data_1OZU
# 
_entry.id   1OZU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_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   1OZU         pdb_00001ozu 10.2210/pdb1ozu/pdb 
RCSB  RCSB018850   ?            ?                   
WWPDB D_1000018850 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1OZT 'Crystal Structure of apo H46R Mutant of human Cu,Zn Superoxide Dismutase (CuZnSOD)'       unspecified 
PDB 1OEZ 'Crystal Structure of Zn-loaded H46R Mutant of human Cu,Zn Superoxide Dismutase (CuZnSOD)' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1OZU 
_pdbx_database_status.recvd_initial_deposition_date   2003-04-09 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Elam, J.S.'      1  
'Taylor, A.B.'    2  
'Strange, R.'     3  
'Antonyuk, S.'    4  
'Doucette, P.A.'  5  
'Rodriguez, J.A.' 6  
'Hasnain, S.S.'   7  
'Hayward, L.J.'   8  
'Valentine, J.S.' 9  
'Yeates, T.O.'    10 
'Hart, P.J.'      11 
# 
_citation.id                        primary 
_citation.title                     
'Amyloid-like Filaments and Water-filled Nanotubes Formed by SOD1 Mutant Proteins Linked to Familial ALS' 
_citation.journal_abbrev            Nat.Struct.Biol. 
_citation.journal_volume            10 
_citation.page_first                461 
_citation.page_last                 467 
_citation.year                      2003 
_citation.journal_id_ASTM           NSBIEW 
_citation.country                   US 
_citation.journal_id_ISSN           1072-8368 
_citation.journal_id_CSD            2024 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12754496 
_citation.pdbx_database_id_DOI      10.1038/nsb935 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Elam, J.S.'      1  ? 
primary 'Taylor, A.B.'    2  ? 
primary 'Strange, R.'     3  ? 
primary 'Antonyuk, S.'    4  ? 
primary 'Doucette, P.A.'  5  ? 
primary 'Rodriguez, J.A.' 6  ? 
primary 'Hasnain, S.S.'   7  ? 
primary 'Hayward, L.J.'   8  ? 
primary 'Valentine, J.S.' 9  ? 
primary 'Yeates, T.O.'    10 ? 
primary 'Hart, P.J.'      11 ? 
# 
_cell.entry_id           1OZU 
_cell.length_a           40.086 
_cell.length_b           56.457 
_cell.length_c           105.350 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1OZU 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 'Superoxide dismutase [Cu-Zn]' 15870.586 2   1.15.1.1 S134N ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    3   ?        ?     ? ? 
3 non-polymer syn 'SULFATE ION'                  96.063    2   ?        ?     ? ? 
4 water       nat water                          18.015    247 ?        ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDH(CSX)IIGRTLVVHEKADDLGKGGNEENTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEENTKTGNAGSRLACGVIGIAQ
;
_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   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CSX n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 ASN n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_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               
;baker's yeast
;
_entity_src_gen.pdbx_host_org_scientific_name      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     Saccharomyces 
_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               EG103 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'YEp 351' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1OZU A 1 ? 153 ? P00441 1 ? 153 ? 1   153 
2 1 1OZU B 1 ? 153 ? P00441 1 ? 153 ? 201 353 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1OZU CSX A 111 ? UNP P00441 CYS 111 'modified residue'    111 1 
1 1OZU ASN A 134 ? UNP P00441 SER 134 'engineered mutation' 134 2 
2 1OZU CSX B 111 ? UNP P00441 CYS 111 'modified residue'    311 3 
2 1OZU ASN B 134 ? UNP P00441 SER 134 'engineered mutation' 334 4 
# 
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 
CSX 'L-peptide linking' n 'S-OXY CYSTEINE' ? 'C3 H7 N O3 S'   137.158 
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'    ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'       ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1OZU 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.89 
_exptl_crystal.density_percent_sol   34.28 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298.0 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pdbx_details    'Ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2002-04-21 
_diffrn_detector.details                mirrors 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    mirrors 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.1000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'NSLS BEAMLINE X8C' 
_diffrn_source.pdbx_synchrotron_site       NSLS 
_diffrn_source.pdbx_synchrotron_beamline   X8C 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.1000 
# 
_reflns.entry_id                     1OZU 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.d_resolution_high            1.30 
_reflns.d_resolution_low             52.70 
_reflns.number_all                   58507 
_reflns.number_obs                   58507 
_reflns.percent_possible_obs         97.9 
_reflns.pdbx_Rmerge_I_obs            0.05 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        23.70 
_reflns.B_iso_Wilson_estimate        12.6 
_reflns.pdbx_redundancy              4.62 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.30 
_reflns_shell.d_res_low              1.38 
_reflns_shell.percent_possible_all   87.1 
_reflns_shell.Rmerge_I_obs           0.498 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.86 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      5121 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1OZU 
_refine.ls_number_reflns_obs                     55502 
_refine.ls_number_reflns_all                     55502 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             52.70 
_refine.ls_d_res_high                            1.30 
_refine.ls_percent_reflns_obs                    98.61 
_refine.ls_R_factor_obs                          0.17806 
_refine.ls_R_factor_all                          0.17806 
_refine.ls_R_factor_R_work                       0.17722 
_refine.ls_R_factor_R_free                       0.19339 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  2945 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_refine.B_iso_mean                               13.417 
_refine.aniso_B[1][1]                            -0.44 
_refine.aniso_B[2][2]                            0.34 
_refine.aniso_B[3][3]                            0.10 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB Entry 1AZV' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Anisotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.060 
_refine.pdbx_overall_ESU_R_Free                  0.052 
_refine.overall_SU_ML                            0.048 
_refine.overall_SU_B                             2.158 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1997 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             247 
_refine_hist.number_atoms_total               2257 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        52.70 
# 
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 
r_bond_refined_d         0.010  0.021  ? 2034 'X-RAY DIFFRACTION' ? 
r_bond_other_d           0.001  0.020  ? 1794 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      1.541  1.950  ? 2739 'X-RAY DIFFRACTION' ? 
r_angle_other_deg        0.854  3.000  ? 4200 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   4.643  3.000  ? 268  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   19.138 15.000 ? 328  'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.282  0.200  ? 308  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.005  0.020  ? 2299 'X-RAY DIFFRACTION' ? 
r_gen_planes_other       0.003  0.020  ? 365  'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.311  0.300  ? 381  'X-RAY DIFFRACTION' ? 
r_nbd_other              0.225  0.300  ? 1721 'X-RAY DIFFRACTION' ? 
r_nbtor_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.166  0.500  ? 237  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other      ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.265  0.300  ? 16   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other     0.231  0.300  ? 40   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.174  0.500  ? 25   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it              1.021  1.500  ? 1341 'X-RAY DIFFRACTION' ? 
r_mcangle_it             1.762  2.000  ? 2121 'X-RAY DIFFRACTION' ? 
r_scbond_it              2.258  3.000  ? 693  'X-RAY DIFFRACTION' ? 
r_scangle_it             3.586  4.500  ? 618  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr       1.179  2.000  ? 2034 'X-RAY DIFFRACTION' ? 
r_sphericity_free        2.292  2.000  ? 253  'X-RAY DIFFRACTION' ? 
r_sphericity_bonded      1.698  2.000  ? 2007 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.303 
_refine_ls_shell.d_res_low                        1.337 
_refine_ls_shell.number_reflns_R_work             3833 
_refine_ls_shell.R_factor_R_work                  0.234 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.249 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             177 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  1OZU 
_struct.title                     
'Crystal Structure of Familial ALS Mutant S134N of human Cu,Zn Superoxide Dismutase (CuZnSOD) to 1.3A resolution' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1OZU 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'beta barrel, amyloid-like linear filaments, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               
;The biological assembly is a homodimer.  
There is one homodimer in asymmetric unit.
;
_struct_biol.pdbx_parent_biol_id   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 55 ? ALA A 60 ? ALA A 55  ALA A 60  5 ? 6 
HELX_P HELX_P2 2 ALA B 55 ? ALA B 60 ? ALA B 255 ALA B 260 5 ? 6 
# 
_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 
disulf1  disulf ?    ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
disulf2  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 257 B CYS 346 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
covale1  covale both ? A HIS 110 C   ? ? ? 1_555 A CSX 111 N  ? ? A HIS 110 A CSX 111 1_555 ? ? ? ? ? ? ? 1.365 ? ? 
covale2  covale both ? A CSX 111 C   ? ? ? 1_555 A ILE 112 N  ? ? A CSX 111 A ILE 112 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale3  covale none ? B HIS 63  NE2 ? ? ? 1_555 G SO4 .   O1 ? ? B HIS 263 B SO4 401 1_555 ? ? ? ? ? ? ? 1.692 ? ? 
covale4  covale both ? B HIS 110 C   ? ? ? 1_555 B CSX 111 N  ? ? B HIS 310 B CSX 311 1_555 ? ? ? ? ? ? ? 1.362 ? ? 
covale5  covale both ? B CSX 111 C   ? ? ? 1_555 B ILE 112 N  ? ? B CSX 311 B ILE 312 1_555 ? ? ? ? ? ? ? 1.411 ? ? 
metalc1  metalc ?    ? A HIS 46  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 46  A ZN  354 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
metalc2  metalc ?    ? A HIS 48  NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 48  A ZN  354 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc3  metalc ?    ? A HIS 63  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  355 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc4  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  355 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc5  metalc ?    ? A HIS 80  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  355 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc6  metalc ?    ? A ASP 83  OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  355 1_555 ? ? ? ? ? ? ? 2.786 ? ? 
metalc7  metalc ?    ? A ASP 83  OD2 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  355 1_555 ? ? ? ? ? ? ? 1.904 ? ? 
metalc8  metalc ?    ? A HIS 120 NE2 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 120 A ZN  354 1_555 ? ? ? ? ? ? ? 1.952 ? ? 
metalc9  metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 E SO4 .   O4 ? ? A ZN  354 A SO4 402 1_555 ? ? ? ? ? ? ? 2.598 ? ? 
metalc10 metalc ?    ? B HIS 46  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 246 B ZN  356 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc11 metalc ?    ? B HIS 48  NE2 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 248 B ZN  356 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc12 metalc ?    ? B HIS 120 NE2 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 320 B ZN  356 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc13 metalc ?    ? F ZN  .   ZN  ? ? ? 1_555 G SO4 .   O1 ? ? B ZN  356 B SO4 401 1_555 ? ? ? ? ? ? ? 1.835 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 295 ASP B 301 
C 2 VAL B 29  ? LYS B 36  ? VAL B 229 LYS B 236 
C 3 GLN B 15  ? GLU B 21  ? GLN B 215 GLU B 221 
C 4 LYS B 3   ? LEU B 8   ? LYS B 203 LEU B 208 
C 5 GLY B 150 ? GLN B 153 ? GLY B 350 GLN B 353 
D 1 ASP B 83  ? ALA B 89  ? ASP B 283 ALA B 289 
D 2 GLY B 41  ? HIS B 48  ? GLY B 241 HIS B 248 
D 3 THR B 116 ? HIS B 120 ? THR B 316 HIS B 320 
D 4 ARG B 143 ? VAL B 148 ? ARG B 343 VAL B 348 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O GLN A 22  ? O GLN A 22  N THR A 2   ? N THR A 2   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ALA B 95  ? O ALA B 295 N ILE B 35  ? N ILE B 235 
C 2 3 O TRP B 32  ? O TRP B 232 N ASN B 19  ? N ASN B 219 
C 3 4 O GLY B 16  ? O GLY B 216 N LEU B 8   ? N LEU B 208 
C 4 5 N VAL B 5   ? N VAL B 205 O GLY B 150 ? O GLY B 350 
D 1 2 O ALA B 89  ? O ALA B 289 N GLY B 41  ? N GLY B 241 
D 2 3 N HIS B 48  ? N HIS B 248 O THR B 116 ? O THR B 316 
D 3 4 N LEU B 117 ? N LEU B 317 O GLY B 147 ? O GLY B 347 
# 
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 ZN  354 ? 5 'BINDING SITE FOR RESIDUE ZN A 354'  
AC2 Software A ZN  355 ? 4 'BINDING SITE FOR RESIDUE ZN A 355'  
AC3 Software B ZN  356 ? 5 'BINDING SITE FOR RESIDUE ZN B 356'  
AC4 Software B SO4 401 ? 9 'BINDING SITE FOR RESIDUE SO4 B 401' 
AC5 Software A SO4 402 ? 8 'BINDING SITE FOR RESIDUE SO4 A 402' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5 HIS A 46  ? HIS A 46  . ? 1_555 ? 
2  AC1 5 HIS A 48  ? HIS A 48  . ? 1_555 ? 
3  AC1 5 HIS A 63  ? HIS A 63  . ? 1_555 ? 
4  AC1 5 HIS A 120 ? HIS A 120 . ? 1_555 ? 
5  AC1 5 SO4 E .   ? SO4 A 402 . ? 1_555 ? 
6  AC2 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
7  AC2 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
8  AC2 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
9  AC2 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
10 AC3 5 HIS B 46  ? HIS B 246 . ? 1_555 ? 
11 AC3 5 HIS B 48  ? HIS B 248 . ? 1_555 ? 
12 AC3 5 HIS B 63  ? HIS B 263 . ? 1_555 ? 
13 AC3 5 HIS B 120 ? HIS B 320 . ? 1_555 ? 
14 AC3 5 SO4 G .   ? SO4 B 401 . ? 1_555 ? 
15 AC4 9 HIS B 46  ? HIS B 246 . ? 1_555 ? 
16 AC4 9 HIS B 48  ? HIS B 248 . ? 1_555 ? 
17 AC4 9 HIS B 63  ? HIS B 263 . ? 1_555 ? 
18 AC4 9 HIS B 120 ? HIS B 320 . ? 1_555 ? 
19 AC4 9 ARG B 143 ? ARG B 343 . ? 1_555 ? 
20 AC4 9 ZN  F .   ? ZN  B 356 . ? 1_555 ? 
21 AC4 9 HOH I .   ? HOH B 405 . ? 1_555 ? 
22 AC4 9 HOH I .   ? HOH B 428 . ? 1_555 ? 
23 AC4 9 HOH I .   ? HOH B 431 . ? 1_555 ? 
24 AC5 8 HIS A 46  ? HIS A 46  . ? 1_555 ? 
25 AC5 8 HIS A 48  ? HIS A 48  . ? 1_555 ? 
26 AC5 8 HIS A 63  ? HIS A 63  . ? 1_555 ? 
27 AC5 8 HIS A 120 ? HIS A 120 . ? 1_555 ? 
28 AC5 8 THR A 137 ? THR A 137 . ? 1_555 ? 
29 AC5 8 ARG A 143 ? ARG A 143 . ? 1_555 ? 
30 AC5 8 ZN  C .   ? ZN  A 354 . ? 1_555 ? 
31 AC5 8 HOH H .   ? HOH A 408 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1OZU 
_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                    1OZU 
_atom_sites.fract_transf_matrix[1][1]   0.024946 
_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]   0.017713 
_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]   0.009492 
_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  
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   . ALA A 1 1   ? 33.188 19.200  36.478 1.00 23.07 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 32.124 20.249  36.597 1.00 21.74 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 30.751 19.615  36.794 1.00 20.83 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 30.374 18.705  36.052 1.00 21.89 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 32.108 21.147  35.364 1.00 22.38 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 30.074 19.998  37.868 1.00 18.49 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 28.688 19.624  38.092 1.00 16.72 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 27.736 20.285  37.099 1.00 13.90 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 27.822 21.482  36.816 1.00 12.39 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 28.298 19.973  39.514 1.00 17.33 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 29.255 19.402  40.416 1.00 19.76 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 27.006 19.320  39.903 1.00 18.02 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 26.829 19.474  36.579 1.00 12.77 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 25.848 19.912  35.607 1.00 12.46 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 24.451 19.439  35.987 1.00 10.75 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 24.272 18.378  36.596 1.00 10.54 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 26.214 19.372  34.235 1.00 13.50 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 27.496 19.984  33.688 1.00 17.87 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 27.788 19.575  32.260 1.00 22.32 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 29.079 20.222  31.770 1.00 24.76 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 29.555 19.666  30.481 1.00 26.84 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 23.462 20.247  35.636 1.00 9.59  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 22.078 19.912  35.909 1.00 9.18  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 21.244 20.399  34.741 1.00 8.47  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 21.714 21.177  33.895 1.00 9.12  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 21.602 20.533  37.226 1.00 9.08  ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 19.996 19.945  34.683 1.00 8.07  ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 19.091 20.302  33.605 1.00 8.56  ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 17.666 20.287  34.134 1.00 7.96  ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 17.350 19.580  35.098 1.00 8.38  ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 19.269 19.347  32.395 1.00 9.72  ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 18.746 17.962  32.698 1.00 10.67 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 18.613 19.927  31.141 1.00 10.80 ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 16.797 21.054  33.501 1.00 8.44  ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 15.398 21.109  33.878 1.00 8.24  ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 14.548 21.272  32.626 1.00 8.39  ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 14.818 22.156  31.809 1.00 9.28  ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 15.165 22.310  34.774 1.00 8.46  ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 13.484 22.439  35.408 1.00 9.94  ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 13.527 20.441  32.488 1.00 8.27  ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 12.555 20.557  31.411 1.00 9.38  ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 11.304 21.191  31.996 1.00 9.14  ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 10.654 20.630  32.882 1.00 10.29 ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 12.215 19.195  30.812 1.00 10.35 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 11.165 19.333  29.715 1.00 12.19 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 13.447 18.540  30.260 1.00 11.73 ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 10.987 22.391  31.548 1.00 9.75  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 9.805  23.110  32.018 1.00 9.87  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 8.612  22.733  31.162 1.00 10.96 ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 8.688  22.797  29.925 1.00 11.53 ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 10.010 24.627  31.897 1.00 10.70 ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 11.154 25.270  32.672 1.00 13.41 ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 11.517 26.610  31.998 1.00 15.41 ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 10.784 25.496  34.078 1.00 16.67 ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 7.516  22.365  31.823 1.00 11.44 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 6.277  21.983  31.163 1.00 13.47 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 5.125  22.541  31.971 1.00 13.44 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 5.230  22.762  33.170 1.00 12.60 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 6.148  20.455  31.101 1.00 15.23 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 6.553  19.788  29.806 1.00 20.45 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 7.929  20.144  29.342 1.00 23.98 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 8.163  19.650  27.919 1.00 26.08 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 9.458  20.148  27.363 1.00 28.08 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 4.007  22.769  31.299 1.00 14.54 ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 2.810  23.239  31.953 1.00 15.87 ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 1.597  22.724  31.198 1.00 17.51 ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 1.687  21.802  30.374 1.00 18.45 ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 0.464  23.341  31.478 1.00 18.96 ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? -0.804 22.935  30.874 1.00 20.00 ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? -1.043 23.583  29.504 1.00 19.80 ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? -1.942 23.168  28.770 1.00 20.80 ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? -1.947 23.251  31.837 1.00 21.41 ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? -1.869 22.437  33.123 1.00 24.43 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? -1.349 21.300  33.084 1.00 28.46 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? -2.306 22.849  34.220 1.00 28.69 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? -0.227 24.575  29.153 1.00 18.77 ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? -0.364 25.305  27.903 1.00 17.78 ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 0.847  25.150  26.993 1.00 16.72 ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 1.469  24.106  26.971 1.00 16.09 ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 1.158  26.182  26.210 1.00 15.16 ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 2.250  26.145  25.235 1.00 14.50 ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 3.644  26.368  25.801 1.00 13.85 ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 4.628  26.223  25.077 1.00 14.36 ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 1.893  27.322  24.315 1.00 14.09 ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 1.254  28.260  25.207 1.00 15.04 ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 0.400  27.438  26.107 1.00 15.64 ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 3.725  26.738  27.072 1.00 13.22 ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 5.021  27.098  27.638 1.00 13.03 ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 5.853  25.870  27.925 1.00 13.27 ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 5.421  24.967  28.644 1.00 13.67 ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 4.876  27.929  28.901 1.00 12.92 ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 6.262  28.326  29.424 1.00 13.11 ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 4.032  29.169  28.639 1.00 13.88 ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 7.047  25.819  27.363 1.00 14.01 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 7.919  24.669  27.554 1.00 15.01 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 9.348  25.112  27.287 1.00 14.55 ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 9.588  26.025  26.503 1.00 15.70 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 7.520  23.511  26.639 1.00 16.16 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 7.613  23.798  25.153 1.00 19.76 ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 7.044  22.650  24.322 1.00 24.56 ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 5.970  22.125  24.633 1.00 27.66 ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 7.770  22.246  23.281 1.00 26.59 ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 10.312 24.493  27.948 1.00 13.36 ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 11.681 24.911  27.750 1.00 12.90 ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 12.646 23.929  28.352 1.00 12.03 ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 12.259 22.994  29.062 1.00 12.19 ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 13.911 24.150  28.039 1.00 11.42 ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 15.005 23.362  28.578 1.00 11.42 ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 16.019 24.344  29.125 1.00 11.15 ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 16.490 25.223  28.404 1.00 11.30 ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 15.653 22.494  27.492 1.00 12.33 ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 14.662 21.448  26.972 1.00 14.02 ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 16.945 21.883  28.030 1.00 12.82 ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 15.159 20.668  25.781 1.00 16.32 ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 16.360 24.201  30.402 1.00 10.49 ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 17.343 25.052  31.068 1.00 10.19 ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 18.458 24.201  31.631 1.00 9.82  ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 18.215 23.233  32.354 1.00 10.07 ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 16.694 25.855  32.203 1.00 10.20 ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 15.567 26.756  31.679 1.00 11.53 ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 17.747 26.657  32.957 1.00 10.19 ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 16.027 27.857  30.710 1.00 13.27 ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 19.683 24.550  31.272 1.00 10.01 ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 20.889 23.884  31.732 1.00 10.16 ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 21.560 24.689  32.827 1.00 9.66  ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 21.438 25.907  32.887 1.00 10.61 ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 21.869 23.764  30.576 1.00 11.05 ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 21.259 23.116  29.384 1.00 13.05 ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 21.154 21.900  29.319 1.00 15.13 ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 20.849 23.919  28.422 1.00 14.01 ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 22.278 23.981  33.693 1.00 9.70  ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 23.043 24.561  34.776 1.00 9.56  ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 24.433 23.945  34.787 1.00 9.81  ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 24.594 22.748  34.568 1.00 10.27 ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 22.413 24.210  36.120 1.00 9.40  ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 20.997 24.681  36.289 1.00 10.46 ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 19.944 23.930  35.812 1.00 11.30 ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 20.709 25.854  36.967 1.00 10.95 ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 18.630 24.365  35.989 1.00 11.25 ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 19.381 26.274  37.147 1.00 12.01 ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 18.370 25.514  36.662 1.00 11.83 ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 25.434 24.769  35.062 1.00 10.04 ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 26.790 24.264  35.194 1.00 10.93 ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 27.524 25.043  36.275 1.00 10.56 ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 27.450 26.268  36.323 1.00 11.52 ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 27.539 24.365  33.865 1.00 12.03 ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 28.992 23.918  33.917 1.00 15.62 ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 29.619 23.837  32.542 1.00 20.37 ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 30.862 23.801  32.460 1.00 24.01 ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 28.866 23.800  31.548 1.00 22.95 ? 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 28.245 24.317  37.129 1.00 10.80 ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 29.042 24.920  38.199 1.00 11.37 ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 30.412 24.250  38.207 1.00 12.92 ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 30.511 23.066  38.467 1.00 13.90 ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 28.345 24.733  39.541 1.00 11.16 ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 28.984 25.522  40.657 1.00 10.90 ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 28.278 25.320  41.980 1.00 10.35 ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 27.662 24.272  42.205 1.00 11.79 ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 28.377 26.304  42.872 1.00 11.63 ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 31.456 25.018  37.910 1.00 13.64 ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 32.819 24.490  37.816 1.00 15.52 ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 33.460 24.163  39.162 1.00 15.81 ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 34.253 23.237  39.243 1.00 17.37 ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 33.707 25.469  37.036 1.00 16.36 ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 33.295 25.669  35.585 1.00 20.34 ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 34.356 26.446  34.806 1.00 23.67 ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 33.899 26.803  33.400 1.00 26.11 ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 34.964 27.491  32.608 1.00 28.48 ? 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 33.145 24.934  40.191 1.00 15.70 ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 33.659 24.658  41.528 1.00 16.06 ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 32.576 24.958  42.547 1.00 15.19 ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 31.718 25.807  42.334 1.00 14.07 ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 34.940 25.437  41.821 1.00 17.62 ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 34.840 26.923  41.609 1.00 21.33 ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 36.148 27.498  41.112 1.00 26.38 ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 36.337 27.580  39.872 1.00 30.08 ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 36.997 27.847  41.959 1.00 29.30 ? 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 32.606 24.248  43.663 1.00 14.67 ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 31.532 24.372  44.643 1.00 15.62 ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 31.365 25.773  45.216 1.00 17.06 ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 30.268 26.123  45.658 1.00 18.30 ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 31.711 23.347  45.768 1.00 15.69 ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 32.873 23.598  46.527 1.00 15.63 ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 32.427 26.566  45.183 1.00 18.51 ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 32.403 27.931  45.685 1.00 20.13 ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 32.150 28.954  44.591 1.00 19.98 ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 32.160 30.156  44.854 1.00 21.50 ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 33.746 28.239  46.350 1.00 21.17 ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 34.930 27.852  45.469 1.00 23.83 ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 35.190 26.654  45.215 1.00 26.65 ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 35.644 28.860  44.981 1.00 27.66 ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 31.911 28.477  43.374 1.00 18.88 ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 31.778 29.349  42.226 1.00 17.64 ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 30.351 29.565  41.767 1.00 16.54 ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 29.412 28.960  42.263 1.00 15.89 ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 30.192 30.457  40.800 1.00 15.83 ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 28.878 30.746  40.240 1.00 15.26 ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 28.360 29.596  39.392 1.00 13.93 ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 29.088 28.753  38.882 1.00 14.02 ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 29.141 31.977  39.374 1.00 16.07 ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 30.535 31.823  38.975 1.00 17.03 ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 31.240 31.288  40.177 1.00 16.30 ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 27.048 29.590  39.249 1.00 13.24 ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 26.356 28.634  38.417 1.00 12.28 ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 25.921 29.346  37.139 1.00 11.92 ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 25.295 30.398  37.203 1.00 12.78 ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 25.107 28.102  39.138 1.00 11.83 ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 24.398 27.092  38.270 1.00 11.72 ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 25.464 27.482  40.494 1.00 12.31 ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 26.298 28.780  36.005 1.00 12.07 ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 25.872 29.276  34.692 1.00 13.15 ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 24.521 28.620  34.439 1.00 13.03 ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 24.377 27.404  34.611 1.00 12.75 ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 26.866 28.853  33.606 1.00 14.71 ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 26.917 29.701  32.326 1.00 19.37 ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 25.598 30.179  31.811 1.00 23.74 ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 25.803 31.105  30.625 1.00 25.62 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 26.785 30.519  29.644 1.00 27.09 ? 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 23.533 29.427  34.044 1.00 12.51 ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 22.178 28.967  33.735 1.00 12.53 ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 21.875 29.375  32.297 1.00 12.70 ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 21.977 30.561  31.957 1.00 14.22 ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 21.174 29.625  34.663 1.00 12.35 ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 19.758 29.073  34.445 1.00 13.90 ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 21.618 29.471  36.093 1.00 12.44 ? 31  VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? 21.549 28.423  31.435 1.00 12.25 ? 32  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? 21.290 28.781  30.047 1.00 12.27 ? 32  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? 20.363 27.810  29.358 1.00 11.95 ? 32  TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? 20.342 26.620  29.649 1.00 12.00 ? 32  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? 22.609 28.898  29.272 1.00 12.78 ? 32  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 23.218 27.610  28.835 1.00 13.53 ? 32  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 23.199 27.077  27.577 1.00 14.22 ? 32  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 23.976 26.693  29.636 1.00 12.80 ? 32  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 23.886 25.890  27.546 1.00 15.01 ? 32  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 24.367 25.627  28.802 1.00 14.17 ? 32  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? 24.355 26.657  30.983 1.00 14.02 ? 32  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 25.118 24.553  29.267 1.00 14.37 ? 32  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 25.093 25.587  31.439 1.00 14.65 ? 32  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 25.477 24.560  30.582 1.00 13.97 ? 32  TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? 19.599 28.330  28.410 1.00 12.07 ? 33  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? 18.694 27.511  27.633 1.00 11.96 ? 33  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? 17.648 28.418  27.038 1.00 12.26 ? 33  GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? 17.878 29.610  26.820 1.00 12.07 ? 33  GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? 16.469 27.877  26.777 1.00 13.11 ? 34  SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? 15.411 28.706  26.221 1.00 14.19 ? 34  SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? 14.065 28.206  26.690 1.00 14.10 ? 34  SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? 13.909 27.036  27.080 1.00 14.50 ? 34  SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? 15.480 28.744  24.693 1.00 15.83 ? 34  SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? 15.164 27.491  24.135 1.00 18.84 ? 34  SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? 13.122 29.128  26.704 1.00 14.29 ? 35  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? 11.739 28.841  27.054 1.00 13.76 ? 35  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? 10.883 29.398  25.935 1.00 14.40 ? 35  ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? 11.025 30.581  25.586 1.00 15.11 ? 35  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? 11.340 29.526  28.353 1.00 13.65 ? 35  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? 12.333 29.187  29.466 1.00 13.78 ? 35  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? 9.918  29.125  28.761 1.00 13.54 ? 35  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? 12.194 30.053  30.655 1.00 14.39 ? 35  ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? 10.004 28.555  25.395 1.00 13.70 ? 36  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? 9.102  28.917  24.305 1.00 14.21 ? 36  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? 7.669  29.025  24.821 1.00 13.21 ? 36  LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? 7.340  28.610  25.939 1.00 13.42 ? 36  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? 9.178  27.862  23.200 1.00 15.82 ? 36  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? 10.589 27.625  22.703 1.00 19.38 ? 36  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? 10.635 26.503  21.694 1.00 23.13 ? 36  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? 11.958 26.475  20.935 1.00 25.21 ? 36  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? 11.945 25.469  19.828 1.00 27.39 ? 36  LYS A NZ  1 
ATOM   267  N  N   . GLY A 1 37  ? 6.804  29.576  23.979 1.00 12.21 ? 37  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 37  ? 5.386  29.685  24.285 1.00 11.72 ? 37  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 37  ? 4.968  30.808  25.204 1.00 11.83 ? 37  GLY A C   1 
ATOM   270  O  O   . GLY A 1 37  ? 3.841  30.818  25.716 1.00 12.16 ? 37  GLY A O   1 
ATOM   271  N  N   . LEU A 1 38  ? 5.869  31.749  25.441 1.00 11.66 ? 38  LEU A N   1 
ATOM   272  C  CA  . LEU A 1 38  ? 5.608  32.860  26.313 1.00 11.80 ? 38  LEU A CA  1 
ATOM   273  C  C   . LEU A 1 38  ? 5.089  34.085  25.580 1.00 12.65 ? 38  LEU A C   1 
ATOM   274  O  O   . LEU A 1 38  ? 5.342  34.256  24.393 1.00 12.74 ? 38  LEU A O   1 
ATOM   275  C  CB  . LEU A 1 38  ? 6.917  33.274  27.007 1.00 12.05 ? 38  LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 38  ? 7.555  32.278  27.983 1.00 11.85 ? 38  LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 38  ? 9.010  32.669  28.287 1.00 12.37 ? 38  LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 38  ? 6.736  32.196  29.265 1.00 12.64 ? 38  LEU A CD2 1 
ATOM   279  N  N   . THR A 1 39  ? 4.399  34.948  26.304 1.00 12.47 ? 39  THR A N   1 
ATOM   280  C  CA  . THR A 1 39  ? 4.078  36.251  25.745 1.00 13.78 ? 39  THR A CA  1 
ATOM   281  C  C   . THR A 1 39  ? 5.381  37.045  25.665 1.00 14.46 ? 39  THR A C   1 
ATOM   282  O  O   . THR A 1 39  ? 6.270  36.931  26.509 1.00 14.98 ? 39  THR A O   1 
ATOM   283  C  CB  . THR A 1 39  ? 3.082  37.027  26.606 1.00 13.49 ? 39  THR A CB  1 
ATOM   284  O  OG1 . THR A 1 39  ? 3.549  37.091  27.963 1.00 14.44 ? 39  THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 39  ? 1.708  36.348  26.669 1.00 14.95 ? 39  THR A CG2 1 
ATOM   286  N  N   . GLU A 1 40  ? 5.498  37.871  24.642 1.00 14.75 ? 40  GLU A N   1 
ATOM   287  C  CA  . GLU A 1 40  ? 6.667  38.717  24.477 1.00 15.00 ? 40  GLU A CA  1 
ATOM   288  C  C   . GLU A 1 40  ? 6.854  39.548  25.742 1.00 14.53 ? 40  GLU A C   1 
ATOM   289  O  O   . GLU A 1 40  ? 5.892  40.040  26.329 1.00 15.90 ? 40  GLU A O   1 
ATOM   290  C  CB  . GLU A 1 40  ? 6.475  39.621  23.251 1.00 15.65 ? 40  GLU A CB  1 
ATOM   291  C  CG  . GLU A 1 40  ? 7.638  40.571  22.983 1.00 17.57 ? 40  GLU A CG  1 
ATOM   292  C  CD  . GLU A 1 40  ? 7.465  41.397  21.712 1.00 20.22 ? 40  GLU A CD  1 
ATOM   293  O  OE1 . GLU A 1 40  ? 6.390  41.323  21.081 1.00 21.51 ? 40  GLU A OE1 1 
ATOM   294  O  OE2 . GLU A 1 40  ? 8.419  42.114  21.342 1.00 24.52 ? 40  GLU A OE2 1 
ATOM   295  N  N   . GLY A 1 41  ? 8.099  39.708  26.186 1.00 14.19 ? 41  GLY A N   1 
ATOM   296  C  CA  . GLY A 1 41  ? 8.347  40.502  27.370 1.00 14.15 ? 41  GLY A CA  1 
ATOM   297  C  C   . GLY A 1 41  ? 8.889  39.726  28.569 1.00 14.24 ? 41  GLY A C   1 
ATOM   298  O  O   . GLY A 1 41  ? 9.387  38.606  28.438 1.00 13.94 ? 41  GLY A O   1 
ATOM   299  N  N   . LEU A 1 42  ? 8.763  40.342  29.738 1.00 13.98 ? 42  LEU A N   1 
ATOM   300  C  CA  . LEU A 1 42  ? 9.375  39.835  30.961 1.00 14.65 ? 42  LEU A CA  1 
ATOM   301  C  C   . LEU A 1 42  ? 8.538  38.791  31.661 1.00 14.30 ? 42  LEU A C   1 
ATOM   302  O  O   . LEU A 1 42  ? 7.318  38.911  31.757 1.00 15.15 ? 42  LEU A O   1 
ATOM   303  C  CB  . LEU A 1 42  ? 9.593  40.975  31.946 1.00 15.11 ? 42  LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 42  ? 10.549 42.083  31.503 1.00 17.25 ? 42  LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 42  ? 10.438 43.276  32.416 1.00 19.64 ? 42  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 42  ? 11.974 41.581  31.494 1.00 18.54 ? 42  LEU A CD2 1 
ATOM   307  N  N   . HIS A 1 43  ? 9.230  37.779  32.192 1.00 13.31 ? 43  HIS A N   1 
ATOM   308  C  CA  . HIS A 1 43  ? 8.614  36.699  32.977 1.00 12.68 ? 43  HIS A CA  1 
ATOM   309  C  C   . HIS A 1 43  ? 9.463  36.333  34.186 1.00 12.25 ? 43  HIS A C   1 
ATOM   310  O  O   . HIS A 1 43  ? 10.642 36.066  34.036 1.00 12.00 ? 43  HIS A O   1 
ATOM   311  C  CB  . HIS A 1 43  ? 8.446  35.483  32.082 1.00 12.48 ? 43  HIS A CB  1 
ATOM   312  C  CG  . HIS A 1 43  ? 7.497  35.729  30.959 1.00 12.19 ? 43  HIS A CG  1 
ATOM   313  N  ND1 . HIS A 1 43  ? 6.144  35.523  31.090 1.00 13.43 ? 43  HIS A ND1 1 
ATOM   314  C  CD2 . HIS A 1 43  ? 7.687  36.244  29.719 1.00 11.47 ? 43  HIS A CD2 1 
ATOM   315  C  CE1 . HIS A 1 43  ? 5.541  35.875  29.968 1.00 13.91 ? 43  HIS A CE1 1 
ATOM   316  N  NE2 . HIS A 1 43  ? 6.454  36.311  29.120 1.00 13.55 ? 43  HIS A NE2 1 
ATOM   317  N  N   . GLY A 1 44  ? 8.868  36.344  35.367 1.00 11.87 ? 44  GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? 9.563  35.962  36.588 1.00 11.76 ? 44  GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? 10.116 34.547  36.495 1.00 10.99 ? 44  GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? 9.546  33.662  35.866 1.00 10.58 ? 44  GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? 11.268 34.341  37.128 1.00 10.51 ? 45  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? 12.016 33.091  36.981 1.00 10.55 ? 45  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? 12.591 32.713  38.333 1.00 10.18 ? 45  PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? 13.471 33.399  38.837 1.00 10.26 ? 45  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? 13.121 33.362  35.967 1.00 10.93 ? 45  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? 13.819 32.151  35.406 1.00 10.91 ? 45  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? 13.131 31.078  34.856 1.00 12.49 ? 45  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? 15.202 32.138  35.352 1.00 11.79 ? 45  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? 13.825 30.012  34.280 1.00 12.36 ? 45  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? 15.879 31.083  34.775 1.00 11.59 ? 45  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? 15.196 30.033  34.245 1.00 11.60 ? 45  PHE A CZ  1 
ATOM   332  N  N   . HIS A 1 46  ? 12.100 31.617  38.920 1.00 9.53  ? 46  HIS A N   1 
ATOM   333  C  CA  . HIS A 1 46  ? 12.466 31.273  40.287 1.00 9.90  ? 46  HIS A CA  1 
ATOM   334  C  C   . HIS A 1 46  ? 12.679 29.791  40.529 1.00 9.11  ? 46  HIS A C   1 
ATOM   335  O  O   . HIS A 1 46  ? 12.060 28.947  39.875 1.00 9.67  ? 46  HIS A O   1 
ATOM   336  C  CB  . HIS A 1 46  ? 11.357 31.636  41.264 1.00 11.66 ? 46  HIS A CB  1 
ATOM   337  C  CG  . HIS A 1 46  ? 10.787 33.001  41.084 1.00 12.44 ? 46  HIS A CG  1 
ATOM   338  N  ND1 . HIS A 1 46  ? 9.431  33.209  40.964 1.00 15.38 ? 46  HIS A ND1 1 
ATOM   339  C  CD2 . HIS A 1 46  ? 11.369 34.222  41.061 1.00 13.17 ? 46  HIS A CD2 1 
ATOM   340  C  CE1 . HIS A 1 46  ? 9.207  34.508  40.842 1.00 15.67 ? 46  HIS A CE1 1 
ATOM   341  N  NE2 . HIS A 1 46  ? 10.365 35.144  40.896 1.00 14.19 ? 46  HIS A NE2 1 
ATOM   342  N  N   . VAL A 1 47  ? 13.539 29.493  41.495 1.00 8.90  ? 47  VAL A N   1 
ATOM   343  C  CA  . VAL A 1 47  ? 13.650 28.136  42.019 1.00 8.57  ? 47  VAL A CA  1 
ATOM   344  C  C   . VAL A 1 47  ? 12.743 28.109  43.239 1.00 8.35  ? 47  VAL A C   1 
ATOM   345  O  O   . VAL A 1 47  ? 12.894 28.940  44.140 1.00 9.16  ? 47  VAL A O   1 
ATOM   346  C  CB  . VAL A 1 47  ? 15.088 27.752  42.411 1.00 8.55  ? 47  VAL A CB  1 
ATOM   347  C  CG1 . VAL A 1 47  ? 15.109 26.343  42.953 1.00 8.19  ? 47  VAL A CG1 1 
ATOM   348  C  CG2 . VAL A 1 47  ? 16.010 27.874  41.245 1.00 9.62  ? 47  VAL A CG2 1 
ATOM   349  N  N   . HIS A 1 48  ? 11.787 27.186  43.235 1.00 8.59  ? 48  HIS A N   1 
ATOM   350  C  CA  . HIS A 1 48  ? 10.870 26.967  44.335 1.00 8.28  ? 48  HIS A CA  1 
ATOM   351  C  C   . HIS A 1 48  ? 11.355 25.786  45.191 1.00 9.12  ? 48  HIS A C   1 
ATOM   352  O  O   . HIS A 1 48  ? 12.117 24.960  44.737 1.00 9.92  ? 48  HIS A O   1 
ATOM   353  C  CB  . HIS A 1 48  ? 9.449  26.768  43.824 1.00 8.63  ? 48  HIS A CB  1 
ATOM   354  C  CG  . HIS A 1 48  ? 8.803  28.040  43.329 1.00 9.95  ? 48  HIS A CG  1 
ATOM   355  N  ND1 . HIS A 1 48  ? 7.664  28.568  43.899 1.00 11.77 ? 48  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A 1 48  ? 9.153  28.894  42.330 1.00 10.94 ? 48  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A 1 48  ? 7.339  29.688  43.268 1.00 12.95 ? 48  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A 1 48  ? 8.220  29.907  42.307 1.00 12.45 ? 48  HIS A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? 10.884 25.705  46.422 1.00 9.12  ? 49  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? 11.448 24.810  47.420 1.00 9.49  ? 49  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? 11.387 23.309  47.134 1.00 9.20  ? 49  GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? 12.363 22.595  47.359 1.00 10.45 ? 49  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? 10.778 25.105  48.762 1.00 10.90 ? 49  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? 11.366 24.342  49.923 1.00 12.86 ? 49  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? 10.793 24.764  51.255 1.00 15.91 ? 49  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? 9.877  25.598  51.260 1.00 16.76 ? 49  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? 11.268 24.238  52.287 1.00 19.16 ? 49  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? 10.248 22.832  46.670 1.00 8.66  ? 50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 10.040 21.396  46.546 1.00 8.40  ? 50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 10.037 20.927  45.120 1.00 8.24  ? 50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 9.414  21.561  44.246 1.00 8.58  ? 50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 8.718  20.986  47.202 1.00 8.72  ? 50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 8.580  21.438  48.628 1.00 10.83 ? 50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 9.427  20.953  49.593 1.00 11.87 ? 50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 7.604  22.355  48.989 1.00 12.30 ? 50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 9.312  21.397  50.919 1.00 14.20 ? 50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 7.492  22.812  50.296 1.00 13.86 ? 50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 8.347  22.330  51.247 1.00 14.44 ? 50  PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? 10.702 19.808  44.873 1.00 7.67  ? 51  GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? 10.656 19.138  43.577 1.00 7.65  ? 51  GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? 9.439  18.229  43.474 1.00 7.18  ? 51  GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? 9.522  17.055  43.098 1.00 7.75  ? 51  GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? 8.285  18.788  43.834 1.00 8.40  ? 52  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? 7.027  18.054  43.898 1.00 8.01  ? 52  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? 6.107  18.593  42.824 1.00 8.45  ? 52  ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? 5.589  19.714  42.933 1.00 8.39  ? 52  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? 6.410  18.239  45.284 1.00 8.04  ? 52  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? 5.159  17.455  45.482 1.00 8.87  ? 52  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? 4.414  17.197  44.516 1.00 8.40  ? 52  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? 4.851  17.051  46.629 1.00 11.08 ? 52  ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? 5.916  17.804  41.780 1.00 8.91  ? 53  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? 5.076  18.216  40.684 1.00 10.49 ? 53  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? 3.789  17.374  40.625 1.00 9.81  ? 53  ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? 3.145  17.247  39.588 1.00 10.23 ? 53  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? 5.895  18.249  39.392 1.00 12.86 ? 53  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? 6.893  19.462  39.334 1.00 15.28 ? 53  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? 7.595  19.624  38.344 1.00 20.01 ? 53  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? 6.959  20.285  40.396 1.00 16.58 ? 53  ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? 3.380  16.844  41.774 1.00 8.83  ? 54  THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? 2.156  16.054  41.850 1.00 9.32  ? 54  THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? 0.906  16.852  41.523 1.00 9.63  ? 54  THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? -0.074 16.290  41.055 1.00 11.11 ? 54  THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? 1.979  15.350  43.207 1.00 9.43  ? 54  THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? 1.923  16.309  44.263 1.00 9.59  ? 54  THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? 3.147  14.404  43.508 1.00 10.39 ? 54  THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? 0.934  18.153  41.778 1.00 9.41  ? 55  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? -0.178 19.025  41.389 1.00 10.29 ? 55  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? 0.364  20.067  40.408 1.00 11.03 ? 55  ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? 0.097  21.259  40.511 1.00 12.39 ? 55  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? -0.782 19.704  42.620 1.00 10.84 ? 55  ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? 1.156  19.620  39.451 1.00 10.67 ? 56  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? 1.758  20.553  38.518 1.00 10.90 ? 56  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? 2.684  21.494  39.267 1.00 10.56 ? 56  GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? 3.396  21.100  40.174 1.00 12.34 ? 56  GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? 2.646  22.771  38.924 1.00 10.72 ? 57  CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? 3.512  23.744  39.563 1.00 10.53 ? 57  CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? 3.000  24.203  40.921 1.00 10.64 ? 57  CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? 3.727  24.803  41.702 1.00 10.66 ? 57  CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? 3.666  24.945  38.642 1.00 11.10 ? 57  CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? 4.285  24.505  36.972 1.00 12.31 ? 57  CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? 1.735  23.898  41.187 1.00 11.04 ? 58  THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? 1.069  24.317  42.406 1.00 12.63 ? 58  THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? 1.698  23.702  43.645 1.00 11.85 ? 58  THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? 1.641  24.304  44.690 1.00 14.47 ? 58  THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? -0.426 23.907  42.326 1.00 13.90 ? 58  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? -0.997 24.410  41.106 1.00 17.40 ? 58  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? -1.270 24.512  43.461 1.00 15.89 ? 58  THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? 2.309  22.519  43.518 1.00 9.61  ? 59  SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? 2.880  21.793  44.639 1.00 9.28  ? 59  SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? 4.358  22.083  44.891 1.00 9.16  ? 59  SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? 4.954  21.482  45.767 1.00 9.49  ? 59  SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? 2.659  20.284  44.427 1.00 9.53  ? 59  SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? 2.871  19.873  43.080 1.00 8.51  ? 59  SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? 4.952  23.012  44.135 1.00 9.61  ? 60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? 6.379  23.336  44.273 1.00 9.79  ? 60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? 6.730  24.138  45.511 1.00 9.47  ? 60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? 7.899  24.306  45.822 1.00 9.94  ? 60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? 6.882  24.071  43.050 1.00 9.95  ? 60  ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? 5.730  24.628  46.224 1.00 10.13 ? 61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? 6.011  25.432  47.399 1.00 11.33 ? 61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? 6.416  26.853  47.072 1.00 11.89 ? 61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? 6.284  27.283  45.936 1.00 11.71 ? 61  GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? 6.948  27.566  48.063 1.00 12.71 ? 62  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? 7.365  28.963  47.872 1.00 13.28 ? 62  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? 8.745  29.069  47.239 1.00 12.62 ? 62  PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? 9.369  28.050  46.934 1.00 12.23 ? 62  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? 7.409  29.487  49.304 1.00 14.22 ? 62  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? 7.883  28.337  50.080 1.00 14.20 ? 62  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? 7.238  27.099  49.434 1.00 13.44 ? 62  PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? 9.244  30.284  47.041 1.00 12.62 ? 63  HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? 10.593 30.454  46.526 1.00 12.55 ? 63  HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? 11.568 29.786  47.489 1.00 12.02 ? 63  HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? 11.429 29.868  48.712 1.00 12.91 ? 63  HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? 10.965 31.932  46.403 1.00 13.17 ? 63  HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? 10.089 32.705  45.473 1.00 13.70 ? 63  HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? 10.283 34.047  45.217 1.00 14.45 ? 63  HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? 9.009  32.331  44.748 1.00 14.78 ? 63  HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? 9.349  34.464  44.381 1.00 14.24 ? 63  HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? 8.571  33.444  44.073 1.00 14.75 ? 63  HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? 12.577 29.128  46.950 1.00 11.02 ? 64  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? 13.585 28.473  47.787 1.00 11.47 ? 64  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? 14.326 29.534  48.595 1.00 12.40 ? 64  PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? 14.908 30.454  48.040 1.00 12.54 ? 64  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? 14.522 27.688  46.877 1.00 10.77 ? 64  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? 15.625 26.949  47.594 1.00 10.52 ? 64  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? 15.393 26.193  48.729 1.00 12.27 ? 64  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? 16.909 27.003  47.107 1.00 10.92 ? 64  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? 16.441 25.505  49.353 1.00 13.31 ? 64  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? 17.938 26.325  47.731 1.00 12.54 ? 64  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? 17.699 25.585  48.852 1.00 12.91 ? 64  PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? 14.332 29.362  49.907 1.00 13.51 ? 65  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? 14.789 30.417  50.805 1.00 15.31 ? 65  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? 15.422 29.838  52.070 1.00 16.77 ? 65  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? 14.912 30.049  53.166 1.00 17.55 ? 65  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? 13.563 31.278  51.160 1.00 15.71 ? 65  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? 13.908 32.540  51.932 1.00 16.58 ? 65  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? 15.019 33.039  51.860 1.00 17.18 ? 65  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? 12.933 33.065  52.669 1.00 19.16 ? 65  ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? 16.565 29.168  51.934 1.00 17.98 ? 66  PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? 17.207 28.521  53.084 1.00 19.41 ? 66  PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? 17.725 29.512  54.120 1.00 20.95 ? 66  PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? 17.823 29.139  55.286 1.00 21.86 ? 66  PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? 18.367 27.751  52.448 1.00 19.49 ? 66  PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? 18.664 28.455  51.204 1.00 18.61 ? 66  PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? 17.373 29.039  50.710 1.00 18.32 ? 66  PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? 18.041 30.738  53.703 1.00 22.16 ? 67  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? 18.565 31.769  54.607 1.00 23.25 ? 67  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? 17.483 32.665  55.220 1.00 23.96 ? 67  LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? 17.802 33.608  55.946 1.00 24.65 ? 67  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? 19.601 32.629  53.872 1.00 23.48 ? 67  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? 20.822 31.867  53.349 1.00 24.84 ? 67  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? 21.758 32.770  52.554 1.00 26.01 ? 67  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? 21.549 31.218  54.513 1.00 25.49 ? 67  LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? 16.215 32.379  54.946 1.00 24.50 ? 68  SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? 15.110 33.141  55.534 1.00 24.98 ? 68  SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? 15.210 34.644  55.257 1.00 25.12 ? 68  SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? 15.024 35.464  56.164 1.00 25.41 ? 68  SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? 15.043 32.897  57.044 1.00 25.47 ? 68  SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? 14.803 31.527  57.314 1.00 26.23 ? 68  SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? 15.498 35.002  54.007 1.00 24.97 ? 69  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? 15.597 36.399  53.605 1.00 24.89 ? 69  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? 14.319 36.856  52.917 1.00 24.17 ? 69  ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? 13.402 36.063  52.694 1.00 23.64 ? 69  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? 16.768 36.597  52.643 1.00 25.45 ? 69  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? 18.115 36.168  53.184 1.00 27.60 ? 69  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? 18.721 37.113  54.205 1.00 30.56 ? 69  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? 19.940 36.527  54.757 1.00 32.96 ? 69  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? 19.998 35.817  55.879 1.00 34.95 ? 69  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? 18.905 35.613  56.609 1.00 36.04 ? 69  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? 21.158 35.309  56.279 1.00 35.60 ? 69  ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? 14.274 38.143  52.582 1.00 23.28 ? 70  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? 13.144 38.729  51.870 1.00 22.60 ? 70  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? 13.343 38.575  50.361 1.00 21.16 ? 70  LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? 14.470 38.449  49.890 1.00 20.43 ? 70  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? 13.008 40.214  52.220 1.00 23.20 ? 70  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? 12.702 40.497  53.691 1.00 25.40 ? 70  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? 12.304 41.952  53.887 1.00 28.06 ? 70  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? 12.061 42.292  55.344 1.00 29.62 ? 70  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? 11.823 43.755  55.513 1.00 31.29 ? 70  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? 12.241 38.588  49.616 1.00 19.79 ? 71  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? 12.291 38.487  48.163 1.00 18.75 ? 71  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? 13.028 39.678  47.542 1.00 18.74 ? 71  HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? 12.896 40.820  48.011 1.00 18.88 ? 71  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? 10.872 38.418  47.581 1.00 17.89 ? 71  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? 10.852 38.345  46.092 1.00 15.94 ? 71  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? 11.255 37.217  45.408 1.00 14.63 ? 71  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? 10.516 39.262  45.152 1.00 15.31 ? 71  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? 11.179 37.453  44.109 1.00 14.50 ? 71  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? 10.721 38.679  43.928 1.00 14.67 ? 71  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? 13.793 39.421  46.489 1.00 18.51 ? 72  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? 14.498 40.472  45.776 1.00 19.02 ? 72  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? 14.905 40.025  44.387 1.00 19.42 ? 72  GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? 14.452 38.996  43.896 1.00 18.92 ? 72  GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? 15.744 40.824  43.744 1.00 20.11 ? 73  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? 16.291 40.480  42.448 1.00 20.81 ? 73  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? 17.616 39.769  42.650 1.00 21.52 ? 73  GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? 18.163 39.777  43.758 1.00 21.65 ? 73  GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? 18.125 39.146  41.595 1.00 22.49 ? 74  PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 19.367 38.366  41.668 1.00 23.75 ? 74  PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 20.596 39.159  42.121 1.00 24.95 ? 74  PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 21.444 38.597  42.821 1.00 24.67 ? 74  PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 19.540 37.845  40.233 1.00 23.76 ? 74  PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 18.672 38.711  39.402 1.00 23.46 ? 74  PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 17.513 39.082  40.256 1.00 22.85 ? 74  PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? 20.691 40.434  41.752 1.00 26.42 ? 75  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? 21.857 41.235  42.130 1.00 27.80 ? 75  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? 21.665 41.983  43.454 1.00 28.35 ? 75  LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? 22.496 42.815  43.830 1.00 29.01 ? 75  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? 22.248 42.190  40.995 1.00 28.45 ? 75  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? 22.907 41.463  39.825 1.00 30.25 ? 75  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? 23.533 42.405  38.801 1.00 32.51 ? 75  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? 24.748 43.137  39.349 1.00 33.78 ? 75  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? 25.659 43.559  38.239 1.00 35.11 ? 75  LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? 20.584 41.672  44.166 1.00 28.84 ? 76  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? 20.311 42.287  45.464 1.00 29.38 ? 76  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? 20.942 41.475  46.586 1.00 29.57 ? 76  ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? 21.032 40.250  46.504 1.00 29.66 ? 76  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? 18.807 42.377  45.716 1.00 29.64 ? 76  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? 18.125 43.378  44.820 1.00 30.67 ? 76  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? 18.575 44.542  44.779 1.00 32.39 ? 76  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? 17.125 43.092  44.133 1.00 31.66 ? 76  ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? 21.364 42.158  47.645 1.00 29.56 ? 77  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? 21.958 41.485  48.793 1.00 29.43 ? 77  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? 20.877 40.672  49.493 1.00 28.45 ? 77  GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? 21.072 39.493  49.822 1.00 29.03 ? 77  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? 22.570 42.503  49.759 1.00 30.04 ? 77  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? 23.680 43.345  49.150 1.00 31.95 ? 77  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? 24.263 44.352  50.127 1.00 34.53 ? 77  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? 23.831 44.373  51.302 1.00 36.31 ? 77  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? 25.155 45.128  49.716 1.00 36.20 ? 77  GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? 19.732 41.314  49.705 1.00 26.90 ? 78  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? 18.574 40.679  50.314 1.00 25.52 ? 78  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? 17.722 40.048  49.214 1.00 23.63 ? 78  GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? 17.058 40.747  48.449 1.00 23.23 ? 78  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? 17.761 41.715  51.099 1.00 25.91 ? 78  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? 16.577 41.150  51.873 1.00 26.91 ? 78  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? 16.977 40.372  53.113 1.00 28.86 ? 78  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? 18.185 40.289  53.415 1.00 31.03 ? 78  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? 16.075 39.837  53.791 1.00 30.18 ? 78  GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? 17.774 38.721  49.131 1.00 21.53 ? 79  ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? 17.012 37.962  48.145 1.00 19.92 ? 79  ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? 16.858 36.535  48.626 1.00 18.46 ? 79  ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? 17.592 36.072  49.505 1.00 18.62 ? 79  ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? 17.728 37.936  46.793 1.00 19.55 ? 79  ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? 19.111 37.302  46.837 1.00 19.07 ? 79  ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? 19.747 37.075  45.484 1.00 17.65 ? 79  ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? 19.457 35.738  44.973 1.00 16.77 ? 79  ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? 20.080 35.187  43.946 1.00 16.19 ? 79  ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? 21.013 35.863  43.281 1.00 15.89 ? 79  ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? 19.770 33.954  43.568 1.00 15.21 ? 79  ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? 15.900 35.833  48.041 1.00 16.57 ? 80  HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? 15.780 34.410  48.267 1.00 15.61 ? 80  HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? 16.854 33.761  47.417 1.00 14.47 ? 80  HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? 17.194 34.277  46.363 1.00 14.48 ? 80  HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? 14.436 33.912  47.783 1.00 15.47 ? 80  HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? 13.276 34.504  48.513 1.00 14.75 ? 80  HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? 12.078 34.809  47.902 1.00 14.64 ? 80  HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? 13.137 34.853  49.814 1.00 15.38 ? 80  HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? 11.244 35.299  48.805 1.00 14.98 ? 80  HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? 11.864 35.338  49.970 1.00 16.07 ? 80  HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? 17.385 32.625  47.845 1.00 14.35 ? 81  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? 18.331 31.904  47.011 1.00 13.99 ? 81  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? 17.713 31.662  45.630 1.00 12.91 ? 81  VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? 18.386 31.796  44.615 1.00 12.74 ? 81  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? 18.753 30.549  47.656 1.00 14.23 ? 81  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? 19.492 29.653  46.658 1.00 14.49 ? 81  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? 19.634 30.787  48.863 1.00 15.39 ? 81  VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? 16.427 31.327  45.593 1.00 12.82 ? 82  GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? 15.781 31.008  44.330 1.00 12.82 ? 82  GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? 15.388 32.168  43.429 1.00 12.27 ? 82  GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? 14.791 31.921  42.385 1.00 12.69 ? 82  GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? 15.714 33.407  43.809 1.00 11.76 ? 83  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? 15.335 34.587  43.032 1.00 12.14 ? 83  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? 16.264 34.824  41.845 1.00 12.37 ? 83  ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? 17.299 35.474  41.974 1.00 14.29 ? 83  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? 15.336 35.811  43.952 1.00 12.55 ? 83  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? 14.198 35.793  44.948 1.00 13.14 ? 83  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? 14.241 36.546  45.963 1.00 13.66 ? 83  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? 13.211 35.045  44.770 1.00 13.95 ? 83  ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? 15.883 34.309  40.686 1.00 11.76 ? 84  LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? 16.695 34.464  39.479 1.00 12.49 ? 84  LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? 16.197 35.592  38.564 1.00 13.01 ? 84  LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? 16.592 35.676  37.405 1.00 14.39 ? 84  LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? 16.789 33.145  38.711 1.00 12.53 ? 84  LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? 17.573 32.055  39.451 1.00 14.67 ? 84  LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? 17.494 30.764  38.642 1.00 15.34 ? 84  LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? 19.027 32.474  39.740 1.00 15.97 ? 84  LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? 15.326 36.443  39.088 1.00 12.74 ? 85  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? 14.898 37.619  38.339 1.00 12.93 ? 85  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? 13.872 37.344  37.250 1.00 13.33 ? 85  GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? 12.866 36.680  37.474 1.00 13.79 ? 85  GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? 14.121 37.904  36.073 1.00 12.69 ? 86  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? 13.232 37.760  34.928 1.00 13.33 ? 86  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? 13.958 37.322  33.688 1.00 13.28 ? 86  ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? 15.129 37.628  33.498 1.00 14.42 ? 86  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? 12.579 39.107  34.582 1.00 13.34 ? 86  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? 11.624 39.588  35.643 1.00 14.11 ? 86  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? 10.549 39.051  35.804 1.00 15.60 ? 86  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? 12.002 40.644  36.352 1.00 16.96 ? 86  ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? 13.246 36.598  32.837 1.00 12.23 ? 87  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? 13.715 36.270  31.502 1.00 12.56 ? 87  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? 12.859 37.096  30.530 1.00 12.98 ? 87  VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? 11.781 37.546  30.902 1.00 13.67 ? 87  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? 13.609 34.764  31.222 1.00 12.28 ? 87  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? 14.419 33.983  32.246 1.00 13.37 ? 87  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? 12.157 34.316  31.211 1.00 14.14 ? 87  VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? 13.345 37.281  29.304 1.00 12.85 ? 88  THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? 12.635 38.081  28.299 1.00 13.66 ? 88  THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? 12.364 37.285  27.038 1.00 12.93 ? 88  THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? 13.281 36.756  26.427 1.00 14.07 ? 88  THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? 13.481 39.309  27.938 1.00 14.59 ? 88  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? 13.796 40.032  29.130 1.00 17.39 ? 88  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? 12.679 40.293  27.091 1.00 16.20 ? 88  THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? 11.087 37.212  26.643 1.00 12.26 ? 89  ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? 10.693 36.489  25.433 1.00 12.14 ? 89  ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? 10.622 37.433  24.228 1.00 12.04 ? 89  ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? 10.192 38.557  24.386 1.00 12.79 ? 89  ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? 9.336  35.819  25.646 1.00 12.05 ? 89  ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? 11.070 36.948  23.069 1.00 12.09 ? 90  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? 11.004 37.681  21.801 1.00 12.66 ? 90  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? 9.557  37.632  21.239 1.00 13.77 ? 90  ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? 8.635  37.113  21.876 1.00 13.71 ? 90  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? 12.070 37.143  20.819 1.00 12.69 ? 90  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? 11.769 35.770  20.288 1.00 12.90 ? 90  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? 12.662 35.154  19.652 1.00 13.53 ? 90  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? 10.641 35.243  20.400 1.00 12.99 ? 90  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? 9.344  38.216  20.062 1.00 14.52 ? 91  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? 8.006  38.315  19.471 1.00 16.02 ? 91  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? 7.433  36.964  19.073 1.00 15.78 ? 91  LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? 6.231  36.856  18.806 1.00 16.78 ? 91  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? 8.039  39.222  18.242 1.00 16.67 ? 91  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? 8.797  38.628  17.096 1.00 20.08 ? 91  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? 8.758  39.538  15.889 1.00 23.92 ? 91  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? 9.465  38.905  14.712 1.00 25.94 ? 91  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? 9.283  39.734  13.475 1.00 27.73 ? 91  LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? 8.283  35.948  18.984 1.00 15.16 ? 92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? 7.842  34.584  18.702 1.00 15.20 ? 92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? 7.589  33.795  20.003 1.00 14.49 ? 92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? 7.321  32.606  19.951 1.00 14.66 ? 92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 8.879  33.837  17.854 1.00 15.80 ? 92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 8.905  34.289  16.410 1.00 18.17 ? 92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 7.941  34.952  15.964 1.00 19.42 ? 92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 9.861  34.013  15.654 1.00 20.08 ? 92  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? 7.713  34.454  21.147 1.00 13.90 ? 93  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? 7.485  33.789  22.432 1.00 13.08 ? 93  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? 8.671  33.010  22.982 1.00 12.73 ? 93  GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? 8.509  32.238  23.928 1.00 12.70 ? 93  GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? 9.852  33.224  22.412 1.00 12.87 ? 94  VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? 11.059 32.517  22.826 1.00 12.71 ? 94  VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? 11.932 33.395  23.709 1.00 12.94 ? 94  VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? 12.359 34.474  23.285 1.00 13.31 ? 94  VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? 11.893 32.059  21.606 1.00 13.31 ? 94  VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? 13.134 31.310  22.060 1.00 13.70 ? 94  VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? 11.059 31.202  20.688 1.00 13.59 ? 94  VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? 12.183 32.926  24.935 1.00 12.42 ? 95  ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? 13.068 33.611  25.870 1.00 13.10 ? 95  ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? 14.387 32.881  25.936 1.00 13.13 ? 95  ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? 14.445 31.724  26.340 1.00 15.01 ? 95  ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? 12.464 33.665  27.274 1.00 13.15 ? 95  ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? 15.447 33.553  25.519 1.00 13.16 ? 96  ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? 16.777 33.005  25.621 1.00 13.13 ? 96  ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? 17.298 33.320  26.997 1.00 13.43 ? 96  ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? 17.289 34.476  27.427 1.00 15.03 ? 96  ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 17.677 33.636  24.577 1.00 13.55 ? 96  ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 19.063 33.061  24.594 1.00 15.66 ? 96  ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 19.189 31.835  24.432 1.00 18.29 ? 96  ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 20.069 33.784  24.753 1.00 18.80 ? 96  ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? 17.742 32.288  27.703 1.00 13.23 ? 97  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? 18.197 32.464  29.068 1.00 13.83 ? 97  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? 19.695 32.316  29.141 1.00 13.65 ? 97  VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? 20.247 31.342  28.671 1.00 12.74 ? 97  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? 17.542 31.431  30.000 1.00 13.71 ? 97  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? 17.985 31.656  31.450 1.00 14.17 ? 97  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? 16.029 31.505  29.868 1.00 14.67 ? 97  VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? 20.343 33.318  29.707 1.00 16.07 ? 98  SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? 21.782 33.291  29.900 1.00 17.55 ? 98  SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? 22.034 34.077  31.178 1.00 18.28 ? 98  SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? 22.030 35.313  31.191 1.00 19.85 ? 98  SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? 22.517 33.877  28.694 1.00 18.19 ? 98  SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 23.904 33.571  28.738 1.00 20.11 ? 98  SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? 22.215 33.346  32.270 1.00 18.50 ? 99  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? 22.367 33.927  33.588 1.00 18.52 ? 99  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? 23.622 33.320  34.217 1.00 18.19 ? 99  ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? 24.009 32.191  33.905 1.00 17.69 ? 99  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? 21.111 33.597  34.482 1.00 18.81 ? 99  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? 19.841 34.276  33.945 1.00 19.49 ? 99  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? 21.332 34.056  35.905 1.00 20.49 ? 99  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? 18.564 33.975  34.760 1.00 20.79 ? 99  ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? 24.278 34.092  35.070 1.00 17.93 ? 100 GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? 25.374 33.587  35.874 1.00 18.25 ? 100 GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? 25.004 34.023  37.279 1.00 17.31 ? 100 GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? 24.795 35.205  37.532 1.00 18.00 ? 100 GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? 26.708 34.179  35.434 1.00 19.36 ? 100 GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? 27.894 33.490  36.062 1.00 23.05 ? 100 GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? 28.963 33.170  35.044 1.00 27.36 ? 100 GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? 28.659 32.450  34.062 1.00 30.24 ? 100 GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? 30.100 33.642  35.225 1.00 30.85 ? 100 GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? 24.882 33.074  38.200 1.00 16.38 ? 101 ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? 24.451 33.405  39.547 1.00 16.28 ? 101 ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? 25.337 32.774  40.614 1.00 16.56 ? 101 ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? 25.626 31.585  40.560 1.00 16.69 ? 101 ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? 22.999 32.991  39.758 1.00 16.03 ? 101 ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? 22.411 33.627  40.970 1.00 17.15 ? 101 ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? 22.348 32.965  42.026 1.00 15.63 ? 101 ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? 22.035 34.823  40.977 1.00 20.72 ? 101 ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? 25.741 33.557  41.607 1.00 16.79 ? 102 SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? 26.644 33.045  42.639 1.00 17.50 ? 102 SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? 25.951 32.714  43.953 1.00 16.56 ? 102 SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? 26.608 32.329  44.918 1.00 17.92 ? 102 SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? 27.758 34.048  42.916 1.00 18.34 ? 102 SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? 27.211 35.208  43.485 1.00 21.88 ? 102 SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? 24.628 32.827  43.995 1.00 15.32 ? 103 VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? 23.866 32.517  45.197 1.00 14.77 ? 103 VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? 23.295 31.079  45.128 1.00 13.93 ? 103 VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? 23.375 30.332  46.098 1.00 14.38 ? 103 VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? 22.767 33.569  45.452 1.00 15.21 ? 103 VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? 21.929 33.183  46.633 1.00 15.07 ? 103 VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? 23.391 34.942  45.683 1.00 15.78 ? 103 VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? 22.700 30.691  44.006 1.00 12.83 ? 104 ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? 22.310 29.291  43.838 1.00 12.16 ? 104 ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? 23.571 28.433  43.786 1.00 11.84 ? 104 ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? 24.665 28.946  43.502 1.00 12.27 ? 104 ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? 21.483 29.080  42.546 1.00 12.45 ? 104 ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? 22.233 29.563  41.301 1.00 13.37 ? 104 ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? 20.085 29.712  42.690 1.00 12.24 ? 104 ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? 21.575 29.164  39.994 1.00 14.05 ? 104 ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? 23.427 27.132  44.030 1.00 11.05 ? 105 SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? 24.557 26.213  43.954 1.00 11.03 ? 105 SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? 24.052 24.861  43.499 1.00 10.44 ? 105 SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? 22.853 24.586  43.572 1.00 10.05 ? 105 SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? 25.260 26.076  45.307 1.00 11.23 ? 105 SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? 26.489 25.384  45.164 1.00 12.07 ? 105 SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? 24.973 24.029  43.025 1.00 10.45 ? 106 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? 24.658 22.641  42.698 1.00 10.71 ? 106 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? 25.197 21.690  43.767 1.00 12.35 ? 106 LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? 25.188 20.478  43.573 1.00 13.56 ? 106 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? 25.152 22.247  41.305 1.00 10.44 ? 106 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? 24.623 23.131  40.161 1.00 10.99 ? 106 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? 25.134 22.607  38.841 1.00 11.36 ? 106 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? 23.096 23.186  40.116 1.00 10.29 ? 106 LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? 25.638 22.260  44.883 1.00 12.92 ? 107 SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? 26.023 21.490  46.078 1.00 14.60 ? 107 SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? 25.879 22.374  47.326 1.00 14.99 ? 107 SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? 25.599 23.561  47.228 1.00 15.49 ? 107 SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? 27.434 20.937  45.950 1.00 16.12 ? 107 SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? 28.364 21.978  45.852 1.00 17.97 ? 107 SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? 26.019 21.779  48.511 1.00 15.56 ? 108 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? 25.895 22.533  49.753 1.00 15.80 ? 108 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? 24.477 22.923  50.119 1.00 15.78 ? 108 GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? 23.526 22.408  49.541 1.00 15.32 ? 108 GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? 24.314 23.861  51.054 1.00 15.68 ? 109 ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? 22.968 24.259  51.509 1.00 16.02 ? 109 ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? 22.180 25.134  50.526 1.00 15.48 ? 109 ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? 20.966 25.264  50.660 1.00 16.54 ? 109 ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? 22.988 24.911  52.903 1.00 16.31 ? 109 ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? 23.770 26.190  52.955 1.00 16.40 ? 109 ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? 24.782 26.316  52.235 1.00 18.77 ? 109 ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? 23.466 27.116  53.755 1.00 19.70 ? 109 ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? 22.858 25.727  49.556 1.00 14.66 ? 110 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? 22.153 26.504  48.530 1.00 13.98 ? 110 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? 21.811 25.625  47.341 1.00 12.75 ? 110 HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? 21.435 26.098  46.283 1.00 11.18 ? 110 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? 22.997 27.669  48.064 1.00 14.82 ? 110 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? 23.111 28.756  49.072 1.00 17.51 ? 110 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? 23.475 30.041  48.732 1.00 19.62 ? 110 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? 22.880 28.764  50.404 1.00 20.66 ? 110 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? 23.481 30.790  49.821 1.00 21.76 ? 110 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? 23.122 30.040  50.848 1.00 22.46 ? 110 HIS A NE2 1 
HETATM 809  N  N   . CSX A 1 111 ? 22.065 24.289  47.460 1.00 11.71 ? 111 CSX A N   1 
HETATM 810  C  CA  . CSX A 1 111 ? 21.667 23.269  46.606 1.00 12.30 ? 111 CSX A CA  1 
HETATM 811  C  CB  . CSX A 1 111 ? 22.314 21.913  46.768 1.00 12.43 ? 111 CSX A CB  1 
HETATM 812  S  SG  . CSX A 1 111 ? 22.241 20.751  45.410 1.00 14.40 ? 111 CSX A SG  1 
HETATM 813  C  C   . CSX A 1 111 ? 20.390 23.252  45.886 1.00 11.64 ? 111 CSX A C   1 
HETATM 814  O  O   . CSX A 1 111 ? 19.401 23.169  46.584 1.00 11.55 ? 111 CSX A O   1 
HETATM 815  O  OD  . CSX A 1 111 ? 22.311 19.364  45.894 1.00 21.91 ? 111 CSX A OD  1 
ATOM   816  N  N   . ILE A 1 112 ? 20.272 23.425  44.471 1.00 9.41  ? 112 ILE A N   1 
ATOM   817  C  CA  . ILE A 1 112 ? 18.924 23.479  43.846 1.00 9.04  ? 112 ILE A CA  1 
ATOM   818  C  C   . ILE A 1 112 ? 18.552 22.181  43.143 1.00 8.54  ? 112 ILE A C   1 
ATOM   819  O  O   . ILE A 1 112 ? 17.460 22.059  42.613 1.00 7.46  ? 112 ILE A O   1 
ATOM   820  C  CB  . ILE A 1 112 ? 18.836 24.691  42.889 1.00 9.21  ? 112 ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 112 ? 19.855 24.589  41.752 1.00 10.15 ? 112 ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 112 ? 18.970 25.992  43.698 1.00 10.26 ? 112 ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 112 ? 19.683 25.676  40.679 1.00 11.50 ? 112 ILE A CD1 1 
ATOM   824  N  N   . ILE A 1 113 ? 19.475 21.232  43.053 1.00 8.81  ? 113 ILE A N   1 
ATOM   825  C  CA  . ILE A 1 113 ? 19.130 19.926  42.511 1.00 9.01  ? 113 ILE A CA  1 
ATOM   826  C  C   . ILE A 1 113 ? 17.989 19.298  43.315 1.00 8.48  ? 113 ILE A C   1 
ATOM   827  O  O   . ILE A 1 113 ? 17.984 19.296  44.545 1.00 9.51  ? 113 ILE A O   1 
ATOM   828  C  CB  . ILE A 1 113 ? 20.368 19.030  42.430 1.00 10.46 ? 113 ILE A CB  1 
ATOM   829  C  CG1 . ILE A 1 113 ? 21.330 19.571  41.335 1.00 12.86 ? 113 ILE A CG1 1 
ATOM   830  C  CG2 . ILE A 1 113 ? 19.985 17.588  42.109 1.00 10.03 ? 113 ILE A CG2 1 
ATOM   831  C  CD1 . ILE A 1 113 ? 22.700 18.958  41.349 1.00 15.52 ? 113 ILE A CD1 1 
ATOM   832  N  N   . GLY A 1 114 ? 16.997 18.786  42.600 1.00 7.25  ? 114 GLY A N   1 
ATOM   833  C  CA  . GLY A 1 114 ? 15.826 18.199  43.227 1.00 7.38  ? 114 GLY A CA  1 
ATOM   834  C  C   . GLY A 1 114 ? 14.733 19.187  43.581 1.00 6.93  ? 114 GLY A C   1 
ATOM   835  O  O   . GLY A 1 114 ? 13.713 18.797  44.148 1.00 7.21  ? 114 GLY A O   1 
ATOM   836  N  N   . ARG A 1 115 ? 14.953 20.469  43.287 1.00 7.12  ? 115 ARG A N   1 
ATOM   837  C  CA  . ARG A 1 115 ? 13.937 21.502  43.525 1.00 7.28  ? 115 ARG A CA  1 
ATOM   838  C  C   . ARG A 1 115 ? 13.263 21.855  42.206 1.00 7.60  ? 115 ARG A C   1 
ATOM   839  O  O   . ARG A 1 115 ? 13.543 21.219  41.205 1.00 8.53  ? 115 ARG A O   1 
ATOM   840  C  CB  . ARG A 1 115 ? 14.554 22.687  44.246 1.00 7.56  ? 115 ARG A CB  1 
ATOM   841  C  CG  . ARG A 1 115 ? 15.289 22.219  45.506 1.00 9.33  ? 115 ARG A CG  1 
ATOM   842  C  CD  . ARG A 1 115 ? 15.636 23.301  46.465 1.00 11.30 ? 115 ARG A CD  1 
ATOM   843  N  NE  . ARG A 1 115 ? 16.462 22.812  47.566 1.00 12.03 ? 115 ARG A NE  1 
ATOM   844  C  CZ  . ARG A 1 115 ? 15.997 22.358  48.724 1.00 11.67 ? 115 ARG A CZ  1 
ATOM   845  N  NH1 . ARG A 1 115 ? 14.706 22.316  49.001 1.00 11.94 ? 115 ARG A NH1 1 
ATOM   846  N  NH2 . ARG A 1 115 ? 16.866 21.977  49.652 1.00 13.53 ? 115 ARG A NH2 1 
ATOM   847  N  N   . THR A 1 116 ? 12.334 22.795  42.207 1.00 7.59  ? 116 THR A N   1 
ATOM   848  C  CA  . THR A 1 116 ? 11.553 23.104  41.005 1.00 7.27  ? 116 THR A CA  1 
ATOM   849  C  C   . THR A 1 116 ? 11.864 24.468  40.439 1.00 7.86  ? 116 THR A C   1 
ATOM   850  O  O   . THR A 1 116 ? 11.848 25.454  41.159 1.00 9.59  ? 116 THR A O   1 
ATOM   851  C  CB  . THR A 1 116 ? 10.051 23.022  41.320 1.00 7.27  ? 116 THR A CB  1 
ATOM   852  O  OG1 . THR A 1 116 ? 9.711  21.659  41.604 1.00 8.45  ? 116 THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 116 ? 9.180  23.428  40.115 1.00 8.10  ? 116 THR A CG2 1 
ATOM   854  N  N   . LEU A 1 117 ? 12.178 24.523  39.150 1.00 7.21  ? 117 LEU A N   1 
ATOM   855  C  CA  . LEU A 1 117 ? 12.326 25.783  38.446 1.00 7.64  ? 117 LEU A CA  1 
ATOM   856  C  C   . LEU A 1 117 ? 10.975 26.168  37.867 1.00 8.00  ? 117 LEU A C   1 
ATOM   857  O  O   . LEU A 1 117 ? 10.308 25.347  37.282 1.00 8.36  ? 117 LEU A O   1 
ATOM   858  C  CB  . LEU A 1 117 ? 13.360 25.626  37.338 1.00 8.58  ? 117 LEU A CB  1 
ATOM   859  C  CG  . LEU A 1 117 ? 13.784 26.864  36.548 1.00 9.38  ? 117 LEU A CG  1 
ATOM   860  C  CD1 . LEU A 1 117 ? 14.493 27.875  37.433 1.00 11.43 ? 117 LEU A CD1 1 
ATOM   861  C  CD2 . LEU A 1 117 ? 14.659 26.403  35.390 1.00 9.82  ? 117 LEU A CD2 1 
ATOM   862  N  N   . VAL A 1 118 ? 10.574 27.424  38.039 1.00 8.15  ? 118 VAL A N   1 
ATOM   863  C  CA  . VAL A 1 118 ? 9.269  27.906  37.592 1.00 8.49  ? 118 VAL A CA  1 
ATOM   864  C  C   . VAL A 1 118 ? 9.415  29.192  36.785 1.00 8.89  ? 118 VAL A C   1 
ATOM   865  O  O   . VAL A 1 118 ? 10.175 30.080  37.173 1.00 10.08 ? 118 VAL A O   1 
ATOM   866  C  CB  . VAL A 1 118 ? 8.360  28.250  38.796 1.00 8.57  ? 118 VAL A CB  1 
ATOM   867  C  CG1 . VAL A 1 118 ? 6.996  28.743  38.320 1.00 9.65  ? 118 VAL A CG1 1 
ATOM   868  C  CG2 . VAL A 1 118 ? 8.202  27.043  39.731 1.00 9.01  ? 118 VAL A CG2 1 
ATOM   869  N  N   . VAL A 1 119 ? 8.679  29.284  35.675 1.00 9.15  ? 119 VAL A N   1 
ATOM   870  C  CA  . VAL A 1 119 ? 8.581  30.533  34.905 1.00 9.72  ? 119 VAL A CA  1 
ATOM   871  C  C   . VAL A 1 119 ? 7.160  31.049  35.064 1.00 10.36 ? 119 VAL A C   1 
ATOM   872  O  O   . VAL A 1 119 ? 6.190  30.287  35.004 1.00 10.56 ? 119 VAL A O   1 
ATOM   873  C  CB  . VAL A 1 119 ? 9.009  30.355  33.432 1.00 9.92  ? 119 VAL A CB  1 
ATOM   874  C  CG1 . VAL A 1 119 ? 8.127  29.391  32.685 1.00 10.14 ? 119 VAL A CG1 1 
ATOM   875  C  CG2 . VAL A 1 119 ? 9.089  31.728  32.708 1.00 10.63 ? 119 VAL A CG2 1 
ATOM   876  N  N   . HIS A 1 120 ? 7.060  32.350  35.287 1.00 11.59 ? 120 HIS A N   1 
ATOM   877  C  CA  . HIS A 1 120 ? 5.795  32.997  35.591 1.00 13.08 ? 120 HIS A CA  1 
ATOM   878  C  C   . HIS A 1 120 ? 5.161  33.798  34.460 1.00 13.90 ? 120 HIS A C   1 
ATOM   879  O  O   . HIS A 1 120 ? 5.793  34.166  33.466 1.00 13.74 ? 120 HIS A O   1 
ATOM   880  C  CB  . HIS A 1 120 ? 5.984  33.922  36.785 1.00 13.71 ? 120 HIS A CB  1 
ATOM   881  C  CG  . HIS A 1 120 ? 6.167  33.193  38.066 1.00 14.65 ? 120 HIS A CG  1 
ATOM   882  N  ND1 . HIS A 1 120 ? 5.120  32.919  38.917 1.00 15.74 ? 120 HIS A ND1 1 
ATOM   883  C  CD2 . HIS A 1 120 ? 7.261  32.610  38.611 1.00 14.85 ? 120 HIS A CD2 1 
ATOM   884  C  CE1 . HIS A 1 120 ? 5.571  32.235  39.954 1.00 15.64 ? 120 HIS A CE1 1 
ATOM   885  N  NE2 . HIS A 1 120 ? 6.870  32.039  39.798 1.00 14.70 ? 120 HIS A NE2 1 
ATOM   886  N  N   . GLU A 1 121 ? 3.874  34.049  34.670 1.00 14.98 ? 121 GLU A N   1 
ATOM   887  C  CA  . GLU A 1 121 ? 3.011  34.789  33.760 1.00 16.35 ? 121 GLU A CA  1 
ATOM   888  C  C   . GLU A 1 121 ? 3.443  36.231  33.519 1.00 16.85 ? 121 GLU A C   1 
ATOM   889  O  O   . GLU A 1 121 ? 3.398  36.711  32.379 1.00 17.89 ? 121 GLU A O   1 
ATOM   890  C  CB  . GLU A 1 121 ? 1.597  34.762  34.366 1.00 16.56 ? 121 GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 121 ? 0.577  35.731  33.771 1.00 19.29 ? 121 GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 121 ? -0.628 35.983  34.679 1.00 22.03 ? 121 GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 121 ? -1.574 36.654  34.217 1.00 25.25 ? 121 GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 121 ? -0.660 35.541  35.848 1.00 21.89 ? 121 GLU A OE2 1 
ATOM   895  N  N   . LYS A 1 122 ? 3.848  36.904  34.595 1.00 17.45 ? 122 LYS A N   1 
ATOM   896  C  CA  . LYS A 1 122 ? 4.213  38.322  34.551 1.00 18.40 ? 122 LYS A CA  1 
ATOM   897  C  C   . LYS A 1 122 ? 5.636  38.557  35.013 1.00 17.48 ? 122 LYS A C   1 
ATOM   898  O  O   . LYS A 1 122 ? 6.335  37.640  35.455 1.00 16.79 ? 122 LYS A O   1 
ATOM   899  C  CB  . LYS A 1 122 ? 3.302  39.137  35.478 1.00 19.87 ? 122 LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 122 ? 1.863  38.743  35.472 1.00 22.44 ? 122 LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 122 ? 0.974  39.889  35.918 1.00 25.44 ? 122 LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 122 ? 0.845  39.970  37.425 1.00 27.09 ? 122 LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 122 ? 1.888  40.831  38.047 1.00 29.06 ? 122 LYS A NZ  1 
ATOM   904  N  N   . ALA A 1 123 ? 6.045  39.811  34.953 1.00 16.67 ? 123 ALA A N   1 
ATOM   905  C  CA  . ALA A 1 123 ? 7.344  40.205  35.440 1.00 16.48 ? 123 ALA A CA  1 
ATOM   906  C  C   . ALA A 1 123 ? 7.386  40.149  36.961 1.00 16.28 ? 123 ALA A C   1 
ATOM   907  O  O   . ALA A 1 123 ? 6.399  40.407  37.652 1.00 16.97 ? 123 ALA A O   1 
ATOM   908  C  CB  . ALA A 1 123 ? 7.658  41.612  34.966 1.00 16.57 ? 123 ALA A CB  1 
ATOM   909  N  N   . ASP A 1 124 ? 8.556  39.798  37.474 1.00 15.91 ? 124 ASP A N   1 
ATOM   910  C  CA  . ASP A 1 124 ? 8.851  39.837  38.889 1.00 16.00 ? 124 ASP A CA  1 
ATOM   911  C  C   . ASP A 1 124 ? 9.317  41.270  39.152 1.00 16.54 ? 124 ASP A C   1 
ATOM   912  O  O   . ASP A 1 124 ? 10.280 41.705  38.546 1.00 17.16 ? 124 ASP A O   1 
ATOM   913  C  CB  . ASP A 1 124 ? 9.961  38.819  39.168 1.00 16.25 ? 124 ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 124 ? 10.367 38.731  40.628 1.00 16.56 ? 124 ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 124 ? 10.122 39.660  41.440 1.00 16.83 ? 124 ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 124 ? 10.970 37.724  41.054 1.00 17.31 ? 124 ASP A OD2 1 
ATOM   917  N  N   . ASP A 1 125 ? 8.646  41.999  40.039 1.00 17.27 ? 125 ASP A N   1 
ATOM   918  C  CA  . ASP A 1 125 ? 9.028  43.397  40.288 1.00 18.08 ? 125 ASP A CA  1 
ATOM   919  C  C   . ASP A 1 125 ? 10.250 43.538  41.212 1.00 18.29 ? 125 ASP A C   1 
ATOM   920  O  O   . ASP A 1 125 ? 10.673 44.641  41.539 1.00 18.63 ? 125 ASP A O   1 
ATOM   921  C  CB  . ASP A 1 125 ? 7.829  44.237  40.778 1.00 18.42 ? 125 ASP A CB  1 
ATOM   922  C  CG  . ASP A 1 125 ? 7.376  43.905  42.195 1.00 19.70 ? 125 ASP A CG  1 
ATOM   923  O  OD1 . ASP A 1 125 ? 8.084  43.201  42.952 1.00 20.93 ? 125 ASP A OD1 1 
ATOM   924  O  OD2 . ASP A 1 125 ? 6.292  44.347  42.651 1.00 21.95 ? 125 ASP A OD2 1 
ATOM   925  N  N   . LEU A 1 126 ? 10.811 42.402  41.631 1.00 19.06 ? 126 LEU A N   1 
ATOM   926  C  CA  . LEU A 1 126 ? 12.038 42.362  42.439 1.00 19.84 ? 126 LEU A CA  1 
ATOM   927  C  C   . LEU A 1 126 ? 11.905 43.082  43.785 1.00 19.83 ? 126 LEU A C   1 
ATOM   928  O  O   . LEU A 1 126 ? 12.911 43.374  44.443 1.00 19.85 ? 126 LEU A O   1 
ATOM   929  C  CB  . LEU A 1 126 ? 13.232 42.914  41.638 1.00 20.11 ? 126 LEU A CB  1 
ATOM   930  C  CG  . LEU A 1 126 ? 13.379 42.396  40.199 1.00 21.49 ? 126 LEU A CG  1 
ATOM   931  C  CD1 . LEU A 1 126 ? 14.678 42.843  39.552 1.00 23.19 ? 126 LEU A CD1 1 
ATOM   932  C  CD2 . LEU A 1 126 ? 13.294 40.882  40.159 1.00 21.92 ? 126 LEU A CD2 1 
ATOM   933  N  N   . GLY A 1 127 ? 10.669 43.329  44.213 1.00 20.03 ? 127 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 127 ? 10.432 44.083  45.432 1.00 20.70 ? 127 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 127 ? 10.695 45.573  45.259 1.00 21.01 ? 127 GLY A C   1 
ATOM   936  O  O   . GLY A 1 127 ? 10.843 46.303  46.241 1.00 22.11 ? 127 GLY A O   1 
ATOM   937  N  N   . LYS A 1 128 ? 10.764 46.032  44.014 1.00 20.80 ? 128 LYS A N   1 
ATOM   938  C  CA  . LYS A 1 128 ? 11.017 47.444  43.737 1.00 20.77 ? 128 LYS A CA  1 
ATOM   939  C  C   . LYS A 1 128 ? 9.842  48.024  42.966 1.00 19.54 ? 128 LYS A C   1 
ATOM   940  O  O   . LYS A 1 128 ? 10.036 48.666  41.949 1.00 19.75 ? 128 LYS A O   1 
ATOM   941  C  CB  . LYS A 1 128 ? 12.305 47.607  42.927 1.00 21.57 ? 128 LYS A CB  1 
ATOM   942  C  CG  . LYS A 1 128 ? 13.550 47.075  43.628 1.00 23.68 ? 128 LYS A CG  1 
ATOM   943  C  CD  . LYS A 1 128 ? 14.799 47.235  42.775 1.00 26.11 ? 128 LYS A CD  1 
ATOM   944  C  CE  . LYS A 1 128 ? 15.997 46.548  43.410 1.00 27.42 ? 128 LYS A CE  1 
ATOM   945  N  NZ  . LYS A 1 128 ? 15.905 45.063  43.282 1.00 28.66 ? 128 LYS A NZ  1 
ATOM   946  N  N   . GLY A 1 129 ? 8.632  47.807  43.470 1.00 18.67 ? 129 GLY A N   1 
ATOM   947  C  CA  . GLY A 1 129 ? 7.417  48.263  42.803 1.00 18.15 ? 129 GLY A CA  1 
ATOM   948  C  C   . GLY A 1 129 ? 7.013  49.678  43.147 1.00 17.80 ? 129 GLY A C   1 
ATOM   949  O  O   . GLY A 1 129 ? 6.062  50.192  42.570 1.00 17.31 ? 129 GLY A O   1 
ATOM   950  N  N   . GLY A 1 130 ? 7.698  50.288  44.106 1.00 17.35 ? 130 GLY A N   1 
ATOM   951  C  CA  . GLY A 1 130 ? 7.454  51.687  44.435 1.00 17.66 ? 130 GLY A CA  1 
ATOM   952  C  C   . GLY A 1 130 ? 6.242  52.006  45.282 1.00 18.45 ? 130 GLY A C   1 
ATOM   953  O  O   . GLY A 1 130 ? 5.940  53.185  45.478 1.00 17.99 ? 130 GLY A O   1 
ATOM   954  N  N   . ASN A 1 131 ? 5.538  50.992  45.774 1.00 20.03 ? 131 ASN A N   1 
ATOM   955  C  CA  . ASN A 1 131 ? 4.348  51.226  46.592 1.00 21.20 ? 131 ASN A CA  1 
ATOM   956  C  C   . ASN A 1 131 ? 4.471  50.560  47.957 1.00 22.53 ? 131 ASN A C   1 
ATOM   957  O  O   . ASN A 1 131 ? 5.579  50.369  48.468 1.00 23.75 ? 131 ASN A O   1 
ATOM   958  N  N   . THR A 1 135 ? 6.514  42.221  49.405 1.00 32.75 ? 135 THR A N   1 
ATOM   959  C  CA  . THR A 1 135 ? 6.133  41.037  48.654 1.00 32.61 ? 135 THR A CA  1 
ATOM   960  C  C   . THR A 1 135 ? 7.084  39.894  48.942 1.00 32.36 ? 135 THR A C   1 
ATOM   961  O  O   . THR A 1 135 ? 8.254  40.102  49.261 1.00 32.53 ? 135 THR A O   1 
ATOM   962  C  CB  . THR A 1 135 ? 6.164  41.317  47.144 1.00 32.72 ? 135 THR A CB  1 
ATOM   963  O  OG1 . THR A 1 135 ? 5.407  40.319  46.449 1.00 32.65 ? 135 THR A OG1 1 
ATOM   964  C  CG2 . THR A 1 135 ? 7.574  41.151  46.593 1.00 33.05 ? 135 THR A CG2 1 
ATOM   965  N  N   . LYS A 1 136 ? 6.567  38.684  48.786 1.00 31.91 ? 136 LYS A N   1 
ATOM   966  C  CA  . LYS A 1 136 ? 7.335  37.467  48.986 1.00 31.37 ? 136 LYS A CA  1 
ATOM   967  C  C   . LYS A 1 136 ? 7.483  36.761  47.658 1.00 30.30 ? 136 LYS A C   1 
ATOM   968  O  O   . LYS A 1 136 ? 8.218  35.779  47.529 1.00 30.16 ? 136 LYS A O   1 
ATOM   969  C  CB  . LYS A 1 136 ? 6.574  36.535  49.913 1.00 31.77 ? 136 LYS A CB  1 
ATOM   970  C  CG  . LYS A 1 136 ? 6.637  36.898  51.366 1.00 33.06 ? 136 LYS A CG  1 
ATOM   971  C  CD  . LYS A 1 136 ? 6.407  35.644  52.173 1.00 34.56 ? 136 LYS A CD  1 
ATOM   972  C  CE  . LYS A 1 136 ? 5.792  35.935  53.517 1.00 35.44 ? 136 LYS A CE  1 
ATOM   973  N  NZ  . LYS A 1 136 ? 4.908  34.813  53.926 1.00 36.46 ? 136 LYS A NZ  1 
ATOM   974  N  N   . THR A 1 137 ? 6.760  37.266  46.669 1.00 29.03 ? 137 THR A N   1 
ATOM   975  C  CA  . THR A 1 137 ? 6.691  36.635  45.369 1.00 27.99 ? 137 THR A CA  1 
ATOM   976  C  C   . THR A 1 137 ? 7.213  37.515  44.239 1.00 27.12 ? 137 THR A C   1 
ATOM   977  O  O   . THR A 1 137 ? 7.754  37.009  43.261 1.00 26.95 ? 137 THR A O   1 
ATOM   978  C  CB  . THR A 1 137 ? 5.230  36.279  45.079 1.00 28.03 ? 137 THR A CB  1 
ATOM   979  O  OG1 . THR A 1 137 ? 4.457  37.485  44.963 1.00 27.74 ? 137 THR A OG1 1 
ATOM   980  C  CG2 . THR A 1 137 ? 4.599  35.537  46.259 1.00 28.28 ? 137 THR A CG2 1 
ATOM   981  N  N   . GLY A 1 138 ? 7.040  38.829  44.361 1.00 26.10 ? 138 GLY A N   1 
ATOM   982  C  CA  . GLY A 1 138 ? 7.430  39.738  43.296 1.00 25.05 ? 138 GLY A CA  1 
ATOM   983  C  C   . GLY A 1 138 ? 6.271  39.993  42.344 1.00 24.25 ? 138 GLY A C   1 
ATOM   984  O  O   . GLY A 1 138 ? 6.432  40.648  41.312 1.00 23.78 ? 138 GLY A O   1 
ATOM   985  N  N   . ASN A 1 139 ? 5.100  39.460  42.682 1.00 23.54 ? 139 ASN A N   1 
ATOM   986  C  CA  . ASN A 1 139 ? 3.886  39.689  41.902 1.00 23.19 ? 139 ASN A CA  1 
ATOM   987  C  C   . ASN A 1 139 ? 4.007  39.240  40.454 1.00 22.12 ? 139 ASN A C   1 
ATOM   988  O  O   . ASN A 1 139 ? 3.520  39.908  39.549 1.00 21.83 ? 139 ASN A O   1 
ATOM   989  C  CB  . ASN A 1 139 ? 3.504  41.168  41.975 1.00 23.64 ? 139 ASN A CB  1 
ATOM   990  C  CG  . ASN A 1 139 ? 3.202  41.611  43.387 1.00 25.48 ? 139 ASN A CG  1 
ATOM   991  O  OD1 . ASN A 1 139 ? 2.299  41.073  44.039 1.00 27.74 ? 139 ASN A OD1 1 
ATOM   992  N  ND2 . ASN A 1 139 ? 3.964  42.582  43.878 1.00 26.90 ? 139 ASN A ND2 1 
ATOM   993  N  N   . ALA A 1 140 ? 4.629  38.082  40.244 1.00 21.19 ? 140 ALA A N   1 
ATOM   994  C  CA  . ALA A 1 140 ? 4.873  37.568  38.900 1.00 20.62 ? 140 ALA A CA  1 
ATOM   995  C  C   . ALA A 1 140 ? 3.718  36.748  38.348 1.00 19.98 ? 140 ALA A C   1 
ATOM   996  O  O   . ALA A 1 140 ? 3.813  36.197  37.259 1.00 19.08 ? 140 ALA A O   1 
ATOM   997  C  CB  . ALA A 1 140 ? 6.178  36.763  38.860 1.00 20.64 ? 140 ALA A CB  1 
ATOM   998  N  N   . GLY A 1 141 ? 2.617  36.677  39.082 1.00 19.78 ? 141 GLY A N   1 
ATOM   999  C  CA  . GLY A 1 141 ? 1.447  35.993  38.576 1.00 19.38 ? 141 GLY A CA  1 
ATOM   1000 C  C   . GLY A 1 141 ? 1.560  34.477  38.582 1.00 18.72 ? 141 GLY A C   1 
ATOM   1001 O  O   . GLY A 1 141 ? 2.371  33.880  39.310 1.00 18.93 ? 141 GLY A O   1 
ATOM   1002 N  N   . SER A 1 142 ? 0.756  33.840  37.746 1.00 18.01 ? 142 SER A N   1 
ATOM   1003 C  CA  . SER A 1 142 ? 0.672  32.392  37.760 1.00 17.40 ? 142 SER A CA  1 
ATOM   1004 C  C   . SER A 1 142 ? 1.943  31.687  37.316 1.00 15.69 ? 142 SER A C   1 
ATOM   1005 O  O   . SER A 1 142 ? 2.797  32.230  36.614 1.00 15.25 ? 142 SER A O   1 
ATOM   1006 C  CB  . SER A 1 142 ? -0.485 31.915  36.900 1.00 18.52 ? 142 SER A CB  1 
ATOM   1007 O  OG  . SER A 1 142 ? -0.199 32.095  35.542 1.00 21.24 ? 142 SER A OG  1 
ATOM   1008 N  N   . ARG A 1 143 ? 2.020  30.428  37.725 1.00 13.93 ? 143 ARG A N   1 
ATOM   1009 C  CA  . ARG A 1 143 ? 3.120  29.548  37.385 1.00 13.21 ? 143 ARG A CA  1 
ATOM   1010 C  C   . ARG A 1 143 ? 2.797  28.889  36.052 1.00 13.56 ? 143 ARG A C   1 
ATOM   1011 O  O   . ARG A 1 143 ? 1.991  27.967  35.985 1.00 15.51 ? 143 ARG A O   1 
ATOM   1012 C  CB  . ARG A 1 143 ? 3.278  28.501  38.491 1.00 12.81 ? 143 ARG A CB  1 
ATOM   1013 C  CG  . ARG A 1 143 ? 3.495  29.129  39.854 1.00 12.11 ? 143 ARG A CG  1 
ATOM   1014 C  CD  . ARG A 1 143 ? 3.706  28.153  40.998 1.00 12.36 ? 143 ARG A CD  1 
ATOM   1015 N  NE  . ARG A 1 143 ? 3.878  28.860  42.258 1.00 13.24 ? 143 ARG A NE  1 
ATOM   1016 C  CZ  . ARG A 1 143 ? 4.113  28.300  43.423 1.00 13.83 ? 143 ARG A CZ  1 
ATOM   1017 N  NH1 . ARG A 1 143 ? 4.223  26.986  43.518 1.00 15.24 ? 143 ARG A NH1 1 
ATOM   1018 N  NH2 . ARG A 1 143 ? 4.256  29.061  44.496 1.00 14.63 ? 143 ARG A NH2 1 
ATOM   1019 N  N   . LEU A 1 144 ? 3.429  29.343  34.975 1.00 12.24 ? 144 LEU A N   1 
ATOM   1020 C  CA  . LEU A 1 144 ? 3.072  28.863  33.649 1.00 12.42 ? 144 LEU A CA  1 
ATOM   1021 C  C   . LEU A 1 144 ? 3.650  27.513  33.293 1.00 11.49 ? 144 LEU A C   1 
ATOM   1022 O  O   . LEU A 1 144 ? 3.045  26.731  32.561 1.00 13.07 ? 144 LEU A O   1 
ATOM   1023 C  CB  . LEU A 1 144 ? 3.511  29.876  32.594 1.00 13.28 ? 144 LEU A CB  1 
ATOM   1024 C  CG  . LEU A 1 144 ? 2.797  31.222  32.685 1.00 15.70 ? 144 LEU A CG  1 
ATOM   1025 C  CD1 . LEU A 1 144 ? 3.206  32.075  31.504 1.00 17.50 ? 144 LEU A CD1 1 
ATOM   1026 C  CD2 . LEU A 1 144 ? 1.291  31.089  32.720 1.00 17.28 ? 144 LEU A CD2 1 
ATOM   1027 N  N   . ALA A 1 145 ? 4.858  27.255  33.783 1.00 10.40 ? 145 ALA A N   1 
ATOM   1028 C  CA  . ALA A 1 145 ? 5.535  26.002  33.514 1.00 10.02 ? 145 ALA A CA  1 
ATOM   1029 C  C   . ALA A 1 145 ? 6.607  25.806  34.553 1.00 8.39  ? 145 ALA A C   1 
ATOM   1030 O  O   . ALA A 1 145 ? 7.102  26.750  35.145 1.00 8.51  ? 145 ALA A O   1 
ATOM   1031 C  CB  . ALA A 1 145 ? 6.150  25.995  32.133 1.00 9.87  ? 145 ALA A CB  1 
ATOM   1032 N  N   . CYS A 1 146 ? 6.947  24.553  34.774 1.00 8.27  ? 146 CYS A N   1 
ATOM   1033 C  CA  . CYS A 1 146 ? 7.948  24.218  35.762 1.00 8.56  ? 146 CYS A CA  1 
ATOM   1034 C  C   . CYS A 1 146 ? 8.473  22.822  35.498 1.00 7.19  ? 146 CYS A C   1 
ATOM   1035 O  O   . CYS A 1 146 ? 7.925  22.058  34.723 1.00 8.34  ? 146 CYS A O   1 
ATOM   1036 C  CB  . CYS A 1 146 ? 7.311  24.252  37.147 1.00 8.93  ? 146 CYS A CB  1 
ATOM   1037 S  SG  . CYS A 1 146 ? 5.848  23.184  37.337 1.00 11.41 ? 146 CYS A SG  1 
ATOM   1038 N  N   . GLY A 1 147 ? 9.560  22.502  36.183 1.00 6.99  ? 147 GLY A N   1 
ATOM   1039 C  CA  . GLY A 1 147 ? 10.090 21.146  36.158 1.00 7.00  ? 147 GLY A CA  1 
ATOM   1040 C  C   . GLY A 1 147 ? 11.060 20.952  37.313 1.00 6.67  ? 147 GLY A C   1 
ATOM   1041 O  O   . GLY A 1 147 ? 11.504 21.911  37.932 1.00 7.12  ? 147 GLY A O   1 
ATOM   1042 N  N   . VAL A 1 148 ? 11.376 19.696  37.604 1.00 6.64  ? 148 VAL A N   1 
ATOM   1043 C  CA  . VAL A 1 148 ? 12.305 19.353  38.668 1.00 6.95  ? 148 VAL A CA  1 
ATOM   1044 C  C   . VAL A 1 148 ? 13.724 19.426  38.114 1.00 6.62  ? 148 VAL A C   1 
ATOM   1045 O  O   . VAL A 1 148 ? 13.994 18.945  37.009 1.00 8.08  ? 148 VAL A O   1 
ATOM   1046 C  CB  . VAL A 1 148 ? 12.009 17.961  39.230 1.00 7.04  ? 148 VAL A CB  1 
ATOM   1047 C  CG1 . VAL A 1 148 ? 12.994 17.621  40.358 1.00 8.37  ? 148 VAL A CG1 1 
ATOM   1048 C  CG2 . VAL A 1 148 ? 10.575 17.892  39.707 1.00 8.21  ? 148 VAL A CG2 1 
ATOM   1049 N  N   . ILE A 1 149 ? 14.642 20.013  38.861 1.00 6.41  ? 149 ILE A N   1 
ATOM   1050 C  CA  . ILE A 1 149 ? 16.026 20.159  38.430 1.00 6.92  ? 149 ILE A CA  1 
ATOM   1051 C  C   . ILE A 1 149 ? 16.781 18.868  38.696 1.00 7.33  ? 149 ILE A C   1 
ATOM   1052 O  O   . ILE A 1 149 ? 16.853 18.397  39.831 1.00 7.89  ? 149 ILE A O   1 
ATOM   1053 C  CB  . ILE A 1 149 ? 16.672 21.333  39.173 1.00 7.80  ? 149 ILE A CB  1 
ATOM   1054 C  CG1 . ILE A 1 149 ? 15.890 22.627  38.893 1.00 8.19  ? 149 ILE A CG1 1 
ATOM   1055 C  CG2 . ILE A 1 149 ? 18.126 21.465  38.785 1.00 8.04  ? 149 ILE A CG2 1 
ATOM   1056 C  CD1 . ILE A 1 149 ? 16.311 23.779  39.744 1.00 8.81  ? 149 ILE A CD1 1 
ATOM   1057 N  N   . GLY A 1 150 ? 17.314 18.270  37.637 1.00 7.08  ? 150 GLY A N   1 
ATOM   1058 C  CA  . GLY A 1 150 ? 17.981 16.981  37.721 1.00 7.36  ? 150 GLY A CA  1 
ATOM   1059 C  C   . GLY A 1 150 ? 19.444 17.034  37.372 1.00 7.79  ? 150 GLY A C   1 
ATOM   1060 O  O   . GLY A 1 150 ? 19.921 17.948  36.715 1.00 8.54  ? 150 GLY A O   1 
ATOM   1061 N  N   . ILE A 1 151 ? 20.151 16.009  37.807 1.00 7.96  ? 151 ILE A N   1 
ATOM   1062 C  CA  . ILE A 1 151 ? 21.556 15.844  37.497 1.00 8.65  ? 151 ILE A CA  1 
ATOM   1063 C  C   . ILE A 1 151 ? 21.690 15.535  36.016 1.00 9.01  ? 151 ILE A C   1 
ATOM   1064 O  O   . ILE A 1 151 ? 20.940 14.733  35.470 1.00 9.44  ? 151 ILE A O   1 
ATOM   1065 C  CB  . ILE A 1 151 ? 22.145 14.706  38.353 1.00 9.39  ? 151 ILE A CB  1 
ATOM   1066 C  CG1 . ILE A 1 151 ? 22.080 15.070  39.831 1.00 10.96 ? 151 ILE A CG1 1 
ATOM   1067 C  CG2 . ILE A 1 151 ? 23.575 14.393  37.919 1.00 11.37 ? 151 ILE A CG2 1 
ATOM   1068 C  CD1 . ILE A 1 151 ? 22.354 13.915  40.747 1.00 13.03 ? 151 ILE A CD1 1 
ATOM   1069 N  N   . ALA A 1 152 ? 22.660 16.176  35.372 1.00 9.86  ? 152 ALA A N   1 
ATOM   1070 C  CA  . ALA A 1 152 ? 22.852 16.027  33.934 1.00 11.48 ? 152 ALA A CA  1 
ATOM   1071 C  C   . ALA A 1 152 ? 24.278 15.618  33.589 1.00 13.72 ? 152 ALA A C   1 
ATOM   1072 O  O   . ALA A 1 152 ? 25.175 15.716  34.415 1.00 13.55 ? 152 ALA A O   1 
ATOM   1073 C  CB  . ALA A 1 152 ? 22.502 17.336  33.225 1.00 11.44 ? 152 ALA A CB  1 
ATOM   1074 N  N   . GLN A 1 153 ? 24.435 15.157  32.352 1.00 16.56 ? 153 GLN A N   1 
ATOM   1075 C  CA  . GLN A 1 153 ? 25.716 14.726  31.795 1.00 19.15 ? 153 GLN A CA  1 
ATOM   1076 C  C   . GLN A 1 153 ? 26.427 15.959  31.285 1.00 20.06 ? 153 GLN A C   1 
ATOM   1077 O  O   . GLN A 1 153 ? 25.810 16.806  30.638 1.00 21.23 ? 153 GLN A O   1 
ATOM   1078 C  CB  . GLN A 1 153 ? 25.482 13.732  30.651 1.00 20.39 ? 153 GLN A CB  1 
ATOM   1079 C  CG  . GLN A 1 153 ? 26.742 13.120  30.057 1.00 23.98 ? 153 GLN A CG  1 
ATOM   1080 C  CD  . GLN A 1 153 ? 26.440 12.050  29.026 1.00 27.17 ? 153 GLN A CD  1 
ATOM   1081 O  OE1 . GLN A 1 153 ? 27.326 11.282  28.654 1.00 30.80 ? 153 GLN A OE1 1 
ATOM   1082 N  NE2 . GLN A 1 153 ? 25.199 12.006  28.546 1.00 28.45 ? 153 GLN A NE2 1 
ATOM   1083 N  N   . ALA B 1 1   ? 17.590 15.653  52.536 1.00 20.96 ? 201 ALA B N   1 
ATOM   1084 C  CA  . ALA B 1 1   ? 16.176 15.373  52.327 1.00 19.37 ? 201 ALA B CA  1 
ATOM   1085 C  C   . ALA B 1 1   ? 15.767 14.125  53.098 1.00 18.29 ? 201 ALA B C   1 
ATOM   1086 O  O   . ALA B 1 1   ? 16.514 13.153  53.137 1.00 18.99 ? 201 ALA B O   1 
ATOM   1087 C  CB  . ALA B 1 1   ? 15.892 15.177  50.856 1.00 19.82 ? 201 ALA B CB  1 
ATOM   1088 N  N   . THR B 1 2   ? 14.585 14.163  53.694 1.00 16.07 ? 202 THR B N   1 
ATOM   1089 C  CA  . THR B 1 2   ? 14.025 12.994  54.360 1.00 15.41 ? 202 THR B CA  1 
ATOM   1090 C  C   . THR B 1 2   ? 12.943 12.346  53.483 1.00 12.46 ? 202 THR B C   1 
ATOM   1091 O  O   . THR B 1 2   ? 12.600 11.179  53.666 1.00 11.06 ? 202 THR B O   1 
ATOM   1092 C  CB  . THR B 1 2   ? 13.420 13.370  55.742 1.00 16.29 ? 202 THR B CB  1 
ATOM   1093 O  OG1 . THR B 1 2   ? 12.376 14.318  55.584 1.00 19.81 ? 202 THR B OG1 1 
ATOM   1094 C  CG2 . THR B 1 2   ? 14.404 14.138  56.611 1.00 18.56 ? 202 THR B CG2 1 
ATOM   1095 N  N   . LYS B 1 3   ? 12.385 13.105  52.540 1.00 10.94 ? 203 LYS B N   1 
ATOM   1096 C  CA  . LYS B 1 3   ? 11.330 12.597  51.682 1.00 10.39 ? 203 LYS B CA  1 
ATOM   1097 C  C   . LYS B 1 3   ? 11.551 13.109  50.275 1.00 9.01  ? 203 LYS B C   1 
ATOM   1098 O  O   . LYS B 1 3   ? 11.999 14.242  50.064 1.00 8.30  ? 203 LYS B O   1 
ATOM   1099 C  CB  . LYS B 1 3   ? 9.968  13.069  52.183 1.00 12.32 ? 203 LYS B CB  1 
ATOM   1100 C  CG  . LYS B 1 3   ? 8.845  12.090  52.011 1.00 17.65 ? 203 LYS B CG  1 
ATOM   1101 C  CD  . LYS B 1 3   ? 7.690  12.422  52.972 1.00 21.74 ? 203 LYS B CD  1 
ATOM   1102 C  CE  . LYS B 1 3   ? 6.345  12.333  52.283 1.00 24.77 ? 203 LYS B CE  1 
ATOM   1103 N  NZ  . LYS B 1 3   ? 5.225  12.851  53.130 1.00 26.89 ? 203 LYS B NZ  1 
ATOM   1104 N  N   . ALA B 1 4   ? 11.247 12.256  49.311 1.00 7.35  ? 204 ALA B N   1 
ATOM   1105 C  CA  . ALA B 1 4   ? 11.317 12.614  47.902 1.00 7.03  ? 204 ALA B CA  1 
ATOM   1106 C  C   . ALA B 1 4   ? 10.062 12.103  47.205 1.00 6.63  ? 204 ALA B C   1 
ATOM   1107 O  O   . ALA B 1 4   ? 9.323  11.280  47.755 1.00 7.07  ? 204 ALA B O   1 
ATOM   1108 C  CB  . ALA B 1 4   ? 12.541 12.042  47.274 1.00 7.40  ? 204 ALA B CB  1 
ATOM   1109 N  N   . VAL B 1 5   ? 9.788  12.619  46.012 1.00 6.62  ? 205 VAL B N   1 
ATOM   1110 C  CA  . VAL B 1 5   ? 8.603  12.222  45.275 1.00 6.83  ? 205 VAL B CA  1 
ATOM   1111 C  C   . VAL B 1 5   ? 8.939  12.276  43.793 1.00 6.76  ? 205 VAL B C   1 
ATOM   1112 O  O   . VAL B 1 5   ? 9.821  13.020  43.372 1.00 7.08  ? 205 VAL B O   1 
ATOM   1113 C  CB  . VAL B 1 5   ? 7.392  13.124  45.647 1.00 7.08  ? 205 VAL B CB  1 
ATOM   1114 C  CG1 . VAL B 1 5   ? 7.624  14.549  45.182 1.00 7.93  ? 205 VAL B CG1 1 
ATOM   1115 C  CG2 . VAL B 1 5   ? 6.076  12.583  45.105 1.00 8.49  ? 205 VAL B CG2 1 
ATOM   1116 N  N   . CYS B 1 6   ? 8.231  11.470  43.016 1.00 6.99  ? 206 CYS B N   1 
ATOM   1117 C  CA  . CYS B 1 6   ? 8.456  11.391  41.600 1.00 7.49  ? 206 CYS B CA  1 
ATOM   1118 C  C   . CYS B 1 6   ? 7.129  11.151  40.897 1.00 7.12  ? 206 CYS B C   1 
ATOM   1119 O  O   . CYS B 1 6   ? 6.376  10.243  41.260 1.00 8.10  ? 206 CYS B O   1 
ATOM   1120 C  CB  . CYS B 1 6   ? 9.376  10.220  41.304 1.00 8.08  ? 206 CYS B CB  1 
ATOM   1121 S  SG  . CYS B 1 6   ? 9.818  10.048  39.560 1.00 9.96  ? 206 CYS B SG  1 
ATOM   1122 N  N   . VAL B 1 7   ? 6.863  11.976  39.895 1.00 7.48  ? 207 VAL B N   1 
ATOM   1123 C  CA  . VAL B 1 7   ? 5.713  11.813  39.029 1.00 7.74  ? 207 VAL B CA  1 
ATOM   1124 C  C   . VAL B 1 7   ? 6.179  11.122  37.756 1.00 7.90  ? 207 VAL B C   1 
ATOM   1125 O  O   . VAL B 1 7   ? 6.998  11.665  37.010 1.00 8.86  ? 207 VAL B O   1 
ATOM   1126 C  CB  . VAL B 1 7   ? 5.065  13.147  38.677 1.00 8.33  ? 207 VAL B CB  1 
ATOM   1127 C  CG1 . VAL B 1 7   ? 3.867  12.912  37.753 1.00 10.47 ? 207 VAL B CG1 1 
ATOM   1128 C  CG2 . VAL B 1 7   ? 4.634  13.875  39.938 1.00 9.10  ? 207 VAL B CG2 1 
ATOM   1129 N  N   . LEU B 1 8   ? 5.652  9.929   37.505 1.00 8.61  ? 208 LEU B N   1 
ATOM   1130 C  CA  . LEU B 1 8   ? 5.993  9.169   36.316 1.00 9.03  ? 208 LEU B CA  1 
ATOM   1131 C  C   . LEU B 1 8   ? 5.006  9.480   35.190 1.00 9.59  ? 208 LEU B C   1 
ATOM   1132 O  O   . LEU B 1 8   ? 3.803  9.388   35.379 1.00 10.27 ? 208 LEU B O   1 
ATOM   1133 C  CB  . LEU B 1 8   ? 5.930  7.670   36.624 1.00 9.98  ? 208 LEU B CB  1 
ATOM   1134 C  CG  . LEU B 1 8   ? 6.897  7.119   37.662 1.00 11.17 ? 208 LEU B CG  1 
ATOM   1135 C  CD1 . LEU B 1 8   ? 6.504  5.692   38.069 1.00 13.09 ? 208 LEU B CD1 1 
ATOM   1136 C  CD2 . LEU B 1 8   ? 8.276  7.135   37.140 1.00 11.90 ? 208 LEU B CD2 1 
ATOM   1137 N  N   . LYS B 1 9   ? 5.548  9.833   34.031 1.00 9.76  ? 209 LYS B N   1 
ATOM   1138 C  CA  . LYS B 1 9   ? 4.763  10.096  32.821 1.00 11.31 ? 209 LYS B CA  1 
ATOM   1139 C  C   . LYS B 1 9   ? 5.591  9.655   31.609 1.00 11.31 ? 209 LYS B C   1 
ATOM   1140 O  O   . LYS B 1 9   ? 6.809  9.573   31.666 1.00 10.64 ? 209 LYS B O   1 
ATOM   1141 C  CB  . LYS B 1 9   ? 4.449  11.590  32.696 1.00 13.27 ? 209 LYS B CB  1 
ATOM   1142 C  CG  . LYS B 1 9   ? 3.487  12.112  33.745 1.00 17.13 ? 209 LYS B CG  1 
ATOM   1143 C  CD  . LYS B 1 9   ? 2.966  13.507  33.451 1.00 21.62 ? 209 LYS B CD  1 
ATOM   1144 C  CE  . LYS B 1 9   ? 1.986  13.934  34.531 1.00 23.54 ? 209 LYS B CE  1 
ATOM   1145 N  NZ  . LYS B 1 9   ? 0.734  13.116  34.521 1.00 25.44 ? 209 LYS B NZ  1 
ATOM   1146 N  N   . GLY B 1 10  ? 4.919  9.381   30.498 1.00 12.49 ? 210 GLY B N   1 
ATOM   1147 C  CA  . GLY B 1 10  ? 5.613  8.969   29.289 1.00 13.58 ? 210 GLY B CA  1 
ATOM   1148 C  C   . GLY B 1 10  ? 4.795  9.358   28.079 1.00 14.76 ? 210 GLY B C   1 
ATOM   1149 O  O   . GLY B 1 10  ? 3.875  10.169  28.180 1.00 15.52 ? 210 GLY B O   1 
ATOM   1150 N  N   . ASP B 1 11  ? 5.108  8.752   26.943 1.00 15.90 ? 211 ASP B N   1 
ATOM   1151 C  CA  . ASP B 1 11  ? 4.383  9.060   25.702 1.00 17.23 ? 211 ASP B CA  1 
ATOM   1152 C  C   . ASP B 1 11  ? 3.033  8.328   25.611 1.00 16.93 ? 211 ASP B C   1 
ATOM   1153 O  O   . ASP B 1 11  ? 2.189  8.671   24.777 1.00 18.83 ? 211 ASP B O   1 
ATOM   1154 C  CB  . ASP B 1 11  ? 5.245  8.734   24.472 1.00 18.74 ? 211 ASP B CB  1 
ATOM   1155 C  CG  . ASP B 1 11  ? 6.552  9.498   24.445 1.00 21.82 ? 211 ASP B CG  1 
ATOM   1156 O  OD1 . ASP B 1 11  ? 6.535  10.742  24.568 1.00 25.34 ? 211 ASP B OD1 1 
ATOM   1157 O  OD2 . ASP B 1 11  ? 7.652  8.933   24.289 1.00 26.73 ? 211 ASP B OD2 1 
ATOM   1158 N  N   . GLY B 1 12  ? 2.831  7.327   26.456 1.00 15.50 ? 212 GLY B N   1 
ATOM   1159 C  CA  . GLY B 1 12  ? 1.626  6.525   26.473 1.00 14.68 ? 212 GLY B CA  1 
ATOM   1160 C  C   . GLY B 1 12  ? 0.821  6.748   27.736 1.00 13.69 ? 212 GLY B C   1 
ATOM   1161 O  O   . GLY B 1 12  ? 0.856  7.832   28.308 1.00 13.70 ? 212 GLY B O   1 
ATOM   1162 N  N   . PRO B 1 13  ? 0.085  5.735   28.174 1.00 12.50 ? 213 PRO B N   1 
ATOM   1163 C  CA  . PRO B 1 13  ? -0.829 5.870   29.313 1.00 13.03 ? 213 PRO B CA  1 
ATOM   1164 C  C   . PRO B 1 13  ? -0.229 5.591   30.686 1.00 12.49 ? 213 PRO B C   1 
ATOM   1165 O  O   . PRO B 1 13  ? -0.956 5.661   31.672 1.00 13.09 ? 213 PRO B O   1 
ATOM   1166 C  CB  . PRO B 1 13  ? -1.852 4.777   29.030 1.00 13.24 ? 213 PRO B CB  1 
ATOM   1167 C  CG  . PRO B 1 13  ? -1.053 3.715   28.351 1.00 13.28 ? 213 PRO B CG  1 
ATOM   1168 C  CD  . PRO B 1 13  ? -0.011 4.398   27.552 1.00 13.19 ? 213 PRO B CD  1 
ATOM   1169 N  N   . VAL B 1 14  ? 1.044  5.234   30.766 1.00 12.42 ? 214 VAL B N   1 
ATOM   1170 C  CA  . VAL B 1 14  ? 1.612  4.877   32.061 1.00 12.46 ? 214 VAL B CA  1 
ATOM   1171 C  C   . VAL B 1 14  ? 1.836  6.131   32.905 1.00 12.13 ? 214 VAL B C   1 
ATOM   1172 O  O   . VAL B 1 14  ? 2.479  7.080   32.465 1.00 12.55 ? 214 VAL B O   1 
ATOM   1173 C  CB  . VAL B 1 14  ? 2.891  4.053   31.904 1.00 12.10 ? 214 VAL B CB  1 
ATOM   1174 C  CG1 . VAL B 1 14  ? 3.431  3.688   33.263 1.00 12.82 ? 214 VAL B CG1 1 
ATOM   1175 C  CG2 . VAL B 1 14  ? 2.613  2.791   31.082 1.00 12.68 ? 214 VAL B CG2 1 
ATOM   1176 N  N   . GLN B 1 15  ? 1.257  6.140   34.097 1.00 12.89 ? 215 GLN B N   1 
ATOM   1177 C  CA  . GLN B 1 15  ? 1.364  7.295   34.972 1.00 13.34 ? 215 GLN B CA  1 
ATOM   1178 C  C   . GLN B 1 15  ? 1.302  6.860   36.416 1.00 12.07 ? 215 GLN B C   1 
ATOM   1179 O  O   . GLN B 1 15  ? 0.661  5.867   36.776 1.00 12.64 ? 215 GLN B O   1 
ATOM   1180 C  CB  . GLN B 1 15  ? 0.274  8.315   34.658 1.00 15.21 ? 215 GLN B CB  1 
ATOM   1181 C  CG  . GLN B 1 15  ? -1.114 7.824   34.814 1.00 17.75 ? 215 GLN B CG  1 
ATOM   1182 C  CD  . GLN B 1 15  ? -2.137 8.843   34.311 1.00 19.87 ? 215 GLN B CD  1 
ATOM   1183 O  OE1 . GLN B 1 15  ? -2.059 10.026  34.661 1.00 23.61 ? 215 GLN B OE1 1 
ATOM   1184 N  NE2 . GLN B 1 15  ? -3.084 8.396   33.483 1.00 20.20 ? 215 GLN B NE2 1 
ATOM   1185 N  N   . GLY B 1 16  ? 1.983  7.609   37.270 1.00 10.84 ? 216 GLY B N   1 
ATOM   1186 C  CA  . GLY B 1 16  ? 1.913  7.308   38.686 1.00 11.11 ? 216 GLY B CA  1 
ATOM   1187 C  C   . GLY B 1 16  ? 2.709  8.266   39.532 1.00 9.89  ? 216 GLY B C   1 
ATOM   1188 O  O   . GLY B 1 16  ? 3.406  9.119   39.008 1.00 9.95  ? 216 GLY B O   1 
ATOM   1189 N  N   . ILE B 1 17  ? 2.577  8.104   40.838 1.00 9.39  ? 217 ILE B N   1 
ATOM   1190 C  CA  . ILE B 1 17  ? 3.308  8.895   41.809 1.00 9.28  ? 217 ILE B CA  1 
ATOM   1191 C  C   . ILE B 1 17  ? 3.998  7.922   42.750 1.00 8.35  ? 217 ILE B C   1 
ATOM   1192 O  O   . ILE B 1 17  ? 3.355  7.044   43.334 1.00 8.75  ? 217 ILE B O   1 
ATOM   1193 C  CB  . ILE B 1 17  ? 2.354  9.808   42.603 1.00 9.39  ? 217 ILE B CB  1 
ATOM   1194 C  CG1 . ILE B 1 17  ? 1.742  10.850  41.661 1.00 11.53 ? 217 ILE B CG1 1 
ATOM   1195 C  CG2 . ILE B 1 17  ? 3.098  10.473  43.755 1.00 10.50 ? 217 ILE B CG2 1 
ATOM   1196 C  CD1 . ILE B 1 17  ? 0.636  11.700  42.269 1.00 13.61 ? 217 ILE B CD1 1 
ATOM   1197 N  N   . ILE B 1 18  ? 5.298  8.109   42.930 1.00 7.51  ? 218 ILE B N   1 
ATOM   1198 C  CA  . ILE B 1 18  ? 6.088  7.279   43.836 1.00 7.38  ? 218 ILE B CA  1 
ATOM   1199 C  C   . ILE B 1 18  ? 6.747  8.171   44.882 1.00 8.08  ? 218 ILE B C   1 
ATOM   1200 O  O   . ILE B 1 18  ? 7.370  9.189   44.563 1.00 7.64  ? 218 ILE B O   1 
ATOM   1201 C  CB  . ILE B 1 18  ? 7.140  6.477   43.048 1.00 7.38  ? 218 ILE B CB  1 
ATOM   1202 C  CG1 . ILE B 1 18  ? 6.469  5.530   42.025 1.00 8.43  ? 218 ILE B CG1 1 
ATOM   1203 C  CG2 . ILE B 1 18  ? 8.056  5.720   44.011 1.00 7.33  ? 218 ILE B CG2 1 
ATOM   1204 C  CD1 . ILE B 1 18  ? 5.707  4.359   42.671 1.00 10.17 ? 218 ILE B CD1 1 
ATOM   1205 N  N   . ASN B 1 19  ? 6.577  7.762   46.127 1.00 7.54  ? 219 ASN B N   1 
ATOM   1206 C  CA  . ASN B 1 19  ? 7.134  8.445   47.276 1.00 8.07  ? 219 ASN B CA  1 
ATOM   1207 C  C   . ASN B 1 19  ? 8.350  7.697   47.803 1.00 7.83  ? 219 ASN B C   1 
ATOM   1208 O  O   . ASN B 1 19  ? 8.419  6.465   47.701 1.00 8.35  ? 219 ASN B O   1 
ATOM   1209 C  CB  . ASN B 1 19  ? 6.097  8.490   48.397 1.00 9.03  ? 219 ASN B CB  1 
ATOM   1210 C  CG  . ASN B 1 19  ? 4.818  9.138   47.964 1.00 11.44 ? 219 ASN B CG  1 
ATOM   1211 O  OD1 . ASN B 1 19  ? 4.759  10.353  47.834 1.00 13.29 ? 219 ASN B OD1 1 
ATOM   1212 N  ND2 . ASN B 1 19  ? 3.790  8.334   47.709 1.00 13.72 ? 219 ASN B ND2 1 
ATOM   1213 N  N   . PHE B 1 20  ? 9.301  8.432   48.359 1.00 7.61  ? 220 PHE B N   1 
ATOM   1214 C  CA  . PHE B 1 20  ? 10.493 7.871   48.978 1.00 8.03  ? 220 PHE B CA  1 
ATOM   1215 C  C   . PHE B 1 20  ? 10.627 8.518   50.351 1.00 8.47  ? 220 PHE B C   1 
ATOM   1216 O  O   . PHE B 1 20  ? 10.478 9.732   50.484 1.00 9.11  ? 220 PHE B O   1 
ATOM   1217 C  CB  . PHE B 1 20  ? 11.764 8.223   48.202 1.00 8.44  ? 220 PHE B CB  1 
ATOM   1218 C  CG  . PHE B 1 20  ? 11.786 7.740   46.792 1.00 8.68  ? 220 PHE B CG  1 
ATOM   1219 C  CD1 . PHE B 1 20  ? 11.143 8.451   45.797 1.00 9.69  ? 220 PHE B CD1 1 
ATOM   1220 C  CD2 . PHE B 1 20  ? 12.489 6.601   46.453 1.00 10.72 ? 220 PHE B CD2 1 
ATOM   1221 C  CE1 . PHE B 1 20  ? 11.182 8.014   44.489 1.00 10.58 ? 220 PHE B CE1 1 
ATOM   1222 C  CE2 . PHE B 1 20  ? 12.526 6.169   45.154 1.00 11.39 ? 220 PHE B CE2 1 
ATOM   1223 C  CZ  . PHE B 1 20  ? 11.882 6.889   44.170 1.00 10.47 ? 220 PHE B CZ  1 
ATOM   1224 N  N   . GLU B 1 21  ? 10.912 7.725   51.377 1.00 8.53  ? 221 GLU B N   1 
ATOM   1225 C  CA  . GLU B 1 21  ? 11.158 8.279   52.714 1.00 9.00  ? 221 GLU B CA  1 
ATOM   1226 C  C   . GLU B 1 21  ? 12.354 7.617   53.354 1.00 8.47  ? 221 GLU B C   1 
ATOM   1227 O  O   . GLU B 1 21  ? 12.483 6.389   53.362 1.00 9.28  ? 221 GLU B O   1 
ATOM   1228 C  CB  . GLU B 1 21  ? 9.939  8.161   53.629 1.00 10.38 ? 221 GLU B CB  1 
ATOM   1229 C  CG  . GLU B 1 21  ? 10.106 8.898   54.956 1.00 13.53 ? 221 GLU B CG  1 
ATOM   1230 C  CD  . GLU B 1 21  ? 8.808  9.135   55.714 1.00 18.86 ? 221 GLU B CD  1 
ATOM   1231 O  OE1 . GLU B 1 21  ? 8.800  10.049  56.569 1.00 24.29 ? 221 GLU B OE1 1 
ATOM   1232 O  OE2 . GLU B 1 21  ? 7.827  8.397   55.504 1.00 22.55 ? 221 GLU B OE2 1 
ATOM   1233 N  N   . GLN B 1 22  ? 13.237 8.447   53.882 1.00 8.46  ? 222 GLN B N   1 
ATOM   1234 C  CA  . GLN B 1 22  ? 14.443 7.989   54.564 1.00 8.93  ? 222 GLN B CA  1 
ATOM   1235 C  C   . GLN B 1 22  ? 14.605 8.846   55.811 1.00 9.81  ? 222 GLN B C   1 
ATOM   1236 O  O   . GLN B 1 22  ? 15.279 9.878   55.791 1.00 11.30 ? 222 GLN B O   1 
ATOM   1237 C  CB  . GLN B 1 22  ? 15.669 8.122   53.651 1.00 8.84  ? 222 GLN B CB  1 
ATOM   1238 C  CG  . GLN B 1 22  ? 16.910 7.448   54.198 1.00 8.45  ? 222 GLN B CG  1 
ATOM   1239 C  CD  . GLN B 1 22  ? 18.150 7.709   53.371 1.00 8.94  ? 222 GLN B CD  1 
ATOM   1240 O  OE1 . GLN B 1 22  ? 18.300 8.798   52.784 1.00 10.06 ? 222 GLN B OE1 1 
ATOM   1241 N  NE2 . GLN B 1 22  ? 19.036 6.725   53.300 1.00 9.62  ? 222 GLN B NE2 1 
ATOM   1242 N  N   . LYS B 1 23  ? 13.943 8.430   56.879 1.00 10.09 ? 223 LYS B N   1 
ATOM   1243 C  CA  . LYS B 1 23  ? 13.949 9.186   58.118 1.00 11.70 ? 223 LYS B CA  1 
ATOM   1244 C  C   . LYS B 1 23  ? 15.299 9.244   58.804 1.00 10.94 ? 223 LYS B C   1 
ATOM   1245 O  O   . LYS B 1 23  ? 15.549 10.186  59.559 1.00 12.95 ? 223 LYS B O   1 
ATOM   1246 C  CB  . LYS B 1 23  ? 12.962 8.567   59.100 1.00 13.39 ? 223 LYS B CB  1 
ATOM   1247 C  CG  . LYS B 1 23  ? 11.611 9.236   59.153 1.00 18.81 ? 223 LYS B CG  1 
ATOM   1248 C  CD  . LYS B 1 23  ? 11.355 9.720   60.590 1.00 23.70 ? 223 LYS B CD  1 
ATOM   1249 C  CE  . LYS B 1 23  ? 10.417 8.823   61.351 1.00 26.09 ? 223 LYS B CE  1 
ATOM   1250 N  NZ  . LYS B 1 23  ? 9.020  9.009   60.886 1.00 28.50 ? 223 LYS B NZ  1 
ATOM   1251 N  N   . GLU B 1 24  ? 16.140 8.245   58.568 1.00 9.64  ? 224 GLU B N   1 
ATOM   1252 C  CA  . GLU B 1 24  ? 17.468 8.171   59.172 1.00 9.74  ? 224 GLU B CA  1 
ATOM   1253 C  C   . GLU B 1 24  ? 18.540 8.262   58.093 1.00 10.25 ? 224 GLU B C   1 
ATOM   1254 O  O   . GLU B 1 24  ? 18.489 7.538   57.101 1.00 10.46 ? 224 GLU B O   1 
ATOM   1255 C  CB  . GLU B 1 24  ? 17.622 6.866   59.953 1.00 10.19 ? 224 GLU B CB  1 
ATOM   1256 C  CG  . GLU B 1 24  ? 16.630 6.688   61.091 1.00 10.89 ? 224 GLU B CG  1 
ATOM   1257 C  CD  . GLU B 1 24  ? 15.348 5.967   60.708 1.00 11.84 ? 224 GLU B CD  1 
ATOM   1258 O  OE1 . GLU B 1 24  ? 15.323 5.182   59.732 1.00 12.39 ? 224 GLU B OE1 1 
ATOM   1259 O  OE2 . GLU B 1 24  ? 14.352 6.163   61.435 1.00 15.47 ? 224 GLU B OE2 1 
ATOM   1260 N  N   . SER B 1 25  ? 19.514 9.149   58.276 1.00 10.05 ? 225 SER B N   1 
ATOM   1261 C  CA  . SER B 1 25  ? 20.594 9.265   57.313 1.00 10.56 ? 225 SER B CA  1 
ATOM   1262 C  C   . SER B 1 25  ? 21.246 7.900   57.144 1.00 10.22 ? 225 SER B C   1 
ATOM   1263 O  O   . SER B 1 25  ? 21.477 7.197   58.116 1.00 10.68 ? 225 SER B O   1 
ATOM   1264 C  CB  . SER B 1 25  ? 21.620 10.292  57.782 1.00 11.30 ? 225 SER B CB  1 
ATOM   1265 O  OG  . SER B 1 25  ? 21.096 11.611  57.691 1.00 15.50 ? 225 SER B OG  1 
ATOM   1266 N  N   . ASN B 1 26  ? 21.497 7.504   55.906 1.00 10.41 ? 226 ASN B N   1 
ATOM   1267 C  CA  . ASN B 1 26  ? 22.092 6.224   55.565 1.00 11.20 ? 226 ASN B CA  1 
ATOM   1268 C  C   . ASN B 1 26  ? 21.244 5.029   55.939 1.00 11.24 ? 226 ASN B C   1 
ATOM   1269 O  O   . ASN B 1 26  ? 21.718 3.910   55.878 1.00 13.23 ? 226 ASN B O   1 
ATOM   1270 C  CB  . ASN B 1 26  ? 23.479 6.080   56.189 1.00 12.09 ? 226 ASN B CB  1 
ATOM   1271 C  CG  . ASN B 1 26  ? 24.351 7.236   55.862 1.00 12.98 ? 226 ASN B CG  1 
ATOM   1272 O  OD1 . ASN B 1 26  ? 24.513 7.593   54.681 1.00 15.14 ? 226 ASN B OD1 1 
ATOM   1273 N  ND2 . ASN B 1 26  ? 24.898 7.873   56.882 1.00 12.26 ? 226 ASN B ND2 1 
ATOM   1274 N  N   . GLY B 1 27  ? 19.979 5.258   56.264 1.00 11.19 ? 227 GLY B N   1 
ATOM   1275 C  CA  . GLY B 1 27  ? 19.120 4.158   56.635 1.00 10.95 ? 227 GLY B CA  1 
ATOM   1276 C  C   . GLY B 1 27  ? 18.326 3.649   55.453 1.00 11.09 ? 227 GLY B C   1 
ATOM   1277 O  O   . GLY B 1 27  ? 18.470 4.129   54.321 1.00 10.33 ? 227 GLY B O   1 
ATOM   1278 N  N   . PRO B 1 28  ? 17.490 2.652   55.682 1.00 11.46 ? 228 PRO B N   1 
ATOM   1279 C  CA  . PRO B 1 28  ? 16.693 2.121   54.581 1.00 11.52 ? 228 PRO B CA  1 
ATOM   1280 C  C   . PRO B 1 28  ? 15.697 3.164   54.072 1.00 10.92 ? 228 PRO B C   1 
ATOM   1281 O  O   . PRO B 1 28  ? 15.180 4.005   54.802 1.00 11.11 ? 228 PRO B O   1 
ATOM   1282 C  CB  . PRO B 1 28  ? 16.014 0.899   55.194 1.00 12.67 ? 228 PRO B CB  1 
ATOM   1283 C  CG  . PRO B 1 28  ? 16.875 0.578   56.347 1.00 14.38 ? 228 PRO B CG  1 
ATOM   1284 C  CD  . PRO B 1 28  ? 17.275 1.904   56.931 1.00 12.80 ? 228 PRO B CD  1 
ATOM   1285 N  N   . VAL B 1 29  ? 15.464 3.094   52.773 1.00 10.36 ? 229 VAL B N   1 
ATOM   1286 C  CA  . VAL B 1 29  ? 14.513 3.973   52.108 1.00 9.82  ? 229 VAL B CA  1 
ATOM   1287 C  C   . VAL B 1 29  ? 13.231 3.206   51.802 1.00 9.47  ? 229 VAL B C   1 
ATOM   1288 O  O   . VAL B 1 29  ? 13.274 2.138   51.187 1.00 10.39 ? 229 VAL B O   1 
ATOM   1289 C  CB  . VAL B 1 29  ? 15.084 4.512   50.789 1.00 9.55  ? 229 VAL B CB  1 
ATOM   1290 C  CG1 . VAL B 1 29  ? 14.092 5.478   50.120 1.00 9.38  ? 229 VAL B CG1 1 
ATOM   1291 C  CG2 . VAL B 1 29  ? 16.445 5.153   51.023 1.00 10.37 ? 229 VAL B CG2 1 
ATOM   1292 N  N   . LYS B 1 30  ? 12.110 3.733   52.261 1.00 9.54  ? 230 LYS B N   1 
ATOM   1293 C  CA  . LYS B 1 30  ? 10.796 3.199   51.924 1.00 9.86  ? 230 LYS B CA  1 
ATOM   1294 C  C   . LYS B 1 30  ? 10.330 3.851   50.622 1.00 9.53  ? 230 LYS B C   1 
ATOM   1295 O  O   . LYS B 1 30  ? 10.404 5.073   50.474 1.00 10.13 ? 230 LYS B O   1 
ATOM   1296 C  CB  . LYS B 1 30  ? 9.797  3.506   53.039 1.00 11.04 ? 230 LYS B CB  1 
ATOM   1297 C  CG  . LYS B 1 30  ? 10.188 2.983   54.388 1.00 15.24 ? 230 LYS B CG  1 
ATOM   1298 C  CD  . LYS B 1 30  ? 9.247  3.451   55.436 1.00 19.92 ? 230 LYS B CD  1 
ATOM   1299 C  CE  . LYS B 1 30  ? 9.293  2.500   56.588 1.00 22.78 ? 230 LYS B CE  1 
ATOM   1300 N  NZ  . LYS B 1 30  ? 9.897  1.177   56.284 1.00 25.16 ? 230 LYS B NZ  1 
ATOM   1301 N  N   . VAL B 1 31  ? 9.898  3.029   49.671 1.00 9.45  ? 231 VAL B N   1 
ATOM   1302 C  CA  . VAL B 1 31  ? 9.442  3.467   48.362 1.00 9.36  ? 231 VAL B CA  1 
ATOM   1303 C  C   . VAL B 1 31  ? 8.006  2.966   48.196 1.00 9.52  ? 231 VAL B C   1 
ATOM   1304 O  O   . VAL B 1 31  ? 7.764  1.761   48.291 1.00 10.75 ? 231 VAL B O   1 
ATOM   1305 C  CB  . VAL B 1 31  ? 10.321 2.852   47.254 1.00 9.74  ? 231 VAL B CB  1 
ATOM   1306 C  CG1 . VAL B 1 31  ? 9.921  3.396   45.905 1.00 9.70  ? 231 VAL B CG1 1 
ATOM   1307 C  CG2 . VAL B 1 31  ? 11.809 3.094   47.505 1.00 11.45 ? 231 VAL B CG2 1 
ATOM   1308 N  N   . TRP B 1 32  ? 7.055  3.853   47.936 1.00 9.06  ? 232 TRP B N   1 
ATOM   1309 C  CA  . TRP B 1 32  ? 5.673  3.412   47.787 1.00 9.11  ? 232 TRP B CA  1 
ATOM   1310 C  C   . TRP B 1 32  ? 4.862  4.329   46.915 1.00 9.32  ? 232 TRP B C   1 
ATOM   1311 O  O   . TRP B 1 32  ? 5.178  5.501   46.737 1.00 9.08  ? 232 TRP B O   1 
ATOM   1312 C  CB  . TRP B 1 32  ? 4.997  3.259   49.145 1.00 9.48  ? 232 TRP B CB  1 
ATOM   1313 C  CG  . TRP B 1 32  ? 4.588  4.551   49.778 1.00 9.90  ? 232 TRP B CG  1 
ATOM   1314 C  CD1 . TRP B 1 32  ? 3.349  5.111   49.738 1.00 12.12 ? 232 TRP B CD1 1 
ATOM   1315 C  CD2 . TRP B 1 32  ? 5.397  5.431   50.578 1.00 10.76 ? 232 TRP B CD2 1 
ATOM   1316 N  NE1 . TRP B 1 32  ? 3.331  6.281   50.455 1.00 11.98 ? 232 TRP B NE1 1 
ATOM   1317 C  CE2 . TRP B 1 32  ? 4.576  6.503   50.980 1.00 11.18 ? 232 TRP B CE2 1 
ATOM   1318 C  CE3 . TRP B 1 32  ? 6.732  5.427   50.982 1.00 10.44 ? 232 TRP B CE3 1 
ATOM   1319 C  CZ2 . TRP B 1 32  ? 5.040  7.556   51.767 1.00 11.70 ? 232 TRP B CZ2 1 
ATOM   1320 C  CZ3 . TRP B 1 32  ? 7.190  6.475   51.776 1.00 11.27 ? 232 TRP B CZ3 1 
ATOM   1321 C  CH2 . TRP B 1 32  ? 6.343  7.522   52.159 1.00 12.39 ? 232 TRP B CH2 1 
ATOM   1322 N  N   . GLY B 1 33  ? 3.799  3.775   46.356 1.00 9.25  ? 233 GLY B N   1 
ATOM   1323 C  CA  . GLY B 1 33  ? 2.905  4.537   45.521 1.00 9.82  ? 233 GLY B CA  1 
ATOM   1324 C  C   . GLY B 1 33  ? 2.151  3.625   44.595 1.00 10.57 ? 233 GLY B C   1 
ATOM   1325 O  O   . GLY B 1 33  ? 1.989  2.440   44.858 1.00 11.47 ? 233 GLY B O   1 
ATOM   1326 N  N   . SER B 1 34  ? 1.700  4.172   43.485 1.00 11.31 ? 234 SER B N   1 
ATOM   1327 C  CA  . SER B 1 34  ? 0.932  3.402   42.525 1.00 13.02 ? 234 SER B CA  1 
ATOM   1328 C  C   . SER B 1 34  ? 1.240  3.890   41.125 1.00 12.45 ? 234 SER B C   1 
ATOM   1329 O  O   . SER B 1 34  ? 1.581  5.061   40.918 1.00 12.99 ? 234 SER B O   1 
ATOM   1330 C  CB  . SER B 1 34  ? -0.566 3.508   42.821 1.00 14.63 ? 234 SER B CB  1 
ATOM   1331 O  OG  . SER B 1 34  ? -0.956 2.570   43.800 1.00 20.19 ? 234 SER B OG  1 
ATOM   1332 N  N   . ILE B 1 35  ? 1.173  2.947   40.189 1.00 12.10 ? 235 ILE B N   1 
ATOM   1333 C  CA  . ILE B 1 35  ? 1.386  3.209   38.779 1.00 11.86 ? 235 ILE B CA  1 
ATOM   1334 C  C   . ILE B 1 35  ? 0.253  2.547   38.022 1.00 12.13 ? 235 ILE B C   1 
ATOM   1335 O  O   . ILE B 1 35  ? -0.057 1.391   38.265 1.00 12.55 ? 235 ILE B O   1 
ATOM   1336 C  CB  . ILE B 1 35  ? 2.702  2.604   38.294 1.00 11.63 ? 235 ILE B CB  1 
ATOM   1337 C  CG1 . ILE B 1 35  ? 3.845  3.025   39.218 1.00 11.68 ? 235 ILE B CG1 1 
ATOM   1338 C  CG2 . ILE B 1 35  ? 2.974  3.023   36.858 1.00 11.91 ? 235 ILE B CG2 1 
ATOM   1339 C  CD1 . ILE B 1 35  ? 5.169  2.345   38.962 1.00 11.88 ? 235 ILE B CD1 1 
ATOM   1340 N  N   . LYS B 1 36  ? -0.378 3.292   37.129 1.00 11.91 ? 236 LYS B N   1 
ATOM   1341 C  CA  . LYS B 1 36  ? -1.460 2.743   36.303 1.00 12.28 ? 236 LYS B CA  1 
ATOM   1342 C  C   . LYS B 1 36  ? -1.091 2.810   34.824 1.00 11.59 ? 236 LYS B C   1 
ATOM   1343 O  O   . LYS B 1 36  ? -0.113 3.444   34.444 1.00 11.48 ? 236 LYS B O   1 
ATOM   1344 C  CB  . LYS B 1 36  ? -2.790 3.453   36.599 1.00 12.95 ? 236 LYS B CB  1 
ATOM   1345 C  CG  . LYS B 1 36  ? -2.833 4.920   36.232 1.00 14.27 ? 236 LYS B CG  1 
ATOM   1346 C  CD  . LYS B 1 36  ? -4.123 5.610   36.723 1.00 17.02 ? 236 LYS B CD  1 
ATOM   1347 C  CE  . LYS B 1 36  ? -4.228 7.043   36.225 1.00 18.72 ? 236 LYS B CE  1 
ATOM   1348 N  NZ  . LYS B 1 36  ? -5.326 7.820   36.885 1.00 19.44 ? 236 LYS B NZ  1 
ATOM   1349 N  N   . GLY B 1 37  ? -1.895 2.146   33.986 1.00 11.39 ? 237 GLY B N   1 
ATOM   1350 C  CA  . GLY B 1 37  ? -1.680 2.118   32.549 1.00 11.43 ? 237 GLY B CA  1 
ATOM   1351 C  C   . GLY B 1 37  ? -0.743 1.040   32.037 1.00 11.06 ? 237 GLY B C   1 
ATOM   1352 O  O   . GLY B 1 37  ? -0.309 1.077   30.888 1.00 11.71 ? 237 GLY B O   1 
ATOM   1353 N  N   . LEU B 1 38  ? -0.405 0.103   32.910 1.00 11.30 ? 238 LEU B N   1 
ATOM   1354 C  CA  . LEU B 1 38  ? 0.533  -0.968  32.597 1.00 11.23 ? 238 LEU B CA  1 
ATOM   1355 C  C   . LEU B 1 38  ? -0.150 -2.238  32.115 1.00 12.00 ? 238 LEU B C   1 
ATOM   1356 O  O   . LEU B 1 38  ? -1.284 -2.525  32.512 1.00 13.32 ? 238 LEU B O   1 
ATOM   1357 C  CB  . LEU B 1 38  ? 1.312  -1.321  33.871 1.00 10.94 ? 238 LEU B CB  1 
ATOM   1358 C  CG  . LEU B 1 38  ? 2.256  -0.232  34.397 1.00 11.31 ? 238 LEU B CG  1 
ATOM   1359 C  CD1 . LEU B 1 38  ? 2.707  -0.559  35.821 1.00 11.79 ? 238 LEU B CD1 1 
ATOM   1360 C  CD2 . LEU B 1 38  ? 3.432  -0.089  33.459 1.00 12.74 ? 238 LEU B CD2 1 
ATOM   1361 N  N   . THR B 1 39  ? 0.556  -3.008  31.299 1.00 12.67 ? 239 THR B N   1 
ATOM   1362 C  CA  . THR B 1 39  ? 0.098  -4.351  30.981 1.00 13.27 ? 239 THR B CA  1 
ATOM   1363 C  C   . THR B 1 39  ? 0.231  -5.213  32.243 1.00 13.65 ? 239 THR B C   1 
ATOM   1364 O  O   . THR B 1 39  ? 1.158  -5.044  33.049 1.00 13.37 ? 239 THR B O   1 
ATOM   1365 C  CB  . THR B 1 39  ? 0.927  -4.988  29.867 1.00 13.67 ? 239 THR B CB  1 
ATOM   1366 O  OG1 . THR B 1 39  ? 2.317  -4.967  30.228 1.00 14.04 ? 239 THR B OG1 1 
ATOM   1367 C  CG2 . THR B 1 39  ? 0.822  -4.232  28.542 1.00 14.28 ? 239 THR B CG2 1 
ATOM   1368 N  N   . GLU B 1 40  ? -0.684 -6.151  32.423 1.00 14.26 ? 240 GLU B N   1 
ATOM   1369 C  CA  . GLU B 1 40  ? -0.673 -7.035  33.570 1.00 15.10 ? 240 GLU B CA  1 
ATOM   1370 C  C   . GLU B 1 40  ? 0.659  -7.765  33.638 1.00 15.00 ? 240 GLU B C   1 
ATOM   1371 O  O   . GLU B 1 40  ? 1.164  -8.228  32.625 1.00 16.11 ? 240 GLU B O   1 
ATOM   1372 C  CB  . GLU B 1 40  ? -1.809 -8.053  33.427 1.00 16.07 ? 240 GLU B CB  1 
ATOM   1373 C  CG  . GLU B 1 40  ? -1.981 -8.971  34.620 1.00 18.72 ? 240 GLU B CG  1 
ATOM   1374 C  CD  . GLU B 1 40  ? -3.147 -9.934  34.477 1.00 22.01 ? 240 GLU B CD  1 
ATOM   1375 O  OE1 . GLU B 1 40  ? -3.302 -10.795 35.372 1.00 25.13 ? 240 GLU B OE1 1 
ATOM   1376 O  OE2 . GLU B 1 40  ? -3.901 -9.835  33.487 1.00 24.70 ? 240 GLU B OE2 1 
ATOM   1377 N  N   . GLY B 1 41  ? 1.230  -7.877  34.829 1.00 14.43 ? 241 GLY B N   1 
ATOM   1378 C  CA  . GLY B 1 41  ? 2.476  -8.603  34.981 1.00 14.14 ? 241 GLY B CA  1 
ATOM   1379 C  C   . GLY B 1 41  ? 3.609  -7.757  35.521 1.00 13.28 ? 241 GLY B C   1 
ATOM   1380 O  O   . GLY B 1 41  ? 3.382  -6.661  36.081 1.00 13.21 ? 241 GLY B O   1 
ATOM   1381 N  N   . LEU B 1 42  ? 4.820  -8.275  35.348 1.00 13.19 ? 242 LEU B N   1 
ATOM   1382 C  CA  . LEU B 1 42  ? 6.022  -7.670  35.915 1.00 12.84 ? 242 LEU B CA  1 
ATOM   1383 C  C   . LEU B 1 42  ? 6.642  -6.615  35.021 1.00 12.05 ? 242 LEU B C   1 
ATOM   1384 O  O   . LEU B 1 42  ? 6.757  -6.783  33.815 1.00 12.69 ? 242 LEU B O   1 
ATOM   1385 C  CB  . LEU B 1 42  ? 7.061  -8.763  36.175 1.00 12.92 ? 242 LEU B CB  1 
ATOM   1386 C  CG  . LEU B 1 42  ? 6.696  -9.809  37.224 1.00 14.49 ? 242 LEU B CG  1 
ATOM   1387 C  CD1 . LEU B 1 42  ? 7.608  -11.028 37.145 1.00 16.07 ? 242 LEU B CD1 1 
ATOM   1388 C  CD2 . LEU B 1 42  ? 6.754  -9.199  38.602 1.00 15.49 ? 242 LEU B CD2 1 
ATOM   1389 N  N   . HIS B 1 43  ? 7.106  -5.540  35.659 1.00 10.86 ? 243 HIS B N   1 
ATOM   1390 C  CA  . HIS B 1 43  ? 7.731  -4.431  34.969 1.00 10.50 ? 243 HIS B CA  1 
ATOM   1391 C  C   . HIS B 1 43  ? 8.967  -3.974  35.727 1.00 9.84  ? 243 HIS B C   1 
ATOM   1392 O  O   . HIS B 1 43  ? 8.892  -3.667  36.914 1.00 9.87  ? 243 HIS B O   1 
ATOM   1393 C  CB  . HIS B 1 43  ? 6.752  -3.268  34.851 1.00 10.65 ? 243 HIS B CB  1 
ATOM   1394 C  CG  . HIS B 1 43  ? 5.587  -3.575  33.966 1.00 11.15 ? 243 HIS B CG  1 
ATOM   1395 N  ND1 . HIS B 1 43  ? 5.634  -3.391  32.600 1.00 11.85 ? 243 HIS B ND1 1 
ATOM   1396 C  CD2 . HIS B 1 43  ? 4.380  -4.127  34.238 1.00 11.64 ? 243 HIS B CD2 1 
ATOM   1397 C  CE1 . HIS B 1 43  ? 4.484  -3.791  32.077 1.00 11.33 ? 243 HIS B CE1 1 
ATOM   1398 N  NE2 . HIS B 1 43  ? 3.707  -4.230  33.049 1.00 12.35 ? 243 HIS B NE2 1 
ATOM   1399 N  N   . GLY B 1 44  ? 10.089 -3.880  35.027 1.00 9.90  ? 244 GLY B N   1 
ATOM   1400 C  CA  . GLY B 1 44  ? 11.319 -3.447  35.670 1.00 10.03 ? 244 GLY B CA  1 
ATOM   1401 C  C   . GLY B 1 44  ? 11.185 -2.040  36.229 1.00 9.63  ? 244 GLY B C   1 
ATOM   1402 O  O   . GLY B 1 44  ? 10.552 -1.188  35.609 1.00 10.03 ? 244 GLY B O   1 
ATOM   1403 N  N   . PHE B 1 45  ? 11.855 -1.793  37.347 1.00 9.31  ? 245 PHE B N   1 
ATOM   1404 C  CA  . PHE B 1 45  ? 11.664 -0.558  38.121 1.00 9.04  ? 245 PHE B CA  1 
ATOM   1405 C  C   . PHE B 1 45  ? 13.065 -0.105  38.518 1.00 8.79  ? 245 PHE B C   1 
ATOM   1406 O  O   . PHE B 1 45  ? 13.701 -0.739  39.364 1.00 9.19  ? 245 PHE B O   1 
ATOM   1407 C  CB  . PHE B 1 45  ? 10.803 -0.896  39.339 1.00 9.13  ? 245 PHE B CB  1 
ATOM   1408 C  CG  . PHE B 1 45  ? 10.216 0.298   40.082 1.00 9.35  ? 245 PHE B CG  1 
ATOM   1409 C  CD1 . PHE B 1 45  ? 10.208 0.317   41.464 1.00 10.83 ? 245 PHE B CD1 1 
ATOM   1410 C  CD2 . PHE B 1 45  ? 9.582  1.341   39.419 1.00 9.84  ? 245 PHE B CD2 1 
ATOM   1411 C  CE1 . PHE B 1 45  ? 9.618  1.365   42.162 1.00 11.15 ? 245 PHE B CE1 1 
ATOM   1412 C  CE2 . PHE B 1 45  ? 9.006  2.395   40.131 1.00 11.16 ? 245 PHE B CE2 1 
ATOM   1413 C  CZ  . PHE B 1 45  ? 9.020  2.393   41.488 1.00 11.66 ? 245 PHE B CZ  1 
ATOM   1414 N  N   . HIS B 1 46  ? 13.544 0.978   37.911 1.00 8.87  ? 246 HIS B N   1 
ATOM   1415 C  CA  . HIS B 1 46  ? 14.946 1.356   38.037 1.00 9.12  ? 246 HIS B CA  1 
ATOM   1416 C  C   . HIS B 1 46  ? 15.134 2.839   38.238 1.00 8.16  ? 246 HIS B C   1 
ATOM   1417 O  O   . HIS B 1 46  ? 14.413 3.635   37.651 1.00 9.62  ? 246 HIS B O   1 
ATOM   1418 C  CB  . HIS B 1 46  ? 15.690 1.125   36.711 1.00 9.89  ? 246 HIS B CB  1 
ATOM   1419 C  CG  . HIS B 1 46  ? 15.763 -0.291  36.243 1.00 12.11 ? 246 HIS B CG  1 
ATOM   1420 N  ND1 . HIS B 1 46  ? 16.056 -0.592  34.927 1.00 13.04 ? 246 HIS B ND1 1 
ATOM   1421 C  CD2 . HIS B 1 46  ? 15.598 -1.474  36.880 1.00 12.90 ? 246 HIS B CD2 1 
ATOM   1422 C  CE1 . HIS B 1 46  ? 16.070 -1.906  34.781 1.00 13.41 ? 246 HIS B CE1 1 
ATOM   1423 N  NE2 . HIS B 1 46  ? 15.796 -2.463  35.947 1.00 13.72 ? 246 HIS B NE2 1 
ATOM   1424 N  N   . VAL B 1 47  ? 16.181 3.203   38.959 1.00 8.09  ? 247 VAL B N   1 
ATOM   1425 C  CA  . VAL B 1 47  ? 16.664 4.578   38.959 1.00 8.26  ? 247 VAL B CA  1 
ATOM   1426 C  C   . VAL B 1 47  ? 17.759 4.655   37.896 1.00 7.86  ? 247 VAL B C   1 
ATOM   1427 O  O   . VAL B 1 47  ? 18.688 3.827   37.902 1.00 9.46  ? 247 VAL B O   1 
ATOM   1428 C  CB  . VAL B 1 47  ? 17.234 5.008   40.325 1.00 7.83  ? 247 VAL B CB  1 
ATOM   1429 C  CG1 . VAL B 1 47  ? 17.736 6.470   40.283 1.00 8.61  ? 247 VAL B CG1 1 
ATOM   1430 C  CG2 . VAL B 1 47  ? 16.179 4.843   41.397 1.00 9.66  ? 247 VAL B CG2 1 
ATOM   1431 N  N   . HIS B 1 48  ? 17.615 5.596   36.970 1.00 7.43  ? 248 HIS B N   1 
ATOM   1432 C  CA  . HIS B 1 48  ? 18.585 5.870   35.925 1.00 7.99  ? 248 HIS B CA  1 
ATOM   1433 C  C   . HIS B 1 48  ? 19.397 7.095   36.322 1.00 8.16  ? 248 HIS B C   1 
ATOM   1434 O  O   . HIS B 1 48  ? 18.944 7.932   37.112 1.00 8.94  ? 248 HIS B O   1 
ATOM   1435 C  CB  . HIS B 1 48  ? 17.882 5.998   34.574 1.00 8.69  ? 248 HIS B CB  1 
ATOM   1436 C  CG  . HIS B 1 48  ? 17.538 4.667   33.980 1.00 9.27  ? 248 HIS B CG  1 
ATOM   1437 N  ND1 . HIS B 1 48  ? 18.144 4.192   32.839 1.00 10.57 ? 248 HIS B ND1 1 
ATOM   1438 C  CD2 . HIS B 1 48  ? 16.684 3.691   34.389 1.00 10.25 ? 248 HIS B CD2 1 
ATOM   1439 C  CE1 . HIS B 1 48  ? 17.673 2.985   32.566 1.00 12.33 ? 248 HIS B CE1 1 
ATOM   1440 N  NE2 . HIS B 1 48  ? 16.792 2.653   33.490 1.00 10.89 ? 248 HIS B NE2 1 
ATOM   1441 N  N   . GLU B 1 49  ? 20.600 7.184   35.777 1.00 8.83  ? 249 GLU B N   1 
ATOM   1442 C  CA  . GLU B 1 49  ? 21.603 8.127   36.237 1.00 9.01  ? 249 GLU B CA  1 
ATOM   1443 C  C   . GLU B 1 49  ? 21.253 9.600   36.198 1.00 8.96  ? 249 GLU B C   1 
ATOM   1444 O  O   . GLU B 1 49  ? 21.556 10.334  37.150 1.00 9.53  ? 249 GLU B O   1 
ATOM   1445 C  CB  . GLU B 1 49  ? 22.875 7.915   35.400 1.00 9.77  ? 249 GLU B CB  1 
ATOM   1446 C  CG  . GLU B 1 49  ? 24.072 8.729   35.869 1.00 10.81 ? 249 GLU B CG  1 
ATOM   1447 C  CD  . GLU B 1 49  ? 25.352 8.429   35.102 1.00 12.99 ? 249 GLU B CD  1 
ATOM   1448 O  OE1 . GLU B 1 49  ? 25.302 7.722   34.068 1.00 13.16 ? 249 GLU B OE1 1 
ATOM   1449 O  OE2 . GLU B 1 49  ? 26.424 8.901   35.532 1.00 14.17 ? 249 GLU B OE2 1 
ATOM   1450 N  N   . PHE B 1 50  ? 20.647 10.047  35.116 1.00 8.80  ? 250 PHE B N   1 
ATOM   1451 C  CA  . PHE B 1 50  ? 20.448 11.477  34.918 1.00 9.05  ? 250 PHE B CA  1 
ATOM   1452 C  C   . PHE B 1 50  ? 19.003 11.868  35.042 1.00 9.23  ? 250 PHE B C   1 
ATOM   1453 O  O   . PHE B 1 50  ? 18.115 11.196  34.511 1.00 9.52  ? 250 PHE B O   1 
ATOM   1454 C  CB  . PHE B 1 50  ? 20.964 11.883  33.533 1.00 10.19 ? 250 PHE B CB  1 
ATOM   1455 C  CG  . PHE B 1 50  ? 22.435 11.627  33.342 1.00 11.64 ? 250 PHE B CG  1 
ATOM   1456 C  CD1 . PHE B 1 50  ? 23.363 12.230  34.162 1.00 12.99 ? 250 PHE B CD1 1 
ATOM   1457 C  CD2 . PHE B 1 50  ? 22.873 10.720  32.385 1.00 12.94 ? 250 PHE B CD2 1 
ATOM   1458 C  CE1 . PHE B 1 50  ? 24.717 11.974  34.003 1.00 14.31 ? 250 PHE B CE1 1 
ATOM   1459 C  CE2 . PHE B 1 50  ? 24.218 10.467  32.224 1.00 14.66 ? 250 PHE B CE2 1 
ATOM   1460 C  CZ  . PHE B 1 50  ? 25.125 11.081  33.038 1.00 15.08 ? 250 PHE B CZ  1 
ATOM   1461 N  N   . GLY B 1 51  ? 18.791 12.984  35.740 1.00 9.15  ? 251 GLY B N   1 
ATOM   1462 C  CA  . GLY B 1 51  ? 17.468 13.590  35.840 1.00 9.47  ? 251 GLY B CA  1 
ATOM   1463 C  C   . GLY B 1 51  ? 17.235 14.485  34.639 1.00 10.17 ? 251 GLY B C   1 
ATOM   1464 O  O   . GLY B 1 51  ? 16.901 15.669  34.772 1.00 9.63  ? 251 GLY B O   1 
ATOM   1465 N  N   . ASP B 1 52  ? 17.416 13.892  33.454 1.00 10.77 ? 252 ASP B N   1 
ATOM   1466 C  CA  . ASP B 1 52  ? 17.393 14.610  32.190 1.00 12.02 ? 252 ASP B CA  1 
ATOM   1467 C  C   . ASP B 1 52  ? 16.263 14.042  31.385 1.00 12.43 ? 252 ASP B C   1 
ATOM   1468 O  O   . ASP B 1 52  ? 16.326 12.914  30.893 1.00 12.77 ? 252 ASP B O   1 
ATOM   1469 C  CB  . ASP B 1 52  ? 18.711 14.386  31.460 1.00 11.84 ? 252 ASP B CB  1 
ATOM   1470 C  CG  . ASP B 1 52  ? 18.803 15.123  30.135 1.00 12.96 ? 252 ASP B CG  1 
ATOM   1471 O  OD1 . ASP B 1 52  ? 17.753 15.437  29.538 1.00 13.47 ? 252 ASP B OD1 1 
ATOM   1472 O  OD2 . ASP B 1 52  ? 19.910 15.396  29.622 1.00 15.40 ? 252 ASP B OD2 1 
ATOM   1473 N  N   . ASN B 1 53  ? 15.202 14.804  31.266 1.00 13.06 ? 253 ASN B N   1 
ATOM   1474 C  CA  . ASN B 1 53  ? 14.067 14.356  30.500 1.00 14.71 ? 253 ASN B CA  1 
ATOM   1475 C  C   . ASN B 1 53  ? 13.872 15.207  29.228 1.00 14.34 ? 253 ASN B C   1 
ATOM   1476 O  O   . ASN B 1 53  ? 12.771 15.306  28.684 1.00 14.63 ? 253 ASN B O   1 
ATOM   1477 C  CB  . ASN B 1 53  ? 12.843 14.296  31.415 1.00 16.27 ? 253 ASN B CB  1 
ATOM   1478 C  CG  . ASN B 1 53  ? 12.920 13.137  32.460 1.00 18.94 ? 253 ASN B CG  1 
ATOM   1479 O  OD1 . ASN B 1 53  ? 12.022 12.992  33.304 1.00 22.80 ? 253 ASN B OD1 1 
ATOM   1480 N  ND2 . ASN B 1 53  ? 13.985 12.317  32.407 1.00 19.96 ? 253 ASN B ND2 1 
ATOM   1481 N  N   . THR B 1 54  ? 14.971 15.777  28.730 1.00 14.38 ? 254 THR B N   1 
ATOM   1482 C  CA  . THR B 1 54  ? 14.911 16.620  27.525 1.00 15.21 ? 254 THR B CA  1 
ATOM   1483 C  C   . THR B 1 54  ? 14.416 15.850  26.302 1.00 15.73 ? 254 THR B C   1 
ATOM   1484 O  O   . THR B 1 54  ? 13.803 16.444  25.405 1.00 16.42 ? 254 THR B O   1 
ATOM   1485 C  CB  . THR B 1 54  ? 16.282 17.254  27.195 1.00 15.11 ? 254 THR B CB  1 
ATOM   1486 O  OG1 . THR B 1 54  ? 17.284 16.237  27.045 1.00 15.85 ? 254 THR B OG1 1 
ATOM   1487 C  CG2 . THR B 1 54  ? 16.765 18.165  28.297 1.00 15.37 ? 254 THR B CG2 1 
ATOM   1488 N  N   . ALA B 1 55  ? 14.707 14.554  26.247 1.00 15.94 ? 255 ALA B N   1 
ATOM   1489 C  CA  . ALA B 1 55  ? 14.222 13.666  25.179 1.00 16.39 ? 255 ALA B CA  1 
ATOM   1490 C  C   . ALA B 1 55  ? 13.333 12.588  25.794 1.00 16.08 ? 255 ALA B C   1 
ATOM   1491 O  O   . ALA B 1 55  ? 13.426 11.397  25.482 1.00 16.95 ? 255 ALA B O   1 
ATOM   1492 C  CB  . ALA B 1 55  ? 15.377 13.030  24.426 1.00 16.83 ? 255 ALA B CB  1 
ATOM   1493 N  N   . GLY B 1 56  ? 12.463 13.010  26.696 1.00 15.84 ? 256 GLY B N   1 
ATOM   1494 C  CA  . GLY B 1 56  ? 11.603 12.083  27.388 1.00 15.45 ? 256 GLY B CA  1 
ATOM   1495 C  C   . GLY B 1 56  ? 12.471 11.157  28.215 1.00 15.17 ? 256 GLY B C   1 
ATOM   1496 O  O   . GLY B 1 56  ? 13.535 11.555  28.708 1.00 15.88 ? 256 GLY B O   1 
ATOM   1497 N  N   . CYS B 1 57  ? 12.057 9.898   28.305 1.00 13.99 ? 257 CYS B N   1 
ATOM   1498 C  CA  . CYS B 1 57  ? 12.797 8.931   29.080 1.00 13.94 ? 257 CYS B CA  1 
ATOM   1499 C  C   . CYS B 1 57  ? 14.075 8.486   28.385 1.00 14.11 ? 257 CYS B C   1 
ATOM   1500 O  O   . CYS B 1 57  ? 14.931 7.884   29.021 1.00 13.56 ? 257 CYS B O   1 
ATOM   1501 C  CB  . CYS B 1 57  ? 11.910 7.730   29.391 1.00 13.97 ? 257 CYS B CB  1 
ATOM   1502 S  SG  . CYS B 1 57  ? 10.361 8.186   30.215 1.00 13.97 ? 257 CYS B SG  1 
ATOM   1503 N  N   . THR B 1 58  ? 14.211 8.795   27.096 1.00 13.98 ? 258 THR B N   1 
ATOM   1504 C  CA  . THR B 1 58  ? 15.376 8.334   26.343 1.00 14.68 ? 258 THR B CA  1 
ATOM   1505 C  C   . THR B 1 58  ? 16.663 9.028   26.754 1.00 14.08 ? 258 THR B C   1 
ATOM   1506 O  O   . THR B 1 58  ? 17.728 8.513   26.450 1.00 15.41 ? 258 THR B O   1 
ATOM   1507 C  CB  . THR B 1 58  ? 15.198 8.471   24.809 1.00 15.45 ? 258 THR B CB  1 
ATOM   1508 O  OG1 . THR B 1 58  ? 15.321 9.843   24.423 1.00 17.05 ? 258 THR B OG1 1 
ATOM   1509 C  CG2 . THR B 1 58  ? 13.822 8.064   24.340 1.00 16.17 ? 258 THR B CG2 1 
ATOM   1510 N  N   . SER B 1 59  ? 16.570 10.175  27.445 1.00 12.93 ? 259 SER B N   1 
ATOM   1511 C  CA  . SER B 1 59  ? 17.744 10.930  27.887 1.00 13.51 ? 259 SER B CA  1 
ATOM   1512 C  C   . SER B 1 59  ? 18.126 10.691  29.357 1.00 12.92 ? 259 SER B C   1 
ATOM   1513 O  O   . SER B 1 59  ? 19.029 11.343  29.878 1.00 13.17 ? 259 SER B O   1 
ATOM   1514 C  CB  . SER B 1 59  ? 17.524 12.433  27.664 1.00 13.93 ? 259 SER B CB  1 
ATOM   1515 O  OG  . SER B 1 59  ? 16.249 12.827  28.095 1.00 14.09 ? 259 SER B OG  1 
ATOM   1516 N  N   . ALA B 1 60  ? 17.483 9.729   30.000 1.00 12.23 ? 260 ALA B N   1 
ATOM   1517 C  CA  . ALA B 1 60  ? 17.730 9.469   31.428 1.00 12.03 ? 260 ALA B CA  1 
ATOM   1518 C  C   . ALA B 1 60  ? 19.068 8.792   31.704 1.00 11.05 ? 260 ALA B C   1 
ATOM   1519 O  O   . ALA B 1 60  ? 19.451 8.625   32.854 1.00 10.71 ? 260 ALA B O   1 
ATOM   1520 C  CB  . ALA B 1 60  ? 16.622 8.648   32.001 1.00 12.79 ? 260 ALA B CB  1 
ATOM   1521 N  N   . GLY B 1 61  ? 19.765 8.347   30.665 1.00 10.83 ? 261 GLY B N   1 
ATOM   1522 C  CA  . GLY B 1 61  ? 21.038 7.699   30.877 1.00 10.77 ? 261 GLY B CA  1 
ATOM   1523 C  C   . GLY B 1 61  ? 20.910 6.246   31.257 1.00 10.82 ? 261 GLY B C   1 
ATOM   1524 O  O   . GLY B 1 61  ? 19.823 5.681   31.255 1.00 10.62 ? 261 GLY B O   1 
ATOM   1525 N  N   . PRO B 1 62  ? 22.030 5.640   31.623 1.00 10.88 ? 262 PRO B N   1 
ATOM   1526 C  CA  . PRO B 1 62  ? 22.033 4.224   31.980 1.00 12.11 ? 262 PRO B CA  1 
ATOM   1527 C  C   . PRO B 1 62  ? 21.490 4.002   33.380 1.00 12.20 ? 262 PRO B C   1 
ATOM   1528 O  O   . PRO B 1 62  ? 21.210 4.973   34.082 1.00 11.33 ? 262 PRO B O   1 
ATOM   1529 C  CB  . PRO B 1 62  ? 23.516 3.867   31.936 1.00 12.77 ? 262 PRO B CB  1 
ATOM   1530 C  CG  . PRO B 1 62  ? 24.221 5.117   32.263 1.00 12.25 ? 262 PRO B CG  1 
ATOM   1531 C  CD  . PRO B 1 62  ? 23.370 6.237   31.726 1.00 11.03 ? 262 PRO B CD  1 
ATOM   1532 N  N   . HIS B 1 63  ? 21.346 2.749   33.788 1.00 13.12 ? 263 HIS B N   1 
ATOM   1533 C  CA  . HIS B 1 63  ? 20.947 2.429   35.153 1.00 14.93 ? 263 HIS B CA  1 
ATOM   1534 C  C   . HIS B 1 63  ? 21.942 3.094   36.071 1.00 14.53 ? 263 HIS B C   1 
ATOM   1535 O  O   . HIS B 1 63  ? 23.143 3.068   35.809 1.00 15.35 ? 263 HIS B O   1 
ATOM   1536 C  CB  . HIS B 1 63  ? 21.059 0.942   35.463 1.00 17.15 ? 263 HIS B CB  1 
ATOM   1537 C  CG  . HIS B 1 63  ? 20.073 0.087   34.753 1.00 21.48 ? 263 HIS B CG  1 
ATOM   1538 N  ND1 . HIS B 1 63  ? 19.816 -1.212  35.134 1.00 24.70 ? 263 HIS B ND1 1 
ATOM   1539 C  CD2 . HIS B 1 63  ? 19.298 0.325   33.673 1.00 23.98 ? 263 HIS B CD2 1 
ATOM   1540 C  CE1 . HIS B 1 63  ? 18.924 -1.739  34.316 1.00 25.88 ? 263 HIS B CE1 1 
ATOM   1541 N  NE2 . HIS B 1 63  ? 18.590 -0.825  33.422 1.00 26.16 ? 263 HIS B NE2 1 
ATOM   1542 N  N   . PHE B 1 64  ? 21.462 3.681   37.151 1.00 13.80 ? 264 PHE B N   1 
ATOM   1543 C  CA  . PHE B 1 64  ? 22.343 4.320   38.107 1.00 13.75 ? 264 PHE B CA  1 
ATOM   1544 C  C   . PHE B 1 64  ? 23.219 3.252   38.782 1.00 15.09 ? 264 PHE B C   1 
ATOM   1545 O  O   . PHE B 1 64  ? 22.729 2.321   39.427 1.00 14.58 ? 264 PHE B O   1 
ATOM   1546 C  CB  . PHE B 1 64  ? 21.503 5.088   39.125 1.00 13.14 ? 264 PHE B CB  1 
ATOM   1547 C  CG  . PHE B 1 64  ? 22.308 5.815   40.156 1.00 13.54 ? 264 PHE B CG  1 
ATOM   1548 C  CD1 . PHE B 1 64  ? 23.392 6.594   39.804 1.00 14.15 ? 264 PHE B CD1 1 
ATOM   1549 C  CD2 . PHE B 1 64  ? 21.965 5.716   41.493 1.00 13.57 ? 264 PHE B CD2 1 
ATOM   1550 C  CE1 . PHE B 1 64  ? 24.115 7.258   40.781 1.00 15.24 ? 264 PHE B CE1 1 
ATOM   1551 C  CE2 . PHE B 1 64  ? 22.680 6.367   42.462 1.00 14.51 ? 264 PHE B CE2 1 
ATOM   1552 C  CZ  . PHE B 1 64  ? 23.757 7.139   42.108 1.00 14.89 ? 264 PHE B CZ  1 
ATOM   1553 N  N   . ASN B 1 65  ? 24.526 3.397   38.619 1.00 16.46 ? 265 ASN B N   1 
ATOM   1554 C  CA  . ASN B 1 65  ? 25.467 2.439   39.173 1.00 18.74 ? 265 ASN B CA  1 
ATOM   1555 C  C   . ASN B 1 65  ? 26.851 3.047   39.272 1.00 19.57 ? 265 ASN B C   1 
ATOM   1556 O  O   . ASN B 1 65  ? 27.742 2.749   38.469 1.00 19.65 ? 265 ASN B O   1 
ATOM   1557 C  CB  . ASN B 1 65  ? 25.508 1.174   38.330 1.00 19.49 ? 265 ASN B CB  1 
ATOM   1558 C  CG  . ASN B 1 65  ? 26.133 0.015   39.076 1.00 22.13 ? 265 ASN B CG  1 
ATOM   1559 O  OD1 . ASN B 1 65  ? 25.823 -0.213  40.248 1.00 24.20 ? 265 ASN B OD1 1 
ATOM   1560 N  ND2 . ASN B 1 65  ? 27.013 -0.718  38.410 1.00 25.15 ? 265 ASN B ND2 1 
ATOM   1561 N  N   . PRO B 1 66  ? 27.040 3.895   40.272 1.00 21.19 ? 266 PRO B N   1 
ATOM   1562 C  CA  . PRO B 1 66  ? 28.308 4.611   40.443 1.00 22.42 ? 266 PRO B CA  1 
ATOM   1563 C  C   . PRO B 1 66  ? 29.502 3.691   40.713 1.00 23.25 ? 266 PRO B C   1 
ATOM   1564 O  O   . PRO B 1 66  ? 30.413 3.731   39.876 1.00 24.92 ? 266 PRO B O   1 
ATOM   1565 C  CB  . PRO B 1 66  ? 28.037 5.534   41.637 1.00 22.82 ? 266 PRO B CB  1 
ATOM   1566 C  CG  . PRO B 1 66  ? 26.881 4.980   42.322 1.00 22.05 ? 266 PRO B CG  1 
ATOM   1567 C  CD  . PRO B 1 66  ? 26.074 4.203   41.338 1.00 21.30 ? 266 PRO B CD  1 
ATOM   1568 N  N   . HIS B 1 80  ? 23.010 -3.529  40.682 1.00 23.77 ? 280 HIS B N   1 
ATOM   1569 C  CA  . HIS B 1 80  ? 22.996 -2.109  40.375 1.00 22.90 ? 280 HIS B CA  1 
ATOM   1570 C  C   . HIS B 1 80  ? 22.341 -1.334  41.505 1.00 20.88 ? 280 HIS B C   1 
ATOM   1571 O  O   . HIS B 1 80  ? 21.270 -1.707  41.949 1.00 19.51 ? 280 HIS B O   1 
ATOM   1572 C  CB  . HIS B 1 80  ? 22.194 -1.865  39.102 1.00 24.36 ? 280 HIS B CB  1 
ATOM   1573 C  CG  . HIS B 1 80  ? 22.976 -2.058  37.842 1.00 26.97 ? 280 HIS B CG  1 
ATOM   1574 N  ND1 . HIS B 1 80  ? 22.451 -1.782  36.599 1.00 29.64 ? 280 HIS B ND1 1 
ATOM   1575 C  CD2 . HIS B 1 80  ? 24.242 -2.490  37.628 1.00 29.11 ? 280 HIS B CD2 1 
ATOM   1576 C  CE1 . HIS B 1 80  ? 23.358 -2.029  35.673 1.00 30.10 ? 280 HIS B CE1 1 
ATOM   1577 N  NE2 . HIS B 1 80  ? 24.455 -2.462  36.270 1.00 30.63 ? 280 HIS B NE2 1 
ATOM   1578 N  N   . VAL B 1 81  ? 22.970 -0.244  41.932 1.00 18.32 ? 281 VAL B N   1 
ATOM   1579 C  CA  . VAL B 1 81  ? 22.417 0.610   42.973 1.00 16.99 ? 281 VAL B CA  1 
ATOM   1580 C  C   . VAL B 1 81  ? 20.981 1.030   42.635 1.00 15.12 ? 281 VAL B C   1 
ATOM   1581 O  O   . VAL B 1 81  ? 20.095 1.018   43.492 1.00 14.85 ? 281 VAL B O   1 
ATOM   1582 C  CB  . VAL B 1 81  ? 23.289 1.876   43.173 1.00 17.28 ? 281 VAL B CB  1 
ATOM   1583 C  CG1 . VAL B 1 81  ? 22.595 2.879   44.060 1.00 18.00 ? 281 VAL B CG1 1 
ATOM   1584 C  CG2 . VAL B 1 81  ? 24.652 1.499   43.754 1.00 17.84 ? 281 VAL B CG2 1 
ATOM   1585 N  N   . GLY B 1 82  ? 20.756 1.385   41.375 1.00 13.74 ? 282 GLY B N   1 
ATOM   1586 C  CA  . GLY B 1 82  ? 19.442 1.850   40.950 1.00 13.26 ? 282 GLY B CA  1 
ATOM   1587 C  C   . GLY B 1 82  ? 18.395 0.785   40.713 1.00 13.67 ? 282 GLY B C   1 
ATOM   1588 O  O   . GLY B 1 82  ? 17.251 1.120   40.439 1.00 14.08 ? 282 GLY B O   1 
ATOM   1589 N  N   . ASP B 1 83  ? 18.750 -0.488  40.839 1.00 13.81 ? 283 ASP B N   1 
ATOM   1590 C  CA  . ASP B 1 83  ? 17.828 -1.570  40.550 1.00 14.49 ? 283 ASP B CA  1 
ATOM   1591 C  C   . ASP B 1 83  ? 16.869 -1.823  41.697 1.00 13.83 ? 283 ASP B C   1 
ATOM   1592 O  O   . ASP B 1 83  ? 17.256 -2.366  42.739 1.00 15.55 ? 283 ASP B O   1 
ATOM   1593 C  CB  . ASP B 1 83  ? 18.625 -2.835  40.257 1.00 15.40 ? 283 ASP B CB  1 
ATOM   1594 C  CG  . ASP B 1 83  ? 17.774 -3.933  39.686 1.00 18.73 ? 283 ASP B CG  1 
ATOM   1595 O  OD1 . ASP B 1 83  ? 18.348 -4.958  39.249 1.00 22.62 ? 283 ASP B OD1 1 
ATOM   1596 O  OD2 . ASP B 1 83  ? 16.526 -3.861  39.637 1.00 20.15 ? 283 ASP B OD2 1 
ATOM   1597 N  N   . LEU B 1 84  ? 15.602 -1.465  41.499 1.00 12.80 ? 284 LEU B N   1 
ATOM   1598 C  CA  . LEU B 1 84  ? 14.578 -1.643  42.516 1.00 13.37 ? 284 LEU B CA  1 
ATOM   1599 C  C   . LEU B 1 84  ? 13.679 -2.831  42.213 1.00 13.99 ? 284 LEU B C   1 
ATOM   1600 O  O   . LEU B 1 84  ? 12.555 -2.887  42.690 1.00 16.11 ? 284 LEU B O   1 
ATOM   1601 C  CB  . LEU B 1 84  ? 13.730 -0.376  42.660 1.00 13.61 ? 284 LEU B CB  1 
ATOM   1602 C  CG  . LEU B 1 84  ? 14.502 0.864   43.108 1.00 14.35 ? 284 LEU B CG  1 
ATOM   1603 C  CD1 . LEU B 1 84  ? 13.589 2.061   43.096 1.00 14.98 ? 284 LEU B CD1 1 
ATOM   1604 C  CD2 . LEU B 1 84  ? 15.113 0.663   44.491 1.00 16.96 ? 284 LEU B CD2 1 
ATOM   1605 N  N   . GLY B 1 85  ? 14.176 -3.763  41.411 1.00 12.74 ? 285 GLY B N   1 
ATOM   1606 C  CA  . GLY B 1 85  ? 13.439 -4.980  41.103 1.00 12.74 ? 285 GLY B CA  1 
ATOM   1607 C  C   . GLY B 1 85  ? 12.342 -4.742  40.093 1.00 11.99 ? 285 GLY B C   1 
ATOM   1608 O  O   . GLY B 1 85  ? 12.550 -4.066  39.094 1.00 12.17 ? 285 GLY B O   1 
ATOM   1609 N  N   . ASN B 1 86  ? 11.182 -5.329  40.347 1.00 12.63 ? 286 ASN B N   1 
ATOM   1610 C  CA  . ASN B 1 86  ? 10.020 -5.171  39.482 1.00 13.03 ? 286 ASN B CA  1 
ATOM   1611 C  C   . ASN B 1 86  ? 8.823  -4.643  40.265 1.00 12.85 ? 286 ASN B C   1 
ATOM   1612 O  O   . ASN B 1 86  ? 8.788  -4.712  41.496 1.00 14.64 ? 286 ASN B O   1 
ATOM   1613 C  CB  . ASN B 1 86  ? 9.637  -6.525  38.872 1.00 14.04 ? 286 ASN B CB  1 
ATOM   1614 C  CG  . ASN B 1 86  ? 10.668 -7.045  37.901 1.00 15.42 ? 286 ASN B CG  1 
ATOM   1615 O  OD1 . ASN B 1 86  ? 10.867 -6.492  36.830 1.00 15.43 ? 286 ASN B OD1 1 
ATOM   1616 N  ND2 . ASN B 1 86  ? 11.353 -8.119  38.291 1.00 19.20 ? 286 ASN B ND2 1 
ATOM   1617 N  N   . VAL B 1 87  ? 7.870  -4.070  39.543 1.00 12.15 ? 287 VAL B N   1 
ATOM   1618 C  CA  . VAL B 1 87  ? 6.568  -3.789  40.112 1.00 12.52 ? 287 VAL B CA  1 
ATOM   1619 C  C   . VAL B 1 87  ? 5.609  -4.744  39.381 1.00 12.57 ? 287 VAL B C   1 
ATOM   1620 O  O   . VAL B 1 87  ? 5.897  -5.203  38.274 1.00 12.48 ? 287 VAL B O   1 
ATOM   1621 C  CB  . VAL B 1 87  ? 6.141  -2.311  39.988 1.00 12.37 ? 287 VAL B CB  1 
ATOM   1622 C  CG1 . VAL B 1 87  ? 7.119  -1.410  40.733 1.00 13.42 ? 287 VAL B CG1 1 
ATOM   1623 C  CG2 . VAL B 1 87  ? 6.006  -1.899  38.531 1.00 13.05 ? 287 VAL B CG2 1 
ATOM   1624 N  N   . THR B 1 88  ? 4.489  -5.059  40.022 1.00 12.84 ? 288 THR B N   1 
ATOM   1625 C  CA  . THR B 1 88  ? 3.530  -6.007  39.473 1.00 13.72 ? 288 THR B CA  1 
ATOM   1626 C  C   . THR B 1 88  ? 2.194  -5.339  39.226 1.00 13.61 ? 288 THR B C   1 
ATOM   1627 O  O   . THR B 1 88  ? 1.548  -4.861  40.155 1.00 14.17 ? 288 THR B O   1 
ATOM   1628 C  CB  . THR B 1 88  ? 3.337  -7.160  40.455 1.00 14.52 ? 288 THR B CB  1 
ATOM   1629 O  OG1 . THR B 1 88  ? 4.610  -7.744  40.777 1.00 14.89 ? 288 THR B OG1 1 
ATOM   1630 C  CG2 . THR B 1 88  ? 2.516  -8.277  39.825 1.00 15.35 ? 288 THR B CG2 1 
ATOM   1631 N  N   . ALA B 1 89  ? 1.787  -5.302  37.967 1.00 13.26 ? 289 ALA B N   1 
ATOM   1632 C  CA  . ALA B 1 89  ? 0.498  -4.735  37.603 1.00 14.00 ? 289 ALA B CA  1 
ATOM   1633 C  C   . ALA B 1 89  ? -0.585 -5.809  37.597 1.00 14.83 ? 289 ALA B C   1 
ATOM   1634 O  O   . ALA B 1 89  ? -0.365 -6.895  37.079 1.00 15.21 ? 289 ALA B O   1 
ATOM   1635 C  CB  . ALA B 1 89  ? 0.585  -4.083  36.246 1.00 13.90 ? 289 ALA B CB  1 
ATOM   1636 N  N   . ASP B 1 90  ? -1.735 -5.485  38.175 1.00 16.01 ? 290 ASP B N   1 
ATOM   1637 C  CA  . ASP B 1 90  ? -2.881 -6.399  38.199 1.00 17.36 ? 290 ASP B CA  1 
ATOM   1638 C  C   . ASP B 1 90  ? -3.647 -6.348  36.874 1.00 18.53 ? 290 ASP B C   1 
ATOM   1639 O  O   . ASP B 1 90  ? -3.217 -5.692  35.920 1.00 17.56 ? 290 ASP B O   1 
ATOM   1640 C  CB  . ASP B 1 90  ? -3.783 -6.095  39.402 1.00 18.10 ? 290 ASP B CB  1 
ATOM   1641 C  CG  . ASP B 1 90  ? -4.449 -4.730  39.338 1.00 18.49 ? 290 ASP B CG  1 
ATOM   1642 O  OD1 . ASP B 1 90  ? -4.525 -4.107  38.261 1.00 17.61 ? 290 ASP B OD1 1 
ATOM   1643 O  OD2 . ASP B 1 90  ? -4.942 -4.197  40.360 1.00 21.27 ? 290 ASP B OD2 1 
ATOM   1644 N  N   . LYS B 1 91  ? -4.775 -7.059  36.815 1.00 19.66 ? 291 LYS B N   1 
ATOM   1645 C  CA  . LYS B 1 91  ? -5.601 -7.135  35.604 1.00 21.00 ? 291 LYS B CA  1 
ATOM   1646 C  C   . LYS B 1 91  ? -6.126 -5.778  35.124 1.00 20.72 ? 291 LYS B C   1 
ATOM   1647 O  O   . LYS B 1 91  ? -6.429 -5.611  33.940 1.00 21.64 ? 291 LYS B O   1 
ATOM   1648 C  CB  . LYS B 1 91  ? -6.779 -8.103  35.822 1.00 21.89 ? 291 LYS B CB  1 
ATOM   1649 C  CG  . LYS B 1 91  ? -6.359 -9.524  36.150 1.00 25.19 ? 291 LYS B CG  1 
ATOM   1650 C  CD  . LYS B 1 91  ? -7.552 -10.462 36.304 1.00 28.15 ? 291 LYS B CD  1 
ATOM   1651 C  CE  . LYS B 1 91  ? -7.113 -11.863 36.723 1.00 30.08 ? 291 LYS B CE  1 
ATOM   1652 N  NZ  . LYS B 1 91  ? -8.254 -12.826 36.774 1.00 31.86 ? 291 LYS B NZ  1 
ATOM   1653 N  N   . ASP B 1 92  ? -6.221 -4.811  36.035 1.00 19.78 ? 292 ASP B N   1 
ATOM   1654 C  CA  . ASP B 1 92  ? -6.681 -3.464  35.704 1.00 19.38 ? 292 ASP B CA  1 
ATOM   1655 C  C   . ASP B 1 92  ? -5.537 -2.541  35.261 1.00 17.15 ? 292 ASP B C   1 
ATOM   1656 O  O   . ASP B 1 92  ? -5.766 -1.350  34.995 1.00 16.90 ? 292 ASP B O   1 
ATOM   1657 C  CB  . ASP B 1 92  ? -7.355 -2.819  36.914 1.00 20.14 ? 292 ASP B CB  1 
ATOM   1658 C  CG  . ASP B 1 92  ? -8.733 -3.355  37.171 1.00 23.52 ? 292 ASP B CG  1 
ATOM   1659 O  OD1 . ASP B 1 92  ? -9.498 -3.527  36.197 1.00 26.33 ? 292 ASP B OD1 1 
ATOM   1660 O  OD2 . ASP B 1 92  ? -9.132 -3.616  38.324 1.00 27.10 ? 292 ASP B OD2 1 
ATOM   1661 N  N   . GLY B 1 93  ? -4.315 -3.076  35.203 1.00 15.84 ? 293 GLY B N   1 
ATOM   1662 C  CA  . GLY B 1 93  ? -3.156 -2.293  34.791 1.00 14.70 ? 293 GLY B CA  1 
ATOM   1663 C  C   . GLY B 1 93  ? -2.527 -1.467  35.904 1.00 13.71 ? 293 GLY B C   1 
ATOM   1664 O  O   . GLY B 1 93  ? -1.697 -0.613  35.632 1.00 12.83 ? 293 GLY B O   1 
ATOM   1665 N  N   . VAL B 1 94  ? -2.903 -1.740  37.144 1.00 12.94 ? 294 VAL B N   1 
ATOM   1666 C  CA  . VAL B 1 94  ? -2.436 -0.973  38.284 1.00 13.67 ? 294 VAL B CA  1 
ATOM   1667 C  C   . VAL B 1 94  ? -1.418 -1.759  39.096 1.00 13.45 ? 294 VAL B C   1 
ATOM   1668 O  O   . VAL B 1 94  ? -1.656 -2.897  39.481 1.00 14.12 ? 294 VAL B O   1 
ATOM   1669 C  CB  . VAL B 1 94  ? -3.613 -0.592  39.195 1.00 14.23 ? 294 VAL B CB  1 
ATOM   1670 C  CG1 . VAL B 1 94  ? -3.123 0.150   40.402 1.00 14.52 ? 294 VAL B CG1 1 
ATOM   1671 C  CG2 . VAL B 1 94  ? -4.593 0.265   38.425 1.00 14.98 ? 294 VAL B CG2 1 
ATOM   1672 N  N   . ALA B 1 95  ? -0.277 -1.136  39.355 1.00 13.21 ? 295 ALA B N   1 
ATOM   1673 C  CA  . ALA B 1 95  ? 0.742  -1.708  40.219 1.00 13.52 ? 295 ALA B CA  1 
ATOM   1674 C  C   . ALA B 1 95  ? 0.838  -0.915  41.511 1.00 13.51 ? 295 ALA B C   1 
ATOM   1675 O  O   . ALA B 1 95  ? 1.151  0.272   41.491 1.00 14.39 ? 295 ALA B O   1 
ATOM   1676 C  CB  . ALA B 1 95  ? 2.092  -1.717  39.531 1.00 13.40 ? 295 ALA B CB  1 
ATOM   1677 N  N   . ASP B 1 96  ? 0.553  -1.558  42.630 1.00 13.87 ? 296 ASP B N   1 
ATOM   1678 C  CA  . ASP B 1 96  ? 0.727  -0.932  43.930 1.00 14.88 ? 296 ASP B CA  1 
ATOM   1679 C  C   . ASP B 1 96  ? 2.149  -1.253  44.335 1.00 14.18 ? 296 ASP B C   1 
ATOM   1680 O  O   . ASP B 1 96  ? 2.576  -2.399  44.248 1.00 15.60 ? 296 ASP B O   1 
ATOM   1681 C  CB  . ASP B 1 96  ? -0.270 -1.474  44.941 1.00 16.56 ? 296 ASP B CB  1 
ATOM   1682 C  CG  . ASP B 1 96  ? -1.610 -0.788  44.845 1.00 19.73 ? 296 ASP B CG  1 
ATOM   1683 O  OD1 . ASP B 1 96  ? -2.542 -1.169  45.586 1.00 24.49 ? 296 ASP B OD1 1 
ATOM   1684 O  OD2 . ASP B 1 96  ? -1.828 0.150   44.063 1.00 22.65 ? 296 ASP B OD2 1 
ATOM   1685 N  N   . VAL B 1 97  ? 2.878  -0.235  44.770 1.00 12.48 ? 297 VAL B N   1 
ATOM   1686 C  CA  . VAL B 1 97  ? 4.289  -0.359  45.081 1.00 12.08 ? 297 VAL B CA  1 
ATOM   1687 C  C   . VAL B 1 97  ? 4.541  -0.122  46.561 1.00 11.14 ? 297 VAL B C   1 
ATOM   1688 O  O   . VAL B 1 97  ? 4.075  0.845   47.117 1.00 10.82 ? 297 VAL B O   1 
ATOM   1689 C  CB  . VAL B 1 97  ? 5.077  0.698   44.263 1.00 12.32 ? 297 VAL B CB  1 
ATOM   1690 C  CG1 . VAL B 1 97  ? 6.541  0.606   44.547 1.00 12.92 ? 297 VAL B CG1 1 
ATOM   1691 C  CG2 . VAL B 1 97  ? 4.796  0.530   42.780 1.00 13.32 ? 297 VAL B CG2 1 
ATOM   1692 N  N   . SER B 1 98  ? 5.253  -1.039  47.199 1.00 11.48 ? 298 SER B N   1 
ATOM   1693 C  CA  . SER B 1 98  ? 5.698  -0.881  48.584 1.00 12.51 ? 298 SER B CA  1 
ATOM   1694 C  C   . SER B 1 98  ? 6.990  -1.687  48.707 1.00 13.55 ? 298 SER B C   1 
ATOM   1695 O  O   . SER B 1 98  ? 6.972  -2.916  48.709 1.00 15.15 ? 298 SER B O   1 
ATOM   1696 C  CB  . SER B 1 98  ? 4.637  -1.326  49.590 1.00 12.67 ? 298 SER B CB  1 
ATOM   1697 O  OG  . SER B 1 98  ? 5.004  -0.908  50.898 1.00 15.71 ? 298 SER B OG  1 
ATOM   1698 N  N   . ILE B 1 99  ? 8.107  -0.975  48.767 1.00 13.47 ? 299 ILE B N   1 
ATOM   1699 C  CA  . ILE B 1 99  ? 9.446  -1.540  48.730 1.00 14.39 ? 299 ILE B CA  1 
ATOM   1700 C  C   . ILE B 1 99  ? 10.270 -0.919  49.859 1.00 13.94 ? 299 ILE B C   1 
ATOM   1701 O  O   . ILE B 1 99  ? 10.068 0.250   50.214 1.00 14.02 ? 299 ILE B O   1 
ATOM   1702 C  CB  . ILE B 1 99  ? 10.113 -1.163  47.350 1.00 14.89 ? 299 ILE B CB  1 
ATOM   1703 C  CG1 . ILE B 1 99  ? 9.429  -1.896  46.187 1.00 16.24 ? 299 ILE B CG1 1 
ATOM   1704 C  CG2 . ILE B 1 99  ? 11.609 -1.423  47.367 1.00 16.74 ? 299 ILE B CG2 1 
ATOM   1705 C  CD1 . ILE B 1 99  ? 9.875  -1.397  44.827 1.00 17.35 ? 299 ILE B CD1 1 
ATOM   1706 N  N   . GLU B 1 100 ? 11.202 -1.675  50.425 1.00 13.97 ? 300 GLU B N   1 
ATOM   1707 C  CA  . GLU B 1 100 ? 12.205 -1.134  51.331 1.00 14.82 ? 300 GLU B CA  1 
ATOM   1708 C  C   . GLU B 1 100 ? 13.546 -1.438  50.679 1.00 14.30 ? 300 GLU B C   1 
ATOM   1709 O  O   . GLU B 1 100 ? 13.791 -2.579  50.291 1.00 14.84 ? 300 GLU B O   1 
ATOM   1710 C  CB  . GLU B 1 100 ? 12.108 -1.785  52.712 1.00 15.90 ? 300 GLU B CB  1 
ATOM   1711 C  CG  . GLU B 1 100 ? 13.048 -1.210  53.755 1.00 19.12 ? 300 GLU B CG  1 
ATOM   1712 C  CD  . GLU B 1 100 ? 12.771 -1.780  55.143 1.00 24.10 ? 300 GLU B CD  1 
ATOM   1713 O  OE1 . GLU B 1 100 ? 12.689 -3.021  55.281 1.00 27.77 ? 300 GLU B OE1 1 
ATOM   1714 O  OE2 . GLU B 1 100 ? 12.618 -0.994  56.100 1.00 27.89 ? 300 GLU B OE2 1 
ATOM   1715 N  N   . ASP B 1 101 ? 14.399 -0.431  50.517 1.00 13.12 ? 301 ASP B N   1 
ATOM   1716 C  CA  . ASP B 1 101 ? 15.699 -0.632  49.885 1.00 13.20 ? 301 ASP B CA  1 
ATOM   1717 C  C   . ASP B 1 101 ? 16.770 0.076   50.682 1.00 13.66 ? 301 ASP B C   1 
ATOM   1718 O  O   . ASP B 1 101 ? 16.635 1.255   50.990 1.00 13.62 ? 301 ASP B O   1 
ATOM   1719 C  CB  . ASP B 1 101 ? 15.687 -0.108  48.445 1.00 13.66 ? 301 ASP B CB  1 
ATOM   1720 C  CG  . ASP B 1 101 ? 16.897 -0.553  47.644 1.00 14.96 ? 301 ASP B CG  1 
ATOM   1721 O  OD1 . ASP B 1 101 ? 17.987 0.015   47.803 1.00 14.30 ? 301 ASP B OD1 1 
ATOM   1722 O  OD2 . ASP B 1 101 ? 16.865 -1.513  46.832 1.00 20.38 ? 301 ASP B OD2 1 
ATOM   1723 N  N   . SER B 1 102 ? 17.837 -0.648  51.012 1.00 14.50 ? 302 SER B N   1 
ATOM   1724 C  CA  . SER B 1 102 ? 18.922 -0.114  51.838 1.00 16.09 ? 302 SER B CA  1 
ATOM   1725 C  C   . SER B 1 102 ? 20.150 0.311   51.037 1.00 15.59 ? 302 SER B C   1 
ATOM   1726 O  O   . SER B 1 102 ? 21.152 0.713   51.626 1.00 17.28 ? 302 SER B O   1 
ATOM   1727 C  CB  . SER B 1 102 ? 19.357 -1.158  52.877 1.00 17.34 ? 302 SER B CB  1 
ATOM   1728 O  OG  . SER B 1 102 ? 18.278 -1.534  53.710 1.00 21.67 ? 302 SER B OG  1 
ATOM   1729 N  N   . VAL B 1 103 ? 20.095 0.206   49.717 1.00 14.41 ? 303 VAL B N   1 
ATOM   1730 C  CA  . VAL B 1 103 ? 21.220 0.565   48.844 1.00 14.35 ? 303 VAL B CA  1 
ATOM   1731 C  C   . VAL B 1 103 ? 21.056 1.990   48.262 1.00 13.59 ? 303 VAL B C   1 
ATOM   1732 O  O   . VAL B 1 103 ? 22.026 2.749   48.212 1.00 14.84 ? 303 VAL B O   1 
ATOM   1733 C  CB  . VAL B 1 103 ? 21.425 -0.489  47.746 1.00 14.96 ? 303 VAL B CB  1 
ATOM   1734 C  CG1 . VAL B 1 103 ? 22.603 -0.130  46.883 1.00 15.74 ? 303 VAL B CG1 1 
ATOM   1735 C  CG2 . VAL B 1 103 ? 21.624 -1.889  48.388 1.00 16.07 ? 303 VAL B CG2 1 
ATOM   1736 N  N   . ILE B 1 104 ? 19.853 2.331   47.799 1.00 12.33 ? 304 ILE B N   1 
ATOM   1737 C  CA  . ILE B 1 104 ? 19.575 3.709   47.412 1.00 11.16 ? 304 ILE B CA  1 
ATOM   1738 C  C   . ILE B 1 104 ? 19.565 4.581   48.650 1.00 10.61 ? 304 ILE B C   1 
ATOM   1739 O  O   . ILE B 1 104 ? 19.447 4.089   49.764 1.00 11.37 ? 304 ILE B O   1 
ATOM   1740 C  CB  . ILE B 1 104 ? 18.227 3.843   46.659 1.00 11.14 ? 304 ILE B CB  1 
ATOM   1741 C  CG1 . ILE B 1 104 ? 17.060 3.382   47.529 1.00 11.33 ? 304 ILE B CG1 1 
ATOM   1742 C  CG2 . ILE B 1 104 ? 18.284 3.101   45.322 1.00 11.88 ? 304 ILE B CG2 1 
ATOM   1743 C  CD1 . ILE B 1 104 ? 15.712 3.793   46.985 1.00 10.84 ? 304 ILE B CD1 1 
ATOM   1744 N  N   . SER B 1 105 ? 19.655 5.884   48.449 1.00 9.94  ? 305 SER B N   1 
ATOM   1745 C  CA  . SER B 1 105 ? 19.643 6.816   49.549 1.00 9.27  ? 305 SER B CA  1 
ATOM   1746 C  C   . SER B 1 105 ? 19.138 8.163   49.058 1.00 9.54  ? 305 SER B C   1 
ATOM   1747 O  O   . SER B 1 105 ? 19.133 8.421   47.849 1.00 9.67  ? 305 SER B O   1 
ATOM   1748 C  CB  . SER B 1 105 ? 21.064 6.961   50.085 1.00 10.17 ? 305 SER B CB  1 
ATOM   1749 O  OG  . SER B 1 105 ? 21.064 7.696   51.271 1.00 10.72 ? 305 SER B OG  1 
ATOM   1750 N  N   . LEU B 1 106 ? 18.749 9.015   49.996 1.00 9.49  ? 306 LEU B N   1 
ATOM   1751 C  CA  . LEU B 1 106 ? 18.360 10.383  49.690 1.00 10.79 ? 306 LEU B CA  1 
ATOM   1752 C  C   . LEU B 1 106 ? 19.501 11.359  50.020 1.00 12.84 ? 306 LEU B C   1 
ATOM   1753 O  O   . LEU B 1 106 ? 19.290 12.571  50.019 1.00 14.40 ? 306 LEU B O   1 
ATOM   1754 C  CB  . LEU B 1 106 ? 17.059 10.767  50.401 1.00 10.60 ? 306 LEU B CB  1 
ATOM   1755 C  CG  . LEU B 1 106 ? 15.875 9.844   50.086 1.00 10.67 ? 306 LEU B CG  1 
ATOM   1756 C  CD1 . LEU B 1 106 ? 14.608 10.384  50.717 1.00 10.70 ? 306 LEU B CD1 1 
ATOM   1757 C  CD2 . LEU B 1 106 ? 15.656 9.653   48.589 1.00 10.57 ? 306 LEU B CD2 1 
ATOM   1758 N  N   . SER B 1 107 ? 20.699 10.815  50.260 1.00 14.25 ? 307 SER B N   1 
ATOM   1759 C  CA  . SER B 1 107 ? 21.930 11.597  50.436 1.00 16.21 ? 307 SER B CA  1 
ATOM   1760 C  C   . SER B 1 107 ? 23.145 10.722  50.098 1.00 16.85 ? 307 SER B C   1 
ATOM   1761 O  O   . SER B 1 107 ? 23.028 9.514   49.921 1.00 17.23 ? 307 SER B O   1 
ATOM   1762 C  CB  . SER B 1 107 ? 22.068 12.109  51.869 1.00 17.07 ? 307 SER B CB  1 
ATOM   1763 O  OG  . SER B 1 107 ? 22.482 11.071  52.752 1.00 19.58 ? 307 SER B OG  1 
ATOM   1764 N  N   . GLY B 1 108 ? 24.322 11.326  50.001 1.00 17.79 ? 308 GLY B N   1 
ATOM   1765 C  CA  . GLY B 1 108 ? 25.521 10.531  49.838 1.00 18.07 ? 308 GLY B CA  1 
ATOM   1766 C  C   . GLY B 1 108 ? 25.838 10.036  48.444 1.00 18.30 ? 308 GLY B C   1 
ATOM   1767 O  O   . GLY B 1 108 ? 25.292 10.520  47.454 1.00 18.50 ? 308 GLY B O   1 
ATOM   1768 N  N   . ASP B 1 109 ? 26.740 9.055   48.383 1.00 17.90 ? 309 ASP B N   1 
ATOM   1769 C  CA  . ASP B 1 109 ? 27.218 8.485   47.122 1.00 18.21 ? 309 ASP B CA  1 
ATOM   1770 C  C   . ASP B 1 109 ? 26.104 7.757   46.378 1.00 17.15 ? 309 ASP B C   1 
ATOM   1771 O  O   . ASP B 1 109 ? 26.135 7.658   45.148 1.00 18.26 ? 309 ASP B O   1 
ATOM   1772 C  CB  . ASP B 1 109 ? 28.399 7.529   47.358 1.00 19.01 ? 309 ASP B CB  1 
ATOM   1773 C  CG  . ASP B 1 109 ? 29.694 8.257   47.745 1.00 22.42 ? 309 ASP B CG  1 
ATOM   1774 O  OD1 . ASP B 1 109 ? 29.919 9.401   47.309 1.00 25.78 ? 309 ASP B OD1 1 
ATOM   1775 O  OD2 . ASP B 1 109 ? 30.555 7.748   48.485 1.00 26.42 ? 309 ASP B OD2 1 
ATOM   1776 N  N   . HIS B 1 110 ? 25.127 7.251   47.125 1.00 15.09 ? 310 HIS B N   1 
ATOM   1777 C  CA  . HIS B 1 110 ? 24.000 6.539   46.530 1.00 14.09 ? 310 HIS B CA  1 
ATOM   1778 C  C   . HIS B 1 110 ? 22.731 7.388   46.488 1.00 12.70 ? 310 HIS B C   1 
ATOM   1779 O  O   . HIS B 1 110 ? 21.656 6.891   46.192 1.00 11.35 ? 310 HIS B O   1 
ATOM   1780 C  CB  . HIS B 1 110 ? 23.715 5.263   47.300 1.00 14.20 ? 310 HIS B CB  1 
ATOM   1781 C  CG  . HIS B 1 110 ? 24.773 4.223   47.145 1.00 16.59 ? 310 HIS B CG  1 
ATOM   1782 N  ND1 . HIS B 1 110 ? 24.671 2.973   47.713 1.00 17.96 ? 310 HIS B ND1 1 
ATOM   1783 C  CD2 . HIS B 1 110 ? 25.945 4.243   46.472 1.00 17.23 ? 310 HIS B CD2 1 
ATOM   1784 C  CE1 . HIS B 1 110 ? 25.748 2.268   47.401 1.00 19.20 ? 310 HIS B CE1 1 
ATOM   1785 N  NE2 . HIS B 1 110 ? 26.533 3.014   46.645 1.00 18.52 ? 310 HIS B NE2 1 
HETATM 1786 N  N   . CSX B 1 111 ? 22.957 8.730   46.553 1.00 11.02 ? 311 CSX B N   1 
HETATM 1787 C  CA  . CSX B 1 111 ? 22.052 9.770   46.261 1.00 12.35 ? 311 CSX B CA  1 
HETATM 1788 C  CB  . CSX B 1 111 ? 22.294 11.152  46.806 1.00 12.05 ? 311 CSX B CB  1 
HETATM 1789 S  SG  . CSX B 1 111 ? 20.910 12.293  46.888 1.00 14.60 ? 311 CSX B SG  1 
HETATM 1790 C  C   . CSX B 1 111 ? 21.114 9.635   45.140 1.00 11.45 ? 311 CSX B C   1 
HETATM 1791 O  O   . CSX B 1 111 ? 21.689 9.664   44.066 1.00 11.90 ? 311 CSX B O   1 
HETATM 1792 O  OD  . CSX B 1 111 ? 21.339 13.691  46.926 1.00 22.38 ? 311 CSX B OD  1 
ATOM   1793 N  N   . ILE B 1 112 ? 19.714 9.476   45.213 1.00 8.73  ? 312 ILE B N   1 
ATOM   1794 C  CA  . ILE B 1 112 ? 18.924 9.429   43.966 1.00 8.47  ? 312 ILE B CA  1 
ATOM   1795 C  C   . ILE B 1 112 ? 18.131 10.708  43.685 1.00 7.92  ? 312 ILE B C   1 
ATOM   1796 O  O   . ILE B 1 112 ? 17.420 10.784  42.686 1.00 7.22  ? 312 ILE B O   1 
ATOM   1797 C  CB  . ILE B 1 112 ? 18.018 8.193   43.966 1.00 8.42  ? 312 ILE B CB  1 
ATOM   1798 C  CG1 . ILE B 1 112 ? 17.016 8.288   45.097 1.00 9.52  ? 312 ILE B CG1 1 
ATOM   1799 C  CG2 . ILE B 1 112 ? 18.857 6.892   44.046 1.00 9.91  ? 312 ILE B CG2 1 
ATOM   1800 C  CD1 . ILE B 1 112 ? 15.973 7.185   45.065 1.00 11.23 ? 312 ILE B CD1 1 
ATOM   1801 N  N   . ILE B 1 113 ? 18.164 11.667  44.603 1.00 7.97  ? 313 ILE B N   1 
ATOM   1802 C  CA  . ILE B 1 113 ? 17.578 12.978  44.333 1.00 8.19  ? 313 ILE B CA  1 
ATOM   1803 C  C   . ILE B 1 113 ? 18.178 13.567  43.062 1.00 7.77  ? 313 ILE B C   1 
ATOM   1804 O  O   . ILE B 1 113 ? 19.389 13.598  42.879 1.00 7.60  ? 313 ILE B O   1 
ATOM   1805 C  CB  . ILE B 1 113 ? 17.844 13.970  45.503 1.00 9.36  ? 313 ILE B CB  1 
ATOM   1806 C  CG1 . ILE B 1 113 ? 17.304 13.469  46.828 1.00 12.16 ? 313 ILE B CG1 1 
ATOM   1807 C  CG2 . ILE B 1 113 ? 17.269 15.350  45.175 1.00 9.76  ? 313 ILE B CG2 1 
ATOM   1808 C  CD1 . ILE B 1 113 ? 15.933 13.200  46.796 1.00 13.49 ? 313 ILE B CD1 1 
ATOM   1809 N  N   . GLY B 1 114 ? 17.312 14.034  42.178 1.00 6.60  ? 314 GLY B N   1 
ATOM   1810 C  CA  . GLY B 1 114 ? 17.767 14.595  40.922 1.00 6.85  ? 314 GLY B CA  1 
ATOM   1811 C  C   . GLY B 1 114 ? 18.048 13.585  39.839 1.00 6.86  ? 314 GLY B C   1 
ATOM   1812 O  O   . GLY B 1 114 ? 18.501 13.978  38.772 1.00 7.04  ? 314 GLY B O   1 
ATOM   1813 N  N   . ARG B 1 115 ? 17.814 12.301  40.116 1.00 6.87  ? 315 ARG B N   1 
ATOM   1814 C  CA  . ARG B 1 115 ? 17.971 11.263  39.098 1.00 7.10  ? 315 ARG B CA  1 
ATOM   1815 C  C   . ARG B 1 115 ? 16.582 10.880  38.570 1.00 7.36  ? 315 ARG B C   1 
ATOM   1816 O  O   . ARG B 1 115 ? 15.601 11.498  38.958 1.00 8.05  ? 315 ARG B O   1 
ATOM   1817 C  CB  . ARG B 1 115 ? 18.783 10.101  39.674 1.00 7.43  ? 315 ARG B CB  1 
ATOM   1818 C  CG  . ARG B 1 115 ? 20.134 10.582  40.204 1.00 8.91  ? 315 ARG B CG  1 
ATOM   1819 C  CD  . ARG B 1 115 ? 21.113 9.483   40.503 1.00 9.09  ? 315 ARG B CD  1 
ATOM   1820 N  NE  . ARG B 1 115 ? 22.320 9.979   41.172 1.00 11.07 ? 315 ARG B NE  1 
ATOM   1821 C  CZ  . ARG B 1 115 ? 23.401 10.439  40.563 1.00 11.14 ? 315 ARG B CZ  1 
ATOM   1822 N  NH1 . ARG B 1 115 ? 23.475 10.500  39.249 1.00 11.55 ? 315 ARG B NH1 1 
ATOM   1823 N  NH2 . ARG B 1 115 ? 24.431 10.847  41.298 1.00 12.53 ? 315 ARG B NH2 1 
ATOM   1824 N  N   . THR B 1 116 ? 16.500 9.911   37.668 1.00 7.04  ? 316 THR B N   1 
ATOM   1825 C  CA  . THR B 1 116 ? 15.224 9.552   37.064 1.00 7.74  ? 316 THR B CA  1 
ATOM   1826 C  C   . THR B 1 116 ? 14.756 8.172   37.470 1.00 7.75  ? 316 THR B C   1 
ATOM   1827 O  O   . THR B 1 116 ? 15.499 7.207   37.396 1.00 9.89  ? 316 THR B O   1 
ATOM   1828 C  CB  . THR B 1 116 ? 15.350 9.612   35.530 1.00 8.18  ? 316 THR B CB  1 
ATOM   1829 O  OG1 . THR B 1 116 ? 15.559 10.966  35.096 1.00 10.03 ? 316 THR B OG1 1 
ATOM   1830 C  CG2 . THR B 1 116 ? 14.095 9.151   34.848 1.00 9.15  ? 316 THR B CG2 1 
ATOM   1831 N  N   . LEU B 1 117 ? 13.509 8.077   37.900 1.00 7.50  ? 317 LEU B N   1 
ATOM   1832 C  CA  . LEU B 1 117 ? 12.866 6.805   38.141 1.00 7.72  ? 317 LEU B CA  1 
ATOM   1833 C  C   . LEU B 1 117 ? 12.178 6.386   36.844 1.00 7.14  ? 317 LEU B C   1 
ATOM   1834 O  O   . LEU B 1 117 ? 11.511 7.196   36.209 1.00 7.71  ? 317 LEU B O   1 
ATOM   1835 C  CB  . LEU B 1 117 ? 11.822 6.936   39.249 1.00 7.80  ? 317 LEU B CB  1 
ATOM   1836 C  CG  . LEU B 1 117 ? 11.147 5.643   39.715 1.00 8.39  ? 317 LEU B CG  1 
ATOM   1837 C  CD1 . LEU B 1 117 ? 12.109 4.686   40.365 1.00 9.60  ? 317 LEU B CD1 1 
ATOM   1838 C  CD2 . LEU B 1 117 ? 10.009 6.015   40.655 1.00 8.87  ? 317 LEU B CD2 1 
ATOM   1839 N  N   . VAL B 1 118 ? 12.330 5.118   36.460 1.00 7.61  ? 318 VAL B N   1 
ATOM   1840 C  CA  . VAL B 1 118 ? 11.800 4.579   35.217 1.00 7.78  ? 318 VAL B CA  1 
ATOM   1841 C  C   . VAL B 1 118 ? 11.054 3.269   35.470 1.00 8.44  ? 318 VAL B C   1 
ATOM   1842 O  O   . VAL B 1 118 ? 11.506 2.407   36.231 1.00 8.62  ? 318 VAL B O   1 
ATOM   1843 C  CB  . VAL B 1 118 ? 12.951 4.277   34.214 1.00 8.39  ? 318 VAL B CB  1 
ATOM   1844 C  CG1 . VAL B 1 118 ? 12.415 3.621   32.939 1.00 9.71  ? 318 VAL B CG1 1 
ATOM   1845 C  CG2 . VAL B 1 118 ? 13.732 5.538   33.903 1.00 8.41  ? 318 VAL B CG2 1 
ATOM   1846 N  N   . VAL B 1 119 ? 9.898  3.129   34.820 1.00 8.70  ? 319 VAL B N   1 
ATOM   1847 C  CA  . VAL B 1 119 ? 9.179  1.864   34.800 1.00 9.43  ? 319 VAL B CA  1 
ATOM   1848 C  C   . VAL B 1 119 ? 9.252  1.349   33.358 1.00 9.68  ? 319 VAL B C   1 
ATOM   1849 O  O   . VAL B 1 119 ? 8.994  2.077   32.402 1.00 9.55  ? 319 VAL B O   1 
ATOM   1850 C  CB  . VAL B 1 119 ? 7.734  1.961   35.354 1.00 9.81  ? 319 VAL B CB  1 
ATOM   1851 C  CG1 . VAL B 1 119 ? 6.873  2.937   34.583 1.00 11.38 ? 319 VAL B CG1 1 
ATOM   1852 C  CG2 . VAL B 1 119 ? 7.104  0.588   35.384 1.00 10.17 ? 319 VAL B CG2 1 
ATOM   1853 N  N   . HIS B 1 120 ? 9.649  0.091   33.233 1.00 10.40 ? 320 HIS B N   1 
ATOM   1854 C  CA  . HIS B 1 120 ? 9.929  -0.526  31.945 1.00 11.13 ? 320 HIS B CA  1 
ATOM   1855 C  C   . HIS B 1 120 ? 8.810  -1.413  31.397 1.00 11.80 ? 320 HIS B C   1 
ATOM   1856 O  O   . HIS B 1 120 ? 7.945  -1.867  32.123 1.00 12.14 ? 320 HIS B O   1 
ATOM   1857 C  CB  . HIS B 1 120 ? 11.190 -1.373  32.079 1.00 11.17 ? 320 HIS B CB  1 
ATOM   1858 C  CG  . HIS B 1 120 ? 12.470 -0.597  32.038 1.00 12.74 ? 320 HIS B CG  1 
ATOM   1859 N  ND1 . HIS B 1 120 ? 13.102 -0.270  30.858 1.00 13.83 ? 320 HIS B ND1 1 
ATOM   1860 C  CD2 . HIS B 1 120 ? 13.262 -0.126  33.033 1.00 12.64 ? 320 HIS B CD2 1 
ATOM   1861 C  CE1 . HIS B 1 120 ? 14.223 0.375   31.128 1.00 13.56 ? 320 HIS B CE1 1 
ATOM   1862 N  NE2 . HIS B 1 120 ? 14.354 0.464   32.440 1.00 13.87 ? 320 HIS B NE2 1 
ATOM   1863 N  N   . GLU B 1 121 ? 8.883  -1.634  30.085 1.00 12.63 ? 321 GLU B N   1 
ATOM   1864 C  CA  . GLU B 1 121 ? 7.958  -2.460  29.315 1.00 13.98 ? 321 GLU B CA  1 
ATOM   1865 C  C   . GLU B 1 121 ? 7.892  -3.889  29.816 1.00 14.37 ? 321 GLU B C   1 
ATOM   1866 O  O   . GLU B 1 121 ? 6.803  -4.458  29.930 1.00 15.42 ? 321 GLU B O   1 
ATOM   1867 C  CB  . GLU B 1 121 ? 8.434  -2.457  27.860 1.00 14.50 ? 321 GLU B CB  1 
ATOM   1868 C  CG  . GLU B 1 121 ? 7.607  -3.297  26.891 1.00 16.52 ? 321 GLU B CG  1 
ATOM   1869 C  CD  . GLU B 1 121 ? 8.247  -3.397  25.511 1.00 18.41 ? 321 GLU B CD  1 
ATOM   1870 O  OE1 . GLU B 1 121 ? 9.407  -2.959  25.338 1.00 18.67 ? 321 GLU B OE1 1 
ATOM   1871 O  OE2 . GLU B 1 121 ? 7.589  -3.954  24.592 1.00 21.33 ? 321 GLU B OE2 1 
ATOM   1872 N  N   . LYS B 1 122 ? 9.057  -4.450  30.119 1.00 15.53 ? 322 LYS B N   1 
ATOM   1873 C  CA  . LYS B 1 122 ? 9.174  -5.848  30.497 1.00 17.07 ? 322 LYS B CA  1 
ATOM   1874 C  C   . LYS B 1 122 ? 9.794  -6.009  31.863 1.00 16.83 ? 322 LYS B C   1 
ATOM   1875 O  O   . LYS B 1 122 ? 10.272 -5.049  32.466 1.00 15.93 ? 322 LYS B O   1 
ATOM   1876 C  CB  . LYS B 1 122 ? 10.036 -6.586  29.474 1.00 18.28 ? 322 LYS B CB  1 
ATOM   1877 C  CG  . LYS B 1 122 ? 9.448  -6.582  28.073 1.00 21.35 ? 322 LYS B CG  1 
ATOM   1878 C  CD  . LYS B 1 122 ? 10.154 -7.576  27.162 1.00 24.78 ? 322 LYS B CD  1 
ATOM   1879 C  CE  . LYS B 1 122 ? 9.550  -7.590  25.766 1.00 27.01 ? 322 LYS B CE  1 
ATOM   1880 N  NZ  . LYS B 1 122 ? 10.239 -8.576  24.879 1.00 28.81 ? 322 LYS B NZ  1 
ATOM   1881 N  N   . ALA B 1 123 ? 9.789  -7.239  32.353 1.00 17.59 ? 323 ALA B N   1 
ATOM   1882 C  CA  . ALA B 1 123 ? 10.395 -7.551  33.623 1.00 19.05 ? 323 ALA B CA  1 
ATOM   1883 C  C   . ALA B 1 123 ? 11.898 -7.381  33.539 1.00 20.95 ? 323 ALA B C   1 
ATOM   1884 O  O   . ALA B 1 123 ? 12.505 -7.464  32.476 1.00 21.06 ? 323 ALA B O   1 
ATOM   1885 C  CB  . ALA B 1 123 ? 10.062 -8.973  34.045 1.00 18.99 ? 323 ALA B CB  1 
ATOM   1886 N  N   . ASP B 1 124 ? 12.472 -7.186  34.708 1.00 23.74 ? 324 ASP B N   1 
ATOM   1887 C  CA  . ASP B 1 124 ? 13.881 -6.994  34.918 1.00 26.29 ? 324 ASP B CA  1 
ATOM   1888 C  C   . ASP B 1 124 ? 14.126 -8.296  35.716 1.00 27.79 ? 324 ASP B C   1 
ATOM   1889 O  O   . ASP B 1 124 ? 13.905 -8.344  36.916 1.00 28.64 ? 324 ASP B O   1 
ATOM   1890 C  CB  . ASP B 1 124 ? 13.949 -5.617  35.634 1.00 26.99 ? 324 ASP B CB  1 
ATOM   1891 C  CG  . ASP B 1 124 ? 15.209 -5.349  36.432 1.00 28.40 ? 324 ASP B CG  1 
ATOM   1892 O  OD1 . ASP B 1 124 ? 15.062 -4.625  37.450 1.00 29.81 ? 324 ASP B OD1 1 
ATOM   1893 O  OD2 . ASP B 1 124 ? 16.360 -5.702  36.125 1.00 30.79 ? 324 ASP B OD2 1 
ATOM   1894 N  N   . ASP B 1 125 ? 14.449 -9.391  35.013 1.00 29.54 ? 325 ASP B N   1 
ATOM   1895 C  CA  . ASP B 1 125 ? 14.605 -10.715 35.663 1.00 30.60 ? 325 ASP B CA  1 
ATOM   1896 C  C   . ASP B 1 125 ? 15.853 -10.790 36.531 1.00 30.88 ? 325 ASP B C   1 
ATOM   1897 O  O   . ASP B 1 125 ? 15.897 -11.546 37.504 1.00 31.22 ? 325 ASP B O   1 
ATOM   1898 C  CB  . ASP B 1 125 ? 14.629 -11.868 34.644 1.00 31.16 ? 325 ASP B CB  1 
ATOM   1899 C  CG  . ASP B 1 125 ? 14.951 -13.224 35.291 1.00 32.68 ? 325 ASP B CG  1 
ATOM   1900 O  OD1 . ASP B 1 125 ? 16.135 -13.478 35.598 1.00 34.41 ? 325 ASP B OD1 1 
ATOM   1901 O  OD2 . ASP B 1 125 ? 14.095 -14.103 35.534 1.00 34.39 ? 325 ASP B OD2 1 
ATOM   1902 N  N   . ASN B 1 139 ? 17.055 -6.115  28.827 1.00 23.49 ? 339 ASN B N   1 
ATOM   1903 C  CA  . ASN B 1 139 ? 15.976 -7.092  28.851 1.00 23.55 ? 339 ASN B CA  1 
ATOM   1904 C  C   . ASN B 1 139 ? 14.658 -6.455  29.241 1.00 22.65 ? 339 ASN B C   1 
ATOM   1905 O  O   . ASN B 1 139 ? 13.589 -6.970  28.905 1.00 23.71 ? 339 ASN B O   1 
ATOM   1906 C  CB  . ASN B 1 139 ? 16.290 -8.242  29.813 1.00 23.89 ? 339 ASN B CB  1 
ATOM   1907 N  N   . ALA B 1 140 ? 14.726 -5.307  29.912 1.00 21.15 ? 340 ALA B N   1 
ATOM   1908 C  CA  . ALA B 1 140 ? 13.519 -4.650  30.402 1.00 19.72 ? 340 ALA B CA  1 
ATOM   1909 C  C   . ALA B 1 140 ? 12.736 -3.904  29.318 1.00 18.39 ? 340 ALA B C   1 
ATOM   1910 O  O   . ALA B 1 140 ? 11.612 -3.484  29.551 1.00 17.42 ? 340 ALA B O   1 
ATOM   1911 C  CB  . ALA B 1 140 ? 13.860 -3.725  31.552 1.00 19.87 ? 340 ALA B CB  1 
ATOM   1912 N  N   . GLY B 1 141 ? 13.316 -3.758  28.131 1.00 17.35 ? 341 GLY B N   1 
ATOM   1913 C  CA  . GLY B 1 141 ? 12.616 -3.132  27.023 1.00 16.64 ? 341 GLY B CA  1 
ATOM   1914 C  C   . GLY B 1 141 ? 12.446 -1.629  27.179 1.00 15.88 ? 341 GLY B C   1 
ATOM   1915 O  O   . GLY B 1 141 ? 13.199 -0.966  27.892 1.00 16.17 ? 341 GLY B O   1 
ATOM   1916 N  N   . SER B 1 142 ? 11.412 -1.100  26.546 1.00 15.34 ? 342 SER B N   1 
ATOM   1917 C  CA  . SER B 1 142 ? 11.204 0.330   26.495 1.00 15.16 ? 342 SER B CA  1 
ATOM   1918 C  C   . SER B 1 142 ? 10.948 0.954   27.865 1.00 13.78 ? 342 SER B C   1 
ATOM   1919 O  O   . SER B 1 142 ? 10.547 0.289   28.819 1.00 13.74 ? 342 SER B O   1 
ATOM   1920 C  CB  . SER B 1 142 ? 10.050 0.659   25.555 1.00 16.08 ? 342 SER B CB  1 
ATOM   1921 O  OG  . SER B 1 142 ? 8.825  0.467   26.189 1.00 19.72 ? 342 SER B OG  1 
ATOM   1922 N  N   . ARG B 1 143 ? 11.200 2.252   27.928 1.00 12.61 ? 343 ARG B N   1 
ATOM   1923 C  CA  . ARG B 1 143 ? 10.984 3.044   29.124 1.00 11.82 ? 343 ARG B CA  1 
ATOM   1924 C  C   . ARG B 1 143 ? 9.593  3.638   28.979 1.00 11.53 ? 343 ARG B C   1 
ATOM   1925 O  O   . ARG B 1 143 ? 9.388  4.612   28.259 1.00 13.63 ? 343 ARG B O   1 
ATOM   1926 C  CB  . ARG B 1 143 ? 12.046 4.124   29.206 1.00 11.51 ? 343 ARG B CB  1 
ATOM   1927 C  CG  . ARG B 1 143 ? 13.443 3.541   29.286 1.00 11.40 ? 343 ARG B CG  1 
ATOM   1928 C  CD  . ARG B 1 143 ? 14.521 4.570   29.396 1.00 12.82 ? 343 ARG B CD  1 
ATOM   1929 N  NE  . ARG B 1 143 ? 15.809 3.900   29.426 1.00 12.97 ? 343 ARG B NE  1 
ATOM   1930 C  CZ  . ARG B 1 143 ? 16.982 4.494   29.316 1.00 12.68 ? 343 ARG B CZ  1 
ATOM   1931 N  NH1 . ARG B 1 143 ? 17.052 5.804   29.206 1.00 14.43 ? 343 ARG B NH1 1 
ATOM   1932 N  NH2 . ARG B 1 143 ? 18.093 3.776   29.358 1.00 11.95 ? 343 ARG B NH2 1 
ATOM   1933 N  N   . LEU B 1 144 ? 8.626  3.042   29.654 1.00 10.35 ? 344 LEU B N   1 
ATOM   1934 C  CA  . LEU B 1 144 ? 7.231  3.445   29.484 1.00 10.81 ? 344 LEU B CA  1 
ATOM   1935 C  C   . LEU B 1 144 ? 6.919  4.789   30.097 1.00 10.24 ? 344 LEU B C   1 
ATOM   1936 O  O   . LEU B 1 144 ? 6.099  5.531   29.569 1.00 10.39 ? 344 LEU B O   1 
ATOM   1937 C  CB  . LEU B 1 144 ? 6.313  2.422   30.116 1.00 11.17 ? 344 LEU B CB  1 
ATOM   1938 C  CG  . LEU B 1 144 ? 6.421  0.997   29.574 1.00 13.91 ? 344 LEU B CG  1 
ATOM   1939 C  CD1 . LEU B 1 144 ? 5.514  0.093   30.382 1.00 15.63 ? 344 LEU B CD1 1 
ATOM   1940 C  CD2 . LEU B 1 144 ? 6.067  0.981   28.102 1.00 15.87 ? 344 LEU B CD2 1 
ATOM   1941 N  N   . ALA B 1 145 ? 7.515  5.075   31.246 1.00 9.84  ? 345 ALA B N   1 
ATOM   1942 C  CA  . ALA B 1 145 ? 7.265  6.312   31.949 1.00 9.55  ? 345 ALA B CA  1 
ATOM   1943 C  C   . ALA B 1 145 ? 8.432  6.557   32.860 1.00 9.07  ? 345 ALA B C   1 
ATOM   1944 O  O   . ALA B 1 145 ? 9.129  5.626   33.283 1.00 9.73  ? 345 ALA B O   1 
ATOM   1945 C  CB  . ALA B 1 145 ? 5.992  6.237   32.752 1.00 9.52  ? 345 ALA B CB  1 
ATOM   1946 N  N   . CYS B 1 146 ? 8.616  7.827   33.178 1.00 8.63  ? 346 CYS B N   1 
ATOM   1947 C  CA  . CYS B 1 146 ? 9.744  8.235   34.003 1.00 8.73  ? 346 CYS B CA  1 
ATOM   1948 C  C   . CYS B 1 146 ? 9.466  9.598   34.609 1.00 8.64  ? 346 CYS B C   1 
ATOM   1949 O  O   . CYS B 1 146 ? 8.552  10.300  34.184 1.00 8.80  ? 346 CYS B O   1 
ATOM   1950 C  CB  . CYS B 1 146 ? 11.038 8.294   33.179 1.00 9.56  ? 346 CYS B CB  1 
ATOM   1951 S  SG  . CYS B 1 146 ? 10.916 9.421   31.778 1.00 12.39 ? 346 CYS B SG  1 
ATOM   1952 N  N   . GLY B 1 147 ? 10.267 9.987   35.593 1.00 8.28  ? 347 GLY B N   1 
ATOM   1953 C  CA  . GLY B 1 147 ? 10.190 11.317  36.149 1.00 8.16  ? 347 GLY B CA  1 
ATOM   1954 C  C   . GLY B 1 147 ? 11.440 11.585  36.954 1.00 7.52  ? 347 GLY B C   1 
ATOM   1955 O  O   . GLY B 1 147 ? 12.138 10.653  37.340 1.00 7.88  ? 347 GLY B O   1 
ATOM   1956 N  N   . VAL B 1 148 ? 11.726 12.851  37.212 1.00 7.09  ? 348 VAL B N   1 
ATOM   1957 C  CA  . VAL B 1 148 ? 12.866 13.241  38.012 1.00 7.37  ? 348 VAL B CA  1 
ATOM   1958 C  C   . VAL B 1 148 ? 12.460 13.180  39.475 1.00 6.73  ? 348 VAL B C   1 
ATOM   1959 O  O   . VAL B 1 148 ? 11.357 13.587  39.850 1.00 8.08  ? 348 VAL B O   1 
ATOM   1960 C  CB  . VAL B 1 148 ? 13.343 14.653  37.619 1.00 7.63  ? 348 VAL B CB  1 
ATOM   1961 C  CG1 . VAL B 1 148 ? 14.578 15.051  38.419 1.00 7.61  ? 348 VAL B CG1 1 
ATOM   1962 C  CG2 . VAL B 1 148 ? 13.628 14.709  36.110 1.00 8.84  ? 348 VAL B CG2 1 
ATOM   1963 N  N   . ILE B 1 149 ? 13.349 12.655  40.299 1.00 7.08  ? 349 ILE B N   1 
ATOM   1964 C  CA  . ILE B 1 149 ? 13.059 12.460  41.714 1.00 6.93  ? 349 ILE B CA  1 
ATOM   1965 C  C   . ILE B 1 149 ? 13.360 13.780  42.437 1.00 6.92  ? 349 ILE B C   1 
ATOM   1966 O  O   . ILE B 1 149 ? 14.489 14.274  42.425 1.00 7.68  ? 349 ILE B O   1 
ATOM   1967 C  CB  . ILE B 1 149 ? 13.903 11.285  42.250 1.00 7.36  ? 349 ILE B CB  1 
ATOM   1968 C  CG1 . ILE B 1 149 ? 13.556 9.988   41.518 1.00 8.36  ? 349 ILE B CG1 1 
ATOM   1969 C  CG2 . ILE B 1 149 ? 13.750 11.132  43.775 1.00 7.48  ? 349 ILE B CG2 1 
ATOM   1970 C  CD1 . ILE B 1 149 ? 14.547 8.869   41.781 1.00 9.42  ? 349 ILE B CD1 1 
ATOM   1971 N  N   . GLY B 1 150 ? 12.342 14.353  43.061 1.00 6.06  ? 350 GLY B N   1 
ATOM   1972 C  CA  . GLY B 1 150 ? 12.447 15.668  43.664 1.00 6.10  ? 350 GLY B CA  1 
ATOM   1973 C  C   . GLY B 1 150 ? 12.334 15.645  45.172 1.00 6.45  ? 350 GLY B C   1 
ATOM   1974 O  O   . GLY B 1 150 ? 11.785 14.706  45.750 1.00 6.71  ? 350 GLY B O   1 
ATOM   1975 N  N   . ILE B 1 151 ? 12.847 16.685  45.802 1.00 6.94  ? 351 ILE B N   1 
ATOM   1976 C  CA  . ILE B 1 151 ? 12.765 16.858  47.248 1.00 7.95  ? 351 ILE B CA  1 
ATOM   1977 C  C   . ILE B 1 151 ? 11.324 17.151  47.624 1.00 8.01  ? 351 ILE B C   1 
ATOM   1978 O  O   . ILE B 1 151 ? 10.713 18.065  47.070 1.00 8.79  ? 351 ILE B O   1 
ATOM   1979 C  CB  . ILE B 1 151 ? 13.705 17.987  47.720 1.00 8.11  ? 351 ILE B CB  1 
ATOM   1980 C  CG1 . ILE B 1 151 ? 15.158 17.615  47.456 1.00 9.28  ? 351 ILE B CG1 1 
ATOM   1981 C  CG2 . ILE B 1 151 ? 13.460 18.293  49.192 1.00 8.96  ? 351 ILE B CG2 1 
ATOM   1982 C  CD1 . ILE B 1 151 ? 16.124 18.735  47.673 1.00 10.80 ? 351 ILE B CD1 1 
ATOM   1983 N  N   . ALA B 1 152 ? 10.781 16.391  48.574 1.00 9.06  ? 352 ALA B N   1 
ATOM   1984 C  CA  . ALA B 1 152 ? 9.389  16.549  48.996 1.00 11.06 ? 352 ALA B CA  1 
ATOM   1985 C  C   . ALA B 1 152 ? 9.243  17.082  50.391 1.00 13.53 ? 352 ALA B C   1 
ATOM   1986 O  O   . ALA B 1 152 ? 8.200  17.617  50.729 1.00 14.38 ? 352 ALA B O   1 
ATOM   1987 C  CB  . ALA B 1 152 ? 8.640  15.213  48.880 1.00 11.19 ? 352 ALA B CB  1 
ATOM   1988 N  N   . GLN B 1 153 ? 10.268 16.867  51.198 1.00 16.49 ? 353 GLN B N   1 
ATOM   1989 C  CA  . GLN B 1 153 ? 10.285 17.258  52.583 1.00 19.60 ? 353 GLN B CA  1 
ATOM   1990 C  C   . GLN B 1 153 ? 11.768 17.407  52.838 1.00 20.66 ? 353 GLN B C   1 
ATOM   1991 O  O   . GLN B 1 153 ? 12.511 16.400  52.864 1.00 19.65 ? 353 GLN B O   1 
ATOM   1992 C  CB  . GLN B 1 153 ? 9.661  16.151  53.418 1.00 20.47 ? 353 GLN B CB  1 
ATOM   1993 C  CG  . GLN B 1 153 ? 8.500  16.552  54.264 1.00 24.14 ? 353 GLN B CG  1 
ATOM   1994 C  CD  . GLN B 1 153 ? 8.855  16.543  55.724 1.00 27.65 ? 353 GLN B CD  1 
ATOM   1995 O  OE1 . GLN B 1 153 ? 8.477  15.630  56.443 1.00 30.90 ? 353 GLN B OE1 1 
ATOM   1996 N  NE2 . GLN B 1 153 ? 9.594  17.553  56.165 1.00 30.50 ? 353 GLN B NE2 1 
ATOM   1997 O  OXT . GLN B 1 153 ? 12.157 18.578  52.888 1.00 24.21 ? 353 GLN B OXT 1 
HETATM 1998 ZN ZN  . ZN  C 2 .   ? 8.006  31.652  41.337 1.00 25.61 ? 354 ZN  A ZN  1 
HETATM 1999 ZN ZN  . ZN  D 2 .   ? 11.750 35.299  45.964 1.00 14.82 ? 355 ZN  A ZN  1 
HETATM 2000 S  S   . SO4 E 3 .   ? 4.962  32.575  43.381 1.00 22.33 ? 402 SO4 A S   1 
HETATM 2001 O  O1  . SO4 E 3 .   ? 4.109  33.762  43.480 1.00 25.93 ? 402 SO4 A O1  1 
HETATM 2002 O  O2  . SO4 E 3 .   ? 5.209  31.961  44.681 1.00 24.30 ? 402 SO4 A O2  1 
HETATM 2003 O  O3  . SO4 E 3 .   ? 4.264  31.589  42.575 1.00 24.09 ? 402 SO4 A O3  1 
HETATM 2004 O  O4  . SO4 E 3 .   ? 6.254  32.919  42.778 1.00 23.32 ? 402 SO4 A O4  1 
HETATM 2005 ZN ZN  . ZN  F 2 .   ? 16.199 0.713   33.331 1.00 14.67 ? 356 ZN  B ZN  1 
HETATM 2006 S  S   . SO4 G 3 .   ? 17.714 -0.322  30.914 1.00 22.76 ? 401 SO4 B S   1 
HETATM 2007 O  O1  . SO4 G 3 .   ? 17.504 -0.111  32.338 1.00 21.42 ? 401 SO4 B O1  1 
HETATM 2008 O  O2  . SO4 G 3 .   ? 16.891 -1.458  30.509 1.00 23.57 ? 401 SO4 B O2  1 
HETATM 2009 O  O3  . SO4 G 3 .   ? 17.320 0.826   30.120 1.00 21.67 ? 401 SO4 B O3  1 
HETATM 2010 O  O4  . SO4 G 3 .   ? 19.114 -0.706  30.700 1.00 23.66 ? 401 SO4 B O4  1 
HETATM 2011 O  O   . HOH H 4 .   ? 13.141 18.334  34.471 1.00 8.78  ? 403 HOH A O   1 
HETATM 2012 O  O   . HOH H 4 .   ? 7.661  15.593  41.539 1.00 8.97  ? 404 HOH A O   1 
HETATM 2013 O  O   . HOH H 4 .   ? -0.650 17.077  44.972 1.00 13.25 ? 405 HOH A O   1 
HETATM 2014 O  O   . HOH H 4 .   ? 32.229 22.142  48.871 1.00 14.06 ? 406 HOH A O   1 
HETATM 2015 O  O   . HOH H 4 .   ? 13.312 22.170  51.679 1.00 32.65 ? 407 HOH A O   1 
HETATM 2016 O  O   . HOH H 4 .   ? 6.094  31.948  46.866 1.00 36.56 ? 408 HOH A O   1 
HETATM 2017 O  O   . HOH H 4 .   ? 25.694 25.941  48.858 1.00 18.36 ? 409 HOH A O   1 
HETATM 2018 O  O   . HOH H 4 .   ? 3.365  33.935  28.821 1.00 14.89 ? 410 HOH A O   1 
HETATM 2019 O  O   . HOH H 4 .   ? 16.050 36.233  29.081 1.00 18.72 ? 411 HOH A O   1 
HETATM 2020 O  O   . HOH H 4 .   ? 7.417  30.099  21.111 1.00 16.18 ? 412 HOH A O   1 
HETATM 2021 O  O   . HOH H 4 .   ? 3.297  14.956  47.321 1.00 17.13 ? 413 HOH A O   1 
HETATM 2022 O  O   . HOH H 4 .   ? 10.668 17.621  35.645 1.00 16.77 ? 414 HOH A O   1 
HETATM 2023 O  O   . HOH H 4 .   ? 21.078 30.593  26.049 1.00 20.63 ? 415 HOH A O   1 
HETATM 2024 O  O   . HOH H 4 .   ? 12.901 27.345  51.121 1.00 19.48 ? 416 HOH A O   1 
HETATM 2025 O  O   . HOH H 4 .   ? 2.211  31.818  27.682 1.00 15.49 ? 417 HOH A O   1 
HETATM 2026 O  O   . HOH H 4 .   ? 11.418 40.120  19.182 1.00 20.22 ? 418 HOH A O   1 
HETATM 2027 O  O   . HOH H 4 .   ? 13.765 37.323  41.478 1.00 18.57 ? 419 HOH A O   1 
HETATM 2028 O  O   . HOH H 4 .   ? 8.999  18.601  33.584 1.00 18.49 ? 420 HOH A O   1 
HETATM 2029 O  O   . HOH H 4 .   ? 13.074 32.833  18.038 1.00 20.33 ? 421 HOH A O   1 
HETATM 2030 O  O   . HOH H 4 .   ? 14.831 35.664  23.597 1.00 19.69 ? 422 HOH A O   1 
HETATM 2031 O  O   . HOH H 4 .   ? 1.901  26.463  29.684 1.00 20.11 ? 423 HOH A O   1 
HETATM 2032 O  O   . HOH H 4 .   ? 3.013  24.880  46.831 1.00 23.33 ? 424 HOH A O   1 
HETATM 2033 O  O   . HOH H 4 .   ? 29.026 22.197  43.239 1.00 20.61 ? 425 HOH A O   1 
HETATM 2034 O  O   . HOH H 4 .   ? 6.050  17.754  48.944 1.00 16.97 ? 426 HOH A O   1 
HETATM 2035 O  O   . HOH H 4 .   ? 5.026  31.911  18.752 1.00 19.75 ? 427 HOH A O   1 
HETATM 2036 O  O   . HOH H 4 .   ? 26.877 16.538  36.852 1.00 23.04 ? 428 HOH A O   1 
HETATM 2037 O  O   . HOH H 4 .   ? 31.196 22.040  41.160 1.00 22.05 ? 429 HOH A O   1 
HETATM 2038 O  O   . HOH H 4 .   ? 31.663 27.701  39.327 1.00 18.79 ? 430 HOH A O   1 
HETATM 2039 O  O   . HOH H 4 .   ? 3.414  37.840  22.594 1.00 20.59 ? 431 HOH A O   1 
HETATM 2040 O  O   . HOH H 4 .   ? 5.827  35.980  41.756 1.00 29.85 ? 432 HOH A O   1 
HETATM 2041 O  O   . HOH H 4 .   ? 8.071  32.860  48.102 1.00 24.95 ? 433 HOH A O   1 
HETATM 2042 O  O   . HOH H 4 .   ? 3.747  22.976  28.455 1.00 20.38 ? 434 HOH A O   1 
HETATM 2043 O  O   . HOH H 4 .   ? -0.188 29.178  39.100 1.00 23.93 ? 435 HOH A O   1 
HETATM 2044 O  O   . HOH H 4 .   ? 22.684 20.456  31.223 1.00 20.32 ? 436 HOH A O   1 
HETATM 2045 O  O   . HOH H 4 .   ? 7.190  42.931  29.744 1.00 26.93 ? 437 HOH A O   1 
HETATM 2046 O  O   . HOH H 4 .   ? 18.400 37.159  35.991 1.00 23.05 ? 438 HOH A O   1 
HETATM 2047 O  O   . HOH H 4 .   ? 10.285 31.981  49.992 1.00 27.92 ? 439 HOH A O   1 
HETATM 2048 O  O   . HOH H 4 .   ? 0.502  21.264  26.833 1.00 32.15 ? 440 HOH A O   1 
HETATM 2049 O  O   . HOH H 4 .   ? 1.789  35.616  30.331 1.00 22.65 ? 441 HOH A O   1 
HETATM 2050 O  O   . HOH H 4 .   ? 15.952 36.699  25.647 1.00 30.23 ? 442 HOH A O   1 
HETATM 2051 O  O   . HOH H 4 .   ? -0.209 30.448  28.174 1.00 20.35 ? 443 HOH A O   1 
HETATM 2052 O  O   . HOH H 4 .   ? -2.107 29.698  26.073 1.00 19.85 ? 444 HOH A O   1 
HETATM 2053 O  O   . HOH H 4 .   ? 18.327 35.525  30.667 1.00 26.17 ? 445 HOH A O   1 
HETATM 2054 O  O   . HOH H 4 .   ? 19.518 22.443  49.321 1.00 24.32 ? 446 HOH A O   1 
HETATM 2055 O  O   . HOH H 4 .   ? 0.782  23.033  36.613 1.00 29.12 ? 447 HOH A O   1 
HETATM 2056 O  O   . HOH H 4 .   ? 27.362 29.192  44.163 1.00 23.67 ? 448 HOH A O   1 
HETATM 2057 O  O   . HOH H 4 .   ? 16.718 39.481  36.056 1.00 23.23 ? 449 HOH A O   1 
HETATM 2058 O  O   . HOH H 4 .   ? 25.094 36.323  41.377 1.00 28.46 ? 450 HOH A O   1 
HETATM 2059 O  O   . HOH H 4 .   ? 4.498  45.872  41.435 1.00 24.06 ? 451 HOH A O   1 
HETATM 2060 O  O   . HOH H 4 .   ? 15.806 39.083  30.865 1.00 29.77 ? 452 HOH A O   1 
HETATM 2061 O  O   . HOH H 4 .   ? 14.177 24.895  24.916 1.00 28.98 ? 453 HOH A O   1 
HETATM 2062 O  O   . HOH H 4 .   ? 6.548  19.629  34.796 1.00 31.72 ? 454 HOH A O   1 
HETATM 2063 O  O   . HOH H 4 .   ? 29.191 12.994  28.692 1.00 36.33 ? 455 HOH A O   1 
HETATM 2064 O  O   . HOH H 4 .   ? 25.184 32.803  26.588 1.00 33.94 ? 456 HOH A O   1 
HETATM 2065 O  O   . HOH H 4 .   ? 5.241  40.454  31.128 1.00 27.62 ? 457 HOH A O   1 
HETATM 2066 O  O   . HOH H 4 .   ? 15.020 42.631  48.592 1.00 32.70 ? 458 HOH A O   1 
HETATM 2067 O  O   . HOH H 4 .   ? 19.867 18.435  46.593 1.00 32.40 ? 459 HOH A O   1 
HETATM 2068 O  O   . HOH H 4 .   ? 18.571 42.322  40.670 1.00 31.89 ? 460 HOH A O   1 
HETATM 2069 O  O   . HOH H 4 .   ? 7.039  45.107  32.454 1.00 43.88 ? 461 HOH A O   1 
HETATM 2070 O  O   . HOH H 4 .   ? 4.668  41.535  33.143 1.00 28.75 ? 462 HOH A O   1 
HETATM 2071 O  O   . HOH H 4 .   ? 10.149 50.174  45.753 1.00 27.26 ? 463 HOH A O   1 
HETATM 2072 O  O   . HOH H 4 .   ? 20.368 19.792  27.458 1.00 31.59 ? 464 HOH A O   1 
HETATM 2073 O  O   . HOH H 4 .   ? 18.526 29.555  23.404 1.00 32.29 ? 465 HOH A O   1 
HETATM 2074 O  O   . HOH H 4 .   ? 27.899 33.526  31.310 1.00 41.47 ? 466 HOH A O   1 
HETATM 2075 O  O   . HOH H 4 .   ? 17.869 36.895  33.022 1.00 30.78 ? 467 HOH A O   1 
HETATM 2076 O  O   . HOH H 4 .   ? 4.829  28.980  21.076 1.00 17.42 ? 468 HOH A O   1 
HETATM 2077 O  O   . HOH H 4 .   ? 4.349  35.394  22.119 1.00 17.29 ? 469 HOH A O   1 
HETATM 2078 O  O   . HOH H 4 .   ? 5.250  26.346  22.437 1.00 24.01 ? 470 HOH A O   1 
HETATM 2079 O  O   . HOH H 4 .   ? -3.609 27.861  27.448 1.00 31.62 ? 471 HOH A O   1 
HETATM 2080 O  O   . HOH H 4 .   ? 25.351 34.422  31.341 1.00 30.68 ? 472 HOH A O   1 
HETATM 2081 O  O   . HOH H 4 .   ? 9.101  16.398  31.893 1.00 31.80 ? 473 HOH A O   1 
HETATM 2082 O  O   . HOH H 4 .   ? 26.719 28.117  48.178 1.00 35.75 ? 474 HOH A O   1 
HETATM 2083 O  O   . HOH H 4 .   ? 0.454  26.477  39.546 1.00 29.06 ? 475 HOH A O   1 
HETATM 2084 O  O   . HOH H 4 .   ? 30.553 27.790  36.795 1.00 29.98 ? 476 HOH A O   1 
HETATM 2085 O  O   . HOH H 4 .   ? 7.262  25.655  21.085 1.00 36.75 ? 477 HOH A O   1 
HETATM 2086 O  O   . HOH H 4 .   ? 27.486 27.242  29.330 1.00 38.31 ? 478 HOH A O   1 
HETATM 2087 O  O   . HOH H 4 .   ? 2.258  22.214  25.066 1.00 40.04 ? 479 HOH A O   1 
HETATM 2088 O  O   . HOH H 4 .   ? 2.834  45.922  43.808 1.00 41.69 ? 480 HOH A O   1 
HETATM 2089 O  O   . HOH H 4 .   ? 33.309 25.506  48.576 1.00 30.92 ? 481 HOH A O   1 
HETATM 2090 O  O   . HOH H 4 .   ? 5.060  48.365  45.617 1.00 42.15 ? 482 HOH A O   1 
HETATM 2091 O  O   . HOH H 4 .   ? 1.165  25.156  34.988 1.00 35.17 ? 483 HOH A O   1 
HETATM 2092 O  O   . HOH H 4 .   ? 8.777  35.419  13.179 1.00 35.92 ? 484 HOH A O   1 
HETATM 2093 O  O   . HOH H 4 .   ? -2.704 16.696  43.160 1.00 32.32 ? 485 HOH A O   1 
HETATM 2094 O  O   . HOH H 4 .   ? 22.421 37.306  48.395 1.00 36.02 ? 486 HOH A O   1 
HETATM 2095 O  O   . HOH H 4 .   ? 29.365 31.552  44.920 1.00 31.14 ? 487 HOH A O   1 
HETATM 2096 O  O   . HOH H 4 .   ? 4.250  39.714  20.597 1.00 36.90 ? 488 HOH A O   1 
HETATM 2097 O  O   . HOH H 4 .   ? 16.182 23.898  23.522 1.00 36.07 ? 489 HOH A O   1 
HETATM 2098 O  O   . HOH H 4 .   ? 20.508 37.194  50.572 1.00 38.14 ? 490 HOH A O   1 
HETATM 2099 O  O   . HOH H 4 .   ? 8.262  28.119  54.546 1.00 43.10 ? 491 HOH A O   1 
HETATM 2100 O  O   . HOH H 4 .   ? 28.516 28.395  46.456 1.00 40.59 ? 492 HOH A O   1 
HETATM 2101 O  O   . HOH H 4 .   ? 16.001 27.375  21.112 1.00 39.31 ? 493 HOH A O   1 
HETATM 2102 O  O   . HOH H 4 .   ? -0.105 28.317  29.796 1.00 26.51 ? 494 HOH A O   1 
HETATM 2103 O  O   . HOH H 4 .   ? 4.298  42.040  37.434 1.00 33.16 ? 495 HOH A O   1 
HETATM 2104 O  O   . HOH H 4 .   ? 10.677 42.242  49.116 1.00 33.39 ? 496 HOH A O   1 
HETATM 2105 O  O   . HOH H 4 .   ? 7.888  25.702  53.200 1.00 39.23 ? 497 HOH A O   1 
HETATM 2106 O  O   . HOH H 4 .   ? 3.101  27.635  46.851 1.00 35.75 ? 498 HOH A O   1 
HETATM 2107 O  O   . HOH H 4 .   ? 4.299  17.174  36.983 1.00 39.37 ? 499 HOH A O   1 
HETATM 2108 O  O   . HOH H 4 .   ? 23.349 37.035  35.089 1.00 24.33 ? 500 HOH A O   1 
HETATM 2109 O  O   . HOH H 4 .   ? 12.192 35.299  15.073 1.00 31.14 ? 501 HOH A O   1 
HETATM 2110 O  O   . HOH H 4 .   ? 22.353 16.555  45.595 1.00 49.43 ? 502 HOH A O   1 
HETATM 2111 O  O   . HOH H 4 .   ? 21.075 37.265  36.213 1.00 29.49 ? 503 HOH A O   1 
HETATM 2112 O  O   . HOH H 4 .   ? 8.831  42.553  14.818 1.00 43.35 ? 504 HOH A O   1 
HETATM 2113 O  O   . HOH H 4 .   ? 17.754 26.172  24.107 1.00 38.70 ? 505 HOH A O   1 
HETATM 2114 O  O   . HOH H 4 .   ? 0.233  27.489  46.887 1.00 42.44 ? 506 HOH A O   1 
HETATM 2115 O  O   . HOH H 4 .   ? 0.547  30.611  46.853 1.00 44.22 ? 507 HOH A O   1 
HETATM 2116 O  O   . HOH H 4 .   ? -3.086 22.474  40.210 1.00 39.47 ? 508 HOH A O   1 
HETATM 2117 O  O   . HOH H 4 .   ? 4.687  19.643  37.939 1.00 37.77 ? 509 HOH A O   1 
HETATM 2118 O  O   . HOH H 4 .   ? 17.482 32.194  51.051 1.00 19.03 ? 510 HOH A O   1 
HETATM 2119 O  O   . HOH H 4 .   ? 2.898  43.524  35.018 1.00 39.19 ? 511 HOH A O   1 
HETATM 2120 O  O   . HOH H 4 .   ? -0.303 42.786  36.465 1.00 36.81 ? 512 HOH A O   1 
HETATM 2121 O  O   . HOH H 4 .   ? 19.880 23.187  25.586 1.00 28.02 ? 513 HOH A O   1 
HETATM 2122 O  O   . HOH H 4 .   ? 19.316 34.105  50.235 1.00 23.96 ? 514 HOH A O   1 
HETATM 2123 O  O   . HOH H 4 .   ? 19.789 39.642  34.189 1.00 42.73 ? 515 HOH A O   1 
HETATM 2124 O  O   . HOH H 4 .   ? 1.491  37.253  42.110 1.00 40.05 ? 516 HOH A O   1 
HETATM 2125 O  O   . HOH H 4 .   ? 5.764  15.759  35.532 1.00 29.20 ? 517 HOH A O   1 
HETATM 2126 O  O   . HOH H 4 .   ? 19.079 23.841  52.081 1.00 33.51 ? 518 HOH A O   1 
HETATM 2127 O  O   . HOH H 4 .   ? 19.502 19.557  49.203 1.00 35.79 ? 519 HOH A O   1 
HETATM 2128 O  O   . HOH H 4 .   ? 30.255 27.058  33.918 1.00 39.61 ? 520 HOH A O   1 
HETATM 2129 O  O   . HOH H 4 .   ? 3.071  49.064  44.560 1.00 44.55 ? 521 HOH A O   1 
HETATM 2130 O  O   . HOH H 4 .   ? 10.738 21.400  25.544 1.00 41.33 ? 522 HOH A O   1 
HETATM 2131 O  O   . HOH H 4 .   ? 9.951  35.517  52.323 1.00 34.14 ? 523 HOH A O   1 
HETATM 2132 O  O   . HOH H 4 .   ? 22.011 35.109  49.843 1.00 40.63 ? 524 HOH A O   1 
HETATM 2133 O  O   . HOH H 4 .   ? 16.576 24.240  52.852 1.00 37.15 ? 525 HOH A O   1 
HETATM 2134 O  O   . HOH H 4 .   ? 26.851 15.441  39.637 1.00 36.69 ? 526 HOH A O   1 
HETATM 2135 O  O   . HOH H 4 .   ? 27.751 35.503  39.537 1.00 38.21 ? 527 HOH A O   1 
HETATM 2136 O  O   . HOH H 4 .   ? -5.114 14.844  42.524 1.00 40.60 ? 528 HOH A O   1 
HETATM 2137 O  O   . HOH H 4 .   ? 31.166 33.007  43.551 1.00 39.30 ? 529 HOH A O   1 
HETATM 2138 O  O   . HOH H 4 .   ? 2.806  44.442  40.718 1.00 40.14 ? 530 HOH A O   1 
HETATM 2139 O  O   . HOH H 4 .   ? 4.910  17.121  33.296 1.00 39.25 ? 531 HOH A O   1 
HETATM 2140 O  O   . HOH H 4 .   ? 31.946 20.100  29.777 1.00 41.46 ? 532 HOH A O   1 
HETATM 2141 O  O   . HOH H 4 .   ? 3.051  40.351  46.492 1.00 39.04 ? 533 HOH A O   1 
HETATM 2142 O  O   . HOH H 4 .   ? 0.842  43.784  33.859 1.00 42.33 ? 534 HOH A O   1 
HETATM 2143 O  O   . HOH I 4 .   ? 8.706  14.161  39.381 1.00 7.51  ? 402 HOH B O   1 
HETATM 2144 O  O   . HOH I 4 .   ? 15.170 17.039  33.062 1.00 11.14 ? 403 HOH B O   1 
HETATM 2145 O  O   . HOH I 4 .   ? 15.677 5.656   57.024 1.00 11.15 ? 404 HOH B O   1 
HETATM 2146 O  O   . HOH I 4 .   ? 15.821 -0.575  28.018 1.00 25.94 ? 405 HOH B O   1 
HETATM 2147 O  O   . HOH I 4 .   ? 2.891  -1.857  30.054 1.00 15.79 ? 406 HOH B O   1 
HETATM 2148 O  O   . HOH I 4 .   ? 2.022  8.953   30.652 1.00 14.47 ? 407 HOH B O   1 
HETATM 2149 O  O   . HOH I 4 .   ? 3.438  5.452   28.715 1.00 16.59 ? 408 HOH B O   1 
HETATM 2150 O  O   . HOH I 4 .   ? 20.531 4.171   52.384 1.00 16.33 ? 409 HOH B O   1 
HETATM 2151 O  O   . HOH I 4 .   ? 4.280  -3.779  42.616 1.00 20.08 ? 410 HOH B O   1 
HETATM 2152 O  O   . HOH I 4 .   ? 1.688  0.305   29.163 1.00 14.89 ? 411 HOH B O   1 
HETATM 2153 O  O   . HOH I 4 .   ? 20.865 9.596   53.889 1.00 16.11 ? 412 HOH B O   1 
HETATM 2154 O  O   . HOH I 4 .   ? 26.066 10.695  37.832 1.00 19.67 ? 413 HOH B O   1 
HETATM 2155 O  O   . HOH I 4 .   ? 25.541 5.583   36.955 1.00 16.77 ? 414 HOH B O   1 
HETATM 2156 O  O   . HOH I 4 .   ? 10.116 14.934  35.972 1.00 18.33 ? 415 HOH B O   1 
HETATM 2157 O  O   . HOH I 4 .   ? 10.845 -4.547  50.049 1.00 23.37 ? 416 HOH B O   1 
HETATM 2158 O  O   . HOH I 4 .   ? 12.412 3.726   25.681 1.00 22.88 ? 417 HOH B O   1 
HETATM 2159 O  O   . HOH I 4 .   ? 9.361  6.022   56.904 1.00 23.06 ? 418 HOH B O   1 
HETATM 2160 O  O   . HOH I 4 .   ? 22.185 14.429  30.710 1.00 20.45 ? 419 HOH B O   1 
HETATM 2161 O  O   . HOH I 4 .   ? 23.497 6.982   52.294 1.00 21.20 ? 420 HOH B O   1 
HETATM 2162 O  O   . HOH I 4 .   ? 10.719 -4.740  43.577 1.00 18.33 ? 421 HOH B O   1 
HETATM 2163 O  O   . HOH I 4 .   ? 9.999  8.790   26.464 1.00 26.95 ? 422 HOH B O   1 
HETATM 2164 O  O   . HOH I 4 .   ? 7.248  13.680  35.275 1.00 21.26 ? 423 HOH B O   1 
HETATM 2165 O  O   . HOH I 4 .   ? 4.510  -3.521  28.648 1.00 22.33 ? 424 HOH B O   1 
HETATM 2166 O  O   . HOH I 4 .   ? 20.705 1.642   54.490 1.00 22.80 ? 425 HOH B O   1 
HETATM 2167 O  O   . HOH I 4 .   ? 4.973  -10.729 33.799 1.00 22.62 ? 426 HOH B O   1 
HETATM 2168 O  O   . HOH I 4 .   ? -2.808 -6.417  30.619 1.00 22.69 ? 427 HOH B O   1 
HETATM 2169 O  O   . HOH I 4 .   ? 21.421 0.759   31.587 1.00 24.14 ? 428 HOH B O   1 
HETATM 2170 O  O   . HOH I 4 .   ? 19.976 8.288   27.773 1.00 19.50 ? 429 HOH B O   1 
HETATM 2171 O  O   . HOH I 4 .   ? 16.288 2.039   27.129 1.00 22.33 ? 430 HOH B O   1 
HETATM 2172 O  O   . HOH I 4 .   ? 19.593 -0.196  27.786 1.00 23.64 ? 431 HOH B O   1 
HETATM 2173 O  O   . HOH I 4 .   ? 26.823 12.394  40.080 1.00 27.06 ? 432 HOH B O   1 
HETATM 2174 O  O   . HOH I 4 .   ? 5.522  -8.270  31.942 1.00 33.32 ? 433 HOH B O   1 
HETATM 2175 O  O   . HOH I 4 .   ? 21.436 11.993  29.168 1.00 26.39 ? 434 HOH B O   1 
HETATM 2176 O  O   . HOH I 4 .   ? 0.878  7.311   44.838 1.00 26.12 ? 435 HOH B O   1 
HETATM 2177 O  O   . HOH I 4 .   ? 16.086 -4.476  27.197 1.00 22.71 ? 436 HOH B O   1 
HETATM 2178 O  O   . HOH I 4 .   ? 18.278 11.423  54.037 1.00 29.01 ? 437 HOH B O   1 
HETATM 2179 O  O   . HOH I 4 .   ? 1.240  8.502   50.752 1.00 33.24 ? 438 HOH B O   1 
HETATM 2180 O  O   . HOH I 4 .   ? 3.701  3.643   26.647 1.00 25.98 ? 439 HOH B O   1 
HETATM 2181 O  O   . HOH I 4 .   ? -0.281 7.236   41.823 1.00 29.14 ? 440 HOH B O   1 
HETATM 2182 O  O   . HOH I 4 .   ? 7.754  15.687  37.180 1.00 21.77 ? 441 HOH B O   1 
HETATM 2183 O  O   . HOH I 4 .   ? 25.390 2.389   34.425 1.00 21.61 ? 442 HOH B O   1 
HETATM 2184 O  O   . HOH I 4 .   ? 21.550 14.209  44.434 1.00 25.88 ? 443 HOH B O   1 
HETATM 2185 O  O   . HOH I 4 .   ? 4.226  13.693  55.444 1.00 42.00 ? 444 HOH B O   1 
HETATM 2186 O  O   . HOH I 4 .   ? 19.028 -1.111  37.742 1.00 28.63 ? 445 HOH B O   1 
HETATM 2187 O  O   . HOH I 4 .   ? -3.481 -3.731  31.325 1.00 25.08 ? 446 HOH B O   1 
HETATM 2188 O  O   . HOH I 4 .   ? 8.634  -5.245  48.140 1.00 25.94 ? 447 HOH B O   1 
HETATM 2189 O  O   . HOH I 4 .   ? 2.907  12.353  47.144 1.00 25.69 ? 448 HOH B O   1 
HETATM 2190 O  O   . HOH I 4 .   ? 10.821 6.238   26.381 1.00 31.14 ? 449 HOH B O   1 
HETATM 2191 O  O   . HOH I 4 .   ? -8.046 -0.165  33.424 1.00 28.72 ? 450 HOH B O   1 
HETATM 2192 O  O   . HOH I 4 .   ? 0.892  10.526  27.356 1.00 26.58 ? 451 HOH B O   1 
HETATM 2193 O  O   . HOH I 4 .   ? 10.425 14.254  30.493 1.00 36.79 ? 452 HOH B O   1 
HETATM 2194 O  O   . HOH I 4 .   ? 23.291 4.118   52.374 1.00 31.30 ? 453 HOH B O   1 
HETATM 2195 O  O   . HOH I 4 .   ? 8.190  12.613  32.662 1.00 26.35 ? 454 HOH B O   1 
HETATM 2196 O  O   . HOH I 4 .   ? 1.381  10.954  36.400 1.00 28.17 ? 455 HOH B O   1 
HETATM 2197 O  O   . HOH I 4 .   ? 0.517  -4.567  42.708 1.00 31.35 ? 456 HOH B O   1 
HETATM 2198 O  O   . HOH I 4 .   ? 3.395  -7.472  30.949 1.00 34.20 ? 457 HOH B O   1 
HETATM 2199 O  O   . HOH I 4 .   ? 24.627 10.405  44.031 1.00 24.98 ? 458 HOH B O   1 
HETATM 2200 O  O   . HOH I 4 .   ? 23.824 11.203  54.629 1.00 33.90 ? 459 HOH B O   1 
HETATM 2201 O  O   . HOH I 4 .   ? 28.833 3.539   36.138 1.00 25.40 ? 460 HOH B O   1 
HETATM 2202 O  O   . HOH I 4 .   ? 5.683  9.443   57.220 1.00 39.97 ? 461 HOH B O   1 
HETATM 2203 O  O   . HOH I 4 .   ? 24.160 2.657   55.068 1.00 29.36 ? 462 HOH B O   1 
HETATM 2204 O  O   . HOH I 4 .   ? 19.703 15.309  50.189 1.00 37.53 ? 463 HOH B O   1 
HETATM 2205 O  O   . HOH I 4 .   ? 7.065  6.615   27.113 1.00 31.31 ? 464 HOH B O   1 
HETATM 2206 O  O   . HOH I 4 .   ? -4.508 0.906   34.224 1.00 14.32 ? 465 HOH B O   1 
HETATM 2207 O  O   . HOH I 4 .   ? -3.536 5.592   32.602 1.00 16.36 ? 466 HOH B O   1 
HETATM 2208 O  O   . HOH I 4 .   ? 6.731  11.851  48.990 1.00 15.11 ? 467 HOH B O   1 
HETATM 2209 O  O   . HOH I 4 .   ? 6.497  19.242  52.163 1.00 17.90 ? 468 HOH B O   1 
HETATM 2210 O  O   . HOH I 4 .   ? 7.618  0.797   52.171 1.00 36.48 ? 469 HOH B O   1 
HETATM 2211 O  O   . HOH I 4 .   ? 30.622 7.996   50.904 1.00 28.37 ? 470 HOH B O   1 
HETATM 2212 O  O   . HOH I 4 .   ? 5.103  -2.853  52.584 1.00 30.85 ? 471 HOH B O   1 
HETATM 2213 O  O   . HOH I 4 .   ? -4.077 12.035  34.727 1.00 34.43 ? 472 HOH B O   1 
HETATM 2214 O  O   . HOH I 4 .   ? -2.673 -2.464  47.437 1.00 39.26 ? 473 HOH B O   1 
HETATM 2215 O  O   . HOH I 4 .   ? 11.812 -12.067 36.919 1.00 40.43 ? 474 HOH B O   1 
HETATM 2216 O  O   . HOH I 4 .   ? 0.748  7.135   22.900 1.00 30.27 ? 475 HOH B O   1 
HETATM 2217 O  O   . HOH I 4 .   ? 6.596  10.921  58.732 1.00 45.27 ? 476 HOH B O   1 
HETATM 2218 O  O   . HOH I 4 .   ? 18.305 -3.333  27.845 1.00 36.00 ? 477 HOH B O   1 
HETATM 2219 O  O   . HOH I 4 .   ? -0.531 -9.498  38.284 1.00 31.09 ? 478 HOH B O   1 
HETATM 2220 O  O   . HOH I 4 .   ? -0.686 1.735   46.783 1.00 35.83 ? 479 HOH B O   1 
HETATM 2221 O  O   . HOH I 4 .   ? 18.028 -3.391  50.148 1.00 31.38 ? 480 HOH B O   1 
HETATM 2222 O  O   . HOH I 4 .   ? 29.416 0.717   34.724 1.00 35.09 ? 481 HOH B O   1 
HETATM 2223 O  O   . HOH I 4 .   ? -7.093 -2.046  40.312 1.00 38.36 ? 482 HOH B O   1 
HETATM 2224 O  O   . HOH I 4 .   ? 0.636  -7.804  43.580 1.00 44.54 ? 483 HOH B O   1 
HETATM 2225 O  O   . HOH I 4 .   ? 24.469 7.119   49.803 1.00 18.65 ? 484 HOH B O   1 
HETATM 2226 O  O   . HOH I 4 .   ? 17.883 9.677   23.042 1.00 44.14 ? 485 HOH B O   1 
HETATM 2227 O  O   . HOH I 4 .   ? 27.434 8.927   39.621 1.00 37.71 ? 486 HOH B O   1 
HETATM 2228 O  O   . HOH I 4 .   ? 21.026 12.554  55.261 1.00 37.21 ? 487 HOH B O   1 
HETATM 2229 O  O   . HOH I 4 .   ? 13.853 17.010  55.535 1.00 37.70 ? 488 HOH B O   1 
HETATM 2230 O  O   . HOH I 4 .   ? 1.336  4.241   23.303 1.00 42.30 ? 489 HOH B O   1 
HETATM 2231 O  O   . HOH I 4 .   ? 23.783 2.666   50.603 1.00 39.55 ? 490 HOH B O   1 
HETATM 2232 O  O   . HOH I 4 .   ? 1.113  9.694   47.081 1.00 40.15 ? 491 HOH B O   1 
HETATM 2233 O  O   . HOH I 4 .   ? 18.844 -1.184  44.818 1.00 20.87 ? 492 HOH B O   1 
HETATM 2234 O  O   . HOH I 4 .   ? 27.830 7.814   50.898 1.00 23.93 ? 493 HOH B O   1 
HETATM 2235 O  O   . HOH I 4 .   ? -5.274 -8.873  38.897 1.00 32.52 ? 494 HOH B O   1 
HETATM 2236 O  O   . HOH I 4 .   ? 18.356 15.480  24.664 1.00 35.66 ? 495 HOH B O   1 
HETATM 2237 O  O   . HOH I 4 .   ? 17.749 -15.178 34.743 1.00 45.24 ? 496 HOH B O   1 
HETATM 2238 O  O   . HOH I 4 .   ? 8.513  -9.471  30.816 1.00 37.59 ? 497 HOH B O   1 
HETATM 2239 O  O   . HOH I 4 .   ? 10.305 -2.071  22.778 1.00 40.34 ? 498 HOH B O   1 
HETATM 2240 O  O   . HOH I 4 .   ? 14.831 -3.367  46.180 1.00 42.94 ? 499 HOH B O   1 
HETATM 2241 O  O   . HOH I 4 .   ? 17.246 -14.982 37.635 1.00 40.20 ? 500 HOH B O   1 
HETATM 2242 O  O   . HOH I 4 .   ? 8.450  -5.509  22.665 1.00 37.05 ? 501 HOH B O   1 
HETATM 2243 O  O   . HOH I 4 .   ? 16.866 -5.526  43.590 1.00 47.83 ? 502 HOH B O   1 
HETATM 2244 O  O   . HOH I 4 .   ? 18.159 12.855  58.323 1.00 31.95 ? 503 HOH B O   1 
HETATM 2245 O  O   . HOH I 4 .   ? 2.798  11.409  23.360 1.00 40.32 ? 504 HOH B O   1 
HETATM 2246 O  O   . HOH I 4 .   ? 7.464  -2.956  52.355 1.00 41.88 ? 505 HOH B O   1 
HETATM 2247 O  O   . HOH I 4 .   ? 16.545 -7.081  39.199 1.00 40.71 ? 506 HOH B O   1 
HETATM 2248 O  O   . HOH I 4 .   ? 2.356  13.289  50.035 1.00 48.67 ? 507 HOH B O   1 
HETATM 2249 O  O   . HOH I 4 .   ? -1.523 5.698   39.771 1.00 41.63 ? 508 HOH B O   1 
HETATM 2250 O  O   . HOH I 4 .   ? 19.570 -6.263  42.486 1.00 42.89 ? 509 HOH B O   1 
HETATM 2251 O  O   . HOH I 4 .   ? -3.733 4.144   41.219 1.00 40.47 ? 510 HOH B O   1 
HETATM 2252 O  O   . HOH I 4 .   ? 4.997  14.144  49.584 1.00 38.62 ? 511 HOH B O   1 
HETATM 2253 O  O   . HOH I 4 .   ? 0.773  11.626  24.691 1.00 37.25 ? 512 HOH B O   1 
HETATM 2254 O  O   . HOH I 4 .   ? 3.068  10.708  50.870 1.00 41.14 ? 513 HOH B O   1 
HETATM 2255 O  O   . HOH I 4 .   ? 28.767 2.176   45.268 1.00 42.60 ? 514 HOH B O   1 
HETATM 2256 O  O   . HOH I 4 .   ? -0.930 9.949   38.137 1.00 42.63 ? 515 HOH B O   1 
HETATM 2257 O  O   . HOH I 4 .   ? 16.971 16.348  54.964 1.00 33.54 ? 516 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   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CSX 111 111 111 CSX CSX A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 ?   ?   ?   A . n 
A 1 133 GLU 133 133 ?   ?   ?   A . n 
A 1 134 ASN 134 134 ?   ?   ?   A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   201 201 ALA ALA B . n 
B 1 2   THR 2   202 202 THR THR B . n 
B 1 3   LYS 3   203 203 LYS LYS B . n 
B 1 4   ALA 4   204 204 ALA ALA B . n 
B 1 5   VAL 5   205 205 VAL VAL B . n 
B 1 6   CYS 6   206 206 CYS CYS B . n 
B 1 7   VAL 7   207 207 VAL VAL B . n 
B 1 8   LEU 8   208 208 LEU LEU B . n 
B 1 9   LYS 9   209 209 LYS LYS B . n 
B 1 10  GLY 10  210 210 GLY GLY B . n 
B 1 11  ASP 11  211 211 ASP ASP B . n 
B 1 12  GLY 12  212 212 GLY GLY B . n 
B 1 13  PRO 13  213 213 PRO PRO B . n 
B 1 14  VAL 14  214 214 VAL VAL B . n 
B 1 15  GLN 15  215 215 GLN GLN B . n 
B 1 16  GLY 16  216 216 GLY GLY B . n 
B 1 17  ILE 17  217 217 ILE ILE B . n 
B 1 18  ILE 18  218 218 ILE ILE B . n 
B 1 19  ASN 19  219 219 ASN ASN B . n 
B 1 20  PHE 20  220 220 PHE PHE B . n 
B 1 21  GLU 21  221 221 GLU GLU B . n 
B 1 22  GLN 22  222 222 GLN GLN B . n 
B 1 23  LYS 23  223 223 LYS LYS B . n 
B 1 24  GLU 24  224 224 GLU GLU B . n 
B 1 25  SER 25  225 225 SER SER B . n 
B 1 26  ASN 26  226 226 ASN ASN B . n 
B 1 27  GLY 27  227 227 GLY GLY B . n 
B 1 28  PRO 28  228 228 PRO PRO B . n 
B 1 29  VAL 29  229 229 VAL VAL B . n 
B 1 30  LYS 30  230 230 LYS LYS B . n 
B 1 31  VAL 31  231 231 VAL VAL B . n 
B 1 32  TRP 32  232 232 TRP TRP B . n 
B 1 33  GLY 33  233 233 GLY GLY B . n 
B 1 34  SER 34  234 234 SER SER B . n 
B 1 35  ILE 35  235 235 ILE ILE B . n 
B 1 36  LYS 36  236 236 LYS LYS B . n 
B 1 37  GLY 37  237 237 GLY GLY B . n 
B 1 38  LEU 38  238 238 LEU LEU B . n 
B 1 39  THR 39  239 239 THR THR B . n 
B 1 40  GLU 40  240 240 GLU GLU B . n 
B 1 41  GLY 41  241 241 GLY GLY B . n 
B 1 42  LEU 42  242 242 LEU LEU B . n 
B 1 43  HIS 43  243 243 HIS HIS B . n 
B 1 44  GLY 44  244 244 GLY GLY B . n 
B 1 45  PHE 45  245 245 PHE PHE B . n 
B 1 46  HIS 46  246 246 HIS HIS B . n 
B 1 47  VAL 47  247 247 VAL VAL B . n 
B 1 48  HIS 48  248 248 HIS HIS B . n 
B 1 49  GLU 49  249 249 GLU GLU B . n 
B 1 50  PHE 50  250 250 PHE PHE B . n 
B 1 51  GLY 51  251 251 GLY GLY B . n 
B 1 52  ASP 52  252 252 ASP ASP B . n 
B 1 53  ASN 53  253 253 ASN ASN B . n 
B 1 54  THR 54  254 254 THR THR B . n 
B 1 55  ALA 55  255 255 ALA ALA B . n 
B 1 56  GLY 56  256 256 GLY GLY B . n 
B 1 57  CYS 57  257 257 CYS CYS B . n 
B 1 58  THR 58  258 258 THR THR B . n 
B 1 59  SER 59  259 259 SER SER B . n 
B 1 60  ALA 60  260 260 ALA ALA B . n 
B 1 61  GLY 61  261 261 GLY GLY B . n 
B 1 62  PRO 62  262 262 PRO PRO B . n 
B 1 63  HIS 63  263 263 HIS HIS B . n 
B 1 64  PHE 64  264 264 PHE PHE B . n 
B 1 65  ASN 65  265 265 ASN ASN B . n 
B 1 66  PRO 66  266 266 PRO PRO B . n 
B 1 67  LEU 67  267 ?   ?   ?   B . n 
B 1 68  SER 68  268 ?   ?   ?   B . n 
B 1 69  ARG 69  269 ?   ?   ?   B . n 
B 1 70  LYS 70  270 ?   ?   ?   B . n 
B 1 71  HIS 71  271 ?   ?   ?   B . n 
B 1 72  GLY 72  272 ?   ?   ?   B . n 
B 1 73  GLY 73  273 ?   ?   ?   B . n 
B 1 74  PRO 74  274 ?   ?   ?   B . n 
B 1 75  LYS 75  275 ?   ?   ?   B . n 
B 1 76  ASP 76  276 ?   ?   ?   B . n 
B 1 77  GLU 77  277 ?   ?   ?   B . n 
B 1 78  GLU 78  278 ?   ?   ?   B . n 
B 1 79  ARG 79  279 ?   ?   ?   B . n 
B 1 80  HIS 80  280 280 HIS HIS B . n 
B 1 81  VAL 81  281 281 VAL VAL B . n 
B 1 82  GLY 82  282 282 GLY GLY B . n 
B 1 83  ASP 83  283 283 ASP ASP B . n 
B 1 84  LEU 84  284 284 LEU LEU B . n 
B 1 85  GLY 85  285 285 GLY GLY B . n 
B 1 86  ASN 86  286 286 ASN ASN B . n 
B 1 87  VAL 87  287 287 VAL VAL B . n 
B 1 88  THR 88  288 288 THR THR B . n 
B 1 89  ALA 89  289 289 ALA ALA B . n 
B 1 90  ASP 90  290 290 ASP ASP B . n 
B 1 91  LYS 91  291 291 LYS LYS B . n 
B 1 92  ASP 92  292 292 ASP ASP B . n 
B 1 93  GLY 93  293 293 GLY GLY B . n 
B 1 94  VAL 94  294 294 VAL VAL B . n 
B 1 95  ALA 95  295 295 ALA ALA B . n 
B 1 96  ASP 96  296 296 ASP ASP B . n 
B 1 97  VAL 97  297 297 VAL VAL B . n 
B 1 98  SER 98  298 298 SER SER B . n 
B 1 99  ILE 99  299 299 ILE ILE B . n 
B 1 100 GLU 100 300 300 GLU GLU B . n 
B 1 101 ASP 101 301 301 ASP ASP B . n 
B 1 102 SER 102 302 302 SER SER B . n 
B 1 103 VAL 103 303 303 VAL VAL B . n 
B 1 104 ILE 104 304 304 ILE ILE B . n 
B 1 105 SER 105 305 305 SER SER B . n 
B 1 106 LEU 106 306 306 LEU LEU B . n 
B 1 107 SER 107 307 307 SER SER B . n 
B 1 108 GLY 108 308 308 GLY GLY B . n 
B 1 109 ASP 109 309 309 ASP ASP B . n 
B 1 110 HIS 110 310 310 HIS HIS B . n 
B 1 111 CSX 111 311 311 CSX CSX B . n 
B 1 112 ILE 112 312 312 ILE ILE B . n 
B 1 113 ILE 113 313 313 ILE ILE B . n 
B 1 114 GLY 114 314 314 GLY GLY B . n 
B 1 115 ARG 115 315 315 ARG ARG B . n 
B 1 116 THR 116 316 316 THR THR B . n 
B 1 117 LEU 117 317 317 LEU LEU B . n 
B 1 118 VAL 118 318 318 VAL VAL B . n 
B 1 119 VAL 119 319 319 VAL VAL B . n 
B 1 120 HIS 120 320 320 HIS HIS B . n 
B 1 121 GLU 121 321 321 GLU GLU B . n 
B 1 122 LYS 122 322 322 LYS LYS B . n 
B 1 123 ALA 123 323 323 ALA ALA B . n 
B 1 124 ASP 124 324 324 ASP ASP B . n 
B 1 125 ASP 125 325 325 ASP ASP B . n 
B 1 126 LEU 126 326 ?   ?   ?   B . n 
B 1 127 GLY 127 327 ?   ?   ?   B . n 
B 1 128 LYS 128 328 ?   ?   ?   B . n 
B 1 129 GLY 129 329 ?   ?   ?   B . n 
B 1 130 GLY 130 330 ?   ?   ?   B . n 
B 1 131 ASN 131 331 ?   ?   ?   B . n 
B 1 132 GLU 132 332 ?   ?   ?   B . n 
B 1 133 GLU 133 333 ?   ?   ?   B . n 
B 1 134 ASN 134 334 ?   ?   ?   B . n 
B 1 135 THR 135 335 ?   ?   ?   B . n 
B 1 136 LYS 136 336 ?   ?   ?   B . n 
B 1 137 THR 137 337 ?   ?   ?   B . n 
B 1 138 GLY 138 338 ?   ?   ?   B . n 
B 1 139 ASN 139 339 339 ASN ASN B . n 
B 1 140 ALA 140 340 340 ALA ALA B . n 
B 1 141 GLY 141 341 341 GLY GLY B . n 
B 1 142 SER 142 342 342 SER SER B . n 
B 1 143 ARG 143 343 343 ARG ARG B . n 
B 1 144 LEU 144 344 344 LEU LEU B . n 
B 1 145 ALA 145 345 345 ALA ALA B . n 
B 1 146 CYS 146 346 346 CYS CYS B . n 
B 1 147 GLY 147 347 347 GLY GLY B . n 
B 1 148 VAL 148 348 348 VAL VAL B . n 
B 1 149 ILE 149 349 349 ILE ILE B . n 
B 1 150 GLY 150 350 350 GLY GLY B . n 
B 1 151 ILE 151 351 351 ILE ILE B . n 
B 1 152 ALA 152 352 352 ALA ALA B . n 
B 1 153 GLN 153 353 353 GLN GLN 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 ZN  1   354 354 ZN  ZN  A . 
D 2 ZN  1   355 355 ZN  ZN  A . 
E 3 SO4 1   402 2   SO4 SO4 A . 
F 2 ZN  1   356 356 ZN  ZN  B . 
G 3 SO4 1   401 1   SO4 SO4 B . 
H 4 HOH 1   403 2   HOH HOH A . 
H 4 HOH 2   404 3   HOH HOH A . 
H 4 HOH 3   405 6   HOH HOH A . 
H 4 HOH 4   406 7   HOH HOH A . 
H 4 HOH 5   407 9   HOH HOH A . 
H 4 HOH 6   408 10  HOH HOH A . 
H 4 HOH 7   409 12  HOH HOH A . 
H 4 HOH 8   410 14  HOH HOH A . 
H 4 HOH 9   411 17  HOH HOH A . 
H 4 HOH 10  412 20  HOH HOH A . 
H 4 HOH 11  413 21  HOH HOH A . 
H 4 HOH 12  414 23  HOH HOH A . 
H 4 HOH 13  415 24  HOH HOH A . 
H 4 HOH 14  416 26  HOH HOH A . 
H 4 HOH 15  417 27  HOH HOH A . 
H 4 HOH 16  418 29  HOH HOH A . 
H 4 HOH 17  419 31  HOH HOH A . 
H 4 HOH 18  420 34  HOH HOH A . 
H 4 HOH 19  421 35  HOH HOH A . 
H 4 HOH 20  422 37  HOH HOH A . 
H 4 HOH 21  423 38  HOH HOH A . 
H 4 HOH 22  424 39  HOH HOH A . 
H 4 HOH 23  425 41  HOH HOH A . 
H 4 HOH 24  426 44  HOH HOH A . 
H 4 HOH 25  427 45  HOH HOH A . 
H 4 HOH 26  428 46  HOH HOH A . 
H 4 HOH 27  429 47  HOH HOH A . 
H 4 HOH 28  430 49  HOH HOH A . 
H 4 HOH 29  431 50  HOH HOH A . 
H 4 HOH 30  432 57  HOH HOH A . 
H 4 HOH 31  433 59  HOH HOH A . 
H 4 HOH 32  434 61  HOH HOH A . 
H 4 HOH 33  435 62  HOH HOH A . 
H 4 HOH 34  436 65  HOH HOH A . 
H 4 HOH 35  437 68  HOH HOH A . 
H 4 HOH 36  438 69  HOH HOH A . 
H 4 HOH 37  439 72  HOH HOH A . 
H 4 HOH 38  440 73  HOH HOH A . 
H 4 HOH 39  441 74  HOH HOH A . 
H 4 HOH 40  442 76  HOH HOH A . 
H 4 HOH 41  443 78  HOH HOH A . 
H 4 HOH 42  444 79  HOH HOH A . 
H 4 HOH 43  445 83  HOH HOH A . 
H 4 HOH 44  446 85  HOH HOH A . 
H 4 HOH 45  447 87  HOH HOH A . 
H 4 HOH 46  448 90  HOH HOH A . 
H 4 HOH 47  449 91  HOH HOH A . 
H 4 HOH 48  450 92  HOH HOH A . 
H 4 HOH 49  451 93  HOH HOH A . 
H 4 HOH 50  452 94  HOH HOH A . 
H 4 HOH 51  453 96  HOH HOH A . 
H 4 HOH 52  454 99  HOH HOH A . 
H 4 HOH 53  455 100 HOH HOH A . 
H 4 HOH 54  456 104 HOH HOH A . 
H 4 HOH 55  457 105 HOH HOH A . 
H 4 HOH 56  458 107 HOH HOH A . 
H 4 HOH 57  459 108 HOH HOH A . 
H 4 HOH 58  460 112 HOH HOH A . 
H 4 HOH 59  461 115 HOH HOH A . 
H 4 HOH 60  462 116 HOH HOH A . 
H 4 HOH 61  463 119 HOH HOH A . 
H 4 HOH 62  464 120 HOH HOH A . 
H 4 HOH 63  465 122 HOH HOH A . 
H 4 HOH 64  466 124 HOH HOH A . 
H 4 HOH 65  467 128 HOH HOH A . 
H 4 HOH 66  468 132 HOH HOH A . 
H 4 HOH 67  469 133 HOH HOH A . 
H 4 HOH 68  470 134 HOH HOH A . 
H 4 HOH 69  471 136 HOH HOH A . 
H 4 HOH 70  472 137 HOH HOH A . 
H 4 HOH 71  473 140 HOH HOH A . 
H 4 HOH 72  474 142 HOH HOH A . 
H 4 HOH 73  475 147 HOH HOH A . 
H 4 HOH 74  476 148 HOH HOH A . 
H 4 HOH 75  477 149 HOH HOH A . 
H 4 HOH 76  478 150 HOH HOH A . 
H 4 HOH 77  479 152 HOH HOH A . 
H 4 HOH 78  480 153 HOH HOH A . 
H 4 HOH 79  481 154 HOH HOH A . 
H 4 HOH 80  482 158 HOH HOH A . 
H 4 HOH 81  483 159 HOH HOH A . 
H 4 HOH 82  484 160 HOH HOH A . 
H 4 HOH 83  485 161 HOH HOH A . 
H 4 HOH 84  486 163 HOH HOH A . 
H 4 HOH 85  487 164 HOH HOH A . 
H 4 HOH 86  488 165 HOH HOH A . 
H 4 HOH 87  489 166 HOH HOH A . 
H 4 HOH 88  490 167 HOH HOH A . 
H 4 HOH 89  491 168 HOH HOH A . 
H 4 HOH 90  492 169 HOH HOH A . 
H 4 HOH 91  493 170 HOH HOH A . 
H 4 HOH 92  494 172 HOH HOH A . 
H 4 HOH 93  495 174 HOH HOH A . 
H 4 HOH 94  496 175 HOH HOH A . 
H 4 HOH 95  497 176 HOH HOH A . 
H 4 HOH 96  498 177 HOH HOH A . 
H 4 HOH 97  499 179 HOH HOH A . 
H 4 HOH 98  500 181 HOH HOH A . 
H 4 HOH 99  501 182 HOH HOH A . 
H 4 HOH 100 502 188 HOH HOH A . 
H 4 HOH 101 503 190 HOH HOH A . 
H 4 HOH 102 504 191 HOH HOH A . 
H 4 HOH 103 505 192 HOH HOH A . 
H 4 HOH 104 506 193 HOH HOH A . 
H 4 HOH 105 507 194 HOH HOH A . 
H 4 HOH 106 508 195 HOH HOH A . 
H 4 HOH 107 509 196 HOH HOH A . 
H 4 HOH 108 510 197 HOH HOH A . 
H 4 HOH 109 511 198 HOH HOH A . 
H 4 HOH 110 512 200 HOH HOH A . 
H 4 HOH 111 513 201 HOH HOH A . 
H 4 HOH 112 514 204 HOH HOH A . 
H 4 HOH 113 515 206 HOH HOH A . 
H 4 HOH 114 516 208 HOH HOH A . 
H 4 HOH 115 517 209 HOH HOH A . 
H 4 HOH 116 518 210 HOH HOH A . 
H 4 HOH 117 519 212 HOH HOH A . 
H 4 HOH 118 520 219 HOH HOH A . 
H 4 HOH 119 521 220 HOH HOH A . 
H 4 HOH 120 522 221 HOH HOH A . 
H 4 HOH 121 523 225 HOH HOH A . 
H 4 HOH 122 524 228 HOH HOH A . 
H 4 HOH 123 525 233 HOH HOH A . 
H 4 HOH 124 526 235 HOH HOH A . 
H 4 HOH 125 527 236 HOH HOH A . 
H 4 HOH 126 528 237 HOH HOH A . 
H 4 HOH 127 529 238 HOH HOH A . 
H 4 HOH 128 530 239 HOH HOH A . 
H 4 HOH 129 531 240 HOH HOH A . 
H 4 HOH 130 532 242 HOH HOH A . 
H 4 HOH 131 533 245 HOH HOH A . 
H 4 HOH 132 534 246 HOH HOH A . 
I 4 HOH 1   402 1   HOH HOH B . 
I 4 HOH 2   403 4   HOH HOH B . 
I 4 HOH 3   404 5   HOH HOH B . 
I 4 HOH 4   405 8   HOH HOH B . 
I 4 HOH 5   406 11  HOH HOH B . 
I 4 HOH 6   407 13  HOH HOH B . 
I 4 HOH 7   408 15  HOH HOH B . 
I 4 HOH 8   409 16  HOH HOH B . 
I 4 HOH 9   410 18  HOH HOH B . 
I 4 HOH 10  411 19  HOH HOH B . 
I 4 HOH 11  412 22  HOH HOH B . 
I 4 HOH 12  413 25  HOH HOH B . 
I 4 HOH 13  414 28  HOH HOH B . 
I 4 HOH 14  415 30  HOH HOH B . 
I 4 HOH 15  416 32  HOH HOH B . 
I 4 HOH 16  417 33  HOH HOH B . 
I 4 HOH 17  418 36  HOH HOH B . 
I 4 HOH 18  419 40  HOH HOH B . 
I 4 HOH 19  420 42  HOH HOH B . 
I 4 HOH 20  421 43  HOH HOH B . 
I 4 HOH 21  422 48  HOH HOH B . 
I 4 HOH 22  423 51  HOH HOH B . 
I 4 HOH 23  424 52  HOH HOH B . 
I 4 HOH 24  425 53  HOH HOH B . 
I 4 HOH 25  426 54  HOH HOH B . 
I 4 HOH 26  427 55  HOH HOH B . 
I 4 HOH 27  428 56  HOH HOH B . 
I 4 HOH 28  429 58  HOH HOH B . 
I 4 HOH 29  430 60  HOH HOH B . 
I 4 HOH 30  431 63  HOH HOH B . 
I 4 HOH 31  432 64  HOH HOH B . 
I 4 HOH 32  433 66  HOH HOH B . 
I 4 HOH 33  434 67  HOH HOH B . 
I 4 HOH 34  435 70  HOH HOH B . 
I 4 HOH 35  436 71  HOH HOH B . 
I 4 HOH 36  437 75  HOH HOH B . 
I 4 HOH 37  438 77  HOH HOH B . 
I 4 HOH 38  439 80  HOH HOH B . 
I 4 HOH 39  440 81  HOH HOH B . 
I 4 HOH 40  441 82  HOH HOH B . 
I 4 HOH 41  442 84  HOH HOH B . 
I 4 HOH 42  443 86  HOH HOH B . 
I 4 HOH 43  444 88  HOH HOH B . 
I 4 HOH 44  445 89  HOH HOH B . 
I 4 HOH 45  446 95  HOH HOH B . 
I 4 HOH 46  447 97  HOH HOH B . 
I 4 HOH 47  448 98  HOH HOH B . 
I 4 HOH 48  449 101 HOH HOH B . 
I 4 HOH 49  450 102 HOH HOH B . 
I 4 HOH 50  451 103 HOH HOH B . 
I 4 HOH 51  452 106 HOH HOH B . 
I 4 HOH 52  453 109 HOH HOH B . 
I 4 HOH 53  454 110 HOH HOH B . 
I 4 HOH 54  455 111 HOH HOH B . 
I 4 HOH 55  456 113 HOH HOH B . 
I 4 HOH 56  457 114 HOH HOH B . 
I 4 HOH 57  458 117 HOH HOH B . 
I 4 HOH 58  459 118 HOH HOH B . 
I 4 HOH 59  460 121 HOH HOH B . 
I 4 HOH 60  461 123 HOH HOH B . 
I 4 HOH 61  462 125 HOH HOH B . 
I 4 HOH 62  463 126 HOH HOH B . 
I 4 HOH 63  464 127 HOH HOH B . 
I 4 HOH 64  465 129 HOH HOH B . 
I 4 HOH 65  466 130 HOH HOH B . 
I 4 HOH 66  467 131 HOH HOH B . 
I 4 HOH 67  468 135 HOH HOH B . 
I 4 HOH 68  469 138 HOH HOH B . 
I 4 HOH 69  470 139 HOH HOH B . 
I 4 HOH 70  471 141 HOH HOH B . 
I 4 HOH 71  472 143 HOH HOH B . 
I 4 HOH 72  473 144 HOH HOH B . 
I 4 HOH 73  474 145 HOH HOH B . 
I 4 HOH 74  475 146 HOH HOH B . 
I 4 HOH 75  476 151 HOH HOH B . 
I 4 HOH 76  477 155 HOH HOH B . 
I 4 HOH 77  478 156 HOH HOH B . 
I 4 HOH 78  479 157 HOH HOH B . 
I 4 HOH 79  480 162 HOH HOH B . 
I 4 HOH 80  481 171 HOH HOH B . 
I 4 HOH 81  482 173 HOH HOH B . 
I 4 HOH 82  483 178 HOH HOH B . 
I 4 HOH 83  484 180 HOH HOH B . 
I 4 HOH 84  485 183 HOH HOH B . 
I 4 HOH 85  486 184 HOH HOH B . 
I 4 HOH 86  487 185 HOH HOH B . 
I 4 HOH 87  488 186 HOH HOH B . 
I 4 HOH 88  489 187 HOH HOH B . 
I 4 HOH 89  490 189 HOH HOH B . 
I 4 HOH 90  491 199 HOH HOH B . 
I 4 HOH 91  492 202 HOH HOH B . 
I 4 HOH 92  493 203 HOH HOH B . 
I 4 HOH 93  494 205 HOH HOH B . 
I 4 HOH 94  495 207 HOH HOH B . 
I 4 HOH 95  496 211 HOH HOH B . 
I 4 HOH 96  497 213 HOH HOH B . 
I 4 HOH 97  498 214 HOH HOH B . 
I 4 HOH 98  499 215 HOH HOH B . 
I 4 HOH 99  500 216 HOH HOH B . 
I 4 HOH 100 501 217 HOH HOH B . 
I 4 HOH 101 502 218 HOH HOH B . 
I 4 HOH 102 503 222 HOH HOH B . 
I 4 HOH 103 504 223 HOH HOH B . 
I 4 HOH 104 505 224 HOH HOH B . 
I 4 HOH 105 506 226 HOH HOH B . 
I 4 HOH 106 507 227 HOH HOH B . 
I 4 HOH 107 508 229 HOH HOH B . 
I 4 HOH 108 509 230 HOH HOH B . 
I 4 HOH 109 510 231 HOH HOH B . 
I 4 HOH 110 511 232 HOH HOH B . 
I 4 HOH 111 512 234 HOH HOH B . 
I 4 HOH 112 513 241 HOH HOH B . 
I 4 HOH 113 514 243 HOH HOH B . 
I 4 HOH 114 515 244 HOH HOH B . 
I 4 HOH 115 516 247 HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSX 111 A CSX 111 ? CYS 'S-OXY CYSTEINE' 
2 B CSX 111 B CSX 311 ? CYS 'S-OXY CYSTEINE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1850  ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  12780 ? 
# 
_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  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 130.1 ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 96.1  ? 
3  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 128.0 ? 
4  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 O4  ? E SO4 .   ? A SO4 402 ? 1_555 101.0 ? 
5  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 O4  ? E SO4 .   ? A SO4 402 ? 1_555 103.2 ? 
6  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? C ZN . ? A ZN 354 ? 1_555 O4  ? E SO4 .   ? A SO4 402 ? 1_555 87.0  ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 107.2 ? 
8  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 108.3 ? 
9  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 121.5 ? 
10 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 154.8 ? 
11 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 78.3  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 87.9  ? 
13 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 103.7 ? 
14 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 98.0  ? 
15 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 116.3 ? 
16 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 355 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 51.2  ? 
17 ND1 ? B HIS 46  ? B HIS 246 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 NE2 ? B HIS 48  ? B HIS 248 ? 1_555 124.2 ? 
18 ND1 ? B HIS 46  ? B HIS 246 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 NE2 ? B HIS 120 ? B HIS 320 ? 1_555 101.3 ? 
19 NE2 ? B HIS 48  ? B HIS 248 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 NE2 ? B HIS 120 ? B HIS 320 ? 1_555 114.2 ? 
20 ND1 ? B HIS 46  ? B HIS 246 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 O1  ? G SO4 .   ? B SO4 401 ? 1_555 100.6 ? 
21 NE2 ? B HIS 48  ? B HIS 248 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 O1  ? G SO4 .   ? B SO4 401 ? 1_555 105.3 ? 
22 NE2 ? B HIS 120 ? B HIS 320 ? 1_555 ZN ? F ZN . ? B ZN 356 ? 1_555 O1  ? G SO4 .   ? B SO4 401 ? 1_555 110.4 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2003-05-27 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-10-27 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
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 4 'Structure model' database_2             
2 4 'Structure model' pdbx_struct_conn_angle 
3 4 'Structure model' struct_conn            
4 4 'Structure model' struct_conn_type       
5 4 'Structure model' struct_ref_seq_dif     
6 4 '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  4 'Structure model' '_database_2.pdbx_DOI'                        
2  4 'Structure model' '_database_2.pdbx_database_accession'         
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 4 'Structure model' '_pdbx_struct_conn_angle.value'               
16 4 'Structure model' '_struct_conn.conn_type_id'                   
17 4 'Structure model' '_struct_conn.id'                             
18 4 'Structure model' '_struct_conn.pdbx_dist_value'                
19 4 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
20 4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
21 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
22 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
23 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
24 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
25 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
26 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
27 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
28 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
29 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
30 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
31 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
32 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
33 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
34 4 'Structure model' '_struct_conn_type.id'                        
35 4 'Structure model' '_struct_ref_seq_dif.details'                 
36 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
37 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
38 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC    refinement       5.0 ? 1 
HKL-2000  'data reduction' .   ? 2 
SCALEPACK 'data scaling'   .   ? 3 
AMoRE     phasing          .   ? 4 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB B ASP 324 ? ? CG B ASP 324 ? ? OD2 B ASP 324 ? ? 126.15 118.30 7.85 0.90 N 
2 1 CB B ASP 325 ? ? CG B ASP 325 ? ? OD2 B ASP 325 ? ? 123.96 118.30 5.66 0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CSX A 111 ? ? -35.05  109.66 
2 1 LYS A 128 ? ? -119.32 50.51  
3 1 ASN B 265 ? ? -160.56 76.57  
4 1 CSX B 311 ? ? -38.20  110.42 
# 
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 A ASN 131 ? CB  ? A ASN 131 CB  
2 1 Y 1 A ASN 131 ? CG  ? A ASN 131 CG  
3 1 Y 1 A ASN 131 ? OD1 ? A ASN 131 OD1 
4 1 Y 1 A ASN 131 ? ND2 ? A ASN 131 ND2 
5 1 Y 1 B ASN 339 ? CG  ? B ASN 139 CG  
6 1 Y 1 B ASN 339 ? OD1 ? B ASN 139 OD1 
7 1 Y 1 B ASN 339 ? ND2 ? B ASN 139 ND2 
# 
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 GLU 132 ? A GLU 132 
2  1 Y 1 A GLU 133 ? A GLU 133 
3  1 Y 1 A ASN 134 ? A ASN 134 
4  1 Y 1 B LEU 267 ? B LEU 67  
5  1 Y 1 B SER 268 ? B SER 68  
6  1 Y 1 B ARG 269 ? B ARG 69  
7  1 Y 1 B LYS 270 ? B LYS 70  
8  1 Y 1 B HIS 271 ? B HIS 71  
9  1 Y 1 B GLY 272 ? B GLY 72  
10 1 Y 1 B GLY 273 ? B GLY 73  
11 1 Y 1 B PRO 274 ? B PRO 74  
12 1 Y 1 B LYS 275 ? B LYS 75  
13 1 Y 1 B ASP 276 ? B ASP 76  
14 1 Y 1 B GLU 277 ? B GLU 77  
15 1 Y 1 B GLU 278 ? B GLU 78  
16 1 Y 1 B ARG 279 ? B ARG 79  
17 1 Y 1 B LEU 326 ? B LEU 126 
18 1 Y 1 B GLY 327 ? B GLY 127 
19 1 Y 1 B LYS 328 ? B LYS 128 
20 1 Y 1 B GLY 329 ? B GLY 129 
21 1 Y 1 B GLY 330 ? B GLY 130 
22 1 Y 1 B ASN 331 ? B ASN 131 
23 1 Y 1 B GLU 332 ? B GLU 132 
24 1 Y 1 B GLU 333 ? B GLU 133 
25 1 Y 1 B ASN 334 ? B ASN 134 
26 1 Y 1 B THR 335 ? B THR 135 
27 1 Y 1 B LYS 336 ? B LYS 136 
28 1 Y 1 B THR 337 ? B THR 137 
29 1 Y 1 B GLY 338 ? B GLY 138 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'    ZN  
3 'SULFATE ION' SO4 
4 water         HOH 
# 
