00 18.58 ? 139  ASP B O   1 
ATOM   1508 C  CB  . ASP B 1 34  ? 60.768 24.621 137.762 1.00 16.77 ? 139  ASP B CB  1 
ATOM   1509 C  CG  . ASP B 1 34  ? 60.207 25.919 137.221 1.00 19.24 ? 139  ASP B CG  1 
ATOM   1510 O  OD1 . ASP B 1 34  ? 60.611 26.985 137.721 1.00 20.16 ? 139  ASP B OD1 1 
ATOM   1511 O  OD2 . ASP B 1 34  ? 59.362 25.870 136.297 1.00 18.28 ? 139  ASP B OD2 1 
ATOM   1512 N  N   . ALA B 1 35  ? 58.135 23.276 138.850 1.00 12.86 ? 140  ALA B N   1 
ATOM   1513 C  CA  . ALA B 1 35  ? 56.679 23.204 138.907 1.00 10.91 ? 140  ALA B CA  1 
ATOM   1514 C  C   . ALA B 1 35  ? 56.174 23.343 140.347 1.00 13.69 ? 140  ALA B C   1 
ATOM   1515 O  O   . ALA B 1 35  ? 55.184 24.034 140.601 1.00 14.16 ? 140  ALA B O   1 
ATOM   1516 C  CB  . ALA B 1 35  ? 56.196 21.882 138.315 1.00 9.57  ? 140  ALA B CB  1 
ATOM   1517 N  N   . PHE B 1 36  ? 56.831 22.668 141.289 1.00 15.83 ? 141  PHE B N   1 
ATOM   1518 C  CA  . PHE B 1 36  ? 56.425 22.758 142.694 1.00 16.29 ? 141  PHE B CA  1 
ATOM   1519 C  C   . PHE B 1 36  ? 56.670 24.172 143.226 1.00 16.78 ? 141  PHE B C   1 
ATOM   1520 O  O   . PHE B 1 36  ? 55.871 24.709 143.990 1.00 19.28 ? 141  PHE B O   1 
ATOM   1521 C  CB  . PHE B 1 36  ? 57.182 21.737 143.559 1.00 13.24 ? 141  PHE B CB  1 
ATOM   1522 C  CG  . PHE B 1 36  ? 56.731 20.304 143.363 1.00 12.26 ? 141  PHE B CG  1 
ATOM   1523 C  CD1 . PHE B 1 36  ? 55.409 20.007 143.025 1.00 13.72 ? 141  PHE B CD1 1 
ATOM   1524 C  CD2 . PHE B 1 36  ? 57.628 19.251 143.516 1.00 9.81  ? 141  PHE B CD2 1 
ATOM   1525 C  CE1 . PHE B 1 36  ? 54.995 18.679 142.841 1.00 13.46 ? 141  PHE B CE1 1 
ATOM   1526 C  CE2 . PHE B 1 36  ? 57.224 17.927 143.337 1.00 7.35  ? 141  PHE B CE2 1 
ATOM   1527 C  CZ  . PHE B 1 36  ? 55.907 17.641 142.998 1.00 11.80 ? 141  PHE B CZ  1 
ATOM   1528 N  N   . ALA B 1 37  ? 57.772 24.783 142.807 1.00 17.38 ? 142  ALA B N   1 
ATOM   1529 C  CA  . ALA B 1 37  ? 58.093 26.136 143.246 1.00 17.57 ? 142  ALA B CA  1 
ATOM   1530 C  C   . ALA B 1 37  ? 57.061 27.149 142.738 1.00 18.95 ? 142  ALA B C   1 
ATOM   1531 O  O   . ALA B 1 37  ? 56.664 28.060 143.467 1.00 19.80 ? 142  ALA B O   1 
ATOM   1532 C  CB  . ALA B 1 37  ? 59.490 26.521 142.770 1.00 14.41 ? 142  ALA B CB  1 
ATOM   1533 N  N   . ARG B 1 38  ? 56.628 26.993 141.490 1.00 19.15 ? 143  ARG B N   1 
ATOM   1534 C  CA  . ARG B 1 38  ? 55.642 27.906 140.917 1.00 17.98 ? 143  ARG B CA  1 
ATOM   1535 C  C   . ARG B 1 38  ? 54.274 27.638 141.531 1.00 18.29 ? 143  ARG B C   1 
ATOM   1536 O  O   . ARG B 1 38  ? 53.451 28.544 141.661 1.00 22.02 ? 143  ARG B O   1 
ATOM   1537 C  CB  . ARG B 1 38  ? 55.596 27.761 139.388 1.00 16.03 ? 143  ARG B CB  1 
ATOM   1538 C  CG  . ARG B 1 38  ? 56.888 28.201 138.707 1.00 16.18 ? 143  ARG B CG  1 
ATOM   1539 C  CD  . ARG B 1 38  ? 56.812 28.138 137.181 1.00 18.32 ? 143  ARG B CD  1 
ATOM   1540 N  NE  . ARG B 1 38  ? 56.746 26.768 136.685 1.00 14.27 ? 143  ARG B NE  1 
ATOM   1541 C  CZ  . ARG B 1 38  ? 55.666 26.213 136.150 1.00 14.50 ? 143  ARG B CZ  1 
ATOM   1542 N  NH1 . ARG B 1 38  ? 54.548 26.912 136.030 1.00 12.39 ? 143  ARG B NH1 1 
ATOM   1543 N  NH2 . ARG B 1 38  ? 55.701 24.946 135.753 1.00 14.50 ? 143  ARG B NH2 1 
ATOM   1544 N  N   . ALA B 1 39  ? 54.036 26.392 141.927 1.00 17.80 ? 144  ALA B N   1 
ATOM   1545 C  CA  . ALA B 1 39  ? 52.768 26.030 142.552 1.00 17.21 ? 144  ALA B CA  1 
ATOM   1546 C  C   . ALA B 1 39  ? 52.660 26.677 143.941 1.00 19.87 ? 144  ALA B C   1 
ATOM   1547 O  O   . ALA B 1 39  ? 51.572 27.056 144.369 1.00 19.56 ? 144  ALA B O   1 
ATOM   1548 C  CB  . ALA B 1 39  ? 52.656 24.520 142.660 1.00 17.90 ? 144  ALA B CB  1 
ATOM   1549 N  N   . PHE B 1 40  ? 53.787 26.795 144.645 1.00 20.99 ? 145  PHE B N   1 
ATOM   1550 C  CA  . PHE B 1 40  ? 53.798 27.427 145.970 1.00 21.67 ? 145  PHE B CA  1 
ATOM   1551 C  C   . PHE B 1 40  ? 53.719 28.942 145.832 1.00 21.95 ? 145  PHE B C   1 
ATOM   1552 O  O   . PHE B 1 40  ? 53.101 29.613 146.652 1.00 25.86 ? 145  PHE B O   1 
ATOM   1553 C  CB  . PHE B 1 40  ? 55.072 27.069 146.759 1.00 18.85 ? 145  PHE B CB  1 
ATOM   1554 C  CG  . PHE B 1 40  ? 55.008 25.734 147.446 1.00 16.57 ? 145  PHE B CG  1 
ATOM   1555 C  CD1 . PHE B 1 40  ? 53.976 25.449 148.333 1.00 14.21 ? 145  PHE B CD1 1 
ATOM   1556 C  CD2 . PHE B 1 40  ? 55.974 24.764 147.204 1.00 14.86 ? 145  PHE B CD2 1 
ATOM   1557 C  CE1 . PHE B 1 40  ? 53.904 24.220 148.972 1.00 18.27 ? 145  PHE B CE1 1 
ATOM   1558 C  CE2 . PHE B 1 40  ? 55.917 23.527 147.836 1.00 19.57 ? 145  PHE B CE2 1 
ATOM   1559 C  CZ  . PHE B 1 40  ? 54.879 23.251 148.724 1.00 20.55 ? 145  PHE B CZ  1 
ATOM   1560 N  N   . ALA B 1 41  ? 54.356 29.481 144.802 1.00 20.87 ? 146  ALA B N   1 
ATOM   1561 C  CA  . ALA B 1 41  ? 54.344 30.921 144.576 1.00 21.45 ? 146  ALA B CA  1 
ATOM   1562 C  C   . ALA B 1 41  ? 52.930 31.466 144.360 1.00 23.06 ? 146  ALA B C   1 
ATOM   1563 O  O   . ALA B 1 41  ? 52.661 32.629 144.658 1.00 25.48 ? 146  ALA B O   1 
ATOM   1564 C  CB  . ALA B 1 41  ? 55.222 31.268 143.390 1.00 17.43 ? 146  ALA B CB  1 
ATOM   1565 N  N   . LEU B 1 42  ? 52.029 30.636 143.841 1.00 24.74 ? 147  LEU B N   1 
ATOM   1566 C  CA  . LEU B 1 42  ? 50.652 31.075 143.615 1.00 26.04 ? 147  LEU B CA  1 
ATOM   1567 C  C   . LEU B 1 42  ? 50.020 31.481 144.934 1.00 28.47 ? 147  LEU B C   1 
ATOM   1568 O  O   . LEU B 1 42  ? 49.343 32.500 145.030 1.00 30.66 ? 147  LEU B O   1 
ATOM   1569 C  CB  . LEU B 1 42  ? 49.797 29.958 143.010 1.00 24.21 ? 147  LEU B CB  1 
ATOM   1570 C  CG  . LEU B 1 42  ? 49.951 29.560 141.539 1.00 27.50 ? 147  LEU B CG  1 
ATOM   1571 C  CD1 . LEU B 1 42  ? 48.945 28.468 141.230 1.00 25.16 ? 147  LEU B CD1 1 
ATOM   1572 C  CD2 . LEU B 1 42  ? 49.718 30.754 140.630 1.00 23.79 ? 147  LEU B CD2 1 
ATOM   1573 N  N   . TRP B 1 43  ? 50.245 30.664 145.951 1.00 28.49 ? 148  TRP B N   1 
ATOM   1574 C  CA  . TRP B 1 43  ? 49.680 30.913 147.265 1.00 29.54 ? 148  TRP B CA  1 
ATOM   1575 C  C   . TRP B 1 43  ? 50.397 31.995 148.064 1.00 28.97 ? 148  TRP B C   1 
ATOM   1576 O  O   . TRP B 1 43  ? 49.752 32.844 148.674 1.00 29.64 ? 148  TRP B O   1 
ATOM   1577 C  CB  . TRP B 1 43  ? 49.652 29.609 148.053 1.00 26.39 ? 148  TRP B CB  1 
ATOM   1578 C  CG  . TRP B 1 43  ? 48.796 28.553 147.417 1.00 24.57 ? 148  TRP B CG  1 
ATOM   1579 C  CD1 . TRP B 1 43  ? 49.214 27.369 146.885 1.00 22.40 ? 148  TRP B CD1 1 
ATOM   1580 C  CD2 . TRP B 1 43  ? 47.366 28.550 147.330 1.00 25.64 ? 148  TRP B CD2 1 
ATOM   1581 N  NE1 . TRP B 1 43  ? 48.133 26.619 146.483 1.00 22.24 ? 148  TRP B NE1 1 
ATOM   1582 C  CE2 . TRP B 1 43  ? 46.986 27.320 146.747 1.00 24.80 ? 148  TRP B CE2 1 
ATOM   1583 C  CE3 . TRP B 1 43  ? 46.366 29.464 147.695 1.00 25.42 ? 148  TRP B CE3 1 
ATOM   1584 C  CZ2 . TRP B 1 43  ? 45.644 26.977 146.522 1.00 27.07 ? 148  TRP B CZ2 1 
ATOM   1585 C  CZ3 . TRP B 1 43  ? 45.029 29.122 147.471 1.00 26.11 ? 148  TRP B CZ3 1 
ATOM   1586 C  CH2 . TRP B 1 43  ? 44.684 27.889 146.892 1.00 24.97 ? 148  TRP B CH2 1 
ATOM   1587 N  N   . SER B 1 44  ? 51.724 31.979 148.063 1.00 30.94 ? 149  SER B N   1 
ATOM   1588 C  CA  . SER B 1 44  ? 52.474 32.986 148.808 1.00 33.11 ? 149  SER B CA  1 
ATOM   1589 C  C   . SER B 1 44  ? 52.241 34.372 148.221 1.00 35.39 ? 149  SER B C   1 
ATOM   1590 O  O   . SER B 1 44  ? 52.600 35.381 148.827 1.00 38.15 ? 149  SER B O   1 
ATOM   1591 C  CB  . SER B 1 44  ? 53.967 32.675 148.776 1.00 31.16 ? 149  SER B CB  1 
ATOM   1592 O  OG  . SER B 1 44  ? 54.465 32.773 147.457 1.00 34.33 ? 149  SER B OG  1 
ATOM   1593 N  N   . ALA B 1 45  ? 51.641 34.418 147.039 1.00 35.46 ? 150  ALA B N   1 
ATOM   1594 C  CA  . ALA B 1 45  ? 51.379 35.683 146.374 1.00 35.64 ? 150  ALA B CA  1 
ATOM   1595 C  C   . ALA B 1 45  ? 50.160 36.380 146.949 1.00 36.30 ? 150  ALA B C   1 
ATOM   1596 O  O   . ALA B 1 45  ? 50.054 37.600 146.875 1.00 35.93 ? 150  ALA B O   1 
ATOM   1597 C  CB  . ALA B 1 45  ? 51.187 35.457 144.883 1.00 35.78 ? 150  ALA B CB  1 
ATOM   1598 N  N   . VAL B 1 46  ? 49.238 35.611 147.519 1.00 36.26 ? 151  VAL B N   1 
ATOM   1599 C  CA  . VAL B 1 46  ? 48.031 36.196 148.089 1.00 37.29 ? 151  VAL B CA  1 
ATOM   1600 C  C   . VAL B 1 46  ? 47.926 36.035 149.606 1.00 37.54 ? 151  VAL B C   1 
ATOM   1601 O  O   . VAL B 1 46  ? 46.838 36.144 150.173 1.00 38.76 ? 151  VAL B O   1 
ATOM   1602 C  CB  . VAL B 1 46  ? 46.761 35.601 147.435 1.00 37.45 ? 151  VAL B CB  1 
ATOM   1603 C  CG1 . VAL B 1 46  ? 46.728 35.952 145.959 1.00 39.35 ? 151  VAL B CG1 1 
ATOM   1604 C  CG2 . VAL B 1 46  ? 46.735 34.099 147.614 1.00 37.42 ? 151  VAL B CG2 1 
ATOM   1605 N  N   . THR B 1 47  ? 49.057 35.774 150.257 1.00 36.72 ? 152  THR B N   1 
ATOM   1606 C  CA  . THR B 1 47  ? 49.098 35.611 151.711 1.00 34.50 ? 152  THR B CA  1 
ATOM   1607 C  C   . THR B 1 47  ? 50.484 35.975 152.241 1.00 34.43 ? 152  THR B C   1 
ATOM   1608 O  O   . THR B 1 47  ? 51.424 36.166 151.466 1.00 33.86 ? 152  THR B O   1 
ATOM   1609 C  CB  . THR B 1 47  ? 48.815 34.159 152.139 1.00 32.69 ? 152  THR B CB  1 
ATOM   1610 O  OG1 . THR B 1 47  ? 49.872 33.313 151.672 1.00 34.10 ? 152  THR B OG1 1 
ATOM   1611 C  CG2 . THR B 1 47  ? 47.492 33.677 151.587 1.00 33.09 ? 152  THR B CG2 1 
ATOM   1612 N  N   . PRO B 1 48  ? 50.624 36.084 153.576 1.00 35.88 ? 153  PRO B N   1 
ATOM   1613 C  CA  . PRO B 1 48  ? 51.909 36.423 154.199 1.00 35.29 ? 153  PRO B CA  1 
ATOM   1614 C  C   . PRO B 1 48  ? 52.810 35.190 154.341 1.00 33.55 ? 153  PRO B C   1 
ATOM   1615 O  O   . PRO B 1 48  ? 53.889 35.259 154.928 1.00 33.85 ? 153  PRO B O   1 
ATOM   1616 C  CB  . PRO B 1 48  ? 51.491 36.993 155.548 1.00 33.79 ? 153  PRO B CB  1 
ATOM   1617 C  CG  . PRO B 1 48  ? 50.313 36.136 155.894 1.00 36.98 ? 153  PRO B CG  1 
ATOM   1618 C  CD  . PRO B 1 48  ? 49.542 36.096 154.582 1.00 36.97 ? 153  PRO B CD  1 
ATOM   1619 N  N   . LEU B 1 49  ? 52.357 34.064 153.796 1.00 32.24 ? 154  LEU B N   1 
ATOM   1620 C  CA  . LEU B 1 49  ? 53.111 32.813 153.850 1.00 29.72 ? 154  LEU B CA  1 
ATOM   1621 C  C   . LEU B 1 49  ? 54.301 32.796 152.897 1.00 28.80 ? 154  LEU B C   1 
ATOM   1622 O  O   . LEU B 1 49  ? 54.253 33.384 151.817 1.00 29.79 ? 154  LEU B O   1 
ATOM   1623 C  CB  . LEU B 1 49  ? 52.210 31.634 153.485 1.00 28.34 ? 154  LEU B CB  1 
ATOM   1624 C  CG  . LEU B 1 49  ? 50.920 31.386 154.263 1.00 29.72 ? 154  LEU B CG  1 
ATOM   1625 C  CD1 . LEU B 1 49  ? 50.115 30.308 153.547 1.00 25.73 ? 154  LEU B CD1 1 
ATOM   1626 C  CD2 . LEU B 1 49  ? 51.241 30.971 155.697 1.00 27.68 ? 154  LEU B CD2 1 
ATOM   1627 N  N   . THR B 1 50  ? 55.370 32.123 153.307 1.00 26.47 ? 155  THR B N   1 
ATOM   1628 C  CA  . THR B 1 50  ? 56.550 31.968 152.468 1.00 26.48 ? 155  THR B CA  1 
ATOM   1629 C  C   . THR B 1 50  ? 56.822 30.469 152.444 1.00 27.63 ? 155  THR B C   1 
ATOM   1630 O  O   . THR B 1 50  ? 56.361 29.731 153.321 1.00 28.65 ? 155  THR B O   1 
ATOM   1631 C  CB  . THR B 1 50  ? 57.786 32.697 153.018 1.00 25.05 ? 155  THR B CB  1 
ATOM   1632 O  OG1 . THR B 1 50  ? 58.199 32.092 154.250 1.00 26.56 ? 155  THR B OG1 1 
ATOM   1633 C  CG2 . THR B 1 50  ? 57.478 34.161 153.235 1.00 26.91 ? 155  THR B CG2 1 
ATOM   1634 N  N   . PHE B 1 51  ? 57.561 30.020 151.438 1.00 26.34 ? 156  PHE B N   1 
ATOM   1635 C  CA  . PHE B 1 51  ? 57.858 28.603 151.289 1.00 24.22 ? 156  PHE B CA  1 
ATOM   1636 C  C   . PHE B 1 51  ? 59.338 28.362 151.045 1.00 23.36 ? 156  PHE B C   1 
ATOM   1637 O  O   . PHE B 1 51  ? 59.910 28.853 150.079 1.00 25.84 ? 156  PHE B O   1 
ATOM   1638 C  CB  . PHE B 1 51  ? 57.010 28.041 150.147 1.00 21.10 ? 156  PHE B CB  1 
ATOM   1639 C  CG  . PHE B 1 51  ? 55.531 28.101 150.419 1.00 21.18 ? 156  PHE B CG  1 
ATOM   1640 C  CD1 . PHE B 1 51  ? 54.916 27.141 151.229 1.00 19.72 ? 156  PHE B CD1 1 
ATOM   1641 C  CD2 . PHE B 1 51  ? 54.761 29.150 149.924 1.00 18.40 ? 156  PHE B CD2 1 
ATOM   1642 C  CE1 . PHE B 1 51  ? 53.560 27.231 151.541 1.00 18.13 ? 156  PHE B CE1 1 
ATOM   1643 C  CE2 . PHE B 1 51  ? 53.404 29.249 150.231 1.00 15.81 ? 156  PHE B CE2 1 
ATOM   1644 C  CZ  . PHE B 1 51  ? 52.803 28.291 151.040 1.00 17.61 ? 156  PHE B CZ  1 
ATOM   1645 N  N   . THR B 1 52  ? 59.951 27.596 151.938 1.00 24.03 ? 157  THR B N   1 
ATOM   1646 C  CA  . THR B 1 52  ? 61.375 27.302 151.858 1.00 22.52 ? 157  THR B CA  1 
ATOM   1647 C  C   . THR B 1 52  ? 61.629 25.824 151.638 1.00 21.11 ? 157  THR B C   1 
ATOM   1648 O  O   . THR B 1 52  ? 61.050 24.977 152.317 1.00 21.31 ? 157  THR B O   1 
ATOM   1649 C  CB  . THR B 1 52  ? 62.075 27.739 153.149 1.00 21.34 ? 157  THR B CB  1 
ATOM   1650 O  OG1 . THR B 1 52  ? 61.867 29.138 153.328 1.00 25.73 ? 157  THR B OG1 1 
ATOM   1651 C  CG2 . THR B 1 52  ? 63.567 27.461 153.091 1.00 20.97 ? 157  THR B CG2 1 
ATOM   1652 N  N   . ARG B 1 53  ? 62.502 25.521 150.688 1.00 21.15 ? 158  ARG B N   1 
ATOM   1653 C  CA  . ARG B 1 53  ? 62.831 24.138 150.385 1.00 21.88 ? 158  ARG B CA  1 
ATOM   1654 C  C   . ARG B 1 53  ? 63.963 23.657 151.284 1.00 22.35 ? 158  ARG B C   1 
ATOM   1655 O  O   . ARG B 1 53  ? 64.973 24.341 151.435 1.00 23.68 ? 158  ARG B O   1 
ATOM   1656 C  CB  . ARG B 1 53  ? 63.248 23.996 148.919 1.00 23.11 ? 158  ARG B CB  1 
ATOM   1657 C  CG  . ARG B 1 53  ? 63.532 22.559 148.524 1.00 20.37 ? 158  ARG B CG  1 
ATOM   1658 C  CD  . ARG B 1 53  ? 64.052 22.459 147.121 1.00 21.66 ? 158  ARG B CD  1 
ATOM   1659 N  NE  . ARG B 1 53  ? 64.381 21.083 146.772 1.00 18.52 ? 158  ARG B NE  1 
ATOM   1660 C  CZ  . ARG B 1 53  ? 64.905 20.721 145.610 1.00 17.45 ? 158  ARG B CZ  1 
ATOM   1661 N  NH1 . ARG B 1 53  ? 65.158 21.637 144.689 1.00 16.66 ? 158  ARG B NH1 1 
ATOM   1662 N  NH2 . ARG B 1 53  ? 65.174 19.447 145.372 1.00 15.63 ? 158  ARG B NH2 1 
ATOM   1663 N  N   . VAL B 1 54  ? 63.784 22.486 151.888 1.00 21.22 ? 159  VAL B N   1 
ATOM   1664 C  CA  . VAL B 1 54  ? 64.795 21.904 152.760 1.00 21.38 ? 159  VAL B CA  1 
ATOM   1665 C  C   . VAL B 1 54  ? 64.951 20.447 152.345 1.00 23.15 ? 159  VAL B C   1 
ATOM   1666 O  O   . VAL B 1 54  ? 64.240 19.988 151.456 1.00 23.36 ? 159  VAL B O   1 
ATOM   1667 C  CB  . VAL B 1 54  ? 64.384 22.006 154.252 1.00 21.61 ? 159  VAL B CB  1 
ATOM   1668 C  CG1 . VAL B 1 54  ? 64.096 23.462 154.600 1.00 19.88 ? 159  VAL B CG1 1 
ATOM   1669 C  CG2 . VAL B 1 54  ? 63.158 21.135 154.537 1.00 20.58 ? 159  VAL B CG2 1 
ATOM   1670 N  N   . TYR B 1 55  ? 65.864 19.717 152.982 1.00 24.51 ? 160  TYR B N   1 
ATOM   1671 C  CA  . TYR B 1 55  ? 66.100 18.321 152.613 1.00 25.70 ? 160  TYR B CA  1 
ATOM   1672 C  C   . TYR B 1 55  ? 65.991 17.297 153.735 1.00 27.77 ? 160  TYR B C   1 
ATOM   1673 O  O   . TYR B 1 55  ? 66.644 16.254 153.696 1.00 28.36 ? 160  TYR B O   1 
ATOM   1674 C  CB  . TYR B 1 55  ? 67.475 18.190 151.956 1.00 23.43 ? 160  TYR B CB  1 
ATOM   1675 C  CG  . TYR B 1 55  ? 67.634 19.050 150.728 1.00 23.94 ? 160  TYR B CG  1 
ATOM   1676 C  CD1 . TYR B 1 55  ? 67.800 20.430 150.837 1.00 22.81 ? 160  TYR B CD1 1 
ATOM   1677 C  CD2 . TYR B 1 55  ? 67.567 18.492 149.451 1.00 24.09 ? 160  TYR B CD2 1 
ATOM   1678 C  CE1 . TYR B 1 55  ? 67.891 21.233 149.703 1.00 24.82 ? 160  TYR B CE1 1 
ATOM   1679 C  CE2 . TYR B 1 55  ? 67.658 19.285 148.313 1.00 24.05 ? 160  TYR B CE2 1 
ATOM   1680 C  CZ  . TYR B 1 55  ? 67.820 20.652 148.445 1.00 25.74 ? 160  TYR B CZ  1 
ATOM   1681 O  OH  . TYR B 1 55  ? 67.919 21.438 147.319 1.00 32.12 ? 160  TYR B OH  1 
ATOM   1682 N  N   . SER B 1 56  ? 65.162 17.576 154.731 1.00 29.96 ? 161  SER B N   1 
ATOM   1683 C  CA  . SER B 1 56  ? 65.006 16.641 155.834 1.00 32.14 ? 161  SER B CA  1 
ATOM   1684 C  C   . SER B 1 56  ? 63.549 16.412 156.178 1.00 33.22 ? 161  SER B C   1 
ATOM   1685 O  O   . SER B 1 56  ? 62.667 17.155 155.750 1.00 29.83 ? 161  SER B O   1 
ATOM   1686 C  CB  . SER B 1 56  ? 65.751 17.144 157.077 1.00 32.84 ? 161  SER B CB  1 
ATOM   1687 O  OG  . SER B 1 56  ? 65.274 18.414 157.490 1.00 34.79 ? 161  SER B OG  1 
ATOM   1688 N  N   . ARG B 1 57  ? 63.319 15.376 156.973 1.00 37.03 ? 162  ARG B N   1 
ATOM   1689 C  CA  . ARG B 1 57  ? 61.990 14.999 157.418 1.00 40.29 ? 162  ARG B CA  1 
ATOM   1690 C  C   . ARG B 1 57  ? 61.395 16.078 158.325 1.00 38.61 ? 162  ARG B C   1 
ATOM   1691 O  O   . ARG B 1 57  ? 60.264 15.949 158.781 1.00 39.20 ? 162  ARG B O   1 
ATOM   1692 C  CB  . ARG B 1 57  ? 62.071 13.676 158.176 1.00 46.56 ? 162  ARG B CB  1 
ATOM   1693 C  CG  . ARG B 1 57  ? 60.957 12.699 157.863 1.00 57.91 ? 162  ARG B CG  1 
ATOM   1694 C  CD  . ARG B 1 57  ? 61.049 11.467 158.757 1.00 64.70 ? 162  ARG B CD  1 
ATOM   1695 N  NE  . ARG B 1 57  ? 59.974 10.514 158.490 1.00 70.47 ? 162  ARG B NE  1 
ATOM   1696 C  CZ  . ARG B 1 57  ? 59.694 9.466  159.260 1.00 73.51 ? 162  ARG B CZ  1 
ATOM   1697 N  NH1 . ARG B 1 57  ? 58.698 8.651  158.937 1.00 74.22 ? 162  ARG B NH1 1 
ATOM   1698 N  NH2 . ARG B 1 57  ? 60.406 9.237  160.357 1.00 74.50 ? 162  ARG B NH2 1 
ATOM   1699 N  N   . ASP B 1 58  ? 62.160 17.135 158.583 1.00 37.90 ? 163  ASP B N   1 
ATOM   1700 C  CA  . ASP B 1 58  ? 61.707 18.233 159.438 1.00 36.97 ? 163  ASP B CA  1 
ATOM   1701 C  C   . ASP B 1 58  ? 60.784 19.198 158.706 1.00 33.52 ? 163  ASP B C   1 
ATOM   1702 O  O   . ASP B 1 58  ? 60.165 20.065 159.326 1.00 33.69 ? 163  ASP B O   1 
ATOM   1703 C  CB  . ASP B 1 58  ? 62.894 19.043 159.971 1.00 42.42 ? 163  ASP B CB  1 
ATOM   1704 C  CG  . ASP B 1 58  ? 63.908 18.195 160.698 1.00 46.87 ? 163  ASP B CG  1 
ATOM   1705 O  OD1 . ASP B 1 58  ? 63.505 17.346 161.523 1.00 49.44 ? 163  ASP B OD1 1 
ATOM   1706 O  OD2 . ASP B 1 58  ? 65.116 18.393 160.451 1.00 50.63 ? 163  ASP B OD2 1 
ATOM   1707 N  N   . ALA B 1 59  ? 60.706 19.065 157.389 1.00 29.73 ? 164  ALA B N   1 
ATOM   1708 C  CA  . ALA B 1 59  ? 59.864 19.948 156.594 1.00 25.02 ? 164  ALA B CA  1 
ATOM   1709 C  C   . ALA B 1 59  ? 58.408 19.808 157.005 1.00 22.73 ? 164  ALA B C   1 
ATOM   1710 O  O   . ALA B 1 59  ? 57.983 18.743 157.453 1.00 18.59 ? 164  ALA B O   1 
ATOM   1711 C  CB  . ALA B 1 59  ? 60.019 19.620 155.116 1.00 24.48 ? 164  ALA B CB  1 
ATOM   1712 N  N   . ASP B 1 60  ? 57.644 20.886 156.865 1.00 20.01 ? 165  ASP B N   1 
ATOM   1713 C  CA  . ASP B 1 60  ? 56.226 20.835 157.207 1.00 19.49 ? 165  ASP B CA  1 
ATOM   1714 C  C   . ASP B 1 60  ? 55.486 20.055 156.128 1.00 20.86 ? 165  ASP B C   1 
ATOM   1715 O  O   . ASP B 1 60  ? 54.620 19.240 156.417 1.00 19.12 ? 165  ASP B O   1 
ATOM   1716 C  CB  . ASP B 1 60  ? 55.625 22.240 157.298 1.00 17.17 ? 165  ASP B CB  1 
ATOM   1717 C  CG  . ASP B 1 60  ? 56.279 23.087 158.365 1.00 15.31 ? 165  ASP B CG  1 
ATOM   1718 O  OD1 . ASP B 1 60  ? 56.422 22.601 159.505 1.00 16.45 ? 165  ASP B OD1 1 
ATOM   1719 O  OD2 . ASP B 1 60  ? 56.643 24.242 158.066 1.00 14.81 ? 165  ASP B OD2 1 
ATOM   1720 N  N   . ILE B 1 61  ? 55.836 20.312 154.875 1.00 20.30 ? 166  ILE B N   1 
ATOM   1721 C  CA  . ILE B 1 61  ? 55.183 19.646 153.760 1.00 17.16 ? 166  ILE B CA  1 
ATOM   1722 C  C   . ILE B 1 61  ? 56.138 18.694 153.058 1.00 15.84 ? 166  ILE B C   1 
ATOM   1723 O  O   . ILE B 1 61  ? 57.096 19.114 152.411 1.00 16.45 ? 166  ILE B O   1 
ATOM   1724 C  CB  . ILE B 1 61  ? 54.640 20.692 152.748 1.00 19.96 ? 166  ILE B CB  1 
ATOM   1725 C  CG1 . ILE B 1 61  ? 53.611 21.587 153.449 1.00 20.77 ? 166  ILE B CG1 1 
ATOM   1726 C  CG2 . ILE B 1 61  ? 54.032 19.995 151.530 1.00 16.75 ? 166  ILE B CG2 1 
ATOM   1727 C  CD1 . ILE B 1 61  ? 53.139 22.769 152.625 1.00 16.61 ? 166  ILE B CD1 1 
ATOM   1728 N  N   . VAL B 1 62  ? 55.883 17.405 153.207 1.00 13.42 ? 167  VAL B N   1 
ATOM   1729 C  CA  . VAL B 1 62  ? 56.711 16.408 152.567 1.00 13.63 ? 167  VAL B CA  1 
ATOM   1730 C  C   . VAL B 1 62  ? 55.991 15.939 151.310 1.00 14.94 ? 167  VAL B C   1 
ATOM   1731 O  O   . VAL B 1 62  ? 54.826 15.535 151.358 1.00 15.76 ? 167  VAL B O   1 
ATOM   1732 C  CB  . VAL B 1 62  ? 56.977 15.221 153.498 1.00 13.46 ? 167  VAL B CB  1 
ATOM   1733 C  CG1 . VAL B 1 62  ? 57.737 14.136 152.750 1.00 11.25 ? 167  VAL B CG1 1 
ATOM   1734 C  CG2 . VAL B 1 62  ? 57.773 15.694 154.713 1.00 12.79 ? 167  VAL B CG2 1 
ATOM   1735 N  N   . ILE B 1 63  ? 56.698 16.015 150.187 1.00 13.79 ? 168  ILE B N   1 
ATOM   1736 C  CA  . ILE B 1 63  ? 56.165 15.636 148.886 1.00 12.71 ? 168  ILE B CA  1 
ATOM   1737 C  C   . ILE B 1 63  ? 56.749 14.334 148.381 1.00 13.67 ? 168  ILE B C   1 
ATOM   1738 O  O   . ILE B 1 63  ? 57.949 14.096 148.491 1.00 11.91 ? 168  ILE B O   1 
ATOM   1739 C  CB  . ILE B 1 63  ? 56.472 16.714 147.857 1.00 14.97 ? 168  ILE B CB  1 
ATOM   1740 C  CG1 . ILE B 1 63  ? 55.919 18.059 148.348 1.00 13.19 ? 168  ILE B CG1 1 
ATOM   1741 C  CG2 . ILE B 1 63  ? 55.912 16.306 146.503 1.00 13.61 ? 168  ILE B CG2 1 
ATOM   1742 C  CD1 . ILE B 1 63  ? 56.377 19.259 147.543 1.00 14.12 ? 168  ILE B CD1 1 
ATOM   1743 N  N   . GLN B 1 64  ? 55.903 13.481 147.820 1.00 14.64 ? 169  GLN B N   1 
ATOM   1744 C  CA  . GLN B 1 64  ? 56.400 12.230 147.291 1.00 17.38 ? 169  GLN B CA  1 
ATOM   1745 C  C   . GLN B 1 64  ? 55.511 11.625 146.226 1.00 16.18 ? 169  GLN B C   1 
ATOM   1746 O  O   . GLN B 1 64  ? 54.304 11.856 146.204 1.00 14.81 ? 169  GLN B O   1 
ATOM   1747 C  CB  . GLN B 1 64  ? 56.599 11.209 148.412 1.00 20.52 ? 169  GLN B CB  1 
ATOM   1748 C  CG  . GLN B 1 64  ? 55.328 10.614 148.956 1.00 28.99 ? 169  GLN B CG  1 
ATOM   1749 C  CD  . GLN B 1 64  ? 55.589 9.395  149.828 1.00 34.11 ? 169  GLN B CD  1 
ATOM   1750 O  OE1 . GLN B 1 64  ? 55.972 8.329  149.334 1.00 34.45 ? 169  GLN B OE1 1 
ATOM   1751 N  NE2 . GLN B 1 64  ? 55.392 9.550  151.134 1.00 36.00 ? 169  GLN B NE2 1 
ATOM   1752 N  N   . PHE B 1 65  ? 56.141 10.859 145.339 1.00 14.40 ? 170  PHE B N   1 
ATOM   1753 C  CA  . PHE B 1 65  ? 55.463 10.147 144.274 1.00 13.46 ? 170  PHE B CA  1 
ATOM   1754 C  C   . PHE B 1 65  ? 55.414 8.685  144.681 1.00 14.78 ? 170  PHE B C   1 
ATOM   1755 O  O   . PHE B 1 65  ? 56.389 8.160  145.202 1.00 16.19 ? 170  PHE B O   1 
ATOM   1756 C  CB  . PHE B 1 65  ? 56.237 10.257 142.959 1.00 9.79  ? 170  PHE B CB  1 
ATOM   1757 C  CG  . PHE B 1 65  ? 56.265 11.642 142.386 1.00 11.55 ? 170  PHE B CG  1 
ATOM   1758 C  CD1 . PHE B 1 65  ? 57.172 12.581 142.852 1.00 12.24 ? 170  PHE B CD1 1 
ATOM   1759 C  CD2 . PHE B 1 65  ? 55.371 12.012 141.388 1.00 12.04 ? 170  PHE B CD2 1 
ATOM   1760 C  CE1 . PHE B 1 65  ? 57.191 13.874 142.334 1.00 12.05 ? 170  PHE B CE1 1 
ATOM   1761 C  CE2 . PHE B 1 65  ? 55.379 13.306 140.865 1.00 11.98 ? 170  PHE B CE2 1 
ATOM   1762 C  CZ  . PHE B 1 65  ? 56.288 14.237 141.338 1.00 13.47 ? 170  PHE B CZ  1 
ATOM   1763 N  N   . GLY B 1 66  ? 54.283 8.028  144.446 1.00 16.63 ? 171  GLY B N   1 
ATOM   1764 C  CA  . GLY B 1 66  ? 54.170 6.626  144.795 1.00 18.19 ? 171  GLY B CA  1 
ATOM   1765 C  C   . GLY B 1 66  ? 53.143 5.900  143.951 1.00 20.06 ? 171  GLY B C   1 
ATOM   1766 O  O   . GLY B 1 66  ? 52.352 6.535  143.260 1.00 21.45 ? 171  GLY B O   1 
ATOM   1767 N  N   . VAL B 1 67  ? 53.168 4.572  143.988 1.00 21.07 ? 172  VAL B N   1 
ATOM   1768 C  CA  . VAL B 1 67  ? 52.206 3.764  143.247 1.00 22.74 ? 172  VAL B CA  1 
ATOM   1769 C  C   . VAL B 1 67  ? 51.547 2.773  144.203 1.00 24.58 ? 172  VAL B C   1 
ATOM   1770 O  O   . VAL B 1 67  ? 52.210 2.174  145.055 1.00 24.53 ? 172  VAL B O   1 
ATOM   1771 C  CB  . VAL B 1 67  ? 52.875 2.967  142.109 1.00 22.64 ? 172  VAL B CB  1 
ATOM   1772 C  CG1 . VAL B 1 67  ? 53.593 3.913  141.170 1.00 22.95 ? 172  VAL B CG1 1 
ATOM   1773 C  CG2 . VAL B 1 67  ? 53.832 1.943  142.686 1.00 23.18 ? 172  VAL B CG2 1 
ATOM   1774 N  N   . ALA B 1 68  ? 50.238 2.607  144.061 1.00 25.72 ? 173  ALA B N   1 
ATOM   1775 C  CA  . ALA B 1 68  ? 49.498 1.690  144.912 1.00 25.50 ? 173  ALA B CA  1 
ATOM   1776 C  C   . ALA B 1 68  ? 49.826 1.959  146.379 1.00 25.00 ? 173  ALA B C   1 
ATOM   1777 O  O   . ALA B 1 68  ? 49.761 3.106  146.836 1.00 23.10 ? 173  ALA B O   1 
ATOM   1778 C  CB  . ALA B 1 68  ? 49.845 0.256  144.543 1.00 24.40 ? 173  ALA B CB  1 
ATOM   1779 N  N   . GLU B 1 69  ? 50.179 0.902  147.105 1.00 26.18 ? 174  GLU B N   1 
ATOM   1780 C  CA  . GLU B 1 69  ? 50.521 1.002  148.523 1.00 30.44 ? 174  GLU B CA  1 
ATOM   1781 C  C   . GLU B 1 69  ? 51.810 1.802  148.647 1.00 28.21 ? 174  GLU B C   1 
ATOM   1782 O  O   . GLU B 1 69  ? 52.839 1.399  148.108 1.00 26.23 ? 174  GLU B O   1 
ATOM   1783 C  CB  . GLU B 1 69  ? 50.756 -0.391 149.113 1.00 37.69 ? 174  GLU B CB  1 
ATOM   1784 C  CG  . GLU B 1 69  ? 49.929 -1.502 148.484 1.00 50.32 ? 174  GLU B CG  1 
ATOM   1785 C  CD  . GLU B 1 69  ? 48.452 -1.388 148.800 1.00 56.96 ? 174  GLU B CD  1 
ATOM   1786 O  OE1 . GLU B 1 69  ? 47.671 -2.226 148.296 1.00 59.68 ? 174  GLU B OE1 1 
ATOM   1787 O  OE2 . GLU B 1 69  ? 48.074 -0.464 149.555 1.00 61.18 ? 174  GLU B OE2 1 
ATOM   1788 N  N   . HIS B 1 70  ? 51.776 2.922  149.360 1.00 26.31 ? 175  HIS B N   1 
ATOM   1789 C  CA  . HIS B 1 70  ? 52.989 3.723  149.488 1.00 26.29 ? 175  HIS B CA  1 
ATOM   1790 C  C   . HIS B 1 70  ? 53.334 4.246  150.890 1.00 27.55 ? 175  HIS B C   1 
ATOM   1791 O  O   . HIS B 1 70  ? 54.057 5.231  151.019 1.00 26.45 ? 175  HIS B O   1 
ATOM   1792 C  CB  . HIS B 1 70  ? 52.935 4.898  148.500 1.00 21.05 ? 175  HIS B CB  1 
ATOM   1793 C  CG  . HIS B 1 70  ? 51.733 5.777  148.671 1.00 19.27 ? 175  HIS B CG  1 
ATOM   1794 N  ND1 . HIS B 1 70  ? 50.526 5.519  148.056 1.00 15.56 ? 175  HIS B ND1 1 
ATOM   1795 C  CD2 . HIS B 1 70  ? 51.536 6.874  149.438 1.00 17.23 ? 175  HIS B CD2 1 
ATOM   1796 C  CE1 . HIS B 1 70  ? 49.638 6.416  148.441 1.00 14.96 ? 175  HIS B CE1 1 
ATOM   1797 N  NE2 . HIS B 1 70  ? 50.225 7.248  149.281 1.00 13.17 ? 175  HIS B NE2 1 
ATOM   1798 N  N   . GLY B 1 71  ? 52.831 3.601  151.940 1.00 30.22 ? 176  GLY B N   1 
ATOM   1799 C  CA  . GLY B 1 71  ? 53.154 4.070  153.280 1.00 32.63 ? 176  GLY B CA  1 
ATOM   1800 C  C   . GLY B 1 71  ? 51.972 4.307  154.198 1.00 35.23 ? 176  GLY B C   1 
ATOM   1801 O  O   . GLY B 1 71  ? 51.827 3.621  155.209 1.00 39.12 ? 176  GLY B O   1 
ATOM   1802 N  N   . ASP B 1 72  ? 51.138 5.289  153.875 1.00 33.34 ? 177  ASP B N   1 
ATOM   1803 C  CA  . ASP B 1 72  ? 49.968 5.563  154.692 1.00 33.01 ? 177  ASP B CA  1 
ATOM   1804 C  C   . ASP B 1 72  ? 48.969 4.438  154.475 1.00 33.84 ? 177  ASP B C   1 
ATOM   1805 O  O   . ASP B 1 72  ? 49.323 3.368  153.982 1.00 35.39 ? 177  ASP B O   1 
ATOM   1806 C  CB  . ASP B 1 72  ? 49.343 6.899  154.299 1.00 34.56 ? 177  ASP B CB  1 
ATOM   1807 C  CG  . ASP B 1 72  ? 49.366 7.138  152.797 1.00 33.72 ? 177  ASP B CG  1 
ATOM   1808 O  OD1 . ASP B 1 72  ? 49.119 6.191  152.023 1.00 30.99 ? 177  ASP B OD1 1 
ATOM   1809 O  OD2 . ASP B 1 72  ? 49.623 8.286  152.395 1.00 32.06 ? 177  ASP B OD2 1 
ATOM   1810 N  N   . GLY B 1 73  ? 47.719 4.666  154.837 1.00 34.25 ? 178  GLY B N   1 
ATOM   1811 C  CA  . GLY B 1 73  ? 46.732 3.620  154.641 1.00 36.75 ? 178  GLY B CA  1 
ATOM   1812 C  C   . GLY B 1 73  ? 45.836 3.952  153.474 1.00 35.04 ? 178  GLY B C   1 
ATOM   1813 O  O   . GLY B 1 73  ? 44.705 3.478  153.390 1.00 37.61 ? 178  GLY B O   1 
ATOM   1814 N  N   . TYR B 1 74  ? 46.359 4.768  152.566 1.00 33.73 ? 179  TYR B N   1 
ATOM   1815 C  CA  . TYR B 1 74  ? 45.597 5.200  151.409 1.00 32.53 ? 179  TYR B CA  1 
ATOM   1816 C  C   . TYR B 1 74  ? 46.309 4.931  150.089 1.00 30.01 ? 179  TYR B C   1 
ATOM   1817 O  O   . TYR B 1 74  ? 46.907 5.825  149.503 1.00 29.44 ? 179  TYR B O   1 
ATOM   1818 C  CB  . TYR B 1 74  ? 45.285 6.690  151.545 1.00 35.60 ? 179  TYR B CB  1 
ATOM   1819 C  CG  . TYR B 1 74  ? 44.636 7.044  152.867 1.00 40.89 ? 179  TYR B CG  1 
ATOM   1820 C  CD1 . TYR B 1 74  ? 45.334 6.907  154.070 1.00 43.33 ? 179  TYR B CD1 1 
ATOM   1821 C  CD2 . TYR B 1 74  ? 43.318 7.492  152.922 1.00 42.09 ? 179  TYR B CD2 1 
ATOM   1822 C  CE1 . TYR B 1 74  ? 44.736 7.204  155.290 1.00 43.67 ? 179  TYR B CE1 1 
ATOM   1823 C  CE2 . TYR B 1 74  ? 42.711 7.794  154.140 1.00 42.63 ? 179  TYR B CE2 1 
ATOM   1824 C  CZ  . TYR B 1 74  ? 43.426 7.647  155.317 1.00 43.63 ? 179  TYR B CZ  1 
ATOM   1825 O  OH  . TYR B 1 74  ? 42.835 7.947  156.519 1.00 45.29 ? 179  TYR B OH  1 
ATOM   1826 N  N   . PRO B 1 75  ? 46.255 3.686  149.604 1.00 29.94 ? 180  PRO B N   1 
ATOM   1827 C  CA  . PRO B 1 75  ? 46.918 3.366  148.335 1.00 28.82 ? 180  PRO B CA  1 
ATOM   1828 C  C   . PRO B 1 75  ? 46.253 4.029  147.128 1.00 28.62 ? 180  PRO B C   1 
ATOM   1829 O  O   . PRO B 1 75  ? 45.070 4.372  147.167 1.00 30.61 ? 180  PRO B O   1 
ATOM   1830 C  CB  . PRO B 1 75  ? 46.838 1.843  148.280 1.00 29.21 ? 180  PRO B CB  1 
ATOM   1831 C  CG  . PRO B 1 75  ? 45.590 1.533  149.067 1.00 30.96 ? 180  PRO B CG  1 
ATOM   1832 C  CD  . PRO B 1 75  ? 45.706 2.475  150.238 1.00 28.60 ? 180  PRO B CD  1 
ATOM   1833 N  N   . PHE B 1 76  ? 47.023 4.225  146.062 1.00 26.71 ? 181  PHE B N   1 
ATOM   1834 C  CA  . PHE B 1 76  ? 46.475 4.825  144.851 1.00 26.70 ? 181  PHE B CA  1 
ATOM   1835 C  C   . PHE B 1 76  ? 45.810 3.733  144.017 1.00 26.77 ? 181  PHE B C   1 
ATOM   1836 O  O   . PHE B 1 76  ? 46.020 2.546  144.261 1.00 23.82 ? 181  PHE B O   1 
ATOM   1837 C  CB  . PHE B 1 76  ? 47.568 5.547  144.055 1.00 22.42 ? 181  PHE B CB  1 
ATOM   1838 C  CG  . PHE B 1 76  ? 48.019 6.842  144.687 1.00 17.95 ? 181  PHE B CG  1 
ATOM   1839 C  CD1 . PHE B 1 76  ? 47.108 7.871  144.919 1.00 16.47 ? 181  PHE B CD1 1 
ATOM   1840 C  CD2 . PHE B 1 76  ? 49.349 7.029  145.058 1.00 17.30 ? 181  PHE B CD2 1 
ATOM   1841 C  CE1 . PHE B 1 76  ? 47.511 9.069  145.511 1.00 14.31 ? 181  PHE B CE1 1 
ATOM   1842 C  CE2 . PHE B 1 76  ? 49.765 8.221  145.650 1.00 14.81 ? 181  PHE B CE2 1 
ATOM   1843 C  CZ  . PHE B 1 76  ? 48.842 9.245  145.877 1.00 16.31 ? 181  PHE B CZ  1 
ATOM   1844 N  N   . ASP B 1 77  ? 45.017 4.142  143.032 1.00 28.61 ? 182  ASP B N   1 
ATOM   1845 C  CA  . ASP B 1 77  ? 44.259 3.209  142.203 1.00 29.98 ? 182  ASP B CA  1 
ATOM   1846 C  C   . ASP B 1 77  ? 44.731 2.976  140.768 1.00 30.43 ? 182  ASP B C   1 
ATOM   1847 O  O   . ASP B 1 77  ? 43.924 2.646  139.909 1.00 30.49 ? 182  ASP B O   1 
ATOM   1848 C  CB  . ASP B 1 77  ? 42.808 3.674  142.164 1.00 29.97 ? 182  ASP B CB  1 
ATOM   1849 C  CG  . ASP B 1 77  ? 42.698 5.131  141.810 1.00 30.41 ? 182  ASP B CG  1 
ATOM   1850 O  OD1 . ASP B 1 77  ? 43.709 5.661  141.331 1.00 35.31 ? 182  ASP B OD1 1 
ATOM   1851 O  OD2 . ASP B 1 77  ? 41.631 5.750  141.995 1.00 33.11 ? 182  ASP B OD2 1 
ATOM   1852 N  N   . GLY B 1 78  ? 46.020 3.128  140.499 1.00 30.89 ? 183  GLY B N   1 
ATOM   1853 C  CA  . GLY B 1 78  ? 46.493 2.905  139.146 1.00 29.05 ? 183  GLY B CA  1 
ATOM   1854 C  C   . GLY B 1 78  ? 46.142 4.064  138.237 1.00 29.44 ? 183  GLY B C   1 
ATOM   1855 O  O   . GLY B 1 78  ? 45.789 5.131  138.723 1.00 25.58 ? 183  GLY B O   1 
ATOM   1856 N  N   . LYS B 1 79  ? 46.217 3.849  136.925 1.00 29.06 ? 184  LYS B N   1 
ATOM   1857 C  CA  . LYS B 1 79  ? 45.936 4.895  135.943 1.00 30.26 ? 184  LYS B CA  1 
ATOM   1858 C  C   . LYS B 1 79  ? 44.565 5.565  136.087 1.00 28.94 ? 184  LYS B C   1 
ATOM   1859 O  O   . LYS B 1 79  ? 43.545 4.901  136.239 1.00 30.47 ? 184  LYS B O   1 
ATOM   1860 C  CB  . LYS B 1 79  ? 46.100 4.322  134.535 1.00 33.27 ? 184  LYS B CB  1 
ATOM   1861 C  CG  . LYS B 1 79  ? 45.992 5.346  133.426 1.00 36.93 ? 184  LYS B CG  1 
ATOM   1862 C  CD  . LYS B 1 79  ? 46.258 4.704  132.077 1.00 41.28 ? 184  LYS B CD  1 
ATOM   1863 C  CE  . LYS B 1 79  ? 46.044 5.691  130.936 1.00 44.88 ? 184  LYS B CE  1 
ATOM   1864 N  NZ  . LYS B 1 79  ? 44.634 6.176  130.859 1.00 43.95 ? 184  LYS B NZ  1 
ATOM   1865 N  N   . ASP B 1 80  ? 44.561 6.892  136.034 1.00 29.99 ? 185  ASP B N   1 
ATOM   1866 C  CA  . ASP B 1 80  ? 43.347 7.692  136.166 1.00 30.47 ? 185  ASP B CA  1 
ATOM   1867 C  C   . ASP B 1 80  ? 42.642 7.509  137.506 1.00 31.65 ? 185  ASP B C   1 
ATOM   1868 O  O   . ASP B 1 80  ? 43.099 6.765  138.363 1.00 32.44 ? 185  ASP B O   1 
ATOM   1869 C  CB  . ASP B 1 80  ? 42.367 7.376  135.035 1.00 35.39 ? 185  ASP B CB  1 
ATOM   1870 C  CG  . ASP B 1 80  ? 42.877 7.826  133.684 1.00 38.40 ? 185  ASP B CG  1 
ATOM   1871 O  OD1 . ASP B 1 80  ? 43.081 9.045  133.491 1.00 39.28 ? 185  ASP B OD1 1 
ATOM   1872 O  OD2 . ASP B 1 80  ? 43.078 6.954  132.814 1.00 42.49 ? 185  ASP B OD2 1 
ATOM   1873 N  N   . GLY B 1 81  ? 41.509 8.181  137.670 1.00 29.41 ? 186  GLY B N   1 
ATOM   1874 C  CA  . GLY B 1 81  ? 40.774 8.091  138.912 1.00 27.84 ? 186  GLY B CA  1 
ATOM   1875 C  C   . GLY B 1 81  ? 41.335 9.123  139.864 1.00 27.88 ? 186  GLY B C   1 
ATOM   1876 O  O   . GLY B 1 81  ? 41.355 10.310 139.549 1.00 29.24 ? 186  GLY B O   1 
ATOM   1877 N  N   . LEU B 1 82  ? 41.792 8.678  141.030 1.00 27.15 ? 187  LEU B N   1 
ATOM   1878 C  CA  . LEU B 1 82  ? 42.376 9.585  142.015 1.00 25.82 ? 187  LEU B CA  1 
ATOM   1879 C  C   . LEU B 1 82  ? 43.771 9.971  141.520 1.00 22.60 ? 187  LEU B C   1 
ATOM   1880 O  O   . LEU B 1 82  ? 44.593 9.106  141.265 1.00 17.85 ? 187  LEU B O   1 
ATOM   1881 C  CB  . LEU B 1 82  ? 42.493 8.878  143.359 1.00 27.95 ? 187  LEU B CB  1 
ATOM   1882 C  CG  . LEU B 1 82  ? 42.940 9.772  144.507 1.00 30.41 ? 187  LEU B CG  1 
ATOM   1883 C  CD1 . LEU B 1 82  ? 41.855 10.797 144.779 1.00 28.19 ? 187  LEU B CD1 1 
ATOM   1884 C  CD2 . LEU B 1 82  ? 43.205 8.927  145.746 1.00 34.06 ? 187  LEU B CD2 1 
ATOM   1885 N  N   . LEU B 1 83  ? 44.047 11.262 141.397 1.00 22.16 ? 188  LEU B N   1 
ATOM   1886 C  CA  . LEU B 1 83  ? 45.346 11.700 140.884 1.00 22.33 ? 188  LEU B CA  1 
ATOM   1887 C  C   . LEU B 1 83  ? 46.400 11.897 141.965 1.00 23.14 ? 188  LEU B C   1 
ATOM   1888 O  O   . LEU B 1 83  ? 47.593 11.658 141.749 1.00 22.98 ? 188  LEU B O   1 
ATOM   1889 C  CB  . LEU B 1 83  ? 45.177 13.002 140.095 1.00 19.27 ? 188  LEU B CB  1 
ATOM   1890 C  CG  . LEU B 1 83  ? 44.127 12.970 138.979 1.00 20.81 ? 188  LEU B CG  1 
ATOM   1891 C  CD1 . LEU B 1 83  ? 44.110 14.305 138.252 1.00 12.81 ? 188  LEU B CD1 1 
ATOM   1892 C  CD2 . LEU B 1 83  ? 44.425 11.823 138.013 1.00 17.71 ? 188  LEU B CD2 1 
ATOM   1893 N  N   . ALA B 1 84  ? 45.948 12.331 143.131 1.00 23.03 ? 189  ALA B N   1 
ATOM   1894 C  CA  . ALA B 1 84  ? 46.830 12.585 144.255 1.00 22.63 ? 189  ALA B CA  1 
ATOM   1895 C  C   . ALA B 1 84  ? 45.974 12.896 145.472 1.00 23.10 ? 189  ALA B C   1 
ATOM   1896 O  O   . ALA B 1 84  ? 44.751 12.932 145.378 1.00 25.16 ? 189  ALA B O   1 
ATOM   1897 C  CB  . ALA B 1 84  ? 47.717 13.768 143.942 1.00 21.82 ? 189  ALA B CB  1 
ATOM   1898 N  N   . HIS B 1 85  ? 46.622 13.104 146.613 1.00 22.01 ? 190  HIS B N   1 
ATOM   1899 C  CA  . HIS B 1 85  ? 45.927 13.458 147.840 1.00 21.61 ? 190  HIS B CA  1 
ATOM   1900 C  C   . HIS B 1 85  ? 46.898 14.097 148.822 1.00 22.17 ? 190  HIS B C   1 
ATOM   1901 O  O   . HIS B 1 85  ? 48.086 13.786 148.818 1.00 21.16 ? 190  HIS B O   1 
ATOM   1902 C  CB  . HIS B 1 85  ? 45.218 12.237 148.451 1.00 19.44 ? 190  HIS B CB  1 
ATOM   1903 C  CG  . HIS B 1 85  ? 46.126 11.110 148.838 1.00 21.62 ? 190  HIS B CG  1 
ATOM   1904 N  ND1 . HIS B 1 85  ? 45.771 9.787  148.673 1.00 20.29 ? 190  HIS B ND1 1 
ATOM   1905 C  CD2 . HIS B 1 85  ? 47.343 11.101 149.434 1.00 23.01 ? 190  HIS B CD2 1 
ATOM   1906 C  CE1 . HIS B 1 85  ? 46.730 9.013  149.151 1.00 20.79 ? 190  HIS B CE1 1 
ATOM   1907 N  NE2 . HIS B 1 85  ? 47.695 9.786  149.619 1.00 19.38 ? 190  HIS B NE2 1 
ATOM   1908 N  N   . ALA B 1 86  ? 46.386 15.015 149.637 1.00 19.90 ? 191  ALA B N   1 
ATOM   1909 C  CA  . ALA B 1 86  ? 47.191 15.727 150.615 1.00 21.04 ? 191  ALA B CA  1 
ATOM   1910 C  C   . ALA B 1 86  ? 46.511 15.689 151.981 1.00 24.29 ? 191  ALA B C   1 
ATOM   1911 O  O   . ALA B 1 86  ? 45.342 15.313 152.091 1.00 23.00 ? 191  ALA B O   1 
ATOM   1912 C  CB  . ALA B 1 86  ? 47.386 17.165 150.169 1.00 16.20 ? 191  ALA B CB  1 
ATOM   1913 N  N   . PHE B 1 87  ? 47.248 16.076 153.020 1.00 25.22 ? 192  PHE B N   1 
ATOM   1914 C  CA  . PHE B 1 87  ? 46.712 16.081 154.373 1.00 23.69 ? 192  PHE B CA  1 
ATOM   1915 C  C   . PHE B 1 87  ? 46.712 17.491 154.932 1.00 24.15 ? 192  PHE B C   1 
ATOM   1916 O  O   . PHE B 1 87  ? 47.600 18.286 154.632 1.00 23.64 ? 192  PHE B O   1 
ATOM   1917 C  CB  . PHE B 1 87  ? 47.532 15.162 155.290 1.00 23.93 ? 192  PHE B CB  1 
ATOM   1918 C  CG  . PHE B 1 87  ? 47.565 13.731 154.839 1.00 26.85 ? 192  PHE B CG  1 
ATOM   1919 C  CD1 . PHE B 1 87  ? 48.483 13.308 153.881 1.00 29.60 ? 192  PHE B CD1 1 
ATOM   1920 C  CD2 . PHE B 1 87  ? 46.668 12.806 155.358 1.00 27.63 ? 192  PHE B CD2 1 
ATOM   1921 C  CE1 . PHE B 1 87  ? 48.510 11.984 153.447 1.00 27.95 ? 192  PHE B CE1 1 
ATOM   1922 C  CE2 . PHE B 1 87  ? 46.685 11.480 154.930 1.00 29.13 ? 192  PHE B CE2 1 
ATOM   1923 C  CZ  . PHE B 1 87  ? 47.609 11.069 153.972 1.00 29.53 ? 192  PHE B CZ  1 
ATOM   1924 N  N   . PRO B 1 88  ? 45.703 17.818 155.761 1.00 25.45 ? 193  PRO B N   1 
ATOM   1925 C  CA  . PRO B 1 88  ? 45.535 19.135 156.399 1.00 23.84 ? 193  PRO B CA  1 
ATOM   1926 C  C   . PRO B 1 88  ? 46.693 19.452 157.355 1.00 24.12 ? 193  PRO B C   1 
ATOM   1927 O  O   . PRO B 1 88  ? 47.364 18.544 157.851 1.00 24.59 ? 193  PRO B O   1 
ATOM   1928 C  CB  . PRO B 1 88  ? 44.211 18.998 157.151 1.00 23.85 ? 193  PRO B CB  1 
ATOM   1929 C  CG  . PRO B 1 88  ? 43.517 17.859 156.470 1.00 27.72 ? 193  PRO B CG  1 
ATOM   1930 C  CD  . PRO B 1 88  ? 44.626 16.901 156.165 1.00 24.82 ? 193  PRO B CD  1 
ATOM   1931 N  N   . PRO B 1 89  ? 46.929 20.745 157.633 1.00 23.67 ? 194  PRO B N   1 
ATOM   1932 C  CA  . PRO B 1 89  ? 48.005 21.193 158.527 1.00 24.52 ? 194  PRO B CA  1 
ATOM   1933 C  C   . PRO B 1 89  ? 48.077 20.402 159.834 1.00 26.78 ? 194  PRO B C   1 
ATOM   1934 O  O   . PRO B 1 89  ? 47.054 19.982 160.374 1.00 27.80 ? 194  PRO B O   1 
ATOM   1935 C  CB  . PRO B 1 89  ? 47.668 22.660 158.756 1.00 23.21 ? 194  PRO B CB  1 
ATOM   1936 C  CG  . PRO B 1 89  ? 47.036 23.056 157.463 1.00 23.95 ? 194  PRO B CG  1 
ATOM   1937 C  CD  . PRO B 1 89  ? 46.130 21.889 157.160 1.00 22.01 ? 194  PRO B CD  1 
ATOM   1938 N  N   . GLY B 1 90  ? 49.294 20.207 160.334 1.00 26.68 ? 195  GLY B N   1 
ATOM   1939 C  CA  . GLY B 1 90  ? 49.490 19.459 161.563 1.00 25.28 ? 195  GLY B CA  1 
ATOM   1940 C  C   . GLY B 1 90  ? 50.851 18.786 161.573 1.00 26.25 ? 195  GLY B C   1 
ATOM   1941 O  O   . GLY B 1 90  ? 51.653 19.026 160.671 1.00 27.65 ? 195  GLY B O   1 
ATOM   1942 N  N   . PRO B 1 91  ? 51.145 17.935 162.574 1.00 26.70 ? 196  PRO B N   1 
ATOM   1943 C  CA  . PRO B 1 91  ? 52.428 17.233 162.685 1.00 26.43 ? 196  PRO B CA  1 
ATOM   1944 C  C   . PRO B 1 91  ? 52.463 15.901 161.947 1.00 25.56 ? 196  PRO B C   1 
ATOM   1945 O  O   . PRO B 1 91  ? 51.423 15.356 161.592 1.00 28.95 ? 196  PRO B O   1 
ATOM   1946 C  CB  . PRO B 1 91  ? 52.572 17.049 164.189 1.00 26.13 ? 196  PRO B CB  1 
ATOM   1947 C  CG  . PRO B 1 91  ? 51.173 16.742 164.588 1.00 24.53 ? 196  PRO B CG  1 
ATOM   1948 C  CD  . PRO B 1 91  ? 50.356 17.760 163.808 1.00 23.89 ? 196  PRO B CD  1 
ATOM   1949 N  N   . GLY B 1 92  ? 53.665 15.379 161.721 1.00 24.12 ? 197  GLY B N   1 
ATOM   1950 C  CA  . GLY B 1 92  ? 53.803 14.100 161.046 1.00 22.38 ? 197  GLY B CA  1 
ATOM   1951 C  C   . GLY B 1 92  ? 53.338 14.098 159.605 1.00 23.14 ? 197  GLY B C   1 
ATOM   1952 O  O   . GLY B 1 92  ? 53.602 15.036 158.868 1.00 21.24 ? 197  GLY B O   1 
ATOM   1953 N  N   . ILE B 1 93  ? 52.633 13.048 159.202 1.00 24.37 ? 198  ILE B N   1 
ATOM   1954 C  CA  . ILE B 1 93  ? 52.147 12.941 157.832 1.00 26.26 ? 198  ILE B CA  1 
ATOM   1955 C  C   . ILE B 1 93  ? 51.194 14.085 157.479 1.00 26.36 ? 198  ILE B C   1 
ATOM   1956 O  O   . ILE B 1 93  ? 50.921 14.343 156.309 1.00 27.06 ? 198  ILE B O   1 
ATOM   1957 C  CB  . ILE B 1 93  ? 51.440 11.590 157.613 1.00 27.60 ? 198  ILE B CB  1 
ATOM   1958 C  CG1 . ILE B 1 93  ? 51.200 11.365 156.119 1.00 29.76 ? 198  ILE B CG1 1 
ATOM   1959 C  CG2 . ILE B 1 93  ? 50.131 11.561 158.386 1.00 27.08 ? 198  ILE B CG2 1 
ATOM   1960 C  CD1 . ILE B 1 93  ? 50.620 10.012 155.789 1.00 31.30 ? 198  ILE B CD1 1 
ATOM   1961 N  N   . GLN B 1 94  ? 50.704 14.781 158.498 1.00 26.62 ? 199  GLN B N   1 
ATOM   1962 C  CA  . GLN B 1 94  ? 49.790 15.901 158.298 1.00 26.46 ? 199  GLN B CA  1 
ATOM   1963 C  C   . GLN B 1 94  ? 50.459 16.998 157.482 1.00 23.79 ? 199  GLN B C   1 
ATOM   1964 O  O   . GLN B 1 94  ? 51.576 17.367 157.768 1.00 25.59 ? 199  GLN B O   1 
ATOM   1965 C  CB  . GLN B 1 94  ? 49.359 16.457 159.654 1.00 29.46 ? 199  GLN B CB  1 
ATOM   1966 C  CG  . GLN B 1 94  ? 47.864 16.383 159.914 1.00 38.14 ? 199  GLN B CG  1 
ATOM   1967 C  CD  . GLN B 1 94  ? 47.323 14.967 159.860 1.00 41.94 ? 199  GLN B CD  1 
ATOM   1968 O  OE1 . GLN B 1 94  ? 46.116 14.751 159.940 1.00 44.27 ? 199  GLN B OE1 1 
ATOM   1969 N  NE2 . GLN B 1 94  ? 48.215 13.993 159.727 1.00 46.11 ? 199  GLN B NE2 1 
ATOM   1970 N  N   . GLY B 1 95  ? 49.774 17.524 156.472 1.00 23.38 ? 200  GLY B N   1 
ATOM   1971 C  CA  . GLY B 1 95  ? 50.364 18.568 155.650 1.00 18.35 ? 200  GLY B CA  1 
ATOM   1972 C  C   . GLY B 1 95  ? 51.149 18.047 154.450 1.00 20.05 ? 200  GLY B C   1 
ATOM   1973 O  O   . GLY B 1 95  ? 51.606 18.835 153.619 1.00 21.28 ? 200  GLY B O   1 
ATOM   1974 N  N   . ASP B 1 96  ? 51.308 16.727 154.354 1.00 18.69 ? 201  ASP B N   1 
ATOM   1975 C  CA  . ASP B 1 96  ? 52.049 16.115 153.253 1.00 18.67 ? 201  ASP B CA  1 
ATOM   1976 C  C   . ASP B 1 96  ? 51.203 15.996 151.974 1.00 20.96 ? 201  ASP B C   1 
ATOM   1977 O  O   . ASP B 1 96  ? 49.971 16.042 152.029 1.00 21.22 ? 201  ASP B O   1 
ATOM   1978 C  CB  . ASP B 1 96  ? 52.557 14.730 153.668 1.00 17.24 ? 201  ASP B CB  1 
ATOM   1979 C  CG  . ASP B 1 96  ? 53.613 14.794 154.764 1.00 19.44 ? 201  ASP B CG  1 
ATOM   1980 O  OD1 . ASP B 1 96  ? 53.978 15.912 155.160 1.00 14.37 ? 201  ASP B OD1 1 
ATOM   1981 O  OD2 . ASP B 1 96  ? 54.080 13.730 155.220 1.00 16.31 ? 201  ASP B OD2 1 
ATOM   1982 N  N   . ALA B 1 97  ? 51.872 15.836 150.831 1.00 18.26 ? 202  ALA B N   1 
ATOM   1983 C  CA  . ALA B 1 97  ? 51.197 15.722 149.536 1.00 17.33 ? 202  ALA B CA  1 
ATOM   1984 C  C   . ALA B 1 97  ? 51.803 14.586 148.728 1.00 18.72 ? 202  ALA B C   1 
ATOM   1985 O  O   . ALA B 1 97  ? 53.004 14.569 148.483 1.00 20.07 ? 202  ALA B O   1 
ATOM   1986 C  CB  . ALA B 1 97  ? 51.326 17.027 148.771 1.00 16.82 ? 202  ALA B CB  1 
ATOM   1987 N  N   . HIS B 1 98  ? 50.968 13.639 148.314 1.00 17.89 ? 203  HIS B N   1 
ATOM   1988 C  CA  . HIS B 1 98  ? 51.424 12.481 147.555 1.00 15.98 ? 203  HIS B CA  1 
ATOM   1989 C  C   . HIS B 1 98  ? 50.786 12.427 146.168 1.00 18.64 ? 203  HIS B C   1 
ATOM   1990 O  O   . HIS B 1 98  ? 49.591 12.668 146.016 1.00 18.44 ? 203  HIS B O   1 
ATOM   1991 C  CB  . HIS B 1 98  ? 51.092 11.215 148.334 1.00 17.39 ? 203  HIS B CB  1 
ATOM   1992 C  CG  . HIS B 1 98  ? 51.623 11.212 149.736 1.00 20.36 ? 203  HIS B CG  1 
ATOM   1993 N  ND1 . HIS B 1 98  ? 51.160 10.349 150.704 1.00 18.51 ? 203  HIS B ND1 1 
ATOM   1994 C  CD2 . HIS B 1 98  ? 52.599 11.944 150.325 1.00 17.40 ? 203  HIS B CD2 1 
ATOM   1995 C  CE1 . HIS B 1 98  ? 51.827 10.546 151.826 1.00 17.19 ? 203  HIS B CE1 1 
ATOM   1996 N  NE2 . HIS B 1 98  ? 52.706 11.508 151.623 1.00 17.14 ? 203  HIS B NE2 1 
ATOM   1997 N  N   . PHE B 1 99  ? 51.594 12.105 145.160 1.00 19.00 ? 204  PHE B N   1 
ATOM   1998 C  CA  . PHE B 1 99  ? 51.128 12.046 143.776 1.00 15.37 ? 204  PHE B CA  1 
ATOM   1999 C  C   . PHE B 1 99  ? 51.227 10.650 143.185 1.00 15.36 ? 204  PHE B C   1 
ATOM   2000 O  O   . PHE B 1 99  ? 52.257 9.993  143.293 1.00 15.05 ? 204  PHE B O   1 
ATOM   2001 C  CB  . PHE B 1 99  ? 51.929 13.027 142.912 1.00 16.11 ? 204  PHE B CB  1 
ATOM   2002 C  CG  . PHE B 1 99  ? 51.907 14.444 143.421 1.00 14.27 ? 204  PHE B CG  1 
ATOM   2003 C  CD1 . PHE B 1 99  ? 52.747 14.840 144.459 1.00 15.41 ? 204  PHE B CD1 1 
ATOM   2004 C  CD2 . PHE B 1 99  ? 51.017 15.374 142.887 1.00 13.45 ? 204  PHE B CD2 1 
ATOM   2005 C  CE1 . PHE B 1 99  ? 52.704 16.143 144.961 1.00 15.16 ? 204  PHE B CE1 1 
ATOM   2006 C  CE2 . PHE B 1 99  ? 50.962 16.685 143.380 1.00 14.52 ? 204  PHE B CE2 1 
ATOM   2007 C  CZ  . PHE B 1 99  ? 51.806 17.071 144.418 1.00 14.98 ? 204  PHE B CZ  1 
ATOM   2008 N  N   . ASP B 1 100 ? 50.144 10.204 142.555 1.00 16.99 ? 205  ASP B N   1 
ATOM   2009 C  CA  . ASP B 1 100 ? 50.094 8.877  141.941 1.00 18.47 ? 205  ASP B CA  1 
ATOM   2010 C  C   . ASP B 1 100 ? 50.944 8.843  140.673 1.00 17.99 ? 205  ASP B C   1 
ATOM   2011 O  O   . ASP B 1 100 ? 50.604 9.460  139.670 1.00 16.40 ? 205  ASP B O   1 
ATOM   2012 C  CB  . ASP B 1 100 ? 48.660 8.502  141.583 1.00 16.97 ? 205  ASP B CB  1 
ATOM   2013 C  CG  . ASP B 1 100 ? 48.546 7.080  141.116 1.00 17.69 ? 205  ASP B CG  1 
ATOM   2014 O  OD1 . ASP B 1 100 ? 49.567 6.496  140.725 1.00 24.22 ? 205  ASP B OD1 1 
ATOM   2015 O  OD2 . ASP B 1 100 ? 47.442 6.530  141.132 1.00 22.67 ? 205  ASP B OD2 1 
ATOM   2016 N  N   . ASP B 1 101 ? 52.039 8.101  140.722 1.00 18.18 ? 206  ASP B N   1 
ATOM   2017 C  CA  . ASP B 1 101 ? 52.943 8.020  139.593 1.00 19.10 ? 206  ASP B CA  1 
ATOM   2018 C  C   . ASP B 1 101 ? 52.522 6.977  138.560 1.00 22.02 ? 206  ASP B C   1 
ATOM   2019 O  O   . ASP B 1 101 ? 53.328 6.553  137.739 1.00 22.79 ? 206  ASP B O   1 
ATOM   2020 C  CB  . ASP B 1 101 ? 54.360 7.745  140.098 1.00 18.63 ? 206  ASP B CB  1 
ATOM   2021 C  CG  . ASP B 1 101 ? 55.424 8.234  139.147 1.00 21.55 ? 206  ASP B CG  1 
ATOM   2022 O  OD1 . ASP B 1 101 ? 55.153 9.165  138.359 1.00 22.68 ? 206  ASP B OD1 1 
ATOM   2023 O  OD2 . ASP B 1 101 ? 56.546 7.700  139.204 1.00 24.38 ? 206  ASP B OD2 1 
ATOM   2024 N  N   . ASP B 1 102 ? 51.274 6.529  138.627 1.00 21.73 ? 207  ASP B N   1 
ATOM   2025 C  CA  . ASP B 1 102 ? 50.772 5.589  137.631 1.00 20.62 ? 207  ASP B CA  1 
ATOM   2026 C  C   . ASP B 1 102 ? 50.123 6.478  136.570 1.00 20.79 ? 207  ASP B C   1 
ATOM   2027 O  O   . ASP B 1 102 ? 49.739 6.016  135.504 1.00 23.31 ? 207  ASP B O   1 
ATOM   2028 C  CB  . ASP B 1 102 ? 49.729 4.635  138.212 1.00 19.80 ? 207  ASP B CB  1 
ATOM   2029 C  CG  . ASP B 1 102 ? 50.304 3.270  138.551 1.00 22.45 ? 207  ASP B CG  1 
ATOM   2030 O  OD1 . ASP B 1 102 ? 51.334 2.884  137.963 1.00 20.45 ? 207  ASP B OD1 1 
ATOM   2031 O  OD2 . ASP B 1 102 ? 49.709 2.571  139.399 1.00 23.05 ? 207  ASP B OD2 1 
ATOM   2032 N  N   . GLU B 1 103 ? 50.008 7.763  136.890 1.00 18.69 ? 208  GLU B N   1 
ATOM   2033 C  CA  . GLU B 1 103 ? 49.441 8.755  135.987 1.00 20.13 ? 208  GLU B CA  1 
ATOM   2034 C  C   . GLU B 1 103 ? 50.560 9.285  135.099 1.00 21.01 ? 208  GLU B C   1 
ATOM   2035 O  O   . GLU B 1 103 ? 51.725 9.238  135.477 1.00 19.13 ? 208  GLU B O   1 
ATOM   2036 C  CB  . GLU B 1 103 ? 48.874 9.931  136.778 1.00 20.83 ? 208  GLU B CB  1 
ATOM   2037 C  CG  . GLU B 1 103 ? 47.935 9.526  137.894 1.00 29.96 ? 208  GLU B CG  1 
ATOM   2038 C  CD  . GLU B 1 103 ? 46.627 8.986  137.377 1.00 33.57 ? 208  GLU B CD  1 
ATOM   2039 O  OE1 . GLU B 1 103 ? 46.617 8.360  136.293 1.00 36.59 ? 208  GLU B OE1 1 
ATOM   2040 O  OE2 . GLU B 1 103 ? 45.607 9.185  138.060 1.00 40.04 ? 208  GLU B OE2 1 
ATOM   2041 N  N   . LEU B 1 104 ? 50.207 9.795  133.924 1.00 18.61 ? 209  LEU B N   1 
ATOM   2042 C  CA  . LEU B 1 104 ? 51.204 10.366 133.026 1.00 17.96 ? 209  LEU B CA  1 
ATOM   2043 C  C   . LEU B 1 104 ? 51.312 11.837 133.399 1.00 18.42 ? 209  LEU B C   1 
ATOM   2044 O  O   . LEU B 1 104 ? 50.379 12.603 133.160 1.00 18.49 ? 209  LEU B O   1 
ATOM   2045 C  CB  . LEU B 1 104 ? 50.758 10.242 131.568 1.00 18.74 ? 209  LEU B CB  1 
ATOM   2046 C  CG  . LEU B 1 104 ? 51.617 10.985 130.532 1.00 19.98 ? 209  LEU B CG  1 
ATOM   2047 C  CD1 . LEU B 1 104 ? 53.062 10.519 130.627 1.00 18.61 ? 209  LEU B CD1 1 
ATOM   2048 C  CD2 . LEU B 1 104 ? 51.064 10.740 129.131 1.00 17.02 ? 209  LEU B CD2 1 
ATOM   2049 N  N   . TRP B 1 105 ? 52.434 12.230 133.998 1.00 17.94 ? 210  TRP B N   1 
ATOM   2050 C  CA  . TRP B 1 105 ? 52.618 13.622 134.401 1.00 16.68 ? 210  TRP B CA  1 
ATOM   2051 C  C   . TRP B 1 105 ? 53.267 14.435 133.299 1.00 16.25 ? 210  TRP B C   1 
ATOM   2052 O  O   . TRP B 1 105 ? 54.230 14.003 132.665 1.00 14.91 ? 210  TRP B O   1 
ATOM   2053 C  CB  . TRP B 1 105 ? 53.454 13.723 135.694 1.00 15.77 ? 210  TRP B CB  1 
ATOM   2054 C  CG  . TRP B 1 105 ? 52.752 13.143 136.870 1.00 14.61 ? 210  TRP B CG  1 
ATOM   2055 C  CD1 . TRP B 1 105 ? 53.051 11.979 137.511 1.00 13.93 ? 210  TRP B CD1 1 
ATOM   2056 C  CD2 . TRP B 1 105 ? 51.546 13.636 137.469 1.00 14.73 ? 210  TRP B CD2 1 
ATOM   2057 N  NE1 . TRP B 1 105 ? 52.101 11.708 138.467 1.00 15.76 ? 210  TRP B NE1 1 
ATOM   2058 C  CE2 . TRP B 1 105 ? 51.165 12.708 138.464 1.00 14.79 ? 210  TRP B CE2 1 
ATOM   2059 C  CE3 . TRP B 1 105 ? 50.744 14.769 137.255 1.00 16.70 ? 210  TRP B CE3 1 
ATOM   2060 C  CZ2 . TRP B 1 105 ? 50.012 12.876 139.248 1.00 13.38 ? 210  TRP B CZ2 1 
ATOM   2061 C  CZ3 . TRP B 1 105 ? 49.591 14.935 138.034 1.00 13.30 ? 210  TRP B CZ3 1 
ATOM   2062 C  CH2 . TRP B 1 105 ? 49.241 13.990 139.016 1.00 13.83 ? 210  TRP B CH2 1 
ATOM   2063 N  N   . SER B 1 106 ? 52.731 15.630 133.092 1.00 16.82 ? 211  SER B N   1 
ATOM   2064 C  CA  . SER B 1 106 ? 53.218 16.521 132.061 1.00 15.97 ? 211  SER B CA  1 
ATOM   2065 C  C   . SER B 1 106 ? 52.924 17.953 132.496 1.00 17.15 ? 211  SER B C   1 
ATOM   2066 O  O   . SER B 1 106 ? 52.677 18.207 133.676 1.00 20.26 ? 211  SER B O   1 
ATOM   2067 C  CB  . SER B 1 106 ? 52.497 16.187 130.747 1.00 16.80 ? 211  SER B CB  1 
ATOM   2068 O  OG  . SER B 1 106 ? 53.111 16.799 129.634 1.00 12.64 ? 211  SER B OG  1 
ATOM   2069 N  N   . LEU B 1 107 ? 52.954 18.881 131.543 1.00 15.88 ? 212  LEU B N   1 
ATOM   2070 C  CA  . LEU B 1 107 ? 52.680 20.294 131.800 1.00 15.39 ? 212  LEU B CA  1 
ATOM   2071 C  C   . LEU B 1 107 ? 52.044 20.901 130.558 1.00 16.86 ? 212  LEU B C   1 
ATOM   2072 O  O   . LEU B 1 107 ? 52.335 20.471 129.453 1.00 16.65 ? 212  LEU B O   1 
ATOM   2073 C  CB  . LEU B 1 107 ? 53.972 21.049 132.105 1.00 12.60 ? 212  LEU B CB  1 
ATOM   2074 C  CG  . LEU B 1 107 ? 54.744 20.758 133.401 1.00 16.29 ? 212  LEU B CG  1 
ATOM   2075 C  CD1 . LEU B 1 107 ? 56.029 21.560 133.386 1.00 12.54 ? 212  LEU B CD1 1 
ATOM   2076 C  CD2 . LEU B 1 107 ? 53.904 21.118 134.638 1.00 12.78 ? 212  LEU B CD2 1 
ATOM   2077 N  N   . GLY B 1 108 ? 51.181 21.898 130.739 1.00 20.56 ? 213  GLY B N   1 
ATOM   2078 C  CA  . GLY B 1 108 ? 50.545 22.557 129.602 1.00 20.23 ? 213  GLY B CA  1 
ATOM   2079 C  C   . GLY B 1 108 ? 49.475 21.767 128.864 1.00 21.25 ? 213  GLY B C   1 
ATOM   2080 O  O   . GLY B 1 108 ? 48.885 20.835 129.409 1.00 21.72 ? 213  GLY B O   1 
ATOM   2081 N  N   . LYS B 1 109 ? 49.207 22.158 127.621 1.00 20.99 ? 214  LYS B N   1 
ATOM   2082 C  CA  . LYS B 1 109 ? 48.217 21.473 126.795 1.00 21.58 ? 214  LYS B CA  1 
ATOM   2083 C  C   . LYS B 1 109 ? 48.804 20.142 126.355 1.00 22.13 ? 214  LYS B C   1 
ATOM   2084 O  O   . LYS B 1 109 ? 50.029 19.997 126.286 1.00 23.20 ? 214  LYS B O   1 
ATOM   2085 C  CB  . LYS B 1 109 ? 47.879 22.314 125.560 1.00 22.10 ? 214  LYS B CB  1 
ATOM   2086 C  CG  . LYS B 1 109 ? 47.094 23.564 125.878 1.00 24.12 ? 214  LYS B CG  1 
ATOM   2087 C  CD  . LYS B 1 109 ? 46.828 24.410 124.647 1.00 27.19 ? 214  LYS B CD  1 
ATOM   2088 C  CE  . LYS B 1 109 ? 48.099 25.058 124.149 1.00 30.98 ? 214  LYS B CE  1 
ATOM   2089 N  NZ  . LYS B 1 109 ? 47.812 26.127 123.147 1.00 36.83 ? 214  LYS B NZ  1 
ATOM   2090 N  N   . GLY B 1 110 ? 47.940 19.180 126.044 1.00 18.79 ? 215  GLY B N   1 
ATOM   2091 C  CA  . GLY B 1 110 ? 48.420 17.877 125.623 1.00 17.78 ? 215  GLY B CA  1 
ATOM   2092 C  C   . GLY B 1 110 ? 47.925 16.758 126.521 1.00 18.87 ? 215  GLY B C   1 
ATOM   2093 O  O   . GLY B 1 110 ? 47.238 17.010 127.515 1.00 19.58 ? 215  GLY B O   1 
ATOM   2094 N  N   . GLN B 1 111 ? 48.268 15.519 126.181 1.00 19.71 ? 391  GLN B N   1 
ATOM   2095 C  CA  . GLN B 1 111 ? 47.828 14.384 126.978 1.00 24.27 ? 391  GLN B CA  1 
ATOM   2096 C  C   . GLN B 1 111 ? 48.582 14.369 128.311 1.00 22.67 ? 391  GLN B C   1 
ATOM   2097 O  O   . GLN B 1 111 ? 49.614 15.024 128.456 1.00 19.97 ? 391  GLN B O   1 
ATOM   2098 C  CB  . GLN B 1 111 ? 48.024 13.073 126.200 1.00 26.88 ? 391  GLN B CB  1 
ATOM   2099 C  CG  . GLN B 1 111 ? 49.371 12.436 126.354 1.00 36.19 ? 391  GLN B CG  1 
ATOM   2100 C  CD  . GLN B 1 111 ? 50.489 13.421 126.157 1.00 42.59 ? 391  GLN B CD  1 
ATOM   2101 O  OE1 . GLN B 1 111 ? 50.568 14.090 125.131 1.00 51.17 ? 391  GLN B OE1 1 
ATOM   2102 N  NE2 . GLN B 1 111 ? 51.368 13.520 127.144 1.00 50.82 ? 391  GLN B NE2 1 
ATOM   2103 N  N   . GLY B 1 112 ? 48.050 13.635 129.284 1.00 22.31 ? 392  GLY B N   1 
ATOM   2104 C  CA  . GLY B 1 112 ? 48.672 13.586 130.592 1.00 20.72 ? 392  GLY B CA  1 
ATOM   2105 C  C   . GLY B 1 112 ? 48.050 14.651 131.473 1.00 19.93 ? 392  GLY B C   1 
ATOM   2106 O  O   . GLY B 1 112 ? 47.238 15.452 131.010 1.00 20.51 ? 392  GLY B O   1 
ATOM   2107 N  N   . TYR B 1 113 ? 48.433 14.672 132.744 1.00 20.46 ? 393  TYR B N   1 
ATOM   2108 C  CA  . TYR B 1 113 ? 47.896 15.643 133.692 1.00 18.29 ? 393  TYR B CA  1 
ATOM   2109 C  C   . TYR B 1 113 ? 48.964 16.653 134.050 1.00 17.76 ? 393  TYR B C   1 
ATOM   2110 O  O   . TYR B 1 113 ? 50.138 16.304 134.130 1.00 22.05 ? 393  TYR B O   1 
ATOM   2111 C  CB  . TYR B 1 113 ? 47.421 14.924 134.962 1.00 20.08 ? 393  TYR B CB  1 
ATOM   2112 C  CG  . TYR B 1 113 ? 46.248 13.989 134.746 1.00 16.50 ? 393  TYR B CG  1 
ATOM   2113 C  CD1 . TYR B 1 113 ? 44.957 14.490 134.602 1.00 17.97 ? 393  TYR B CD1 1 
ATOM   2114 C  CD2 . TYR B 1 113 ? 46.429 12.610 134.675 1.00 18.06 ? 393  TYR B CD2 1 
ATOM   2115 C  CE1 . TYR B 1 113 ? 43.871 13.647 134.397 1.00 16.85 ? 393  TYR B CE1 1 
ATOM   2116 C  CE2 . TYR B 1 113 ? 45.342 11.747 134.467 1.00 17.10 ? 393  TYR B CE2 1 
ATOM   2117 C  CZ  . TYR B 1 113 ? 44.064 12.281 134.329 1.00 18.56 ? 393  TYR B CZ  1 
ATOM   2118 O  OH  . TYR B 1 113 ? 42.974 11.463 134.100 1.00 18.94 ? 393  TYR B OH  1 
ATOM   2119 N  N   . SER B 1 114 ? 48.560 17.901 134.271 1.00 17.69 ? 394  SER B N   1 
ATOM   2120 C  CA  . SER B 1 114 ? 49.505 18.955 134.627 1.00 18.43 ? 394  SER B CA  1 
ATOM   2121 C  C   . SER B 1 114 ? 49.974 18.806 136.066 1.00 19.32 ? 394  SER B C   1 
ATOM   2122 O  O   . SER B 1 114 ? 49.185 18.953 136.997 1.00 23.73 ? 394  SER B O   1 
ATOM   2123 C  CB  . SER B 1 114 ? 48.864 20.331 134.464 1.00 15.87 ? 394  SER B CB  1 
ATOM   2124 O  OG  . SER B 1 114 ? 49.799 21.357 134.756 1.00 17.63 ? 394  SER B OG  1 
ATOM   2125 N  N   . LEU B 1 115 ? 51.253 18.512 136.255 1.00 18.56 ? 395  LEU B N   1 
ATOM   2126 C  CA  . LEU B 1 115 ? 51.785 18.373 137.604 1.00 17.72 ? 395  LEU B CA  1 
ATOM   2127 C  C   . LEU B 1 115 ? 51.624 19.710 138.329 1.00 18.62 ? 395  LEU B C   1 
ATOM   2128 O  O   . LEU B 1 115 ? 51.285 19.746 139.507 1.00 19.25 ? 395  LEU B O   1 
ATOM   2129 C  CB  . LEU B 1 115 ? 53.265 17.972 137.556 1.00 16.48 ? 395  LEU B CB  1 
ATOM   2130 C  CG  . LEU B 1 115 ? 53.993 17.751 138.889 1.00 15.25 ? 395  LEU B CG  1 
ATOM   2131 C  CD1 . LEU B 1 115 ? 53.311 16.631 139.670 1.00 13.74 ? 395  LEU B CD1 1 
ATOM   2132 C  CD2 . LEU B 1 115 ? 55.457 17.409 138.628 1.00 10.40 ? 395  LEU B CD2 1 
ATOM   2133 N  N   . PHE B 1 116 ? 51.853 20.803 137.605 1.00 16.65 ? 396  PHE B N   1 
ATOM   2134 C  CA  . PHE B 1 116 ? 51.741 22.152 138.152 1.00 17.42 ? 396  PHE B CA  1 
ATOM   2135 C  C   . PHE B 1 116 ? 50.369 22.429 138.749 1.00 20.69 ? 396  PHE B C   1 
ATOM   2136 O  O   . PHE B 1 116 ? 50.257 22.821 139.916 1.00 20.46 ? 396  PHE B O   1 
ATOM   2137 C  CB  . PHE B 1 116 ? 52.035 23.181 137.057 1.00 16.61 ? 396  PHE B CB  1 
ATOM   2138 C  CG  . PHE B 1 116 ? 51.661 24.592 137.421 1.00 17.86 ? 396  PHE B CG  1 
ATOM   2139 C  CD1 . PHE B 1 116 ? 52.306 25.261 138.456 1.00 17.66 ? 396  PHE B CD1 1 
ATOM   2140 C  CD2 . PHE B 1 116 ? 50.666 25.259 136.714 1.00 19.99 ? 396  PHE B CD2 1 
ATOM   2141 C  CE1 . PHE B 1 116 ? 51.966 26.580 138.782 1.00 17.56 ? 396  PHE B CE1 1 
ATOM   2142 C  CE2 . PHE B 1 116 ? 50.319 26.573 137.030 1.00 20.09 ? 396  PHE B CE2 1 
ATOM   2143 C  CZ  . PHE B 1 116 ? 50.974 27.236 138.070 1.00 19.48 ? 396  PHE B CZ  1 
ATOM   2144 N  N   . LEU B 1 117 ? 49.329 22.234 137.942 1.00 20.63 ? 397  LEU B N   1 
ATOM   2145 C  CA  . LEU B 1 117 ? 47.958 22.472 138.381 1.00 19.67 ? 397  LEU B CA  1 
ATOM   2146 C  C   . LEU B 1 117 ? 47.512 21.550 139.510 1.00 18.44 ? 397  LEU B C   1 
ATOM   2147 O  O   . LEU B 1 117 ? 46.858 21.997 140.452 1.00 19.34 ? 397  LEU B O   1 
ATOM   2148 C  CB  . LEU B 1 117 ? 46.985 22.340 137.201 1.00 19.64 ? 397  LEU B CB  1 
ATOM   2149 C  CG  . LEU B 1 117 ? 47.038 23.424 136.122 1.00 18.58 ? 397  LEU B CG  1 
ATOM   2150 C  CD1 . LEU B 1 117 ? 45.965 23.156 135.086 1.00 15.91 ? 397  LEU B CD1 1 
ATOM   2151 C  CD2 . LEU B 1 117 ? 46.843 24.793 136.748 1.00 18.23 ? 397  LEU B CD2 1 
ATOM   2152 N  N   . VAL B 1 118 ? 47.846 20.266 139.417 1.00 17.99 ? 398  VAL B N   1 
ATOM   2153 C  CA  . VAL B 1 118 ? 47.464 19.326 140.466 1.00 19.04 ? 398  VAL B CA  1 
ATOM   2154 C  C   . VAL B 1 118 ? 48.211 19.629 141.773 1.00 20.64 ? 398  VAL B C   1 
ATOM   2155 O  O   . VAL B 1 118 ? 47.659 19.469 142.862 1.00 21.46 ? 398  VAL B O   1 
ATOM   2156 C  CB  . VAL B 1 118 ? 47.733 17.866 140.043 1.00 19.35 ? 398  VAL B CB  1 
ATOM   2157 C  CG1 . VAL B 1 118 ? 47.353 16.905 141.173 1.00 15.55 ? 398  VAL B CG1 1 
ATOM   2158 C  CG2 . VAL B 1 118 ? 46.913 17.538 138.809 1.00 19.62 ? 398  VAL B CG2 1 
ATOM   2159 N  N   . ALA B 1 119 ? 49.457 20.079 141.660 1.00 18.80 ? 399  ALA B N   1 
ATOM   2160 C  CA  . ALA B 1 119 ? 50.254 20.411 142.834 1.00 21.04 ? 399  ALA B CA  1 
ATOM   2161 C  C   . ALA B 1 119 ? 49.636 21.599 143.566 1.00 21.74 ? 399  ALA B C   1 
ATOM   2162 O  O   . ALA B 1 119 ? 49.548 21.615 144.795 1.00 22.28 ? 399  ALA B O   1 
ATOM   2163 C  CB  . ALA B 1 119 ? 51.701 20.743 142.421 1.00 17.73 ? 399  ALA B CB  1 
ATOM   2164 N  N   . ALA B 1 120 ? 49.210 22.597 142.802 1.00 21.01 ? 400  ALA B N   1 
ATOM   2165 C  CA  . ALA B 1 120 ? 48.611 23.787 143.378 1.00 20.55 ? 400  ALA B CA  1 
ATOM   2166 C  C   . ALA B 1 120 ? 47.363 23.413 144.168 1.00 22.57 ? 400  ALA B C   1 
ATOM   2167 O  O   . ALA B 1 120 ? 47.090 23.992 145.220 1.00 23.97 ? 400  ALA B O   1 
ATOM   2168 C  CB  . ALA B 1 120 ? 48.270 24.788 142.274 1.00 19.74 ? 400  ALA B CB  1 
ATOM   2169 N  N   . HIS B 1 121 ? 46.612 22.442 143.658 1.00 22.90 ? 401  HIS B N   1 
ATOM   2170 C  CA  . HIS B 1 121 ? 45.397 21.980 144.321 1.00 23.48 ? 401  HIS B CA  1 
ATOM   2171 C  C   . HIS B 1 121 ? 45.763 21.246 145.615 1.00 24.30 ? 401  HIS B C   1 
ATOM   2172 O  O   . HIS B 1 121 ? 45.192 21.519 146.673 1.00 24.53 ? 401  HIS B O   1 
ATOM   2173 C  CB  . HIS B 1 121 ? 44.616 21.041 143.395 1.00 22.18 ? 401  HIS B CB  1 
ATOM   2174 C  CG  . HIS B 1 121 ? 43.328 20.544 143.976 1.00 23.80 ? 401  HIS B CG  1 
ATOM   2175 N  ND1 . HIS B 1 121 ? 42.138 21.230 143.847 1.00 23.81 ? 401  HIS B ND1 1 
ATOM   2176 C  CD2 . HIS B 1 121 ? 43.044 19.429 144.691 1.00 21.37 ? 401  HIS B CD2 1 
ATOM   2177 C  CE1 . HIS B 1 121 ? 41.177 20.557 144.454 1.00 24.18 ? 401  HIS B CE1 1 
ATOM   2178 N  NE2 . HIS B 1 121 ? 41.699 19.461 144.976 1.00 21.29 ? 401  HIS B NE2 1 
ATOM   2179 N  N   . GLU B 1 122 ? 46.714 20.317 145.529 1.00 23.82 ? 402  GLU B N   1 
ATOM   2180 C  CA  . GLU B 1 122 ? 47.150 19.566 146.708 1.00 22.77 ? 402  GLU B CA  1 
ATOM   2181 C  C   . GLU B 1 122 ? 47.710 20.486 147.785 1.00 22.14 ? 402  GLU B C   1 
ATOM   2182 O  O   . GLU B 1 122 ? 47.431 20.301 148.966 1.00 24.45 ? 402  GLU B O   1 
ATOM   2183 C  CB  . GLU B 1 122 ? 48.217 18.530 146.341 1.00 22.35 ? 402  GLU B CB  1 
ATOM   2184 C  CG  . GLU B 1 122 ? 47.744 17.435 145.406 1.00 21.55 ? 402  GLU B CG  1 
ATOM   2185 C  CD  . GLU B 1 122 ? 46.298 17.071 145.636 1.00 21.21 ? 402  GLU B CD  1 
ATOM   2186 O  OE1 . GLU B 1 122 ? 45.914 16.813 146.790 1.00 23.03 ? 402  GLU B OE1 1 
ATOM   2187 O  OE2 . GLU B 1 122 ? 45.539 17.043 144.654 1.00 26.51 ? 402  GLU B OE2 1 
ATOM   2188 N  N   . PHE B 1 123 ? 48.504 21.473 147.382 1.00 22.87 ? 403  PHE B N   1 
ATOM   2189 C  CA  . PHE B 1 123 ? 49.079 22.396 148.348 1.00 23.58 ? 403  PHE B CA  1 
ATOM   2190 C  C   . PHE B 1 123 ? 47.975 23.229 148.981 1.00 25.40 ? 403  PHE B C   1 
ATOM   2191 O  O   . PHE B 1 123 ? 48.155 23.801 150.055 1.00 27.88 ? 403  PHE B O   1 
ATOM   2192 C  CB  . PHE B 1 123 ? 50.124 23.308 147.688 1.00 20.83 ? 403  PHE B CB  1 
ATOM   2193 C  CG  . PHE B 1 123 ? 51.322 22.571 147.140 1.00 22.36 ? 403  PHE B CG  1 
ATOM   2194 C  CD1 . PHE B 1 123 ? 51.587 21.252 147.518 1.00 20.84 ? 403  PHE B CD1 1 
ATOM   2195 C  CD2 . PHE B 1 123 ? 52.175 23.189 146.230 1.00 18.11 ? 403  PHE B CD2 1 
ATOM   2196 C  CE1 . PHE B 1 123 ? 52.682 20.560 146.989 1.00 21.54 ? 403  PHE B CE1 1 
ATOM   2197 C  CE2 . PHE B 1 123 ? 53.272 22.507 145.695 1.00 18.09 ? 403  PHE B CE2 1 
ATOM   2198 C  CZ  . PHE B 1 123 ? 53.525 21.193 146.072 1.00 19.86 ? 403  PHE B CZ  1 
ATOM   2199 N  N   . GLY B 1 124 ? 46.829 23.288 148.310 1.00 25.83 ? 404  GLY B N   1 
ATOM   2200 C  CA  . GLY B 1 124 ? 45.703 24.038 148.833 1.00 25.16 ? 404  GLY B CA  1 
ATOM   2201 C  C   . GLY B 1 124 ? 45.208 23.328 150.076 1.00 25.03 ? 404  GLY B C   1 
ATOM   2202 O  O   . GLY B 1 124 ? 44.922 23.953 151.096 1.00 24.69 ? 404  GLY B O   1 
ATOM   2203 N  N   . HIS B 1 125 ? 45.110 22.008 149.980 1.00 23.03 ? 405  HIS B N   1 
ATOM   2204 C  CA  . HIS B 1 125 ? 44.689 21.186 151.102 1.00 23.37 ? 405  HIS B CA  1 
ATOM   2205 C  C   . HIS B 1 125 ? 45.736 21.262 152.215 1.00 26.13 ? 405  HIS B C   1 
ATOM   2206 O  O   . HIS B 1 125 ? 45.407 21.507 153.371 1.00 27.66 ? 405  HIS B O   1 
ATOM   2207 C  CB  . HIS B 1 125 ? 44.537 19.731 150.668 1.00 21.33 ? 405  HIS B CB  1 
ATOM   2208 C  CG  . HIS B 1 125 ? 43.325 19.474 149.834 1.00 26.14 ? 405  HIS B CG  1 
ATOM   2209 N  ND1 . HIS B 1 125 ? 42.076 19.944 150.178 1.00 25.46 ? 405  HIS B ND1 1 
ATOM   2210 C  CD2 . HIS B 1 125 ? 43.164 18.781 148.683 1.00 23.33 ? 405  HIS B CD2 1 
ATOM   2211 C  CE1 . HIS B 1 125 ? 41.198 19.551 149.274 1.00 26.71 ? 405  HIS B CE1 1 
ATOM   2212 N  NE2 . HIS B 1 125 ? 41.833 18.844 148.357 1.00 25.66 ? 405  HIS B NE2 1 
ATOM   2213 N  N   . ALA B 1 126 ? 46.998 21.053 151.850 1.00 24.97 ? 406  ALA B N   1 
ATOM   2214 C  CA  . ALA B 1 126 ? 48.099 21.082 152.802 1.00 25.23 ? 406  ALA B CA  1 
ATOM   2215 C  C   . ALA B 1 126 ? 48.150 22.374 153.606 1.00 24.96 ? 406  ALA B C   1 
ATOM   2216 O  O   . ALA B 1 126 ? 48.822 22.433 154.634 1.00 24.90 ? 406  ALA B O   1 
ATOM   2217 C  CB  . ALA B 1 126 ? 49.424 20.868 152.075 1.00 25.56 ? 406  ALA B CB  1 
ATOM   2218 N  N   . LEU B 1 127 ? 47.450 23.407 153.139 1.00 25.75 ? 407  LEU B N   1 
ATOM   2219 C  CA  . LEU B 1 127 ? 47.424 24.683 153.849 1.00 26.02 ? 407  LEU B CA  1 
ATOM   2220 C  C   . LEU B 1 127 ? 46.121 24.869 154.627 1.00 27.45 ? 407  LEU B C   1 
ATOM   2221 O  O   . LEU B 1 127 ? 45.947 25.868 155.323 1.00 28.27 ? 407  LEU B O   1 
ATOM   2222 C  CB  . LEU B 1 127 ? 47.613 25.856 152.887 1.00 24.31 ? 407  LEU B CB  1 
ATOM   2223 C  CG  . LEU B 1 127 ? 48.951 25.959 152.146 1.00 27.21 ? 407  LEU B CG  1 
ATOM   2224 C  CD1 . LEU B 1 127 ? 48.960 27.227 151.301 1.00 24.05 ? 407  LEU B CD1 1 
ATOM   2225 C  CD2 . LEU B 1 127 ? 50.110 25.979 153.132 1.00 25.82 ? 407  LEU B CD2 1 
ATOM   2226 N  N   . GLY B 1 128 ? 45.208 23.910 154.504 1.00 27.89 ? 408  GLY B N   1 
ATOM   2227 C  CA  . GLY B 1 128 ? 43.957 23.998 155.234 1.00 30.11 ? 408  GLY B CA  1 
ATOM   2228 C  C   . GLY B 1 128 ? 42.673 24.146 154.437 1.00 31.82 ? 408  GLY B C   1 
ATOM   2229 O  O   . GLY B 1 128 ? 41.588 23.994 154.989 1.00 34.34 ? 408  GLY B O   1 
ATOM   2230 N  N   . LEU B 1 129 ? 42.772 24.438 153.147 1.00 33.15 ? 409  LEU B N   1 
ATOM   2231 C  CA  . LEU B 1 129 ? 41.575 24.601 152.325 1.00 32.57 ? 409  LEU B CA  1 
ATOM   2232 C  C   . LEU B 1 129 ? 40.826 23.305 152.034 1.00 33.31 ? 409  LEU B C   1 
ATOM   2233 O  O   . LEU B 1 129 ? 41.427 22.250 151.850 1.00 32.51 ? 409  LEU B O   1 
ATOM   2234 C  CB  . LEU B 1 129 ? 41.925 25.260 150.991 1.00 31.21 ? 409  LEU B CB  1 
ATOM   2235 C  CG  . LEU B 1 129 ? 42.400 26.711 151.009 1.00 32.82 ? 409  LEU B CG  1 
ATOM   2236 C  CD1 . LEU B 1 129 ? 42.551 27.189 149.581 1.00 31.72 ? 409  LEU B CD1 1 
ATOM   2237 C  CD2 . LEU B 1 129 ? 41.397 27.589 151.747 1.00 33.90 ? 409  LEU B CD2 1 
ATOM   2238 N  N   . ASP B 1 130 ? 39.500 23.396 152.003 1.00 35.18 ? 410  ASP B N   1 
ATOM   2239 C  CA  . ASP B 1 130 ? 38.660 22.248 151.684 1.00 35.77 ? 410  ASP B CA  1 
ATOM   2240 C  C   . ASP B 1 130 ? 38.213 22.438 150.232 1.00 34.97 ? 410  ASP B C   1 
ATOM   2241 O  O   . ASP B 1 130 ? 38.553 23.442 149.592 1.00 31.85 ? 410  ASP B O   1 
ATOM   2242 C  CB  . ASP B 1 130 ? 37.422 22.186 152.595 1.00 42.82 ? 410  ASP B CB  1 
ATOM   2243 C  CG  . ASP B 1 130 ? 37.767 21.848 154.046 1.00 51.30 ? 410  ASP B CG  1 
ATOM   2244 O  OD1 . ASP B 1 130 ? 38.706 21.050 154.273 1.00 53.65 ? 410  ASP B OD1 1 
ATOM   2245 O  OD2 . ASP B 1 130 ? 37.084 22.365 154.963 1.00 54.35 ? 410  ASP B OD2 1 
ATOM   2246 N  N   . HIS B 1 131 ? 37.452 21.482 149.713 1.00 32.49 ? 411  HIS B N   1 
ATOM   2247 C  CA  . HIS B 1 131 ? 36.967 21.565 148.342 1.00 33.78 ? 411  HIS B CA  1 
ATOM   2248 C  C   . HIS B 1 131 ? 35.985 22.704 148.128 1.00 35.95 ? 411  HIS B C   1 
ATOM   2249 O  O   . HIS B 1 131 ? 35.224 23.062 149.028 1.00 38.94 ? 411  HIS B O   1 
ATOM   2250 C  CB  . HIS B 1 131 ? 36.312 20.248 147.944 1.00 30.30 ? 411  HIS B CB  1 
ATOM   2251 C  CG  . HIS B 1 131 ? 37.294 19.186 147.573 1.00 29.54 ? 411  HIS B CG  1 
ATOM   2252 N  ND1 . HIS B 1 131 ? 37.039 17.843 147.741 1.00 28.79 ? 411  HIS B ND1 1 
ATOM   2253 C  CD2 . HIS B 1 131 ? 38.532 19.270 147.036 1.00 27.76 ? 411  HIS B CD2 1 
ATOM   2254 C  CE1 . HIS B 1 131 ? 38.079 17.144 147.325 1.00 28.07 ? 411  HIS B CE1 1 
ATOM   2255 N  NE2 . HIS B 1 131 ? 38.998 17.986 146.892 1.00 31.97 ? 411  HIS B NE2 1 
ATOM   2256 N  N   . SER B 1 132 ? 36.013 23.274 146.927 1.00 37.78 ? 412  SER B N   1 
ATOM   2257 C  CA  . SER B 1 132 ? 35.115 24.365 146.566 1.00 38.30 ? 412  SER B CA  1 
ATOM   2258 C  C   . SER B 1 132 ? 33.957 23.800 145.763 1.00 39.44 ? 412  SER B C   1 
ATOM   2259 O  O   . SER B 1 132 ? 34.050 22.703 145.213 1.00 38.62 ? 412  SER B O   1 
ATOM   2260 C  CB  . SER B 1 132 ? 35.846 25.417 145.726 1.00 37.72 ? 412  SER B CB  1 
ATOM   2261 O  OG  . SER B 1 132 ? 34.953 26.426 145.281 1.00 34.94 ? 412  SER B OG  1 
ATOM   2262 N  N   . SER B 1 133 ? 32.862 24.553 145.715 1.00 41.65 ? 413  SER B N   1 
ATOM   2263 C  CA  . SER B 1 133 ? 31.672 24.149 144.973 1.00 43.35 ? 413  SER B CA  1 
ATOM   2264 C  C   . SER B 1 133 ? 31.620 24.910 143.644 1.00 43.39 ? 413  SER B C   1 
ATOM   2265 O  O   . SER B 1 133 ? 30.789 24.627 142.782 1.00 43.76 ? 413  SER B O   1 
ATOM   2266 C  CB  . SER B 1 133 ? 30.414 24.431 145.806 1.00 43.75 ? 413  SER B CB  1 
ATOM   2267 O  OG  . SER B 1 133 ? 30.416 25.759 146.311 1.00 45.44 ? 413  SER B OG  1 
ATOM   2268 N  N   . VAL B 1 134 ? 32.520 25.878 143.495 1.00 43.36 ? 414  VAL B N   1 
ATOM   2269 C  CA  . VAL B 1 134 ? 32.613 26.679 142.282 1.00 45.01 ? 414  VAL B CA  1 
ATOM   2270 C  C   . VAL B 1 134 ? 33.418 25.873 141.257 1.00 49.61 ? 414  VAL B C   1 
ATOM   2271 O  O   . VAL B 1 134 ? 34.639 25.731 141.384 1.00 50.35 ? 414  VAL B O   1 
ATOM   2272 C  CB  . VAL B 1 134 ? 33.330 28.015 142.569 1.00 43.92 ? 414  VAL B CB  1 
ATOM   2273 C  CG1 . VAL B 1 134 ? 33.395 28.862 141.307 1.00 42.90 ? 414  VAL B CG1 1 
ATOM   2274 C  CG2 . VAL B 1 134 ? 32.606 28.761 143.691 1.00 42.04 ? 414  VAL B CG2 1 
ATOM   2275 N  N   . PRO B 1 135 ? 32.739 25.326 140.231 1.00 53.34 ? 415  PRO B N   1 
ATOM   2276 C  CA  . PRO B 1 135 ? 33.348 24.518 139.166 1.00 54.30 ? 415  PRO B CA  1 
ATOM   2277 C  C   . PRO B 1 135 ? 34.614 25.060 138.505 1.00 52.96 ? 415  PRO B C   1 
ATOM   2278 O  O   . PRO B 1 135 ? 35.396 24.287 137.955 1.00 54.37 ? 415  PRO B O   1 
ATOM   2279 C  CB  . PRO B 1 135 ? 32.200 24.343 138.173 1.00 56.11 ? 415  PRO B CB  1 
ATOM   2280 C  CG  . PRO B 1 135 ? 31.014 24.261 139.078 1.00 55.46 ? 415  PRO B CG  1 
ATOM   2281 C  CD  . PRO B 1 135 ? 31.281 25.415 140.033 1.00 54.43 ? 415  PRO B CD  1 
ATOM   2282 N  N   . GLU B 1 136 ? 34.818 26.373 138.544 1.00 50.37 ? 416  GLU B N   1 
ATOM   2283 C  CA  . GLU B 1 136 ? 36.016 26.946 137.940 1.00 48.82 ? 416  GLU B CA  1 
ATOM   2284 C  C   . GLU B 1 136 ? 37.059 27.369 138.971 1.00 45.83 ? 416  GLU B C   1 
ATOM   2285 O  O   . GLU B 1 136 ? 38.023 28.060 138.646 1.00 45.77 ? 416  GLU B O   1 
ATOM   2286 C  CB  . GLU B 1 136 ? 35.662 28.135 137.041 1.00 53.26 ? 416  GLU B CB  1 
ATOM   2287 C  CG  . GLU B 1 136 ? 34.714 29.151 137.651 1.00 58.55 ? 416  GLU B CG  1 
ATOM   2288 C  CD  . GLU B 1 136 ? 33.266 28.900 137.270 1.00 61.82 ? 416  GLU B CD  1 
ATOM   2289 O  OE1 . GLU B 1 136 ? 32.399 29.699 137.684 1.00 62.91 ? 416  GLU B OE1 1 
ATOM   2290 O  OE2 . GLU B 1 136 ? 32.994 27.907 136.556 1.00 63.31 ? 416  GLU B OE2 1 
ATOM   2291 N  N   . ALA B 1 137 ? 36.859 26.964 140.220 1.00 40.82 ? 417  ALA B N   1 
ATOM   2292 C  CA  . ALA B 1 137 ? 37.811 27.283 141.278 1.00 37.74 ? 417  ALA B CA  1 
ATOM   2293 C  C   . ALA B 1 137 ? 38.867 26.181 141.281 1.00 36.14 ? 417  ALA B C   1 
ATOM   2294 O  O   . ALA B 1 137 ? 38.561 25.018 140.984 1.00 34.99 ? 417  ALA B O   1 
ATOM   2295 C  CB  . ALA B 1 137 ? 37.105 27.337 142.632 1.00 33.86 ? 417  ALA B CB  1 
ATOM   2296 N  N   . LEU B 1 138 ? 40.107 26.543 141.605 1.00 34.03 ? 418  LEU B N   1 
ATOM   2297 C  CA  . LEU B 1 138 ? 41.191 25.569 141.648 1.00 30.71 ? 418  LEU B CA  1 
ATOM   2298 C  C   . LEU B 1 138 ? 40.886 24.445 142.629 1.00 30.37 ? 418  LEU B C   1 
ATOM   2299 O  O   . LEU B 1 138 ? 41.261 23.295 142.402 1.00 31.03 ? 418  LEU B O   1 
ATOM   2300 C  CB  . LEU B 1 138 ? 42.502 26.248 142.048 1.00 31.54 ? 418  LEU B CB  1 
ATOM   2301 C  CG  . LEU B 1 138 ? 43.718 25.338 142.279 1.00 30.96 ? 418  LEU B CG  1 
ATOM   2302 C  CD1 . LEU B 1 138 ? 44.048 24.554 141.013 1.00 28.41 ? 418  LEU B CD1 1 
ATOM   2303 C  CD2 . LEU B 1 138 ? 44.908 26.190 142.704 1.00 29.00 ? 418  LEU B CD2 1 
ATOM   2304 N  N   . MET B 1 139 ? 40.197 24.772 143.719 1.00 29.50 ? 419  MET B N   1 
ATOM   2305 C  CA  . MET B 1 139 ? 39.871 23.764 144.717 1.00 30.42 ? 419  MET B CA  1 
ATOM   2306 C  C   . MET B 1 139 ? 38.688 22.862 144.381 1.00 30.21 ? 419  MET B C   1 
ATOM   2307 O  O   . MET B 1 139 ? 38.301 22.021 145.193 1.00 30.07 ? 419  MET B O   1 
ATOM   2308 C  CB  . MET B 1 139 ? 39.657 24.418 146.085 1.00 31.33 ? 419  MET B CB  1 
ATOM   2309 C  CG  . MET B 1 139 ? 40.933 24.997 146.691 1.00 31.92 ? 419  MET B CG  1 
ATOM   2310 S  SD  . MET B 1 139 ? 42.360 23.881 146.543 1.00 33.33 ? 419  MET B SD  1 
ATOM   2311 C  CE  . MET B 1 139 ? 41.836 22.484 147.532 1.00 27.72 ? 419  MET B CE  1 
ATOM   2312 N  N   . TYR B 1 140 ? 38.119 23.026 143.190 1.00 31.40 ? 420  TYR B N   1 
ATOM   2313 C  CA  . TYR B 1 140 ? 37.006 22.180 142.769 1.00 31.95 ? 420  TYR B CA  1 
ATOM   2314 C  C   . TYR B 1 140 ? 37.558 20.749 142.790 1.00 31.80 ? 420  TYR B C   1 
ATOM   2315 O  O   . TYR B 1 140 ? 38.658 20.498 142.310 1.00 35.03 ? 420  TYR B O   1 
ATOM   2316 C  CB  . TYR B 1 140 ? 36.550 22.570 141.356 1.00 36.57 ? 420  TYR B CB  1 
ATOM   2317 C  CG  . TYR B 1 140 ? 35.227 21.951 140.953 1.00 41.51 ? 420  TYR B CG  1 
ATOM   2318 C  CD1 . TYR B 1 140 ? 34.035 22.330 141.577 1.00 43.15 ? 420  TYR B CD1 1 
ATOM   2319 C  CD2 . TYR B 1 140 ? 35.173 20.947 139.986 1.00 42.71 ? 420  TYR B CD2 1 
ATOM   2320 C  CE1 . TYR B 1 140 ? 32.824 21.719 141.250 1.00 43.91 ? 420  TYR B CE1 1 
ATOM   2321 C  CE2 . TYR B 1 140 ? 33.971 20.330 139.655 1.00 43.77 ? 420  TYR B CE2 1 
ATOM   2322 C  CZ  . TYR B 1 140 ? 32.803 20.717 140.290 1.00 44.73 ? 420  TYR B CZ  1 
ATOM   2323 O  OH  . TYR B 1 140 ? 31.628 20.080 139.969 1.00 45.83 ? 420  TYR B OH  1 
ATOM   2324 N  N   . PRO B 1 141 ? 36.797 19.792 143.340 1.00 31.81 ? 421  PRO B N   1 
ATOM   2325 C  CA  . PRO B 1 141 ? 37.177 18.376 143.455 1.00 31.76 ? 421  PRO B CA  1 
ATOM   2326 C  C   . PRO B 1 141 ? 37.462 17.536 142.212 1.00 32.82 ? 421  PRO B C   1 
ATOM   2327 O  O   . PRO B 1 141 ? 37.890 16.383 142.329 1.00 33.44 ? 421  PRO B O   1 
ATOM   2328 C  CB  . PRO B 1 141 ? 36.033 17.783 144.277 1.00 32.37 ? 421  PRO B CB  1 
ATOM   2329 C  CG  . PRO B 1 141 ? 34.869 18.597 143.833 1.00 31.84 ? 421  PRO B CG  1 
ATOM   2330 C  CD  . PRO B 1 141 ? 35.430 20.002 143.846 1.00 31.47 ? 421  PRO B CD  1 
ATOM   2331 N  N   . MET B 1 142 ? 37.225 18.078 141.028 1.00 34.03 ? 422  MET B N   1 
ATOM   2332 C  CA  . MET B 1 142 ? 37.469 17.303 139.819 1.00 34.21 ? 422  MET B CA  1 
ATOM   2333 C  C   . MET B 1 142 ? 38.520 17.987 138.965 1.00 30.07 ? 422  MET B C   1 
ATOM   2334 O  O   . MET B 1 142 ? 38.610 19.208 138.960 1.00 27.30 ? 422  MET B O   1 
ATOM   2335 C  CB  . MET B 1 142 ? 36.156 17.127 139.050 1.00 40.49 ? 422  MET B CB  1 
ATOM   2336 C  CG  . MET B 1 142 ? 35.093 16.379 139.863 1.00 46.52 ? 422  MET B CG  1 
ATOM   2337 S  SD  . MET B 1 142 ? 33.548 16.039 138.978 1.00 54.83 ? 422  MET B SD  1 
ATOM   2338 C  CE  . MET B 1 142 ? 33.899 14.421 138.287 1.00 48.46 ? 422  MET B CE  1 
ATOM   2339 N  N   . TYR B 1 143 ? 39.328 17.205 138.256 1.00 30.57 ? 423  TYR B N   1 
ATOM   2340 C  CA  . TYR B 1 143 ? 40.386 17.789 137.423 1.00 30.47 ? 423  TYR B CA  1 
ATOM   2341 C  C   . TYR B 1 143 ? 39.891 18.450 136.132 1.00 29.81 ? 423  TYR B C   1 
ATOM   2342 O  O   . TYR B 1 143 ? 38.997 17.941 135.456 1.00 28.16 ? 423  TYR B O   1 
ATOM   2343 C  CB  . TYR B 1 143 ? 41.432 16.730 137.066 1.00 28.25 ? 423  TYR B CB  1 
ATOM   2344 C  CG  . TYR B 1 143 ? 42.541 17.261 136.179 1.00 28.83 ? 423  TYR B CG  1 
ATOM   2345 C  CD1 . TYR B 1 143 ? 43.549 18.077 136.695 1.00 26.05 ? 423  TYR B CD1 1 
ATOM   2346 C  CD2 . TYR B 1 143 ? 42.557 16.984 134.809 1.00 29.17 ? 423  TYR B CD2 1 
ATOM   2347 C  CE1 . TYR B 1 143 ? 44.547 18.607 135.866 1.00 26.97 ? 423  TYR B CE1 1 
ATOM   2348 C  CE2 . TYR B 1 143 ? 43.548 17.509 133.973 1.00 28.79 ? 423  TYR B CE2 1 
ATOM   2349 C  CZ  . TYR B 1 143 ? 44.537 18.319 134.508 1.00 27.46 ? 423  TYR B CZ  1 
ATOM   2350 O  OH  . TYR B 1 143 ? 45.499 18.848 133.679 1.00 29.00 ? 423  TYR B OH  1 
ATOM   2351 N  N   . ARG B 1 144 ? 40.496 19.583 135.795 1.00 30.84 ? 424  ARG B N   1 
ATOM   2352 C  CA  . ARG B 1 144 ? 40.155 20.320 134.582 1.00 30.74 ? 424  ARG B CA  1 
ATOM   2353 C  C   . ARG B 1 144 ? 41.316 21.241 134.201 1.00 31.98 ? 424  ARG B C   1 
ATOM   2354 O  O   . ARG B 1 144 ? 41.662 22.147 134.960 1.00 30.87 ? 424  ARG B O   1 
ATOM   2355 C  CB  . ARG B 1 144 ? 38.891 21.137 134.809 1.00 30.80 ? 424  ARG B CB  1 
ATOM   2356 N  N   . PHE B 1 145 ? 41.916 21.016 133.030 1.00 32.65 ? 425  PHE B N   1 
ATOM   2357 C  CA  . PHE B 1 145 ? 43.037 21.847 132.587 1.00 32.21 ? 425  PHE B CA  1 
ATOM   2358 C  C   . PHE B 1 145 ? 42.612 23.261 132.226 1.00 32.08 ? 425  PHE B C   1 
ATOM   2359 O  O   . PHE B 1 145 ? 41.517 23.474 131.723 1.00 35.15 ? 425  PHE B O   1 
ATOM   2360 C  CB  . PHE B 1 145 ? 43.761 21.219 131.387 1.00 29.42 ? 425  PHE B CB  1 
ATOM   2361 C  CG  . PHE B 1 145 ? 44.871 22.085 130.837 1.00 28.07 ? 425  PHE B CG  1 
ATOM   2362 C  CD1 . PHE B 1 145 ? 44.635 22.967 129.783 1.00 26.46 ? 425  PHE B CD1 1 
ATOM   2363 C  CD2 . PHE B 1 145 ? 46.130 22.075 131.427 1.00 26.10 ? 425  PHE B CD2 1 
ATOM   2364 C  CE1 . PHE B 1 145 ? 45.636 23.828 129.334 1.00 26.71 ? 425  PHE B CE1 1 
ATOM   2365 C  CE2 . PHE B 1 145 ? 47.138 22.933 130.986 1.00 23.65 ? 425  PHE B CE2 1 
ATOM   2366 C  CZ  . PHE B 1 145 ? 46.890 23.811 129.941 1.00 24.65 ? 425  PHE B CZ  1 
ATOM   2367 N  N   . THR B 1 146 ? 43.489 24.226 132.480 1.00 32.53 ? 426  THR B N   1 
ATOM   2368 C  CA  . THR B 1 146 ? 43.193 25.618 132.170 1.00 31.99 ? 426  THR B CA  1 
ATOM   2369 C  C   . THR B 1 146 ? 44.470 26.415 131.960 1.00 32.40 ? 426  THR B C   1 
ATOM   2370 O  O   . THR B 1 146 ? 45.515 26.082 132.515 1.00 31.41 ? 426  THR B O   1 
ATOM   2371 C  CB  . THR B 1 146 ? 42.377 26.297 133.309 1.00 33.76 ? 426  THR B CB  1 
ATOM   2372 O  OG1 . THR B 1 146 ? 42.153 27.674 132.979 1.00 35.23 ? 426  THR B OG1 1 
ATOM   2373 C  CG2 . THR B 1 146 ? 43.132 26.236 134.638 1.00 32.87 ? 426  THR B CG2 1 
ATOM   2374 N  N   . GLU B 1 147 ? 44.376 27.458 131.143 1.00 32.69 ? 427  GLU B N   1 
ATOM   2375 C  CA  . GLU B 1 147 ? 45.505 28.338 130.877 1.00 34.12 ? 427  GLU B CA  1 
ATOM   2376 C  C   . GLU B 1 147 ? 45.237 29.605 131.680 1.00 33.67 ? 427  GLU B C   1 
ATOM   2377 O  O   . GLU B 1 147 ? 44.133 29.793 132.186 1.00 35.20 ? 427  GLU B O   1 
ATOM   2378 C  CB  . GLU B 1 147 ? 45.593 28.670 129.384 1.00 36.51 ? 427  GLU B CB  1 
ATOM   2379 C  CG  . GLU B 1 147 ? 45.967 27.493 128.490 1.00 41.69 ? 427  GLU B CG  1 
ATOM   2380 C  CD  . GLU B 1 147 ? 46.103 27.888 127.024 1.00 45.50 ? 427  GLU B CD  1 
ATOM   2381 O  OE1 . GLU B 1 147 ? 45.082 28.269 126.410 1.00 44.55 ? 427  GLU B OE1 1 
ATOM   2382 O  OE2 . GLU B 1 147 ? 47.235 27.822 126.488 1.00 47.29 ? 427  GLU B OE2 1 
ATOM   2383 N  N   . GLY B 1 148 ? 46.234 30.471 131.800 1.00 33.34 ? 428  GLY B N   1 
ATOM   2384 C  CA  . GLY B 1 148 ? 46.041 31.692 132.561 1.00 34.51 ? 428  GLY B CA  1 
ATOM   2385 C  C   . GLY B 1 148 ? 46.066 31.428 134.057 1.00 36.70 ? 428  GLY B C   1 
ATOM   2386 O  O   . GLY B 1 148 ? 46.241 30.281 134.475 1.00 35.95 ? 428  GLY B O   1 
ATOM   2387 N  N   . PRO B 1 149 ? 45.887 32.468 134.893 1.00 37.61 ? 429  PRO B N   1 
ATOM   2388 C  CA  . PRO B 1 149 ? 45.888 32.363 136.361 1.00 35.27 ? 429  PRO B CA  1 
ATOM   2389 C  C   . PRO B 1 149 ? 44.969 31.258 136.882 1.00 34.51 ? 429  PRO B C   1 
ATOM   2390 O  O   . PRO B 1 149 ? 43.769 31.248 136.605 1.00 35.20 ? 429  PRO B O   1 
ATOM   2391 C  CB  . PRO B 1 149 ? 45.444 33.753 136.806 1.00 36.80 ? 429  PRO B CB  1 
ATOM   2392 C  CG  . PRO B 1 149 ? 44.594 34.224 135.655 1.00 38.82 ? 429  PRO B CG  1 
ATOM   2393 C  CD  . PRO B 1 149 ? 45.427 33.803 134.473 1.00 37.68 ? 429  PRO B CD  1 
ATOM   2394 N  N   . PRO B 1 150 ? 45.533 30.312 137.648 1.00 32.84 ? 430  PRO B N   1 
ATOM   2395 C  CA  . PRO B 1 150 ? 44.843 29.160 138.246 1.00 33.23 ? 430  PRO B CA  1 
ATOM   2396 C  C   . PRO B 1 150 ? 43.870 29.482 139.381 1.00 33.86 ? 430  PRO B C   1 
ATOM   2397 O  O   . PRO B 1 150 ? 42.786 28.891 139.475 1.00 32.09 ? 430  PRO B O   1 
ATOM   2398 C  CB  . PRO B 1 150 ? 45.997 28.284 138.747 1.00 32.15 ? 430  PRO B CB  1 
ATOM   2399 C  CG  . PRO B 1 150 ? 47.172 28.722 137.930 1.00 32.06 ? 430  PRO B CG  1 
ATOM   2400 C  CD  . PRO B 1 150 ? 46.984 30.207 137.866 1.00 30.88 ? 430  PRO B CD  1 
ATOM   2401 N  N   . LEU B 1 151 ? 44.271 30.405 140.250 1.00 34.56 ? 431  LEU B N   1 
ATOM   2402 C  CA  . LEU B 1 151 ? 43.456 30.778 141.401 1.00 35.70 ? 431  LEU B CA  1 
ATOM   2403 C  C   . LEU B 1 151 ? 42.207 31.588 141.084 1.00 36.24 ? 431  LEU B C   1 
ATOM   2404 O  O   . LEU B 1 151 ? 42.271 32.661 140.479 1.00 36.37 ? 431  LEU B O   1 
ATOM   2405 C  CB  . LEU B 1 151 ? 44.300 31.550 142.419 1.00 33.79 ? 431  LEU B CB  1 
ATOM   2406 C  CG  . LEU B 1 151 ? 45.449 30.793 143.080 1.00 33.47 ? 431  LEU B CG  1 
ATOM   2407 C  CD1 . LEU B 1 151 ? 46.049 31.651 144.190 1.00 33.46 ? 431  LEU B CD1 1 
ATOM   2408 C  CD2 . LEU B 1 151 ? 44.934 29.481 143.649 1.00 36.47 ? 431  LEU B CD2 1 
ATOM   2409 N  N   . HIS B 1 152 ? 41.064 31.064 141.505 1.00 36.71 ? 432  HIS B N   1 
ATOM   2410 C  CA  . HIS B 1 152 ? 39.811 31.760 141.299 1.00 41.25 ? 432  HIS B CA  1 
ATOM   2411 C  C   . HIS B 1 152 ? 39.613 32.670 142.507 1.00 44.37 ? 432  HIS B C   1 
ATOM   2412 O  O   . HIS B 1 152 ? 40.151 32.400 143.588 1.00 46.02 ? 432  HIS B O   1 
ATOM   2413 C  CB  . HIS B 1 152 ? 38.662 30.761 141.191 1.00 40.99 ? 432  HIS B CB  1 
ATOM   2414 C  CG  . HIS B 1 152 ? 37.332 31.404 140.963 1.00 44.68 ? 432  HIS B CG  1 
ATOM   2415 N  ND1 . HIS B 1 152 ? 36.626 32.031 141.967 1.00 46.47 ? 432  HIS B ND1 1 
ATOM   2416 C  CD2 . HIS B 1 152 ? 36.589 31.541 139.838 1.00 44.42 ? 432  HIS B CD2 1 
ATOM   2417 C  CE1 . HIS B 1 152 ? 35.504 32.524 141.472 1.00 45.59 ? 432  HIS B CE1 1 
ATOM   2418 N  NE2 . HIS B 1 152 ? 35.459 32.241 140.182 1.00 46.62 ? 432  HIS B NE2 1 
ATOM   2419 N  N   . LYS B 1 153 ? 38.859 33.751 142.330 1.00 46.58 ? 433  LYS B N   1 
ATOM   2420 C  CA  . LYS B 1 153 ? 38.627 34.678 143.428 1.00 46.70 ? 433  LYS B CA  1 
ATOM   2421 C  C   . LYS B 1 153 ? 38.062 33.973 144.658 1.00 43.89 ? 433  LYS B C   1 
ATOM   2422 O  O   . LYS B 1 153 ? 38.150 34.491 145.767 1.00 44.99 ? 433  LYS B O   1 
ATOM   2423 C  CB  . LYS B 1 153 ? 37.717 35.822 142.972 1.00 51.43 ? 433  LYS B CB  1 
ATOM   2424 C  CG  . LYS B 1 153 ? 38.355 36.668 141.865 1.00 55.90 ? 433  LYS B CG  1 
ATOM   2425 C  CD  . LYS B 1 153 ? 37.589 37.956 141.584 1.00 59.77 ? 433  LYS B CD  1 
ATOM   2426 C  CE  . LYS B 1 153 ? 38.320 38.811 140.549 1.00 61.80 ? 433  LYS B CE  1 
ATOM   2427 N  NZ  . LYS B 1 153 ? 37.720 40.171 140.380 1.00 62.64 ? 433  LYS B NZ  1 
ATOM   2428 N  N   . ASP B 1 154 ? 37.501 32.783 144.460 1.00 40.87 ? 434  ASP B N   1 
ATOM   2429 C  CA  . ASP B 1 154 ? 36.964 31.998 145.565 1.00 39.24 ? 434  ASP B CA  1 
ATOM   2430 C  C   . ASP B 1 154 ? 38.127 31.365 146.337 1.00 40.97 ? 434  ASP B C   1 
ATOM   2431 O  O   . ASP B 1 154 ? 38.102 31.288 147.571 1.00 41.38 ? 434  ASP B O   1 
ATOM   2432 C  CB  . ASP B 1 154 ? 36.032 30.905 145.038 1.00 38.77 ? 434  ASP B CB  1 
ATOM   2433 C  CG  . ASP B 1 154 ? 35.520 29.999 146.138 1.00 39.93 ? 434  ASP B CG  1 
ATOM   2434 O  OD1 . ASP B 1 154 ? 36.053 28.882 146.286 1.00 43.55 ? 434  ASP B OD1 1 
ATOM   2435 O  OD2 . ASP B 1 154 ? 34.593 30.408 146.866 1.00 42.42 ? 434  ASP B OD2 1 
ATOM   2436 N  N   . ASP B 1 155 ? 39.144 30.915 145.601 1.00 39.44 ? 435  ASP B N   1 
ATOM   2437 C  CA  . ASP B 1 155 ? 40.324 30.305 146.204 1.00 37.18 ? 435  ASP B CA  1 
ATOM   2438 C  C   . ASP B 1 155 ? 41.088 31.354 147.007 1.00 38.01 ? 435  ASP B C   1 
ATOM   2439 O  O   . ASP B 1 155 ? 41.591 31.077 148.098 1.00 39.15 ? 435  ASP B O   1 
ATOM   2440 C  CB  . ASP B 1 155 ? 41.258 29.737 145.128 1.00 36.04 ? 435  ASP B CB  1 
ATOM   2441 C  CG  . ASP B 1 155 ? 40.608 28.653 144.293 1.00 37.10 ? 435  ASP B CG  1 
ATOM   2442 O  OD1 . ASP B 1 155 ? 40.086 27.671 144.868 1.00 35.74 ? 435  ASP B OD1 1 
ATOM   2443 O  OD2 . ASP B 1 155 ? 40.632 28.779 143.050 1.00 40.79 ? 435  ASP B OD2 1 
ATOM   2444 N  N   . VAL B 1 156 ? 41.178 32.560 146.459 1.00 37.34 ? 436  VAL B N   1 
ATOM   2445 C  CA  . VAL B 1 156 ? 41.893 33.637 147.127 1.00 37.88 ? 436  VAL B CA  1 
ATOM   2446 C  C   . VAL B 1 156 ? 41.203 34.051 148.426 1.00 41.35 ? 436  VAL B C   1 
ATOM   2447 O  O   . VAL B 1 156 ? 41.870 34.444 149.392 1.00 40.58 ? 436  VAL B O   1 
ATOM   2448 C  CB  . VAL B 1 156 ? 42.018 34.863 146.209 1.00 37.00 ? 436  VAL B CB  1 
ATOM   2449 C  CG1 . VAL B 1 156 ? 42.850 35.939 146.887 1.00 37.16 ? 436  VAL B CG1 1 
ATOM   2450 C  CG2 . VAL B 1 156 ? 42.654 34.454 144.893 1.00 37.45 ? 436  VAL B CG2 1 
ATOM   2451 N  N   . ASN B 1 157 ? 39.872 33.964 148.445 1.00 42.61 ? 437  ASN B N   1 
ATOM   2452 C  CA  . ASN B 1 157 ? 39.103 34.323 149.633 1.00 42.98 ? 437  ASN B CA  1 
ATOM   2453 C  C   . ASN B 1 157 ? 39.341 33.309 150.732 1.00 41.97 ? 437  ASN B C   1 
ATOM   2454 O  O   . ASN B 1 157 ? 39.656 33.665 151.863 1.00 44.18 ? 437  ASN B O   1 
ATOM   2455 C  CB  . ASN B 1 157 ? 37.602 34.372 149.331 1.00 44.38 ? 437  ASN B CB  1 
ATOM   2456 C  CG  . ASN B 1 157 ? 37.199 35.607 148.564 1.00 46.07 ? 437  ASN B CG  1 
ATOM   2457 O  OD1 . ASN B 1 157 ? 37.778 36.681 148.743 1.00 49.54 ? 437  ASN B OD1 1 
ATOM   2458 N  ND2 . ASN B 1 157 ? 36.182 35.471 147.721 1.00 46.44 ? 437  ASN B ND2 1 
ATOM   2459 N  N   . GLY B 1 158 ? 39.177 32.038 150.391 1.00 42.23 ? 438  GLY B N   1 
ATOM   2460 C  CA  . GLY B 1 158 ? 39.373 30.980 151.364 1.00 41.20 ? 438  GLY B CA  1 
ATOM   2461 C  C   . GLY B 1 158 ? 40.737 31.015 152.030 1.00 40.27 ? 438  GLY B C   1 
ATOM   2462 O  O   . GLY B 1 158 ? 40.851 30.821 153.241 1.00 40.43 ? 438  GLY B O   1 
ATOM   2463 N  N   . ILE B 1 159 ? 41.778 31.269 151.246 1.00 39.21 ? 439  ILE B N   1 
ATOM   2464 C  CA  . ILE B 1 159 ? 43.125 31.305 151.796 1.00 38.89 ? 439  ILE B CA  1 
ATOM   2465 C  C   . ILE B 1 159 ? 43.317 32.597 152.587 1.00 40.47 ? 439  ILE B C   1 
ATOM   2466 O  O   . ILE B 1 159 ? 44.034 32.625 153.588 1.00 41.20 ? 439  ILE B O   1 
ATOM   2467 C  CB  . ILE B 1 159 ? 44.195 31.186 150.666 1.00 34.85 ? 439  ILE B CB  1 
ATOM   2468 C  CG1 . ILE B 1 159 ? 45.546 30.783 151.262 1.00 34.00 ? 439  ILE B CG1 1 
ATOM   2469 C  CG2 . ILE B 1 159 ? 44.318 32.488 149.913 1.00 32.27 ? 439  ILE B CG2 1 
ATOM   2470 C  CD1 . ILE B 1 159 ? 45.558 29.373 151.853 1.00 32.09 ? 439  ILE B CD1 1 
ATOM   2471 N  N   . ARG B 1 160 ? 42.654 33.658 152.134 1.00 43.75 ? 440  ARG B N   1 
ATOM   2472 C  CA  . ARG B 1 160 ? 42.725 34.967 152.782 1.00 44.46 ? 440  ARG B CA  1 
ATOM   2473 C  C   . ARG B 1 160 ? 42.006 34.908 154.128 1.00 44.17 ? 440  ARG B C   1 
ATOM   2474 O  O   . ARG B 1 160 ? 42.320 35.666 155.047 1.00 43.24 ? 440  ARG B O   1 
ATOM   2475 C  CB  . ARG B 1 160 ? 42.048 36.030 151.909 1.00 46.94 ? 440  ARG B CB  1 
ATOM   2476 C  CG  . ARG B 1 160 ? 42.937 37.185 151.471 1.00 49.56 ? 440  ARG B CG  1 
ATOM   2477 C  CD  . ARG B 1 160 ? 43.845 36.769 150.334 1.00 54.73 ? 440  ARG B CD  1 
ATOM   2478 N  NE  . ARG B 1 160 ? 44.726 37.850 149.901 1.00 58.03 ? 440  ARG B NE  1 
ATOM   2479 C  CZ  . ARG B 1 160 ? 44.306 38.991 149.362 1.00 60.42 ? 440  ARG B CZ  1 
ATOM   2480 N  NH1 . ARG B 1 160 ? 43.009 39.211 149.186 1.00 60.93 ? 440  ARG B NH1 1 
ATOM   2481 N  NH2 . ARG B 1 160 ? 45.188 39.910 148.988 1.00 60.50 ? 440  ARG B NH2 1 
ATOM   2482 N  N   . HIS B 1 161 ? 41.033 34.004 154.221 1.00 42.88 ? 441  HIS B N   1 
ATOM   2483 C  CA  . HIS B 1 161 ? 40.235 33.818 155.428 1.00 43.46 ? 441  HIS B CA  1 
ATOM   2484 C  C   . HIS B 1 161 ? 41.029 33.144 156.538 1.00 42.38 ? 441  HIS B C   1 
ATOM   2485 O  O   . HIS B 1 161 ? 40.835 33.448 157.713 1.00 43.43 ? 441  HIS B O   1 
ATOM   2486 C  CB  . HIS B 1 161 ? 38.997 32.972 155.112 1.00 46.73 ? 441  HIS B CB  1 
ATOM   2487 C  CG  . HIS B 1 161 ? 38.118 32.713 156.297 1.00 52.22 ? 441  HIS B CG  1 
ATOM   2488 N  ND1 . HIS B 1 161 ? 37.331 33.690 156.871 1.00 54.78 ? 441  HIS B ND1 1 
ATOM   2489 C  CD2 . HIS B 1 161 ? 37.906 31.588 157.022 1.00 53.91 ? 441  HIS B CD2 1 
ATOM   2490 C  CE1 . HIS B 1 161 ? 36.673 33.178 157.896 1.00 54.20 ? 441  HIS B CE1 1 
ATOM   2491 N  NE2 . HIS B 1 161 ? 37.005 31.904 158.010 1.00 54.76 ? 441  HIS B NE2 1 
ATOM   2492 N  N   . LEU B 1 162 ? 41.924 32.233 156.158 1.00 40.54 ? 442  LEU B N   1 
ATOM   2493 C  CA  . LEU B 1 162 ? 42.747 31.495 157.118 1.00 37.84 ? 442  LEU B CA  1 
ATOM   2494 C  C   . LEU B 1 162 ? 44.012 32.232 157.548 1.00 35.29 ? 442  LEU B C   1 
ATOM   2495 O  O   . LEU B 1 162 ? 44.367 32.218 158.721 1.00 37.44 ? 442  LEU B O   1 
ATOM   2496 C  CB  . LEU B 1 162 ? 43.136 30.124 156.542 1.00 36.23 ? 442  LEU B CB  1 
ATOM   2497 C  CG  . LEU B 1 162 ? 42.020 29.121 156.224 1.00 36.95 ? 442  LEU B CG  1 
ATOM   2498 C  CD1 . LEU B 1 162 ? 42.600 27.921 155.494 1.00 37.45 ? 442  LEU B CD1 1 
ATOM   2499 C  CD2 . LEU B 1 162 ? 41.337 28.676 157.507 1.00 38.67 ? 442  LEU B CD2 1 
ATOM   2500 N  N   . TYR B 1 163 ? 44.693 32.872 156.605 1.00 34.38 ? 443  TYR B N   1 
ATOM   2501 C  CA  . TYR B 1 163 ? 45.932 33.581 156.920 1.00 36.23 ? 443  TYR B CA  1 
ATOM   2502 C  C   . TYR B 1 163 ? 45.855 35.082 156.659 1.00 38.24 ? 443  TYR B C   1 
ATOM   2503 O  O   . TYR B 1 163 ? 46.801 35.794 157.063 1.00 40.58 ? 443  TYR B O   1 
ATOM   2504 C  CB  . TYR B 1 163 ? 47.105 32.984 156.123 1.00 34.25 ? 443  TYR B CB  1 
ATOM   2505 C  CG  . TYR B 1 163 ? 47.261 31.490 156.300 1.00 31.93 ? 443  TYR B CG  1 
ATOM   2506 C  CD1 . TYR B 1 163 ? 46.614 30.596 155.446 1.00 29.81 ? 443  TYR B CD1 1 
ATOM   2507 C  CD2 . TYR B 1 163 ? 48.004 30.968 157.366 1.00 29.17 ? 443  TYR B CD2 1 
ATOM   2508 C  CE1 . TYR B 1 163 ? 46.695 29.215 155.649 1.00 28.03 ? 443  TYR B CE1 1 
ATOM   2509 C  CE2 . TYR B 1 163 ? 48.092 29.592 157.578 1.00 28.10 ? 443  TYR B CE2 1 
ATOM   2510 C  CZ  . TYR B 1 163 ? 47.433 28.721 156.718 1.00 29.15 ? 443  TYR B CZ  1 
ATOM   2511 O  OH  . TYR B 1 163 ? 47.496 27.360 156.932 1.00 27.85 ? 443  TYR B OH  1 
ATOM   2512 O  OXT . TYR B 1 163 ? 44.864 35.527 156.044 1.00 41.15 ? 443  TYR B OXT 1 
HETATM 2513 CA CA  . CA  C 2 .   ? 71.413 25.140 121.665 1.00 25.39 ? 1444 CA  A CA  1 
HETATM 2514 CA CA  . CA  D 2 .   ? 63.107 15.170 103.757 1.00 28.86 ? 1445 CA  A CA  1 
HETATM 2515 CA CA  . CA  E 2 .   ? 67.687 17.476 126.440 1.00 49.10 ? 1446 CA  A CA  1 
HETATM 2516 CA CA  . CA  F 2 .   ? 57.389 24.336 131.008 1.00 56.13 ? 1447 CA  A CA  1 
HETATM 2517 C  C   . NFH G 3 .   ? 66.274 30.187 117.629 1.00 22.72 ? 1448 NFH A C   1 
HETATM 2518 N  N   . NFH G 3 .   ? 65.323 29.140 114.074 1.00 19.54 ? 1448 NFH A N   1 
HETATM 2519 O  O   . NFH G 3 .   ? 66.882 29.180 118.067 1.00 22.29 ? 1448 NFH A O   1 
HETATM 2520 C  C1  . NFH G 3 .   ? 66.491 31.847 120.586 1.00 23.15 ? 1448 NFH A C1  1 
HETATM 2521 N  N1  . NFH G 3 .   ? 66.450 31.428 118.131 1.00 21.65 ? 1448 NFH A N1  1 
HETATM 2522 O  O1  . NFH G 3 .   ? 65.406 32.468 120.589 1.00 24.19 ? 1448 NFH A O1  1 
HETATM 2523 N  N2  . NFH G 3 .   ? 67.003 31.196 121.667 1.00 21.19 ? 1448 NFH A N2  1 
HETATM 2524 C  CA  . NFH G 3 .   ? 65.268 30.026 116.452 1.00 20.30 ? 1448 NFH A CA  1 
HETATM 2525 C  CB  . NFH G 3 .   ? 64.019 29.134 116.841 1.00 18.44 ? 1448 NFH A CB  1 
HETATM 2526 C  CG  . NFH G 3 .   ? 63.038 29.608 117.942 1.00 19.42 ? 1448 NFH A CG  1 
HETATM 2527 C  CM  . NFH G 3 .   ? 64.851 27.958 113.673 1.00 20.49 ? 1448 NFH A CM  1 
HETATM 2528 O  OM  . NFH G 3 .   ? 64.213 27.793 112.689 1.00 19.70 ? 1448 NFH A OM  1 
HETATM 2529 C  CN  . NFH G 3 .   ? 66.093 29.344 115.298 1.00 21.58 ? 1448 NFH A CN  1 
HETATM 2530 O  ON  . NFH G 3 .   ? 65.083 30.177 113.358 1.00 20.40 ? 1448 NFH A ON  1 
HETATM 2531 C  CA1 . NFH G 3 .   ? 67.389 31.754 119.271 1.00 23.60 ? 1448 NFH A CA1 1 
HETATM 2532 C  CB1 . NFH G 3 .   ? 68.279 33.067 118.969 1.00 24.52 ? 1448 NFH A CB1 1 
HETATM 2533 C  CD1 . NFH G 3 .   ? 62.295 30.885 117.488 1.00 16.45 ? 1448 NFH A CD1 1 
HETATM 2534 C  CD2 . NFH G 3 .   ? 61.951 28.564 118.122 1.00 18.32 ? 1448 NFH A CD2 1 
HETATM 2535 C  CG1 . NFH G 3 .   ? 69.263 33.407 120.153 1.00 23.38 ? 1448 NFH A CG1 1 
HETATM 2536 C  CG2 . NFH G 3 .   ? 69.119 32.883 117.677 1.00 21.36 ? 1448 NFH A CG2 1 
HETATM 2537 C  CG3 . NFH G 3 .   ? 67.424 34.373 118.736 1.00 23.95 ? 1448 NFH A CG3 1 
HETATM 2538 C  CN2 . NFH G 3 .   ? 66.350 31.137 122.996 1.00 25.36 ? 1448 NFH A CN2 1 
HETATM 2539 ZN ZN  . ZN  H 4 .   ? 63.267 29.950 112.382 1.00 18.93 ? 1450 ZN  A ZN  1 
HETATM 2540 ZN ZN  . ZN  I 4 .   ? 70.729 19.617 111.673 1.00 22.07 ? 1451 ZN  A ZN  1 
HETATM 2541 CA CA  . CA  J 2 .   ? 41.603 20.860 107.667 1.00 99.94 ? 1452 CA  A CA  1 
HETATM 2542 CA CA  . CA  K 2 .   ? 45.250 7.241  139.948 1.00 21.01 ? 1444 CA  B CA  1 
HETATM 2543 CA CA  . CA  L 2 .   ? 54.013 17.086 157.486 1.00 25.83 ? 1445 CA  B CA  1 
HETATM 2544 CA CA  . CA  M 2 .   ? 54.046 8.303  135.827 1.00 47.76 ? 1446 CA  B CA  1 
HETATM 2545 CA CA  . CA  N 2 .   ? 50.701 18.541 128.694 1.00 57.49 ? 1447 CA  B CA  1 
HETATM 2546 CA CA  . CA  O 2 .   ? 53.492 38.165 150.097 1.00 99.62 ? 1448 CA  B CA  1 
HETATM 2547 C  C   . NFH P 3 .   ? 41.103 13.852 141.935 1.00 24.21 ? 1449 NFH B C   1 
HETATM 2548 N  N   . NFH P 3 .   ? 41.894 15.346 145.441 1.00 26.66 ? 1449 NFH B N   1 
HETATM 2549 O  O   . NFH P 3 .   ? 42.049 13.051 141.732 1.00 25.04 ? 1449 NFH B O   1 
HETATM 2550 C  C1  . NFH P 3 .   ? 39.789 13.241 138.843 1.00 26.03 ? 1449 NFH B C1  1 
HETATM 2551 N  N1  . NFH P 3 .   ? 39.910 13.731 141.312 1.00 24.87 ? 1449 NFH B N1  1 
HETATM 2552 O  O1  . NFH P 3 .   ? 39.414 14.401 138.550 1.00 27.42 ? 1449 NFH B O1  1 
HETATM 2553 N  N2  . NFH P 3 .   ? 40.416 12.393 137.981 1.00 25.15 ? 1449 NFH B N2  1 
HETATM 2554 C  CA  . NFH P 3 .   ? 41.287 15.047 142.944 1.00 22.68 ? 1449 NFH B CA  1 
HETATM 2555 C  CB  . NFH P 3 .   ? 42.395 16.088 142.486 1.00 20.53 ? 1449 NFH B CB  1 
HETATM 2556 C  CG  . NFH P 3 .   ? 42.202 16.892 141.164 1.00 23.04 ? 1449 NFH B CG  1 
HETATM 2557 C  CM  . NFH P 3 .   ? 43.101 15.578 145.982 1.00 25.43 ? 1449 NFH B CM  1 
HETATM 2558 O  OM  . NFH P 3 .   ? 43.304 16.343 146.865 1.00 27.78 ? 1449 NFH B OM  1 
HETATM 2559 C  CN  . NFH P 3 .   ? 41.674 14.384 144.328 1.00 21.04 ? 1449 NFH B CN  1 
HETATM 2560 O  ON  . NFH P 3 .   ? 40.878 16.003 145.917 1.00 16.04 ? 1449 NFH B ON  1 
HETATM 2561 C  CA1 . NFH P 3 .   ? 39.558 12.636 140.307 1.00 25.69 ? 1449 NFH B CA1 1 
HETATM 2562 C  CB1 . NFH P 3 .   ? 38.064 12.068 140.550 1.00 26.41 ? 1449 NFH B CB1 1 
HETATM 2563 C  CD1 . NFH P 3 .   ? 40.988 17.843 141.282 1.00 21.42 ? 1449 NFH B CD1 1 
HETATM 2564 C  CD2 . NFH P 3 .   ? 43.397 17.813 140.945 1.00 21.68 ? 1449 NFH B CD2 1 
HETATM 2565 C  CG1 . NFH P 3 .   ? 37.671 10.934 139.534 1.00 23.54 ? 1449 NFH B CG1 1 
HETATM 2566 C  CG2 . NFH P 3 .   ? 37.918 11.501 141.991 1.00 25.52 ? 1449 NFH B CG2 1 
HETATM 2567 C  CG3 . NFH P 3 .   ? 36.936 13.161 140.404 1.00 25.14 ? 1449 NFH B CG3 1 
HETATM 2568 C  CN2 . NFH P 3 .   ? 40.752 12.702 136.573 1.00 30.05 ? 1449 NFH B CN2 1 
HETATM 2569 ZN ZN  . ZN  Q 4 .   ? 41.275 17.840 146.537 1.00 30.01 ? 1451 ZN  B ZN  1 
HETATM 2570 ZN ZN  . ZN  R 4 .   ? 49.676 8.887  150.296 1.00 22.73 ? 1452 ZN  B ZN  1 
HETATM 2571 O  O   . HOH S 5 .   ? 56.995 17.921 96.140  1.00 26.85 ? 2001 HOH A O   1 
HETATM 2572 O  O   . HOH S 5 .   ? 56.870 18.582 90.415  1.00 50.62 ? 2002 HOH A O   1 
HETATM 2573 O  O   . HOH S 5 .   ? 50.921 22.489 96.419  1.00 38.17 ? 2003 HOH A O   1 
HETATM 2574 O  O   . HOH S 5 .   ? 52.957 12.041 116.137 1.00 15.20 ? 2004 HOH A O   1 
HETATM 2575 O  O   . HOH S 5 .   ? 49.226 13.404 112.556 1.00 36.10 ? 2005 HOH A O   1 
HETATM 2576 O  O   . HOH S 5 .   ? 60.170 4.215  113.980 1.00 40.21 ? 2006 HOH A O   1 
HETATM 2577 O  O   . HOH S 5 .   ? 58.587 7.014  115.292 1.00 27.11 ? 2007 HOH A O   1 
HETATM 2578 O  O   . HOH S 5 .   ? 65.295 7.257  120.405 1.00 1.00  ? 2008 HOH A O   1 
HETATM 2579 O  O   . HOH S 5 .   ? 57.979 5.727  117.915 1.00 65.95 ? 2009 HOH A O   1 
HETATM 2580 O  O   . HOH S 5 .   ? 61.756 9.877  125.515 1.00 40.50 ? 2010 HOH A O   1 
HETATM 2581 O  O   . HOH S 5 .   ? 58.454 6.855  127.071 1.00 27.25 ? 2011 HOH A O   1 
HETATM 2582 O  O   . HOH S 5 .   ? 50.275 10.441 122.477 1.00 33.64 ? 2012 HOH A O   1 
HETATM 2583 O  O   . HOH S 5 .   ? 55.278 7.063  126.543 1.00 22.51 ? 2013 HOH A O   1 
HETATM 2584 O  O   . HOH S 5 .   ? 45.881 15.698 122.389 1.00 39.53 ? 2014 HOH A O   1 
HETATM 2585 O  O   . HOH S 5 .   ? 52.144 16.494 124.475 1.00 14.30 ? 2015 HOH A O   1 
HETATM 2586 O  O   . HOH S 5 .   ? 48.380 16.148 113.137 1.00 26.43 ? 2016 HOH A O   1 
HETATM 2587 O  O   . HOH S 5 .   ? 47.341 22.271 121.211 1.00 20.31 ? 2017 HOH A O   1 
HETATM 2588 O  O   . HOH S 5 .   ? 51.666 21.908 124.829 1.00 15.33 ? 2018 HOH A O   1 
HETATM 2589 O  O   . HOH S 5 .   ? 45.806 26.797 113.582 1.00 25.06 ? 2019 HOH A O   1 
HETATM 2590 O  O   . HOH S 5 .   ? 47.043 17.179 110.619 1.00 27.88 ? 2020 HOH A O   1 
HETATM 2591 O  O   . HOH S 5 .   ? 41.594 23.567 106.694 1.00 35.95 ? 2021 HOH A O   1 
HETATM 2592 O  O   . HOH S 5 .   ? 43.961 20.340 105.825 1.00 34.92 ? 2022 HOH A O   1 
HETATM 2593 O  O   . HOH S 5 .   ? 49.364 12.911 104.335 1.00 26.01 ? 2023 HOH A O   1 
HETATM 2594 O  O   . HOH S 5 .   ? 49.177 9.855  111.408 1.00 25.21 ? 2024 HOH A O   1 
HETATM 2595 O  O   . HOH S 5 .   ? 57.185 8.107  113.191 1.00 17.03 ? 2025 HOH A O   1 
HETATM 2596 O  O   . HOH S 5 .   ? 51.253 9.646  116.663 1.00 29.59 ? 2026 HOH A O   1 
HETATM 2597 O  O   . HOH S 5 .   ? 56.922 8.730  101.984 1.00 51.25 ? 2027 HOH A O   1 
HETATM 2598 O  O   . HOH S 5 .   ? 63.090 12.420 103.873 1.00 23.17 ? 2028 HOH A O   1 
HETATM 2599 O  O   . HOH S 5 .   ? 59.941 14.152 100.157 1.00 27.50 ? 2029 HOH A O   1 
HETATM 2600 O  O   . HOH S 5 .   ? 56.901 12.608 98.500  1.00 45.22 ? 2030 HOH A O   1 
HETATM 2601 O  O   . HOH S 5 .   ? 70.118 14.389 108.156 1.00 55.54 ? 2031 HOH A O   1 
HETATM 2602 O  O   . HOH S 5 .   ? 73.852 13.594 117.386 1.00 26.01 ? 2032 HOH A O   1 
HETATM 2603 O  O   . HOH S 5 .   ? 74.083 20.414 120.913 1.00 21.76 ? 2033 HOH A O   1 
HETATM 2604 O  O   . HOH S 5 .   ? 76.248 14.005 117.780 1.00 38.05 ? 2034 HOH A O   1 
HETATM 2605 O  O   . HOH S 5 .   ? 71.699 14.944 110.281 1.00 31.13 ? 2035 HOH A O   1 
HETATM 2606 O  O   . HOH S 5 .   ? 78.432 18.341 111.530 1.00 33.10 ? 2036 HOH A O   1 
HETATM 2607 O  O   . HOH S 5 .   ? 75.605 18.864 112.249 1.00 18.56 ? 2037 HOH A O   1 
HETATM 2608 O  O   . HOH S 5 .   ? 65.759 26.751 110.354 1.00 19.28 ? 2038 HOH A O   1 
HETATM 2609 O  O   . HOH S 5 .   ? 61.912 15.434 101.221 1.00 22.75 ? 2039 HOH A O   1 
HETATM 2610 O  O   . HOH S 5 .   ? 64.469 12.077 98.818  1.00 47.82 ? 2040 HOH A O   1 
HETATM 2611 O  O   . HOH S 5 .   ? 67.365 14.751 108.625 1.00 21.02 ? 2041 HOH A O   1 
HETATM 2612 O  O   . HOH S 5 .   ? 65.856 12.461 105.207 1.00 34.23 ? 2042 HOH A O   1 
HETATM 2613 O  O   . HOH S 5 .   ? 67.629 24.639 127.665 1.00 20.55 ? 2043 HOH A O   1 
HETATM 2614 O  O   . HOH S 5 .   ? 53.389 24.883 133.848 1.00 20.87 ? 2044 HOH A O   1 
HETATM 2615 O  O   . HOH S 5 .   ? 51.613 25.829 131.530 1.00 40.97 ? 2045 HOH A O   1 
HETATM 2616 O  O   . HOH S 5 .   ? 50.505 31.197 136.475 1.00 33.10 ? 2046 HOH A O   1 
HETATM 2617 O  O   . HOH S 5 .   ? 59.242 23.420 132.602 1.00 16.67 ? 2047 HOH A O   1 
HETATM 2618 O  O   . HOH S 5 .   ? 64.674 28.352 131.418 1.00 31.06 ? 2048 HOH A O   1 
HETATM 2619 O  O   . HOH S 5 .   ? 66.159 25.939 129.659 1.00 45.73 ? 2049 HOH A O   1 
HETATM 2620 O  O   . HOH S 5 .   ? 58.837 25.317 128.952 1.00 21.05 ? 2050 HOH A O   1 
HETATM 2621 O  O   . HOH S 5 .   ? 53.372 24.644 125.318 1.00 1.00  ? 2051 HOH A O   1 
HETATM 2622 O  O   . HOH S 5 .   ? 62.131 28.235 104.517 1.00 40.71 ? 2052 HOH A O   1 
HETATM 2623 O  O   . HOH S 5 .   ? 56.644 33.927 107.571 1.00 25.40 ? 2053 HOH A O   1 
HETATM 2624 O  O   . HOH S 5 .   ? 56.828 39.659 107.746 1.00 37.53 ? 2054 HOH A O   1 
HETATM 2625 O  O   . HOH S 5 .   ? 58.791 32.739 117.544 1.00 24.04 ? 2055 HOH A O   1 
HETATM 2626 O  O   . HOH S 5 .   ? 66.292 32.682 114.288 1.00 25.89 ? 2056 HOH A O   1 
HETATM 2627 O  O   . HOH S 5 .   ? 52.849 33.406 118.492 1.00 33.45 ? 2057 HOH A O   1 
HETATM 2628 O  O   . HOH S 5 .   ? 56.442 35.249 118.352 1.00 28.89 ? 2058 HOH A O   1 
HETATM 2629 O  O   . HOH S 5 .   ? 59.332 33.793 126.661 1.00 37.65 ? 2059 HOH A O   1 
HETATM 2630 O  O   . HOH S 5 .   ? 46.526 37.510 114.770 1.00 35.71 ? 2060 HOH A O   1 
HETATM 2631 O  O   . HOH S 5 .   ? 54.832 34.703 109.520 1.00 17.56 ? 2061 HOH A O   1 
HETATM 2632 O  O   . HOH S 5 .   ? 45.873 28.448 97.477  1.00 25.98 ? 2062 HOH A O   1 
HETATM 2633 O  O   . HOH T 5 .   ? 52.106 25.451 162.757 1.00 26.05 ? 2001 HOH B O   1 
HETATM 2634 O  O   . HOH T 5 .   ? 51.102 26.318 167.875 1.00 28.44 ? 2002 HOH B O   1 
HETATM 2635 O  O   . HOH T 5 .   ? 47.734 34.009 159.841 1.00 57.14 ? 2003 HOH B O   1 
HETATM 2636 O  O   . HOH T 5 .   ? 60.317 27.514 146.861 1.00 50.28 ? 2004 HOH B O   1 
HETATM 2637 O  O   . HOH T 5 .   ? 61.472 23.563 144.309 1.00 18.90 ? 2005 HOH B O   1 
HETATM 2638 O  O   . HOH T 5 .   ? 66.399 14.925 149.889 1.00 36.21 ? 2006 HOH B O   1 
HETATM 2639 O  O   . HOH T 5 .   ? 64.850 17.232 147.313 1.00 21.84 ? 2007 HOH B O   1 
HETATM 2640 O  O   . HOH T 5 .   ? 60.964 7.915  148.510 1.00 28.43 ? 2008 HOH B O   1 
HETATM 2641 O  O   . HOH T 5 .   ? 61.356 7.072  144.041 1.00 52.29 ? 2009 HOH B O   1 
HETATM 2642 O  O   . HOH T 5 .   ? 62.401 12.111 136.745 1.00 22.15 ? 2010 HOH B O   1 
HETATM 2643 O  O   . HOH T 5 .   ? 56.086 6.461  135.385 1.00 47.82 ? 2011 HOH B O   1 
HETATM 2644 O  O   . HOH T 5 .   ? 66.979 17.779 135.834 1.00 30.64 ? 2012 HOH B O   1 
HETATM 2645 O  O   . HOH T 5 .   ? 64.533 23.652 138.613 1.00 23.45 ? 2013 HOH B O   1 
HETATM 2646 O  O   . HOH T 5 .   ? 60.935 29.269 136.385 1.00 24.27 ? 2014 HOH B O   1 
HETATM 2647 O  O   . HOH T 5 .   ? 58.300 23.513 135.522 1.00 22.04 ? 2015 HOH B O   1 
HETATM 2648 O  O   . HOH T 5 .   ? 58.245 29.246 145.388 1.00 26.64 ? 2016 HOH B O   1 
HETATM 2649 O  O   . HOH T 5 .   ? 53.514 30.754 139.864 1.00 31.81 ? 2017 HOH B O   1 
HETATM 2650 O  O   . HOH T 5 .   ? 53.453 29.741 136.903 1.00 25.90 ? 2018 HOH B O   1 
HETATM 2651 O  O   . HOH T 5 .   ? 48.564 34.049 142.813 1.00 37.03 ? 2019 HOH B O   1 
HETATM 2652 O  O   . HOH T 5 .   ? 56.949 31.429 147.112 1.00 30.39 ? 2020 HOH B O   1 
HETATM 2653 O  O   . HOH T 5 .   ? 52.273 39.562 147.763 1.00 51.12 ? 2021 HOH B O   1 
HETATM 2654 O  O   . HOH T 5 .   ? 54.579 35.721 151.192 1.00 51.01 ? 2022 HOH B O   1 
HETATM 2655 O  O   . HOH T 5 .   ? 58.105 32.269 149.264 1.00 23.65 ? 2023 HOH B O   1 
HETATM 2656 O  O   . HOH T 5 .   ? 59.625 29.594 154.497 1.00 17.76 ? 2024 HOH B O   1 
HETATM 2657 O  O   . HOH T 5 .   ? 63.745 27.746 148.959 1.00 20.88 ? 2025 HOH B O   1 
HETATM 2658 O  O   . HOH T 5 .   ? 63.912 24.339 144.017 1.00 19.40 ? 2026 HOH B O   1 
HETATM 2659 O  O   . HOH T 5 .   ? 63.774 19.112 148.870 1.00 12.98 ? 2027 HOH B O   1 
HETATM 2660 O  O   . HOH T 5 .   ? 65.313 13.049 157.092 1.00 26.96 ? 2028 HOH B O   1 
HETATM 2661 O  O   . HOH T 5 .   ? 60.965 22.491 159.169 1.00 36.88 ? 2029 HOH B O   1 
HETATM 2662 O  O   . HOH T 5 .   ? 56.540 16.675 157.926 1.00 22.67 ? 2030 HOH B O   1 
HETATM 2663 O  O   . HOH T 5 .   ? 66.201 11.386 155.250 1.00 48.24 ? 2031 HOH B O   1 
HETATM 2664 O  O   . HOH T 5 .   ? 54.530 9.056  154.663 1.00 34.56 ? 2032 HOH B O   1 
HETATM 2665 O  O   . HOH T 5 .   ? 55.037 3.104  145.929 1.00 22.70 ? 2033 HOH B O   1 
HETATM 2666 O  O   . HOH T 5 .   ? 53.996 0.840  145.922 1.00 34.76 ? 2034 HOH B O   1 
HETATM 2667 O  O   . HOH T 5 .   ? 56.078 0.717  148.547 1.00 47.62 ? 2035 HOH B O   1 
HETATM 2668 O  O   . HOH T 5 .   ? 53.679 7.411  152.678 1.00 24.59 ? 2036 HOH B O   1 
HETATM 2669 O  O   . HOH T 5 .   ? 49.724 1.457  152.163 1.00 31.25 ? 2037 HOH B O   1 
HETATM 2670 O  O   . HOH T 5 .   ? 49.326 3.982  150.548 1.00 24.48 ? 2038 HOH B O   1 
HETATM 2671 O  O   . HOH T 5 .   ? 46.202 0.833  136.125 1.00 47.74 ? 2039 HOH B O   1 
HETATM 2672 O  O   . HOH T 5 .   ? 38.602 9.525  136.215 1.00 34.41 ? 2040 HOH B O   1 
HETATM 2673 O  O   . HOH T 5 .   ? 54.023 18.711 159.706 1.00 18.27 ? 2041 HOH B O   1 
HETATM 2674 O  O   . HOH T 5 .   ? 55.863 15.629 163.760 1.00 28.09 ? 2042 HOH B O   1 
HETATM 2675 O  O   . HOH T 5 .   ? 52.591 10.981 161.536 1.00 34.69 ? 2043 HOH B O   1 
HETATM 2676 O  O   . HOH T 5 .   ? 55.862 13.242 157.045 1.00 22.19 ? 2044 HOH B O   1 
HETATM 2677 O  O   . HOH T 5 .   ? 54.340 11.753 153.786 1.00 25.99 ? 2045 HOH B O   1 
HETATM 2678 O  O   . HOH T 5 .   ? 48.871 4.037  141.580 1.00 13.61 ? 2046 HOH B O   1 
HETATM 2679 O  O   . HOH T 5 .   ? 47.215 9.463  133.451 1.00 38.63 ? 2047 HOH B O   1 
HETATM 2680 O  O   . HOH T 5 .   ? 47.008 25.477 120.702 1.00 23.76 ? 2048 HOH B O   1 
HETATM 2681 O  O   . HOH T 5 .   ? 50.264 24.639 126.956 1.00 19.43 ? 2049 HOH B O   1 
HETATM 2682 O  O   . HOH T 5 .   ? 46.668 19.140 128.889 1.00 23.88 ? 2050 HOH B O   1 
HETATM 2683 O  O   . HOH T 5 .   ? 45.122 15.259 128.545 1.00 36.82 ? 2051 HOH B O   1 
HETATM 2684 O  O   . HOH T 5 .   ? 51.570 16.588 127.129 1.00 18.01 ? 2052 HOH B O   1 
HETATM 2685 O  O   . HOH T 5 .   ? 45.451 12.416 128.248 1.00 32.22 ? 2053 HOH B O   1 
HETATM 2686 O  O   . HOH T 5 .   ? 40.064 12.132 132.917 1.00 45.44 ? 2054 HOH B O   1 
HETATM 2687 O  O   . HOH T 5 .   ? 50.540 23.541 133.215 1.00 2.46  ? 2055 HOH B O   1 
HETATM 2688 O  O   . HOH T 5 .   ? 45.448 17.802 130.938 1.00 37.87 ? 2056 HOH B O   1 
HETATM 2689 O  O   . HOH T 5 .   ? 32.586 28.259 147.755 1.00 53.44 ? 2057 HOH B O   1 
HETATM 2690 O  O   . HOH T 5 .   ? 45.079 38.240 157.288 1.00 46.25 ? 2058 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   106 ?   ?   ?   A . n 
A 1 2   PHE 2   107 ?   ?   ?   A . n 
A 1 3   GLN 3   108 ?   ?   ?   A . n 
A 1 4   THR 4   109 ?   ?   ?   A . n 
A 1 5   PHE 5   110 110 PHE PHE A . n 
A 1 6   GLU 6   111 111 GLU GLU A . n 
A 1 7   GLY 7   112 112 GLY GLY A . n 
A 1 8   ASP 8   113 113 ASP ASP A . n 
A 1 9   LEU 9   114 114 LEU LEU A . n 
A 1 10  LYS 10  115 115 LYS LYS A . n 
A 1 11  TRP 11  116 116 TRP TRP A . n 
A 1 12  HIS 12  117 117 HIS HIS A . n 
A 1 13  HIS 13  118 118 HIS HIS A . n 
A 1 14  HIS 14  119 119 HIS HIS A . n 
A 1 15  ASN 15  120 120 ASN ASN A . n 
A 1 16  ILE 16  121 121 ILE ILE A . n 
A 1 17  THR 17  122 122 THR THR A . n 
A 1 18  TYR 18  123 123 TYR TYR A . n 
A 1 19  TRP 19  124 124 TRP TRP A . n 
A 1 20  ILE 20  125 125 ILE ILE A . n 
A 1 21  GLN 21  126 126 GLN GLN A . n 
A 1 22  ASN 22  127 127 ASN ASN A . n 
A 1 23  TYR 23  128 128 TYR TYR A . n 
A 1 24  SER 24  129 129 SER SER A . n 
A 1 25  GLU 25  130 130 GLU GLU A . n 
A 1 26  ASP 26  131 131 ASP ASP A . n 
A 1 27  LEU 27  132 132 LEU LEU A . n 
A 1 28  PRO 28  133 133 PRO PRO A . n 
A 1 29  ARG 29  134 134 ARG ARG A . n 
A 1 30  ALA 30  135 135 ALA ALA A . n 
A 1 31  VAL 31  136 136 VAL VAL A . n 
A 1 32  ILE 32  137 137 ILE ILE A . n 
A 1 33  ASP 33  138 138 ASP ASP A . n 
A 1 34  ASP 34  139 139 ASP ASP A . n 
A 1 35  ALA 35  140 140 ALA ALA A . n 
A 1 36  PHE 36  141 141 PHE PHE A . n 
A 1 37  ALA 37  142 142 ALA ALA A . n 
A 1 38  ARG 38  143 143 ARG ARG A . n 
A 1 39  ALA 39  144 144 ALA ALA A . n 
A 1 40  PHE 40  145 145 PHE PHE A . n 
A 1 41  ALA 41  146 146 ALA ALA A . n 
A 1 42  LEU 42  147 147 LEU LEU A . n 
A 1 43  TRP 43  148 148 TRP TRP A . n 
A 1 44  SER 44  149 149 SER SER A . n 
A 1 45  ALA 45  150 150 ALA ALA A . n 
A 1 46  VAL 46  151 151 VAL VAL A . n 
A 1 47  THR 47  152 152 THR THR A . n 
A 1 48  PRO 48  153 153 PRO PRO A . n 
A 1 49  LEU 49  154 154 LEU LEU A . n 
A 1 50  THR 50  155 155 THR THR A . n 
A 1 51  PHE 51  156 156 PHE PHE A . n 
A 1 52  THR 52  157 157 THR THR A . n 
A 1 53  ARG 53  158 158 ARG ARG A . n 
A 1 54  VAL 54  159 159 VAL VAL A . n 
A 1 55  TYR 55  160 160 TYR TYR A . n 
A 1 56  SER 56  161 161 SER SER A . n 
A 1 57  ARG 57  162 162 ARG ARG A . n 
A 1 58  ASP 58  163 163 ASP ASP A . n 
A 1 59  ALA 59  164 164 ALA ALA A . n 
A 1 60  ASP 60  165 165 ASP ASP A . n 
A 1 61  ILE 61  166 166 ILE ILE A . n 
A 1 62  VAL 62  167 167 VAL VAL A . n 
A 1 63  ILE 63  168 168 ILE ILE A . n 
A 1 64  GLN 64  169 169 GLN GLN A . n 
A 1 65  PHE 65  170 170 PHE PHE A . n 
A 1 66  GLY 66  171 171 GLY GLY A . n 
A 1 67  VAL 67  172 172 VAL VAL A . n 
A 1 68  ALA 68  173 173 ALA ALA A . n 
A 1 69  GLU 69  174 174 GLU GLU A . n 
A 1 70  HIS 70  175 175 HIS HIS A . n 
A 1 71  GLY 71  176 176 GLY GLY A . n 
A 1 72  ASP 72  177 177 ASP ASP A . n 
A 1 73  GLY 73  178 178 GLY GLY A . n 
A 1 74  TYR 74  179 179 TYR TYR A . n 
A 1 75  PRO 75  180 180 PRO PRO A . n 
A 1 76  PHE 76  181 181 PHE PHE A . n 
A 1 77  ASP 77  182 182 ASP ASP A . n 
A 1 78  GLY 78  183 183 GLY GLY A . n 
A 1 79  LYS 79  184 184 LYS LYS A . n 
A 1 80  ASP 80  185 185 ASP ASP A . n 
A 1 81  GLY 81  186 186 GLY GLY A . n 
A 1 82  LEU 82  187 187 LEU LEU A . n 
A 1 83  LEU 83  188 188 LEU LEU A . n 
A 1 84  ALA 84  189 189 ALA ALA A . n 
A 1 85  HIS 85  190 190 HIS HIS A . n 
A 1 86  ALA 86  191 191 ALA ALA A . n 
A 1 87  PHE 87  192 192 PHE PHE A . n 
A 1 88  PRO 88  193 193 PRO PRO A . n 
A 1 89  PRO 89  194 194 PRO PRO A . n 
A 1 90  GLY 90  195 195 GLY GLY A . n 
A 1 91  PRO 91  196 196 PRO PRO A . n 
A 1 92  GLY 92  197 197 GLY GLY A . n 
A 1 93  ILE 93  198 198 ILE ILE A . n 
A 1 94  GLN 94  199 199 GLN GLN A . n 
A 1 95  GLY 95  200 200 GLY GLY A . n 
A 1 96  ASP 96  201 201 ASP ASP A . n 
A 1 97  ALA 97  202 202 ALA ALA A . n 
A 1 98  HIS 98  203 203 HIS HIS A . n 
A 1 99  PHE 99  204 204 PHE PHE A . n 
A 1 100 ASP 100 205 205 ASP ASP A . n 
A 1 101 ASP 101 206 206 ASP ASP A . n 
A 1 102 ASP 102 207 207 ASP ASP A . n 
A 1 103 GLU 103 208 208 GLU GLU A . n 
A 1 104 LEU 104 209 209 LEU LEU A . n 
A 1 105 TRP 105 210 210 TRP TRP A . n 
A 1 106 SER 106 211 211 SER SER A . n 
A 1 107 LEU 107 212 212 LEU LEU A . n 
A 1 108 GLY 108 213 213 GLY GLY A . n 
A 1 109 LYS 109 214 214 LYS LYS A . n 
A 1 110 GLY 110 215 215 GLY GLY A . n 
A 1 111 GLN 111 391 391 GLN GLN A . n 
A 1 112 GLY 112 392 392 GLY GLY A . n 
A 1 113 TYR 113 393 393 TYR TYR A . n 
A 1 114 SER 114 394 394 SER SER A . n 
A 1 115 LEU 115 395 395 LEU LEU A . n 
A 1 116 PHE 116 396 396 PHE PHE A . n 
A 1 117 LEU 117 397 397 LEU LEU A . n 
A 1 118 VAL 118 398 398 VAL VAL A . n 
A 1 119 ALA 119 399 399 ALA ALA A . n 
A 1 120 ALA 120 400 400 ALA ALA A . n 
A 1 121 HIS 121 401 401 HIS HIS A . n 
A 1 122 GLU 122 402 402 GLU GLU A . n 
A 1 123 PHE 123 403 403 PHE PHE A . n 
A 1 124 GLY 124 404 404 GLY GLY A . n 
A 1 125 HIS 125 405 405 HIS HIS A . n 
A 1 126 ALA 126 406 406 ALA ALA A . n 
A 1 127 LEU 127 407 407 LEU LEU A . n 
A 1 128 GLY 128 408 408 GLY GLY A . n 
A 1 129 LEU 129 409 409 LEU LEU A . n 
A 1 130 ASP 130 410 410 ASP ASP A . n 
A 1 131 HIS 131 411 411 HIS HIS A . n 
A 1 132 SER 132 412 412 SER SER A . n 
A 1 133 SER 133 413 413 SER SER A . n 
A 1 134 VAL 134 414 414 VAL VAL A . n 
A 1 135 PRO 135 415 415 PRO PRO A . n 
A 1 136 GLU 136 416 416 GLU GLU A . n 
A 1 137 ALA 137 417 417 ALA ALA A . n 
A 1 138 LEU 138 418 418 LEU LEU A . n 
A 1 139 MET 139 419 419 MET MET A . n 
A 1 140 TYR 140 420 420 TYR TYR A . n 
A 1 141 PRO 141 421 421 PRO PRO A . n 
A 1 142 MET 142 422 422 MET MET A . n 
A 1 143 TYR 143 423 423 TYR TYR A . n 
A 1 144 ARG 144 424 424 ARG ARG A . n 
A 1 145 PHE 145 425 425 PHE PHE A . n 
A 1 146 THR 146 426 426 THR THR A . n 
A 1 147 GLU 147 427 427 GLU GLU A . n 
A 1 148 GLY 148 428 428 GLY GLY A . n 
A 1 149 PRO 149 429 429 PRO PRO A . n 
A 1 150 PRO 150 430 430 PRO PRO A . n 
A 1 151 LEU 151 431 431 LEU LEU A . n 
A 1 152 HIS 152 432 432 HIS HIS A . n 
A 1 153 LYS 153 433 433 LYS LYS A . n 
A 1 154 ASP 154 434 434 ASP ASP A . n 
A 1 155 ASP 155 435 435 ASP ASP A . n 
A 1 156 VAL 156 436 436 VAL VAL A . n 
A 1 157 ASN 157 437 437 ASN ASN A . n 
A 1 158 GLY 158 438 438 GLY GLY A . n 
A 1 159 ILE 159 439 439 ILE ILE A . n 
A 1 160 ARG 160 440 440 ARG ARG A . n 
A 1 161 HIS 161 441 441 HIS HIS A . n 
A 1 162 LEU 162 442 442 LEU LEU A . n 
A 1 163 TYR 163 443 443 TYR TYR A . n 
B 1 1   MET 1   106 ?   ?   ?   B . n 
B 1 2   PHE 2   107 ?   ?   ?   B . n 
B 1 3   GLN 3   108 ?   ?   ?   B . n 
B 1 4   THR 4   109 ?   ?   ?   B . n 
B 1 5   PHE 5   110 ?   ?   ?   B . n 
B 1 6   GLU 6   111 ?   ?   ?   B . n 
B 1 7   GLY 7   112 ?   ?   ?   B . n 
B 1 8   ASP 8   113 113 ASP ASP B . n 
B 1 9   LEU 9   114 114 LEU LEU B . n 
B 1 10  LYS 10  115 115 LYS LYS B . n 
B 1 11  TRP 11  116 116 TRP TRP B . n 
B 1 12  HIS 12  117 117 HIS HIS B . n 
B 1 13  HIS 13  118 118 HIS HIS B . n 
B 1 14  HIS 14  119 119 HIS HIS B . n 
B 1 15  ASN 15  120 120 ASN ASN B . n 
B 1 16  ILE 16  121 121 ILE ILE B . n 
B 1 17  THR 17  122 122 THR THR B . n 
B 1 18  TYR 18  123 123 TYR TYR B . n 
B 1 19  TRP 19  124 124 TRP TRP B . n 
B 1 20  ILE 20  125 125 ILE ILE B . n 
B 1 21  GLN 21  126 126 GLN GLN B . n 
B 1 22  ASN 22  127 127 ASN ASN B . n 
B 1 23  TYR 23  128 128 TYR TYR B . n 
B 1 24  SER 24  129 129 SER SER B . n 
B 1 25  GLU 25  130 130 GLU GLU B . n 
B 1 26  ASP 26  131 131 ASP ASP B . n 
B 1 27  LEU 27  132 132 LEU LEU B . n 
B 1 28  PRO 28  133 133 PRO PRO B . n 
B 1 29  ARG 29  134 134 ARG ARG B . n 
B 1 30  ALA 30  135 135 ALA ALA B . n 
B 1 31  VAL 31  136 136 VAL VAL B . n 
B 1 32  ILE 32  137 137 ILE ILE B . n 
B 1 33  ASP 33  138 138 ASP ASP B . n 
B 1 34  ASP 34  139 139 ASP ASP B . n 
B 1 35  ALA 35  140 140 ALA ALA B . n 
B 1 36  PHE 36  141 141 PHE PHE B . n 
B 1 37  ALA 37  142 142 ALA ALA B . n 
B 1 38  ARG 38  143 143 ARG ARG B . n 
B 1 39  ALA 39  144 144 ALA ALA B . n 
B 1 40  PHE 40  145 145 PHE PHE B . n 
B 1 41  ALA 41  146 146 ALA ALA B . n 
B 1 42  LEU 42  147 147 LEU LEU B . n 
B 1 43  TRP 43  148 148 TRP TRP B . n 
B 1 44  SER 44  149 149 SER SER B . n 
B 1 45  ALA 45  150 150 ALA ALA B . n 
B 1 46  VAL 46  151 151 VAL VAL B . n 
B 1 47  THR 47  152 152 THR THR B . n 
B 1 48  PRO 48  153 153 PRO PRO B . n 
B 1 49  LEU 49  154 154 LEU LEU B . n 
B 1 50  THR 50  155 155 THR THR B . n 
B 1 51  PHE 51  156 156 PHE PHE B . n 
B 1 52  THR 52  157 157 THR THR B . n 
B 1 53  ARG 53  158 158 ARG ARG B . n 
B 1 54  VAL 54  159 159 VAL VAL B . n 
B 1 55  TYR 55  160 160 TYR TYR B . n 
B 1 56  SER 56  161 161 SER SER B . n 
B 1 57  ARG 57  162 162 ARG ARG B . n 
B 1 58  ASP 58  163 163 ASP ASP B . n 
B 1 59  ALA 59  164 164 ALA ALA B . n 
B 1 60  ASP 60  165 165 ASP ASP B . n 
B 1 61  ILE 61  166 166 ILE ILE B . n 
B 1 62  VAL 62  167 167 VAL VAL B . n 
B 1 63  ILE 63  168 168 ILE ILE B . n 
B 1 64  GLN 64  169 169 GLN GLN B . n 
B 1 65  PHE 65  170 170 PHE PHE B . n 
B 1 66  GLY 66  171 171 GLY GLY B . n 
B 1 67  VAL 67  172 172 VAL VAL B . n 
B 1 68  ALA 68  173 173 ALA ALA B . n 
B 1 69  GLU 69  174 174 GLU GLU B . n 
B 1 70  HIS 70  175 175 HIS HIS B . n 
B 1 71  GLY 71  176 176 GLY GLY B . n 
B 1 72  ASP 72  177 177 ASP ASP B . n 
B 1 73  GLY 73  178 178 GLY GLY B . n 
B 1 74  TYR 74  179 179 TYR TYR B . n 
B 1 75  PRO 75  180 180 PRO PRO B . n 
B 1 76  PHE 76  181 181 PHE PHE B . n 
B 1 77  ASP 77  182 182 ASP ASP B . n 
B 1 78  GLY 78  183 183 GLY GLY B . n 
B 1 79  LYS 79  184 184 LYS LYS B . n 
B 1 80  ASP 80  185 185 ASP ASP B . n 
B 1 81  GLY 81  186 186 GLY GLY B . n 
B 1 82  LEU 82  187 187 LEU LEU B . n 
B 1 83  LEU 83  188 188 LEU LEU B . n 
B 1 84  ALA 84  189 189 ALA ALA B . n 
B 1 85  HIS 85  190 190 HIS HIS B . n 
B 1 86  ALA 86  191 191 ALA ALA B . n 
B 1 87  PHE 87  192 192 PHE PHE B . n 
B 1 88  PRO 88  193 193 PRO PRO B . n 
B 1 89  PRO 89  194 194 PRO PRO B . n 
B 1 90  GLY 90  195 195 GLY GLY B . n 
B 1 91  PRO 91  196 196 PRO PRO B . n 
B 1 92  GLY 92  197 197 GLY GLY B . n 
B 1 93  ILE 93  198 198 ILE ILE B . n 
B 1 94  GLN 94  199 199 GLN GLN B . n 
B 1 95  GLY 95  200 200 GLY GLY B . n 
B 1 96  ASP 96  201 201 ASP ASP B . n 
B 1 97  ALA 97  202 202 ALA ALA B . n 
B 1 98  HIS 98  203 203 HIS HIS B . n 
B 1 99  PHE 99  204 204 PHE PHE B . n 
B 1 100 ASP 100 205 205 ASP ASP B . n 
B 1 101 ASP 101 206 206 ASP ASP B . n 
B 1 102 ASP 102 207 207 ASP ASP B . n 
B 1 103 GLU 103 208 208 GLU GLU B . n 
B 1 104 LEU 104 209 209 LEU LEU B . n 
B 1 105 TRP 105 210 210 TRP TRP B . n 
B 1 106 SER 106 211 211 SER SER B . n 
B 1 107 LEU 107 212 212 LEU LEU B . n 
B 1 108 GLY 108 213 213 GLY GLY B . n 
B 1 109 LYS 109 214 214 LYS LYS B . n 
B 1 110 GLY 110 215 215 GLY GLY B . n 
B 1 111 GLN 111 391 391 GLN GLN B . n 
B 1 112 GLY 112 392 392 GLY GLY B . n 
B 1 113 TYR 113 393 393 TYR TYR B . n 
B 1 114 SER 114 394 394 SER SER B . n 
B 1 115 LEU 115 395 395 LEU LEU B . n 
B 1 116 PHE 116 396 396 PHE PHE B . n 
B 1 117 LEU 117 397 397 LEU LEU B . n 
B 1 118 VAL 118 398 398 VAL VAL B . n 
B 1 119 ALA 119 399 399 ALA ALA B . n 
B 1 120 ALA 120 400 400 ALA ALA B . n 
B 1 121 HIS 121 401 401 HIS HIS B . n 
B 1 122 GLU 122 402 402 GLU GLU B . n 
B 1 123 PHE 123 403 403 PHE PHE B . n 
B 1 124 GLY 124 404 404 GLY GLY B . n 
B 1 125 HIS 125 405 405 HIS HIS B . n 
B 1 126 ALA 126 406 406 ALA ALA B . n 
B 1 127 LEU 127 407 407 LEU LEU B . n 
B 1 128 GLY 128 408 408 GLY GLY B . n 
B 1 129 LEU 129 409 409 LEU LEU B . n 
B 1 130 ASP 130 410 410 ASP ASP B . n 
B 1 131 HIS 131 411 411 HIS HIS B . n 
B 1 132 SER 132 412 412 SER SER B . n 
B 1 133 SER 133 413 413 SER SER B . n 
B 1 134 VAL 134 414 414 VAL VAL B . n 
B 1 135 PRO 135 415 415 PRO PRO B . n 
B 1 136 GLU 136 416 416 GLU GLU B . n 
B 1 137 ALA 137 417 417 ALA ALA B . n 
B 1 138 LEU 138 418 418 LEU LEU B . n 
B 1 139 MET 139 419 419 MET MET B . n 
B 1 140 TYR 140 420 420 TYR TYR B . n 
B 1 141 PRO 141 421 421 PRO PRO B . n 
B 1 142 MET 142 422 422 MET MET B . n 
B 1 143 TYR 143 423 423 TYR TYR B . n 
B 1 144 ARG 144 424 424 ARG ARG B . n 
B 1 145 PHE 145 425 425 PHE PHE B . n 
B 1 146 THR 146 426 426 THR THR B . n 
B 1 147 GLU 147 427 427 GLU GLU B . n 
B 1 148 GLY 148 428 428 GLY GLY B . n 
B 1 149 PRO 149 429 429 PRO PRO B . n 
B 1 150 PRO 150 430 430 PRO PRO B . n 
B 1 151 LEU 151 431 431 LEU LEU B . n 
B 1 152 HIS 152 432 432 HIS HIS B . n 
B 1 153 LYS 153 433 433 LYS LYS B . n 
B 1 154 ASP 154 434 434 ASP ASP B . n 
B 1 155 ASP 155 435 435 ASP ASP B . n 
B 1 156 VAL 156 436 436 VAL VAL B . n 
B 1 157 ASN 157 437 437 ASN ASN B . n 
B 1 158 GLY 158 438 438 GLY GLY B . n 
B 1 159 ILE 159 439 439 ILE ILE B . n 
B 1 160 ARG 160 440 440 ARG ARG B . n 
B 1 161 HIS 161 441 441 HIS HIS B . n 
B 1 162 LEU 162 442 442 LEU LEU B . n 
B 1 163 TYR 163 443 443 TYR TYR B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CA  1  1444 1444 CA  CA  A . 
D 2 CA  1  1445 1445 CA  CA  A . 
E 2 CA  1  1446 1446 CA  CA  A . 
F 2 CA  1  1447 1447 CA  CA  A . 
G 3 NFH 1  1448 1448 NFH NFH A . 
H 4 ZN  1  1450 1450 ZN  ZN  A . 
I 4 ZN  1  1451 1451 ZN  ZN  A . 
J 2 CA  1  1452 1452 CA  CA  A . 
K 2 CA  1  1444 1444 CA  CA  B . 
L 2 CA  1  1445 1445 CA  CA  B . 
M 2 CA  1  1446 1446 CA  CA  B . 
N 2 CA  1  1447 1447 CA  CA  B . 
O 2 CA  1  1448 1448 CA  CA  B . 
P 3 NFH 1  1449 1449 NFH NFH B . 
Q 4 ZN  1  1451 1451 ZN  ZN  B . 
R 4 ZN  1  1452 1452 ZN  ZN  B . 
S 5 HOH 1  2001 2001 HOH HOH A . 
S 5 HOH 2  2002 2002 HOH HOH A . 
S 5 HOH 3  2003 2003 HOH HOH A . 
S 5 HOH 4  2004 2004 HOH HOH A . 
S 5 HOH 5  2005 2005 HOH HOH A . 
S 5 HOH 6  2006 2006 HOH HOH A . 
S 5 HOH 7  2007 2007 HOH HOH A . 
S 5 HOH 8  2008 2008 HOH HOH A . 
S 5 HOH 9  2009 2009 HOH HOH A . 
S 5 HOH 10 2010 2010 HOH HOH A . 
S 5 HOH 11 2011 2011 HOH HOH A . 
S 5 HOH 12 2012 2012 HOH HOH A . 
S 5 HOH 13 2013 2013 HOH HOH A . 
S 5 HOH 14 2014 2014 HOH HOH A . 
S 5 HOH 15 2015 2015 HOH HOH A . 
S 5 HOH 16 2016 2016 HOH HOH A . 
S 5 HOH 17 2017 2017 HOH HOH A . 
S 5 HOH 18 2018 2018 HOH HOH A . 
S 5 HOH 19 2019 2019 HOH HOH A . 
S 5 HOH 20 2020 2020 HOH HOH A . 
S 5 HOH 21 2021 2021 HOH HOH A . 
S 5 HOH 22 2022 2022 HOH HOH A . 
S 5 HOH 23 2023 2023 HOH HOH A . 
S 5 HOH 24 2024 2024 HOH HOH A . 
S 5 HOH 25 2025 2025 HOH HOH A . 
S 5 HOH 26 2026 2026 HOH HOH A . 
S 5 HOH 27 2027 2027 HOH HOH A . 
S 5 HOH 28 2028 2028 HOH HOH A . 
S 5 HOH 29 2029 2029 HOH HOH A . 
S 5 HOH 30 2030 2030 HOH HOH A . 
S 5 HOH 31 2031 2031 HOH HOH A . 
S 5 HOH 32 2032 2032 HOH HOH A . 
S 5 HOH 33 2033 2033 HOH HOH A . 
S 5 HOH 34 2034 2034 HOH HOH A . 
S 5 HOH 35 2035 2035 HOH HOH A . 
S 5 HOH 36 2036 2036 HOH HOH A . 
S 5 HOH 37 2037 2037 HOH HOH A . 
S 5 HOH 38 2038 2038 HOH HOH A . 
S 5 HOH 39 2039 2039 HOH HOH A . 
S 5 HOH 40 2040 2040 HOH HOH A . 
S 5 HOH 41 2041 2041 HOH HOH A . 
S 5 HOH 42 2042 2042 HOH HOH A . 
S 5 HOH 43 2043 2043 HOH HOH A . 
S 5 HOH 44 2044 2044 HOH HOH A . 
S 5 HOH 45 2045 2045 HOH HOH A . 
S 5 HOH 46 2046 2046 HOH HOH A . 
S 5 HOH 47 2047 2047 HOH HOH A . 
S 5 HOH 48 2048 2048 HOH HOH A . 
S 5 HOH 49 2049 2049 HOH HOH A . 
S 5 HOH 50 2050 2050 HOH HOH A . 
S 5 HOH 51 2051 2051 HOH HOH A . 
S 5 HOH 52 2052 2052 HOH HOH A . 
S 5 HOH 53 2053 2053 HOH HOH A . 
S 5 HOH 54 2054 2054 HOH HOH A . 
S 5 HOH 55 2055 2055 HOH HOH A . 
S 5 HOH 56 2056 2056 HOH HOH A . 
S 5 HOH 57 2057 2057 HOH HOH A . 
S 5 HOH 58 2058 2058 HOH HOH A . 
S 5 HOH 59 2059 2059 HOH HOH A . 
S 5 HOH 60 2060 2060 HOH HOH A . 
S 5 HOH 61 2061 2061 HOH HOH A . 
S 5 HOH 62 2062 2062 HOH HOH A . 
T 5 HOH 1  2001 2001 HOH HOH B . 
T 5 HOH 2  2002 2002 HOH HOH B . 
T 5 HOH 3  2003 2003 HOH HOH B . 
T 5 HOH 4  2004 2004 HOH HOH B . 
T 5 HOH 5  2005 2005 HOH HOH B . 
T 5 HOH 6  2006 2006 HOH HOH B . 
T 5 HOH 7  2007 2007 HOH HOH B . 
T 5 HOH 8  2008 2008 HOH HOH B . 
T 5 HOH 9  2009 2009 HOH HOH B . 
T 5 HOH 10 2010 2010 HOH HOH B . 
T 5 HOH 11 2011 2011 HOH HOH B . 
T 5 HOH 12 2012 2012 HOH HOH B . 
T 5 HOH 13 2013 2013 HOH HOH B . 
T 5 HOH 14 2014 2014 HOH HOH B . 
T 5 HOH 15 2015 2015 HOH HOH B . 
T 5 HOH 16 2016 2016 HOH HOH B . 
T 5 HOH 17 2017 2017 HOH HOH B . 
T 5 HOH 18 2018 2018 HOH HOH B . 
T 5 HOH 19 2019 2019 HOH HOH B . 
T 5 HOH 20 2020 2020 HOH HOH B . 
T 5 HOH 21 2021 2021 HOH HOH B . 
T 5 HOH 22 2022 2022 HOH HOH B . 
T 5 HOH 23 2023 2023 HOH HOH B . 
T 5 HOH 24 2024 2024 HOH HOH B . 
T 5 HOH 25 2025 2025 HOH HOH B . 
T 5 HOH 26 2026 2026 HOH HOH B . 
T 5 HOH 27 2027 2027 HOH HOH B . 
T 5 HOH 28 2028 2028 HOH HOH B . 
T 5 HOH 29 2029 2029 HOH HOH B . 
T 5 HOH 30 2030 2030 HOH HOH B . 
T 5 HOH 31 2031 2031 HOH HOH B . 
T 5 HOH 32 2032 2032 HOH HOH B . 
T 5 HOH 33 2033 2033 HOH HOH B . 
T 5 HOH 34 2034 2034 HOH HOH B . 
T 5 HOH 35 2035 2035 HOH HOH B . 
T 5 HOH 36 2036 2036 HOH HOH B . 
T 5 HOH 37 2037 2037 HOH HOH B . 
T 5 HOH 38 2038 2038 HOH HOH B . 
T 5 HOH 39 2039 2039 HOH HOH B . 
T 5 HOH 40 2040 2040 HOH HOH B . 
T 5 HOH 41 2041 2041 HOH HOH B . 
T 5 HOH 42 2042 2042 HOH HOH B . 
T 5 HOH 43 2043 2043 HOH HOH B . 
T 5 HOH 44 2044 2044 HOH HOH B . 
T 5 HOH 45 2045 2045 HOH HOH B . 
T 5 HOH 46 2046 2046 HOH HOH B . 
T 5 HOH 47 2047 2047 HOH HOH B . 
T 5 HOH 48 2048 2048 HOH HOH B . 
T 5 HOH 49 2049 2049 HOH HOH B . 
T 5 HOH 50 2050 2050 HOH HOH B . 
T 5 HOH 51 2051 2051 HOH HOH B . 
T 5 HOH 52 2052 2052 HOH HOH B . 
T 5 HOH 53 2053 2053 HOH HOH B . 
T 5 HOH 54 2054 2054 HOH HOH B . 
T 5 HOH 55 2055 2055 HOH HOH B . 
T 5 HOH 56 2056 2056 HOH HOH B . 
T 5 HOH 57 2057 2057 HOH HOH B . 
T 5 HOH 58 2058 2058 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PQS monomeric 1 
2 author_and_software_defined_assembly PQS monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,S 
2 1 B,K,L,M,N,O,P,Q,R,T 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 OD2 ? A ASP 26  ? A ASP 131  ? 1_555 43.8  ? 
2   OD1 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A ASP 101 ? A ASP 206  ? 1_555 153.8 ? 
3   OD2 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A ASP 101 ? A ASP 206  ? 1_555 161.9 ? 
4   OD1 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 OD1 ? A ASP 101 ? A ASP 206  ? 1_555 109.4 ? 
5   OD2 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 OD1 ? A ASP 101 ? A ASP 206  ? 1_555 98.9  ? 
6   O   ? A ASP 101 ? A ASP 206  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 OD1 ? A ASP 101 ? A ASP 206  ? 1_555 72.7  ? 
7   OD1 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A GLU 103 ? A GLU 208  ? 1_555 113.3 ? 
8   OD2 ? A ASP 26  ? A ASP 131  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A GLU 103 ? A GLU 208  ? 1_555 78.0  ? 
9   O   ? A ASP 101 ? A ASP 206  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A GLU 103 ? A GLU 208  ? 1_555 89.5  ? 
10  OD1 ? A ASP 101 ? A ASP 206  ? 1_555 CA ? E CA . ? A CA 1446 ? 1_555 O   ? A GLU 103 ? A GLU 208  ? 1_555 108.7 ? 
11  O   ? A SER 44  ? A SER 149  ? 1_555 CA ? J CA . ? A CA 1452 ? 1_555 O   ? S HOH .   ? A HOH 2021 ? 1_555 72.3  ? 
12  O   ? A SER 44  ? A SER 149  ? 1_555 CA ? J CA . ? A CA 1452 ? 1_555 O   ? S HOH .   ? A HOH 2022 ? 1_555 54.7  ? 
13  O   ? S HOH .   ? A HOH 2021 ? 1_555 CA ? J CA . ? A CA 1452 ? 1_555 O   ? S HOH .   ? A HOH 2022 ? 1_555 87.6  ? 
14  O   ? A ASP 60  ? A ASP 165  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? A GLY 92  ? A GLY 197  ? 1_555 171.8 ? 
15  O   ? A ASP 60  ? A ASP 165  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? A GLN 94  ? A GLN 199  ? 1_555 96.0  ? 
16  O   ? A GLY 92  ? A GLY 197  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? A GLN 94  ? A GLN 199  ? 1_555 79.8  ? 
17  O   ? A ASP 60  ? A ASP 165  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 OD1 ? A ASP 96  ? A ASP 201  ? 1_555 88.2  ? 
18  O   ? A GLY 92  ? A GLY 197  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 OD1 ? A ASP 96  ? A ASP 201  ? 1_555 99.0  ? 
19  O   ? A GLN 94  ? A GLN 199  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 OD1 ? A ASP 96  ? A ASP 201  ? 1_555 92.7  ? 
20  O   ? A ASP 60  ? A ASP 165  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2028 ? 1_555 94.0  ? 
21  O   ? A GLY 92  ? A GLY 197  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2028 ? 1_555 89.1  ? 
22  O   ? A GLN 94  ? A GLN 199  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2028 ? 1_555 166.0 ? 
23  OD1 ? A ASP 96  ? A ASP 201  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2028 ? 1_555 97.5  ? 
24  O   ? A ASP 60  ? A ASP 165  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2039 ? 1_555 79.2  ? 
25  O   ? A GLY 92  ? A GLY 197  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2039 ? 1_555 92.8  ? 
26  O   ? A GLN 94  ? A GLN 199  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2039 ? 1_555 74.9  ? 
27  OD1 ? A ASP 96  ? A ASP 201  ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2039 ? 1_555 161.1 ? 
28  O   ? S HOH .   ? A HOH 2028 ? 1_555 CA ? D CA . ? A CA 1445 ? 1_555 O   ? S HOH .   ? A HOH 2039 ? 1_555 97.4  ? 
29  NE2 ? A HIS 70  ? A HIS 175  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 OD2 ? A ASP 72  ? A ASP 177  ? 1_555 102.3 ? 
30  NE2 ? A HIS 70  ? A HIS 175  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 NE2 ? A HIS 85  ? A HIS 190  ? 1_555 120.6 ? 
31  OD2 ? A ASP 72  ? A ASP 177  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 NE2 ? A HIS 85  ? A HIS 190  ? 1_555 119.2 ? 
32  NE2 ? A HIS 70  ? A HIS 175  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 ND1 ? A HIS 98  ? A HIS 203  ? 1_555 108.2 ? 
33  OD2 ? A ASP 72  ? A ASP 177  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 ND1 ? A HIS 98  ? A HIS 203  ? 1_555 88.0  ? 
34  NE2 ? A HIS 85  ? A HIS 190  ? 1_555 ZN ? I ZN . ? A ZN 1451 ? 1_555 ND1 ? A HIS 98  ? A HIS 203  ? 1_555 113.3 ? 
35  OD1 ? A ASP 77  ? A ASP 182  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A GLY 78  ? A GLY 183  ? 1_555 83.8  ? 
36  OD1 ? A ASP 77  ? A ASP 182  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A ASP 80  ? A ASP 185  ? 1_555 71.1  ? 
37  O   ? A GLY 78  ? A GLY 183  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A ASP 80  ? A ASP 185  ? 1_555 78.2  ? 
38  OD1 ? A ASP 77  ? A ASP 182  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A LEU 82  ? A LEU 187  ? 1_555 86.1  ? 
39  O   ? A GLY 78  ? A GLY 183  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A LEU 82  ? A LEU 187  ? 1_555 169.9 ? 
40  O   ? A ASP 80  ? A ASP 185  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 O   ? A LEU 82  ? A LEU 187  ? 1_555 98.0  ? 
41  OD1 ? A ASP 77  ? A ASP 182  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OD2 ? A ASP 100 ? A ASP 205  ? 1_555 95.3  ? 
42  O   ? A GLY 78  ? A GLY 183  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OD2 ? A ASP 100 ? A ASP 205  ? 1_555 82.7  ? 
43  O   ? A ASP 80  ? A ASP 185  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OD2 ? A ASP 100 ? A ASP 205  ? 1_555 157.6 ? 
44  O   ? A LEU 82  ? A LEU 187  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OD2 ? A ASP 100 ? A ASP 205  ? 1_555 98.7  ? 
45  OD1 ? A ASP 77  ? A ASP 182  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OE2 ? A GLU 103 ? A GLU 208  ? 1_555 146.1 ? 
46  O   ? A GLY 78  ? A GLY 183  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OE2 ? A GLU 103 ? A GLU 208  ? 1_555 108.7 ? 
47  O   ? A ASP 80  ? A ASP 185  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OE2 ? A GLU 103 ? A GLU 208  ? 1_555 80.6  ? 
48  O   ? A LEU 82  ? A LEU 187  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OE2 ? A GLU 103 ? A GLU 208  ? 1_555 79.6  ? 
49  OD2 ? A ASP 100 ? A ASP 205  ? 1_555 CA ? C CA . ? A CA 1444 ? 1_555 OE2 ? A GLU 103 ? A GLU 208  ? 1_555 117.0 ? 
50  OG  ? A SER 106 ? A SER 211  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A LEU 107 ? A LEU 212  ? 1_555 76.6  ? 
51  OG  ? A SER 106 ? A SER 211  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A GLY 108 ? A GLY 213  ? 1_555 134.1 ? 
52  O   ? A LEU 107 ? A LEU 212  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A GLY 108 ? A GLY 213  ? 1_555 71.1  ? 
53  OG  ? A SER 106 ? A SER 211  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A LYS 109 ? A LYS 214  ? 1_555 141.1 ? 
54  O   ? A LEU 107 ? A LEU 212  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A LYS 109 ? A LYS 214  ? 1_555 93.9  ? 
55  O   ? A GLY 108 ? A GLY 213  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? A LYS 109 ? A LYS 214  ? 1_555 73.7  ? 
56  OG  ? A SER 106 ? A SER 211  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2047 ? 1_555 60.2  ? 
57  O   ? A LEU 107 ? A LEU 212  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2047 ? 1_555 128.5 ? 
58  O   ? A GLY 108 ? A GLY 213  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2047 ? 1_555 160.3 ? 
59  O   ? A LYS 109 ? A LYS 214  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2047 ? 1_555 102.5 ? 
60  OG  ? A SER 106 ? A SER 211  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2050 ? 1_555 90.3  ? 
61  O   ? A LEU 107 ? A LEU 212  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2050 ? 1_555 104.6 ? 
62  O   ? A GLY 108 ? A GLY 213  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2050 ? 1_555 68.1  ? 
63  O   ? A LYS 109 ? A LYS 214  ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2050 ? 1_555 128.4 ? 
64  O   ? S HOH .   ? A HOH 2047 ? 1_555 CA ? F CA . ? A CA 1447 ? 1_555 O   ? S HOH .   ? A HOH 2050 ? 1_555 102.2 ? 
65  NE2 ? A HIS 121 ? A HIS 401  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 NE2 ? A HIS 125 ? A HIS 405  ? 1_555 101.9 ? 
66  NE2 ? A HIS 121 ? A HIS 401  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 NE2 ? A HIS 131 ? A HIS 411  ? 1_555 107.2 ? 
67  NE2 ? A HIS 125 ? A HIS 405  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 NE2 ? A HIS 131 ? A HIS 411  ? 1_555 92.6  ? 
68  NE2 ? A HIS 121 ? A HIS 401  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 ON  ? G NFH .   ? A NFH 1448 ? 1_555 119.9 ? 
69  NE2 ? A HIS 125 ? A HIS 405  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 ON  ? G NFH .   ? A NFH 1448 ? 1_555 137.0 ? 
70  NE2 ? A HIS 131 ? A HIS 411  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 ON  ? G NFH .   ? A NFH 1448 ? 1_555 84.8  ? 
71  NE2 ? A HIS 121 ? A HIS 401  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 OM  ? G NFH .   ? A NFH 1448 ? 1_555 108.2 ? 
72  NE2 ? A HIS 125 ? A HIS 405  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 OM  ? G NFH .   ? A NFH 1448 ? 1_555 86.6  ? 
73  NE2 ? A HIS 131 ? A HIS 411  ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 OM  ? G NFH .   ? A NFH 1448 ? 1_555 144.0 ? 
74  ON  ? G NFH .   ? A NFH 1448 ? 1_555 ZN ? H ZN . ? A ZN 1450 ? 1_555 OM  ? G NFH .   ? A NFH 1448 ? 1_555 71.9  ? 
75  OD2 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 OD1 ? B ASP 26  ? B ASP 131  ? 1_555 42.4  ? 
76  OD2 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 OD1 ? B ASP 101 ? B ASP 206  ? 1_555 97.0  ? 
77  OD1 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 OD1 ? B ASP 101 ? B ASP 206  ? 1_555 107.7 ? 
78  OD2 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B ASP 101 ? B ASP 206  ? 1_555 165.5 ? 
79  OD1 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B ASP 101 ? B ASP 206  ? 1_555 148.0 ? 
80  OD1 ? B ASP 101 ? B ASP 206  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B ASP 101 ? B ASP 206  ? 1_555 71.0  ? 
81  OD2 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B GLU 103 ? B GLU 208  ? 1_555 81.1  ? 
82  OD1 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B GLU 103 ? B GLU 208  ? 1_555 113.8 ? 
83  OD1 ? B ASP 101 ? B ASP 206  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B GLU 103 ? B GLU 208  ? 1_555 111.2 ? 
84  O   ? B ASP 101 ? B ASP 206  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? B GLU 103 ? B GLU 208  ? 1_555 95.4  ? 
85  OD2 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? T HOH .   ? B HOH 2011 ? 1_555 106.4 ? 
86  OD1 ? B ASP 26  ? B ASP 131  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? T HOH .   ? B HOH 2011 ? 1_555 65.0  ? 
87  OD1 ? B ASP 101 ? B ASP 206  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? T HOH .   ? B HOH 2011 ? 1_555 93.2  ? 
88  O   ? B ASP 101 ? B ASP 206  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? T HOH .   ? B HOH 2011 ? 1_555 83.0  ? 
89  O   ? B GLU 103 ? B GLU 208  ? 1_555 CA ? M CA . ? B CA 1446 ? 1_555 O   ? T HOH .   ? B HOH 2011 ? 1_555 153.6 ? 
90  O   ? B SER 44  ? B SER 149  ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? B THR 47  ? B THR 152  ? 1_555 56.0  ? 
91  O   ? B SER 44  ? B SER 149  ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? T HOH .   ? B HOH 2021 ? 1_555 89.0  ? 
92  O   ? B THR 47  ? B THR 152  ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? T HOH .   ? B HOH 2021 ? 1_555 111.4 ? 
93  O   ? B SER 44  ? B SER 149  ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? T HOH .   ? B HOH 2022 ? 1_555 61.2  ? 
94  O   ? B THR 47  ? B THR 152  ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? T HOH .   ? B HOH 2022 ? 1_555 63.3  ? 
95  O   ? T HOH .   ? B HOH 2021 ? 1_555 CA ? O CA . ? B CA 1448 ? 1_555 O   ? T HOH .   ? B HOH 2022 ? 1_555 147.9 ? 
96  O   ? B ASP 60  ? B ASP 165  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? B GLY 92  ? B GLY 197  ? 1_555 171.2 ? 
97  O   ? B ASP 60  ? B ASP 165  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? B GLN 94  ? B GLN 199  ? 1_555 101.1 ? 
98  O   ? B GLY 92  ? B GLY 197  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? B GLN 94  ? B GLN 199  ? 1_555 82.4  ? 
99  O   ? B ASP 60  ? B ASP 165  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 OD1 ? B ASP 96  ? B ASP 201  ? 1_555 90.6  ? 
100 O   ? B GLY 92  ? B GLY 197  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 OD1 ? B ASP 96  ? B ASP 201  ? 1_555 97.0  ? 
101 O   ? B GLN 94  ? B GLN 199  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 OD1 ? B ASP 96  ? B ASP 201  ? 1_555 98.0  ? 
102 O   ? B ASP 60  ? B ASP 165  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2030 ? 1_555 88.4  ? 
103 O   ? B GLY 92  ? B GLY 197  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2030 ? 1_555 86.4  ? 
104 O   ? B GLN 94  ? B GLN 199  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2030 ? 1_555 163.5 ? 
105 OD1 ? B ASP 96  ? B ASP 201  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2030 ? 1_555 95.3  ? 
106 O   ? B ASP 60  ? B ASP 165  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2041 ? 1_555 80.4  ? 
107 O   ? B GLY 92  ? B GLY 197  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2041 ? 1_555 92.2  ? 
108 O   ? B GLN 94  ? B GLN 199  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2041 ? 1_555 81.0  ? 
109 OD1 ? B ASP 96  ? B ASP 201  ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2041 ? 1_555 170.6 ? 
110 O   ? T HOH .   ? B HOH 2030 ? 1_555 CA ? L CA . ? B CA 1445 ? 1_555 O   ? T HOH .   ? B HOH 2041 ? 1_555 87.3  ? 
111 NE2 ? B HIS 70  ? B HIS 175  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 OD2 ? B ASP 72  ? B ASP 177  ? 1_555 105.6 ? 
112 NE2 ? B HIS 70  ? B HIS 175  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 NE2 ? B HIS 85  ? B HIS 190  ? 1_555 114.2 ? 
113 OD2 ? B ASP 72  ? B ASP 177  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 NE2 ? B HIS 85  ? B HIS 190  ? 1_555 111.9 ? 
114 NE2 ? B HIS 70  ? B HIS 175  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 ND1 ? B HIS 98  ? B HIS 203  ? 1_555 118.0 ? 
115 OD2 ? B ASP 72  ? B ASP 177  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 ND1 ? B HIS 98  ? B HIS 203  ? 1_555 91.2  ? 
116 NE2 ? B HIS 85  ? B HIS 190  ? 1_555 ZN ? R ZN . ? B ZN 1452 ? 1_555 ND1 ? B HIS 98  ? B HIS 203  ? 1_555 113.2 ? 
117 OD1 ? B ASP 77  ? B ASP 182  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B GLY 78  ? B GLY 183  ? 1_555 82.9  ? 
118 OD1 ? B ASP 77  ? B ASP 182  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B ASP 80  ? B ASP 185  ? 1_555 74.6  ? 
119 O   ? B GLY 78  ? B GLY 183  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B ASP 80  ? B ASP 185  ? 1_555 74.7  ? 
120 OD1 ? B ASP 77  ? B ASP 182  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B LEU 82  ? B LEU 187  ? 1_555 91.0  ? 
121 O   ? B GLY 78  ? B GLY 183  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B LEU 82  ? B LEU 187  ? 1_555 173.9 ? 
122 O   ? B ASP 80  ? B ASP 185  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 O   ? B LEU 82  ? B LEU 187  ? 1_555 104.0 ? 
123 OD1 ? B ASP 77  ? B ASP 182  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OD2 ? B ASP 100 ? B ASP 205  ? 1_555 95.2  ? 
124 O   ? B GLY 78  ? B GLY 183  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OD2 ? B ASP 100 ? B ASP 205  ? 1_555 79.0  ? 
125 O   ? B ASP 80  ? B ASP 185  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OD2 ? B ASP 100 ? B ASP 205  ? 1_555 152.8 ? 
126 O   ? B LEU 82  ? B LEU 187  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OD2 ? B ASP 100 ? B ASP 205  ? 1_555 101.3 ? 
127 OD1 ? B ASP 77  ? B ASP 182  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OE2 ? B GLU 103 ? B GLU 208  ? 1_555 151.1 ? 
128 O   ? B GLY 78  ? B GLY 183  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OE2 ? B GLU 103 ? B GLU 208  ? 1_555 103.5 ? 
129 O   ? B ASP 80  ? B ASP 185  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OE2 ? B GLU 103 ? B GLU 208  ? 1_555 79.9  ? 
130 O   ? B LEU 82  ? B LEU 187  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OE2 ? B GLU 103 ? B GLU 208  ? 1_555 82.0  ? 
131 OD2 ? B ASP 100 ? B ASP 205  ? 1_555 CA ? K CA . ? B CA 1444 ? 1_555 OE2 ? B GLU 103 ? B GLU 208  ? 1_555 113.6 ? 
132 OG  ? B SER 106 ? B SER 211  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B LEU 107 ? B LEU 212  ? 1_555 81.0  ? 
133 OG  ? B SER 106 ? B SER 211  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B GLY 108 ? B GLY 213  ? 1_555 145.1 ? 
134 O   ? B LEU 107 ? B LEU 212  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B GLY 108 ? B GLY 213  ? 1_555 75.4  ? 
135 OG  ? B SER 106 ? B SER 211  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B LYS 109 ? B LYS 214  ? 1_555 135.4 ? 
136 O   ? B LEU 107 ? B LEU 212  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B LYS 109 ? B LYS 214  ? 1_555 90.9  ? 
137 O   ? B GLY 108 ? B GLY 213  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? B LYS 109 ? B LYS 214  ? 1_555 71.0  ? 
138 OG  ? B SER 106 ? B SER 211  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? T HOH .   ? B HOH 2052 ? 1_555 60.8  ? 
139 O   ? B LEU 107 ? B LEU 212  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? T HOH .   ? B HOH 2052 ? 1_555 120.4 ? 
140 O   ? B GLY 108 ? B GLY 213  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? T HOH .   ? B HOH 2052 ? 1_555 154.1 ? 
141 O   ? B LYS 109 ? B LYS 214  ? 1_555 CA ? N CA . ? B CA 1447 ? 1_555 O   ? T HOH .   ? B HOH 2052 ? 1_555 87.5  ? 
142 NE2 ? B HIS 121 ? B HIS 401  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 NE2 ? B HIS 125 ? B HIS 405  ? 1_555 101.4 ? 
143 NE2 ? B HIS 121 ? B HIS 401  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 NE2 ? B HIS 131 ? B HIS 411  ? 1_555 104.0 ? 
144 NE2 ? B HIS 125 ? B HIS 405  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 NE2 ? B HIS 131 ? B HIS 411  ? 1_555 95.5  ? 
145 NE2 ? B HIS 121 ? B HIS 401  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 ON  ? P NFH .   ? B NFH 1449 ? 1_555 118.7 ? 
146 NE2 ? B HIS 125 ? B HIS 405  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 ON  ? P NFH .   ? B NFH 1449 ? 1_555 138.6 ? 
147 NE2 ? B HIS 131 ? B HIS 411  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 ON  ? P NFH .   ? B NFH 1449 ? 1_555 84.8  ? 
148 NE2 ? B HIS 121 ? B HIS 401  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 OM  ? P NFH .   ? B NFH 1449 ? 1_555 110.9 ? 
149 NE2 ? B HIS 125 ? B HIS 405  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 OM  ? P NFH .   ? B NFH 1449 ? 1_555 87.6  ? 
150 NE2 ? B HIS 131 ? B HIS 411  ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 OM  ? P NFH .   ? B NFH 1449 ? 1_555 143.5 ? 
151 ON  ? P NFH .   ? B NFH 1449 ? 1_555 ZN ? Q ZN . ? B ZN 1451 ? 1_555 OM  ? P NFH .   ? B NFH 1449 ? 1_555 69.8  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2002-05-16 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2023-12-13 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
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' 'Atomic model'              
2  2 'Structure model' 'Database references'       
3  2 'Structure model' 'Derived calculations'      
4  2 'Structure model' 'Non-polymer description'   
5  2 'Structure model' 'Structure summary'         
6  2 'Structure model' 'Version format compliance' 
7  3 'Structure model' 'Data collection'           
8  3 'Structure model' 'Database references'       
9  3 'Structure model' 'Derived calculations'      
10 3 'Structure model' Other                       
11 3 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' chem_comp_atom                
2 3 'Structure model' chem_comp_bond                
3 3 'Structure model' database_2                    
4 3 'Structure model' pdbx_database_status          
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' pdbx_struct_conn_angle        
7 3 'Structure model' struct_conn                   
8 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  3 'Structure model' '_database_2.pdbx_DOI'                        
2  3 'Structure model' '_database_2.pdbx_database_accession'         
3  3 'Structure model' '_pdbx_database_status.status_code_sf'        
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_comp_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_atom_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_comp_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
21 3 'Structure model' '_pdbx_struct_conn_angle.value'               
22 3 'Structure model' '_struct_conn.pdbx_dist_value'                
23 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
24 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
29 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
30 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
31 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
32 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
33 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
34 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
35 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
36 3 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
37 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
38 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
39 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNX    refinement       2000 ? 1 
MOSFLM 'data reduction' .    ? 2 
SCALA  'data scaling'   .    ? 3 
AMoRE  phasing          .    ? 4 
# 
_pdbx_entry_details.entry_id                 1GKC 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         
;THE INITIAL METHIONINE IN THE MATERIAL CRYSTALLISED IS A
 CLONING ARTEFACT.
;
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 173 ? ? 52.07   -129.16 
2 1 HIS A 175 ? ? -141.50 28.96   
3 1 ASP A 177 ? ? -74.70  -164.75 
4 1 ASP A 185 ? ? 55.53   -173.11 
5 1 SER A 211 ? ? -148.73 -156.62 
6 1 PRO A 421 ? ? -58.90  -3.96   
7 1 ALA B 173 ? ? 50.24   -129.37 
8 1 ASP B 177 ? ? -71.71  -162.50 
9 1 ASP B 185 ? ? 61.12   -178.06 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B ARG 424 ? CG  ? B ARG 144 CG  
2 1 Y 1 B ARG 424 ? CD  ? B ARG 144 CD  
3 1 Y 1 B ARG 424 ? NE  ? B ARG 144 NE  
4 1 Y 1 B ARG 424 ? CZ  ? B ARG 144 CZ  
5 1 Y 1 B ARG 424 ? NH1 ? B ARG 144 NH1 
6 1 Y 1 B ARG 424 ? NH2 ? B ARG 144 NH2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 106 ? A MET 1 
2  1 Y 1 A PHE 107 ? A PHE 2 
3  1 Y 1 A GLN 108 ? A GLN 3 
4  1 Y 1 A THR 109 ? A THR 4 
5  1 Y 1 B MET 106 ? B MET 1 
6  1 Y 1 B PHE 107 ? B PHE 2 
7  1 Y 1 B GLN 108 ? B GLN 3 
8  1 Y 1 B THR 109 ? B THR 4 
9  1 Y 1 B PHE 110 ? B PHE 5 
10 1 Y 1 B GLU 111 ? B GLU 6 
11 1 Y 1 B GLY 112 ? B GLY 7 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
HIS N    N  N N 124 
HIS CA   C  N S 125 
HIS C    C  N N 126 
HIS O    O  N N 127 
HIS CB   C  N N 128 
HIS CG   C  Y N 129 
HIS ND1  N  Y N 130 
HIS CD2  C  Y N 131 
HIS CE1  C  Y N 132 
HIS NE2  N  Y N 133 
HIS OXT  O  N N 134 
HIS H    H  N N 135 
HIS H2   H  N N 136 
HIS HA   H  N N 137 
HIS HB2  H  N N 138 
HIS HB3  H  N N 139 
HIS HD1  H  N N 140 
HIS HD2  H  N N 141 
HIS HE1  H  N N 142 
HIS HE2  H  N N 143 
HIS HXT  H  N N 144 
HOH O    O  N N 145 
HOH H1   H  N N 146 
HOH H2   H  N N 147 
ILE N    N  N N 148 
ILE CA   C  N S 149 
ILE C    C  N N 150 
ILE O    O  N N 151 
ILE CB   C  N S 152 
ILE CG1  C  N N 153 
ILE CG2  C  N N 154 
ILE CD1  C  N N 155 
ILE OXT  O  N N 156 
ILE H    H  N N 157 
ILE H2   H  N N 158 
ILE HA   H  N N 159 
ILE HB   H  N N 160 
ILE HG12 H  N N 161 
ILE HG13 H  N N 162 
ILE HG21 H  N N 163 
ILE HG22 H  N N 164 
ILE HG23 H  N N 165 
ILE HD11 H  N N 166 
ILE HD12 H  N N 167 
ILE HD13 H  N N 168 
ILE HXT  H  N N 169 
LEU N    N  N N 170 
LEU CA   C  N S 171 
LEU C    C  N N 172 
LEU O    O  N N 173 
LEU CB   C  N N 174 
LEU CG   C  N N 175 
LEU CD1  C  N N 176 
LEU CD2  C  N N 177 
LEU OXT  O  N N 178 
LEU H    H  N N 179 
LEU H2   H  N N 180 
LEU HA   H  N N 181 
LEU HB2  H  N N 182 
LEU HB3  H  N N 183 
LEU HG   H  N N 184 
LEU HD11 H  N N 185 
LEU HD12 H  N N 186 
LEU HD13 H  N N 187 
LEU HD21 H  N N 188 
LEU HD22 H  N N 189 
LEU HD23 H  N N 190 
LEU HXT  H  N N 191 
LYS N    N  N N 192 
LYS CA   C  N S 193 
LYS C    C  N N 194 
LYS O    O  N N 195 
LYS CB   C  N N 196 
LYS CG   C  N N 197 
LYS CD   C  N N 198 
LYS CE   C  N N 199 
LYS NZ   N  N N 200 
LYS OXT  O  N N 201 
LYS H    H  N N 202 
LYS H2   H  N N 203 
LYS HA   H  N N 204 
LYS HB2  H  N N 205 
LYS HB3  H  N N 206 
LYS HG2  H  N N 207 
LYS HG3  H  N N 208 
LYS HD2  H  N N 209 
LYS HD3  H  N N 210 
LYS HE2  H  N N 211 
LYS HE3  H  N N 212 
LYS HZ1  H  N N 213 
LYS HZ2  H  N N 214 
LYS HZ3  H  N N 215 
LYS HXT  H  N N 216 
MET N    N  N N 217 
MET CA   C  N S 218 
MET C    C  N N 219 
MET O    O  N N 220 
MET CB   C  N N 221 
MET CG   C  N N 222 
MET SD   S  N N 223 
MET CE   C  N N 224 
MET OXT  O  N N 225 
MET H    H  N N 226 
MET H2   H  N N 227 
MET HA   H  N N 228 
MET HB2  H  N N 229 
MET HB3  H  N N 230 
MET HG2  H  N N 231 
MET HG3  H  N N 232 
MET HE1  H  N N 233 
MET HE2  H  N N 234 
MET HE3  H  N N 235 
MET HXT  H  N N 236 
NFH C    C  N N 237 
NFH N    N  N N 238 
NFH O    O  N N 239 
NFH C1   C  N N 240 
NFH N1   N  N N 241 
NFH O1   O  N N 242 
NFH N2   N  N N 243 
NFH CA   C  N R 244 
NFH CB   C  N N 245 
NFH CG   C  N N 246 
NFH CM   C  N N 247 
NFH OM   O  N N 248 
NFH CN   C  N N 249 
NFH ON   O  N N 250 
NFH CA1  C  N S 251 
NFH CB1  C  N N 252 
NFH CD1  C  N N 253 
NFH CD2  C  N N 254 
NFH CG1  C  N N 255 
NFH CG2  C  N N 256 
NFH CG3  C  N N 257 
NFH CN2  C  N N 258 
NFH HN1  H  N N 259 
NFH H2   H  N N 260 
NFH HA   H  N N 261 
NFH HB   H  N N 262 
NFH HBA  H  N N 263 
NFH HG   H  N N 264 
NFH HM   H  N N 265 
NFH HN   H  N N 266 
NFH HNA  H  N N 267 
NFH HON  H  N N 268 
NFH HA1  H  N N 269 
NFH HD1  H  N N 270 
NFH HD1A H  N N 271 
NFH HD1B H  N N 272 
NFH HD2  H  N N 273 
NFH HD2A H  N N 274 
NFH HD2B H  N N 275 
NFH HG1  H  N N 276 
NFH HG1A H  N N 277 
NFH HG1B H  N N 278 
NFH HG2  H  N N 279 
NFH HG2A H  N N 280 
NFH HG2B H  N N 281 
NFH HG3  H  N N 282 
NFH HG3A H  N N 283 
NFH HG3B H  N N 284 
NFH HN2  H  N N 285 
NFH HN2A H  N N 286 
NFH H29  H  N N 287 
PHE N    N  N N 288 
PHE CA   C  N S 289 
PHE C    C  N N 290 
PHE O    O  N N 291 
PHE CB   C  N N 292 
PHE CG   C  Y N 293 
PHE CD1  C  Y N 294 
PHE CD2  C  Y N 295 
PHE CE1  C  Y N 296 
PHE CE2  C  Y N 297 
PHE CZ   C  Y N 298 
PHE OXT  O  N N 299 
PHE H    H  N N 300 
PHE H2   H  N N 301 
PHE HA   H  N N 302 
PHE HB2  H  N N 303 
PHE HB3  H  N N 304 
PHE HD1  H  N N 305 
PHE HD2  H  N N 306 
PHE HE1  H  N N 307 
PHE HE2  H  N N 308 
PHE HZ   H  N N 309 
PHE HXT  H  N N 310 
PRO N    N  N N 311 
PRO CA   C  N S 312 
PRO C    C  N N 313 
PRO O    O  N N 314 
PRO CB   C  N N 315 
PRO CG   C  N N 316 
PRO CD   C  N N 317 
PRO OXT  O  N N 318 
PRO H    H  N N 319 
PRO HA   H  N N 320 
PRO HB2  H  N N 321 
PRO HB3  H  N N 322 
PRO HG2  H  N N 323 
PRO HG3  H  N N 324 
PRO HD2  H  N N 325 
PRO HD3  H  N N 326 
PRO HXT  H  N N 327 
SER N    N  N N 328 
SER CA   C  N S 329 
SER C    C  N N 330 
SER O    O  N N 331 
SER CB   C  N N 332 
SER OG   O  N N 333 
SER OXT  O  N N 334 
SER H    H  N N 335 
SER H2   H  N N 336 
SER HA   H  N N 337 
SER HB2  H  N N 338 
SER HB3  H  N N 339 
SER HG   H  N N 340 
SER HXT  H  N N 341 
THR N    N  N N 342 
THR CA   C  N S 343 
THR C    C  N N 344 
THR O    O  N N 345 
THR CB   C  N R 346 
THR OG1  O  N N 347 
THR CG2  C  N N 348 
THR OXT  O  N N 349 
THR H    H  N N 350 
THR H2   H  N N 351 
THR HA   H  N N 352 
THR HB   H  N N 353 
THR HG1  H  N N 354 
THR HG21 H  N N 355 
THR HG22 H  N N 356 
THR HG23 H  N N 357 
THR HXT  H  N N 358 
TRP N    N  N N 359 
TRP CA   C  N S 360 
TRP C    C  N N 361 
TRP O    O  N N 362 
TRP CB   C  N N 363 
TRP CG   C  Y N 364 
TRP CD1  C  Y N 365 
TRP CD2  C  Y N 366 
TRP NE1  N  Y N 367 
TRP CE2  C  Y N 368 
TRP CE3  C  Y N 369 
TRP CZ2  C  Y N 370 
TRP CZ3  C  Y N 371 
TRP CH2  C  Y N 372 
TRP OXT  O  N N 373 
TRP H    H  N N 374 
TRP H2   H  N N 375 
TRP HA   H  N N 376 
TRP HB2  H  N N 377 
TRP HB3  H  N N 378 
TRP HD1  H  N N 379 
TRP HE1  H  N N 380 
TRP HE3  H  N N 381 
TRP HZ2  H  N N 382 
TRP HZ3  H  N N 383 
TRP HH2  H  N N 384 
TRP HXT  H  N N 385 
TYR N    N  N N 386 
TYR CA   C  N S 387 
TYR C    C  N N 388 
TYR O    O  N N 389 
TYR CB   C  N N 390 
TYR CG   C  Y N 391 
TYR CD1  C  Y N 392 
TYR CD2  C  Y N 393 
TYR CE1  C  Y N 394 
TYR CE2  C  Y N 395 
TYR CZ   C  Y N 396 
TYR OH   O  N N 397 
TYR OXT  O  N N 398 
TYR H    H  N N 399 
TYR H2   H  N N 400 
TYR HA   H  N N 401 
TYR HB2  H  N N 402 
TYR HB3  H  N N 403 
TYR HD1  H  N N 404 
TYR HD2  H  N N 405 
TYR HE1  H  N N 406 
TYR HE2  H  N N 407 
TYR HH   H  N N 408 
TYR HXT  H  N N 409 
VAL N    N  N N 410 
VAL CA   C  N S 411 
VAL C    C  N N 412 
VAL O    O  N N 413 
VAL CB   C  N N 414 
VAL CG1  C  N N 415 
VAL CG2  C  N N 416 
VAL OXT  O  N N 417 
VAL H    H  N N 418 
VAL H2   H  N N 419 
VAL HA   H  N N 420 
VAL HB   H  N N 421 
VAL HG11 H  N N 422 
VAL HG12 H  N N 423 
VAL HG13 H  N N 424 
VAL HG21 H  N N 425 
VAL HG22 H  N N 426 
VAL HG23 H  N N 427 
VAL HXT  H  N N 428 
ZN  ZN   ZN N N 429 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
NFH C   CA   sing N N 224 
NFH N   ON   sing N N 225 
NFH N   CM   sing N N 226 
NFH O   C    doub N N 227 
NFH C1  CA1  sing N N 228 
NFH N1  C    sing N N 229 
NFH O1  C1   doub N N 230 
NFH N2  C1   sing N N 231 
NFH CA  CN   sing N N 232 
NFH CB  CA   sing N N 233 
NFH CG  CB   sing N N 234 
NFH CG  CD1  sing N N 235 
NFH CM  OM   doub N N 236 
NFH CN  N    sing N N 237 
NFH CA1 N1   sing N N 238 
NFH CA1 CB1  sing N N 239 
NFH CB1 CG2  sing N N 240 
NFH CD2 CG   sing N N 241 
NFH CG1 CB1  sing N N 242 
NFH CG3 CB1  sing N N 243 
NFH CN2 N2   sing N N 244 
NFH N1  HN1  sing N N 245 
NFH N2  H2   sing N N 246 
NFH CA  HA   sing N N 247 
NFH CB  HB   sing N N 248 
NFH CB  HBA  sing N N 249 
NFH CG  HG   sing N N 250 
NFH CM  HM   sing N N 251 
NFH CN  HN   sing N N 252 
NFH CN  HNA  sing N N 253 
NFH ON  HON  sing N N 254 
NFH CA1 HA1  sing N N 255 
NFH CD1 HD1  sing N N 256 
NFH CD1 HD1A sing N N 257 
NFH CD1 HD1B sing N N 258 
NFH CD2 HD2  sing N N 259 
NFH CD2 HD2A sing N N 260 
NFH CD2 HD2B sing N N 261 
NFH CG1 HG1  sing N N 262 
NFH CG1 HG1A sing N N 263 
NFH CG1 HG1B sing N N 264 
NFH CG2 HG2  sing N N 265 
NFH CG2 HG2A sing N N 266 
NFH CG2 HG2B sing N N 267 
NFH CG3 HG3  sing N N 268 
NFH CG3 HG3A sing N N 269 
NFH CG3 HG3B sing N N 270 
NFH CN2 HN2  sing N N 271 
NFH CN2 HN2A sing N N 272 
NFH CN2 H29  sing N N 273 
PHE N   CA   sing N N 274 
PHE N   H    sing N N 275 
PHE N   H2   sing N N 276 
PHE CA  C    sing N N 277 
PHE CA  CB   sing N N 278 
PHE CA  HA   sing N N 279 
PHE C   O    doub N N 280 
PHE C   OXT  sing N N 281 
PHE CB  CG   sing N N 282 
PHE CB  HB2  sing N N 283 
PHE CB  HB3  sing N N 284 
PHE CG  CD1  doub Y N 285 
PHE CG  CD2  sing Y N 286 
PHE CD1 CE1  sing Y N 287 
PHE CD1 HD1  sing N N 288 
PHE CD2 CE2  doub Y N 289 
PHE CD2 HD2  sing N N 290 
PHE CE1 CZ   doub Y N 291 
PHE CE1 HE1  sing N N 292 
PHE CE2 CZ   sing Y N 293 
PHE CE2 HE2  sing N N 294 
PHE CZ  HZ   sing N N 295 
PHE OXT HXT  sing N N 296 
PRO N   CA   sing N N 297 
PRO N   CD   sing N N 298 
PRO N   H    sing N N 299 
PRO CA  C    sing N N 300 
PRO CA  CB   sing N N 301 
PRO CA  HA   sing N N 302 
PRO C   O    doub N N 303 
PRO C   OXT  sing N N 304 
PRO CB  CG   sing N N 305 
PRO CB  HB2  sing N N 306 
PRO CB  HB3  sing N N 307 
PRO CG  CD   sing N N 308 
PRO CG  HG2  sing N N 309 
PRO CG  HG3  sing N N 310 
PRO CD  HD2  sing N N 311 
PRO CD  HD3  sing N N 312 
PRO OXT HXT  sing N N 313 
SER N   CA   sing N N 314 
SER N   H    sing N N 315 
SER N   H2   sing N N 316 
SER CA  C    sing N N 317 
SER CA  CB   sing N N 318 
SER CA  HA   sing N N 319 
SER C   O    doub N N 320 
SER C   OXT  sing N N 321 
SER CB  OG   sing N N 322 
SER CB  HB2  sing N N 323 
SER CB  HB3  sing N N 324 
SER OG  HG   sing N N 325 
SER OXT HXT  sing N N 326 
THR N   CA   sing N N 327 
THR N   H    sing N N 328 
THR N   H2   sing N N 329 
THR CA  C    sing N N 330 
THR CA  CB   sing N N 331 
THR CA  HA   sing N N 332 
THR C   O    doub N N 333 
THR C   OXT  sing N N 334 
THR CB  OG1  sing N N 335 
THR CB  CG2  sing N N 336 
THR CB  HB   sing N N 337 
THR OG1 HG1  sing N N 338 
THR CG2 HG21 sing N N 339 
THR CG2 HG22 sing N N 340 
THR CG2 HG23 sing N N 341 
THR OXT HXT  sing N N 342 
TRP N   CA   sing N N 343 
TRP N   H    sing N N 344 
TRP N   H2   sing N N 345 
TRP CA  C    sing N N 346 
TRP CA  CB   sing N N 347 
TRP CA  HA   sing N N 348 
TRP C   O    doub N N 349 
TRP C   OXT  sing N N 350 
TRP CB  CG   sing N N 351 
TRP CB  HB2  sing N N 352 
TRP CB  HB3  sing N N 353 
TRP CG  CD1  doub Y N 354 
TRP CG  CD2  sing Y N 355 
TRP CD1 NE1  sing Y N 356 
TRP CD1 HD1  sing N N 357 
TRP CD2 CE2  doub Y N 358 
TRP CD2 CE3  sing Y N 359 
TRP NE1 CE2  sing Y N 360 
TRP NE1 HE1  sing N N 361 
TRP CE2 CZ2  sing Y N 362 
TRP CE3 CZ3  doub Y N 363 
TRP CE3 HE3  sing N N 364 
TRP CZ2 CH2  doub Y N 365 
TRP CZ2 HZ2  sing N N 366 
TRP CZ3 CH2  sing Y N 367 
TRP CZ3 HZ3  sing N N 368 
TRP CH2 HH2  sing N N 369 
TRP OXT HXT  sing N N 370 
TYR N   CA   sing N N 371 
TYR N   H    sing N N 372 
TYR N   H2   sing N N 373 
TYR CA  C    sing N N 374 
TYR CA  CB   sing N N 375 
TYR CA  HA   sing N N 376 
TYR C   O    doub N N 377 
TYR C   OXT  sing N N 378 
TYR CB  CG   sing N N 379 
TYR CB  HB2  sing N N 380 
TYR CB  HB3  sing N N 381 
TYR CG  CD1  doub Y N 382 
TYR CG  CD2  sing Y N 383 
TYR CD1 CE1  sing Y N 384 
TYR CD1 HD1  sing N N 385 
TYR CD2 CE2  doub Y N 386 
TYR CD2 HD2  sing N N 387 
TYR CE1 CZ   doub Y N 388 
TYR CE1 HE1  sing N N 389 
TYR CE2 CZ   sing Y N 390 
TYR CE2 HE2  sing N N 391 
TYR CZ  OH   sing N N 392 
TYR OH  HH   sing N N 393 
TYR OXT HXT  sing N N 394 
VAL N   CA   sing N N 395 
VAL N   H    sing N N 396 
VAL N   H2   sing N N 397 
VAL CA  C    sing N N 398 
VAL CA  CB   sing N N 399 
VAL CA  HA   sing N N 400 
VAL C   O    doub N N 401 
VAL C   OXT  sing N N 402 
VAL CB  CG1  sing N N 403 
VAL CB  CG2  sing N N 404 
VAL CB  HB   sing N N 405 
VAL CG1 HG11 sing N N 406 
VAL CG1 HG12 sing N N 407 
VAL CG1 HG13 sing N N 408 
VAL CG2 HG21 sing N N 409 
VAL CG2 HG22 sing N N 410 
VAL CG2 HG23 sing N N 411 
VAL OXT HXT  sing N N 412 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION'                                                                              CA  
3 'N~2~-[(2R)-2-{[formyl(hydroxy)amino]methyl}-4-methylpentanoyl]-N,3-dimethyl-L-valinamide' NFH 
4 'ZINC ION'                                                                                 ZN  
5 water                                                                                      HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1HFS 
_pdbx_initial_refinement_model.details          'PDB ENTRY 1HFS' 
# 
