data_2C9S
# 
_entry.id   2C9S 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2C9S         
PDBE  EBI-26807    
WWPDB D_1290026807 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2C9S 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2005-12-14 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strange, R.W.'     1 
'Antonyuk, S.V.'    2 
'Hough, M.A.'       3 
'Doucette, P.A.'    4 
'Valentine S, J.S.' 5 
'Hasnain, S.'       6 
# 
_citation.id                        primary 
_citation.title                     
;Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-Type Enzymes.
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            356 
_citation.page_first                1152 
_citation.page_last                 ? 
_citation.year                      2006 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   16406071 
_citation.pdbx_database_id_DOI      10.1016/J.JMB.2005.11.081 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strange, R.W.'   1 
primary 'Antonyuk, S.V.'  2 
primary 'Hough, M.A.'     3 
primary 'Doucette, P.A.'  4 
primary 'Valentine, J.S.' 5 
primary 'Hasnain, S.S.'   6 
# 
_cell.entry_id           2C9S 
_cell.length_a           38.243 
_cell.length_b           67.742 
_cell.length_c           51.260 
_cell.angle_alpha        90.00 
_cell.angle_beta         106.44 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2C9S 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'SUPEROXIDE DISMUTASE [CU-ZN]' 15843.561 2   1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    6   ?        ? ? ? 
3 non-polymer syn 'ACETATE ION'                  59.044    3   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    6   ?        ? ? ? 
5 water       nat water                          18.015    507 ?        ? ? ? 
# 
_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(CSO)IIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F 
_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 CSO 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 SER 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                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    BLOOD 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'SACCHAROMYCES CEREVISIAE' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_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 2C9S A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 2C9S F 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
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 
ACT non-polymer         . 'ACETATE ION'     ? 'C2 H3 O2 -1'    59.044  
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 
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE ? '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          2C9S 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2 
_exptl_crystal.density_percent_sol   39 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.75 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '2.5M AMMONIUM SULPHATE,0.1M NACL,50MM ACETATE BUFFER, pH 4.75' 
# 
_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                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2003-06-20 
_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                    SILICON 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.89973 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE BM14' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   BM14 
_diffrn_source.pdbx_wavelength             0.89973 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2C9S 
_reflns.observed_criterion_sigma_I   0.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.000 
_reflns.d_resolution_high            1.240 
_reflns.number_obs                   67983 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.0 
_reflns.pdbx_Rmerge_I_obs            0.06000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.0000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.200 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.24 
_reflns_shell.d_res_low              1.28 
_reflns_shell.percent_possible_all   78.4 
_reflns_shell.Rmerge_I_obs           0.37000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.300 
_reflns_shell.pdbx_redundancy        2.20 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2C9S 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     65893 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.90 
_refine.ls_d_res_high                            1.24 
_refine.ls_percent_reflns_obs                    95.9 
_refine.ls_R_factor_obs                          0.154 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.152 
_refine.ls_R_factor_R_free                       0.194 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.000 
_refine.ls_number_reflns_R_free                  2061 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_refine.B_iso_mean                               10.82 
_refine.aniso_B[1][1]                            -0.86000 
_refine.aniso_B[2][2]                            0.07000 
_refine.aniso_B[3][3]                            0.81000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.03000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_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 1HL5' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_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                       0.053 
_refine.pdbx_overall_ESU_R_Free                  0.052 
_refine.overall_SU_ML                            0.037 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.889 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2222 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_refine_hist.number_atoms_solvent             507 
_refine_hist.number_atoms_total               2777 
_refine_hist.d_res_high                       1.24 
_refine_hist.d_res_low                        19.90 
# 
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             0.021  0.021  ? 2496 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 2154 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.105  1.959  ? 3382 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            2.248  3.000  ? 5098 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       13.340 5.117  ? 341  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       41.256 25.872 ? 109  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.800 15.000 ? 417  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       9.233  15.000 ? 9    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.127  0.200  ? 361  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 2885 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 445  'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.260  0.200  ? 549  'X-RAY DIFFRACTION' ? 
r_nbd_other                  0.210  0.200  ? 2364 'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.171  0.200  ? 1166 'X-RAY DIFFRACTION' ? 
r_nbtor_other                0.099  0.200  ? 1464 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.266  0.200  ? 359  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.308  0.200  ? 36   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         0.221  0.200  ? 81   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.272  0.200  ? 84   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.180  1.500  ? 2043 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.619  2.000  ? 2581 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.501  3.000  ? 967  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.468  4.500  ? 797  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.24 
_refine_ls_shell.d_res_low                        1.27 
_refine_ls_shell.number_reflns_R_work             3840 
_refine_ls_shell.R_factor_R_work                  0.2460 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.2580 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             113 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  2C9S 
_struct.title                     '1.24 Angstroms resolution structure of Zn-Zn Human Superoxide dismutase' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE [CU-ZN] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2C9S 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;ACETYLATION, AMYOTROPHIC LATERAL SCLEROSIS, ZINC, ANTIOXIDANT, COPPER, DISEASE MUTATION, HUMAN CU, METAL-BINDING, OXIDOREDUCTASE, ZN SUPEROXIDE DISMUTASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 2 ? 
O N N 2 ? 
P N N 3 ? 
Q N N 2 ? 
R N N 5 ? 
S N N 5 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 55  ? ALA A 60  ? ALA A 55  ALA A 60  5 ? 6 
HELX_P HELX_P2 2 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P3 3 ALA B 55  ? GLY B 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P4 4 GLU B 132 ? LYS B 136 ? GLU F 132 LYS F 136 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57  SG ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57   A CYS 146  1_555 ? ? ? ? ? ? ? 2.167 ? 
disulf2  disulf ? ? B CYS 57  SG ? ? ? 1_555 B CYS 146 SG  ? ? F CYS 57   F CYS 146  1_555 ? ? ? ? ? ? ? 2.127 ? 
covale1  covale ? ? A HIS 110 C  ? ? ? 1_555 A CSO 111 N   ? ? A HIS 110  A CSO 111  1_555 ? ? ? ? ? ? ? 1.338 ? 
covale2  covale ? ? A CSO 111 C  ? ? ? 1_555 A ILE 112 N   ? ? A CSO 111  A ILE 112  1_555 ? ? ? ? ? ? ? 1.343 ? 
metalc1  metalc ? ? C ZN  .   ZN ? ? ? 1_555 A HIS 120 NE2 ? ? A ZN  1155 A HIS 120  1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc2  metalc ? ? C ZN  .   ZN ? ? ? 1_555 I SO4 .   O4  ? ? A ZN  1155 A SO4 1161 1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc3  metalc ? ? C ZN  .   ZN ? ? ? 1_555 A HIS 48  NE2 ? ? A ZN  1155 A HIS 48   1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc4  metalc ? ? C ZN  .   ZN ? ? ? 1_555 A HIS 46  ND1 ? ? A ZN  1155 A HIS 46   1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc5  metalc ? ? D ZN  .   ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  1156 A HIS 63   1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc6  metalc ? ? D ZN  .   ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  1156 A HIS 71   1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc7  metalc ? ? D ZN  .   ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  1156 A HIS 80   1_555 ? ? ? ? ? ? ? 2.004 ? 
metalc8  metalc ? ? D ZN  .   ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  1156 A ASP 83   1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc9  metalc ? ? E ZN  .   ZN ? ? ? 1_555 R HOH .   O   ? ? A ZN  1157 A HOH 2229 1_555 ? ? ? ? ? ? ? 1.879 ? 
metalc10 metalc ? ? E ZN  .   ZN ? ? ? 1_555 K SO4 .   O4  ? ? A ZN  1157 A SO4 1163 1_555 ? ? ? ? ? ? ? 1.859 ? 
metalc11 metalc ? ? E ZN  .   ZN ? ? ? 1_555 R HOH .   O   ? ? A ZN  1157 A HOH 2245 1_555 ? ? ? ? ? ? ? 2.552 ? 
metalc12 metalc ? ? E ZN  .   ZN ? ? ? 1_555 A ARG 143 N   ? ? A ZN  1157 A ARG 143  1_555 ? ? ? ? ? ? ? 2.375 ? 
metalc13 metalc ? ? E ZN  .   ZN ? ? ? 1_555 A ARG 143 O   ? ? A ZN  1157 A ARG 143  1_555 ? ? ? ? ? ? ? 2.353 ? 
covale3  covale ? ? B HIS 110 C  ? ? ? 1_555 B CSO 111 N   ? ? F HIS 110  F CSO 111  1_555 ? ? ? ? ? ? ? 1.335 ? 
covale4  covale ? ? B CSO 111 C  ? ? ? 1_555 B ILE 112 N   ? ? F CSO 111  F ILE 112  1_555 ? ? ? ? ? ? ? 1.330 ? 
metalc14 metalc ? ? L SO4 .   O1 ? ? ? 1_555 N ZN  .   ZN  ? ? F SO4 1154 F ZN  1157 1_555 ? ? ? ? ? ? ? 1.973 ? 
metalc15 metalc ? ? N ZN  .   ZN ? ? ? 1_555 B HIS 120 NE2 ? ? F ZN  1157 F HIS 120  1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc16 metalc ? ? N ZN  .   ZN ? ? ? 1_555 B HIS 48  NE2 ? ? F ZN  1157 F HIS 48   1_555 ? ? ? ? ? ? ? 2.024 ? 
metalc17 metalc ? ? N ZN  .   ZN ? ? ? 1_555 B HIS 46  ND1 ? ? F ZN  1157 F HIS 46   1_555 ? ? ? ? ? ? ? 2.062 ? 
metalc18 metalc ? ? O ZN  .   ZN ? ? ? 1_555 B HIS 80  ND1 ? ? F ZN  1158 F HIS 80   1_555 ? ? ? ? ? ? ? 2.003 ? 
metalc19 metalc ? ? O ZN  .   ZN ? ? ? 1_555 B HIS 71  ND1 ? ? F ZN  1158 F HIS 71   1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc20 metalc ? ? O ZN  .   ZN ? ? ? 1_555 B ASP 83  OD1 ? ? F ZN  1158 F ASP 83   1_555 ? ? ? ? ? ? ? 1.995 ? 
metalc21 metalc ? ? O ZN  .   ZN ? ? ? 1_555 B HIS 63  ND1 ? ? F ZN  1158 F HIS 63   1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc22 metalc ? ? Q ZN  .   ZN ? ? ? 1_555 M SO4 .   O1  ? ? F ZN  1160 F SO4 1155 1_555 ? ? ? ? ? ? ? 2.316 ? 
metalc23 metalc ? ? Q ZN  .   ZN ? ? ? 1_555 B ARG 143 N   ? ? F ZN  1160 F ARG 143  1_555 ? ? ? ? ? ? ? 2.212 ? 
metalc24 metalc ? ? Q ZN  .   ZN ? ? ? 1_555 B ARG 143 O   ? ? F ZN  1160 F ARG 143  1_555 ? ? ? ? ? ? ? 2.183 ? 
metalc25 metalc ? ? Q ZN  .   ZN ? ? ? 1_555 S HOH .   O   ? ? F ZN  1160 F HOH 2260 1_555 ? ? ? ? ? ? ? 2.114 ? 
# 
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 
AA ? 5  ? 
AB ? 4  ? 
FA ? 10 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2  ? anti-parallel 
AA 2 3  ? anti-parallel 
AA 3 4  ? anti-parallel 
AA 4 5  ? anti-parallel 
AB 1 2  ? anti-parallel 
AB 2 3  ? anti-parallel 
AB 3 4  ? anti-parallel 
FA 1 2  ? anti-parallel 
FA 2 3  ? anti-parallel 
FA 3 4  ? anti-parallel 
FA 4 5  ? anti-parallel 
FA 5 6  ? anti-parallel 
FA 6 7  ? anti-parallel 
FA 7 8  ? anti-parallel 
FA 8 9  ? anti-parallel 
FA 9 10 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1  ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA 2  VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 3  GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA 4  THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
AA 5  GLY A 150 ? ALA A 152 ? GLY A 150 ALA A 152 
AB 1  ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AB 2  GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AB 3  THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AB 4  ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
FA 1  THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
FA 2  GLN B 15  ? GLN B 22  ? GLN F 15  GLN F 22  
FA 3  VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
FA 4  ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
FA 5  ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
FA 6  GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
FA 7  THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
FA 8  ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 148 
FA 9  THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
FA 10 THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA 1 2  N ASP A 101 ? N ASP A 101 O VAL A 29  ? O VAL A 29  
AA 2 3  N LYS A 36  ? N LYS A 36  O GLN A 15  ? O GLN A 15  
AA 3 4  N GLN A 22  ? N GLN A 22  O THR A 2   ? O THR A 2   
AA 4 5  N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AB 1 2  N ALA A 89  ? N ALA A 89  O GLY A 41  ? O GLY A 41  
AB 2 3  N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AB 3 4  O VAL A 119 ? O VAL A 119 N LEU A 144 ? N LEU A 144 
FA 1 2  N LEU B 8   ? N LEU F 8   O GLY B 16  ? O GLY F 16  
FA 2 3  N GLU B 21  ? N GLU F 21  O LYS B 30  ? O LYS F 30  
FA 3 4  N ILE B 35  ? N ILE F 35  O ALA B 95  ? O ALA F 95  
FA 4 5  N ASP B 96  ? N ASP F 96  O THR B 88  ? O THR F 88  
FA 5 6  N ALA B 89  ? N ALA F 89  O GLY B 41  ? O GLY F 41  
FA 6 7  N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
FA 7 8  O VAL B 119 ? O VAL F 119 N LEU B 144 ? N LEU F 144 
FA 8 9  N CYS B 146 ? N CYS F 146 O LYS B 9   ? O LYS F 9   
FA 9 10 N LYS B 9   ? N LYS F 9   O VAL B 7   ? O VAL F 7   
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A1155'  
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A1156'  
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A1157'  
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE ACT A1158' 
AC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE ACT A1159' 
AC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A1160' 
AC7 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE SO4 A1161' 
AC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A1162' 
AC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A1163' 
BC1 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE SO4 F1154' 
BC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 F1155' 
BC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN F1157'  
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F1158'  
BC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE ACT F1159' 
BC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN F1160'  
# 
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 I .   ? SO4 A 1161 . ? 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  SER A 142 ? SER A 142  . ? 1_555 ? 
11  AC3 5  ARG A 143 ? ARG A 143  . ? 1_555 ? 
12  AC3 5  SO4 K .   ? SO4 A 1163 . ? 1_555 ? 
13  AC3 5  HOH R .   ? HOH A 2229 . ? 1_555 ? 
14  AC3 5  HOH R .   ? HOH A 2245 . ? 1_555 ? 
15  AC4 7  GLU A 132 ? GLU A 132  . ? 1_555 ? 
16  AC4 7  ACT G .   ? ACT A 1159 . ? 1_555 ? 
17  AC4 7  HOH R .   ? HOH A 2230 . ? 1_555 ? 
18  AC4 7  HOH R .   ? HOH A 2231 . ? 1_555 ? 
19  AC4 7  GLU B 132 ? GLU F 132  . ? 1_555 ? 
20  AC4 7  HOH S .   ? HOH F 2218 . ? 1_555 ? 
21  AC4 7  HOH S .   ? HOH F 2223 . ? 1_555 ? 
22  AC5 7  GLU A 132 ? GLU A 132  . ? 1_555 ? 
23  AC5 7  ACT F .   ? ACT A 1158 . ? 1_555 ? 
24  AC5 7  HOH R .   ? HOH A 2201 . ? 1_555 ? 
25  AC5 7  HOH R .   ? HOH A 2230 . ? 1_555 ? 
26  AC5 7  HOH R .   ? HOH A 2232 . ? 1_555 ? 
27  AC5 7  HOH R .   ? HOH A 2233 . ? 1_555 ? 
28  AC5 7  GLU B 132 ? GLU F 132  . ? 1_555 ? 
29  AC6 8  GLU A 40  ? GLU A 40   . ? 1_555 ? 
30  AC6 8  ARG A 69  ? ARG A 69   . ? 1_555 ? 
31  AC6 8  LYS A 91  ? LYS A 91   . ? 1_555 ? 
32  AC6 8  HOH R .   ? HOH A 2072 . ? 1_555 ? 
33  AC6 8  HOH R .   ? HOH A 2101 . ? 1_555 ? 
34  AC6 8  HOH R .   ? HOH A 2135 . ? 1_555 ? 
35  AC6 8  HOH R .   ? HOH A 2235 . ? 1_555 ? 
36  AC6 8  HOH R .   ? HOH A 2236 . ? 1_555 ? 
37  AC7 12 HIS A 46  ? HIS A 46   . ? 1_555 ? 
38  AC7 12 HIS A 48  ? HIS A 48   . ? 1_555 ? 
39  AC7 12 HIS A 63  ? HIS A 63   . ? 1_555 ? 
40  AC7 12 HIS A 120 ? HIS A 120  . ? 1_555 ? 
41  AC7 12 THR A 137 ? THR A 137  . ? 1_555 ? 
42  AC7 12 ARG A 143 ? ARG A 143  . ? 1_555 ? 
43  AC7 12 ZN  C .   ? ZN  A 1155 . ? 1_555 ? 
44  AC7 12 HOH R .   ? HOH A 2211 . ? 1_555 ? 
45  AC7 12 HOH R .   ? HOH A 2214 . ? 1_555 ? 
46  AC7 12 HOH R .   ? HOH A 2237 . ? 1_555 ? 
47  AC7 12 HOH R .   ? HOH A 2238 . ? 1_555 ? 
48  AC7 12 HOH R .   ? HOH A 2242 . ? 1_555 ? 
49  AC8 10 GLU A 133 ? GLU A 133  . ? 1_555 ? 
50  AC8 10 ASN A 139 ? ASN A 139  . ? 1_555 ? 
51  AC8 10 ALA A 140 ? ALA A 140  . ? 1_555 ? 
52  AC8 10 GLY A 141 ? GLY A 141  . ? 1_555 ? 
53  AC8 10 HOH R .   ? HOH A 2212 . ? 1_555 ? 
54  AC8 10 HOH R .   ? HOH A 2214 . ? 1_555 ? 
55  AC8 10 HOH R .   ? HOH A 2239 . ? 1_555 ? 
56  AC8 10 HOH R .   ? HOH A 2240 . ? 1_555 ? 
57  AC8 10 HOH R .   ? HOH A 2241 . ? 1_555 ? 
58  AC8 10 HOH R .   ? HOH A 2242 . ? 1_555 ? 
59  AC9 8  THR A 58  ? THR A 58   . ? 1_555 ? 
60  AC9 8  ARG A 143 ? ARG A 143  . ? 1_555 ? 
61  AC9 8  ZN  E .   ? ZN  A 1157 . ? 1_555 ? 
62  AC9 8  HOH R .   ? HOH A 2229 . ? 1_555 ? 
63  AC9 8  HOH R .   ? HOH A 2244 . ? 1_555 ? 
64  AC9 8  HOH R .   ? HOH A 2245 . ? 1_555 ? 
65  AC9 8  HOH R .   ? HOH A 2246 . ? 1_555 ? 
66  AC9 8  HOH R .   ? HOH A 2247 . ? 1_555 ? 
67  BC1 13 HIS B 46  ? HIS F 46   . ? 1_555 ? 
68  BC1 13 HIS B 48  ? HIS F 48   . ? 1_555 ? 
69  BC1 13 HIS B 63  ? HIS F 63   . ? 1_555 ? 
70  BC1 13 HIS B 120 ? HIS F 120  . ? 1_555 ? 
71  BC1 13 THR B 137 ? THR F 137  . ? 1_555 ? 
72  BC1 13 ARG B 143 ? ARG F 143  . ? 1_555 ? 
73  BC1 13 ZN  N .   ? ZN  F 1157 . ? 1_555 ? 
74  BC1 13 HOH S .   ? HOH F 2229 . ? 1_555 ? 
75  BC1 13 HOH S .   ? HOH F 2231 . ? 1_555 ? 
76  BC1 13 HOH S .   ? HOH F 2248 . ? 1_555 ? 
77  BC1 13 HOH S .   ? HOH F 2249 . ? 1_555 ? 
78  BC1 13 HOH S .   ? HOH F 2250 . ? 1_555 ? 
79  BC1 13 HOH S .   ? HOH F 2251 . ? 1_555 ? 
80  BC2 7  THR B 58  ? THR F 58   . ? 1_555 ? 
81  BC2 7  SER B 142 ? SER F 142  . ? 1_555 ? 
82  BC2 7  ARG B 143 ? ARG F 143  . ? 1_555 ? 
83  BC2 7  ZN  Q .   ? ZN  F 1160 . ? 1_555 ? 
84  BC2 7  HOH S .   ? HOH F 2252 . ? 1_555 ? 
85  BC2 7  HOH S .   ? HOH F 2253 . ? 1_555 ? 
86  BC2 7  HOH S .   ? HOH F 2255 . ? 1_555 ? 
87  BC3 5  HIS B 46  ? HIS F 46   . ? 1_555 ? 
88  BC3 5  HIS B 48  ? HIS F 48   . ? 1_555 ? 
89  BC3 5  HIS B 63  ? HIS F 63   . ? 1_555 ? 
90  BC3 5  HIS B 120 ? HIS F 120  . ? 1_555 ? 
91  BC3 5  SO4 L .   ? SO4 F 1154 . ? 1_555 ? 
92  BC4 4  HIS B 63  ? HIS F 63   . ? 1_555 ? 
93  BC4 4  HIS B 71  ? HIS F 71   . ? 1_555 ? 
94  BC4 4  HIS B 80  ? HIS F 80   . ? 1_555 ? 
95  BC4 4  ASP B 83  ? ASP F 83   . ? 1_555 ? 
96  BC5 7  PRO B 74  ? PRO F 74   . ? 1_555 ? 
97  BC5 7  GLY B 85  ? GLY F 85   . ? 1_555 ? 
98  BC5 7  ASN B 86  ? ASN F 86   . ? 1_555 ? 
99  BC5 7  LEU B 126 ? LEU F 126  . ? 1_555 ? 
100 BC5 7  HOH S .   ? HOH F 2257 . ? 1_555 ? 
101 BC5 7  HOH S .   ? HOH F 2258 . ? 1_555 ? 
102 BC5 7  HOH S .   ? HOH F 2259 . ? 1_555 ? 
103 BC6 5  SER B 142 ? SER F 142  . ? 1_555 ? 
104 BC6 5  ARG B 143 ? ARG F 143  . ? 1_555 ? 
105 BC6 5  LEU B 144 ? LEU F 144  . ? 1_555 ? 
106 BC6 5  SO4 M .   ? SO4 F 1155 . ? 1_555 ? 
107 BC6 5  HOH S .   ? HOH F 2260 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2C9S 
_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                    2C9S 
_atom_sites.fract_transf_matrix[1][1]   0.026149 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007716 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014762 
_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]   0.020340 
_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   A ALA A 1 1   ? 28.552 5.269   30.446  0.50  17.46 ? 1    ALA A N   1 
ATOM   2    N  N   B ALA A 1 1   ? 29.078 3.644   23.058  0.50  16.47 ? 1    ALA A N   1 
ATOM   3    C  CA  A ALA A 1 1   ? 27.111 4.902   30.292  0.50  16.82 ? 1    ALA A CA  1 
ATOM   4    C  CA  B ALA A 1 1   ? 27.644 3.730   23.523  0.50  14.82 ? 1    ALA A CA  1 
ATOM   5    C  C   A ALA A 1 1   ? 26.754 4.923   28.820  0.50  16.15 ? 1    ALA A C   1 
ATOM   6    C  C   B ALA A 1 1   ? 27.316 3.248   24.958  0.50  14.61 ? 1    ALA A C   1 
ATOM   7    O  O   A ALA A 1 1   ? 26.852 5.961   28.179  0.50  17.34 ? 1    ALA A O   1 
ATOM   8    O  O   B ALA A 1 1   ? 27.732 2.172   25.366  0.50  15.84 ? 1    ALA A O   1 
ATOM   9    C  CB  A ALA A 1 1   ? 26.232 5.873   31.056  0.50  17.98 ? 1    ALA A CB  1 
ATOM   10   C  CB  B ALA A 1 1   ? 26.734 2.992   22.546  0.50  14.85 ? 1    ALA A CB  1 
ATOM   11   N  N   A THR A 1 2   ? 26.371 3.759   28.283  0.50  13.89 ? 2    THR A N   1 
ATOM   12   N  N   B THR A 1 2   ? 26.439 3.981   25.642  0.50  14.76 ? 2    THR A N   1 
ATOM   13   C  CA  A THR A 1 2   ? 25.947 3.614   26.870  0.50  13.23 ? 2    THR A CA  1 
ATOM   14   C  CA  B THR A 1 2   ? 25.926 3.538   26.931  0.50  13.18 ? 2    THR A CA  1 
ATOM   15   C  C   A THR A 1 2   ? 24.519 3.088   26.862  0.50  11.34 ? 2    THR A C   1 
ATOM   16   C  C   B THR A 1 2   ? 24.443 3.181   26.955  0.50  11.26 ? 2    THR A C   1 
ATOM   17   O  O   A THR A 1 2   ? 24.203 2.199   27.673  0.50  10.88 ? 2    THR A O   1 
ATOM   18   O  O   B THR A 1 2   ? 23.993 2.518   27.902  0.50  10.20 ? 2    THR A O   1 
ATOM   19   C  CB  A THR A 1 2   ? 26.837 2.553   26.119  0.50  14.30 ? 2    THR A CB  1 
ATOM   20   C  CB  B THR A 1 2   ? 26.230 4.555   28.049  0.50  15.18 ? 2    THR A CB  1 
ATOM   21   O  OG1 A THR A 1 2   ? 28.224 2.822   26.344  0.50  18.09 ? 2    THR A OG1 1 
ATOM   22   O  OG1 B THR A 1 2   ? 25.403 5.721   27.915  0.50  17.69 ? 2    THR A OG1 1 
ATOM   23   C  CG2 A THR A 1 2   ? 26.587 2.484   24.621  0.50  14.84 ? 2    THR A CG2 1 
ATOM   24   C  CG2 B THR A 1 2   ? 27.684 4.967   27.999  0.50  16.36 ? 2    THR A CG2 1 
ATOM   25   N  N   . LYS A 1 3   ? 23.675 3.586   25.939  1.00  10.35 ? 3    LYS A N   1 
ATOM   26   C  CA  . LYS A 1 3   ? 22.291 3.218   25.844  1.00  9.52  ? 3    LYS A CA  1 
ATOM   27   C  C   . LYS A 1 3   ? 21.970 2.881   24.405  1.00  8.50  ? 3    LYS A C   1 
ATOM   28   O  O   . LYS A 1 3   ? 22.540 3.453   23.452  1.00  9.53  ? 3    LYS A O   1 
ATOM   29   C  CB  . LYS A 1 3   ? 21.357 4.333   26.368  1.00  9.72  ? 3    LYS A CB  1 
ATOM   30   C  CG  . LYS A 1 3   ? 21.533 4.555   27.819  1.00  13.52 ? 3    LYS A CG  1 
ATOM   31   C  CD  . LYS A 1 3   ? 20.704 5.748   28.271  1.00  13.94 ? 3    LYS A CD  1 
ATOM   32   C  CE  . LYS A 1 3   ? 20.860 5.994   29.777  1.00  16.97 ? 3    LYS A CE  1 
ATOM   33   N  NZ  . LYS A 1 3   ? 19.716 6.790   30.270  1.00  22.78 ? 3    LYS A NZ  1 
ATOM   34   N  N   . ALA A 1 4   ? 21.000 1.998   24.242  1.00  7.40  ? 4    ALA A N   1 
ATOM   35   C  CA  . ALA A 1 4   ? 20.498 1.614   22.904  1.00  7.20  ? 4    ALA A CA  1 
ATOM   36   C  C   . ALA A 1 4   ? 19.027 1.389   22.977  1.00  7.27  ? 4    ALA A C   1 
ATOM   37   O  O   . ALA A 1 4   ? 18.473 1.265   24.132  1.00  7.83  ? 4    ALA A O   1 
ATOM   38   C  CB  . ALA A 1 4   ? 21.241 0.403   22.407  1.00  8.13  ? 4    ALA A CB  1 
ATOM   39   N  N   . VAL A 1 5   ? 18.332 1.302   21.854  1.00  7.55  ? 5    VAL A N   1 
ATOM   40   C  CA  . VAL A 1 5   ? 16.922 1.154   21.787  1.00  7.88  ? 5    VAL A CA  1 
ATOM   41   C  C   . VAL A 1 5   ? 16.530 0.384   20.557  1.00  8.21  ? 5    VAL A C   1 
ATOM   42   O  O   . VAL A 1 5   ? 17.241 0.416   19.527  1.00  8.63  ? 5    VAL A O   1 
ATOM   43   C  CB  . VAL A 1 5   ? 16.236 2.533   21.918  1.00  8.73  ? 5    VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 5   ? 16.535 3.362   20.638  1.00  10.28 ? 5    VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 5   ? 14.759 2.388   22.249  1.00  9.48  ? 5    VAL A CG2 1 
ATOM   46   N  N   . CYS A 1 6   ? 15.391 -0.260  20.611  1.00  7.92  ? 6    CYS A N   1 
ATOM   47   C  CA  . CYS A 1 6   ? 14.901 -1.042  19.484  1.00  7.83  ? 6    CYS A CA  1 
ATOM   48   C  C   . CYS A 1 6   ? 13.399 -1.018  19.434  1.00  7.64  ? 6    CYS A C   1 
ATOM   49   O  O   . CYS A 1 6   ? 12.764 -1.290  20.463  1.00  9.29  ? 6    CYS A O   1 
ATOM   50   C  CB  . CYS A 1 6   ? 15.361 -2.476  19.652  1.00  7.95  ? 6    CYS A CB  1 
ATOM   51   S  SG  . CYS A 1 6   ? 14.954 -3.491  18.182  1.00  9.70  ? 6    CYS A SG  1 
ATOM   52   N  N   . VAL A 1 7   ? 12.815 -0.643  18.288  1.00  8.14  ? 7    VAL A N   1 
ATOM   53   C  CA  . VAL A 1 7   ? 11.382 -0.761  18.030  1.00  8.73  ? 7    VAL A CA  1 
ATOM   54   C  C   . VAL A 1 7   ? 11.099 -2.051  17.328  1.00  8.66  ? 7    VAL A C   1 
ATOM   55   O  O   . VAL A 1 7   ? 11.625 -2.261  16.217  1.00  9.83  ? 7    VAL A O   1 
ATOM   56   C  CB  . VAL A 1 7   ? 10.869 0.399   17.194  1.00  10.85 ? 7    VAL A CB  1 
ATOM   57   C  CG1 . VAL A 1 7   ? 9.363  0.248   16.889  1.00  12.23 ? 7    VAL A CG1 1 
ATOM   58   C  CG2 . VAL A 1 7   ? 11.159 1.669   17.861  1.00  12.01 ? 7    VAL A CG2 1 
ATOM   59   N  N   . LEU A 1 8   ? 10.273 -2.907  17.899  1.00  8.72  ? 8    LEU A N   1 
ATOM   60   C  CA  . LEU A 1 8   ? 9.918  -4.174  17.312  1.00  8.62  ? 8    LEU A CA  1 
ATOM   61   C  C   . LEU A 1 8   ? 8.600  -4.026  16.591  1.00  8.62  ? 8    LEU A C   1 
ATOM   62   O  O   . LEU A 1 8   ? 7.616  -3.622  17.146  1.00  11.18 ? 8    LEU A O   1 
ATOM   63   C  CB  . LEU A 1 8   ? 9.768  -5.208  18.393  1.00  9.51  ? 8    LEU A CB  1 
ATOM   64   C  CG  . LEU A 1 8   ? 11.011 -5.619  19.208  1.00  10.70 ? 8    LEU A CG  1 
ATOM   65   C  CD1 . LEU A 1 8   ? 10.613 -6.479  20.499  1.00  11.57 ? 8    LEU A CD1 1 
ATOM   66   C  CD2 . LEU A 1 8   ? 11.985 -6.260  18.327  1.00  14.06 ? 8    LEU A CD2 1 
ATOM   67   N  N   . LYS A 1 9   ? 8.603  -4.382  15.314  1.00  9.20  ? 9    LYS A N   1 
ATOM   68   C  CA  . LYS A 1 9   ? 7.446  -4.374  14.384  1.00  11.78 ? 9    LYS A CA  1 
ATOM   69   C  C   . LYS A 1 9   ? 7.474  -5.592  13.500  1.00  11.06 ? 9    LYS A C   1 
ATOM   70   O  O   . LYS A 1 9   ? 8.532  -6.118  13.241  1.00  10.88 ? 9    LYS A O   1 
ATOM   71   C  CB  . LYS A 1 9   ? 7.489  -3.118  13.497  1.00  13.33 ? 9    LYS A CB  1 
ATOM   72   C  CG  . LYS A 1 9   ? 7.357  -1.826  14.323  0.50  13.27 ? 9    LYS A CG  1 
ATOM   73   C  CD  . LYS A 1 9   ? 7.114  -0.589  13.499  0.50  14.51 ? 9    LYS A CD  1 
ATOM   74   C  CE  . LYS A 1 9   ? 6.664  0.584   14.349  0.50  14.90 ? 9    LYS A CE  1 
ATOM   75   N  NZ  . LYS A 1 9   ? 5.289  0.363   14.860  0.50  17.47 ? 9    LYS A NZ  1 
ATOM   76   N  N   . GLY A 1 10  ? 6.303  -6.044  13.065  1.00  12.83 ? 10   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 10  ? 6.216  -7.133  12.093  1.00  14.74 ? 10   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 10  ? 5.009  -7.043  11.194  1.00  16.05 ? 10   GLY A C   1 
ATOM   79   O  O   . GLY A 1 10  ? 4.455  -5.977  10.972  1.00  18.27 ? 10   GLY A O   1 
ATOM   80   N  N   . ASP A 1 11  ? 4.604  -8.192  10.684  1.00  16.71 ? 11   ASP A N   1 
ATOM   81   C  CA  . ASP A 1 11  ? 3.517  -8.249  9.715   1.00  17.97 ? 11   ASP A CA  1 
ATOM   82   C  C   . ASP A 1 11  ? 2.179  -8.375  10.382  1.00  18.79 ? 11   ASP A C   1 
ATOM   83   O  O   . ASP A 1 11  ? 1.146  -8.224  9.759   1.00  20.95 ? 11   ASP A O   1 
ATOM   84   C  CB  . ASP A 1 11  ? 3.691  -9.424  8.768   1.00  18.97 ? 11   ASP A CB  1 
ATOM   85   C  CG  . ASP A 1 11  ? 4.876  -9.247  7.833   1.00  23.65 ? 11   ASP A CG  1 
ATOM   86   O  OD1 . ASP A 1 11  ? 5.181  -8.098  7.474   1.00  29.00 ? 11   ASP A OD1 1 
ATOM   87   O  OD2 . ASP A 1 11  ? 5.519  -10.261 7.490   1.00  29.86 ? 11   ASP A OD2 1 
ATOM   88   N  N   . GLY A 1 12  ? 2.195  -8.656  11.676  1.00  17.29 ? 12   GLY A N   1 
ATOM   89   C  CA  . GLY A 1 12  ? 0.989  -8.971  12.429  1.00  16.91 ? 12   GLY A CA  1 
ATOM   90   C  C   . GLY A 1 12  ? 0.846  -8.024  13.613  1.00  16.09 ? 12   GLY A C   1 
ATOM   91   O  O   . GLY A 1 12  ? 1.289  -6.878  13.546  1.00  17.68 ? 12   GLY A O   1 
ATOM   92   N  N   . PRO A 1 13  ? 0.232  -8.499  14.722  1.00  16.94 ? 13   PRO A N   1 
ATOM   93   C  CA  . PRO A 1 13  ? -0.139 -7.643  15.817  1.00  16.00 ? 13   PRO A CA  1 
ATOM   94   C  C   . PRO A 1 13  ? 0.985  -7.348  16.771  1.00  14.35 ? 13   PRO A C   1 
ATOM   95   O  O   . PRO A 1 13  ? 0.814  -6.510  17.687  1.00  16.48 ? 13   PRO A O   1 
ATOM   96   C  CB  . PRO A 1 13  ? -1.256 -8.451  16.470  1.00  17.94 ? 13   PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 13  ? -0.827 -9.836  16.317  1.00  16.18 ? 13   PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 13  ? -0.246 -9.873  14.934  1.00  17.22 ? 13   PRO A CD  1 
ATOM   99   N  N   . VAL A 1 14  ? 2.120  -8.007  16.619  1.00  13.23 ? 14   VAL A N   1 
ATOM   100  C  CA  . VAL A 1 14  ? 3.185  -7.895  17.628  1.00  11.46 ? 14   VAL A CA  1 
ATOM   101  C  C   . VAL A 1 14  ? 4.019  -6.641  17.491  1.00  11.72 ? 14   VAL A C   1 
ATOM   102  O  O   . VAL A 1 14  ? 4.515  -6.342  16.419  1.00  13.29 ? 14   VAL A O   1 
ATOM   103  C  CB  . VAL A 1 14  ? 4.090  -9.140  17.660  1.00  11.38 ? 14   VAL A CB  1 
ATOM   104  C  CG1 . VAL A 1 14  ? 5.158  -9.011  18.693  1.00  10.96 ? 14   VAL A CG1 1 
ATOM   105  C  CG2 . VAL A 1 14  ? 3.279  -10.410 17.958  1.00  11.40 ? 14   VAL A CG2 1 
ATOM   106  N  N   . GLN A 1 15  ? 4.128  -5.873  18.564  1.00  11.66 ? 15   GLN A N   1 
ATOM   107  C  CA  . GLN A 1 15  ? 4.928  -4.686  18.552  1.00  12.85 ? 15   GLN A CA  1 
ATOM   108  C  C   . GLN A 1 15  ? 5.434  -4.388  19.930  1.00  10.65 ? 15   GLN A C   1 
ATOM   109  O  O   . GLN A 1 15  ? 4.826  -4.734  20.955  1.00  11.36 ? 15   GLN A O   1 
ATOM   110  C  CB  . GLN A 1 15  ? 4.169  -3.489  18.035  1.00  15.64 ? 15   GLN A CB  1 
ATOM   111  C  CG  . GLN A 1 15  ? 2.980  -3.145  18.808  1.00  16.33 ? 15   GLN A CG  1 
ATOM   112  C  CD  . GLN A 1 15  ? 2.337  -1.806  18.375  0.70  17.12 ? 15   GLN A CD  1 
ATOM   113  O  OE1 . GLN A 1 15  ? 2.679  -0.749  18.905  0.50  21.31 ? 15   GLN A OE1 1 
ATOM   114  N  NE2 . GLN A 1 15  ? 1.453  -1.857  17.387  0.50  20.37 ? 15   GLN A NE2 1 
ATOM   115  N  N   . GLY A 1 16  ? 6.573  -3.730  19.968  1.00  10.59 ? 16   GLY A N   1 
ATOM   116  C  CA  . GLY A 1 16  ? 7.173  -3.420  21.237  1.00  9.50  ? 16   GLY A CA  1 
ATOM   117  C  C   . GLY A 1 16  ? 8.301  -2.451  21.206  1.00  8.96  ? 16   GLY A C   1 
ATOM   118  O  O   . GLY A 1 16  ? 8.708  -1.998  20.128  1.00  9.33  ? 16   GLY A O   1 
ATOM   119  N  N   . ILE A 1 17  ? 8.795  -2.096  22.370  1.00  9.01  ? 17   ILE A N   1 
ATOM   120  C  CA  . ILE A 1 17  ? 9.902  -1.188  22.522  1.00  9.29  ? 17   ILE A CA  1 
ATOM   121  C  C   . ILE A 1 17  ? 10.824 -1.755  23.604  1.00  9.15  ? 17   ILE A C   1 
ATOM   122  O  O   . ILE A 1 17  ? 10.375 -2.110  24.751  1.00  9.34  ? 17   ILE A O   1 
ATOM   123  C  CB  . ILE A 1 17  ? 9.461  0.241   22.958  1.00  11.39 ? 17   ILE A CB  1 
ATOM   124  C  CG1 . ILE A 1 17  ? 8.421  0.859   22.048  1.00  16.74 ? 17   ILE A CG1 1 
ATOM   125  C  CG2 . ILE A 1 17  ? 10.613 1.113   23.282  1.00  12.52 ? 17   ILE A CG2 1 
ATOM   126  C  CD1 . ILE A 1 17  ? 8.962  1.539   20.861  1.00  18.73 ? 17   ILE A CD1 1 
ATOM   127  N  N   . ILE A 1 18  ? 12.100 -1.902  23.299  1.00  8.09  ? 18   ILE A N   1 
ATOM   128  C  CA  . ILE A 1 18  ? 13.132 -2.441  24.149  1.00  7.84  ? 18   ILE A CA  1 
ATOM   129  C  C   . ILE A 1 18  ? 14.310 -1.531  24.283  1.00  7.93  ? 18   ILE A C   1 
ATOM   130  O  O   . ILE A 1 18  ? 14.836 -0.997  23.306  1.00  9.25  ? 18   ILE A O   1 
ATOM   131  C  CB  . ILE A 1 18  ? 13.558 -3.852  23.652  1.00  8.20  ? 18   ILE A CB  1 
ATOM   132  C  CG1 . ILE A 1 18  ? 12.348 -4.817  23.563  1.00  10.37 ? 18   ILE A CG1 1 
ATOM   133  C  CG2 . ILE A 1 18  ? 14.715 -4.396  24.491  1.00  8.83  ? 18   ILE A CG2 1 
ATOM   134  C  CD1 . ILE A 1 18  ? 11.725 -5.239  24.851  1.00  11.29 ? 18   ILE A CD1 1 
ATOM   135  N  N   . ASN A 1 19  ? 14.697 -1.258  25.531  1.00  7.77  ? 19   ASN A N   1 
ATOM   136  C  CA  . ASN A 1 19  ? 15.762 -0.390  25.895  1.00  7.60  ? 19   ASN A CA  1 
ATOM   137  C  C   . ASN A 1 19  ? 16.951 -1.187  26.419  1.00  6.76  ? 19   ASN A C   1 
ATOM   138  O  O   . ASN A 1 19  ? 16.754 -2.218  27.064  1.00  8.01  ? 19   ASN A O   1 
ATOM   139  C  CB  . ASN A 1 19  ? 15.278 0.596   27.017  1.00  8.41  ? 19   ASN A CB  1 
ATOM   140  C  CG  . ASN A 1 19  ? 14.030 1.332   26.635  1.00  10.25 ? 19   ASN A CG  1 
ATOM   141  O  OD1 . ASN A 1 19  ? 12.893 0.996   27.015  1.00  13.51 ? 19   ASN A OD1 1 
ATOM   142  N  ND2 . ASN A 1 19  ? 14.231 2.339   25.891  1.00  10.92 ? 19   ASN A ND2 1 
ATOM   143  N  N   . PHE A 1 20  ? 18.181 -0.735  26.194  1.00  7.64  ? 20   PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 19.391 -1.333  26.653  1.00  7.64  ? 20   PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 20.226 -0.276  27.336  1.00  8.14  ? 20   PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 20.357 0.855   26.828  1.00  8.85  ? 20   PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 20.233 -1.879  25.499  1.00  7.50  ? 20   PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 19.509 -2.900  24.619  1.00  8.24  ? 20   PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 18.611 -2.517  23.599  1.00  9.99  ? 20   PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 19.738 -4.233  24.802  1.00  9.23  ? 20   PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 17.940 -3.459  22.817  1.00  9.00  ? 20   PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 19.090 -5.161  24.023  1.00  9.52  ? 20   PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 18.200 -4.790  23.034  1.00  10.17 ? 20   PHE A CZ  1 
ATOM   154  N  N   . GLU A 1 21  ? 20.815 -0.652  28.464  1.00  8.38  ? 21   GLU A N   1 
ATOM   155  C  CA  . GLU A 1 21  ? 21.653 0.284   29.191  1.00  9.83  ? 21   GLU A CA  1 
ATOM   156  C  C   . GLU A 1 21  ? 22.902 -0.450  29.721  1.00  9.32  ? 21   GLU A C   1 
ATOM   157  O  O   . GLU A 1 21  ? 22.795 -1.500  30.289  1.00  9.65  ? 21   GLU A O   1 
ATOM   158  C  CB  . GLU A 1 21  ? 20.899 1.016   30.321  1.00  11.23 ? 21   GLU A CB  1 
ATOM   159  C  CG  . GLU A 1 21  ? 21.798 2.104   30.904  1.00  14.54 ? 21   GLU A CG  1 
ATOM   160  C  CD  . GLU A 1 21  ? 21.145 2.903   32.020  0.60  15.17 ? 21   GLU A CD  1 
ATOM   161  O  OE1 . GLU A 1 21  ? 19.901 2.943   32.057  0.60  19.26 ? 21   GLU A OE1 1 
ATOM   162  O  OE2 . GLU A 1 21  ? 21.889 3.472   32.847  0.60  23.25 ? 21   GLU A OE2 1 
ATOM   163  N  N   . GLN A 1 22  ? 24.090 0.068   29.495  1.00  9.63  ? 22   GLN A N   1 
ATOM   164  C  CA  . GLN A 1 22  ? 25.350 -0.516  29.959  1.00  11.24 ? 22   GLN A CA  1 
ATOM   165  C  C   . GLN A 1 22  ? 26.128 0.588   30.674  1.00  12.92 ? 22   GLN A C   1 
ATOM   166  O  O   . GLN A 1 22  ? 26.652 1.494   30.044  1.00  14.08 ? 22   GLN A O   1 
ATOM   167  C  CB  . GLN A 1 22  ? 26.152 -1.084  28.769  1.00  11.92 ? 22   GLN A CB  1 
ATOM   168  C  CG  . GLN A 1 22  ? 27.354 -1.880  29.208  1.00  10.94 ? 22   GLN A CG  1 
ATOM   169  C  CD  . GLN A 1 22  ? 28.076 -2.474  28.013  1.00  11.45 ? 22   GLN A CD  1 
ATOM   170  O  OE1 . GLN A 1 22  ? 28.014 -1.937  26.916  1.00  12.59 ? 22   GLN A OE1 1 
ATOM   171  N  NE2 . GLN A 1 22  ? 28.674 -3.604  28.185  1.00  11.95 ? 22   GLN A NE2 1 
ATOM   172  N  N   . LYS A 1 23  ? 26.213 0.465   31.985  1.00  14.67 ? 23   LYS A N   1 
ATOM   173  C  CA  . LYS A 1 23  ? 26.837 1.490   32.847  1.00  16.83 ? 23   LYS A CA  1 
ATOM   174  C  C   . LYS A 1 23  ? 28.329 1.548   32.640  1.00  17.71 ? 23   LYS A C   1 
ATOM   175  O  O   . LYS A 1 23  ? 28.904 2.633   32.655  1.00  20.52 ? 23   LYS A O   1 
ATOM   176  C  CB  . LYS A 1 23  ? 26.534 1.195   34.322  1.00  18.49 ? 23   LYS A CB  1 
ATOM   177  C  CG  . LYS A 1 23  ? 25.129 1.469   34.735  1.00  19.18 ? 23   LYS A CG  1 
ATOM   178  C  CD  . LYS A 1 23  ? 24.845 1.145   36.224  1.00  20.48 ? 23   LYS A CD  1 
ATOM   179  C  CE  . LYS A 1 23  ? 23.533 1.726   36.732  0.30  20.94 ? 23   LYS A CE  1 
ATOM   180  N  NZ  . LYS A 1 23  ? 23.564 3.216   36.794  0.30  18.69 ? 23   LYS A NZ  1 
ATOM   181  N  N   . GLU A 1 24  ? 28.979 0.417   32.458  1.00  19.86 ? 24   GLU A N   1 
ATOM   182  C  CA  . GLU A 1 24  ? 30.415 0.387   32.301  1.00  20.96 ? 24   GLU A CA  1 
ATOM   183  C  C   . GLU A 1 24  ? 30.833 -0.396  31.061  1.00  20.95 ? 24   GLU A C   1 
ATOM   184  O  O   . GLU A 1 24  ? 30.172 -1.358  30.688  1.00  20.50 ? 24   GLU A O   1 
ATOM   185  C  CB  . GLU A 1 24  ? 31.114 -0.137  33.582  1.00  21.73 ? 24   GLU A CB  1 
ATOM   186  C  CG  . GLU A 1 24  ? 30.310 -1.038  34.488  1.00  24.57 ? 24   GLU A CG  1 
ATOM   187  C  CD  . GLU A 1 24  ? 31.031 -1.403  35.788  0.50  23.50 ? 24   GLU A CD  1 
ATOM   188  O  OE1 . GLU A 1 24  ? 31.671 -0.530  36.399  0.50  25.43 ? 24   GLU A OE1 1 
ATOM   189  O  OE2 . GLU A 1 24  ? 30.951 -2.583  36.191  0.50  27.60 ? 24   GLU A OE2 1 
ATOM   190  N  N   A SER A 1 25  ? 31.975 -0.009  30.489  0.50  20.97 ? 25   SER A N   1 
ATOM   191  N  N   B SER A 1 25  ? 31.916 0.029   30.411  0.50  21.25 ? 25   SER A N   1 
ATOM   192  C  CA  A SER A 1 25  ? 32.401 -0.394  29.135  0.50  20.80 ? 25   SER A CA  1 
ATOM   193  C  CA  B SER A 1 25  ? 32.423 -0.737  29.288  0.50  21.29 ? 25   SER A CA  1 
ATOM   194  C  C   A SER A 1 25  ? 32.422 -1.896  28.774  0.50  20.81 ? 25   SER A C   1 
ATOM   195  C  C   B SER A 1 25  ? 32.727 -2.125  29.827  0.50  21.09 ? 25   SER A C   1 
ATOM   196  O  O   A SER A 1 25  ? 32.222 -2.263  27.594  0.50  22.14 ? 25   SER A O   1 
ATOM   197  O  O   B SER A 1 25  ? 33.252 -2.282  30.931  0.50  21.69 ? 25   SER A O   1 
ATOM   198  C  CB  A SER A 1 25  ? 33.778 0.227   28.857  0.50  21.10 ? 25   SER A CB  1 
ATOM   199  C  CB  B SER A 1 25  ? 33.671 -0.111  28.653  0.50  21.97 ? 25   SER A CB  1 
ATOM   200  O  OG  A SER A 1 25  ? 33.659 1.640   28.809  0.50  21.52 ? 25   SER A OG  1 
ATOM   201  O  OG  B SER A 1 25  ? 34.836 -0.410  29.384  0.50  23.09 ? 25   SER A OG  1 
ATOM   202  N  N   A ASN A 1 26  ? 32.668 -2.751  29.768  0.50  20.22 ? 26   ASN A N   1 
ATOM   203  N  N   B ASN A 1 26  ? 32.339 -3.145  29.081  0.50  20.45 ? 26   ASN A N   1 
ATOM   204  C  CA  A ASN A 1 26  ? 32.534 -4.202  29.592  0.50  19.38 ? 26   ASN A CA  1 
ATOM   205  C  CA  B ASN A 1 26  ? 32.518 -4.498  29.599  0.50  20.06 ? 26   ASN A CA  1 
ATOM   206  C  C   A ASN A 1 26  ? 31.678 -4.850  30.695  0.50  18.62 ? 26   ASN A C   1 
ATOM   207  C  C   B ASN A 1 26  ? 31.378 -4.981  30.488  0.50  19.43 ? 26   ASN A C   1 
ATOM   208  O  O   A ASN A 1 26  ? 31.881 -6.029  31.050  0.50  18.03 ? 26   ASN A O   1 
ATOM   209  O  O   B ASN A 1 26  ? 31.095 -6.193  30.508  0.50  20.89 ? 26   ASN A O   1 
ATOM   210  C  CB  A ASN A 1 26  ? 33.914 -4.866  29.538  0.50  19.58 ? 26   ASN A CB  1 
ATOM   211  C  CB  B ASN A 1 26  ? 33.813 -4.571  30.425  0.50  20.41 ? 26   ASN A CB  1 
ATOM   212  C  CG  A ASN A 1 26  ? 34.693 -4.513  28.291  0.50  19.01 ? 26   ASN A CG  1 
ATOM   213  C  CG  B ASN A 1 26  ? 33.563 -4.758  31.931  0.50  21.47 ? 26   ASN A CG  1 
ATOM   214  O  OD1 A ASN A 1 26  ? 35.687 -3.797  28.353  0.50  18.82 ? 26   ASN A OD1 1 
ATOM   215  O  OD1 B ASN A 1 26  ? 34.046 -3.991  32.766  0.50  22.96 ? 26   ASN A OD1 1 
ATOM   216  N  ND2 A ASN A 1 26  ? 34.249 -5.011  27.156  0.50  18.70 ? 26   ASN A ND2 1 
ATOM   217  N  ND2 B ASN A 1 26  ? 32.802 -5.790  32.276  0.50  24.92 ? 26   ASN A ND2 1 
ATOM   218  N  N   . GLY A 1 27  ? 30.739 -4.068  31.223  1.00  18.42 ? 27   GLY A N   1 
ATOM   219  C  CA  . GLY A 1 27  ? 29.835 -4.475  32.290  1.00  16.77 ? 27   GLY A CA  1 
ATOM   220  C  C   . GLY A 1 27  ? 28.527 -5.048  31.777  1.00  14.62 ? 27   GLY A C   1 
ATOM   221  O  O   . GLY A 1 27  ? 28.280 -5.103  30.587  1.00  13.23 ? 27   GLY A O   1 
ATOM   222  N  N   . PRO A 1 28  ? 27.656 -5.471  32.680  1.00  13.01 ? 28   PRO A N   1 
ATOM   223  C  CA  . PRO A 1 28  ? 26.386 -6.043  32.296  1.00  12.26 ? 28   PRO A CA  1 
ATOM   224  C  C   . PRO A 1 28  ? 25.457 -5.030  31.607  1.00  10.31 ? 28   PRO A C   1 
ATOM   225  O  O   . PRO A 1 28  ? 25.562 -3.816  31.854  1.00  11.91 ? 28   PRO A O   1 
ATOM   226  C  CB  . PRO A 1 28  ? 25.803 -6.614  33.602  1.00  14.41 ? 28   PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 28  ? 26.639 -6.108  34.609  1.00  16.14 ? 28   PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 28  ? 27.841 -5.461  34.129  1.00  14.71 ? 28   PRO A CD  1 
ATOM   229  N  N   . VAL A 1 29  ? 24.615 -5.539  30.708  1.00  8.58  ? 29   VAL A N   1 
ATOM   230  C  CA  . VAL A 1 29  ? 23.623 -4.759  30.022  1.00  9.68  ? 29   VAL A CA  1 
ATOM   231  C  C   . VAL A 1 29  ? 22.209 -5.058  30.572  1.00  9.07  ? 29   VAL A C   1 
ATOM   232  O  O   . VAL A 1 29  ? 21.784 -6.217  30.640  1.00  10.29 ? 29   VAL A O   1 
ATOM   233  C  CB  . VAL A 1 29  ? 23.663 -5.073  28.516  1.00  8.79  ? 29   VAL A CB  1 
ATOM   234  C  CG1 . VAL A 1 29  ? 22.684 -4.180  27.775  1.00  8.90  ? 29   VAL A CG1 1 
ATOM   235  C  CG2 . VAL A 1 29  ? 25.055 -4.868  27.991  1.00  9.80  ? 29   VAL A CG2 1 
ATOM   236  N  N   . LYS A 1 30  ? 21.510 -4.010  31.000  1.00  8.61  ? 30   LYS A N   1 
ATOM   237  C  CA  . LYS A 1 30  ? 20.127 -4.066  31.390  1.00  9.12  ? 30   LYS A CA  1 
ATOM   238  C  C   . LYS A 1 30  ? 19.248 -3.913  30.154  1.00  8.29  ? 30   LYS A C   1 
ATOM   239  O  O   . LYS A 1 30  ? 19.493 -3.035  29.343  1.00  10.19 ? 30   LYS A O   1 
ATOM   240  C  CB  . LYS A 1 30  ? 19.816 -2.990  32.437  1.00  10.00 ? 30   LYS A CB  1 
ATOM   241  C  CG  . LYS A 1 30  ? 18.387 -2.855  32.855  1.00  14.31 ? 30   LYS A CG  1 
ATOM   242  C  CD  . LYS A 1 30  ? 18.231 -1.734  33.806  1.00  15.73 ? 30   LYS A CD  1 
ATOM   243  C  CE  . LYS A 1 30  ? 16.841 -1.623  34.345  1.00  18.60 ? 30   LYS A CE  1 
ATOM   244  N  NZ  . LYS A 1 30  ? 16.864 -0.559  35.398  1.00  24.02 ? 30   LYS A NZ  1 
ATOM   245  N  N   . VAL A 1 31  ? 18.287 -4.793  30.039  1.00  8.74  ? 31   VAL A N   1 
ATOM   246  C  CA  . VAL A 1 31  ? 17.347 -4.848  28.934  1.00  8.89  ? 31   VAL A CA  1 
ATOM   247  C  C   . VAL A 1 31  ? 15.928 -4.703  29.475  1.00  8.69  ? 31   VAL A C   1 
ATOM   248  O  O   . VAL A 1 31  ? 15.558 -5.514  30.330  1.00  11.71 ? 31   VAL A O   1 
ATOM   249  C  CB  . VAL A 1 31  ? 17.519 -6.154  28.134  1.00  9.45  ? 31   VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 31  ? 16.606 -6.124  26.917  1.00  10.62 ? 31   VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 31  ? 18.974 -6.389  27.740  1.00  10.20 ? 31   VAL A CG2 1 
ATOM   252  N  N   . TRP A 1 32  ? 15.169 -3.695  29.074  1.00  9.87  ? 32   TRP A N   1 
ATOM   253  C  CA  . TRP A 1 32  ? 13.828 -3.483  29.635  1.00  8.85  ? 32   TRP A CA  1 
ATOM   254  C  C   . TRP A 1 32  ? 12.897 -2.847  28.627  1.00  7.93  ? 32   TRP A C   1 
ATOM   255  O  O   . TRP A 1 32  ? 13.330 -2.073  27.767  1.00  9.08  ? 32   TRP A O   1 
ATOM   256  C  CB  . TRP A 1 32  ? 13.866 -2.619  30.931  1.00  9.76  ? 32   TRP A CB  1 
ATOM   257  C  CG  A TRP A 1 32  ? 14.367 -1.122  30.718  0.70  9.77  ? 32   TRP A CG  1 
ATOM   258  C  CG  B TRP A 1 32  ? 13.994 -1.253  30.757  0.30  8.97  ? 32   TRP A CG  1 
ATOM   259  C  CD1 A TRP A 1 32  ? 15.678 -0.643  30.690  0.70  8.70  ? 32   TRP A CD1 1 
ATOM   260  C  CD1 B TRP A 1 32  ? 13.005 -0.327  30.746  0.30  8.65  ? 32   TRP A CD1 1 
ATOM   261  C  CD2 A TRP A 1 32  ? 13.545 0.021   30.447  0.70  10.61 ? 32   TRP A CD2 1 
ATOM   262  C  CD2 B TRP A 1 32  ? 15.205 -0.576  30.565  0.30  8.11  ? 32   TRP A CD2 1 
ATOM   263  N  NE1 A TRP A 1 32  ? 15.692 0.743   30.519  0.70  10.03 ? 32   TRP A NE1 1 
ATOM   264  N  NE1 B TRP A 1 32  ? 13.544 0.931   30.574  0.30  9.04  ? 32   TRP A NE1 1 
ATOM   265  C  CE2 A TRP A 1 32  ? 14.410 1.170   30.308  0.70  9.19  ? 32   TRP A CE2 1 
ATOM   266  C  CE2 B TRP A 1 32  ? 14.908 0.794   30.464  0.30  8.48  ? 32   TRP A CE2 1 
ATOM   267  C  CE3 A TRP A 1 32  ? 12.162 0.201   30.297  0.70  10.56 ? 32   TRP A CE3 1 
ATOM   268  C  CE3 B TRP A 1 32  ? 16.531 -0.999  30.487  0.30  8.65  ? 32   TRP A CE3 1 
ATOM   269  C  CZ2 A TRP A 1 32  ? 13.909 2.453   30.044  0.70  11.50 ? 32   TRP A CZ2 1 
ATOM   270  C  CZ2 B TRP A 1 32  ? 15.891 1.731   30.256  0.30  9.63  ? 32   TRP A CZ2 1 
ATOM   271  C  CZ3 A TRP A 1 32  ? 11.674 1.484   30.021  0.70  11.26 ? 32   TRP A CZ3 1 
ATOM   272  C  CZ3 B TRP A 1 32  ? 17.507 -0.077  30.294  0.30  9.55  ? 32   TRP A CZ3 1 
ATOM   273  C  CH2 A TRP A 1 32  ? 12.533 2.576   29.891  0.70  10.42 ? 32   TRP A CH2 1 
ATOM   274  C  CH2 B TRP A 1 32  ? 17.189 1.274   30.200  0.30  8.85  ? 32   TRP A CH2 1 
ATOM   275  N  N   . GLY A 1 33  ? 11.636 -3.128  28.747  1.00  7.93  ? 33   GLY A N   1 
ATOM   276  C  CA  . GLY A 1 33  ? 10.617 -2.605  27.899  1.00  7.84  ? 33   GLY A CA  1 
ATOM   277  C  C   . GLY A 1 33  ? 9.371  -3.466  27.909  1.00  8.20  ? 33   GLY A C   1 
ATOM   278  O  O   . GLY A 1 33  ? 9.099  -4.151  28.898  1.00  9.67  ? 33   GLY A O   1 
ATOM   279  N  N   . SER A 1 34  ? 8.595  -3.436  26.844  1.00  9.02  ? 34   SER A N   1 
ATOM   280  C  CA  . SER A 1 34  ? 7.321  -4.127  26.751  1.00  10.01 ? 34   SER A CA  1 
ATOM   281  C  C   . SER A 1 34  ? 7.073  -4.535  25.318  1.00  10.13 ? 34   SER A C   1 
ATOM   282  O  O   . SER A 1 34  ? 7.435  -3.820  24.419  1.00  10.57 ? 34   SER A O   1 
ATOM   283  C  CB  . SER A 1 34  ? 6.147  -3.201  27.206  1.00  11.58 ? 34   SER A CB  1 
ATOM   284  O  OG  A SER A 1 34  ? 5.138  -4.075  27.644  0.65  14.22 ? 34   SER A OG  1 
ATOM   285  O  OG  B SER A 1 34  ? 6.471  -1.974  26.662  0.35  14.40 ? 34   SER A OG  1 
ATOM   286  N  N   . ILE A 1 35  ? 6.425  -5.658  25.146  1.00  9.44  ? 35   ILE A N   1 
ATOM   287  C  CA  . ILE A 1 35  ? 5.998  -6.148  23.874  1.00  9.72  ? 35   ILE A CA  1 
ATOM   288  C  C   . ILE A 1 35  ? 4.523  -6.533  24.000  1.00  9.81  ? 35   ILE A C   1 
ATOM   289  O  O   . ILE A 1 35  ? 4.152  -7.174  24.983  1.00  12.07 ? 35   ILE A O   1 
ATOM   290  C  CB  . ILE A 1 35  ? 6.799  -7.333  23.401  1.00  9.29  ? 35   ILE A CB  1 
ATOM   291  C  CG1 . ILE A 1 35  ? 8.297  -7.036  23.432  1.00  10.78 ? 35   ILE A CG1 1 
ATOM   292  C  CG2 . ILE A 1 35  ? 6.326  -7.752  21.969  1.00  9.47  ? 35   ILE A CG2 1 
ATOM   293  C  CD1 . ILE A 1 35  ? 9.187  -8.256  23.247  1.00  11.51 ? 35   ILE A CD1 1 
ATOM   294  N  N   . LYS A 1 36  ? 3.672  -6.166  23.053  1.00  11.10 ? 36   LYS A N   1 
ATOM   295  C  CA  . LYS A 1 36  ? 2.279  -6.484  23.084  1.00  11.95 ? 36   LYS A CA  1 
ATOM   296  C  C   . LYS A 1 36  ? 1.847  -7.225  21.840  1.00  11.31 ? 36   LYS A C   1 
ATOM   297  O  O   . LYS A 1 36  ? 2.588  -7.275  20.852  1.00  11.67 ? 36   LYS A O   1 
ATOM   298  C  CB  . LYS A 1 36  ? 1.432  -5.227  23.294  1.00  13.40 ? 36   LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 36  ? 1.416  -4.265  22.132  1.00  16.05 ? 36   LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 36  ? 0.617  -3.042  22.498  1.00  17.76 ? 36   LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 36  ? 0.809  -1.947  21.523  1.00  20.57 ? 36   LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 36  ? -0.168 -0.836  21.766  1.00  23.80 ? 36   LYS A NZ  1 
ATOM   303  N  N   . GLY A 1 37  ? 0.645  -7.779  21.880  1.00  11.95 ? 37   GLY A N   1 
ATOM   304  C  CA  . GLY A 1 37  ? 0.068  -8.534  20.789  1.00  11.36 ? 37   GLY A CA  1 
ATOM   305  C  C   . GLY A 1 37  ? 0.494  -9.967  20.690  1.00  10.59 ? 37   GLY A C   1 
ATOM   306  O  O   . GLY A 1 37  ? 0.332  -10.582 19.619  1.00  12.68 ? 37   GLY A O   1 
ATOM   307  N  N   . LEU A 1 38  ? 1.035  -10.512 21.792  1.00  10.30 ? 38   LEU A N   1 
ATOM   308  C  CA  . LEU A 1 38  ? 1.488  -11.869 21.809  1.00  10.91 ? 38   LEU A CA  1 
ATOM   309  C  C   . LEU A 1 38  ? 0.426  -12.854 22.300  1.00  10.38 ? 38   LEU A C   1 
ATOM   310  O  O   . LEU A 1 38  ? -0.441 -12.474 23.071  1.00  12.71 ? 38   LEU A O   1 
ATOM   311  C  CB  . LEU A 1 38  ? 2.734  -11.963 22.699  1.00  10.16 ? 38   LEU A CB  1 
ATOM   312  C  CG  . LEU A 1 38  ? 3.977  -11.244 22.195  1.00  9.47  ? 38   LEU A CG  1 
ATOM   313  C  CD1 . LEU A 1 38  ? 4.933  -10.967 23.299  1.00  11.02 ? 38   LEU A CD1 1 
ATOM   314  C  CD2 . LEU A 1 38  ? 4.647  -12.055 21.081  1.00  10.21 ? 38   LEU A CD2 1 
ATOM   315  N  N   . THR A 1 39  ? 0.635  -14.136 22.028  1.00  10.82 ? 39   THR A N   1 
ATOM   316  C  CA  . THR A 1 39  ? -0.073 -15.233 22.626  1.00  11.02 ? 39   THR A CA  1 
ATOM   317  C  C   . THR A 1 39  ? 0.516  -15.412 24.031  1.00  11.31 ? 39   THR A C   1 
ATOM   318  O  O   . THR A 1 39  ? 1.684  -15.179 24.270  1.00  10.44 ? 39   THR A O   1 
ATOM   319  C  CB  . THR A 1 39  ? 0.051  -16.527 21.837  1.00  11.85 ? 39   THR A CB  1 
ATOM   320  O  OG1 . THR A 1 39  ? 1.424  -16.910 21.725  1.00  12.62 ? 39   THR A OG1 1 
ATOM   321  C  CG2 . THR A 1 39  ? -0.639 -16.392 20.469  1.00  11.99 ? 39   THR A CG2 1 
ATOM   322  N  N   . GLU A 1 40  ? -0.315 -15.858 24.967  1.00  10.82 ? 40   GLU A N   1 
ATOM   323  C  CA  . GLU A 1 40  ? 0.137  -16.071 26.343  1.00  10.40 ? 40   GLU A CA  1 
ATOM   324  C  C   . GLU A 1 40  ? 1.222  -17.156 26.392  1.00  10.16 ? 40   GLU A C   1 
ATOM   325  O  O   . GLU A 1 40  ? 1.082  -18.195 25.722  1.00  12.64 ? 40   GLU A O   1 
ATOM   326  C  CB  . GLU A 1 40  ? -1.063 -16.438 27.205  1.00  10.97 ? 40   GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 40  ? -0.822 -16.199 28.679  1.00  13.43 ? 40   GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 40  ? -0.690 -17.496 29.400  1.00  13.10 ? 40   GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 40  ? -0.090 -18.418 28.767  1.00  14.10 ? 40   GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 40  ? -1.125 -17.608 30.597  1.00  12.14 ? 40   GLU A OE2 1 
ATOM   331  N  N   . GLY A 1 41  ? 2.339  -16.919 27.080  1.00  9.99  ? 41   GLY A N   1 
ATOM   332  C  CA  . GLY A 1 41  ? 3.400  -17.904 27.198  1.00  8.24  ? 41   GLY A CA  1 
ATOM   333  C  C   . GLY A 1 41  ? 4.768  -17.373 26.853  1.00  8.80  ? 41   GLY A C   1 
ATOM   334  O  O   . GLY A 1 41  ? 4.942  -16.195 26.852  1.00  9.58  ? 41   GLY A O   1 
ATOM   335  N  N   . LEU A 1 42  ? 5.703  -18.248 26.538  1.00  8.92  ? 42   LEU A N   1 
ATOM   336  C  CA  . LEU A 1 42  ? 7.089  -17.942 26.256  1.00  8.61  ? 42   LEU A CA  1 
ATOM   337  C  C   . LEU A 1 42  ? 7.301  -17.644 24.807  1.00  7.98  ? 42   LEU A C   1 
ATOM   338  O  O   . LEU A 1 42  ? 6.741  -18.341 23.950  1.00  8.99  ? 42   LEU A O   1 
ATOM   339  C  CB  . LEU A 1 42  ? 7.996  -19.056 26.729  1.00  9.35  ? 42   LEU A CB  1 
ATOM   340  C  CG  . LEU A 1 42  ? 7.949  -19.311 28.259  1.00  12.00 ? 42   LEU A CG  1 
ATOM   341  C  CD1 . LEU A 1 42  ? 8.997  -20.326 28.526  1.00  14.98 ? 42   LEU A CD1 1 
ATOM   342  C  CD2 . LEU A 1 42  ? 8.212  -18.033 29.016  1.00  16.08 ? 42   LEU A CD2 1 
ATOM   343  N  N   . HIS A 1 43  ? 8.105  -16.632 24.538  1.00  7.81  ? 43   HIS A N   1 
ATOM   344  C  CA  . HIS A 1 43  ? 8.453  -16.301 23.125  1.00  8.02  ? 43   HIS A CA  1 
ATOM   345  C  C   . HIS A 1 43  ? 9.933  -16.095 23.030  1.00  7.88  ? 43   HIS A C   1 
ATOM   346  O  O   . HIS A 1 43  ? 10.507 -15.250 23.774  1.00  9.06  ? 43   HIS A O   1 
ATOM   347  C  CB  . HIS A 1 43  ? 7.695  -15.029 22.777  1.00  8.06  ? 43   HIS A CB  1 
ATOM   348  C  CG  . HIS A 1 43  ? 6.232  -15.227 22.695  1.00  9.00  ? 43   HIS A CG  1 
ATOM   349  N  ND1 . HIS A 1 43  ? 5.624  -15.707 21.561  1.00  10.51 ? 43   HIS A ND1 1 
ATOM   350  C  CD2 . HIS A 1 43  ? 5.265  -15.147 23.658  1.00  10.15 ? 43   HIS A CD2 1 
ATOM   351  C  CE1 . HIS A 1 43  ? 4.327  -15.861 21.814  1.00  12.18 ? 43   HIS A CE1 1 
ATOM   352  N  NE2 . HIS A 1 43  ? 4.073  -15.518 23.078  1.00  9.96  ? 43   HIS A NE2 1 
ATOM   353  N  N   . GLY A 1 44  ? 10.595 -16.778 22.099  1.00  8.64  ? 44   GLY A N   1 
ATOM   354  C  CA  . GLY A 1 44  ? 11.992 -16.653 21.950  1.00  8.15  ? 44   GLY A CA  1 
ATOM   355  C  C   . GLY A 1 44  ? 12.433 -15.234 21.658  1.00  7.19  ? 44   GLY A C   1 
ATOM   356  O  O   . GLY A 1 44  ? 11.751 -14.478 20.948  1.00  7.91  ? 44   GLY A O   1 
ATOM   357  N  N   . PHE A 1 45  ? 13.599 -14.881 22.167  1.00  7.10  ? 45   PHE A N   1 
ATOM   358  C  CA  . PHE A 1 45  ? 14.053 -13.504 22.180  1.00  7.26  ? 45   PHE A CA  1 
ATOM   359  C  C   . PHE A 1 45  ? 15.514 -13.481 21.875  1.00  7.15  ? 45   PHE A C   1 
ATOM   360  O  O   . PHE A 1 45  ? 16.338 -13.927 22.670  1.00  7.93  ? 45   PHE A O   1 
ATOM   361  C  CB  . PHE A 1 45  ? 13.798 -12.927 23.601  1.00  7.93  ? 45   PHE A CB  1 
ATOM   362  C  CG  . PHE A 1 45  ? 13.893 -11.414 23.718  1.00  8.56  ? 45   PHE A CG  1 
ATOM   363  C  CD1 . PHE A 1 45  ? 13.171 -10.583 22.919  1.00  9.11  ? 45   PHE A CD1 1 
ATOM   364  C  CD2 . PHE A 1 45  ? 14.657 -10.847 24.702  1.00  9.08  ? 45   PHE A CD2 1 
ATOM   365  C  CE1 . PHE A 1 45  ? 13.207 -9.196  23.079  1.00  9.82  ? 45   PHE A CE1 1 
ATOM   366  C  CE2 . PHE A 1 45  ? 14.666 -9.425  24.918  1.00  10.09 ? 45   PHE A CE2 1 
ATOM   367  C  CZ  . PHE A 1 45  ? 13.956 -8.643  24.090  1.00  9.18  ? 45   PHE A CZ  1 
ATOM   368  N  N   . HIS A 1 46  ? 15.866 -13.038 20.645  1.00  7.26  ? 46   HIS A N   1 
ATOM   369  C  CA  . HIS A 1 46  ? 17.205 -13.212 20.135  1.00  6.73  ? 46   HIS A CA  1 
ATOM   370  C  C   . HIS A 1 46  ? 17.784 -11.945 19.475  1.00  6.70  ? 46   HIS A C   1 
ATOM   371  O  O   . HIS A 1 46  ? 17.053 -11.200 18.840  1.00  7.57  ? 46   HIS A O   1 
ATOM   372  C  CB  . HIS A 1 46  ? 17.204 -14.244 18.968  1.00  7.71  ? 46   HIS A CB  1 
ATOM   373  C  CG  . HIS A 1 46  ? 16.697 -15.564 19.320  1.00  7.71  ? 46   HIS A CG  1 
ATOM   374  N  ND1 . HIS A 1 46  ? 16.037 -16.342 18.404  1.00  9.13  ? 46   HIS A ND1 1 
ATOM   375  C  CD2 . HIS A 1 46  ? 16.765 -16.288 20.469  1.00  8.50  ? 46   HIS A CD2 1 
ATOM   376  C  CE1 . HIS A 1 46  ? 15.713 -17.493 18.969  1.00  8.88  ? 46   HIS A CE1 1 
ATOM   377  N  NE2 . HIS A 1 46  ? 16.118 -17.476 20.223  1.00  9.55  ? 46   HIS A NE2 1 
ATOM   378  N  N   . VAL A 1 47  ? 19.085 -11.779 19.566  1.00  6.93  ? 47   VAL A N   1 
ATOM   379  C  CA  . VAL A 1 47  ? 19.819 -10.821 18.694  1.00  6.74  ? 47   VAL A CA  1 
ATOM   380  C  C   . VAL A 1 47  ? 20.313 -11.677 17.515  1.00  7.51  ? 47   VAL A C   1 
ATOM   381  O  O   . VAL A 1 47  ? 21.054 -12.628 17.688  1.00  8.13  ? 47   VAL A O   1 
ATOM   382  C  CB  . VAL A 1 47  ? 20.956 -10.119 19.363  1.00  6.59  ? 47   VAL A CB  1 
ATOM   383  C  CG1 . VAL A 1 47  ? 21.589 -9.139  18.364  1.00  6.96  ? 47   VAL A CG1 1 
ATOM   384  C  CG2 . VAL A 1 47  ? 20.446 -9.414  20.636  1.00  7.33  ? 47   VAL A CG2 1 
ATOM   385  N  N   . HIS A 1 48  ? 19.828 -11.306 16.319  1.00  7.15  ? 48   HIS A N   1 
ATOM   386  C  CA  . HIS A 1 48  ? 20.287 -11.889 15.053  1.00  6.78  ? 48   HIS A CA  1 
ATOM   387  C  C   . HIS A 1 48  ? 21.370 -11.040 14.468  1.00  6.91  ? 48   HIS A C   1 
ATOM   388  O  O   . HIS A 1 48  ? 21.476 -9.880  14.736  1.00  8.38  ? 48   HIS A O   1 
ATOM   389  C  CB  . HIS A 1 48  ? 19.069 -12.075 14.123  1.00  6.82  ? 48   HIS A CB  1 
ATOM   390  C  CG  . HIS A 1 48  ? 18.200 -13.240 14.477  1.00  7.31  ? 48   HIS A CG  1 
ATOM   391  N  ND1 . HIS A 1 48  ? 18.136 -14.350 13.688  1.00  8.95  ? 48   HIS A ND1 1 
ATOM   392  C  CD2 . HIS A 1 48  ? 17.384 -13.503 15.539  1.00  8.16  ? 48   HIS A CD2 1 
ATOM   393  C  CE1 . HIS A 1 48  ? 17.342 -15.254 14.222  1.00  8.06  ? 48   HIS A CE1 1 
ATOM   394  N  NE2 . HIS A 1 48  ? 16.857 -14.763 15.364  1.00  7.54  ? 48   HIS A NE2 1 
ATOM   395  N  N   . GLU A 1 49  ? 22.153 -11.653 13.607  1.00  7.36  ? 49   GLU A N   1 
ATOM   396  C  CA  . GLU A 1 49  ? 23.431 -11.090 13.192  1.00  7.45  ? 49   GLU A CA  1 
ATOM   397  C  C   . GLU A 1 49  ? 23.330 -9.779  12.417  1.00  7.07  ? 49   GLU A C   1 
ATOM   398  O  O   . GLU A 1 49  ? 24.090 -8.861  12.677  1.00  8.54  ? 49   GLU A O   1 
ATOM   399  C  CB  . GLU A 1 49  ? 24.166 -12.104 12.338  1.00  7.56  ? 49   GLU A CB  1 
ATOM   400  C  CG  . GLU A 1 49  ? 25.568 -11.658 11.995  1.00  8.75  ? 49   GLU A CG  1 
ATOM   401  C  CD  . GLU A 1 49  ? 26.324 -12.651 11.144  1.00  9.50  ? 49   GLU A CD  1 
ATOM   402  O  OE1 . GLU A 1 49  ? 25.746 -13.726 10.835  1.00  11.25 ? 49   GLU A OE1 1 
ATOM   403  O  OE2 . GLU A 1 49  ? 27.513 -12.347 10.846  1.00  12.41 ? 49   GLU A OE2 1 
ATOM   404  N  N   . PHE A 1 50  ? 22.393 -9.684  11.479  1.00  7.69  ? 50   PHE A N   1 
ATOM   405  C  CA  . PHE A 1 50  ? 22.385 -8.526  10.599  1.00  7.34  ? 50   PHE A CA  1 
ATOM   406  C  C   . PHE A 1 50  ? 21.281 -7.596  10.966  1.00  7.14  ? 50   PHE A C   1 
ATOM   407  O  O   . PHE A 1 50  ? 20.164 -7.988  11.222  1.00  7.90  ? 50   PHE A O   1 
ATOM   408  C  CB  . PHE A 1 50  ? 22.220 -8.945  9.132   1.00  8.20  ? 50   PHE A CB  1 
ATOM   409  C  CG  . PHE A 1 50  ? 23.191 -9.990  8.689   1.00  8.65  ? 50   PHE A CG  1 
ATOM   410  C  CD1 . PHE A 1 50  ? 24.535 -9.770  8.844   1.00  9.20  ? 50   PHE A CD1 1 
ATOM   411  C  CD2 . PHE A 1 50  ? 22.750 -11.186 8.178   1.00  8.62  ? 50   PHE A CD2 1 
ATOM   412  C  CE1 . PHE A 1 50  ? 25.489 -10.789 8.479   1.00  9.95  ? 50   PHE A CE1 1 
ATOM   413  C  CE2 . PHE A 1 50  ? 23.647 -12.193 7.821   1.00  10.26 ? 50   PHE A CE2 1 
ATOM   414  C  CZ  . PHE A 1 50  ? 24.972 -12.014 7.983   1.00  10.88 ? 50   PHE A CZ  1 
ATOM   415  N  N   . GLY A 1 51  ? 21.588 -6.310  10.916  1.00  8.13  ? 51   GLY A N   1 
ATOM   416  C  CA  . GLY A 1 51  ? 20.569 -5.235  11.010  1.00  7.96  ? 51   GLY A CA  1 
ATOM   417  C  C   . GLY A 1 51  ? 19.939 -4.916  9.631   1.00  8.55  ? 51   GLY A C   1 
ATOM   418  O  O   . GLY A 1 51  ? 19.824 -3.778  9.244   1.00  8.57  ? 51   GLY A O   1 
ATOM   419  N  N   . ASP A 1 52  ? 19.542 -5.986  8.954   1.00  8.91  ? 52   ASP A N   1 
ATOM   420  C  CA  . ASP A 1 52  ? 18.974 -5.930  7.616   1.00  8.76  ? 52   ASP A CA  1 
ATOM   421  C  C   . ASP A 1 52  ? 17.512 -6.246  7.762   1.00  8.26  ? 52   ASP A C   1 
ATOM   422  O  O   . ASP A 1 52  ? 17.171 -7.386  7.985   1.00  9.09  ? 52   ASP A O   1 
ATOM   423  C  CB  . ASP A 1 52  ? 19.669 -6.948  6.726   1.00  9.15  ? 52   ASP A CB  1 
ATOM   424  C  CG  . ASP A 1 52  ? 19.229 -6.864  5.312   1.00  11.23 ? 52   ASP A CG  1 
ATOM   425  O  OD1 . ASP A 1 52  ? 18.144 -6.322  5.046   1.00  11.76 ? 52   ASP A OD1 1 
ATOM   426  O  OD2 . ASP A 1 52  ? 19.958 -7.407  4.440   1.00  15.02 ? 52   ASP A OD2 1 
ATOM   427  N  N   A ASN A 1 53  ? 16.699 -5.214  7.598   0.70  9.20  ? 53   ASN A N   1 
ATOM   428  N  N   B ASN A 1 53  ? 16.617 -5.290  7.666   0.30  8.33  ? 53   ASN A N   1 
ATOM   429  C  CA  A ASN A 1 53  ? 15.240 -5.204  7.745   0.70  10.29 ? 53   ASN A CA  1 
ATOM   430  C  CA  B ASN A 1 53  ? 15.206 -5.657  7.640   0.30  8.89  ? 53   ASN A CA  1 
ATOM   431  C  C   A ASN A 1 53  ? 14.565 -5.083  6.346   0.70  11.08 ? 53   ASN A C   1 
ATOM   432  C  C   B ASN A 1 53  ? 14.582 -5.118  6.356   0.30  9.79  ? 53   ASN A C   1 
ATOM   433  O  O   A ASN A 1 53  ? 13.353 -4.905  6.250   0.70  11.18 ? 53   ASN A O   1 
ATOM   434  O  O   B ASN A 1 53  ? 13.460 -4.600  6.339   0.30  8.89  ? 53   ASN A O   1 
ATOM   435  C  CB  A ASN A 1 53  ? 14.901 -4.009  8.651   0.70  10.58 ? 53   ASN A CB  1 
ATOM   436  C  CB  B ASN A 1 53  ? 14.461 -5.130  8.866   0.30  8.25  ? 53   ASN A CB  1 
ATOM   437  C  CG  A ASN A 1 53  ? 13.588 -4.114  9.349   0.70  11.89 ? 53   ASN A CG  1 
ATOM   438  C  CG  B ASN A 1 53  ? 15.064 -5.606  10.269  0.30  8.14  ? 53   ASN A CG  1 
ATOM   439  O  OD1 A ASN A 1 53  ? 13.230 -5.176  9.926   0.70  16.98 ? 53   ASN A OD1 1 
ATOM   440  O  OD1 B ASN A 1 53  ? 15.705 -6.671  10.456  0.30  7.20  ? 53   ASN A OD1 1 
ATOM   441  N  ND2 A ASN A 1 53  ? 12.866 -3.030  9.366   0.70  13.83 ? 53   ASN A ND2 1 
ATOM   442  N  ND2 B ASN A 1 53  ? 14.786 -4.793  11.274  0.30  6.72  ? 53   ASN A ND2 1 
ATOM   443  N  N   . THR A 1 54  ? 15.353 -5.245  5.292   1.00  10.26 ? 54   THR A N   1 
ATOM   444  C  CA  . THR A 1 54  ? 14.869 -4.956  3.910   1.00  11.55 ? 54   THR A CA  1 
ATOM   445  C  C   . THR A 1 54  ? 13.734 -5.863  3.528   1.00  12.48 ? 54   THR A C   1 
ATOM   446  O  O   . THR A 1 54  ? 12.871 -5.466  2.768   1.00  12.73 ? 54   THR A O   1 
ATOM   447  C  CB  . THR A 1 54  ? 15.991 -5.001  2.861   1.00  12.12 ? 54   THR A CB  1 
ATOM   448  O  OG1 . THR A 1 54  ? 16.608 -6.289  2.863   1.00  11.96 ? 54   THR A OG1 1 
ATOM   449  C  CG2 . THR A 1 54  ? 17.029 -3.933  3.135   1.00  12.33 ? 54   THR A CG2 1 
ATOM   450  N  N   . ALA A 1 55  ? 13.715 -7.092  4.067   1.00  13.38 ? 55   ALA A N   1 
ATOM   451  C  CA  . ALA A 1 55  ? 12.590 -8.036  3.890   1.00  14.71 ? 55   ALA A CA  1 
ATOM   452  C  C   . ALA A 1 55  ? 11.939 -8.311  5.243   1.00  15.32 ? 55   ALA A C   1 
ATOM   453  O  O   . ALA A 1 55  ? 11.591 -9.485  5.566   1.00  17.88 ? 55   ALA A O   1 
ATOM   454  C  CB  . ALA A 1 55  ? 13.071 -9.316  3.275   1.00  15.97 ? 55   ALA A CB  1 
ATOM   455  N  N   . GLY A 1 56  ? 11.746 -7.274  6.040   1.00  15.67 ? 56   GLY A N   1 
ATOM   456  C  CA  . GLY A 1 56  ? 11.282 -7.432  7.429   1.00  15.83 ? 56   GLY A CA  1 
ATOM   457  C  C   . GLY A 1 56  ? 12.262 -8.272  8.209   1.00  15.15 ? 56   GLY A C   1 
ATOM   458  O  O   . GLY A 1 56  ? 13.461 -8.172  8.059   1.00  18.13 ? 56   GLY A O   1 
ATOM   459  N  N   . CYS A 1 57  ? 11.755 -9.256  8.908   1.00  12.99 ? 57   CYS A N   1 
ATOM   460  C  CA  . CYS A 1 57  ? 12.618 -9.990  9.771   1.00  11.49 ? 57   CYS A CA  1 
ATOM   461  C  C   . CYS A 1 57  ? 13.356 -11.126 9.077   1.00  11.58 ? 57   CYS A C   1 
ATOM   462  O  O   . CYS A 1 57  ? 14.296 -11.612 9.609   1.00  12.71 ? 57   CYS A O   1 
ATOM   463  C  CB  . CYS A 1 57  ? 11.815 -10.566 10.893  1.00  11.72 ? 57   CYS A CB  1 
ATOM   464  S  SG  . CYS A 1 57  ? 10.819 -9.329  11.819  1.00  13.95 ? 57   CYS A SG  1 
ATOM   465  N  N   A THR A 1 58  ? 12.844 -11.423 7.865   0.60  12.00 ? 58   THR A N   1 
ATOM   466  N  N   B THR A 1 58  ? 13.118 -11.554 7.855   0.40  11.74 ? 58   THR A N   1 
ATOM   467  C  CA  A THR A 1 58  ? 13.261 -12.527 6.997   0.60  11.04 ? 58   THR A CA  1 
ATOM   468  C  CA  B THR A 1 58  ? 13.935 -12.725 7.416   0.40  11.30 ? 58   THR A CA  1 
ATOM   469  C  C   A THR A 1 58  ? 14.752 -12.489 6.778   0.60  11.26 ? 58   THR A C   1 
ATOM   470  C  C   B THR A 1 58  ? 15.428 -12.335 7.085   0.40  10.90 ? 58   THR A C   1 
ATOM   471  O  O   A THR A 1 58  ? 15.400 -13.567 6.725   0.60  13.70 ? 58   THR A O   1 
ATOM   472  O  O   B THR A 1 58  ? 16.404 -13.081 7.331   0.40  10.28 ? 58   THR A O   1 
ATOM   473  C  CB  A THR A 1 58  ? 12.527 -12.458 5.617   0.60  11.09 ? 58   THR A CB  1 
ATOM   474  C  CB  B THR A 1 58  ? 13.161 -13.524 6.322   0.40  11.77 ? 58   THR A CB  1 
ATOM   475  O  OG1 A THR A 1 58  ? 11.114 -12.455 5.860   0.60  14.77 ? 58   THR A OG1 1 
ATOM   476  O  OG1 B THR A 1 58  ? 11.922 -13.999 6.894   0.40  17.07 ? 58   THR A OG1 1 
ATOM   477  C  CG2 A THR A 1 58  ? 12.928 -13.619 4.716   0.60  13.01 ? 58   THR A CG2 1 
ATOM   478  C  CG2 B THR A 1 58  ? 13.981 -14.696 5.848   0.40  11.54 ? 58   THR A CG2 1 
ATOM   479  N  N   A SER A 1 59  ? 15.239 -11.245 6.640   0.60  10.30 ? 59   SER A N   1 
ATOM   480  N  N   B SER A 1 59  ? 15.627 -11.149 6.547   0.40  9.76  ? 59   SER A N   1 
ATOM   481  C  CA  A SER A 1 59  ? 16.593 -10.745 6.343   0.60  11.78 ? 59   SER A CA  1 
ATOM   482  C  CA  B SER A 1 59  ? 16.986 -10.707 6.223   0.40  11.38 ? 59   SER A CA  1 
ATOM   483  C  C   A SER A 1 59  ? 17.729 -10.697 7.398   0.60  10.46 ? 59   SER A C   1 
ATOM   484  C  C   B SER A 1 59  ? 17.897 -10.640 7.444   0.40  10.06 ? 59   SER A C   1 
ATOM   485  O  O   A SER A 1 59  ? 18.883 -10.454 7.112   0.60  9.54  ? 59   SER A O   1 
ATOM   486  O  O   B SER A 1 59  ? 19.093 -10.374 7.312   0.40  8.99  ? 59   SER A O   1 
ATOM   487  C  CB  A SER A 1 59  ? 16.447 -9.358  5.621   0.60  12.75 ? 59   SER A CB  1 
ATOM   488  C  CB  B SER A 1 59  ? 16.963 -9.410  5.381   0.40  11.59 ? 59   SER A CB  1 
ATOM   489  O  OG  A SER A 1 59  ? 15.375 -8.583  6.114   0.60  12.33 ? 59   SER A OG  1 
ATOM   490  O  OG  B SER A 1 59  ? 15.851 -9.438  4.503   0.40  10.64 ? 59   SER A OG  1 
ATOM   491  N  N   . ALA A 1 60  ? 17.366 -10.920 8.648   1.00  10.51 ? 60   ALA A N   1 
ATOM   492  C  CA  . ALA A 1 60  ? 18.216 -10.740 9.795   1.00  9.14  ? 60   ALA A CA  1 
ATOM   493  C  C   . ALA A 1 60  ? 19.311 -11.760 10.031  1.00  8.04  ? 60   ALA A C   1 
ATOM   494  O  O   . ALA A 1 60  ? 20.272 -11.537 10.767  1.00  8.14  ? 60   ALA A O   1 
ATOM   495  C  CB  . ALA A 1 60  ? 17.331 -10.653 11.018  1.00  11.07 ? 60   ALA A CB  1 
ATOM   496  N  N   . GLY A 1 61  ? 19.285 -12.871 9.305   1.00  8.18  ? 61   GLY A N   1 
ATOM   497  C  CA  . GLY A 1 61  ? 20.342 -13.825 9.420   1.00  8.03  ? 61   GLY A CA  1 
ATOM   498  C  C   . GLY A 1 61  ? 20.234 -14.715 10.652  1.00  8.24  ? 61   GLY A C   1 
ATOM   499  O  O   . GLY A 1 61  ? 19.170 -14.814 11.226  1.00  8.71  ? 61   GLY A O   1 
ATOM   500  N  N   . PRO A 1 62  ? 21.305 -15.408 10.925  1.00  8.05  ? 62   PRO A N   1 
ATOM   501  C  CA  . PRO A 1 62  ? 21.341 -16.348 11.997  1.00  8.83  ? 62   PRO A CA  1 
ATOM   502  C  C   . PRO A 1 62  ? 21.519 -15.653 13.325  1.00  8.29  ? 62   PRO A C   1 
ATOM   503  O  O   . PRO A 1 62  ? 21.551 -14.448 13.397  1.00  8.63  ? 62   PRO A O   1 
ATOM   504  C  CB  . PRO A 1 62  ? 22.549 -17.236 11.654  1.00  9.85  ? 62   PRO A CB  1 
ATOM   505  C  CG  . PRO A 1 62  ? 23.461 -16.394 10.983  1.00  9.94  ? 62   PRO A CG  1 
ATOM   506  C  CD  . PRO A 1 62  ? 22.565 -15.406 10.180  1.00  8.33  ? 62   PRO A CD  1 
ATOM   507  N  N   . HIS A 1 63  ? 21.570 -16.406 14.424  1.00  8.36  ? 63   HIS A N   1 
ATOM   508  C  CA  . HIS A 1 63  ? 21.802 -15.792 15.736  1.00  7.87  ? 63   HIS A CA  1 
ATOM   509  C  C   . HIS A 1 63  ? 23.151 -15.156 15.760  1.00  8.39  ? 63   HIS A C   1 
ATOM   510  O  O   . HIS A 1 63  ? 24.116 -15.666 15.163  1.00  9.14  ? 63   HIS A O   1 
ATOM   511  C  CB  . HIS A 1 63  ? 21.763 -16.899 16.808  1.00  8.73  ? 63   HIS A CB  1 
ATOM   512  C  CG  . HIS A 1 63  ? 20.432 -17.515 16.972  1.00  8.23  ? 63   HIS A CG  1 
ATOM   513  N  ND1 . HIS A 1 63  ? 20.184 -18.354 18.028  1.00  8.50  ? 63   HIS A ND1 1 
ATOM   514  C  CD2 . HIS A 1 63  ? 19.314 -17.513 16.206  1.00  9.11  ? 63   HIS A CD2 1 
ATOM   515  C  CE1 . HIS A 1 63  ? 18.933 -18.762 17.963  1.00  9.15  ? 63   HIS A CE1 1 
ATOM   516  N  NE2 . HIS A 1 63  ? 18.378 -18.281 16.851  1.00  9.19  ? 63   HIS A NE2 1 
ATOM   517  N  N   . PHE A 1 64  ? 23.282 -14.001 16.421  1.00  7.38  ? 64   PHE A N   1 
ATOM   518  C  CA  . PHE A 1 64  ? 24.565 -13.341 16.490  1.00  7.89  ? 64   PHE A CA  1 
ATOM   519  C  C   . PHE A 1 64  ? 25.495 -14.221 17.315  1.00  8.64  ? 64   PHE A C   1 
ATOM   520  O  O   . PHE A 1 64  ? 25.215 -14.526 18.506  1.00  8.49  ? 64   PHE A O   1 
ATOM   521  C  CB  . PHE A 1 64  ? 24.404 -11.965 17.099  1.00  7.76  ? 64   PHE A CB  1 
ATOM   522  C  CG  . PHE A 1 64  ? 25.668 -11.212 17.297  1.00  7.84  ? 64   PHE A CG  1 
ATOM   523  C  CD1 . PHE A 1 64  ? 26.595 -11.119 16.289  1.00  9.61  ? 64   PHE A CD1 1 
ATOM   524  C  CD2 . PHE A 1 64  ? 25.962 -10.576 18.487  1.00  8.96  ? 64   PHE A CD2 1 
ATOM   525  C  CE1 . PHE A 1 64  ? 27.786 -10.447 16.450  1.00  9.61  ? 64   PHE A CE1 1 
ATOM   526  C  CE2 . PHE A 1 64  ? 27.167 -9.850  18.650  1.00  9.72  ? 64   PHE A CE2 1 
ATOM   527  C  CZ  . PHE A 1 64  ? 28.050 -9.817  17.646  1.00  9.02  ? 64   PHE A CZ  1 
ATOM   528  N  N   . ASN A 1 65  ? 26.577 -14.669 16.715  1.00  9.04  ? 65   ASN A N   1 
ATOM   529  C  CA  . ASN A 1 65  ? 27.425 -15.706 17.267  1.00  8.73  ? 65   ASN A CA  1 
ATOM   530  C  C   . ASN A 1 65  ? 28.905 -15.420 16.962  1.00  9.37  ? 65   ASN A C   1 
ATOM   531  O  O   . ASN A 1 65  ? 29.570 -16.273 16.355  1.00  10.22 ? 65   ASN A O   1 
ATOM   532  C  CB  . ASN A 1 65  ? 26.982 -17.079 16.755  1.00  8.88  ? 65   ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 65  ? 27.724 -18.248 17.361  1.00  9.57  ? 65   ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 65  ? 28.224 -18.179 18.485  1.00  10.91 ? 65   ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 65  ? 27.733 -19.399 16.633  1.00  11.15 ? 65   ASN A ND2 1 
ATOM   536  N  N   . PRO A 1 66  ? 29.453 -14.274 17.426  1.00  9.50  ? 66   PRO A N   1 
ATOM   537  C  CA  . PRO A 1 66  ? 30.831 -13.956 17.130  1.00  10.81 ? 66   PRO A CA  1 
ATOM   538  C  C   . PRO A 1 66  ? 31.875 -14.889 17.680  1.00  12.53 ? 66   PRO A C   1 
ATOM   539  O  O   . PRO A 1 66  ? 32.983 -14.932 17.178  1.00  14.42 ? 66   PRO A O   1 
ATOM   540  C  CB  . PRO A 1 66  ? 30.997 -12.555 17.637  1.00  11.61 ? 66   PRO A CB  1 
ATOM   541  C  CG  . PRO A 1 66  ? 30.045 -12.521 18.799  1.00  11.19 ? 66   PRO A CG  1 
ATOM   542  C  CD  . PRO A 1 66  ? 28.853 -13.262 18.363  1.00  9.15  ? 66   PRO A CD  1 
ATOM   543  N  N   . LEU A 1 67  ? 31.506 -15.702 18.668  1.00  11.55 ? 67   LEU A N   1 
ATOM   544  C  CA  . LEU A 1 67  ? 32.474 -16.585 19.348  1.00  11.93 ? 67   LEU A CA  1 
ATOM   545  C  C   . LEU A 1 67  ? 32.270 -18.053 18.905  1.00  12.57 ? 67   LEU A C   1 
ATOM   546  O  O   . LEU A 1 67  ? 32.845 -18.957 19.498  1.00  14.69 ? 67   LEU A O   1 
ATOM   547  C  CB  . LEU A 1 67  ? 32.390 -16.389 20.876  1.00  11.85 ? 67   LEU A CB  1 
ATOM   548  C  CG  . LEU A 1 67  ? 32.413 -14.942 21.401  1.00  15.17 ? 67   LEU A CG  1 
ATOM   549  C  CD1 . LEU A 1 67  ? 32.228 -14.909 22.866  1.00  15.30 ? 67   LEU A CD1 1 
ATOM   550  C  CD2 . LEU A 1 67  ? 33.684 -14.189 21.032  1.00  18.27 ? 67   LEU A CD2 1 
ATOM   551  N  N   . SER A 1 68  ? 31.435 -18.301 17.892  1.00  11.57 ? 68   SER A N   1 
ATOM   552  C  CA  . SER A 1 68  ? 31.311 -19.622 17.263  1.00  12.67 ? 68   SER A CA  1 
ATOM   553  C  C   . SER A 1 68  ? 30.979 -20.696 18.277  1.00  11.70 ? 68   SER A C   1 
ATOM   554  O  O   . SER A 1 68  ? 31.620 -21.759 18.329  1.00  15.26 ? 68   SER A O   1 
ATOM   555  C  CB  . SER A 1 68  ? 32.591 -20.006 16.484  1.00  13.62 ? 68   SER A CB  1 
ATOM   556  O  OG  . SER A 1 68  ? 32.849 -19.089 15.435  1.00  16.22 ? 68   SER A OG  1 
ATOM   557  N  N   . ARG A 1 69  ? 29.982 -20.388 19.101  1.00  11.34 ? 69   ARG A N   1 
ATOM   558  C  CA  . ARG A 1 69  ? 29.432 -21.360 20.032  1.00  11.87 ? 69   ARG A CA  1 
ATOM   559  C  C   . ARG A 1 69  ? 28.111 -21.973 19.546  1.00  10.53 ? 69   ARG A C   1 
ATOM   560  O  O   . ARG A 1 69  ? 27.592 -21.623 18.474  1.00  12.18 ? 69   ARG A O   1 
ATOM   561  C  CB  . ARG A 1 69  ? 29.215 -20.697 21.398  1.00  11.80 ? 69   ARG A CB  1 
ATOM   562  C  CG  . ARG A 1 69  ? 30.388 -19.910 21.939  1.00  13.88 ? 69   ARG A CG  1 
ATOM   563  C  CD  . ARG A 1 69  ? 31.651 -20.768 22.080  1.00  16.85 ? 69   ARG A CD  1 
ATOM   564  N  NE  . ARG A 1 69  ? 31.418 -21.917 22.956  1.00  15.66 ? 69   ARG A NE  1 
ATOM   565  C  CZ  . ARG A 1 69  ? 31.365 -21.885 24.287  1.00  16.76 ? 69   ARG A CZ  1 
ATOM   566  N  NH1 . ARG A 1 69  ? 31.621 -20.772 24.998  1.00  17.98 ? 69   ARG A NH1 1 
ATOM   567  N  NH2 . ARG A 1 69  ? 31.110 -23.026 24.916  1.00  17.97 ? 69   ARG A NH2 1 
ATOM   568  N  N   . LYS A 1 70  ? 27.597 -22.930 20.307  1.00  10.93 ? 70   LYS A N   1 
ATOM   569  C  CA  . LYS A 1 70  ? 26.304 -23.503 20.031  1.00  11.57 ? 70   LYS A CA  1 
ATOM   570  C  C   . LYS A 1 70  ? 25.193 -22.721 20.744  1.00  9.75  ? 70   LYS A C   1 
ATOM   571  O  O   . LYS A 1 70  ? 25.459 -21.936 21.670  1.00  10.50 ? 70   LYS A O   1 
ATOM   572  C  CB  . LYS A 1 70  ? 26.283 -24.972 20.452  1.00  12.26 ? 70   LYS A CB  1 
ATOM   573  C  CG  . LYS A 1 70  ? 27.310 -25.825 19.698  1.00  15.54 ? 70   LYS A CG  1 
ATOM   574  C  CD  . LYS A 1 70  ? 27.085 -27.225 20.096  1.00  18.15 ? 70   LYS A CD  1 
ATOM   575  C  CE  . LYS A 1 70  ? 27.617 -28.195 19.059  0.40  19.33 ? 70   LYS A CE  1 
ATOM   576  N  NZ  . LYS A 1 70  ? 26.766 -29.427 18.993  0.40  19.85 ? 70   LYS A NZ  1 
ATOM   577  N  N   . HIS A 1 71  ? 23.951 -22.982 20.362  1.00  8.79  ? 71   HIS A N   1 
ATOM   578  C  CA  . HIS A 1 71  ? 22.785 -22.318 20.948  1.00  8.92  ? 71   HIS A CA  1 
ATOM   579  C  C   . HIS A 1 71  ? 22.479 -22.763 22.368  1.00  8.38  ? 71   HIS A C   1 
ATOM   580  O  O   . HIS A 1 71  ? 22.563 -23.910 22.700  1.00  10.12 ? 71   HIS A O   1 
ATOM   581  C  CB  . HIS A 1 71  ? 21.552 -22.535 20.048  1.00  8.06  ? 71   HIS A CB  1 
ATOM   582  C  CG  . HIS A 1 71  ? 20.334 -21.855 20.530  1.00  8.73  ? 71   HIS A CG  1 
ATOM   583  N  ND1 . HIS A 1 71  ? 20.176 -20.493 20.456  1.00  7.69  ? 71   HIS A ND1 1 
ATOM   584  C  CD2 . HIS A 1 71  ? 19.269 -22.343 21.185  1.00  10.50 ? 71   HIS A CD2 1 
ATOM   585  C  CE1 . HIS A 1 71  ? 19.017 -20.187 20.990  1.00  9.19  ? 71   HIS A CE1 1 
ATOM   586  N  NE2 . HIS A 1 71  ? 18.462 -21.288 21.486  1.00  9.59  ? 71   HIS A NE2 1 
ATOM   587  N  N   . GLY A 1 72  ? 22.132 -21.806 23.205  1.00  8.51  ? 72   GLY A N   1 
ATOM   588  C  CA  . GLY A 1 72  ? 21.668 -22.102 24.530  1.00  9.30  ? 72   GLY A CA  1 
ATOM   589  C  C   . GLY A 1 72  ? 20.796 -21.016 25.029  1.00  9.05  ? 72   GLY A C   1 
ATOM   590  O  O   . GLY A 1 72  ? 20.280 -20.170 24.304  1.00  9.41  ? 72   GLY A O   1 
ATOM   591  N  N   . GLY A 1 73  ? 20.700 -21.017 26.345  1.00  10.92 ? 73   GLY A N   1 
ATOM   592  C  CA  . GLY A 1 73  ? 20.028 -19.942 27.053  1.00  10.64 ? 73   GLY A CA  1 
ATOM   593  C  C   . GLY A 1 73  ? 20.998 -18.966 27.667  1.00  9.01  ? 73   GLY A C   1 
ATOM   594  O  O   . GLY A 1 73  ? 22.175 -19.156 27.726  1.00  10.25 ? 73   GLY A O   1 
ATOM   595  N  N   . PRO A 1 74  ? 20.441 -17.834 28.126  1.00  9.49  ? 74   PRO A N   1 
ATOM   596  C  CA  . PRO A 1 74  ? 21.265 -16.755 28.557  1.00  9.50  ? 74   PRO A CA  1 
ATOM   597  C  C   . PRO A 1 74  ? 22.064 -17.081 29.812  1.00  10.57 ? 74   PRO A C   1 
ATOM   598  O  O   . PRO A 1 74  ? 23.120 -16.535 29.995  1.00  13.10 ? 74   PRO A O   1 
ATOM   599  C  CB  . PRO A 1 74  ? 20.284 -15.614 28.820  1.00  9.58  ? 74   PRO A CB  1 
ATOM   600  C  CG  . PRO A 1 74  ? 18.966 -16.276 28.948  1.00  11.45 ? 74   PRO A CG  1 
ATOM   601  C  CD  . PRO A 1 74  ? 19.028 -17.462 28.071  1.00  9.47  ? 74   PRO A CD  1 
ATOM   602  N  N   . LYS A 1 75  ? 21.630 -18.076 30.580  1.00  10.84 ? 75   LYS A N   1 
ATOM   603  C  CA  . LYS A 1 75  ? 22.375 -18.494 31.782  1.00  12.15 ? 75   LYS A CA  1 
ATOM   604  C  C   . LYS A 1 75  ? 23.395 -19.574 31.526  1.00  12.07 ? 75   LYS A C   1 
ATOM   605  O  O   . LYS A 1 75  ? 24.048 -20.061 32.441  1.00  14.47 ? 75   LYS A O   1 
ATOM   606  C  CB  . LYS A 1 75  ? 21.443 -19.085 32.812  0.70  11.24 ? 75   LYS A CB  1 
ATOM   607  C  CG  . LYS A 1 75  ? 20.178 -18.354 33.175  0.70  14.08 ? 75   LYS A CG  1 
ATOM   608  C  CD  . LYS A 1 75  ? 19.577 -19.023 34.398  0.70  15.94 ? 75   LYS A CD  1 
ATOM   609  C  CE  . LYS A 1 75  ? 18.076 -19.305 34.252  0.70  19.21 ? 75   LYS A CE  1 
ATOM   610  N  NZ  . LYS A 1 75  ? 17.350 -18.725 35.422  0.70  22.46 ? 75   LYS A NZ  1 
ATOM   611  N  N   . ASP A 1 76  ? 23.478 -20.039 30.305  1.00  11.75 ? 76   ASP A N   1 
ATOM   612  C  CA  . ASP A 1 76  ? 24.410 -21.070 29.917  1.00  11.40 ? 76   ASP A CA  1 
ATOM   613  C  C   . ASP A 1 76  ? 25.757 -20.518 29.516  1.00  11.63 ? 76   ASP A C   1 
ATOM   614  O  O   . ASP A 1 76  ? 25.850 -19.462 28.916  1.00  11.63 ? 76   ASP A O   1 
ATOM   615  C  CB  . ASP A 1 76  ? 23.895 -21.928 28.749  1.00  12.54 ? 76   ASP A CB  1 
ATOM   616  C  CG  . ASP A 1 76  ? 22.649 -22.657 29.088  1.00  14.37 ? 76   ASP A CG  1 
ATOM   617  O  OD1 . ASP A 1 76  ? 22.505 -23.066 30.259  1.00  17.71 ? 76   ASP A OD1 1 
ATOM   618  O  OD2 . ASP A 1 76  ? 21.792 -22.906 28.230  1.00  14.40 ? 76   ASP A OD2 1 
ATOM   619  N  N   . GLU A 1 77  ? 26.807 -21.279 29.784  1.00  10.70 ? 77   GLU A N   1 
ATOM   620  C  CA  . GLU A 1 77  ? 28.104 -20.969 29.242  1.00  11.11 ? 77   GLU A CA  1 
ATOM   621  C  C   . GLU A 1 77  ? 28.132 -21.165 27.722  1.00  10.69 ? 77   GLU A C   1 
ATOM   622  O  O   . GLU A 1 77  ? 28.742 -20.381 26.942  1.00  11.80 ? 77   GLU A O   1 
ATOM   623  C  CB  . GLU A 1 77  ? 29.142 -21.838 29.942  1.00  11.65 ? 77   GLU A CB  1 
ATOM   624  C  CG  . GLU A 1 77  ? 30.577 -21.467 29.613  1.00  14.08 ? 77   GLU A CG  1 
ATOM   625  C  CD  . GLU A 1 77  ? 31.091 -21.950 28.290  1.00  17.14 ? 77   GLU A CD  1 
ATOM   626  O  OE1 . GLU A 1 77  ? 30.665 -23.055 27.851  1.00  17.44 ? 77   GLU A OE1 1 
ATOM   627  O  OE2 . GLU A 1 77  ? 31.990 -21.261 27.714  1.00  17.07 ? 77   GLU A OE2 1 
ATOM   628  N  N   . GLU A 1 78  ? 27.524 -22.283 27.294  1.00  10.62 ? 78   GLU A N   1 
ATOM   629  C  CA  . GLU A 1 78  ? 27.428 -22.609 25.874  1.00  10.01 ? 78   GLU A CA  1 
ATOM   630  C  C   . GLU A 1 78  ? 26.195 -21.934 25.274  1.00  9.54  ? 78   GLU A C   1 
ATOM   631  O  O   . GLU A 1 78  ? 25.082 -22.406 25.416  1.00  10.23 ? 78   GLU A O   1 
ATOM   632  C  CB  . GLU A 1 78  ? 27.393 -24.122 25.651  1.00  10.39 ? 78   GLU A CB  1 
ATOM   633  C  CG  . GLU A 1 78  ? 27.360 -24.501 24.199  1.00  12.63 ? 78   GLU A CG  1 
ATOM   634  C  CD  . GLU A 1 78  ? 28.730 -24.630 23.616  1.00  20.47 ? 78   GLU A CD  1 
ATOM   635  O  OE1 . GLU A 1 78  ? 29.510 -25.412 24.208  1.00  24.53 ? 78   GLU A OE1 1 
ATOM   636  O  OE2 . GLU A 1 78  ? 29.028 -24.011 22.561  1.00  21.25 ? 78   GLU A OE2 1 
ATOM   637  N  N   . ARG A 1 79  ? 26.426 -20.749 24.725  1.00  8.65  ? 79   ARG A N   1 
ATOM   638  C  CA  . ARG A 1 79  ? 25.393 -19.949 24.122  1.00  8.41  ? 79   ARG A CA  1 
ATOM   639  C  C   . ARG A 1 79  ? 26.032 -19.067 23.074  1.00  8.16  ? 79   ARG A C   1 
ATOM   640  O  O   . ARG A 1 79  ? 27.198 -18.776 23.117  1.00  9.07  ? 79   ARG A O   1 
ATOM   641  C  CB  . ARG A 1 79  ? 24.676 -19.052 25.165  1.00  9.03  ? 79   ARG A CB  1 
ATOM   642  C  CG  . ARG A 1 79  ? 25.624 -18.106 25.904  1.00  8.18  ? 79   ARG A CG  1 
ATOM   643  C  CD  . ARG A 1 79  ? 24.920 -17.087 26.798  1.00  8.59  ? 79   ARG A CD  1 
ATOM   644  N  NE  . ARG A 1 79  ? 24.481 -15.923 26.014  1.00  9.34  ? 79   ARG A NE  1 
ATOM   645  C  CZ  . ARG A 1 79  ? 24.029 -14.821 26.544  1.00  8.00  ? 79   ARG A CZ  1 
ATOM   646  N  NH1 . ARG A 1 79  ? 23.930 -14.748 27.882  1.00  9.10  ? 79   ARG A NH1 1 
ATOM   647  N  NH2 . ARG A 1 79  ? 23.741 -13.764 25.787  1.00  8.93  ? 79   ARG A NH2 1 
ATOM   648  N  N   . HIS A 1 80  ? 25.188 -18.607 22.172  1.00  8.00  ? 80   HIS A N   1 
ATOM   649  C  CA  . HIS A 1 80  ? 25.550 -17.515 21.277  1.00  7.90  ? 80   HIS A CA  1 
ATOM   650  C  C   . HIS A 1 80  ? 25.423 -16.203 22.017  1.00  8.10  ? 80   HIS A C   1 
ATOM   651  O  O   . HIS A 1 80  ? 24.593 -16.085 22.937  1.00  8.73  ? 80   HIS A O   1 
ATOM   652  C  CB  . HIS A 1 80  ? 24.517 -17.481 20.112  1.00  7.92  ? 80   HIS A CB  1 
ATOM   653  C  CG  . HIS A 1 80  ? 24.361 -18.765 19.338  1.00  9.22  ? 80   HIS A CG  1 
ATOM   654  N  ND1 . HIS A 1 80  ? 23.158 -19.248 18.886  1.00  8.11  ? 80   HIS A ND1 1 
ATOM   655  C  CD2 . HIS A 1 80  ? 25.304 -19.612 18.879  1.00  10.48 ? 80   HIS A CD2 1 
ATOM   656  C  CE1 . HIS A 1 80  ? 23.364 -20.324 18.134  1.00  10.01 ? 80   HIS A CE1 1 
ATOM   657  N  NE2 . HIS A 1 80  ? 24.661 -20.567 18.122  1.00  9.95  ? 80   HIS A NE2 1 
ATOM   658  N  N   . VAL A 1 81  ? 26.173 -15.195 21.585  1.00  7.89  ? 81   VAL A N   1 
ATOM   659  C  CA  . VAL A 1 81  ? 26.007 -13.887 22.180  1.00  8.42  ? 81   VAL A CA  1 
ATOM   660  C  C   . VAL A 1 81  ? 24.562 -13.450 22.122  1.00  8.00  ? 81   VAL A C   1 
ATOM   661  O  O   . VAL A 1 81  ? 24.039 -12.862 23.079  1.00  8.29  ? 81   VAL A O   1 
ATOM   662  C  CB  . VAL A 1 81  ? 26.966 -12.844 21.589  1.00  8.92  ? 81   VAL A CB  1 
ATOM   663  C  CG1 . VAL A 1 81  ? 26.585 -11.424 22.087  1.00  8.46  ? 81   VAL A CG1 1 
ATOM   664  C  CG2 . VAL A 1 81  ? 28.396 -13.141 21.957  1.00  8.25  ? 81   VAL A CG2 1 
ATOM   665  N  N   . GLY A 1 82  ? 23.890 -13.680 21.003  1.00  7.99  ? 82   GLY A N   1 
ATOM   666  C  CA  . GLY A 1 82  ? 22.524 -13.214 20.853  1.00  7.62  ? 82   GLY A CA  1 
ATOM   667  C  C   . GLY A 1 82  ? 21.395 -14.000 21.534  1.00  7.74  ? 82   GLY A C   1 
ATOM   668  O  O   . GLY A 1 82  ? 20.214 -13.712 21.361  1.00  9.33  ? 82   GLY A O   1 
ATOM   669  N  N   . ASP A 1 83  ? 21.766 -14.973 22.371  1.00  7.71  ? 83   ASP A N   1 
ATOM   670  C  CA  . ASP A 1 83  ? 20.776 -15.853 23.014  1.00  7.54  ? 83   ASP A CA  1 
ATOM   671  C  C   . ASP A 1 83  ? 20.236 -15.239 24.348  1.00  7.76  ? 83   ASP A C   1 
ATOM   672  O  O   . ASP A 1 83  ? 20.828 -15.472 25.426  1.00  9.75  ? 83   ASP A O   1 
ATOM   673  C  CB  . ASP A 1 83  ? 21.456 -17.186 23.345  1.00  8.83  ? 83   ASP A CB  1 
ATOM   674  C  CG  . ASP A 1 83  ? 21.704 -18.042 22.112  1.00  9.61  ? 83   ASP A CG  1 
ATOM   675  O  OD1 . ASP A 1 83  ? 21.136 -17.677 21.030  1.00  8.23  ? 83   ASP A OD1 1 
ATOM   676  O  OD2 . ASP A 1 83  ? 22.421 -19.056 22.154  1.00  8.44  ? 83   ASP A OD2 1 
ATOM   677  N  N   . LEU A 1 84  ? 19.156 -14.486 24.213  1.00  7.60  ? 84   LEU A N   1 
ATOM   678  C  CA  . LEU A 1 84  ? 18.523 -13.819 25.343  1.00  7.70  ? 84   LEU A CA  1 
ATOM   679  C  C   . LEU A 1 84  ? 17.306 -14.589 25.876  1.00  7.86  ? 84   LEU A C   1 
ATOM   680  O  O   . LEU A 1 84  ? 16.542 -14.049 26.682  1.00  10.69 ? 84   LEU A O   1 
ATOM   681  C  CB  . LEU A 1 84  ? 18.247 -12.359 24.994  1.00  8.06  ? 84   LEU A CB  1 
ATOM   682  C  CG  . LEU A 1 84  ? 19.449 -11.497 24.729  1.00  8.29  ? 84   LEU A CG  1 
ATOM   683  C  CD1 . LEU A 1 84  ? 18.941 -10.132 24.321  1.00  9.67  ? 84   LEU A CD1 1 
ATOM   684  C  CD2 . LEU A 1 84  ? 20.443 -11.466 25.886  1.00  8.75  ? 84   LEU A CD2 1 
ATOM   685  N  N   . GLY A 1 85  ? 17.123 -15.808 25.453  1.00  7.79  ? 85   GLY A N   1 
ATOM   686  C  CA  . GLY A 1 85  ? 16.101 -16.715 26.085  1.00  8.61  ? 85   GLY A CA  1 
ATOM   687  C  C   . GLY A 1 85  ? 14.713 -16.458 25.599  1.00  8.61  ? 85   GLY A C   1 
ATOM   688  O  O   . GLY A 1 85  ? 14.460 -16.493 24.384  1.00  9.96  ? 85   GLY A O   1 
ATOM   689  N  N   . ASN A 1 86  ? 13.776 -16.266 26.528  1.00  9.25  ? 86   ASN A N   1 
ATOM   690  C  CA  . ASN A 1 86  ? 12.419 -16.054 26.240  1.00  9.06  ? 86   ASN A CA  1 
ATOM   691  C  C   . ASN A 1 86  ? 11.937 -14.846 26.982  1.00  9.05  ? 86   ASN A C   1 
ATOM   692  O  O   . ASN A 1 86  ? 12.417 -14.600 28.097  1.00  11.25 ? 86   ASN A O   1 
ATOM   693  C  CB  . ASN A 1 86  ? 11.582 -17.267 26.683  1.00  8.91  ? 86   ASN A CB  1 
ATOM   694  C  CG  . ASN A 1 86  ? 11.812 -18.459 25.832  1.00  10.01 ? 86   ASN A CG  1 
ATOM   695  O  OD1 . ASN A 1 86  ? 11.454 -18.433 24.668  1.00  10.66 ? 86   ASN A OD1 1 
ATOM   696  N  ND2 . ASN A 1 86  ? 12.474 -19.471 26.358  1.00  13.04 ? 86   ASN A ND2 1 
ATOM   697  N  N   . VAL A 1 87  ? 10.928 -14.169 26.430  1.00  7.82  ? 87   VAL A N   1 
ATOM   698  C  CA  . VAL A 1 87  ? 10.109 -13.237 27.182  1.00  8.10  ? 87   VAL A CA  1 
ATOM   699  C  C   . VAL A 1 87  ? 8.803  -13.941 27.455  1.00  8.36  ? 87   VAL A C   1 
ATOM   700  O  O   . VAL A 1 87  ? 8.434  -14.876 26.749  1.00  8.64  ? 87   VAL A O   1 
ATOM   701  C  CB  . VAL A 1 87  ? 9.933  -11.915 26.416  1.00  8.96  ? 87   VAL A CB  1 
ATOM   702  C  CG1 . VAL A 1 87  ? 11.274 -11.260 26.206  1.00  10.32 ? 87   VAL A CG1 1 
ATOM   703  C  CG2 . VAL A 1 87  ? 9.268  -12.097 25.088  1.00  10.33 ? 87   VAL A CG2 1 
ATOM   704  N  N   . THR A 1 88  ? 8.045  -13.430 28.409  1.00  8.75  ? 88   THR A N   1 
ATOM   705  C  CA  . THR A 1 88  ? 6.810  -14.066 28.874  1.00  9.90  ? 88   THR A CA  1 
ATOM   706  C  C   . THR A 1 88  ? 5.640  -13.125 28.729  1.00  8.68  ? 88   THR A C   1 
ATOM   707  O  O   . THR A 1 88  ? 5.613  -12.048 29.324  1.00  10.93 ? 88   THR A O   1 
ATOM   708  C  CB  . THR A 1 88  ? 6.892  -14.476 30.325  1.00  11.63 ? 88   THR A CB  1 
ATOM   709  O  OG1 . THR A 1 88  ? 7.990  -15.363 30.444  1.00  13.02 ? 88   THR A OG1 1 
ATOM   710  C  CG2 . THR A 1 88  ? 5.623  -15.184 30.729  1.00  12.38 ? 88   THR A CG2 1 
ATOM   711  N  N   . ALA A 1 89  ? 4.666  -13.519 27.909  1.00  9.10  ? 89   ALA A N   1 
ATOM   712  C  CA  . ALA A 1 89  ? 3.436  -12.788 27.752  1.00  10.16 ? 89   ALA A CA  1 
ATOM   713  C  C   . ALA A 1 89  ? 2.372  -13.347 28.687  1.00  10.10 ? 89   ALA A C   1 
ATOM   714  O  O   . ALA A 1 89  ? 2.192  -14.530 28.772  1.00  10.94 ? 89   ALA A O   1 
ATOM   715  C  CB  . ALA A 1 89  ? 2.969  -12.796 26.314  1.00  10.35 ? 89   ALA A CB  1 
ATOM   716  N  N   . ASP A 1 90  ? 1.611  -12.412 29.227  1.00  10.44 ? 90   ASP A N   1 
ATOM   717  C  CA  . ASP A 1 90  ? 0.490  -12.739 30.049  1.00  11.60 ? 90   ASP A CA  1 
ATOM   718  C  C   . ASP A 1 90  ? -0.781 -12.936 29.215  1.00  10.54 ? 90   ASP A C   1 
ATOM   719  O  O   . ASP A 1 90  ? -0.697 -12.862 27.985  1.00  11.18 ? 90   ASP A O   1 
ATOM   720  C  CB  A ASP A 1 90  ? 0.375  -11.647 31.143  0.59  12.07 ? 90   ASP A CB  1 
ATOM   721  C  CB  B ASP A 1 90  ? 0.336  -11.629 31.079  0.41  12.20 ? 90   ASP A CB  1 
ATOM   722  C  CG  A ASP A 1 90  ? -0.026 -10.266 30.621  0.59  13.58 ? 90   ASP A CG  1 
ATOM   723  C  CG  B ASP A 1 90  ? 1.312  -11.773 32.234  0.41  14.39 ? 90   ASP A CG  1 
ATOM   724  O  OD1 A ASP A 1 90  ? -0.554 -10.158 29.502  0.59  13.74 ? 90   ASP A OD1 1 
ATOM   725  O  OD1 B ASP A 1 90  ? 1.959  -12.853 32.379  0.41  17.84 ? 90   ASP A OD1 1 
ATOM   726  O  OD2 A ASP A 1 90  ? 0.142  -9.253  31.363  0.59  15.74 ? 90   ASP A OD2 1 
ATOM   727  O  OD2 B ASP A 1 90  ? 1.407  -10.798 33.006  0.41  19.42 ? 90   ASP A OD2 1 
ATOM   728  N  N   . LYS A 1 91  ? -1.944 -13.216 29.833  1.00  11.08 ? 91   LYS A N   1 
ATOM   729  C  CA  . LYS A 1 91  ? -3.178 -13.457 29.055  1.00  11.01 ? 91   LYS A CA  1 
ATOM   730  C  C   . LYS A 1 91  ? -3.688 -12.241 28.296  1.00  12.79 ? 91   LYS A C   1 
ATOM   731  O  O   . LYS A 1 91  ? -4.469 -12.403 27.355  1.00  14.93 ? 91   LYS A O   1 
ATOM   732  C  CB  . LYS A 1 91  ? -4.286 -13.955 29.998  1.00  10.19 ? 91   LYS A CB  1 
ATOM   733  C  CG  . LYS A 1 91  ? -4.184 -15.462 30.321  1.00  11.70 ? 91   LYS A CG  1 
ATOM   734  C  CD  . LYS A 1 91  ? -4.706 -16.340 29.144  1.00  12.83 ? 91   LYS A CD  1 
ATOM   735  C  CE  . LYS A 1 91  ? -4.827 -17.753 29.462  1.00  14.89 ? 91   LYS A CE  1 
ATOM   736  N  NZ  . LYS A 1 91  ? -5.360 -18.487 28.299  1.00  16.52 ? 91   LYS A NZ  1 
ATOM   737  N  N   . ASP A 1 92  ? -3.220 -11.057 28.626  1.00  11.12 ? 92   ASP A N   1 
ATOM   738  C  CA  A ASP A 1 92  ? -3.560 -9.859  27.854  0.70  12.27 ? 92   ASP A CA  1 
ATOM   739  C  CA  B ASP A 1 92  ? -3.530 -9.851  27.846  0.30  11.26 ? 92   ASP A CA  1 
ATOM   740  C  C   . ASP A 1 92  ? -2.640 -9.691  26.624  1.00  11.61 ? 92   ASP A C   1 
ATOM   741  O  O   . ASP A 1 92  ? -2.809 -8.742  25.832  1.00  14.27 ? 92   ASP A O   1 
ATOM   742  C  CB  A ASP A 1 92  ? -3.591 -8.606  28.747  0.70  12.98 ? 92   ASP A CB  1 
ATOM   743  C  CB  B ASP A 1 92  ? -3.357 -8.624  28.715  0.30  11.28 ? 92   ASP A CB  1 
ATOM   744  C  CG  A ASP A 1 92  ? -2.239 -8.299  29.463  0.70  15.19 ? 92   ASP A CG  1 
ATOM   745  C  CG  B ASP A 1 92  ? -4.370 -8.556  29.802  0.30  9.97  ? 92   ASP A CG  1 
ATOM   746  O  OD1 A ASP A 1 92  ? -1.228 -8.964  29.212  0.70  15.94 ? 92   ASP A OD1 1 
ATOM   747  O  OD1 B ASP A 1 92  ? -5.404 -9.232  29.664  0.30  10.45 ? 92   ASP A OD1 1 
ATOM   748  O  OD2 A ASP A 1 92  ? -2.178 -7.366  30.315  0.70  16.78 ? 92   ASP A OD2 1 
ATOM   749  O  OD2 B ASP A 1 92  ? -4.125 -7.828  30.788  0.30  10.80 ? 92   ASP A OD2 1 
ATOM   750  N  N   . GLY A 1 93  ? -1.691 -10.584 26.497  1.00  10.72 ? 93   GLY A N   1 
ATOM   751  C  CA  . GLY A 1 93  ? -0.753 -10.575 25.379  1.00  11.68 ? 93   GLY A CA  1 
ATOM   752  C  C   . GLY A 1 93  ? 0.446  -9.640  25.545  1.00  10.85 ? 93   GLY A C   1 
ATOM   753  O  O   . GLY A 1 93  ? 1.162  -9.417  24.582  1.00  11.02 ? 93   GLY A O   1 
ATOM   754  N  N   . VAL A 1 94  ? 0.660  -9.128  26.745  1.00  10.94 ? 94   VAL A N   1 
ATOM   755  C  CA  . VAL A 1 94  ? 1.732  -8.222  27.046  1.00  10.43 ? 94   VAL A CA  1 
ATOM   756  C  C   . VAL A 1 94  ? 2.898  -8.940  27.774  1.00  9.88  ? 94   VAL A C   1 
ATOM   757  O  O   . VAL A 1 94  ? 2.687  -9.656  28.791  1.00  10.52 ? 94   VAL A O   1 
ATOM   758  C  CB  . VAL A 1 94  ? 1.242  -7.028  27.859  1.00  11.64 ? 94   VAL A CB  1 
ATOM   759  C  CG1 . VAL A 1 94  ? 2.368  -6.085  28.105  1.00  13.94 ? 94   VAL A CG1 1 
ATOM   760  C  CG2 . VAL A 1 94  ? 0.046  -6.353  27.146  1.00  13.85 ? 94   VAL A CG2 1 
ATOM   761  N  N   . ALA A 1 95  ? 4.138  -8.746  27.302  1.00  9.45  ? 95   ALA A N   1 
ATOM   762  C  CA  . ALA A 1 95  ? 5.340  -9.169  27.956  1.00  10.50 ? 95   ALA A CA  1 
ATOM   763  C  C   . ALA A 1 95  ? 6.084  -7.971  28.482  1.00  10.28 ? 95   ALA A C   1 
ATOM   764  O  O   . ALA A 1 95  ? 6.468  -7.078  27.737  1.00  13.13 ? 95   ALA A O   1 
ATOM   765  C  CB  . ALA A 1 95  ? 6.204  -9.887  26.966  1.00  11.09 ? 95   ALA A CB  1 
ATOM   766  N  N   . ASP A 1 96  ? 6.258  -7.924  29.787  1.00  10.14 ? 96   ASP A N   1 
ATOM   767  C  CA  . ASP A 1 96  ? 7.065  -6.902  30.393  1.00  10.30 ? 96   ASP A CA  1 
ATOM   768  C  C   . ASP A 1 96  ? 8.463  -7.470  30.429  1.00  10.33 ? 96   ASP A C   1 
ATOM   769  O  O   . ASP A 1 96  ? 8.666  -8.565  30.952  1.00  13.35 ? 96   ASP A O   1 
ATOM   770  C  CB  . ASP A 1 96  ? 6.454  -6.481  31.733  1.00  11.08 ? 96   ASP A CB  1 
ATOM   771  C  CG  A ASP A 1 96  ? 5.232  -5.582  31.508  0.75  12.83 ? 96   ASP A CG  1 
ATOM   772  C  CG  B ASP A 1 96  ? 6.902  -7.386  32.860  0.25  14.06 ? 96   ASP A CG  1 
ATOM   773  O  OD1 A ASP A 1 96  ? 5.217  -4.647  30.664  0.75  14.91 ? 96   ASP A OD1 1 
ATOM   774  O  OD1 B ASP A 1 96  ? 8.043  -7.279  33.357  0.25  19.24 ? 96   ASP A OD1 1 
ATOM   775  O  OD2 A ASP A 1 96  ? 4.250  -5.842  32.213  0.75  18.78 ? 96   ASP A OD2 1 
ATOM   776  O  OD2 B ASP A 1 96  ? 6.060  -8.201  33.274  0.25  16.42 ? 96   ASP A OD2 1 
ATOM   777  N  N   . VAL A 1 97  ? 9.408  -6.781  29.814  1.00  10.80 ? 97   VAL A N   1 
ATOM   778  C  CA  . VAL A 1 97  ? 10.737 -7.321  29.691  1.00  10.79 ? 97   VAL A CA  1 
ATOM   779  C  C   . VAL A 1 97  ? 11.654 -6.684  30.688  1.00  9.66  ? 97   VAL A C   1 
ATOM   780  O  O   . VAL A 1 97  ? 11.684 -5.470  30.836  1.00  9.90  ? 97   VAL A O   1 
ATOM   781  C  CB  . VAL A 1 97  ? 11.280 -7.120  28.274  1.00  11.41 ? 97   VAL A CB  1 
ATOM   782  C  CG1 . VAL A 1 97  ? 12.668 -7.672  28.154  1.00  13.46 ? 97   VAL A CG1 1 
ATOM   783  C  CG2 . VAL A 1 97  ? 10.366 -7.807  27.245  1.00  11.90 ? 97   VAL A CG2 1 
ATOM   784  N  N   A SER A 1 98  ? 12.382 -7.577  31.320  0.60  10.93 ? 98   SER A N   1 
ATOM   785  N  N   B SER A 1 98  ? 12.363 -7.428  31.553  0.40  10.78 ? 98   SER A N   1 
ATOM   786  C  CA  A SER A 1 98  ? 13.308 -7.209  32.297  0.60  10.86 ? 98   SER A CA  1 
ATOM   787  C  CA  B SER A 1 98  ? 13.343 -6.783  32.499  0.40  11.03 ? 98   SER A CA  1 
ATOM   788  C  C   A SER A 1 98  ? 14.407 -8.258  32.334  0.60  10.13 ? 98   SER A C   1 
ATOM   789  C  C   B SER A 1 98  ? 14.501 -7.708  32.910  0.40  11.55 ? 98   SER A C   1 
ATOM   790  O  O   A SER A 1 98  ? 14.230 -9.278  32.947  0.60  11.10 ? 98   SER A O   1 
ATOM   791  O  O   B SER A 1 98  ? 14.472 -8.352  33.968  0.40  12.33 ? 98   SER A O   1 
ATOM   792  C  CB  A SER A 1 98  ? 12.563 -7.076  33.627  0.60  10.53 ? 98   SER A CB  1 
ATOM   793  C  CB  B SER A 1 98  ? 12.680 -6.206  33.752  0.40  10.88 ? 98   SER A CB  1 
ATOM   794  O  OG  A SER A 1 98  ? 13.463 -6.749  34.660  0.60  14.61 ? 98   SER A OG  1 
ATOM   795  O  OG  B SER A 1 98  ? 13.655 -5.481  34.471  0.40  12.64 ? 98   SER A OG  1 
ATOM   796  N  N   A ILE A 1 99  ? 15.563 -7.957  31.761  0.60  10.25 ? 99   ILE A N   1 
ATOM   797  N  N   B ILE A 1 99  ? 15.533 -7.672  32.067  0.40  11.30 ? 99   ILE A N   1 
ATOM   798  C  CA  A ILE A 1 99  ? 16.716 -8.885  31.621  0.60  10.00 ? 99   ILE A CA  1 
ATOM   799  C  CA  B ILE A 1 99  ? 16.609 -8.673  31.922  0.40  11.30 ? 99   ILE A CA  1 
ATOM   800  C  C   A ILE A 1 99  ? 18.003 -8.151  32.080  0.60  9.51  ? 99   ILE A C   1 
ATOM   801  C  C   B ILE A 1 99  ? 17.968 -8.021  32.287  0.40  10.50 ? 99   ILE A C   1 
ATOM   802  O  O   A ILE A 1 99  ? 18.125 -6.973  31.784  0.60  10.03 ? 99   ILE A O   1 
ATOM   803  O  O   B ILE A 1 99  ? 18.104 -6.799  32.179  0.40  10.00 ? 99   ILE A O   1 
ATOM   804  C  CB  A ILE A 1 99  ? 16.847 -9.318  30.101  0.60  8.87  ? 99   ILE A CB  1 
ATOM   805  C  CB  B ILE A 1 99  ? 16.631 -9.245  30.387  0.40  11.88 ? 99   ILE A CB  1 
ATOM   806  C  CG1 A ILE A 1 99  ? 15.806 -10.391 29.799  0.60  10.05 ? 99   ILE A CG1 1 
ATOM   807  C  CG1 B ILE A 1 99  ? 15.338 -10.000 30.028  0.40  12.48 ? 99   ILE A CG1 1 
ATOM   808  C  CG2 A ILE A 1 99  ? 18.231 -9.823  29.763  0.60  10.89 ? 99   ILE A CG2 1 
ATOM   809  C  CG2 B ILE A 1 99  ? 17.836 -10.154 30.083  0.40  12.12 ? 99   ILE A CG2 1 
ATOM   810  C  CD1 A ILE A 1 99  ? 15.654 -10.664 28.272  0.60  9.82  ? 99   ILE A CD1 1 
ATOM   811  C  CD1 B ILE A 1 99  ? 15.132 -10.276 28.501  0.40  12.17 ? 99   ILE A CD1 1 
ATOM   812  N  N   . GLU A 1 100 ? 18.942 -8.796  32.774  1.00  9.64  ? 100  GLU A N   1 
ATOM   813  C  CA  A GLU A 1 100 ? 20.302 -8.318  32.869  0.50  9.46  ? 100  GLU A CA  1 
ATOM   814  C  CA  B GLU A 1 100 ? 20.299 -8.339  32.878  0.50  10.12 ? 100  GLU A CA  1 
ATOM   815  C  C   . GLU A 1 100 ? 21.154 -9.406  32.199  1.00  9.13  ? 100  GLU A C   1 
ATOM   816  O  O   . GLU A 1 100 ? 20.971 -10.574 32.504  1.00  10.49 ? 100  GLU A O   1 
ATOM   817  C  CB  A GLU A 1 100 ? 20.747 -8.090  34.306  0.50  10.53 ? 100  GLU A CB  1 
ATOM   818  C  CB  B GLU A 1 100 ? 20.711 -8.177  34.334  0.50  10.71 ? 100  GLU A CB  1 
ATOM   819  C  CG  A GLU A 1 100 ? 20.053 -6.909  34.981  0.50  12.78 ? 100  GLU A CG  1 
ATOM   820  C  CG  B GLU A 1 100 ? 22.081 -7.593  34.501  0.50  11.35 ? 100  GLU A CG  1 
ATOM   821  C  CD  A GLU A 1 100 ? 20.782 -5.589  34.799  0.50  16.09 ? 100  GLU A CD  1 
ATOM   822  C  CD  B GLU A 1 100 ? 22.433 -7.318  35.932  0.50  14.95 ? 100  GLU A CD  1 
ATOM   823  O  OE1 A GLU A 1 100 ? 21.778 -5.536  34.047  0.50  19.33 ? 100  GLU A OE1 1 
ATOM   824  O  OE1 B GLU A 1 100 ? 21.838 -6.354  36.440  0.50  18.43 ? 100  GLU A OE1 1 
ATOM   825  O  OE2 A GLU A 1 100 ? 20.364 -4.587  35.448  0.50  18.28 ? 100  GLU A OE2 1 
ATOM   826  O  OE2 B GLU A 1 100 ? 23.313 -8.018  36.484  0.50  20.97 ? 100  GLU A OE2 1 
ATOM   827  N  N   . ASP A 1 101 ? 22.052 -9.002  31.313  1.00  8.56  ? 101  ASP A N   1 
ATOM   828  C  CA  . ASP A 1 101 ? 22.885 -9.985  30.627  1.00  8.39  ? 101  ASP A CA  1 
ATOM   829  C  C   . ASP A 1 101 ? 24.330 -9.518  30.582  1.00  8.85  ? 101  ASP A C   1 
ATOM   830  O  O   . ASP A 1 101 ? 24.579 -8.329  30.290  1.00  9.96  ? 101  ASP A O   1 
ATOM   831  C  CB  . ASP A 1 101 ? 22.391 -10.226 29.169  1.00  8.83  ? 101  ASP A CB  1 
ATOM   832  C  CG  . ASP A 1 101 ? 23.006 -11.449 28.555  1.00  9.27  ? 101  ASP A CG  1 
ATOM   833  O  OD1 . ASP A 1 101 ? 22.591 -12.560 28.979  1.00  10.45 ? 101  ASP A OD1 1 
ATOM   834  O  OD2 . ASP A 1 101 ? 23.926 -11.296 27.720  1.00  9.66  ? 101  ASP A OD2 1 
ATOM   835  N  N   . SER A 1 102 ? 25.287 -10.427 30.832  1.00  9.54  ? 102  SER A N   1 
ATOM   836  C  CA  . SER A 1 102 ? 26.693 -10.025 30.896  1.00  10.20 ? 102  SER A CA  1 
ATOM   837  C  C   . SER A 1 102 ? 27.505 -10.495 29.676  1.00  10.44 ? 102  SER A C   1 
ATOM   838  O  O   . SER A 1 102 ? 28.696 -10.298 29.642  1.00  11.28 ? 102  SER A O   1 
ATOM   839  C  CB  . SER A 1 102 ? 27.410 -10.523 32.114  1.00  12.76 ? 102  SER A CB  1 
ATOM   840  O  OG  A SER A 1 102 ? 26.580 -10.989 33.215  0.50  13.63 ? 102  SER A OG  1 
ATOM   841  O  OG  B SER A 1 102 ? 27.138 -11.817 32.310  0.50  9.57  ? 102  SER A OG  1 
ATOM   842  N  N   . VAL A 1 103 ? 26.857 -11.061 28.662  1.00  9.55  ? 103  VAL A N   1 
ATOM   843  C  CA  . VAL A 1 103 ? 27.513 -11.515 27.416  1.00  8.63  ? 103  VAL A CA  1 
ATOM   844  C  C   . VAL A 1 103 ? 27.311 -10.505 26.287  1.00  8.62  ? 103  VAL A C   1 
ATOM   845  O  O   . VAL A 1 103 ? 28.274 -10.205 25.619  1.00  10.40 ? 103  VAL A O   1 
ATOM   846  C  CB  . VAL A 1 103 ? 27.029 -12.912 27.083  1.00  8.83  ? 103  VAL A CB  1 
ATOM   847  C  CG1 . VAL A 1 103 ? 27.638 -13.392 25.794  1.00  9.66  ? 103  VAL A CG1 1 
ATOM   848  C  CG2 . VAL A 1 103 ? 27.388 -13.898 28.200  1.00  10.17 ? 103  VAL A CG2 1 
ATOM   849  N  N   . ILE A 1 104 ? 26.107 -10.030 26.071  1.00  8.79  ? 104  ILE A N   1 
ATOM   850  C  CA  . ILE A 1 104 ? 25.909 -8.960  25.132  1.00  8.40  ? 104  ILE A CA  1 
ATOM   851  C  C   . ILE A 1 104 ? 26.667 -7.712  25.629  1.00  8.80  ? 104  ILE A C   1 
ATOM   852  O  O   . ILE A 1 104 ? 26.935 -7.563  26.826  1.00  10.45 ? 104  ILE A O   1 
ATOM   853  C  CB  . ILE A 1 104 ? 24.430 -8.622  24.896  1.00  8.45  ? 104  ILE A CB  1 
ATOM   854  C  CG1 . ILE A 1 104 ? 23.727 -8.206  26.183  1.00  8.86  ? 104  ILE A CG1 1 
ATOM   855  C  CG2 . ILE A 1 104 ? 23.704 -9.797  24.246  1.00  8.62  ? 104  ILE A CG2 1 
ATOM   856  C  CD1 . ILE A 1 104 ? 22.339 -7.607  25.973  1.00  8.50  ? 104  ILE A CD1 1 
ATOM   857  N  N   . SER A 1 105 ? 27.010 -6.819  24.718  1.00  8.55  ? 105  SER A N   1 
ATOM   858  C  CA  . SER A 1 105 ? 27.597 -5.564  25.010  1.00  8.57  ? 105  SER A CA  1 
ATOM   859  C  C   . SER A 1 105 ? 27.078 -4.518  24.046  1.00  7.71  ? 105  SER A C   1 
ATOM   860  O  O   . SER A 1 105 ? 26.518 -4.830  23.022  1.00  8.60  ? 105  SER A O   1 
ATOM   861  C  CB  . SER A 1 105 ? 29.096 -5.641  24.917  1.00  9.62  ? 105  SER A CB  1 
ATOM   862  O  OG  . SER A 1 105 ? 29.662 -4.470  25.415  1.00  11.29 ? 105  SER A OG  1 
ATOM   863  N  N   . LEU A 1 106 ? 27.236 -3.250  24.424  1.00  9.54  ? 106  LEU A N   1 
ATOM   864  C  CA  . LEU A 1 106 ? 26.968 -2.105  23.567  1.00  10.64 ? 106  LEU A CA  1 
ATOM   865  C  C   . LEU A 1 106 ? 28.256 -1.483  23.009  1.00  11.77 ? 106  LEU A C   1 
ATOM   866  O  O   . LEU A 1 106 ? 28.191 -0.446  22.338  1.00  13.49 ? 106  LEU A O   1 
ATOM   867  C  CB  . LEU A 1 106 ? 26.110 -1.069  24.281  1.00  10.31 ? 106  LEU A CB  1 
ATOM   868  C  CG  . LEU A 1 106 ? 24.830 -1.600  24.893  1.00  9.81  ? 106  LEU A CG  1 
ATOM   869  C  CD1 . LEU A 1 106 ? 24.046 -0.434  25.548  1.00  11.40 ? 106  LEU A CD1 1 
ATOM   870  C  CD2 . LEU A 1 106 ? 23.931 -2.334  23.900  1.00  10.50 ? 106  LEU A CD2 1 
ATOM   871  N  N   . SER A 1 107 ? 29.379 -2.202  23.082  1.00  13.26 ? 107  SER A N   1 
ATOM   872  C  CA  . SER A 1 107 ? 30.607 -1.867  22.334  1.00  15.38 ? 107  SER A CA  1 
ATOM   873  C  C   . SER A 1 107 ? 31.446 -3.121  22.078  1.00  16.21 ? 107  SER A C   1 
ATOM   874  O  O   . SER A 1 107 ? 31.203 -4.181  22.644  1.00  15.01 ? 107  SER A O   1 
ATOM   875  C  CB  . SER A 1 107 ? 31.459 -0.833  23.038  1.00  17.02 ? 107  SER A CB  1 
ATOM   876  O  OG  . SER A 1 107 ? 31.891 -1.309  24.290  1.00  22.52 ? 107  SER A OG  1 
ATOM   877  N  N   . GLY A 1 108 ? 32.402 -2.998  21.178  1.00  15.56 ? 108  GLY A N   1 
ATOM   878  C  CA  . GLY A 1 108 ? 33.336 -4.072  20.895  1.00  16.40 ? 108  GLY A CA  1 
ATOM   879  C  C   . GLY A 1 108 ? 32.791 -5.261  20.124  1.00  15.13 ? 108  GLY A C   1 
ATOM   880  O  O   . GLY A 1 108 ? 31.767 -5.175  19.474  1.00  14.60 ? 108  GLY A O   1 
ATOM   881  N  N   . ASP A 1 109 ? 33.504 -6.386  20.207  1.00  14.71 ? 109  ASP A N   1 
ATOM   882  C  CA  . ASP A 1 109 ? 33.203 -7.615  19.469  1.00  14.29 ? 109  ASP A CA  1 
ATOM   883  C  C   . ASP A 1 109 ? 31.892 -8.285  19.847  1.00  13.35 ? 109  ASP A C   1 
ATOM   884  O  O   . ASP A 1 109 ? 31.261 -8.941  19.026  1.00  14.68 ? 109  ASP A O   1 
ATOM   885  C  CB  . ASP A 1 109 ? 34.389 -8.573  19.691  1.00  15.93 ? 109  ASP A CB  1 
ATOM   886  C  CG  . ASP A 1 109 ? 34.360 -9.808  18.818  1.00  18.13 ? 109  ASP A CG  1 
ATOM   887  O  OD1 . ASP A 1 109 ? 34.055 -9.699  17.612  1.00  22.25 ? 109  ASP A OD1 1 
ATOM   888  O  OD2 . ASP A 1 109 ? 34.715 -10.896 19.327  1.00  21.05 ? 109  ASP A OD2 1 
ATOM   889  N  N   . HIS A 1 110 ? 31.434 -8.067  21.095  1.00  11.30 ? 110  HIS A N   1 
ATOM   890  C  CA  . HIS A 1 110 ? 30.111 -8.570  21.533  1.00  10.96 ? 110  HIS A CA  1 
ATOM   891  C  C   . HIS A 1 110 ? 28.988 -7.546  21.299  1.00  10.16 ? 110  HIS A C   1 
ATOM   892  O  O   . HIS A 1 110 ? 27.874 -7.737  21.770  1.00  10.24 ? 110  HIS A O   1 
ATOM   893  C  CB  . HIS A 1 110 ? 30.084 -8.946  23.019  1.00  10.23 ? 110  HIS A CB  1 
ATOM   894  C  CG  . HIS A 1 110 ? 31.148 -9.906  23.499  1.00  12.73 ? 110  HIS A CG  1 
ATOM   895  N  ND1 . HIS A 1 110 ? 31.029 -10.514 24.734  1.00  14.18 ? 110  HIS A ND1 1 
ATOM   896  C  CD2 . HIS A 1 110 ? 32.357 -10.284 23.015  1.00  12.42 ? 110  HIS A CD2 1 
ATOM   897  C  CE1 . HIS A 1 110 ? 32.073 -11.309 24.930  1.00  14.53 ? 110  HIS A CE1 1 
ATOM   898  N  NE2 . HIS A 1 110 ? 32.923 -11.151 23.934  1.00  12.78 ? 110  HIS A NE2 1 
HETATM 899  N  N   . CSO A 1 111 ? 29.317 -6.447  20.610  1.00  10.14 ? 111  CSO A N   1 
HETATM 900  C  CA  . CSO A 1 111 ? 28.381 -5.367  20.399  1.00  10.84 ? 111  CSO A CA  1 
HETATM 901  C  CB  . CSO A 1 111 ? 29.065 -4.181  19.713  1.00  12.14 ? 111  CSO A CB  1 
HETATM 902  S  SG  . CSO A 1 111 ? 27.967 -2.709  19.740  1.00  15.11 ? 111  CSO A SG  1 
HETATM 903  C  C   . CSO A 1 111 ? 27.150 -5.773  19.575  1.00  9.78  ? 111  CSO A C   1 
HETATM 904  O  O   . CSO A 1 111 ? 27.306 -6.362  18.491  1.00  10.71 ? 111  CSO A O   1 
HETATM 905  O  OD  . CSO A 1 111 ? 28.826 -1.374  18.786  1.00  20.43 ? 111  CSO A OD  1 
ATOM   906  N  N   . ILE A 1 112 ? 25.949 -5.409  20.054  1.00  7.90  ? 112  ILE A N   1 
ATOM   907  C  CA  . ILE A 1 112 ? 24.701 -5.697  19.394  1.00  8.38  ? 112  ILE A CA  1 
ATOM   908  C  C   . ILE A 1 112 ? 24.093 -4.489  18.669  1.00  7.11  ? 112  ILE A C   1 
ATOM   909  O  O   . ILE A 1 112 ? 23.092 -4.630  18.044  1.00  7.33  ? 112  ILE A O   1 
ATOM   910  C  CB  . ILE A 1 112 ? 23.692 -6.315  20.382  1.00  8.17  ? 112  ILE A CB  1 
ATOM   911  C  CG1 . ILE A 1 112 ? 23.349 -5.344  21.523  1.00  9.17  ? 112  ILE A CG1 1 
ATOM   912  C  CG2 . ILE A 1 112 ? 24.231 -7.632  20.934  1.00  8.39  ? 112  ILE A CG2 1 
ATOM   913  C  CD1 . ILE A 1 112 ? 22.208 -5.842  22.419  1.00  8.40  ? 112  ILE A CD1 1 
ATOM   914  N  N   . ILE A 1 113 ? 24.689 -3.327  18.808  1.00  7.44  ? 113  ILE A N   1 
ATOM   915  C  CA  . ILE A 1 113 ? 24.208 -2.146  18.059  1.00  8.20  ? 113  ILE A CA  1 
ATOM   916  C  C   . ILE A 1 113 ? 24.343 -2.397  16.548  1.00  7.93  ? 113  ILE A C   1 
ATOM   917  O  O   . ILE A 1 113 ? 25.352 -2.927  16.090  1.00  9.80  ? 113  ILE A O   1 
ATOM   918  C  CB  . ILE A 1 113 ? 24.885 -0.862  18.556  1.00  9.62  ? 113  ILE A CB  1 
ATOM   919  C  CG1 . ILE A 1 113 ? 24.376 -0.536  20.017  1.00  11.29 ? 113  ILE A CG1 1 
ATOM   920  C  CG2 . ILE A 1 113 ? 24.645 0.287   17.607  1.00  8.68  ? 113  ILE A CG2 1 
ATOM   921  C  CD1 . ILE A 1 113 ? 24.971 0.536   20.684  1.00  12.81 ? 113  ILE A CD1 1 
ATOM   922  N  N   . GLY A 1 114 ? 23.252 -2.098  15.869  1.00  7.07  ? 114  GLY A N   1 
ATOM   923  C  CA  . GLY A 1 114 ? 23.230 -2.279  14.423  1.00  7.24  ? 114  GLY A CA  1 
ATOM   924  C  C   . GLY A 1 114 ? 22.828 -3.684  14.024  1.00  7.38  ? 114  GLY A C   1 
ATOM   925  O  O   . GLY A 1 114 ? 22.799 -3.998  12.822  1.00  8.36  ? 114  GLY A O   1 
ATOM   926  N  N   . ARG A 1 115 ? 22.464 -4.532  14.983  1.00  7.18  ? 115  ARG A N   1 
ATOM   927  C  CA  . ARG A 1 115 ? 21.965 -5.877  14.771  1.00  6.94  ? 115  ARG A CA  1 
ATOM   928  C  C   . ARG A 1 115 ? 20.478 -5.918  14.970  1.00  6.59  ? 115  ARG A C   1 
ATOM   929  O  O   . ARG A 1 115 ? 19.884 -4.894  15.247  1.00  8.64  ? 115  ARG A O   1 
ATOM   930  C  CB  . ARG A 1 115 ? 22.763 -6.873  15.525  1.00  7.21  ? 115  ARG A CB  1 
ATOM   931  C  CG  . ARG A 1 115 ? 24.244 -6.674  15.283  1.00  8.63  ? 115  ARG A CG  1 
ATOM   932  C  CD  . ARG A 1 115 ? 25.108 -7.763  15.871  1.00  9.04  ? 115  ARG A CD  1 
ATOM   933  N  NE  . ARG A 1 115 ? 26.523 -7.473  15.665  1.00  10.28 ? 115  ARG A NE  1 
ATOM   934  C  CZ  . ARG A 1 115 ? 27.256 -7.796  14.583  1.00  10.54 ? 115  ARG A CZ  1 
ATOM   935  N  NH1 . ARG A 1 115 ? 26.765 -8.429  13.555  1.00  9.72  ? 115  ARG A NH1 1 
ATOM   936  N  NH2 . ARG A 1 115 ? 28.536 -7.537  14.547  1.00  10.68 ? 115  ARG A NH2 1 
ATOM   937  N  N   . THR A 1 116 ? 19.844 -7.046  14.751  1.00  6.85  ? 116  THR A N   1 
ATOM   938  C  CA  . THR A 1 116 ? 18.386 -7.105  14.811  1.00  6.92  ? 116  THR A CA  1 
ATOM   939  C  C   . THR A 1 116 ? 17.928 -7.865  16.050  1.00  6.25  ? 116  THR A C   1 
ATOM   940  O  O   . THR A 1 116 ? 18.362 -8.980  16.292  1.00  8.22  ? 116  THR A O   1 
ATOM   941  C  CB  . THR A 1 116 ? 17.773 -7.784  13.610  1.00  7.13  ? 116  THR A CB  1 
ATOM   942  O  OG1 . THR A 1 116 ? 18.081 -7.002  12.434  1.00  8.88  ? 116  THR A OG1 1 
ATOM   943  C  CG2 . THR A 1 116 ? 16.259 -7.934  13.627  1.00  7.49  ? 116  THR A CG2 1 
ATOM   944  N  N   . LEU A 1 117 ? 17.025 -7.271  16.815  1.00  6.44  ? 117  LEU A N   1 
ATOM   945  C  CA  . LEU A 1 117 ? 16.362 -7.975  17.906  1.00  6.50  ? 117  LEU A CA  1 
ATOM   946  C  C   . LEU A 1 117 ? 15.074 -8.580  17.379  1.00  6.94  ? 117  LEU A C   1 
ATOM   947  O  O   . LEU A 1 117 ? 14.358 -7.921  16.654  1.00  7.51  ? 117  LEU A O   1 
ATOM   948  C  CB  . LEU A 1 117 ? 16.073 -6.957  19.047  1.00  7.32  ? 117  LEU A CB  1 
ATOM   949  C  CG  . LEU A 1 117 ? 15.479 -7.539  20.324  1.00  7.65  ? 117  LEU A CG  1 
ATOM   950  C  CD1 . LEU A 1 117 ? 16.518 -8.384  21.040  1.00  8.97  ? 117  LEU A CD1 1 
ATOM   951  C  CD2 . LEU A 1 117 ? 15.027 -6.390  21.204  1.00  8.85  ? 117  LEU A CD2 1 
ATOM   952  N  N   . VAL A 1 118 ? 14.813 -9.847  17.708  1.00  6.97  ? 118  VAL A N   1 
ATOM   953  C  CA  . VAL A 1 118 ? 13.667 -10.557 17.163  1.00  6.93  ? 118  VAL A CA  1 
ATOM   954  C  C   . VAL A 1 118 ? 12.891 -11.222 18.334  1.00  7.17  ? 118  VAL A C   1 
ATOM   955  O  O   . VAL A 1 118 ? 13.510 -11.840 19.207  1.00  7.25  ? 118  VAL A O   1 
ATOM   956  C  CB  . VAL A 1 118 ? 14.114 -11.667 16.192  1.00  7.65  ? 118  VAL A CB  1 
ATOM   957  C  CG1 . VAL A 1 118 ? 12.930 -12.428 15.624  1.00  8.78  ? 118  VAL A CG1 1 
ATOM   958  C  CG2 . VAL A 1 118 ? 14.972 -11.118 15.067  1.00  7.73  ? 118  VAL A CG2 1 
ATOM   959  N  N   . VAL A 1 119 ? 11.588 -11.117 18.296  1.00  7.35  ? 119  VAL A N   1 
ATOM   960  C  CA  . VAL A 1 119 ? 10.716 -11.907 19.156  1.00  7.26  ? 119  VAL A CA  1 
ATOM   961  C  C   . VAL A 1 119 ? 9.976  -12.944 18.284  1.00  7.91  ? 119  VAL A C   1 
ATOM   962  O  O   . VAL A 1 119 ? 9.472  -12.647 17.197  1.00  8.74  ? 119  VAL A O   1 
ATOM   963  C  CB  . VAL A 1 119 ? 9.739  -11.018 20.028  1.00  7.38  ? 119  VAL A CB  1 
ATOM   964  C  CG1 . VAL A 1 119 ? 8.817  -10.236 19.125  1.00  9.54  ? 119  VAL A CG1 1 
ATOM   965  C  CG2 . VAL A 1 119 ? 8.947  -11.907 20.975  1.00  8.17  ? 119  VAL A CG2 1 
ATOM   966  N  N   . HIS A 1 120 ? 9.910  -14.164 18.822  1.00  7.75  ? 120  HIS A N   1 
ATOM   967  C  CA  . HIS A 1 120 ? 9.476  -15.328 18.085  1.00  7.72  ? 120  HIS A CA  1 
ATOM   968  C  C   . HIS A 1 120 ? 8.071  -15.831 18.476  1.00  7.84  ? 120  HIS A C   1 
ATOM   969  O  O   . HIS A 1 120 ? 7.526  -15.549 19.539  1.00  9.73  ? 120  HIS A O   1 
ATOM   970  C  CB  . HIS A 1 120 ? 10.468 -16.442 18.301  1.00  10.11 ? 120  HIS A CB  1 
ATOM   971  C  CG  . HIS A 1 120 ? 11.683 -16.343 17.473  1.00  8.56  ? 120  HIS A CG  1 
ATOM   972  N  ND1 . HIS A 1 120 ? 11.687 -16.901 16.213  1.00  9.18  ? 120  HIS A ND1 1 
ATOM   973  C  CD2 . HIS A 1 120 ? 12.896 -15.745 17.644  1.00  7.65  ? 120  HIS A CD2 1 
ATOM   974  C  CE1 . HIS A 1 120 ? 12.838 -16.648 15.648  1.00  10.57 ? 120  HIS A CE1 1 
ATOM   975  N  NE2 . HIS A 1 120 ? 13.578 -15.941 16.467  1.00  8.96  ? 120  HIS A NE2 1 
ATOM   976  N  N   . GLU A 1 121 ? 7.532  -16.629 17.574  1.00  9.40  ? 121  GLU A N   1 
ATOM   977  C  CA  . GLU A 1 121 ? 6.232  -17.291 17.715  1.00  10.79 ? 121  GLU A CA  1 
ATOM   978  C  C   . GLU A 1 121 ? 6.109  -18.225 18.882  1.00  11.29 ? 121  GLU A C   1 
ATOM   979  O  O   . GLU A 1 121 ? 5.065  -18.184 19.546  1.00  11.55 ? 121  GLU A O   1 
ATOM   980  C  CB  . GLU A 1 121 ? 5.972  -18.098 16.424  1.00  11.95 ? 121  GLU A CB  1 
ATOM   981  C  CG  . GLU A 1 121 ? 4.790  -18.913 16.344  1.00  13.25 ? 121  GLU A CG  1 
ATOM   982  C  CD  . GLU A 1 121 ? 4.847  -19.998 15.192  1.00  15.48 ? 121  GLU A CD  1 
ATOM   983  O  OE1 . GLU A 1 121 ? 5.874  -20.237 14.502  1.00  17.68 ? 121  GLU A OE1 1 
ATOM   984  O  OE2 . GLU A 1 121 ? 3.786  -20.641 15.010  1.00  21.13 ? 121  GLU A OE2 1 
ATOM   985  N  N   . LYS A 1 122 ? 7.161  -19.018 19.080  1.00  11.16 ? 122  LYS A N   1 
ATOM   986  C  CA  . LYS A 1 122 ? 7.187  -20.122 20.052  1.00  13.19 ? 122  LYS A CA  1 
ATOM   987  C  C   . LYS A 1 122 ? 8.241  -19.875 21.079  1.00  10.37 ? 122  LYS A C   1 
ATOM   988  O  O   . LYS A 1 122 ? 9.011  -18.926 20.951  1.00  10.91 ? 122  LYS A O   1 
ATOM   989  C  CB  . LYS A 1 122 ? 7.406  -21.517 19.347  1.00  13.22 ? 122  LYS A CB  1 
ATOM   990  C  CG  A LYS A 1 122 ? 6.862  -21.681 17.954  0.70  18.85 ? 122  LYS A CG  1 
ATOM   991  C  CG  B LYS A 1 122 ? 6.610  -21.697 18.055  0.30  14.73 ? 122  LYS A CG  1 
ATOM   992  C  CD  A LYS A 1 122 ? 7.022  -23.131 17.450  0.70  17.93 ? 122  LYS A CD  1 
ATOM   993  C  CD  B LYS A 1 122 ? 6.453  -23.171 17.609  0.30  13.70 ? 122  LYS A CD  1 
ATOM   994  C  CE  A LYS A 1 122 ? 6.034  -24.072 18.134  0.70  22.10 ? 122  LYS A CE  1 
ATOM   995  C  CE  B LYS A 1 122 ? 7.587  -23.650 16.698  0.30  13.60 ? 122  LYS A CE  1 
ATOM   996  N  NZ  A LYS A 1 122 ? 6.288  -25.468 17.686  0.70  24.76 ? 122  LYS A NZ  1 
ATOM   997  N  NZ  B LYS A 1 122 ? 7.237  -24.901 15.963  0.10  13.08 ? 122  LYS A NZ  1 
ATOM   998  N  N   . ALA A 1 123 ? 8.290  -20.754 22.063  1.00  10.78 ? 123  ALA A N   1 
ATOM   999  C  CA  . ALA A 1 123 ? 9.371  -20.724 23.029  1.00  9.32  ? 123  ALA A CA  1 
ATOM   1000 C  C   . ALA A 1 123 ? 10.675 -21.168 22.402  1.00  9.06  ? 123  ALA A C   1 
ATOM   1001 O  O   . ALA A 1 123 ? 10.732 -22.070 21.614  1.00  11.04 ? 123  ALA A O   1 
ATOM   1002 C  CB  . ALA A 1 123 ? 9.043  -21.597 24.224  1.00  11.03 ? 123  ALA A CB  1 
ATOM   1003 N  N   . ASP A 1 124 ? 11.763 -20.543 22.811  1.00  9.02  ? 124  ASP A N   1 
ATOM   1004 C  CA  . ASP A 1 124 ? 13.106 -21.038 22.556  1.00  9.16  ? 124  ASP A CA  1 
ATOM   1005 C  C   . ASP A 1 124 ? 13.331 -22.145 23.590  1.00  9.04  ? 124  ASP A C   1 
ATOM   1006 O  O   . ASP A 1 124 ? 13.118 -21.929 24.811  1.00  9.97  ? 124  ASP A O   1 
ATOM   1007 C  CB  . ASP A 1 124 ? 14.094 -19.855 22.735  1.00  9.64  ? 124  ASP A CB  1 
ATOM   1008 C  CG  . ASP A 1 124 ? 15.540 -20.206 22.532  1.00  9.01  ? 124  ASP A CG  1 
ATOM   1009 O  OD1 . ASP A 1 124 ? 15.897 -21.391 22.607  1.00  10.04 ? 124  ASP A OD1 1 
ATOM   1010 O  OD2 . ASP A 1 124 ? 16.312 -19.254 22.194  1.00  10.15 ? 124  ASP A OD2 1 
ATOM   1011 N  N   . ASP A 1 125 ? 13.708 -23.321 23.143  1.00  9.33  ? 125  ASP A N   1 
ATOM   1012 C  CA  . ASP A 1 125 ? 13.922 -24.470 24.068  1.00  10.37 ? 125  ASP A CA  1 
ATOM   1013 C  C   . ASP A 1 125 ? 15.301 -24.451 24.675  1.00  9.93  ? 125  ASP A C   1 
ATOM   1014 O  O   . ASP A 1 125 ? 15.658 -25.367 25.421  1.00  11.31 ? 125  ASP A O   1 
ATOM   1015 C  CB  . ASP A 1 125 ? 13.693 -25.819 23.369  1.00  11.56 ? 125  ASP A CB  1 
ATOM   1016 C  CG  . ASP A 1 125 ? 14.630 -26.092 22.171  1.00  11.42 ? 125  ASP A CG  1 
ATOM   1017 O  OD1 . ASP A 1 125 ? 15.784 -25.639 22.186  1.00  11.25 ? 125  ASP A OD1 1 
ATOM   1018 O  OD2 . ASP A 1 125 ? 14.198 -26.889 21.273  1.00  12.34 ? 125  ASP A OD2 1 
ATOM   1019 N  N   . LEU A 1 126 ? 16.082 -23.388 24.424  1.00  10.99 ? 126  LEU A N   1 
ATOM   1020 C  CA  . LEU A 1 126 ? 17.324 -23.132 25.153  1.00  10.71 ? 126  LEU A CA  1 
ATOM   1021 C  C   . LEU A 1 126 ? 18.363 -24.208 24.957  1.00  10.38 ? 126  LEU A C   1 
ATOM   1022 O  O   . LEU A 1 126 ? 19.271 -24.358 25.774  1.00  12.08 ? 126  LEU A O   1 
ATOM   1023 C  CB  . LEU A 1 126 ? 17.136 -22.816 26.647  1.00  11.14 ? 126  LEU A CB  1 
ATOM   1024 C  CG  . LEU A 1 126 ? 16.005 -21.826 26.958  1.00  10.75 ? 126  LEU A CG  1 
ATOM   1025 C  CD1 . LEU A 1 126 ? 15.962 -21.551 28.422  1.00  13.86 ? 126  LEU A CD1 1 
ATOM   1026 C  CD2 . LEU A 1 126 ? 16.202 -20.506 26.222  1.00  12.34 ? 126  LEU A CD2 1 
ATOM   1027 N  N   A GLY A 1 127 ? 18.256 -24.903 23.833  0.80  11.11 ? 127  GLY A N   1 
ATOM   1028 N  N   B GLY A 1 127 ? 18.298 -24.902 23.819  0.20  10.27 ? 127  GLY A N   1 
ATOM   1029 C  CA  A GLY A 1 127 ? 19.159 -25.994 23.544  0.80  11.28 ? 127  GLY A CA  1 
ATOM   1030 C  CA  B GLY A 1 127 ? 19.293 -25.915 23.464  0.20  9.78  ? 127  GLY A CA  1 
ATOM   1031 C  C   A GLY A 1 127 ? 18.801 -27.335 24.170  0.80  11.35 ? 127  GLY A C   1 
ATOM   1032 C  C   B GLY A 1 127 ? 18.939 -27.290 23.994  0.20  9.07  ? 127  GLY A C   1 
ATOM   1033 O  O   A GLY A 1 127 ? 19.640 -28.244 24.164  0.80  13.77 ? 127  GLY A O   1 
ATOM   1034 O  O   B GLY A 1 127 ? 19.270 -28.320 23.408  0.20  9.19  ? 127  GLY A O   1 
ATOM   1035 N  N   A LYS A 1 128 ? 17.551 -27.465 24.634  0.80  10.99 ? 128  LYS A N   1 
ATOM   1036 N  N   B LYS A 1 128 ? 18.211 -27.310 25.090  0.20  8.19  ? 128  LYS A N   1 
ATOM   1037 C  CA  A LYS A 1 128 ? 17.093 -28.597 25.469  0.80  11.97 ? 128  LYS A CA  1 
ATOM   1038 C  CA  B LYS A 1 128 ? 18.002 -28.541 25.808  0.20  7.58  ? 128  LYS A CA  1 
ATOM   1039 C  C   A LYS A 1 128 ? 15.745 -29.112 24.906  0.80  11.03 ? 128  LYS A C   1 
ATOM   1040 C  C   B LYS A 1 128 ? 16.820 -29.330 25.229  0.20  7.02  ? 128  LYS A C   1 
ATOM   1041 O  O   A LYS A 1 128 ? 14.779 -29.450 25.658  0.80  14.21 ? 128  LYS A O   1 
ATOM   1042 O  O   B LYS A 1 128 ? 16.188 -30.150 25.920  0.20  6.51  ? 128  LYS A O   1 
ATOM   1043 C  CB  A LYS A 1 128 ? 16.979 -28.205 26.978  0.80  11.96 ? 128  LYS A CB  1 
ATOM   1044 C  CB  B LYS A 1 128 ? 17.830 -28.186 27.274  0.20  8.01  ? 128  LYS A CB  1 
ATOM   1045 C  CG  A LYS A 1 128 ? 18.293 -27.758 27.732  0.80  16.80 ? 128  LYS A CG  1 
ATOM   1046 C  CG  B LYS A 1 128 ? 19.063 -27.449 27.804  0.20  9.55  ? 128  LYS A CG  1 
ATOM   1047 C  CD  A LYS A 1 128 ? 18.098 -27.641 29.283  0.80  18.88 ? 128  LYS A CD  1 
ATOM   1048 C  CD  B LYS A 1 128 ? 20.250 -28.417 27.974  0.20  10.31 ? 128  LYS A CD  1 
ATOM   1049 C  CE  A LYS A 1 128 ? 19.186 -27.076 30.267  0.82  21.94 ? 128  LYS A CE  1 
ATOM   1050 C  CE  B LYS A 1 128 ? 21.500 -27.818 28.644  0.20  10.40 ? 128  LYS A CE  1 
ATOM   1051 N  NZ  A LYS A 1 128 ? 18.591 -26.557 31.534  0.20  20.25 ? 128  LYS A NZ  1 
ATOM   1052 N  NZ  B LYS A 1 128 ? 22.484 -28.868 28.995  0.20  11.93 ? 128  LYS A NZ  1 
ATOM   1053 N  N   A GLY A 1 129 ? 15.672 -29.208 23.578  0.80  10.66 ? 129  GLY A N   1 
ATOM   1054 N  N   B GLY A 1 129 ? 16.562 -29.102 23.943  0.20  7.26  ? 129  GLY A N   1 
ATOM   1055 C  CA  A GLY A 1 129 ? 14.459 -29.682 22.927  0.80  11.56 ? 129  GLY A CA  1 
ATOM   1056 C  CA  B GLY A 1 129 ? 15.465 -29.770 23.255  0.20  8.09  ? 129  GLY A CA  1 
ATOM   1057 C  C   A GLY A 1 129 ? 14.535 -31.111 22.389  0.80  10.89 ? 129  GLY A C   1 
ATOM   1058 C  C   B GLY A 1 129 ? 15.860 -31.106 22.644  0.20  8.62  ? 129  GLY A C   1 
ATOM   1059 O  O   A GLY A 1 129 ? 13.521 -31.663 21.995  0.80  13.25 ? 129  GLY A O   1 
ATOM   1060 O  O   B GLY A 1 129 ? 17.011 -31.507 22.691  0.20  9.03  ? 129  GLY A O   1 
ATOM   1061 N  N   A GLY A 1 130 ? 15.727 -31.683 22.318  0.80  9.87  ? 130  GLY A N   1 
ATOM   1062 N  N   B GLY A 1 130 ? 14.902 -31.785 22.036  0.20  8.17  ? 130  GLY A N   1 
ATOM   1063 C  CA  A GLY A 1 130 ? 15.843 -33.050 21.867  0.80  10.48 ? 130  GLY A CA  1 
ATOM   1064 C  CA  B GLY A 1 130 ? 15.129 -33.146 21.580  0.20  8.85  ? 130  GLY A CA  1 
ATOM   1065 C  C   A GLY A 1 130 ? 15.915 -33.322 20.375  0.80  10.93 ? 130  GLY A C   1 
ATOM   1066 C  C   B GLY A 1 130 ? 15.997 -33.394 20.347  0.20  9.77  ? 130  GLY A C   1 
ATOM   1067 O  O   A GLY A 1 130 ? 15.572 -34.426 19.932  0.80  11.76 ? 130  GLY A O   1 
ATOM   1068 O  O   B GLY A 1 130 ? 16.350 -34.557 20.090  0.20  8.97  ? 130  GLY A O   1 
ATOM   1069 N  N   . ASN A 1 131 ? 16.377 -32.350 19.596  1.00  11.33 ? 131  ASN A N   1 
ATOM   1070 C  CA  . ASN A 1 131 ? 16.741 -32.548 18.210  1.00  11.62 ? 131  ASN A CA  1 
ATOM   1071 C  C   . ASN A 1 131 ? 17.904 -31.644 17.845  1.00  13.19 ? 131  ASN A C   1 
ATOM   1072 O  O   . ASN A 1 131 ? 18.345 -30.811 18.629  1.00  13.74 ? 131  ASN A O   1 
ATOM   1073 C  CB  . ASN A 1 131 ? 15.511 -32.316 17.312  1.00  13.52 ? 131  ASN A CB  1 
ATOM   1074 C  CG  . ASN A 1 131 ? 15.044 -30.848 17.303  1.00  13.74 ? 131  ASN A CG  1 
ATOM   1075 O  OD1 . ASN A 1 131 ? 15.696 -29.984 17.856  1.00  15.33 ? 131  ASN A OD1 1 
ATOM   1076 N  ND2 . ASN A 1 131 ? 13.923 -30.578 16.636  1.00  17.25 ? 131  ASN A ND2 1 
ATOM   1077 N  N   . GLU A 1 132 ? 18.397 -31.798 16.626  1.00  13.92 ? 132  GLU A N   1 
ATOM   1078 C  CA  . GLU A 1 132 ? 19.591 -31.087 16.164  1.00  13.71 ? 132  GLU A CA  1 
ATOM   1079 C  C   . GLU A 1 132 ? 19.320 -29.579 16.118  1.00  12.85 ? 132  GLU A C   1 
ATOM   1080 O  O   . GLU A 1 132 ? 20.163 -28.750 16.490  1.00  14.70 ? 132  GLU A O   1 
ATOM   1081 C  CB  . GLU A 1 132 ? 20.047 -31.591 14.773  1.00  14.02 ? 132  GLU A CB  1 
ATOM   1082 C  CG  . GLU A 1 132 ? 21.176 -30.749 14.113  0.70  15.64 ? 132  GLU A CG  1 
ATOM   1083 C  CD  . GLU A 1 132 ? 21.732 -31.182 12.744  0.70  18.34 ? 132  GLU A CD  1 
ATOM   1084 O  OE1 . GLU A 1 132 ? 21.106 -31.931 11.984  0.70  22.28 ? 132  GLU A OE1 1 
ATOM   1085 O  OE2 . GLU A 1 132 ? 22.848 -30.700 12.428  0.70  23.27 ? 132  GLU A OE2 1 
ATOM   1086 N  N   . GLU A 1 133 ? 18.142 -29.213 15.674  1.00  12.36 ? 133  GLU A N   1 
ATOM   1087 C  CA  . GLU A 1 133 ? 17.790 -27.787 15.527  1.00  13.13 ? 133  GLU A CA  1 
ATOM   1088 C  C   . GLU A 1 133 ? 17.836 -27.067 16.881  1.00  12.52 ? 133  GLU A C   1 
ATOM   1089 O  O   . GLU A 1 133 ? 18.093 -25.870 16.974  1.00  13.39 ? 133  GLU A O   1 
ATOM   1090 C  CB  . GLU A 1 133 ? 16.429 -27.689 14.895  1.00  13.08 ? 133  GLU A CB  1 
ATOM   1091 C  CG  . GLU A 1 133 ? 16.025 -26.241 14.639  1.00  14.76 ? 133  GLU A CG  1 
ATOM   1092 C  CD  . GLU A 1 133 ? 14.778 -26.066 13.812  0.60  16.28 ? 133  GLU A CD  1 
ATOM   1093 O  OE1 . GLU A 1 133 ? 14.209 -27.042 13.301  0.60  17.93 ? 133  GLU A OE1 1 
ATOM   1094 O  OE2 . GLU A 1 133 ? 14.347 -24.880 13.745  0.60  20.09 ? 133  GLU A OE2 1 
ATOM   1095 N  N   . SER A 1 134 ? 17.599 -27.797 17.971  1.00  13.07 ? 134  SER A N   1 
ATOM   1096 C  CA  . SER A 1 134 ? 17.597 -27.195 19.309  1.00  11.72 ? 134  SER A CA  1 
ATOM   1097 C  C   . SER A 1 134 ? 18.941 -26.505 19.607  1.00  11.85 ? 134  SER A C   1 
ATOM   1098 O  O   . SER A 1 134 ? 18.977 -25.420 20.211  1.00  12.19 ? 134  SER A O   1 
ATOM   1099 C  CB  . SER A 1 134 ? 17.285 -28.284 20.304  1.00  11.19 ? 134  SER A CB  1 
ATOM   1100 O  OG  . SER A 1 134 ? 17.266 -27.694 21.603  1.00  12.90 ? 134  SER A OG  1 
ATOM   1101 N  N   . THR A 1 135 ? 20.041 -27.133 19.152  1.00  13.91 ? 135  THR A N   1 
ATOM   1102 C  CA  . THR A 1 135 ? 21.421 -26.689 19.339  1.00  14.48 ? 135  THR A CA  1 
ATOM   1103 C  C   . THR A 1 135 ? 21.889 -25.602 18.376  1.00  12.34 ? 135  THR A C   1 
ATOM   1104 O  O   . THR A 1 135 ? 23.024 -25.130 18.468  1.00  13.85 ? 135  THR A O   1 
ATOM   1105 C  CB  . THR A 1 135 ? 22.482 -27.888 19.033  1.00  15.82 ? 135  THR A CB  1 
ATOM   1106 O  OG1 . THR A 1 135 ? 22.581 -28.126 17.610  1.00  20.52 ? 135  THR A OG1 1 
ATOM   1107 C  CG2 . THR A 1 135 ? 22.076 -29.080 19.671  1.00  16.91 ? 135  THR A CG2 1 
ATOM   1108 N  N   . LYS A 1 136 ? 20.985 -25.186 17.493  1.00  12.83 ? 136  LYS A N   1 
ATOM   1109 C  CA  . LYS A 1 136 ? 21.287 -24.168 16.462  1.00  12.05 ? 136  LYS A CA  1 
ATOM   1110 C  C   . LYS A 1 136 ? 20.394 -22.944 16.664  1.00  10.99 ? 136  LYS A C   1 
ATOM   1111 O  O   . LYS A 1 136 ? 20.881 -21.819 16.736  1.00  12.85 ? 136  LYS A O   1 
ATOM   1112 C  CB  . LYS A 1 136 ? 21.125 -24.747 15.038  1.00  13.69 ? 136  LYS A CB  1 
ATOM   1113 C  CG  . LYS A 1 136 ? 22.260 -25.724 14.727  1.00  16.34 ? 136  LYS A CG  1 
ATOM   1114 C  CD  . LYS A 1 136 ? 22.123 -26.478 13.439  1.00  18.02 ? 136  LYS A CD  1 
ATOM   1115 C  CE  . LYS A 1 136 ? 23.325 -27.343 13.244  1.00  22.26 ? 136  LYS A CE  1 
ATOM   1116 N  NZ  . LYS A 1 136 ? 23.722 -27.331 11.828  1.00  25.87 ? 136  LYS A NZ  1 
ATOM   1117 N  N   . THR A 1 137 ? 19.091 -23.153 16.749  1.00  11.16 ? 137  THR A N   1 
ATOM   1118 C  CA  . THR A 1 137 ? 18.149 -22.087 16.772  1.00  10.50 ? 137  THR A CA  1 
ATOM   1119 C  C   . THR A 1 137 ? 17.274 -22.090 18.009  1.00  10.22 ? 137  THR A C   1 
ATOM   1120 O  O   . THR A 1 137 ? 16.700 -21.064 18.330  1.00  10.39 ? 137  THR A O   1 
ATOM   1121 C  CB  . THR A 1 137 ? 17.198 -22.068 15.565  1.00  11.76 ? 137  THR A CB  1 
ATOM   1122 O  OG1 . THR A 1 137 ? 16.265 -23.132 15.697  1.00  11.54 ? 137  THR A OG1 1 
ATOM   1123 C  CG2 . THR A 1 137 ? 17.930 -22.190 14.289  1.00  13.71 ? 137  THR A CG2 1 
ATOM   1124 N  N   . GLY A 1 138 ? 17.037 -23.246 18.650  1.00  9.41  ? 138  GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 138 ? 16.127 -23.316 19.753  1.00  10.48 ? 138  GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 138 ? 14.707 -23.548 19.383  1.00  8.83  ? 138  GLY A C   1 
ATOM   1127 O  O   . GLY A 1 138 ? 13.823 -23.568 20.261  1.00  10.66 ? 138  GLY A O   1 
ATOM   1128 N  N   . ASN A 1 139 ? 14.415 -23.764 18.079  1.00  10.40 ? 139  ASN A N   1 
ATOM   1129 C  CA  . ASN A 1 139 ? 13.047 -24.136 17.667  1.00  11.11 ? 139  ASN A CA  1 
ATOM   1130 C  C   . ASN A 1 139 ? 11.935 -23.171 18.087  1.00  11.05 ? 139  ASN A C   1 
ATOM   1131 O  O   . ASN A 1 139 ? 10.844 -23.565 18.429  1.00  11.60 ? 139  ASN A O   1 
ATOM   1132 C  CB  . ASN A 1 139 ? 12.687 -25.523 18.236  1.00  12.68 ? 139  ASN A CB  1 
ATOM   1133 C  CG  . ASN A 1 139 ? 13.545 -26.631 17.630  1.00  14.50 ? 139  ASN A CG  1 
ATOM   1134 O  OD1 . ASN A 1 139 ? 13.556 -26.870 16.435  1.00  17.18 ? 139  ASN A OD1 1 
ATOM   1135 N  ND2 . ASN A 1 139 ? 14.271 -27.308 18.474  1.00  14.52 ? 139  ASN A ND2 1 
ATOM   1136 N  N   . ALA A 1 140 ? 12.189 -21.867 17.990  1.00  10.97 ? 140  ALA A N   1 
ATOM   1137 C  CA  . ALA A 1 140 ? 11.208 -20.888 18.438  1.00  10.12 ? 140  ALA A CA  1 
ATOM   1138 C  C   . ALA A 1 140 ? 10.289 -20.372 17.335  1.00  10.32 ? 140  ALA A C   1 
ATOM   1139 O  O   . ALA A 1 140 ? 9.491  -19.496 17.578  1.00  10.87 ? 140  ALA A O   1 
ATOM   1140 C  CB  . ALA A 1 140 ? 11.895 -19.745 19.107  1.00  10.86 ? 140  ALA A CB  1 
ATOM   1141 N  N   . GLY A 1 141 ? 10.291 -21.016 16.151  1.00  11.44 ? 141  GLY A N   1 
ATOM   1142 C  CA  . GLY A 1 141 ? 9.241  -20.727 15.184  1.00  11.31 ? 141  GLY A CA  1 
ATOM   1143 C  C   . GLY A 1 141 ? 9.471  -19.399 14.480  1.00  10.12 ? 141  GLY A C   1 
ATOM   1144 O  O   . GLY A 1 141 ? 10.561 -18.842 14.456  1.00  11.47 ? 141  GLY A O   1 
ATOM   1145 N  N   . SER A 1 142 ? 8.398  -18.921 13.897  1.00  10.63 ? 142  SER A N   1 
ATOM   1146 C  CA  . SER A 1 142 ? 8.394  -17.722 13.083  1.00  11.36 ? 142  SER A CA  1 
ATOM   1147 C  C   . SER A 1 142 ? 8.924  -16.482 13.836  1.00  9.69  ? 142  SER A C   1 
ATOM   1148 O  O   . SER A 1 142 ? 8.833  -16.382 15.057  1.00  10.63 ? 142  SER A O   1 
ATOM   1149 C  CB  . SER A 1 142 ? 6.944  -17.469 12.609  1.00  12.28 ? 142  SER A CB  1 
ATOM   1150 O  OG  A SER A 1 142 ? 6.638  -16.187 13.041  0.50  17.58 ? 142  SER A OG  1 
ATOM   1151 O  OG  B SER A 1 142 ? 6.585  -18.581 11.784  0.50  12.85 ? 142  SER A OG  1 
ATOM   1152 N  N   . ARG A 1 143 ? 9.404  -15.516 13.082  1.00  8.90  ? 143  ARG A N   1 
ATOM   1153 C  CA  . ARG A 1 143 ? 9.817  -14.235 13.578  1.00  8.91  ? 143  ARG A CA  1 
ATOM   1154 C  C   . ARG A 1 143 ? 8.614  -13.311 13.546  1.00  8.76  ? 143  ARG A C   1 
ATOM   1155 O  O   . ARG A 1 143 ? 8.214  -12.821 12.522  1.00  12.17 ? 143  ARG A O   1 
ATOM   1156 C  CB  . ARG A 1 143 ? 10.973 -13.680 12.725  1.00  8.31  ? 143  ARG A CB  1 
ATOM   1157 C  CG  . ARG A 1 143 ? 12.155 -14.636 12.708  1.00  9.38  ? 143  ARG A CG  1 
ATOM   1158 C  CD  . ARG A 1 143 ? 13.272 -14.131 11.846  1.00  9.98  ? 143  ARG A CD  1 
ATOM   1159 N  NE  . ARG A 1 143 ? 14.340 -15.128 11.813  1.00  9.77  ? 143  ARG A NE  1 
ATOM   1160 C  CZ  . ARG A 1 143 ? 15.440 -15.095 11.081  1.00  10.42 ? 143  ARG A CZ  1 
ATOM   1161 N  NH1 . ARG A 1 143 ? 15.728 -14.033 10.355  1.00  13.46 ? 143  ARG A NH1 1 
ATOM   1162 N  NH2 . ARG A 1 143 ? 16.307 -16.095 11.153  1.00  10.89 ? 143  ARG A NH2 1 
ATOM   1163 N  N   . LEU A 1 144 ? 8.027  -12.983 14.684  1.00  8.75  ? 144  LEU A N   1 
ATOM   1164 C  CA  . LEU A 1 144 ? 6.835  -12.196 14.717  1.00  9.16  ? 144  LEU A CA  1 
ATOM   1165 C  C   . LEU A 1 144 ? 7.050  -10.704 14.609  1.00  9.30  ? 144  LEU A C   1 
ATOM   1166 O  O   . LEU A 1 144 ? 6.242  -9.978  14.043  1.00  11.64 ? 144  LEU A O   1 
ATOM   1167 C  CB  . LEU A 1 144 ? 6.027  -12.456 15.996  1.00  11.06 ? 144  LEU A CB  1 
ATOM   1168 C  CG  . LEU A 1 144 ? 5.623  -13.891 16.219  1.00  12.88 ? 144  LEU A CG  1 
ATOM   1169 C  CD1 . LEU A 1 144 ? 4.572  -13.954 17.345  1.00  16.60 ? 144  LEU A CD1 1 
ATOM   1170 C  CD2 . LEU A 1 144 ? 5.014  -14.537 15.005  1.00  17.64 ? 144  LEU A CD2 1 
ATOM   1171 N  N   . ALA A 1 145 ? 8.128  -10.224 15.174  1.00  8.12  ? 145  ALA A N   1 
ATOM   1172 C  CA  . ALA A 1 145 ? 8.457  -8.821  15.109  1.00  7.80  ? 145  ALA A CA  1 
ATOM   1173 C  C   . ALA A 1 145 ? 9.944  -8.642  15.327  1.00  7.48  ? 145  ALA A C   1 
ATOM   1174 O  O   . ALA A 1 145 ? 10.577 -9.463  15.972  1.00  8.72  ? 145  ALA A O   1 
ATOM   1175 C  CB  . ALA A 1 145 ? 7.668  -8.039  16.203  1.00  9.02  ? 145  ALA A CB  1 
ATOM   1176 N  N   . CYS A 1 146 ? 10.497 -7.533  14.841  1.00  8.02  ? 146  CYS A N   1 
ATOM   1177 C  CA  . CYS A 1 146 ? 11.888 -7.281  14.945  1.00  8.14  ? 146  CYS A CA  1 
ATOM   1178 C  C   . CYS A 1 146 ? 12.168 -5.801  14.703  1.00  7.07  ? 146  CYS A C   1 
ATOM   1179 O  O   . CYS A 1 146 ? 11.300 -5.107  14.216  1.00  8.54  ? 146  CYS A O   1 
ATOM   1180 C  CB  . CYS A 1 146 ? 12.679 -8.097  13.905  1.00  8.97  ? 146  CYS A CB  1 
ATOM   1181 S  SG  . CYS A 1 146 ? 12.280 -7.777  12.207  1.00  12.34 ? 146  CYS A SG  1 
ATOM   1182 N  N   . GLY A 1 147 ? 13.394 -5.420  14.996  1.00  7.43  ? 147  GLY A N   1 
ATOM   1183 C  CA  . GLY A 1 147 ? 13.907 -4.097  14.660  1.00  7.45  ? 147  GLY A CA  1 
ATOM   1184 C  C   . GLY A 1 147 ? 15.418 -4.050  14.775  1.00  6.62  ? 147  GLY A C   1 
ATOM   1185 O  O   . GLY A 1 147 ? 16.016 -4.924  15.390  1.00  7.12  ? 147  GLY A O   1 
ATOM   1186 N  N   . VAL A 1 148 ? 16.014 -2.983  14.278  1.00  7.24  ? 148  VAL A N   1 
ATOM   1187 C  CA  . VAL A 1 148 ? 17.421 -2.785  14.341  1.00  7.02  ? 148  VAL A CA  1 
ATOM   1188 C  C   . VAL A 1 148 ? 17.737 -2.037  15.653  1.00  6.65  ? 148  VAL A C   1 
ATOM   1189 O  O   . VAL A 1 148 ? 17.070 -1.075  16.046  1.00  9.04  ? 148  VAL A O   1 
ATOM   1190 C  CB  . VAL A 1 148 ? 17.936 -1.981  13.125  1.00  6.98  ? 148  VAL A CB  1 
ATOM   1191 C  CG1 . VAL A 1 148 ? 19.366 -1.802  13.149  1.00  8.07  ? 148  VAL A CG1 1 
ATOM   1192 C  CG2 . VAL A 1 148 ? 17.487 -2.670  11.788  1.00  8.86  ? 148  VAL A CG2 1 
ATOM   1193 N  N   . ILE A 1 149 ? 18.768 -2.506  16.333  1.00  6.63  ? 149  ILE A N   1 
ATOM   1194 C  CA  . ILE A 1 149 ? 19.150 -1.900  17.616  1.00  7.68  ? 149  ILE A CA  1 
ATOM   1195 C  C   . ILE A 1 149 ? 19.949 -0.660  17.330  1.00  7.53  ? 149  ILE A C   1 
ATOM   1196 O  O   . ILE A 1 149 ? 21.013 -0.739  16.675  1.00  8.62  ? 149  ILE A O   1 
ATOM   1197 C  CB  . ILE A 1 149 ? 19.936 -2.957  18.433  1.00  7.85  ? 149  ILE A CB  1 
ATOM   1198 C  CG1 . ILE A 1 149 ? 19.061 -4.183  18.726  1.00  7.60  ? 149  ILE A CG1 1 
ATOM   1199 C  CG2 . ILE A 1 149 ? 20.443 -2.326  19.727  1.00  7.69  ? 149  ILE A CG2 1 
ATOM   1200 C  CD1 . ILE A 1 149 ? 19.866 -5.326  19.333  1.00  9.80  ? 149  ILE A CD1 1 
ATOM   1201 N  N   . GLY A 1 150 ? 19.472 0.482   17.831  1.00  6.91  ? 150  GLY A N   1 
ATOM   1202 C  CA  . GLY A 1 150 ? 20.094 1.735   17.556  1.00  7.53  ? 150  GLY A CA  1 
ATOM   1203 C  C   . GLY A 1 150 ? 20.718 2.387   18.746  1.00  7.29  ? 150  GLY A C   1 
ATOM   1204 O  O   . GLY A 1 150 ? 20.311 2.097   19.895  1.00  9.21  ? 150  GLY A O   1 
ATOM   1205 N  N   . ILE A 1 151 ? 21.654 3.271   18.535  1.00  7.54  ? 151  ILE A N   1 
ATOM   1206 C  CA  . ILE A 1 151 ? 22.253 4.059   19.622  1.00  7.74  ? 151  ILE A CA  1 
ATOM   1207 C  C   . ILE A 1 151 ? 21.253 5.037   20.124  1.00  7.74  ? 151  ILE A C   1 
ATOM   1208 O  O   . ILE A 1 151 ? 20.577 5.734   19.377  1.00  8.32  ? 151  ILE A O   1 
ATOM   1209 C  CB  . ILE A 1 151 ? 23.419 4.832   19.082  1.00  8.57  ? 151  ILE A CB  1 
ATOM   1210 C  CG1 . ILE A 1 151 ? 24.506 3.891   18.536  1.00  11.40 ? 151  ILE A CG1 1 
ATOM   1211 C  CG2 . ILE A 1 151 ? 24.033 5.844   20.005  1.00  11.90 ? 151  ILE A CG2 1 
ATOM   1212 C  CD1 . ILE A 1 151 ? 25.499 4.621   17.713  1.00  12.30 ? 151  ILE A CD1 1 
ATOM   1213 N  N   . ALA A 1 152 ? 21.201 5.144   21.458  1.00  8.61  ? 152  ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 152 ? 20.291 6.041   22.116  1.00  8.74  ? 152  ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 152 ? 21.042 7.111   22.893  1.00  9.85  ? 152  ALA A C   1 
ATOM   1216 O  O   . ALA A 1 152 ? 22.215 6.976   23.188  1.00  11.06 ? 152  ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 152 ? 19.342 5.218   23.079  1.00  9.50  ? 152  ALA A CB  1 
ATOM   1218 N  N   . GLN A 1 153 ? 20.333 8.162   23.245  1.00  10.00 ? 153  GLN A N   1 
ATOM   1219 C  CA  . GLN A 1 153 ? 20.902 9.308   23.960  1.00  11.97 ? 153  GLN A CA  1 
ATOM   1220 C  C   . GLN A 1 153 ? 21.303 8.988   25.330  1.00  14.17 ? 153  GLN A C   1 
ATOM   1221 O  O   . GLN A 1 153 ? 20.574 8.272   25.955  1.00  16.41 ? 153  GLN A O   1 
ATOM   1222 C  CB  . GLN A 1 153 ? 19.885 10.437  23.989  1.00  12.19 ? 153  GLN A CB  1 
ATOM   1223 C  CG  . GLN A 1 153 ? 20.368 11.771  24.541  1.00  12.09 ? 153  GLN A CG  1 
ATOM   1224 C  CD  . GLN A 1 153 ? 19.248 12.804  24.404  1.00  14.68 ? 153  GLN A CD  1 
ATOM   1225 O  OE1 . GLN A 1 153 ? 18.575 12.866  23.372  1.00  15.37 ? 153  GLN A OE1 1 
ATOM   1226 N  NE2 . GLN A 1 153 ? 19.079 13.666  25.412  1.00  15.71 ? 153  GLN A NE2 1 
ATOM   1227 O  OXT . GLN A 1 153 ? 22.355 9.548   25.707  1.00  17.72 ? 153  GLN A OXT 1 
ATOM   1228 N  N   . ALA B 1 1   ? 34.962 -4.552  2.543   1.00  26.85 ? 1    ALA F N   1 
ATOM   1229 C  CA  . ALA B 1 1   ? 34.984 -5.301  3.813   1.00  25.75 ? 1    ALA F CA  1 
ATOM   1230 C  C   . ALA B 1 1   ? 33.647 -5.030  4.471   1.00  25.10 ? 1    ALA F C   1 
ATOM   1231 O  O   . ALA B 1 1   ? 32.825 -5.936  4.583   1.00  26.95 ? 1    ALA F O   1 
ATOM   1232 C  CB  . ALA B 1 1   ? 36.152 -4.858  4.690   1.00  26.09 ? 1    ALA F CB  1 
ATOM   1233 N  N   . THR B 1 2   ? 33.381 -3.777  4.845   1.00  22.92 ? 2    THR F N   1 
ATOM   1234 C  CA  . THR B 1 2   ? 32.195 -3.492  5.709   1.00  19.39 ? 2    THR F CA  1 
ATOM   1235 C  C   . THR B 1 2   ? 30.982 -3.092  4.842   1.00  14.53 ? 2    THR F C   1 
ATOM   1236 O  O   . THR B 1 2   ? 31.115 -2.320  3.864   1.00  14.21 ? 2    THR F O   1 
ATOM   1237 C  CB  . THR B 1 2   ? 32.446 -2.401  6.866   1.00  21.81 ? 2    THR F CB  1 
ATOM   1238 O  OG1 . THR B 1 2   ? 33.702 -2.596  7.510   1.00  28.57 ? 2    THR F OG1 1 
ATOM   1239 C  CG2 . THR B 1 2   ? 31.449 -2.507  7.932   1.00  22.43 ? 2    THR F CG2 1 
ATOM   1240 N  N   . LYS B 1 3   ? 29.786 -3.552  5.248   1.00  11.46 ? 3    LYS F N   1 
ATOM   1241 C  CA  . LYS B 1 3   ? 28.569 -3.207  4.595   1.00  11.19 ? 3    LYS F CA  1 
ATOM   1242 C  C   . LYS B 1 3   ? 27.488 -2.879  5.615   1.00  9.05  ? 3    LYS F C   1 
ATOM   1243 O  O   . LYS B 1 3   ? 27.448 -3.456  6.704   1.00  9.88  ? 3    LYS F O   1 
ATOM   1244 C  CB  . LYS B 1 3   ? 28.145 -4.339  3.677   1.00  11.86 ? 3    LYS F CB  1 
ATOM   1245 C  CG  A LYS B 1 3   ? 29.010 -4.606  2.522   0.70  15.05 ? 3    LYS F CG  1 
ATOM   1246 C  CG  B LYS B 1 3   ? 29.178 -4.555  2.555   0.30  12.26 ? 3    LYS F CG  1 
ATOM   1247 C  CD  A LYS B 1 3   ? 28.292 -5.595  1.614   0.70  13.11 ? 3    LYS F CD  1 
ATOM   1248 C  CD  B LYS B 1 3   ? 29.102 -5.932  1.902   0.30  10.94 ? 3    LYS F CD  1 
ATOM   1249 C  CE  A LYS B 1 3   ? 29.034 -5.792  0.332   0.70  16.55 ? 3    LYS F CE  1 
ATOM   1250 C  CE  B LYS B 1 3   ? 30.029 -6.022  0.655   0.30  11.41 ? 3    LYS F CE  1 
ATOM   1251 N  NZ  A LYS B 1 3   ? 28.183 -6.605  -0.593  0.40  17.39 ? 3    LYS F NZ  1 
ATOM   1252 N  NZ  B LYS B 1 3   ? 29.363 -6.741  -0.465  0.30  11.33 ? 3    LYS F NZ  1 
ATOM   1253 N  N   . ALA B 1 4   ? 26.621 -1.974  5.229   1.00  7.86  ? 4    ALA F N   1 
ATOM   1254 C  CA  . ALA B 1 4   ? 25.475 -1.610  6.025   1.00  7.93  ? 4    ALA F CA  1 
ATOM   1255 C  C   . ALA B 1 4   ? 24.255 -1.350  5.209   1.00  7.95  ? 4    ALA F C   1 
ATOM   1256 O  O   . ALA B 1 4   ? 24.384 -1.267  3.945   1.00  8.95  ? 4    ALA F O   1 
ATOM   1257 C  CB  . ALA B 1 4   ? 25.787 -0.432  6.950   1.00  8.14  ? 4    ALA F CB  1 
ATOM   1258 N  N   . VAL B 1 5   ? 23.058 -1.313  5.741   1.00  7.68  ? 5    VAL F N   1 
ATOM   1259 C  CA  . VAL B 1 5   ? 21.833 -1.171  5.020   1.00  7.96  ? 5    VAL F CA  1 
ATOM   1260 C  C   . VAL B 1 5   ? 20.837 -0.427  5.877   1.00  8.90  ? 5    VAL F C   1 
ATOM   1261 O  O   . VAL B 1 5   ? 20.867 -0.495  7.140   1.00  8.80  ? 5    VAL F O   1 
ATOM   1262 C  CB  . VAL B 1 5   ? 21.351 -2.571  4.540   1.00  9.15  ? 5    VAL F CB  1 
ATOM   1263 C  CG1 . VAL B 1 5   ? 20.856 -3.435  5.725   1.00  11.13 ? 5    VAL F CG1 1 
ATOM   1264 C  CG2 . VAL B 1 5   ? 20.285 -2.418  3.399   1.00  10.69 ? 5    VAL F CG2 1 
ATOM   1265 N  N   . CYS B 1 6   ? 19.897 0.219   5.232   1.00  8.70  ? 6    CYS F N   1 
ATOM   1266 C  CA  . CYS B 1 6   ? 18.867 0.984   5.884   1.00  7.74  ? 6    CYS F CA  1 
ATOM   1267 C  C   . CYS B 1 6   ? 17.550 0.967   5.099   1.00  8.26  ? 6    CYS F C   1 
ATOM   1268 O  O   . CYS B 1 6   ? 17.562 1.235   3.864   1.00  10.50 ? 6    CYS F O   1 
ATOM   1269 C  CB  . CYS B 1 6   ? 19.333 2.432   6.131   1.00  9.43  ? 6    CYS F CB  1 
ATOM   1270 S  SG  . CYS B 1 6   ? 18.169 3.452   6.996   1.00  10.16 ? 6    CYS F SG  1 
ATOM   1271 N  N   . VAL B 1 7   ? 16.425 0.654   5.736   1.00  8.20  ? 7    VAL F N   1 
ATOM   1272 C  CA  . VAL B 1 7   ? 15.109 0.763   5.124   1.00  9.60  ? 7    VAL F CA  1 
ATOM   1273 C  C   . VAL B 1 7   ? 14.493 2.067   5.557   1.00  9.63  ? 7    VAL F C   1 
ATOM   1274 O  O   . VAL B 1 7   ? 14.350 2.324   6.748   1.00  10.27 ? 7    VAL F O   1 
ATOM   1275 C  CB  . VAL B 1 7   ? 14.180 -0.357  5.571   1.00  10.07 ? 7    VAL F CB  1 
ATOM   1276 C  CG1 . VAL B 1 7   ? 12.800 -0.229  4.929   1.00  14.42 ? 7    VAL F CG1 1 
ATOM   1277 C  CG2 . VAL B 1 7   ? 14.786 -1.641  5.203   1.00  12.19 ? 7    VAL F CG2 1 
ATOM   1278 N  N   . LEU B 1 8   ? 14.175 2.929   4.629   1.00  10.44 ? 8    LEU F N   1 
ATOM   1279 C  CA  . LEU B 1 8   ? 13.501 4.216   4.922   1.00  10.45 ? 8    LEU F CA  1 
ATOM   1280 C  C   . LEU B 1 8   ? 12.014 4.010   4.795   1.00  12.58 ? 8    LEU F C   1 
ATOM   1281 O  O   . LEU B 1 8   ? 11.542 3.524   3.750   1.00  12.96 ? 8    LEU F O   1 
ATOM   1282 C  CB  . LEU B 1 8   ? 13.966 5.254   3.942   1.00  10.87 ? 8    LEU F CB  1 
ATOM   1283 C  CG  . LEU B 1 8   ? 15.428 5.678   3.987   1.00  11.38 ? 8    LEU F CG  1 
ATOM   1284 C  CD1 . LEU B 1 8   ? 15.752 6.556   2.762   1.00  11.60 ? 8    LEU F CD1 1 
ATOM   1285 C  CD2 . LEU B 1 8   ? 15.796 6.338   5.227   1.00  12.92 ? 8    LEU F CD2 1 
ATOM   1286 N  N   . LYS B 1 9   ? 11.268 4.387   5.818   1.00  12.54 ? 9    LYS F N   1 
ATOM   1287 C  CA  . LYS B 1 9   ? 9.815  4.314   5.785   1.00  14.95 ? 9    LYS F CA  1 
ATOM   1288 C  C   . LYS B 1 9   ? 9.253  5.560   6.338   1.00  15.58 ? 9    LYS F C   1 
ATOM   1289 O  O   . LYS B 1 9   ? 9.779  6.033   7.336   1.00  13.82 ? 9    LYS F O   1 
ATOM   1290 C  CB  . LYS B 1 9   ? 9.329  3.210   6.696   1.00  16.22 ? 9    LYS F CB  1 
ATOM   1291 C  CG  A LYS B 1 9   ? 9.320  1.861   6.004   0.70  18.24 ? 9    LYS F CG  1 
ATOM   1292 C  CG  B LYS B 1 9   ? 8.376  2.163   6.156   0.30  15.36 ? 9    LYS F CG  1 
ATOM   1293 C  CD  A LYS B 1 9   ? 8.752  0.763   6.860   0.70  18.78 ? 9    LYS F CD  1 
ATOM   1294 C  CD  B LYS B 1 9   ? 7.658  1.526   7.367   0.30  13.85 ? 9    LYS F CD  1 
ATOM   1295 C  CE  A LYS B 1 9   ? 9.279  -0.571  6.420   0.70  21.64 ? 9    LYS F CE  1 
ATOM   1296 C  CE  B LYS B 1 9   ? 6.159  1.361   7.202   0.30  14.02 ? 9    LYS F CE  1 
ATOM   1297 N  NZ  A LYS B 1 9   ? 10.602 -0.775  7.053   0.70  22.39 ? 9    LYS F NZ  1 
ATOM   1298 N  NZ  B LYS B 1 9   ? 5.503  1.219   8.552   0.30  16.41 ? 9    LYS F NZ  1 
ATOM   1299 N  N   A GLY B 1 10  ? 8.066  5.989   5.886   0.50  17.50 ? 10   GLY F N   1 
ATOM   1300 N  N   B GLY B 1 10  ? 8.369  6.133   5.510   0.40  12.14 ? 10   GLY F N   1 
ATOM   1301 C  CA  A GLY B 1 10  ? 7.359  7.168   6.465   0.50  18.15 ? 10   GLY F CA  1 
ATOM   1302 C  CA  B GLY B 1 10  ? 7.488  7.214   5.915   0.40  10.22 ? 10   GLY F CA  1 
ATOM   1303 C  C   A GLY B 1 10  ? 6.038  7.032   7.264   0.50  18.64 ? 10   GLY F C   1 
ATOM   1304 C  C   B GLY B 1 10  ? 6.155  7.273   5.190   0.40  9.76  ? 10   GLY F C   1 
ATOM   1305 O  O   A GLY B 1 10  ? 5.596  5.930   7.611   0.50  19.45 ? 10   GLY F O   1 
ATOM   1306 O  O   B GLY B 1 10  ? 5.911  6.550   4.218   0.40  8.32  ? 10   GLY F O   1 
ATOM   1307 N  N   A ASP B 1 11  ? 5.411  8.179   7.559   0.50  19.57 ? 11   ASP F N   1 
ATOM   1308 N  N   B ASP B 1 11  ? 5.289  8.164   5.649   0.40  9.70  ? 11   ASP F N   1 
ATOM   1309 C  CA  A ASP B 1 11  ? 3.999  8.248   7.992   0.50  19.65 ? 11   ASP F CA  1 
ATOM   1310 C  CA  B ASP B 1 11  ? 3.973  8.295   5.042   0.40  10.57 ? 11   ASP F CA  1 
ATOM   1311 C  C   A ASP B 1 11  ? 3.155  8.454   6.727   0.50  20.09 ? 11   ASP F C   1 
ATOM   1312 C  C   B ASP B 1 11  ? 4.058  8.740   3.576   0.40  10.13 ? 11   ASP F C   1 
ATOM   1313 O  O   A ASP B 1 11  ? 1.918  8.435   6.771   0.50  21.66 ? 11   ASP F O   1 
ATOM   1314 O  O   B ASP B 1 11  ? 4.929  9.529   3.207   0.40  12.23 ? 11   ASP F O   1 
ATOM   1315 C  CB  A ASP B 1 11  ? 3.784  9.368   9.047   0.50  20.58 ? 11   ASP F CB  1 
ATOM   1316 C  CB  B ASP B 1 11  ? 3.083  9.258   5.853   0.40  10.97 ? 11   ASP F CB  1 
ATOM   1317 C  CG  A ASP B 1 11  ? 2.480  9.211   9.861   0.50  21.90 ? 11   ASP F CG  1 
ATOM   1318 C  CG  B ASP B 1 11  ? 2.682  8.700   7.212   0.40  14.36 ? 11   ASP F CG  1 
ATOM   1319 O  OD1 A ASP B 1 11  ? 1.367  9.399   9.315   0.50  25.83 ? 11   ASP F OD1 1 
ATOM   1320 O  OD1 B ASP B 1 11  ? 2.824  7.479   7.449   0.40  17.71 ? 11   ASP F OD1 1 
ATOM   1321 O  OD2 A ASP B 1 11  ? 2.567  8.939   11.080  0.50  27.98 ? 11   ASP F OD2 1 
ATOM   1322 O  OD2 B ASP B 1 11  ? 2.199  9.510   8.037   0.40  18.93 ? 11   ASP F OD2 1 
ATOM   1323 N  N   A GLY B 1 12  ? 3.850  8.641   5.601   0.50  19.81 ? 12   GLY F N   1 
ATOM   1324 N  N   B GLY B 1 12  ? 3.126  8.230   2.777   0.40  10.16 ? 12   GLY F N   1 
ATOM   1325 C  CA  A GLY B 1 12  ? 3.254  8.687   4.269   0.50  19.06 ? 12   GLY F CA  1 
ATOM   1326 C  CA  B GLY B 1 12  ? 3.066  8.535   1.371   0.40  12.19 ? 12   GLY F CA  1 
ATOM   1327 C  C   A GLY B 1 12  ? 3.929  7.637   3.403   0.50  18.66 ? 12   GLY F C   1 
ATOM   1328 C  C   B GLY B 1 12  ? 3.974  7.492   0.811   0.40  13.56 ? 12   GLY F C   1 
ATOM   1329 O  O   A GLY B 1 12  ? 4.651  6.771   3.916   0.50  20.54 ? 12   GLY F O   1 
ATOM   1330 O  O   B GLY B 1 12  ? 5.128  7.771   0.553   0.40  16.28 ? 12   GLY F O   1 
ATOM   1331 N  N   A PRO B 1 13  ? 3.708  7.673   2.086   0.50  18.22 ? 13   PRO F N   1 
ATOM   1332 N  N   B PRO B 1 13  ? 3.486  6.256   0.595   0.40  13.40 ? 13   PRO F N   1 
ATOM   1333 C  CA  A PRO B 1 13  ? 4.223  6.533   1.290   0.50  16.90 ? 13   PRO F CA  1 
ATOM   1334 C  CA  B PRO B 1 13  ? 4.611  5.612   1.202   0.40  14.03 ? 13   PRO F CA  1 
ATOM   1335 C  C   A PRO B 1 13  ? 5.611  6.705   0.621   0.50  15.74 ? 13   PRO F C   1 
ATOM   1336 C  C   B PRO B 1 13  ? 5.856  6.268   0.624   0.40  14.10 ? 13   PRO F C   1 
ATOM   1337 O  O   A PRO B 1 13  ? 5.747  6.596   -0.588  0.50  16.32 ? 13   PRO F O   1 
ATOM   1338 O  O   B PRO B 1 13  ? 6.112  6.121   -0.570  0.40  15.71 ? 13   PRO F O   1 
ATOM   1339 C  CB  A PRO B 1 13  ? 3.099  6.322   0.249   0.50  16.39 ? 13   PRO F CB  1 
ATOM   1340 C  CB  B PRO B 1 13  ? 4.444  4.135   0.824   0.40  13.35 ? 13   PRO F CB  1 
ATOM   1341 C  CG  A PRO B 1 13  ? 2.279  7.626   0.242   0.50  15.58 ? 13   PRO F CG  1 
ATOM   1342 C  CG  B PRO B 1 13  ? 3.425  4.121   -0.283  0.40  13.74 ? 13   PRO F CG  1 
ATOM   1343 C  CD  A PRO B 1 13  ? 2.934  8.593   1.251   0.50  18.21 ? 13   PRO F CD  1 
ATOM   1344 C  CD  B PRO B 1 13  ? 2.579  5.333   -0.110  0.40  13.39 ? 13   PRO F CD  1 
ATOM   1345 N  N   . VAL B 1 14  ? 6.614  7.016   1.438   1.00  16.16 ? 14   VAL F N   1 
ATOM   1346 C  CA  . VAL B 1 14  ? 7.983  7.317   1.046   1.00  14.94 ? 14   VAL F CA  1 
ATOM   1347 C  C   . VAL B 1 14  ? 8.714  6.102   1.559   1.00  15.84 ? 14   VAL F C   1 
ATOM   1348 O  O   . VAL B 1 14  ? 8.645  5.799   2.766   1.00  18.21 ? 14   VAL F O   1 
ATOM   1349 C  CB  . VAL B 1 14  ? 8.566  8.593   1.628   1.00  13.65 ? 14   VAL F CB  1 
ATOM   1350 C  CG1 . VAL B 1 14  ? 10.023 8.740   1.280   1.00  13.85 ? 14   VAL F CG1 1 
ATOM   1351 C  CG2 . VAL B 1 14  ? 7.824  9.788   1.111   1.00  15.77 ? 14   VAL F CG2 1 
ATOM   1352 N  N   . GLN B 1 15  ? 9.287  5.356   0.643   1.00  15.48 ? 15   GLN F N   1 
ATOM   1353 C  CA  A GLN B 1 15  ? 9.889  4.042   0.870   0.50  14.93 ? 15   GLN F CA  1 
ATOM   1354 C  CA  B GLN B 1 15  ? 9.979  4.175   1.031   0.50  16.31 ? 15   GLN F CA  1 
ATOM   1355 C  C   . GLN B 1 15  ? 11.230 3.985   0.193   1.00  14.33 ? 15   GLN F C   1 
ATOM   1356 O  O   . GLN B 1 15  ? 11.320 4.312   -0.975  1.00  16.17 ? 15   GLN F O   1 
ATOM   1357 C  CB  A GLN B 1 15  ? 8.997  2.947   0.254   0.50  14.90 ? 15   GLN F CB  1 
ATOM   1358 C  CB  B GLN B 1 15  ? 9.014  2.969   1.063   0.50  17.18 ? 15   GLN F CB  1 
ATOM   1359 C  CG  A GLN B 1 15  ? 9.128  2.086   2.355   0.50  19.22 ? 15   GLN F CG  1 
ATOM   1360 C  CD  A GLN B 1 15  ? 7.853  1.327   2.763   0.50  18.04 ? 15   GLN F CD  1 
ATOM   1361 O  OE1 A GLN B 1 15  ? 6.727  1.796   2.608   0.50  19.72 ? 15   GLN F OE1 1 
ATOM   1362 N  NE2 A GLN B 1 15  ? 8.050  0.150   3.339   0.50  23.18 ? 15   GLN F NE2 1 
ATOM   1363 N  N   . GLY B 1 16  ? 12.258 3.538   0.851   1.00  11.67 ? 16   GLY F N   1 
ATOM   1364 C  CA  . GLY B 1 16  ? 13.528 3.388   0.247   1.00  12.78 ? 16   GLY F CA  1 
ATOM   1365 C  C   . GLY B 1 16  ? 14.365 2.307   0.835   1.00  10.64 ? 16   GLY F C   1 
ATOM   1366 O  O   . GLY B 1 16  ? 14.110 1.886   1.968   1.00  11.58 ? 16   GLY F O   1 
ATOM   1367 N  N   . ILE B 1 17  ? 15.359 1.897   0.090   1.00  11.40 ? 17   ILE F N   1 
ATOM   1368 C  CA  . ILE B 1 17  ? 16.407 0.994   0.536   1.00  11.04 ? 17   ILE F CA  1 
ATOM   1369 C  C   . ILE B 1 17  ? 17.719 1.645   0.192   1.00  10.65 ? 17   ILE F C   1 
ATOM   1370 O  O   . ILE B 1 17  ? 17.957 2.021   -0.981  1.00  11.23 ? 17   ILE F O   1 
ATOM   1371 C  CB  . ILE B 1 17  ? 16.355 -0.395  -0.234  1.00  13.05 ? 17   ILE F CB  1 
ATOM   1372 C  CG1 . ILE B 1 17  ? 14.977 -1.042  -0.153  1.00  16.86 ? 17   ILE F CG1 1 
ATOM   1373 C  CG2 . ILE B 1 17  ? 17.459 -1.284  0.193   1.00  12.62 ? 17   ILE F CG2 1 
ATOM   1374 C  CD1 . ILE B 1 17  ? 14.681 -1.643  1.149   1.00  16.71 ? 17   ILE F CD1 1 
ATOM   1375 N  N   . ILE B 1 18  ? 18.584 1.820   1.159   1.00  10.09 ? 18   ILE F N   1 
ATOM   1376 C  CA  . ILE B 1 18  ? 19.865 2.411   0.996   1.00  8.85  ? 18   ILE F CA  1 
ATOM   1377 C  C   . ILE B 1 18  ? 20.952 1.503   1.512   1.00  8.20  ? 18   ILE F C   1 
ATOM   1378 O  O   . ILE B 1 18  ? 20.892 1.012   2.636   1.00  9.97  ? 18   ILE F O   1 
ATOM   1379 C  CB  . ILE B 1 18  ? 19.940 3.809   1.665   1.00  8.89  ? 18   ILE F CB  1 
ATOM   1380 C  CG1 . ILE B 1 18  ? 18.848 4.742   1.139   1.00  10.80 ? 18   ILE F CG1 1 
ATOM   1381 C  CG2 . ILE B 1 18  ? 21.325 4.392   1.588   1.00  9.00  ? 18   ILE F CG2 1 
ATOM   1382 C  CD1 . ILE B 1 18  ? 18.979 5.189   -0.251  1.00  10.13 ? 18   ILE F CD1 1 
ATOM   1383 N  N   . ASN B 1 19  ? 21.943 1.228   0.674   1.00  8.66  ? 19   ASN F N   1 
ATOM   1384 C  CA  . ASN B 1 19  ? 23.101 0.413   0.947   1.00  8.55  ? 19   ASN F CA  1 
ATOM   1385 C  C   . ASN B 1 19  ? 24.332 1.217   1.155   1.00  8.61  ? 19   ASN F C   1 
ATOM   1386 O  O   . ASN B 1 19  ? 24.485 2.277   0.547   1.00  9.80  ? 19   ASN F O   1 
ATOM   1387 C  CB  . ASN B 1 19  ? 23.302 -0.566  -0.254  1.00  9.25  ? 19   ASN F CB  1 
ATOM   1388 C  CG  . ASN B 1 19  ? 22.062 -1.394  -0.560  1.00  11.80 ? 19   ASN F CG  1 
ATOM   1389 O  OD1 . ASN B 1 19  ? 21.842 -2.380  0.121   1.00  12.66 ? 19   ASN F OD1 1 
ATOM   1390 N  ND2 . ASN B 1 19  ? 21.284 -1.020  -1.533  1.00  10.37 ? 19   ASN F ND2 1 
ATOM   1391 N  N   . PHE B 1 20  ? 25.209 0.804   2.065   1.00  8.55  ? 20   PHE F N   1 
ATOM   1392 C  CA  . PHE B 1 20  ? 26.473 1.372   2.310   1.00  8.61  ? 20   PHE F CA  1 
ATOM   1393 C  C   . PHE B 1 20  ? 27.560 0.320   2.166   1.00  8.71  ? 20   PHE F C   1 
ATOM   1394 O  O   . PHE B 1 20  ? 27.458 -0.797  2.662   1.00  10.18 ? 20   PHE F O   1 
ATOM   1395 C  CB  . PHE B 1 20  ? 26.545 1.910   3.741   1.00  8.31  ? 20   PHE F CB  1 
ATOM   1396 C  CG  . PHE B 1 20  ? 25.446 2.908   4.104   1.00  8.77  ? 20   PHE F CG  1 
ATOM   1397 C  CD1 . PHE B 1 20  ? 24.170 2.504   4.491   1.00  9.87  ? 20   PHE F CD1 1 
ATOM   1398 C  CD2 . PHE B 1 20  ? 25.708 4.239   4.059   1.00  9.66  ? 20   PHE F CD2 1 
ATOM   1399 C  CE1 . PHE B 1 20  ? 23.208 3.415   4.782   1.00  10.12 ? 20   PHE F CE1 1 
ATOM   1400 C  CE2 . PHE B 1 20  ? 24.742 5.148   4.364   1.00  10.35 ? 20   PHE F CE2 1 
ATOM   1401 C  CZ  . PHE B 1 20  ? 23.496 4.746   4.729   1.00  11.13 ? 20   PHE F CZ  1 
ATOM   1402 N  N   . GLU B 1 21  ? 28.634 0.647   1.491   1.00  10.69 ? 21   GLU F N   1 
ATOM   1403 C  CA  . GLU B 1 21  ? 29.769 -0.250  1.395   1.00  11.71 ? 21   GLU F CA  1 
ATOM   1404 C  C   . GLU B 1 21  ? 31.060 0.493   1.603   1.00  10.60 ? 21   GLU F C   1 
ATOM   1405 O  O   . GLU B 1 21  ? 31.269 1.548   1.017   1.00  11.83 ? 21   GLU F O   1 
ATOM   1406 C  CB  . GLU B 1 21  ? 29.816 -1.004  0.046   1.00  12.75 ? 21   GLU F CB  1 
ATOM   1407 C  CG  A GLU B 1 21  ? 31.115 -1.722  -0.325  0.50  13.91 ? 21   GLU F CG  1 
ATOM   1408 C  CG  B GLU B 1 21  ? 28.585 -1.181  -0.758  0.50  15.54 ? 21   GLU F CG  1 
ATOM   1409 C  CD  A GLU B 1 21  ? 31.007 -2.347  -1.703  0.50  15.55 ? 21   GLU F CD  1 
ATOM   1410 C  CD  B GLU B 1 21  ? 28.980 -1.854  -2.102  0.50  15.45 ? 21   GLU F CD  1 
ATOM   1411 O  OE1 A GLU B 1 21  ? 31.083 -1.591  -2.687  0.50  21.83 ? 21   GLU F OE1 1 
ATOM   1412 O  OE1 B GLU B 1 21  ? 29.798 -2.810  -2.099  0.50  16.09 ? 21   GLU F OE1 1 
ATOM   1413 O  OE2 A GLU B 1 21  ? 30.822 -3.558  -1.783  0.50  20.46 ? 21   GLU F OE2 1 
ATOM   1414 O  OE2 B GLU B 1 21  ? 28.532 -1.403  -3.170  0.50  20.67 ? 21   GLU F OE2 1 
ATOM   1415 N  N   . GLN B 1 22  ? 31.943 -0.022  2.427   1.00  10.72 ? 22   GLN F N   1 
ATOM   1416 C  CA  . GLN B 1 22  ? 33.224 0.598   2.699   1.00  12.62 ? 22   GLN F CA  1 
ATOM   1417 C  C   . GLN B 1 22  ? 34.280 -0.505  2.537   1.00  14.82 ? 22   GLN F C   1 
ATOM   1418 O  O   . GLN B 1 22  ? 34.305 -1.423  3.315   1.00  16.04 ? 22   GLN F O   1 
ATOM   1419 C  CB  . GLN B 1 22  ? 33.208 1.220   4.100   1.00  13.73 ? 22   GLN F CB  1 
ATOM   1420 C  CG  . GLN B 1 22  ? 34.454 2.011   4.422   1.00  11.98 ? 22   GLN F CG  1 
ATOM   1421 C  CD  . GLN B 1 22  ? 34.369 2.642   5.766   1.00  11.67 ? 22   GLN F CD  1 
ATOM   1422 O  OE1 . GLN B 1 22  ? 33.669 2.137   6.619   1.00  14.96 ? 22   GLN F OE1 1 
ATOM   1423 N  NE2 . GLN B 1 22  ? 35.014 3.770   5.938   1.00  12.67 ? 22   GLN F NE2 1 
ATOM   1424 N  N   . LYS B 1 23  ? 35.127 -0.390  1.536   1.00  15.02 ? 23   LYS F N   1 
ATOM   1425 C  CA  . LYS B 1 23  ? 36.130 -1.433  1.233   1.00  16.49 ? 23   LYS F CA  1 
ATOM   1426 C  C   . LYS B 1 23  ? 37.240 -1.503  2.274   1.00  17.88 ? 23   LYS F C   1 
ATOM   1427 O  O   . LYS B 1 23  ? 37.771 -2.574  2.552   1.00  20.87 ? 23   LYS F O   1 
ATOM   1428 C  CB  . LYS B 1 23  ? 36.722 -1.218  -0.165  1.00  16.78 ? 23   LYS F CB  1 
ATOM   1429 C  CG  . LYS B 1 23  ? 35.729 -1.333  -1.292  0.50  15.53 ? 23   LYS F CG  1 
ATOM   1430 C  CD  . LYS B 1 23  ? 36.340 -1.096  -2.667  0.10  15.25 ? 23   LYS F CD  1 
ATOM   1431 C  CE  . LYS B 1 23  ? 35.313 -1.386  -3.757  0.10  15.15 ? 23   LYS F CE  1 
ATOM   1432 N  NZ  . LYS B 1 23  ? 35.895 -1.375  -5.130  0.10  14.56 ? 23   LYS F NZ  1 
ATOM   1433 N  N   . GLU B 1 24  ? 37.616 -0.374  2.860   1.00  19.87 ? 24   GLU F N   1 
ATOM   1434 C  CA  . GLU B 1 24  ? 38.545 -0.334  3.991   1.00  20.35 ? 24   GLU F CA  1 
ATOM   1435 C  C   . GLU B 1 24  ? 38.158 0.810   4.900   1.00  20.18 ? 24   GLU F C   1 
ATOM   1436 O  O   . GLU B 1 24  ? 37.494 1.732   4.456   1.00  20.00 ? 24   GLU F O   1 
ATOM   1437 C  CB  . GLU B 1 24  ? 39.992 -0.167  3.524   1.00  21.10 ? 24   GLU F CB  1 
ATOM   1438 C  CG  . GLU B 1 24  ? 40.256 1.006   2.620   0.50  21.82 ? 24   GLU F CG  1 
ATOM   1439 C  CD  . GLU B 1 24  ? 39.958 0.750   1.175   0.50  23.51 ? 24   GLU F CD  1 
ATOM   1440 O  OE1 . GLU B 1 24  ? 40.148 -0.389  0.687   0.50  25.53 ? 24   GLU F OE1 1 
ATOM   1441 O  OE2 . GLU B 1 24  ? 39.532 1.707   0.503   0.50  24.80 ? 24   GLU F OE2 1 
ATOM   1442 N  N   . SER B 1 25  ? 38.544 0.740   6.174   1.00  20.80 ? 25   SER F N   1 
ATOM   1443 C  CA  . SER B 1 25  ? 38.106 1.738   7.167   1.00  20.93 ? 25   SER F CA  1 
ATOM   1444 C  C   . SER B 1 25  ? 38.660 3.124   6.856   1.00  20.56 ? 25   SER F C   1 
ATOM   1445 O  O   . SER B 1 25  ? 38.095 4.134   7.256   1.00  21.01 ? 25   SER F O   1 
ATOM   1446 C  CB  . SER B 1 25  ? 38.545 1.308   8.553   1.00  22.06 ? 25   SER F CB  1 
ATOM   1447 O  OG  . SER B 1 25  ? 39.939 1.413   8.698   1.00  25.11 ? 25   SER F OG  1 
ATOM   1448 N  N   . ASN B 1 26  ? 39.760 3.169   6.112   1.00  20.57 ? 26   ASN F N   1 
ATOM   1449 C  CA  . ASN B 1 26  ? 40.320 4.458   5.646   1.00  19.87 ? 26   ASN F CA  1 
ATOM   1450 C  C   . ASN B 1 26  ? 39.793 4.894   4.254   1.00  19.90 ? 26   ASN F C   1 
ATOM   1451 O  O   . ASN B 1 26  ? 40.328 5.805   3.625   1.00  20.51 ? 26   ASN F O   1 
ATOM   1452 C  CB  . ASN B 1 26  ? 41.864 4.442   5.702   1.00  21.19 ? 26   ASN F CB  1 
ATOM   1453 C  CG  . ASN B 1 26  ? 42.499 3.415   4.768   1.00  22.47 ? 26   ASN F CG  1 
ATOM   1454 O  OD1 . ASN B 1 26  ? 43.533 3.680   4.113   1.00  25.12 ? 26   ASN F OD1 1 
ATOM   1455 N  ND2 . ASN B 1 26  ? 41.898 2.232   4.699   1.00  25.38 ? 26   ASN F ND2 1 
ATOM   1456 N  N   . GLY B 1 27  ? 38.709 4.286   3.805   1.00  18.04 ? 27   GLY F N   1 
ATOM   1457 C  CA  . GLY B 1 27  ? 38.228 4.593   2.539   1.00  17.19 ? 27   GLY F CA  1 
ATOM   1458 C  C   . GLY B 1 27  ? 36.872 5.214   2.573   1.00  15.28 ? 27   GLY F C   1 
ATOM   1459 O  O   . GLY B 1 27  ? 36.172 5.268   3.611   1.00  13.82 ? 27   GLY F O   1 
ATOM   1460 N  N   . PRO B 1 28  ? 36.438 5.632   1.400   1.00  14.04 ? 28   PRO F N   1 
ATOM   1461 C  CA  . PRO B 1 28  ? 35.136 6.205   1.303   1.00  13.89 ? 28   PRO F CA  1 
ATOM   1462 C  C   . PRO B 1 28  ? 34.065 5.141   1.456   1.00  12.75 ? 28   PRO F C   1 
ATOM   1463 O  O   . PRO B 1 28  ? 34.279 3.953   1.199   1.00  13.18 ? 28   PRO F O   1 
ATOM   1464 C  CB  . PRO B 1 28  ? 35.099 6.744   -0.119  1.00  15.65 ? 28   PRO F CB  1 
ATOM   1465 C  CG  . PRO B 1 28  ? 36.051 5.934   -0.826  1.00  15.64 ? 28   PRO F CG  1 
ATOM   1466 C  CD  . PRO B 1 28  ? 37.122 5.616   0.089   1.00  14.15 ? 28   PRO F CD  1 
ATOM   1467 N  N   . VAL B 1 29  ? 32.877 5.621   1.753   1.00  10.89 ? 29   VAL F N   1 
ATOM   1468 C  CA  . VAL B 1 29  ? 31.720 4.819   1.765   1.00  10.87 ? 29   VAL F CA  1 
ATOM   1469 C  C   . VAL B 1 29  ? 30.874 5.094   0.519   1.00  10.93 ? 29   VAL F C   1 
ATOM   1470 O  O   . VAL B 1 29  ? 30.517 6.246   0.277   1.00  11.52 ? 29   VAL F O   1 
ATOM   1471 C  CB  . VAL B 1 29  ? 30.912 5.144   3.014   1.00  10.63 ? 29   VAL F CB  1 
ATOM   1472 C  CG1 . VAL B 1 29  ? 29.725 4.259   3.150   1.00  11.10 ? 29   VAL F CG1 1 
ATOM   1473 C  CG2 . VAL B 1 29  ? 31.802 4.969   4.266   1.00  11.77 ? 29   VAL F CG2 1 
ATOM   1474 N  N   . LYS B 1 30  ? 30.567 4.044   -0.253  1.00  9.84  ? 30   LYS F N   1 
ATOM   1475 C  CA  . LYS B 1 30  ? 29.615 4.098   -1.355  1.00  11.22 ? 30   LYS F CA  1 
ATOM   1476 C  C   . LYS B 1 30  ? 28.212 3.919   -0.793  1.00  10.29 ? 30   LYS F C   1 
ATOM   1477 O  O   . LYS B 1 30  ? 27.974 3.026   0.036   1.00  11.58 ? 30   LYS F O   1 
ATOM   1478 C  CB  . LYS B 1 30  ? 29.902 2.975   -2.332  1.00  12.89 ? 30   LYS F CB  1 
ATOM   1479 C  CG  . LYS B 1 30  ? 29.078 2.999   -3.584  0.70  12.53 ? 30   LYS F CG  1 
ATOM   1480 C  CD  . LYS B 1 30  ? 29.417 1.792   -4.415  0.70  14.67 ? 30   LYS F CD  1 
ATOM   1481 C  CE  . LYS B 1 30  ? 28.650 1.773   -5.703  0.70  18.07 ? 30   LYS F CE  1 
ATOM   1482 N  NZ  A LYS B 1 30  ? 27.212 1.444   -5.524  0.40  21.67 ? 30   LYS F NZ  1 
ATOM   1483 N  NZ  B LYS B 1 30  ? 27.213 1.446   -5.518  0.30  20.87 ? 30   LYS F NZ  1 
ATOM   1484 N  N   . VAL B 1 31  ? 27.290 4.796   -1.162  1.00  10.62 ? 31   VAL F N   1 
ATOM   1485 C  CA  . VAL B 1 31  ? 25.920 4.842   -0.721  1.00  10.53 ? 31   VAL F CA  1 
ATOM   1486 C  C   . VAL B 1 31  ? 25.078 4.684   -1.962  1.00  10.77 ? 31   VAL F C   1 
ATOM   1487 O  O   . VAL B 1 31  ? 25.166 5.508   -2.876  1.00  12.15 ? 31   VAL F O   1 
ATOM   1488 C  CB  . VAL B 1 31  ? 25.556 6.172   0.027   1.00  10.77 ? 31   VAL F CB  1 
ATOM   1489 C  CG1 . VAL B 1 31  ? 24.127 6.148   0.569   1.00  11.27 ? 31   VAL F CG1 1 
ATOM   1490 C  CG2 . VAL B 1 31  ? 26.543 6.400   1.116   1.00  10.69 ? 31   VAL F CG2 1 
ATOM   1491 N  N   . TRP B 1 32  ? 24.321 3.627   -2.051  1.00  10.62 ? 32   TRP F N   1 
ATOM   1492 C  CA  . TRP B 1 32  ? 23.492 3.416   -3.243  1.00  10.08 ? 32   TRP F CA  1 
ATOM   1493 C  C   . TRP B 1 32  ? 22.129 2.811   -2.894  1.00  9.33  ? 32   TRP F C   1 
ATOM   1494 O  O   . TRP B 1 32  ? 22.042 2.030   -1.929  1.00  9.96  ? 32   TRP F O   1 
ATOM   1495 C  CB  . TRP B 1 32  ? 24.188 2.497   -4.282  1.00  12.54 ? 32   TRP F CB  1 
ATOM   1496 C  CG  . TRP B 1 32  ? 24.477 1.098   -3.845  1.00  13.65 ? 32   TRP F CG  1 
ATOM   1497 C  CD1 . TRP B 1 32  ? 25.557 0.656   -3.116  1.00  12.06 ? 32   TRP F CD1 1 
ATOM   1498 C  CD2 . TRP B 1 32  ? 23.675 -0.048  -4.105  1.00  16.20 ? 32   TRP F CD2 1 
ATOM   1499 N  NE1 . TRP B 1 32  ? 25.513 -0.731  -3.003  1.00  14.39 ? 32   TRP F NE1 1 
ATOM   1500 C  CE2 . TRP B 1 32  ? 24.320 -1.163  -3.509  1.00  14.38 ? 32   TRP F CE2 1 
ATOM   1501 C  CE3 . TRP B 1 32  ? 22.430 -0.229  -4.703  1.00  15.04 ? 32   TRP F CE3 1 
ATOM   1502 C  CZ2 . TRP B 1 32  ? 23.736 -2.450  -3.506  1.00  14.88 ? 32   TRP F CZ2 1 
ATOM   1503 C  CZ3 . TRP B 1 32  ? 21.887 -1.515  -4.737  1.00  14.40 ? 32   TRP F CZ3 1 
ATOM   1504 C  CH2 . TRP B 1 32  ? 22.531 -2.592  -4.169  1.00  15.22 ? 32   TRP F CH2 1 
ATOM   1505 N  N   . GLY B 1 33  ? 21.100 3.090   -3.667  1.00  9.97  ? 33   GLY F N   1 
ATOM   1506 C  CA  . GLY B 1 33  ? 19.813 2.567   -3.539  1.00  9.89  ? 33   GLY F CA  1 
ATOM   1507 C  C   . GLY B 1 33  ? 18.796 3.430   -4.185  1.00  9.98  ? 33   GLY F C   1 
ATOM   1508 O  O   . GLY B 1 33  ? 19.100 4.093   -5.200  1.00  10.66 ? 33   GLY F O   1 
ATOM   1509 N  N   . SER B 1 34  ? 17.572 3.365   -3.749  1.00  9.02  ? 34   SER F N   1 
ATOM   1510 C  CA  . SER B 1 34  ? 16.500 4.088   -4.346  1.00  10.91 ? 34   SER F CA  1 
ATOM   1511 C  C   . SER B 1 34  ? 15.471 4.441   -3.287  1.00  10.12 ? 34   SER F C   1 
ATOM   1512 O  O   . SER B 1 34  ? 15.275 3.724   -2.296  1.00  11.67 ? 34   SER F O   1 
ATOM   1513 C  CB  A SER B 1 34  ? 15.881 3.308   -5.502  0.63  11.31 ? 34   SER F CB  1 
ATOM   1514 C  CB  B SER B 1 34  ? 15.876 3.211   -5.433  0.37  11.06 ? 34   SER F CB  1 
ATOM   1515 O  OG  A SER B 1 34  ? 15.209 2.186   -5.000  0.63  14.34 ? 34   SER F OG  1 
ATOM   1516 O  OG  B SER B 1 34  ? 15.124 3.985   -6.328  0.37  14.09 ? 34   SER F OG  1 
ATOM   1517 N  N   . ILE B 1 35  ? 14.796 5.562   -3.496  1.00  10.47 ? 35   ILE F N   1 
ATOM   1518 C  CA  . ILE B 1 35  ? 13.693 6.037   -2.677  1.00  10.63 ? 35   ILE F CA  1 
ATOM   1519 C  C   . ILE B 1 35  ? 12.509 6.423   -3.560  1.00  10.62 ? 35   ILE F C   1 
ATOM   1520 O  O   . ILE B 1 35  ? 12.716 7.062   -4.615  1.00  12.93 ? 35   ILE F O   1 
ATOM   1521 C  CB  . ILE B 1 35  ? 14.104 7.243   -1.797  1.00  10.88 ? 35   ILE F CB  1 
ATOM   1522 C  CG1 . ILE B 1 35  ? 15.392 6.935   -1.039  1.00  12.02 ? 35   ILE F CG1 1 
ATOM   1523 C  CG2 . ILE B 1 35  ? 12.961 7.612   -0.837  1.00  11.80 ? 35   ILE F CG2 1 
ATOM   1524 C  CD1 . ILE B 1 35  ? 16.079 8.194   -0.452  1.00  12.29 ? 35   ILE F CD1 1 
ATOM   1525 N  N   . LYS B 1 36  ? 11.317 5.937   -3.303  1.00  11.23 ? 36   LYS F N   1 
ATOM   1526 C  CA  . LYS B 1 36  ? 10.147 6.263   -4.065  1.00  12.43 ? 36   LYS F CA  1 
ATOM   1527 C  C   . LYS B 1 36  ? 9.127  7.011   -3.230  1.00  12.74 ? 36   LYS F C   1 
ATOM   1528 O  O   . LYS B 1 36  ? 9.179  7.042   -1.975  1.00  13.05 ? 36   LYS F O   1 
ATOM   1529 C  CB  . LYS B 1 36  ? 9.528  5.009   -4.678  1.00  14.69 ? 36   LYS F CB  1 
ATOM   1530 C  CG  . LYS B 1 36  ? 8.863  4.141   -3.648  1.00  16.88 ? 36   LYS F CG  1 
ATOM   1531 C  CD  . LYS B 1 36  ? 8.271  2.921   -4.339  0.50  15.00 ? 36   LYS F CD  1 
ATOM   1532 C  CE  . LYS B 1 36  ? 7.626  1.977   -3.350  0.50  16.25 ? 36   LYS F CE  1 
ATOM   1533 N  NZ  . LYS B 1 36  ? 7.373  0.701   -4.072  0.50  17.33 ? 36   LYS F NZ  1 
ATOM   1534 N  N   . GLY B 1 37  ? 8.182  7.611   -3.930  1.00  12.56 ? 37   GLY F N   1 
ATOM   1535 C  CA  . GLY B 1 37  ? 7.114  8.363   -3.312  1.00  12.57 ? 37   GLY F CA  1 
ATOM   1536 C  C   . GLY B 1 37  ? 7.443  9.810   -3.003  1.00  11.42 ? 37   GLY F C   1 
ATOM   1537 O  O   . GLY B 1 37  ? 6.716  10.444  -2.263  1.00  14.01 ? 37   GLY F O   1 
ATOM   1538 N  N   . LEU B 1 38  ? 8.493  10.346  -3.614  1.00  11.43 ? 38   LEU F N   1 
ATOM   1539 C  CA  . LEU B 1 38  ? 8.930  11.683  -3.284  1.00  11.02 ? 38   LEU F CA  1 
ATOM   1540 C  C   . LEU B 1 38  ? 8.345  12.685  -4.314  1.00  11.03 ? 38   LEU F C   1 
ATOM   1541 O  O   . LEU B 1 38  ? 8.105  12.334  -5.484  1.00  13.47 ? 38   LEU F O   1 
ATOM   1542 C  CB  . LEU B 1 38  ? 10.456 11.749  -3.429  1.00  10.62 ? 38   LEU F CB  1 
ATOM   1543 C  CG  . LEU B 1 38  ? 11.184 11.005  -2.274  1.00  9.97  ? 38   LEU F CG  1 
ATOM   1544 C  CD1 . LEU B 1 38  ? 12.608 10.784  -2.690  1.00  11.53 ? 38   LEU F CD1 1 
ATOM   1545 C  CD2 . LEU B 1 38  ? 11.033 11.740  -0.934  1.00  10.68 ? 38   LEU F CD2 1 
ATOM   1546 N  N   . THR B 1 39  ? 8.178  13.939  -3.912  1.00  10.80 ? 39   THR F N   1 
ATOM   1547 C  CA  . THR B 1 39  ? 7.909  14.982  -4.890  1.00  11.62 ? 39   THR F CA  1 
ATOM   1548 C  C   . THR B 1 39  ? 9.186  15.242  -5.738  1.00  11.10 ? 39   THR F C   1 
ATOM   1549 O  O   . THR B 1 39  ? 10.323 15.050  -5.318  1.00  10.44 ? 39   THR F O   1 
ATOM   1550 C  CB  . THR B 1 39  ? 7.457  16.265  -4.225  1.00  12.82 ? 39   THR F CB  1 
ATOM   1551 O  OG1 . THR B 1 39  ? 8.492  16.737  -3.342  1.00  12.55 ? 39   THR F OG1 1 
ATOM   1552 C  CG2 . THR B 1 39  ? 6.193  16.043  -3.453  1.00  13.44 ? 39   THR F CG2 1 
ATOM   1553 N  N   . GLU B 1 40  ? 8.963  15.609  -6.988  1.00  11.80 ? 40   GLU F N   1 
ATOM   1554 C  CA  . GLU B 1 40  ? 10.076 15.926  -7.896  1.00  12.07 ? 40   GLU F CA  1 
ATOM   1555 C  C   . GLU B 1 40  ? 10.951 17.022  -7.316  1.00  10.64 ? 40   GLU F C   1 
ATOM   1556 O  O   . GLU B 1 40  ? 10.440 18.068  -6.843  1.00  12.40 ? 40   GLU F O   1 
ATOM   1557 C  CB  . GLU B 1 40  ? 9.511  16.355  -9.239  1.00  12.41 ? 40   GLU F CB  1 
ATOM   1558 C  CG  . GLU B 1 40  ? 10.505 16.173  -10.374 1.00  13.93 ? 40   GLU F CG  1 
ATOM   1559 C  CD  . GLU B 1 40  ? 10.993 17.493  -10.877 1.00  14.72 ? 40   GLU F CD  1 
ATOM   1560 O  OE1 . GLU B 1 40  ? 11.163 18.378  -10.025 1.00  14.63 ? 40   GLU F OE1 1 
ATOM   1561 O  OE2 . GLU B 1 40  ? 11.200 17.663  -12.124 1.00  15.14 ? 40   GLU F OE2 1 
ATOM   1562 N  N   . GLY B 1 41  ? 12.256 16.810  -7.307  1.00  10.93 ? 41   GLY F N   1 
ATOM   1563 C  CA  . GLY B 1 41  ? 13.170 17.819  -6.854  1.00  9.78  ? 41   GLY F CA  1 
ATOM   1564 C  C   . GLY B 1 41  ? 14.153 17.285  -5.821  1.00  9.54  ? 41   GLY F C   1 
ATOM   1565 O  O   . GLY B 1 41  ? 14.361 16.087  -5.703  1.00  11.40 ? 41   GLY F O   1 
ATOM   1566 N  N   . LEU B 1 42  ? 14.722 18.207  -5.088  1.00  9.31  ? 42   LEU F N   1 
ATOM   1567 C  CA  . LEU B 1 42  ? 15.724 17.900  -4.104  1.00  9.80  ? 42   LEU F CA  1 
ATOM   1568 C  C   . LEU B 1 42  ? 15.159 17.590  -2.736  1.00  9.12  ? 42   LEU F C   1 
ATOM   1569 O  O   . LEU B 1 42  ? 14.233 18.276  -2.335  1.00  9.92  ? 42   LEU F O   1 
ATOM   1570 C  CB  . LEU B 1 42  ? 16.733 19.037  -4.035  1.00  10.34 ? 42   LEU F CB  1 
ATOM   1571 C  CG  . LEU B 1 42  ? 17.560 19.279  -5.310  1.00  12.93 ? 42   LEU F CG  1 
ATOM   1572 C  CD1 . LEU B 1 42  ? 18.451 20.436  -5.069  1.00  16.16 ? 42   LEU F CD1 1 
ATOM   1573 C  CD2 . LEU B 1 42  ? 18.371 18.045  -5.727  1.00  14.42 ? 42   LEU F CD2 1 
ATOM   1574 N  N   . HIS B 1 43  ? 15.712 16.595  -2.065  1.00  9.10  ? 43   HIS F N   1 
ATOM   1575 C  CA  . HIS B 1 43  ? 15.285 16.239  -0.699  1.00  8.67  ? 43   HIS F CA  1 
ATOM   1576 C  C   . HIS B 1 43  ? 16.499 16.034  0.158   1.00  8.06  ? 43   HIS F C   1 
ATOM   1577 O  O   . HIS B 1 43  ? 17.383 15.220  -0.128  1.00  9.06  ? 43   HIS F O   1 
ATOM   1578 C  CB  . HIS B 1 43  ? 14.486 14.955  -0.780  1.00  8.49  ? 43   HIS F CB  1 
ATOM   1579 C  CG  . HIS B 1 43  ? 13.196 15.131  -1.485  1.00  9.48  ? 43   HIS F CG  1 
ATOM   1580 N  ND1 . HIS B 1 43  ? 12.049 15.611  -0.887  1.00  10.75 ? 43   HIS F ND1 1 
ATOM   1581 C  CD2 . HIS B 1 43  ? 12.907 15.013  -2.803  1.00  10.42 ? 43   HIS F CD2 1 
ATOM   1582 C  CE1 . HIS B 1 43  ? 11.090 15.711  -1.803  1.00  11.00 ? 43   HIS F CE1 1 
ATOM   1583 N  NE2 . HIS B 1 43  ? 11.606 15.380  -2.977  1.00  10.89 ? 43   HIS F NE2 1 
ATOM   1584 N  N   . GLY B 1 44  ? 16.527 16.698  1.317   1.00  8.13  ? 44   GLY F N   1 
ATOM   1585 C  CA  . GLY B 1 44  ? 17.682 16.610  2.188   1.00  8.36  ? 44   GLY F CA  1 
ATOM   1586 C  C   . GLY B 1 44  ? 17.877 15.198  2.710   1.00  7.49  ? 44   GLY F C   1 
ATOM   1587 O  O   . GLY B 1 44  ? 16.910 14.485  2.930   1.00  8.04  ? 44   GLY F O   1 
ATOM   1588 N  N   . PHE B 1 45  ? 19.125 14.875  2.892   1.00  7.55  ? 45   PHE F N   1 
ATOM   1589 C  CA  . PHE B 1 45  ? 19.551 13.483  3.145   1.00  6.77  ? 45   PHE F CA  1 
ATOM   1590 C  C   . PHE B 1 45  ? 20.638 13.501  4.184   1.00  7.20  ? 45   PHE F C   1 
ATOM   1591 O  O   . PHE B 1 45  ? 21.733 13.976  3.991   1.00  8.00  ? 45   PHE F O   1 
ATOM   1592 C  CB  . PHE B 1 45  ? 20.104 12.898  1.783   1.00  7.67  ? 45   PHE F CB  1 
ATOM   1593 C  CG  . PHE B 1 45  ? 20.218 11.400  1.745   1.00  8.11  ? 45   PHE F CG  1 
ATOM   1594 C  CD1 . PHE B 1 45  ? 19.162 10.580  1.988   1.00  9.59  ? 45   PHE F CD1 1 
ATOM   1595 C  CD2 . PHE B 1 45  ? 21.368 10.832  1.367   1.00  8.35  ? 45   PHE F CD2 1 
ATOM   1596 C  CE1 . PHE B 1 45  ? 19.269 9.188   1.869   1.00  10.58 ? 45   PHE F CE1 1 
ATOM   1597 C  CE2 . PHE B 1 45  ? 21.469 9.424   1.148   1.00  10.85 ? 45   PHE F CE2 1 
ATOM   1598 C  CZ  . PHE B 1 45  ? 20.414 8.642   1.422   1.00  10.27 ? 45   PHE F CZ  1 
ATOM   1599 N  N   . HIS B 1 46  ? 20.253 13.015  5.398   1.00  7.64  ? 46   HIS F N   1 
ATOM   1600 C  CA  . HIS B 1 46  ? 21.065 13.202  6.620   1.00  7.02  ? 46   HIS F CA  1 
ATOM   1601 C  C   . HIS B 1 46  ? 21.194 11.900  7.401   1.00  7.04  ? 46   HIS F C   1 
ATOM   1602 O  O   . HIS B 1 46  ? 20.232 11.182  7.538   1.00  7.93  ? 46   HIS F O   1 
ATOM   1603 C  CB  . HIS B 1 46  ? 20.381 14.200  7.561   1.00  7.66  ? 46   HIS F CB  1 
ATOM   1604 C  CG  . HIS B 1 46  ? 20.183 15.559  7.023   1.00  8.64  ? 46   HIS F CG  1 
ATOM   1605 N  ND1 . HIS B 1 46  ? 19.098 16.322  7.379   1.00  9.10  ? 46   HIS F ND1 1 
ATOM   1606 C  CD2 . HIS B 1 46  ? 20.844 16.263  6.066   1.00  8.73  ? 46   HIS F CD2 1 
ATOM   1607 C  CE1 . HIS B 1 46  ? 19.141 17.470  6.718   1.00  9.19  ? 46   HIS F CE1 1 
ATOM   1608 N  NE2 . HIS B 1 46  ? 20.168 17.447  5.898   1.00  9.71  ? 46   HIS F NE2 1 
ATOM   1609 N  N   . VAL B 1 47  ? 22.340 11.777  8.033   1.00  6.39  ? 47   VAL F N   1 
ATOM   1610 C  CA  . VAL B 1 47  ? 22.462 10.818  9.202   1.00  6.64  ? 47   VAL F CA  1 
ATOM   1611 C  C   . VAL B 1 47  ? 22.250 11.705  10.474  1.00  6.75  ? 47   VAL F C   1 
ATOM   1612 O  O   . VAL B 1 47  ? 22.946 12.651  10.726  1.00  6.36  ? 47   VAL F O   1 
ATOM   1613 C  CB  . VAL B 1 47  ? 23.789 10.121  9.258   1.00  7.30  ? 47   VAL F CB  1 
ATOM   1614 C  CG1 . VAL B 1 47  ? 23.852 9.158   10.452  1.00  7.43  ? 47   VAL F CG1 1 
ATOM   1615 C  CG2 . VAL B 1 47  ? 24.059 9.367   7.958   1.00  8.22  ? 47   VAL F CG2 1 
ATOM   1616 N  N   . HIS B 1 48  ? 21.171 11.327  11.153  1.00  6.53  ? 48   HIS F N   1 
ATOM   1617 C  CA  . HIS B 1 48  ? 20.861 11.881  12.466  1.00  7.34  ? 48   HIS F CA  1 
ATOM   1618 C  C   . HIS B 1 48  ? 21.474 11.031  13.569  1.00  7.44  ? 48   HIS F C   1 
ATOM   1619 O  O   . HIS B 1 48  ? 21.725 9.844   13.378  1.00  8.78  ? 48   HIS F O   1 
ATOM   1620 C  CB  . HIS B 1 48  ? 19.351 12.043  12.596  1.00  6.98  ? 48   HIS F CB  1 
ATOM   1621 C  CG  . HIS B 1 48  ? 18.797 13.222  11.860  1.00  7.78  ? 48   HIS F CG  1 
ATOM   1622 N  ND1 . HIS B 1 48  ? 18.356 14.347  12.500  1.00  8.62  ? 48   HIS F ND1 1 
ATOM   1623 C  CD2 . HIS B 1 48  ? 18.716 13.508  10.532  1.00  9.12  ? 48   HIS F CD2 1 
ATOM   1624 C  CE1 . HIS B 1 48  ? 17.974 15.260  11.630  1.00  9.64  ? 48   HIS F CE1 1 
ATOM   1625 N  NE2 . HIS B 1 48  ? 18.169 14.779  10.393  1.00  7.92  ? 48   HIS F NE2 1 
ATOM   1626 N  N   . GLU B 1 49  ? 21.686 11.639  14.750  1.00  7.26  ? 49   GLU F N   1 
ATOM   1627 C  CA  . GLU B 1 49  ? 22.536 11.058  15.759  1.00  7.91  ? 49   GLU F CA  1 
ATOM   1628 C  C   . GLU B 1 49  ? 22.058 9.750   16.355  1.00  7.62  ? 49   GLU F C   1 
ATOM   1629 O  O   . GLU B 1 49  ? 22.872 8.831   16.494  1.00  8.21  ? 49   GLU F O   1 
ATOM   1630 C  CB  . GLU B 1 49  ? 22.710 12.056  16.878  1.00  7.81  ? 49   GLU F CB  1 
ATOM   1631 C  CG  . GLU B 1 49  ? 23.723 11.599  17.911  1.00  8.08  ? 49   GLU F CG  1 
ATOM   1632 C  CD  . GLU B 1 49  ? 23.945 12.585  18.991  1.00  9.14  ? 49   GLU F CD  1 
ATOM   1633 O  OE1 . GLU B 1 49  ? 23.216 13.623  19.000  1.00  10.74 ? 49   GLU F OE1 1 
ATOM   1634 O  OE2 . GLU B 1 49  ? 24.793 12.276  19.880  1.00  11.97 ? 49   GLU F OE2 1 
ATOM   1635 N  N   . PHE B 1 50  ? 20.783 9.627   16.635  1.00  7.47  ? 50   PHE F N   1 
ATOM   1636 C  CA  . PHE B 1 50  ? 20.335 8.468   17.409  1.00  7.61  ? 50   PHE F CA  1 
ATOM   1637 C  C   . PHE B 1 50  ? 19.586 7.540   16.528  1.00  7.95  ? 50   PHE F C   1 
ATOM   1638 O  O   . PHE B 1 50  ? 18.793 7.978   15.711  1.00  8.38  ? 50   PHE F O   1 
ATOM   1639 C  CB  . PHE B 1 50  ? 19.430 8.868   18.606  1.00  8.74  ? 50   PHE F CB  1 
ATOM   1640 C  CG  . PHE B 1 50  ? 20.012 9.931   19.463  1.00  9.87  ? 50   PHE F CG  1 
ATOM   1641 C  CD1 . PHE B 1 50  ? 21.198 9.747   20.043  1.00  10.75 ? 50   PHE F CD1 1 
ATOM   1642 C  CD2 . PHE B 1 50  ? 19.362 11.165  19.611  1.00  9.94  ? 50   PHE F CD2 1 
ATOM   1643 C  CE1 . PHE B 1 50  ? 21.769 10.755  20.880  1.00  12.22 ? 50   PHE F CE1 1 
ATOM   1644 C  CE2 . PHE B 1 50  ? 19.926 12.181  20.406  1.00  11.86 ? 50   PHE F CE2 1 
ATOM   1645 C  CZ  . PHE B 1 50  ? 21.141 11.956  21.000  1.00  12.05 ? 50   PHE F CZ  1 
ATOM   1646 N  N   . GLY B 1 51  ? 19.788 6.251   16.719  1.00  7.97  ? 51   GLY F N   1 
ATOM   1647 C  CA  . GLY B 1 51  ? 19.022 5.176   16.102  1.00  8.61  ? 51   GLY F CA  1 
ATOM   1648 C  C   . GLY B 1 51  ? 17.768 4.869   16.905  1.00  8.99  ? 51   GLY F C   1 
ATOM   1649 O  O   . GLY B 1 51  ? 17.459 3.719   17.172  1.00  9.66  ? 51   GLY F O   1 
ATOM   1650 N  N   . ASP B 1 52  ? 17.022 5.926   17.215  1.00  9.30  ? 52   ASP F N   1 
ATOM   1651 C  CA  . ASP B 1 52  ? 15.860 5.853   18.109  1.00  9.53  ? 52   ASP F CA  1 
ATOM   1652 C  C   . ASP B 1 52  ? 14.691 6.244   17.249  1.00  9.80  ? 52   ASP F C   1 
ATOM   1653 O  O   . ASP B 1 52  ? 14.566 7.398   16.890  1.00  10.94 ? 52   ASP F O   1 
ATOM   1654 C  CB  . ASP B 1 52  ? 16.019 6.821   19.279  1.00  9.91  ? 52   ASP F CB  1 
ATOM   1655 C  CG  . ASP B 1 52  ? 14.959 6.673   20.273  1.00  11.86 ? 52   ASP F CG  1 
ATOM   1656 O  OD1 . ASP B 1 52  ? 13.832 6.293   19.900  1.00  13.09 ? 52   ASP F OD1 1 
ATOM   1657 O  OD2 . ASP B 1 52  ? 15.255 7.076   21.404  1.00  16.34 ? 52   ASP F OD2 1 
ATOM   1658 N  N   . ASN B 1 53  ? 13.849 5.297   16.877  1.00  11.30 ? 53   ASN F N   1 
ATOM   1659 C  CA  . ASN B 1 53  ? 12.654 5.618   16.107  1.00  12.39 ? 53   ASN F CA  1 
ATOM   1660 C  C   . ASN B 1 53  ? 11.412 5.210   16.866  1.00  12.70 ? 53   ASN F C   1 
ATOM   1661 O  O   . ASN B 1 53  ? 10.367 4.907   16.315  1.00  13.92 ? 53   ASN F O   1 
ATOM   1662 C  CB  . ASN B 1 53  ? 12.670 5.033   14.699  1.00  14.47 ? 53   ASN F CB  1 
ATOM   1663 C  CG  . ASN B 1 53  ? 13.851 5.566   13.774  1.00  16.47 ? 53   ASN F CG  1 
ATOM   1664 O  OD1 . ASN B 1 53  ? 14.460 6.659   13.962  1.00  18.48 ? 53   ASN F OD1 1 
ATOM   1665 N  ND2 . ASN B 1 53  ? 14.176 4.761   12.788  1.00  17.44 ? 53   ASN F ND2 1 
ATOM   1666 N  N   . THR B 1 54  ? 11.558 5.273   18.149  1.00  12.95 ? 54   THR F N   1 
ATOM   1667 C  CA  . THR B 1 54  ? 10.426 4.918   19.029  1.00  14.52 ? 54   THR F CA  1 
ATOM   1668 C  C   . THR B 1 54  ? 9.223  5.816   18.848  1.00  15.12 ? 54   THR F C   1 
ATOM   1669 O  O   . THR B 1 54  ? 8.105  5.365   18.996  1.00  15.29 ? 54   THR F O   1 
ATOM   1670 C  CB  . THR B 1 54  ? 10.761 4.937   20.500  1.00  14.02 ? 54   THR F CB  1 
ATOM   1671 O  OG1 . THR B 1 54  ? 11.317 6.181   20.831  1.00  12.47 ? 54   THR F OG1 1 
ATOM   1672 C  CG2 . THR B 1 54  ? 11.753 3.896   20.828  1.00  12.98 ? 54   THR F CG2 1 
ATOM   1673 N  N   . ALA B 1 55  ? 9.452  7.094   18.515  1.00  17.12 ? 55   ALA F N   1 
ATOM   1674 C  CA  . ALA B 1 55  ? 8.332  7.978   18.175  1.00  18.13 ? 55   ALA F CA  1 
ATOM   1675 C  C   . ALA B 1 55  ? 8.439  8.385   16.706  1.00  19.00 ? 55   ALA F C   1 
ATOM   1676 O  O   . ALA B 1 55  ? 8.125  9.532   16.311  1.00  22.17 ? 55   ALA F O   1 
ATOM   1677 C  CB  . ALA B 1 55  ? 8.307  9.141   19.067  1.00  20.13 ? 55   ALA F CB  1 
ATOM   1678 N  N   . GLY B 1 56  ? 8.850  7.479   15.835  1.00  17.58 ? 56   GLY F N   1 
ATOM   1679 C  CA  . GLY B 1 56  ? 9.095  7.850   14.457  1.00  18.34 ? 56   GLY F CA  1 
ATOM   1680 C  C   . GLY B 1 56  ? 10.369 8.613   14.333  1.00  16.99 ? 56   GLY F C   1 
ATOM   1681 O  O   . GLY B 1 56  ? 11.249 8.595   15.240  1.00  17.74 ? 56   GLY F O   1 
ATOM   1682 N  N   . CYS B 1 57  ? 10.472 9.317   13.194  1.00  14.79 ? 57   CYS F N   1 
ATOM   1683 C  CA  . CYS B 1 57  ? 11.693 9.997   12.869  1.00  13.76 ? 57   CYS F CA  1 
ATOM   1684 C  C   . CYS B 1 57  ? 12.046 11.122  13.860  1.00  12.79 ? 57   CYS F C   1 
ATOM   1685 O  O   . CYS B 1 57  ? 13.212 11.469  13.986  1.00  14.00 ? 57   CYS F O   1 
ATOM   1686 C  CB  . CYS B 1 57  ? 11.607 10.558  11.467  1.00  12.67 ? 57   CYS F CB  1 
ATOM   1687 S  SG  . CYS B 1 57  ? 11.206 9.251   10.194  1.00  15.81 ? 57   CYS F SG  1 
ATOM   1688 N  N   A THR B 1 58  ? 11.156 11.641  14.680  0.70  14.39 ? 58   THR F N   1 
ATOM   1689 N  N   B THR B 1 58  ? 11.005 11.518  14.609  0.30  12.58 ? 58   THR F N   1 
ATOM   1690 C  CA  A THR B 1 58  ? 11.582 12.769  15.558  0.70  14.79 ? 58   THR F CA  1 
ATOM   1691 C  CA  B THR B 1 58  ? 11.053 12.621  15.553  0.30  11.86 ? 58   THR F CA  1 
ATOM   1692 C  C   A THR B 1 58  ? 12.613 12.335  16.620  0.70  13.84 ? 58   THR F C   1 
ATOM   1693 C  C   B THR B 1 58  ? 11.947 12.351  16.749  0.30  11.12 ? 58   THR F C   1 
ATOM   1694 O  O   A THR B 1 58  ? 13.542 13.079  17.046  0.70  14.73 ? 58   THR F O   1 
ATOM   1695 O  O   B THR B 1 58  ? 12.294 13.278  17.508  0.30  9.98  ? 58   THR F O   1 
ATOM   1696 C  CB  A THR B 1 58  ? 10.339 13.459  16.153  0.70  16.97 ? 58   THR F CB  1 
ATOM   1697 C  CB  B THR B 1 58  ? 9.642  13.075  16.029  0.30  12.92 ? 58   THR F CB  1 
ATOM   1698 O  OG1 A THR B 1 58  ? 10.700 14.564  17.013  0.70  19.80 ? 58   THR F OG1 1 
ATOM   1699 O  OG1 B THR B 1 58  ? 8.663  12.053  15.810  0.30  13.55 ? 58   THR F OG1 1 
ATOM   1700 C  CG2 A THR B 1 58  ? 9.474  12.437  16.912  0.70  15.44 ? 58   THR F CG2 1 
ATOM   1701 C  CG2 B THR B 1 58  ? 9.239  14.318  15.291  0.30  13.16 ? 58   THR F CG2 1 
ATOM   1702 N  N   A SER B 1 59  ? 12.428 11.133  17.117  0.70  11.63 ? 59   SER F N   1 
ATOM   1703 N  N   B SER B 1 59  ? 12.358 11.108  16.935  0.30  10.38 ? 59   SER F N   1 
ATOM   1704 C  CA  A SER B 1 59  ? 13.320 10.602  18.107  0.70  12.86 ? 59   SER F CA  1 
ATOM   1705 C  CA  B SER B 1 59  ? 13.249 10.778  18.033  0.30  10.96 ? 59   SER F CA  1 
ATOM   1706 C  C   A SER B 1 59  ? 14.780 10.582  17.714  0.70  10.77 ? 59   SER F C   1 
ATOM   1707 C  C   B SER B 1 59  ? 14.718 10.576  17.688  0.30  10.44 ? 59   SER F C   1 
ATOM   1708 O  O   A SER B 1 59  ? 15.643 10.348  18.532  0.70  11.33 ? 59   SER F O   1 
ATOM   1709 O  O   B SER B 1 59  ? 15.509 10.211  18.543  0.30  11.00 ? 59   SER F O   1 
ATOM   1710 C  CB  A SER B 1 59  ? 12.826 9.211   18.532  0.70  13.52 ? 59   SER F CB  1 
ATOM   1711 C  CB  B SER B 1 59  ? 12.718 9.530   18.761  0.30  11.29 ? 59   SER F CB  1 
ATOM   1712 O  OG  A SER B 1 59  ? 11.520 9.333   19.095  0.70  15.03 ? 59   SER F OG  1 
ATOM   1713 O  OG  B SER B 1 59  ? 12.190 8.578   17.843  0.30  9.97  ? 59   SER F OG  1 
ATOM   1714 N  N   . ALA B 1 60  ? 15.079 10.796  16.424  1.00  11.41 ? 60   ALA F N   1 
ATOM   1715 C  CA  . ALA B 1 60  ? 16.421 10.574  15.954  1.00  10.67 ? 60   ALA F CA  1 
ATOM   1716 C  C   . ALA B 1 60  ? 17.403 11.682  16.355  1.00  9.63  ? 60   ALA F C   1 
ATOM   1717 O  O   . ALA B 1 60  ? 18.591 11.517  16.207  1.00  9.47  ? 60   ALA F O   1 
ATOM   1718 C  CB  . ALA B 1 60  ? 16.485 10.383  14.462  1.00  11.49 ? 60   ALA F CB  1 
ATOM   1719 N  N   . GLY B 1 61  ? 16.933 12.813  16.860  1.00  8.07  ? 61   GLY F N   1 
ATOM   1720 C  CA  . GLY B 1 61  ? 17.845 13.810  17.350  1.00  8.41  ? 61   GLY F CA  1 
ATOM   1721 C  C   . GLY B 1 61  ? 18.406 14.669  16.241  1.00  8.27  ? 61   GLY F C   1 
ATOM   1722 O  O   . GLY B 1 61  ? 17.862 14.743  15.145  1.00  8.62  ? 61   GLY F O   1 
ATOM   1723 N  N   . PRO B 1 62  ? 19.463 15.383  16.535  1.00  7.84  ? 62   PRO F N   1 
ATOM   1724 C  CA  . PRO B 1 62  ? 20.077 16.322  15.585  1.00  7.58  ? 62   PRO F CA  1 
ATOM   1725 C  C   . PRO B 1 62  ? 20.966 15.613  14.566  1.00  7.93  ? 62   PRO F C   1 
ATOM   1726 O  O   . PRO B 1 62  ? 21.116 14.417  14.563  1.00  7.32  ? 62   PRO F O   1 
ATOM   1727 C  CB  . PRO B 1 62  ? 20.928 17.231  16.494  1.00  9.06  ? 62   PRO F CB  1 
ATOM   1728 C  CG  . PRO B 1 62  ? 21.354 16.296  17.587  1.00  9.92  ? 62   PRO F CG  1 
ATOM   1729 C  CD  . PRO B 1 62  ? 20.147 15.375  17.852  1.00  8.99  ? 62   PRO F CD  1 
ATOM   1730 N  N   . HIS B 1 63  ? 21.551 16.410  13.693  1.00  7.55  ? 63   HIS F N   1 
ATOM   1731 C  CA  . HIS B 1 63  ? 22.488 15.837  12.753  1.00  6.82  ? 63   HIS F CA  1 
ATOM   1732 C  C   . HIS B 1 63  ? 23.614 15.165  13.457  1.00  6.84  ? 63   HIS F C   1 
ATOM   1733 O  O   . HIS B 1 63  ? 24.096 15.673  14.468  1.00  8.00  ? 63   HIS F O   1 
ATOM   1734 C  CB  . HIS B 1 63  ? 23.022 16.977  11.851  1.00  7.80  ? 63   HIS F CB  1 
ATOM   1735 C  CG  . HIS B 1 63  ? 21.987 17.539  10.921  1.00  7.50  ? 63   HIS F CG  1 
ATOM   1736 N  ND1 . HIS B 1 63  ? 22.321 18.401  9.920   1.00  8.17  ? 63   HIS F ND1 1 
ATOM   1737 C  CD2 . HIS B 1 63  ? 20.636 17.511  10.966  1.00  10.31 ? 63   HIS F CD2 1 
ATOM   1738 C  CE1 . HIS B 1 63  ? 21.221 18.806  9.321   1.00  9.07  ? 63   HIS F CE1 1 
ATOM   1739 N  NE2 . HIS B 1 63  ? 20.175 18.312  9.955   1.00  9.20  ? 63   HIS F NE2 1 
ATOM   1740 N  N   . PHE B 1 64  ? 24.115 14.038  12.978  1.00  6.73  ? 64   PHE F N   1 
ATOM   1741 C  CA  . PHE B 1 64  ? 25.251 13.409  13.554  1.00  7.09  ? 64   PHE F CA  1 
ATOM   1742 C  C   . PHE B 1 64  ? 26.447 14.286  13.418  1.00  7.73  ? 64   PHE F C   1 
ATOM   1743 O  O   . PHE B 1 64  ? 26.873 14.581  12.265  1.00  7.72  ? 64   PHE F O   1 
ATOM   1744 C  CB  . PHE B 1 64  ? 25.462 11.996  12.998  1.00  7.02  ? 64   PHE F CB  1 
ATOM   1745 C  CG  . PHE B 1 64  ? 26.642 11.294  13.510  1.00  7.36  ? 64   PHE F CG  1 
ATOM   1746 C  CD1 . PHE B 1 64  ? 26.847 11.179  14.880  1.00  9.35  ? 64   PHE F CD1 1 
ATOM   1747 C  CD2 . PHE B 1 64  ? 27.487 10.624  12.650  1.00  8.45  ? 64   PHE F CD2 1 
ATOM   1748 C  CE1 . PHE B 1 64  ? 27.912 10.509  15.347  1.00  10.39 ? 64   PHE F CE1 1 
ATOM   1749 C  CE2 . PHE B 1 64  ? 28.551 9.944   13.099  1.00  9.86  ? 64   PHE F CE2 1 
ATOM   1750 C  CZ  . PHE B 1 64  ? 28.797 9.895   14.475  1.00  10.61 ? 64   PHE F CZ  1 
ATOM   1751 N  N   . ASN B 1 65  ? 26.996 14.761  14.522  1.00  8.38  ? 65   ASN F N   1 
ATOM   1752 C  CA  . ASN B 1 65  ? 28.003 15.835  14.488  1.00  7.56  ? 65   ASN F CA  1 
ATOM   1753 C  C   . ASN B 1 65  ? 29.043 15.539  15.555  1.00  8.29  ? 65   ASN F C   1 
ATOM   1754 O  O   . ASN B 1 65  ? 29.269 16.350  16.458  1.00  8.66  ? 65   ASN F O   1 
ATOM   1755 C  CB  . ASN B 1 65  ? 27.351 17.188  14.743  1.00  8.30  ? 65   ASN F CB  1 
ATOM   1756 C  CG  . ASN B 1 65  ? 28.326 18.357  14.630  1.00  9.62  ? 65   ASN F CG  1 
ATOM   1757 O  OD1 . ASN B 1 65  ? 29.376 18.265  13.972  1.00  9.50  ? 65   ASN F OD1 1 
ATOM   1758 N  ND2 . ASN B 1 65  ? 27.924 19.498  15.225  1.00  9.46  ? 65   ASN F ND2 1 
ATOM   1759 N  N   . PRO B 1 66  ? 29.772 14.433  15.390  1.00  8.58  ? 66   PRO F N   1 
ATOM   1760 C  CA  . PRO B 1 66  ? 30.755 14.086  16.428  1.00  8.90  ? 66   PRO F CA  1 
ATOM   1761 C  C   . PRO B 1 66  ? 31.893 15.098  16.571  1.00  9.01  ? 66   PRO F C   1 
ATOM   1762 O  O   . PRO B 1 66  ? 32.513 15.130  17.636  1.00  9.84  ? 66   PRO F O   1 
ATOM   1763 C  CB  . PRO B 1 66  ? 31.218 12.699  16.002  1.00  9.05  ? 66   PRO F CB  1 
ATOM   1764 C  CG  . PRO B 1 66  ? 31.034 12.744  14.502  1.00  9.60  ? 66   PRO F CG  1 
ATOM   1765 C  CD  . PRO B 1 66  ? 29.742 13.434  14.301  1.00  8.15  ? 66   PRO F CD  1 
ATOM   1766 N  N   . LEU B 1 67  ? 32.178 15.924  15.548  1.00  9.46  ? 67   LEU F N   1 
ATOM   1767 C  CA  . LEU B 1 67  ? 33.323 16.836  15.572  1.00  10.13 ? 67   LEU F CA  1 
ATOM   1768 C  C   . LEU B 1 67  ? 32.949 18.250  15.944  1.00  10.81 ? 67   LEU F C   1 
ATOM   1769 O  O   . LEU B 1 67  ? 33.781 19.152  15.942  1.00  12.95 ? 67   LEU F O   1 
ATOM   1770 C  CB  . LEU B 1 67  ? 34.073 16.815  14.249  1.00  10.86 ? 67   LEU F CB  1 
ATOM   1771 C  CG  . LEU B 1 67  ? 34.786 15.534  13.927  1.00  13.80 ? 67   LEU F CG  1 
ATOM   1772 C  CD1 . LEU B 1 67  ? 35.261 15.537  12.514  1.00  14.92 ? 67   LEU F CD1 1 
ATOM   1773 C  CD2 . LEU B 1 67  ? 35.908 15.334  14.936  1.00  19.39 ? 67   LEU F CD2 1 
ATOM   1774 N  N   . SER B 1 68  ? 31.698 18.455  16.283  1.00  9.46  ? 68   SER F N   1 
ATOM   1775 C  CA  . SER B 1 68  ? 31.240 19.766  16.742  1.00  11.38 ? 68   SER F CA  1 
ATOM   1776 C  C   . SER B 1 68  ? 31.425 20.863  15.722  1.00  11.13 ? 68   SER F C   1 
ATOM   1777 O  O   . SER B 1 68  ? 31.795 21.986  16.032  1.00  14.65 ? 68   SER F O   1 
ATOM   1778 C  CB  . SER B 1 68  ? 31.893 20.125  18.111  1.00  11.14 ? 68   SER F CB  1 
ATOM   1779 O  OG  . SER B 1 68  ? 31.506 19.206  19.104  1.00  11.93 ? 68   SER F OG  1 
ATOM   1780 N  N   . ARG B 1 69  ? 31.099 20.557  14.486  1.00  11.02 ? 69   ARG F N   1 
ATOM   1781 C  CA  . ARG B 1 69  ? 31.216 21.501  13.372  1.00  11.32 ? 69   ARG F CA  1 
ATOM   1782 C  C   . ARG B 1 69  ? 29.833 22.084  13.058  1.00  11.07 ? 69   ARG F C   1 
ATOM   1783 O  O   . ARG B 1 69  ? 28.811 21.731  13.644  1.00  11.09 ? 69   ARG F O   1 
ATOM   1784 C  CB  . ARG B 1 69  ? 31.744 20.831  12.111  1.00  12.11 ? 69   ARG F CB  1 
ATOM   1785 C  CG  A ARG B 1 69  ? 32.989 19.968  12.222  0.70  16.71 ? 69   ARG F CG  1 
ATOM   1786 C  CG  B ARG B 1 69  ? 33.106 20.191  12.272  0.30  12.43 ? 69   ARG F CG  1 
ATOM   1787 C  CD  A ARG B 1 69  ? 34.326 20.642  12.083  0.70  23.67 ? 69   ARG F CD  1 
ATOM   1788 C  CD  B ARG B 1 69  ? 34.165 21.168  12.748  0.30  13.66 ? 69   ARG F CD  1 
ATOM   1789 N  NE  A ARG B 1 69  ? 35.373 19.610  11.985  0.70  22.96 ? 69   ARG F NE  1 
ATOM   1790 N  NE  B ARG B 1 69  ? 34.645 22.070  11.690  0.30  15.30 ? 69   ARG F NE  1 
ATOM   1791 C  CZ  A ARG B 1 69  ? 35.924 19.146  10.857  0.70  26.41 ? 69   ARG F CZ  1 
ATOM   1792 C  CZ  B ARG B 1 69  ? 35.474 21.731  10.689  0.30  15.50 ? 69   ARG F CZ  1 
ATOM   1793 N  NH1 A ARG B 1 69  ? 35.609 19.646  9.667   0.70  28.19 ? 69   ARG F NH1 1 
ATOM   1794 N  NH1 B ARG B 1 69  ? 35.954 20.496  10.573  0.30  16.26 ? 69   ARG F NH1 1 
ATOM   1795 N  NH2 A ARG B 1 69  ? 36.832 18.189  10.923  0.70  26.12 ? 69   ARG F NH2 1 
ATOM   1796 N  NH2 B ARG B 1 69  ? 35.838 22.641  9.783   0.30  15.87 ? 69   ARG F NH2 1 
ATOM   1797 N  N   . LYS B 1 70  ? 29.826 22.992  12.086  1.00  11.38 ? 70   LYS F N   1 
ATOM   1798 C  CA  . LYS B 1 70  ? 28.572 23.561  11.637  1.00  10.62 ? 70   LYS F CA  1 
ATOM   1799 C  C   . LYS B 1 70  ? 28.043 22.829  10.378  1.00  9.35  ? 70   LYS F C   1 
ATOM   1800 O  O   . LYS B 1 70  ? 28.764 22.048  9.746   1.00  10.22 ? 70   LYS F O   1 
ATOM   1801 C  CB  . LYS B 1 70  ? 28.736 25.064  11.357  1.00  11.79 ? 70   LYS F CB  1 
ATOM   1802 C  CG  . LYS B 1 70  ? 29.365 25.879  12.474  0.50  11.19 ? 70   LYS F CG  1 
ATOM   1803 C  CD  . LYS B 1 70  ? 28.582 25.763  13.749  0.50  13.04 ? 70   LYS F CD  1 
ATOM   1804 C  CE  . LYS B 1 70  ? 29.214 26.611  14.812  0.50  13.64 ? 70   LYS F CE  1 
ATOM   1805 N  NZ  . LYS B 1 70  ? 28.719 26.234  16.128  0.50  13.73 ? 70   LYS F NZ  1 
ATOM   1806 N  N   . HIS B 1 71  ? 26.796 23.091  10.020  1.00  8.54  ? 71   HIS F N   1 
ATOM   1807 C  CA  . HIS B 1 71  ? 26.159 22.363  8.924   1.00  8.90  ? 71   HIS F CA  1 
ATOM   1808 C  C   . HIS B 1 71  ? 26.738 22.800  7.560   1.00  9.03  ? 71   HIS F C   1 
ATOM   1809 O  O   . HIS B 1 71  ? 26.997 23.956  7.352   1.00  10.20 ? 71   HIS F O   1 
ATOM   1810 C  CB  . HIS B 1 71  ? 24.650 22.633  8.946   1.00  8.24  ? 71   HIS F CB  1 
ATOM   1811 C  CG  . HIS B 1 71  ? 23.897 21.914  7.907   1.00  8.62  ? 71   HIS F CG  1 
ATOM   1812 N  ND1 . HIS B 1 71  ? 23.665 20.559  7.950   1.00  7.49  ? 71   HIS F ND1 1 
ATOM   1813 C  CD2 . HIS B 1 71  ? 23.368 22.380  6.753   1.00  8.44  ? 71   HIS F CD2 1 
ATOM   1814 C  CE1 . HIS B 1 71  ? 22.987 20.228  6.855   1.00  7.76  ? 71   HIS F CE1 1 
ATOM   1815 N  NE2 . HIS B 1 71  ? 22.794 21.319  6.124   1.00  8.58  ? 71   HIS F NE2 1 
ATOM   1816 N  N   . GLY B 1 72  ? 26.858 21.843  6.648   1.00  8.94  ? 72   GLY F N   1 
ATOM   1817 C  CA  . GLY B 1 72  ? 27.267 22.126  5.301   1.00  8.51  ? 72   GLY F CA  1 
ATOM   1818 C  C   . GLY B 1 72  ? 26.712 21.112  4.354   1.00  8.84  ? 72   GLY F C   1 
ATOM   1819 O  O   . GLY B 1 72  ? 25.881 20.275  4.737   1.00  9.78  ? 72   GLY F O   1 
ATOM   1820 N  N   . GLY B 1 73  ? 27.227 21.169  3.141   1.00  10.23 ? 73   GLY F N   1 
ATOM   1821 C  CA  . GLY B 1 73  ? 27.065 20.096  2.209   1.00  11.37 ? 73   GLY F CA  1 
ATOM   1822 C  C   . GLY B 1 73  ? 28.228 19.087  2.199   1.00  10.28 ? 73   GLY F C   1 
ATOM   1823 O  O   . GLY B 1 73  ? 29.294 19.295  2.822   1.00  11.07 ? 73   GLY F O   1 
ATOM   1824 N  N   . PRO B 1 74  ? 27.974 17.923  1.599   1.00  10.45 ? 74   PRO F N   1 
ATOM   1825 C  CA  . PRO B 1 74  ? 28.942 16.858  1.709   1.00  10.58 ? 74   PRO F CA  1 
ATOM   1826 C  C   . PRO B 1 74  ? 30.305 17.216  1.105   1.00  12.42 ? 74   PRO F C   1 
ATOM   1827 O  O   . PRO B 1 74  ? 31.318 16.694  1.552   1.00  12.67 ? 74   PRO F O   1 
ATOM   1828 C  CB  . PRO B 1 74  ? 28.300 15.695  0.901   1.00  11.15 ? 74   PRO F CB  1 
ATOM   1829 C  CG  . PRO B 1 74  ? 27.211 16.341  0.097   1.00  12.24 ? 74   PRO F CG  1 
ATOM   1830 C  CD  . PRO B 1 74  ? 26.749 17.523  0.896   1.00  9.94  ? 74   PRO F CD  1 
ATOM   1831 N  N   . LYS B 1 75  ? 30.327 18.160  0.156   1.00  13.08 ? 75   LYS F N   1 
ATOM   1832 C  CA  . LYS B 1 75  ? 31.606 18.602  -0.410  1.00  15.81 ? 75   LYS F CA  1 
ATOM   1833 C  C   . LYS B 1 75  ? 32.374 19.599  0.427   1.00  16.36 ? 75   LYS F C   1 
ATOM   1834 O  O   . LYS B 1 75  ? 33.536 19.919  0.095   1.00  19.30 ? 75   LYS F O   1 
ATOM   1835 C  CB  . LYS B 1 75  ? 31.403 19.257  -1.753  1.00  16.56 ? 75   LYS F CB  1 
ATOM   1836 C  CG  . LYS B 1 75  ? 30.859 18.342  -2.795  1.00  19.75 ? 75   LYS F CG  1 
ATOM   1837 C  CD  . LYS B 1 75  ? 30.876 19.023  -4.165  1.00  21.21 ? 75   LYS F CD  1 
ATOM   1838 C  CE  . LYS B 1 75  ? 29.486 19.550  -4.540  1.00  24.74 ? 75   LYS F CE  1 
ATOM   1839 N  NZ  . LYS B 1 75  ? 29.322 20.002  -5.956  1.00  26.54 ? 75   LYS F NZ  1 
ATOM   1840 N  N   . ASP B 1 76  ? 31.759 20.129  1.488   1.00  16.15 ? 76   ASP F N   1 
ATOM   1841 C  CA  . ASP B 1 76  ? 32.391 21.132  2.314   1.00  16.17 ? 76   ASP F CA  1 
ATOM   1842 C  C   . ASP B 1 76  ? 33.309 20.534  3.360   1.00  16.95 ? 76   ASP F C   1 
ATOM   1843 O  O   . ASP B 1 76  ? 33.041 19.483  3.929   1.00  17.19 ? 76   ASP F O   1 
ATOM   1844 C  CB  . ASP B 1 76  ? 31.335 21.988  2.973   1.00  16.88 ? 76   ASP F CB  1 
ATOM   1845 C  CG  . ASP B 1 76  ? 30.514 22.753  1.993   1.00  17.38 ? 76   ASP F CG  1 
ATOM   1846 O  OD1 . ASP B 1 76  ? 31.071 23.185  0.959   1.00  22.95 ? 76   ASP F OD1 1 
ATOM   1847 O  OD2 . ASP B 1 76  ? 29.319 23.008  2.227   1.00  16.63 ? 76   ASP F OD2 1 
ATOM   1848 N  N   . GLU B 1 77  ? 34.420 21.211  3.634   1.00  18.54 ? 77   GLU F N   1 
ATOM   1849 C  CA  . GLU B 1 77  ? 35.217 20.946  4.841   1.00  17.38 ? 77   GLU F CA  1 
ATOM   1850 C  C   . GLU B 1 77  ? 34.393 21.171  6.117   1.00  16.81 ? 77   GLU F C   1 
ATOM   1851 O  O   . GLU B 1 77  ? 34.414 20.353  7.095   1.00  17.03 ? 77   GLU F O   1 
ATOM   1852 C  CB  . GLU B 1 77  ? 36.431 21.876  4.907   1.00  19.10 ? 77   GLU F CB  1 
ATOM   1853 C  CG  . GLU B 1 77  ? 37.261 21.978  3.624   0.010 17.70 ? 77   GLU F CG  1 
ATOM   1854 C  CD  . GLU B 1 77  ? 38.664 22.515  3.863   0.010 17.36 ? 77   GLU F CD  1 
ATOM   1855 O  OE1 . GLU B 1 77  ? 39.325 22.072  4.827   0.010 17.30 ? 77   GLU F OE1 1 
ATOM   1856 O  OE2 . GLU B 1 77  ? 39.111 23.377  3.077   0.010 17.10 ? 77   GLU F OE2 1 
ATOM   1857 N  N   . GLU B 1 78  ? 33.652 22.282  6.143   1.00  14.94 ? 78   GLU F N   1 
ATOM   1858 C  CA  . GLU B 1 78  ? 32.841 22.576  7.301   1.00  14.12 ? 78   GLU F CA  1 
ATOM   1859 C  C   . GLU B 1 78  ? 31.511 21.912  7.084   1.00  11.75 ? 78   GLU F C   1 
ATOM   1860 O  O   . GLU B 1 78  ? 30.672 22.419  6.361   1.00  12.70 ? 78   GLU F O   1 
ATOM   1861 C  CB  . GLU B 1 78  ? 32.631 24.095  7.501   1.00  14.20 ? 78   GLU F CB  1 
ATOM   1862 C  CG  . GLU B 1 78  ? 31.958 24.416  8.824   1.00  17.02 ? 78   GLU F CG  1 
ATOM   1863 C  CD  . GLU B 1 78  ? 32.875 24.193  10.005  1.00  20.83 ? 78   GLU F CD  1 
ATOM   1864 O  OE1 . GLU B 1 78  ? 34.126 24.261  9.880   1.00  25.69 ? 78   GLU F OE1 1 
ATOM   1865 O  OE2 . GLU B 1 78  ? 32.347 23.977  11.090  1.00  20.38 ? 78   GLU F OE2 1 
ATOM   1866 N  N   . ARG B 1 79  ? 31.310 20.751  7.720   1.00  11.12 ? 79   ARG F N   1 
ATOM   1867 C  CA  . ARG B 1 79  ? 30.037 20.028  7.654   1.00  10.31 ? 79   ARG F CA  1 
ATOM   1868 C  C   . ARG B 1 79  ? 29.960 19.176  8.896   1.00  9.20  ? 79   ARG F C   1 
ATOM   1869 O  O   . ARG B 1 79  ? 30.986 18.894  9.499   1.00  9.65  ? 79   ARG F O   1 
ATOM   1870 C  CB  . ARG B 1 79  ? 29.947 19.155  6.378   1.00  8.97  ? 79   ARG F CB  1 
ATOM   1871 C  CG  . ARG B 1 79  ? 31.098 18.161  6.288   1.00  10.21 ? 79   ARG F CG  1 
ATOM   1872 C  CD  . ARG B 1 79  ? 30.977 17.148  5.137   1.00  9.91  ? 79   ARG F CD  1 
ATOM   1873 N  NE  . ARG B 1 79  ? 30.225 16.001  5.574   1.00  9.07  ? 79   ARG F NE  1 
ATOM   1874 C  CZ  . ARG B 1 79  ? 30.152 14.892  4.861   1.00  9.55  ? 79   ARG F CZ  1 
ATOM   1875 N  NH1 . ARG B 1 79  ? 30.752 14.829  3.681   1.00  10.96 ? 79   ARG F NH1 1 
ATOM   1876 N  NH2 . ARG B 1 79  ? 29.515 13.824  5.351   1.00  9.60  ? 79   ARG F NH2 1 
ATOM   1877 N  N   . HIS B 1 80  ? 28.755 18.692  9.174   1.00  8.59  ? 80   HIS F N   1 
ATOM   1878 C  CA  . HIS B 1 80  ? 28.553 17.586  10.095  1.00  8.28  ? 80   HIS F CA  1 
ATOM   1879 C  C   . HIS B 1 80  ? 28.906 16.277  9.455   1.00  8.14  ? 80   HIS F C   1 
ATOM   1880 O  O   . HIS B 1 80  ? 28.714 16.166  8.235   1.00  8.79  ? 80   HIS F O   1 
ATOM   1881 C  CB  . HIS B 1 80  ? 27.127 17.571  10.547  1.00  7.46  ? 80   HIS F CB  1 
ATOM   1882 C  CG  . HIS B 1 80  ? 26.615 18.856  11.104  1.00  9.56  ? 80   HIS F CG  1 
ATOM   1883 N  ND1 . HIS B 1 80  ? 25.335 19.311  10.869  1.00  8.24  ? 80   HIS F ND1 1 
ATOM   1884 C  CD2 . HIS B 1 80  ? 27.184 19.714  11.975  1.00  10.14 ? 80   HIS F CD2 1 
ATOM   1885 C  CE1 . HIS B 1 80  ? 25.143 20.408  11.605  1.00  9.27  ? 80   HIS F CE1 1 
ATOM   1886 N  NE2 . HIS B 1 80  ? 26.250 20.654  12.288  1.00  9.55  ? 80   HIS F NE2 1 
ATOM   1887 N  N   . VAL B 1 81  ? 29.337 15.273  10.187  1.00  8.25  ? 81   VAL F N   1 
ATOM   1888 C  CA  . VAL B 1 81  ? 29.489 13.987  9.593   1.00  7.98  ? 81   VAL F CA  1 
ATOM   1889 C  C   . VAL B 1 81  ? 28.233 13.493  8.866   1.00  8.79  ? 81   VAL F C   1 
ATOM   1890 O  O   . VAL B 1 81  ? 28.338 12.897  7.764   1.00  8.34  ? 81   VAL F O   1 
ATOM   1891 C  CB  . VAL B 1 81  ? 29.957 12.948  10.586  1.00  9.95  ? 81   VAL F CB  1 
ATOM   1892 C  CG1 . VAL B 1 81  ? 29.882 11.529  9.972   1.00  8.58  ? 81   VAL F CG1 1 
ATOM   1893 C  CG2 . VAL B 1 81  ? 31.350 13.228  11.021  1.00  9.10  ? 81   VAL F CG2 1 
ATOM   1894 N  N   . GLY B 1 82  ? 27.069 13.739  9.387   1.00  7.39  ? 82   GLY F N   1 
ATOM   1895 C  CA  . GLY B 1 82  ? 25.831 13.270  8.815   1.00  8.19  ? 82   GLY F CA  1 
ATOM   1896 C  C   . GLY B 1 82  ? 25.314 14.061  7.624   1.00  8.28  ? 82   GLY F C   1 
ATOM   1897 O  O   . GLY B 1 82  ? 24.228 13.784  7.200   1.00  8.61  ? 82   GLY F O   1 
ATOM   1898 N  N   . ASP B 1 83  ? 26.049 15.072  7.163   1.00  8.06  ? 83   ASP F N   1 
ATOM   1899 C  CA  . ASP B 1 83  ? 25.578 15.918  6.046   1.00  8.63  ? 83   ASP F CA  1 
ATOM   1900 C  C   . ASP B 1 83  ? 25.817 15.308  4.658   1.00  8.07  ? 83   ASP F C   1 
ATOM   1901 O  O   . ASP B 1 83  ? 26.852 15.561  4.073   1.00  9.35  ? 83   ASP F O   1 
ATOM   1902 C  CB  . ASP B 1 83  ? 26.299 17.247  6.138   1.00  8.22  ? 83   ASP F CB  1 
ATOM   1903 C  CG  . ASP B 1 83  ? 25.828 18.102  7.329   1.00  8.59  ? 83   ASP F CG  1 
ATOM   1904 O  OD1 . ASP B 1 83  ? 24.792 17.715  7.954   1.00  8.69  ? 83   ASP F OD1 1 
ATOM   1905 O  OD2 . ASP B 1 83  ? 26.431 19.126  7.679   1.00  9.26  ? 83   ASP F OD2 1 
ATOM   1906 N  N   . LEU B 1 84  ? 24.857 14.522  4.221   1.00  7.63  ? 84   LEU F N   1 
ATOM   1907 C  CA  . LEU B 1 84  ? 24.938 13.886  2.923   1.00  8.22  ? 84   LEU F CA  1 
ATOM   1908 C  C   . LEU B 1 84  ? 24.240 14.664  1.809   1.00  8.63  ? 84   LEU F C   1 
ATOM   1909 O  O   . LEU B 1 84  ? 24.047 14.095  0.725   1.00  11.35 ? 84   LEU F O   1 
ATOM   1910 C  CB  . LEU B 1 84  ? 24.500 12.454  3.009   1.00  8.25  ? 84   LEU F CB  1 
ATOM   1911 C  CG  . LEU B 1 84  ? 25.386 11.552  3.888   1.00  9.43  ? 84   LEU F CG  1 
ATOM   1912 C  CD1 . LEU B 1 84  ? 24.781 10.171  3.922   1.00  10.46 ? 84   LEU F CD1 1 
ATOM   1913 C  CD2 . LEU B 1 84  ? 26.818 11.511  3.404   1.00  10.57 ? 84   LEU F CD2 1 
ATOM   1914 N  N   . GLY B 1 85  ? 23.795 15.869  2.029   1.00  7.88  ? 85   GLY F N   1 
ATOM   1915 C  CA  . GLY B 1 85  ? 23.303 16.712  0.907   1.00  8.63  ? 85   GLY F CA  1 
ATOM   1916 C  C   . GLY B 1 85  ? 21.872 16.452  0.617   1.00  8.69  ? 85   GLY F C   1 
ATOM   1917 O  O   . GLY B 1 85  ? 21.026 16.476  1.515   1.00  10.57 ? 85   GLY F O   1 
ATOM   1918 N  N   . ASN B 1 86  ? 21.595 16.263  -0.675  1.00  9.43  ? 86   ASN F N   1 
ATOM   1919 C  CA  . ASN B 1 86  ? 20.272 16.038  -1.174  1.00  9.82  ? 86   ASN F CA  1 
ATOM   1920 C  C   . ASN B 1 86  ? 20.289 14.826  -2.057  1.00  9.31  ? 86   ASN F C   1 
ATOM   1921 O  O   . ASN B 1 86  ? 21.301 14.554  -2.743  1.00  11.94 ? 86   ASN F O   1 
ATOM   1922 C  CB  . ASN B 1 86  ? 19.778 17.252  -1.987  1.00  9.50  ? 86   ASN F CB  1 
ATOM   1923 C  CG  . ASN B 1 86  ? 19.594 18.453  -1.128  1.00  9.66  ? 86   ASN F CG  1 
ATOM   1924 O  OD1 . ASN B 1 86  ? 18.659 18.460  -0.333  1.00  10.03 ? 86   ASN F OD1 1 
ATOM   1925 N  ND2 . ASN B 1 86  ? 20.349 19.494  -1.380  1.00  11.99 ? 86   ASN F ND2 1 
ATOM   1926 N  N   . VAL B 1 87  ? 19.147 14.157  -2.086  1.00  9.22  ? 87   VAL F N   1 
ATOM   1927 C  CA  . VAL B 1 87  ? 18.876 13.240  -3.173  1.00  8.46  ? 87   VAL F CA  1 
ATOM   1928 C  C   . VAL B 1 87  ? 17.912 13.931  -4.136  1.00  9.05  ? 87   VAL F C   1 
ATOM   1929 O  O   . VAL B 1 87  ? 17.192 14.849  -3.758  1.00  10.26 ? 87   VAL F O   1 
ATOM   1930 C  CB  . VAL B 1 87  ? 18.368 11.884  -2.648  1.00  10.00 ? 87   VAL F CB  1 
ATOM   1931 C  CG1 . VAL B 1 87  ? 19.448 11.243  -1.780  1.00  11.38 ? 87   VAL F CG1 1 
ATOM   1932 C  CG2 . VAL B 1 87  ? 17.046 12.029  -1.951  1.00  11.61 ? 87   VAL F CG2 1 
ATOM   1933 N  N   . THR B 1 88  ? 17.857 13.410  -5.374  1.00  10.59 ? 88   THR F N   1 
ATOM   1934 C  CA  . THR B 1 88  ? 17.042 14.017  -6.426  1.00  10.55 ? 88   THR F CA  1 
ATOM   1935 C  C   . THR B 1 88  ? 15.995 13.045  -6.885  1.00  9.51  ? 88   THR F C   1 
ATOM   1936 O  O   . THR B 1 88  ? 16.331 11.966  -7.405  1.00  10.68 ? 88   THR F O   1 
ATOM   1937 C  CB  . THR B 1 88  ? 17.884 14.454  -7.578  1.00  11.41 ? 88   THR F CB  1 
ATOM   1938 O  OG1 . THR B 1 88  ? 18.853 15.384  -7.106  1.00  13.98 ? 88   THR F OG1 1 
ATOM   1939 C  CG2 . THR B 1 88  ? 17.040 15.121  -8.640  1.00  12.56 ? 88   THR F CG2 1 
ATOM   1940 N  N   . ALA B 1 89  ? 14.721 13.432  -6.744  1.00  10.09 ? 89   ALA F N   1 
ATOM   1941 C  CA  . ALA B 1 89  ? 13.629 12.703  -7.296  1.00  11.46 ? 89   ALA F CA  1 
ATOM   1942 C  C   . ALA B 1 89  ? 13.207 13.253  -8.637  1.00  11.94 ? 89   ALA F C   1 
ATOM   1943 O  O   . ALA B 1 89  ? 13.137 14.439  -8.833  1.00  12.54 ? 89   ALA F O   1 
ATOM   1944 C  CB  . ALA B 1 89  ? 12.448 12.687  -6.332  1.00  11.24 ? 89   ALA F CB  1 
ATOM   1945 N  N   . ASP B 1 90  ? 12.892 12.304  -9.507  1.00  11.48 ? 90   ASP F N   1 
ATOM   1946 C  CA  A ASP B 1 90  ? 12.365 12.592  -10.837 0.80  12.24 ? 90   ASP F CA  1 
ATOM   1947 C  CA  B ASP B 1 90  ? 12.338 12.503  -10.851 0.20  11.73 ? 90   ASP F CA  1 
ATOM   1948 C  C   . ASP B 1 90  ? 10.856 12.811  -10.809 1.00  11.95 ? 90   ASP F C   1 
ATOM   1949 O  O   . ASP B 1 90  ? 10.239 12.725  -9.762  1.00  12.10 ? 90   ASP F O   1 
ATOM   1950 C  CB  A ASP B 1 90  ? 12.810 11.465  -11.810 0.80  13.28 ? 90   ASP F CB  1 
ATOM   1951 C  CB  B ASP B 1 90  ? 12.486 11.189  -11.628 0.20  11.43 ? 90   ASP F CB  1 
ATOM   1952 C  CG  A ASP B 1 90  ? 12.199 10.046  -11.534 0.80  17.21 ? 90   ASP F CG  1 
ATOM   1953 C  CG  B ASP B 1 90  ? 13.617 11.218  -12.607 0.20  12.62 ? 90   ASP F CG  1 
ATOM   1954 O  OD1 A ASP B 1 90  ? 11.110 9.840   -10.923 0.80  18.64 ? 90   ASP F OD1 1 
ATOM   1955 O  OD1 B ASP B 1 90  ? 14.754 10.900  -12.231 0.20  12.19 ? 90   ASP F OD1 1 
ATOM   1956 O  OD2 A ASP B 1 90  ? 12.834 9.061   -12.041 0.80  20.39 ? 90   ASP F OD2 1 
ATOM   1957 O  OD2 B ASP B 1 90  ? 13.352 11.564  -13.770 0.20  11.10 ? 90   ASP F OD2 1 
ATOM   1958 N  N   . LYS B 1 91  ? 10.233 13.084  -11.954 1.00  12.21 ? 91   LYS F N   1 
ATOM   1959 C  CA  . LYS B 1 91  ? 8.793  13.293  -12.004 1.00  13.13 ? 91   LYS F CA  1 
ATOM   1960 C  C   . LYS B 1 91  ? 7.998  12.017  -11.649 1.00  13.99 ? 91   LYS F C   1 
ATOM   1961 O  O   . LYS B 1 91  ? 6.799  12.125  -11.366 1.00  16.24 ? 91   LYS F O   1 
ATOM   1962 C  CB  . LYS B 1 91  ? 8.399  13.817  -13.402 1.00  14.29 ? 91   LYS F CB  1 
ATOM   1963 C  CG  . LYS B 1 91  ? 8.647  15.308  -13.545 1.00  14.43 ? 91   LYS F CG  1 
ATOM   1964 C  CD  . LYS B 1 91  ? 7.531  16.117  -12.929 1.00  17.53 ? 91   LYS F CD  1 
ATOM   1965 C  CE  . LYS B 1 91  ? 7.799  17.585  -13.052 1.00  18.52 ? 91   LYS F CE  1 
ATOM   1966 N  NZ  . LYS B 1 91  ? 6.730  18.397  -12.392 1.00  21.89 ? 91   LYS F NZ  1 
ATOM   1967 N  N   . ASP B 1 92  ? 8.625  10.839  -11.670 1.00  14.50 ? 92   ASP F N   1 
ATOM   1968 C  CA  . ASP B 1 92  ? 7.944  9.622   -11.216 1.00  14.51 ? 92   ASP F CA  1 
ATOM   1969 C  C   . ASP B 1 92  ? 8.056  9.459   -9.706  1.00  14.90 ? 92   ASP F C   1 
ATOM   1970 O  O   . ASP B 1 92  ? 7.565  8.495   -9.147  1.00  18.57 ? 92   ASP F O   1 
ATOM   1971 C  CB  A ASP B 1 92  ? 8.340  8.287   -11.934 0.53  15.16 ? 92   ASP F CB  1 
ATOM   1972 C  CB  B ASP B 1 92  ? 8.535  8.387   -11.896 0.47  15.12 ? 92   ASP F CB  1 
ATOM   1973 C  CG  A ASP B 1 92  ? 9.749  8.260   -12.503 0.53  17.73 ? 92   ASP F CG  1 
ATOM   1974 C  CG  B ASP B 1 92  ? 8.188  8.293   -13.364 0.47  17.49 ? 92   ASP F CG  1 
ATOM   1975 O  OD1 A ASP B 1 92  ? 10.483 7.239   -12.362 0.53  17.37 ? 92   ASP F OD1 1 
ATOM   1976 O  OD1 B ASP B 1 92  ? 7.186  8.896   -13.829 0.47  20.05 ? 92   ASP F OD1 1 
ATOM   1977 O  OD2 A ASP B 1 92  ? 10.125 9.246   -13.185 0.53  21.44 ? 92   ASP F OD2 1 
ATOM   1978 O  OD2 B ASP B 1 92  ? 8.934  7.565   -14.034 0.47  22.05 ? 92   ASP F OD2 1 
ATOM   1979 N  N   . GLY B 1 93  ? 8.708  10.393  -9.033  1.00  12.96 ? 93   GLY F N   1 
ATOM   1980 C  CA  . GLY B 1 93  ? 8.783  10.318  -7.574  1.00  13.01 ? 93   GLY F CA  1 
ATOM   1981 C  C   . GLY B 1 93  ? 9.926  9.448   -7.082  1.00  12.08 ? 93   GLY F C   1 
ATOM   1982 O  O   . GLY B 1 93  ? 10.067 9.215   -5.878  1.00  12.59 ? 93   GLY F O   1 
ATOM   1983 N  N   . VAL B 1 94  ? 10.784 8.999   -7.985  1.00  11.73 ? 94   VAL F N   1 
ATOM   1984 C  CA  . VAL B 1 94  ? 11.910 8.125   -7.652  1.00  11.01 ? 94   VAL F CA  1 
ATOM   1985 C  C   . VAL B 1 94  ? 13.245 8.836   -7.614  1.00  10.21 ? 94   VAL F C   1 
ATOM   1986 O  O   . VAL B 1 94  ? 13.647 9.511   -8.560  1.00  11.99 ? 94   VAL F O   1 
ATOM   1987 C  CB  . VAL B 1 94  ? 11.949 6.903   -8.583  1.00  12.66 ? 94   VAL F CB  1 
ATOM   1988 C  CG1 . VAL B 1 94  ? 13.106 5.972   -8.204  1.00  13.89 ? 94   VAL F CG1 1 
ATOM   1989 C  CG2 . VAL B 1 94  ? 10.624 6.182   -8.575  1.00  13.04 ? 94   VAL F CG2 1 
ATOM   1990 N  N   . ALA B 1 95  ? 13.961 8.662   -6.502  1.00  10.81 ? 95   ALA F N   1 
ATOM   1991 C  CA  . ALA B 1 95  ? 15.319 9.093   -6.426  1.00  10.69 ? 95   ALA F CA  1 
ATOM   1992 C  C   . ALA B 1 95  ? 16.235 7.894   -6.492  1.00  11.76 ? 95   ALA F C   1 
ATOM   1993 O  O   . ALA B 1 95  ? 16.143 7.006   -5.641  1.00  13.87 ? 95   ALA F O   1 
ATOM   1994 C  CB  . ALA B 1 95  ? 15.531 9.822   -5.072  1.00  11.21 ? 95   ALA F CB  1 
ATOM   1995 N  N   . ASP B 1 96  ? 17.128 7.852   -7.461  1.00  11.46 ? 96   ASP F N   1 
ATOM   1996 C  CA  . ASP B 1 96  ? 18.172 6.817   -7.536  1.00  11.62 ? 96   ASP F CA  1 
ATOM   1997 C  C   . ASP B 1 96  ? 19.391 7.429   -6.869  1.00  11.89 ? 96   ASP F C   1 
ATOM   1998 O  O   . ASP B 1 96  ? 19.879 8.476   -7.225  1.00  13.93 ? 96   ASP F O   1 
ATOM   1999 C  CB  . ASP B 1 96  ? 18.354 6.352   -8.990  1.00  13.07 ? 96   ASP F CB  1 
ATOM   2000 C  CG  . ASP B 1 96  ? 17.116 5.554   -9.466  1.00  14.78 ? 96   ASP F CG  1 
ATOM   2001 O  OD1 . ASP B 1 96  ? 16.681 4.588   -8.753  1.00  18.33 ? 96   ASP F OD1 1 
ATOM   2002 O  OD2 . ASP B 1 96  ? 16.510 5.910   -10.501 1.00  21.50 ? 96   ASP F OD2 1 
ATOM   2003 N  N   . VAL B 1 97  ? 19.798 6.775   -5.803  1.00  10.96 ? 97   VAL F N   1 
ATOM   2004 C  CA  . VAL B 1 97  ? 20.834 7.278   -4.955  1.00  11.51 ? 97   VAL F CA  1 
ATOM   2005 C  C   . VAL B 1 97  ? 22.134 6.651   -5.270  1.00  11.00 ? 97   VAL F C   1 
ATOM   2006 O  O   . VAL B 1 97  ? 22.243 5.436   -5.365  1.00  11.91 ? 97   VAL F O   1 
ATOM   2007 C  CB  . VAL B 1 97  ? 20.539 7.044   -3.483  1.00  11.23 ? 97   VAL F CB  1 
ATOM   2008 C  CG1 . VAL B 1 97  ? 21.639 7.610   -2.571  1.00  12.38 ? 97   VAL F CG1 1 
ATOM   2009 C  CG2 . VAL B 1 97  ? 19.193 7.664   -3.114  1.00  11.65 ? 97   VAL F CG2 1 
ATOM   2010 N  N   . SER B 1 98  ? 23.108 7.510   -5.485  1.00  12.93 ? 98   SER F N   1 
ATOM   2011 C  CA  . SER B 1 98  ? 24.427 7.115   -5.774  1.00  12.70 ? 98   SER F CA  1 
ATOM   2012 C  C   . SER B 1 98  ? 25.282 8.234   -5.207  1.00  12.33 ? 98   SER F C   1 
ATOM   2013 O  O   . SER B 1 98  ? 25.380 9.341   -5.773  1.00  15.53 ? 98   SER F O   1 
ATOM   2014 C  CB  . SER B 1 98  ? 24.602 6.958   -7.249  1.00  13.48 ? 98   SER F CB  1 
ATOM   2015 O  OG  . SER B 1 98  ? 25.850 6.331   -7.452  1.00  21.12 ? 98   SER F OG  1 
ATOM   2016 N  N   . ILE B 1 99  ? 26.007 7.921   -4.162  1.00  12.72 ? 99   ILE F N   1 
ATOM   2017 C  CA  . ILE B 1 99  ? 26.886 8.856   -3.422  1.00  13.32 ? 99   ILE F CA  1 
ATOM   2018 C  C   . ILE B 1 99  ? 28.202 8.098   -3.097  1.00  12.46 ? 99   ILE F C   1 
ATOM   2019 O  O   . ILE B 1 99  ? 28.136 6.908   -2.769  1.00  13.33 ? 99   ILE F O   1 
ATOM   2020 C  CB  . ILE B 1 99  ? 26.156 9.343   -2.092  1.00  11.84 ? 99   ILE F CB  1 
ATOM   2021 C  CG1 . ILE B 1 99  ? 24.980 10.260  -2.448  1.00  14.82 ? 99   ILE F CG1 1 
ATOM   2022 C  CG2 . ILE B 1 99  ? 27.103 10.043  -1.148  1.00  14.66 ? 99   ILE F CG2 1 
ATOM   2023 C  CD1 . ILE B 1 99  ? 24.105 10.570  -1.249  1.00  16.18 ? 99   ILE F CD1 1 
ATOM   2024 N  N   . GLU B 1 100 ? 29.362 8.775   -3.137  1.00  11.60 ? 100  GLU F N   1 
ATOM   2025 C  CA  . GLU B 1 100 ? 30.568 8.379   -2.454  1.00  11.58 ? 100  GLU F CA  1 
ATOM   2026 C  C   . GLU B 1 100 ? 30.893 9.458   -1.426  1.00  10.98 ? 100  GLU F C   1 
ATOM   2027 O  O   . GLU B 1 100 ? 30.913 10.636  -1.762  1.00  12.31 ? 100  GLU F O   1 
ATOM   2028 C  CB  . GLU B 1 100 ? 31.751 8.262   -3.407  1.00  11.86 ? 100  GLU F CB  1 
ATOM   2029 C  CG  A GLU B 1 100 ? 32.928 7.575   -2.738  0.70  15.53 ? 100  GLU F CG  1 
ATOM   2030 C  CG  B GLU B 1 100 ? 32.792 7.298   -3.007  0.30  15.71 ? 100  GLU F CG  1 
ATOM   2031 C  CD  A GLU B 1 100 ? 33.115 6.109   -3.088  0.50  17.82 ? 100  GLU F CD  1 
ATOM   2032 C  CD  B GLU B 1 100 ? 32.903 6.205   -4.035  0.30  16.88 ? 100  GLU F CD  1 
ATOM   2033 O  OE1 A GLU B 1 100 ? 32.263 5.293   -2.734  0.50  17.91 ? 100  GLU F OE1 1 
ATOM   2034 O  OE1 B GLU B 1 100 ? 31.989 5.360   -4.094  0.30  19.64 ? 100  GLU F OE1 1 
ATOM   2035 O  OE2 A GLU B 1 100 ? 34.166 5.783   -3.680  0.50  18.16 ? 100  GLU F OE2 1 
ATOM   2036 O  OE2 B GLU B 1 100 ? 33.879 6.234   -4.817  0.30  18.62 ? 100  GLU F OE2 1 
ATOM   2037 N  N   . ASP B 1 101 ? 31.157 9.057   -0.187  1.00  10.15 ? 101  ASP F N   1 
ATOM   2038 C  CA  . ASP B 1 101 ? 31.454 10.006  0.853   1.00  10.49 ? 101  ASP F CA  1 
ATOM   2039 C  C   . ASP B 1 101 ? 32.657 9.571   1.629   1.00  10.19 ? 101  ASP F C   1 
ATOM   2040 O  O   . ASP B 1 101 ? 32.756 8.396   2.020   1.00  12.23 ? 101  ASP F O   1 
ATOM   2041 C  CB  . ASP B 1 101 ? 30.217 10.263  1.737   1.00  10.20 ? 101  ASP F CB  1 
ATOM   2042 C  CG  . ASP B 1 101 ? 30.403 11.512  2.617   1.00  10.69 ? 101  ASP F CG  1 
ATOM   2043 O  OD1 . ASP B 1 101 ? 30.317 12.616  2.027   1.00  12.53 ? 101  ASP F OD1 1 
ATOM   2044 O  OD2 . ASP B 1 101 ? 30.732 11.383  3.802   1.00  10.38 ? 101  ASP F OD2 1 
ATOM   2045 N  N   . SER B 1 102 ? 33.535 10.525  1.941   1.00  11.10 ? 102  SER F N   1 
ATOM   2046 C  CA  . SER B 1 102 ? 34.784 10.302  2.577   1.00  13.02 ? 102  SER F CA  1 
ATOM   2047 C  C   . SER B 1 102 ? 34.781 10.621  4.087   1.00  11.99 ? 102  SER F C   1 
ATOM   2048 O  O   . SER B 1 102 ? 35.781 10.403  4.792   1.00  13.95 ? 102  SER F O   1 
ATOM   2049 C  CB  . SER B 1 102 ? 35.822 11.209  1.865   1.00  14.98 ? 102  SER F CB  1 
ATOM   2050 O  OG  A SER B 1 102 ? 35.691 12.526  2.315   0.80  21.35 ? 102  SER F OG  1 
ATOM   2051 O  OG  B SER B 1 102 ? 36.233 10.439  0.759   0.20  11.42 ? 102  SER F OG  1 
ATOM   2052 N  N   . VAL B 1 103 ? 33.658 11.160  4.582   1.00  10.26 ? 103  VAL F N   1 
ATOM   2053 C  CA  . VAL B 1 103 ? 33.517 11.584  5.969   1.00  9.76  ? 103  VAL F CA  1 
ATOM   2054 C  C   . VAL B 1 103 ? 32.722 10.602  6.856   1.00  9.67  ? 103  VAL F C   1 
ATOM   2055 O  O   . VAL B 1 103 ? 33.143 10.277  7.962   1.00  11.84 ? 103  VAL F O   1 
ATOM   2056 C  CB  . VAL B 1 103 ? 32.929 13.019  6.008   1.00  9.80  ? 103  VAL F CB  1 
ATOM   2057 C  CG1 . VAL B 1 103 ? 32.717 13.476  7.457   1.00  11.82 ? 103  VAL F CG1 1 
ATOM   2058 C  CG2 . VAL B 1 103 ? 33.843 14.028  5.303   1.00  11.81 ? 103  VAL F CG2 1 
ATOM   2059 N  N   . ILE B 1 104 ? 31.604 10.116  6.388   1.00  9.47  ? 104  ILE F N   1 
ATOM   2060 C  CA  . ILE B 1 104 ? 30.908 9.029   7.090   1.00  8.58  ? 104  ILE F CA  1 
ATOM   2061 C  C   . ILE B 1 104 ? 31.874 7.809   7.081   1.00  9.24  ? 104  ILE F C   1 
ATOM   2062 O  O   . ILE B 1 104 ? 32.752 7.713   6.189   1.00  10.71 ? 104  ILE F O   1 
ATOM   2063 C  CB  . ILE B 1 104 ? 29.530 8.683   6.451   1.00  8.21  ? 104  ILE F CB  1 
ATOM   2064 C  CG1 . ILE B 1 104 ? 29.655 8.244   4.988   1.00  9.35  ? 104  ILE F CG1 1 
ATOM   2065 C  CG2 . ILE B 1 104 ? 28.589 9.827   6.617   1.00  8.25  ? 104  ILE F CG2 1 
ATOM   2066 C  CD1 . ILE B 1 104 ? 28.443 7.632   4.421   1.00  8.83  ? 104  ILE F CD1 1 
ATOM   2067 N  N   . SER B 1 105 ? 31.637 6.877   8.010   1.00  9.17  ? 105  SER F N   1 
ATOM   2068 C  CA  . SER B 1 105 ? 32.339 5.645   8.037   1.00  10.04 ? 105  SER F CA  1 
ATOM   2069 C  C   . SER B 1 105 ? 31.449 4.578   8.588   1.00  9.34  ? 105  SER F C   1 
ATOM   2070 O  O   . SER B 1 105 ? 30.432 4.857   9.207   1.00  9.69  ? 105  SER F O   1 
ATOM   2071 C  CB  . SER B 1 105 ? 33.572 5.786   8.891   1.00  10.91 ? 105  SER F CB  1 
ATOM   2072 O  OG  . SER B 1 105 ? 34.422 4.666   8.750   1.00  13.20 ? 105  SER F OG  1 
ATOM   2073 N  N   . LEU B 1 106 ? 31.863 3.333   8.385   1.00  9.86  ? 106  LEU F N   1 
ATOM   2074 C  CA  . LEU B 1 106 ? 31.194 2.189   8.976   1.00  11.10 ? 106  LEU F CA  1 
ATOM   2075 C  C   . LEU B 1 106 ? 31.990 1.620   10.131  1.00  13.00 ? 106  LEU F C   1 
ATOM   2076 O  O   . LEU B 1 106 ? 31.642 0.553   10.659  1.00  14.03 ? 106  LEU F O   1 
ATOM   2077 C  CB  . LEU B 1 106 ? 30.881 1.138   7.911   1.00  10.77 ? 106  LEU F CB  1 
ATOM   2078 C  CG  . LEU B 1 106 ? 30.103 1.628   6.723   1.00  10.84 ? 106  LEU F CG  1 
ATOM   2079 C  CD1 . LEU B 1 106 ? 29.809 0.400   5.783   1.00  14.21 ? 106  LEU F CD1 1 
ATOM   2080 C  CD2 . LEU B 1 106 ? 28.876 2.295   7.192   1.00  11.15 ? 106  LEU F CD2 1 
ATOM   2081 N  N   . SER B 1 107 ? 32.991 2.381   10.591  1.00  15.09 ? 107  SER F N   1 
ATOM   2082 C  CA  . SER B 1 107 ? 33.678 2.109   11.893  1.00  15.61 ? 107  SER F CA  1 
ATOM   2083 C  C   . SER B 1 107 ? 34.281 3.391   12.509  1.00  15.91 ? 107  SER F C   1 
ATOM   2084 O  O   . SER B 1 107 ? 34.271 4.476   11.892  1.00  15.75 ? 107  SER F O   1 
ATOM   2085 C  CB  . SER B 1 107 ? 34.704 1.016   11.759  1.00  17.99 ? 107  SER F CB  1 
ATOM   2086 O  OG  . SER B 1 107 ? 35.786 1.455   10.957  1.00  21.39 ? 107  SER F OG  1 
ATOM   2087 N  N   . GLY B 1 108 ? 34.698 3.303   13.778  1.00  16.65 ? 108  GLY F N   1 
ATOM   2088 C  CA  . GLY B 1 108 ? 35.302 4.424   14.481  1.00  16.64 ? 108  GLY F CA  1 
ATOM   2089 C  C   . GLY B 1 108 ? 34.312 5.467   14.941  1.00  16.45 ? 108  GLY F C   1 
ATOM   2090 O  O   . GLY B 1 108 ? 33.137 5.250   14.905  1.00  15.82 ? 108  GLY F O   1 
ATOM   2091 N  N   . ASP B 1 109 ? 34.764 6.628   15.410  1.00  17.13 ? 109  ASP F N   1 
ATOM   2092 C  CA  . ASP B 1 109 ? 33.817 7.570   15.949  1.00  16.71 ? 109  ASP F CA  1 
ATOM   2093 C  C   . ASP B 1 109 ? 33.114 8.402   14.864  1.00  15.94 ? 109  ASP F C   1 
ATOM   2094 O  O   . ASP B 1 109 ? 32.254 9.206   15.206  1.00  17.21 ? 109  ASP F O   1 
ATOM   2095 C  CB  . ASP B 1 109 ? 34.405 8.406   17.117  1.00  18.73 ? 109  ASP F CB  1 
ATOM   2096 C  CG  . ASP B 1 109 ? 35.294 9.517   16.650  1.00  18.78 ? 109  ASP F CG  1 
ATOM   2097 O  OD1 . ASP B 1 109 ? 35.585 9.612   15.423  1.00  22.48 ? 109  ASP F OD1 1 
ATOM   2098 O  OD2 . ASP B 1 109 ? 35.697 10.303  17.511  1.00  20.01 ? 109  ASP F OD2 1 
ATOM   2099 N  N   . HIS B 1 110 ? 33.427 8.174   13.562  1.00  13.74 ? 110  HIS F N   1 
ATOM   2100 C  CA  . HIS B 1 110 ? 32.524 8.696   12.527  1.00  13.37 ? 110  HIS F CA  1 
ATOM   2101 C  C   . HIS B 1 110 ? 31.572 7.606   12.034  1.00  11.23 ? 110  HIS F C   1 
ATOM   2102 O  O   . HIS B 1 110 ? 30.868 7.806   11.030  1.00  11.57 ? 110  HIS F O   1 
ATOM   2103 C  CB  . HIS B 1 110 ? 33.265 9.226   11.305  1.00  14.19 ? 110  HIS F CB  1 
ATOM   2104 C  CG  . HIS B 1 110 ? 34.197 10.362  11.564  1.00  17.40 ? 110  HIS F CG  1 
ATOM   2105 N  ND1 . HIS B 1 110 ? 34.631 11.193  10.550  1.00  19.09 ? 110  HIS F ND1 1 
ATOM   2106 C  CD2 . HIS B 1 110 ? 34.824 10.769  12.683  1.00  21.13 ? 110  HIS F CD2 1 
ATOM   2107 C  CE1 . HIS B 1 110 ? 35.485 12.067  11.045  1.00  22.31 ? 110  HIS F CE1 1 
ATOM   2108 N  NE2 . HIS B 1 110 ? 35.617 11.838  12.337  1.00  23.66 ? 110  HIS F NE2 1 
HETATM 2109 N  N   . CSO B 1 111 ? 31.503 6.479   12.746  1.00  11.66 ? 111  CSO F N   1 
HETATM 2110 C  CA  . CSO B 1 111 ? 30.644 5.373   12.358  1.00  11.89 ? 111  CSO F CA  1 
HETATM 2111 C  CB  . CSO B 1 111 ? 30.881 4.185   13.260  1.00  12.19 ? 111  CSO F CB  1 
HETATM 2112 S  SG  . CSO B 1 111 ? 29.981 2.733   12.694  1.00  15.94 ? 111  CSO F SG  1 
HETATM 2113 C  C   . CSO B 1 111 ? 29.179 5.754   12.430  1.00  9.51  ? 111  CSO F C   1 
HETATM 2114 O  O   . CSO B 1 111 ? 28.707 6.359   13.400  1.00  9.81  ? 111  CSO F O   1 
HETATM 2115 O  OD  . CSO B 1 111 ? 30.383 1.422   13.967  1.00  20.49 ? 111  CSO F OD  1 
ATOM   2116 N  N   . ILE B 1 112 ? 28.437 5.353   11.402  1.00  8.39  ? 112  ILE F N   1 
ATOM   2117 C  CA  . ILE B 1 112 ? 27.033 5.638   11.260  1.00  8.15  ? 112  ILE F CA  1 
ATOM   2118 C  C   . ILE B 1 112 ? 26.096 4.481   11.570  1.00  7.48  ? 112  ILE F C   1 
ATOM   2119 O  O   . ILE B 1 112 ? 24.902 4.610   11.538  1.00  7.66  ? 112  ILE F O   1 
ATOM   2120 C  CB  . ILE B 1 112 ? 26.679 6.312   9.942   1.00  8.16  ? 112  ILE F CB  1 
ATOM   2121 C  CG1 . ILE B 1 112 ? 26.993 5.374   8.792   1.00  8.90  ? 112  ILE F CG1 1 
ATOM   2122 C  CG2 . ILE B 1 112 ? 27.426 7.677   9.749   1.00  8.42  ? 112  ILE F CG2 1 
ATOM   2123 C  CD1 . ILE B 1 112 ? 26.472 5.929   7.446   1.00  9.66  ? 112  ILE F CD1 1 
ATOM   2124 N  N   . ILE B 1 113 ? 26.690 3.303   11.739  1.00  7.85  ? 113  ILE F N   1 
ATOM   2125 C  CA  . ILE B 1 113 ? 25.894 2.143   12.144  1.00  8.54  ? 113  ILE F CA  1 
ATOM   2126 C  C   . ILE B 1 113 ? 25.160 2.365   13.471  1.00  7.74  ? 113  ILE F C   1 
ATOM   2127 O  O   . ILE B 1 113 ? 25.745 2.940   14.382  1.00  9.49  ? 113  ILE F O   1 
ATOM   2128 C  CB  . ILE B 1 113 ? 26.745 0.853   12.134  1.00  9.83  ? 113  ILE F CB  1 
ATOM   2129 C  CG1 . ILE B 1 113 ? 27.122 0.524   10.624  1.00  11.49 ? 113  ILE F CG1 1 
ATOM   2130 C  CG2 . ILE B 1 113 ? 26.019 -0.317  12.808  1.00  10.04 ? 113  ILE F CG2 1 
ATOM   2131 C  CD1 . ILE B 1 113 ? 28.115 -0.545  10.416  1.00  14.42 ? 113  ILE F CD1 1 
ATOM   2132 N  N   . GLY B 1 114 ? 23.883 2.060   13.463  1.00  7.29  ? 114  GLY F N   1 
ATOM   2133 C  CA  . GLY B 1 114 ? 23.070 2.274   14.667  1.00  7.51  ? 114  GLY F CA  1 
ATOM   2134 C  C   . GLY B 1 114 ? 22.519 3.643   14.782  1.00  7.55  ? 114  GLY F C   1 
ATOM   2135 O  O   . GLY B 1 114 ? 21.881 3.985   15.777  1.00  8.54  ? 114  GLY F O   1 
ATOM   2136 N  N   . ARG B 1 115 ? 22.722 4.474   13.773  1.00  8.14  ? 115  ARG F N   1 
ATOM   2137 C  CA  . ARG B 1 115 ? 22.196 5.853   13.707  1.00  7.14  ? 115  ARG F CA  1 
ATOM   2138 C  C   . ARG B 1 115 ? 21.052 5.895   12.724  1.00  7.11  ? 115  ARG F C   1 
ATOM   2139 O  O   . ARG B 1 115 ? 20.685 4.871   12.174  1.00  9.04  ? 115  ARG F O   1 
ATOM   2140 C  CB  . ARG B 1 115 ? 23.304 6.846   13.444  1.00  7.56  ? 115  ARG F CB  1 
ATOM   2141 C  CG  . ARG B 1 115 ? 24.495 6.650   14.381  1.00  7.88  ? 115  ARG F CG  1 
ATOM   2142 C  CD  . ARG B 1 115 ? 25.429 7.792   14.383  1.00  8.86  ? 115  ARG F CD  1 
ATOM   2143 N  NE  . ARG B 1 115 ? 26.537 7.512   15.314  1.00  9.23  ? 115  ARG F NE  1 
ATOM   2144 C  CZ  . ARG B 1 115 ? 26.577 7.817   16.619  1.00  9.81  ? 115  ARG F CZ  1 
ATOM   2145 N  NH1 . ARG B 1 115 ? 25.552 8.404   17.214  1.00  9.16  ? 115  ARG F NH1 1 
ATOM   2146 N  NH2 . ARG B 1 115 ? 27.659 7.552   17.345  1.00  10.27 ? 115  ARG F NH2 1 
ATOM   2147 N  N   . THR B 1 116 ? 20.420 7.040   12.534  1.00  7.14  ? 116  THR F N   1 
ATOM   2148 C  CA  . THR B 1 116 ? 19.208 7.103   11.701  1.00  7.19  ? 116  THR F CA  1 
ATOM   2149 C  C   . THR B 1 116 ? 19.484 7.854   10.386  1.00  7.14  ? 116  THR F C   1 
ATOM   2150 O  O   . THR B 1 116 ? 19.944 8.972   10.424  1.00  8.30  ? 116  THR F O   1 
ATOM   2151 C  CB  . THR B 1 116 ? 18.041 7.751   12.413  1.00  7.15  ? 116  THR F CB  1 
ATOM   2152 O  OG1 . THR B 1 116 ? 17.689 6.949   13.542  1.00  8.67  ? 116  THR F OG1 1 
ATOM   2153 C  CG2 . THR B 1 116 ? 16.796 7.941   11.567  1.00  7.78  ? 116  THR F CG2 1 
ATOM   2154 N  N   . LEU B 1 117 ? 19.126 7.206   9.256   1.00  6.74  ? 117  LEU F N   1 
ATOM   2155 C  CA  . LEU B 1 117 ? 19.143 7.926   7.972   1.00  6.20  ? 117  LEU F CA  1 
ATOM   2156 C  C   . LEU B 1 117 ? 17.770 8.534   7.761   1.00  6.27  ? 117  LEU F C   1 
ATOM   2157 O  O   . LEU B 1 117 ? 16.731 7.902   8.035   1.00  7.58  ? 117  LEU F O   1 
ATOM   2158 C  CB  . LEU B 1 117 ? 19.440 6.913   6.889   1.00  7.35  ? 117  LEU F CB  1 
ATOM   2159 C  CG  . LEU B 1 117 ? 19.676 7.477   5.479   1.00  7.77  ? 117  LEU F CG  1 
ATOM   2160 C  CD1 . LEU B 1 117 ? 20.877 8.336   5.406   1.00  8.06  ? 117  LEU F CD1 1 
ATOM   2161 C  CD2 . LEU B 1 117 ? 19.780 6.339   4.479   1.00  8.49  ? 117  LEU F CD2 1 
ATOM   2162 N  N   . VAL B 1 118 ? 17.765 9.791   7.317   1.00  7.28  ? 118  VAL F N   1 
ATOM   2163 C  CA  . VAL B 1 118 ? 16.520 10.517  7.164   1.00  7.51  ? 118  VAL F CA  1 
ATOM   2164 C  C   . VAL B 1 118 ? 16.503 11.166  5.755   1.00  7.14  ? 118  VAL F C   1 
ATOM   2165 O  O   . VAL B 1 118 ? 17.470 11.798  5.400   1.00  8.06  ? 118  VAL F O   1 
ATOM   2166 C  CB  . VAL B 1 118 ? 16.402 11.664  8.225   1.00  7.19  ? 118  VAL F CB  1 
ATOM   2167 C  CG1 . VAL B 1 118 ? 15.134 12.423  8.044   1.00  8.92  ? 118  VAL F CG1 1 
ATOM   2168 C  CG2 . VAL B 1 118 ? 16.483 11.117  9.619   1.00  7.31  ? 118  VAL F CG2 1 
ATOM   2169 N  N   . VAL B 1 119 ? 15.377 11.081  5.060   1.00  7.18  ? 119  VAL F N   1 
ATOM   2170 C  CA  . VAL B 1 119 ? 15.119 11.897  3.854   1.00  8.10  ? 119  VAL F CA  1 
ATOM   2171 C  C   . VAL B 1 119 ? 14.030 12.925  4.180   1.00  8.68  ? 119  VAL F C   1 
ATOM   2172 O  O   . VAL B 1 119 ? 13.021 12.603  4.819   1.00  9.06  ? 119  VAL F O   1 
ATOM   2173 C  CB  . VAL B 1 119 ? 14.752 11.014  2.578   1.00  8.62  ? 119  VAL F CB  1 
ATOM   2174 C  CG1 . VAL B 1 119 ? 13.532 10.171  2.812   1.00  10.24 ? 119  VAL F CG1 1 
ATOM   2175 C  CG2 . VAL B 1 119 ? 14.578 11.896  1.377   1.00  7.95  ? 119  VAL F CG2 1 
ATOM   2176 N  N   . HIS B 1 120 ? 14.245 14.154  3.697   1.00  8.30  ? 120  HIS F N   1 
ATOM   2177 C  CA  . HIS B 1 120 ? 13.463 15.294  4.062   1.00  8.52  ? 120  HIS F CA  1 
ATOM   2178 C  C   . HIS B 1 120 ? 12.461 15.787  2.997   1.00  8.63  ? 120  HIS F C   1 
ATOM   2179 O  O   . HIS B 1 120 ? 12.576 15.487  1.807   1.00  9.69  ? 120  HIS F O   1 
ATOM   2180 C  CB  . HIS B 1 120 ? 14.391 16.445  4.472   1.00  9.63  ? 120  HIS F CB  1 
ATOM   2181 C  CG  . HIS B 1 120 ? 14.944 16.313  5.844   1.00  8.79  ? 120  HIS F CG  1 
ATOM   2182 N  ND1 . HIS B 1 120 ? 14.306 16.873  6.917   1.00  10.11 ? 120  HIS F ND1 1 
ATOM   2183 C  CD2 . HIS B 1 120 ? 16.077 15.718  6.312   1.00  7.99  ? 120  HIS F CD2 1 
ATOM   2184 C  CE1 . HIS B 1 120 ? 15.002 16.602  7.991   1.00  9.01  ? 120  HIS F CE1 1 
ATOM   2185 N  NE2 . HIS B 1 120 ? 16.054 15.893  7.669   1.00  8.80  ? 120  HIS F NE2 1 
ATOM   2186 N  N   . GLU B 1 121 ? 11.517 16.577  3.510   1.00  10.24 ? 121  GLU F N   1 
ATOM   2187 C  CA  . GLU B 1 121 ? 10.477 17.244  2.705   1.00  11.61 ? 121  GLU F CA  1 
ATOM   2188 C  C   . GLU B 1 121 ? 11.010 18.116  1.588   1.00  12.02 ? 121  GLU F C   1 
ATOM   2189 O  O   . GLU B 1 121 ? 10.513 18.102  0.455   1.00  12.29 ? 121  GLU F O   1 
ATOM   2190 C  CB  . GLU B 1 121 ? 9.653  18.117  3.612   1.00  12.59 ? 121  GLU F CB  1 
ATOM   2191 C  CG  . GLU B 1 121 ? 8.558  18.883  2.950   1.00  15.33 ? 121  GLU F CG  1 
ATOM   2192 C  CD  . GLU B 1 121 ? 7.852  19.838  3.930   1.00  16.63 ? 121  GLU F CD  1 
ATOM   2193 O  OE1 . GLU B 1 121 ? 8.392  20.081  5.023   1.00  17.14 ? 121  GLU F OE1 1 
ATOM   2194 O  OE2 . GLU B 1 121 ? 6.751  20.348  3.586   1.00  22.68 ? 121  GLU F OE2 1 
ATOM   2195 N  N   . LYS B 1 122 ? 11.997 18.930  1.953   1.00  11.77 ? 122  LYS F N   1 
ATOM   2196 C  CA  . LYS B 1 122 ? 12.528 20.028  1.148   1.00  12.67 ? 122  LYS F CA  1 
ATOM   2197 C  C   . LYS B 1 122 ? 14.010 19.798  0.936   1.00  11.56 ? 122  LYS F C   1 
ATOM   2198 O  O   . LYS B 1 122 ? 14.648 18.871  1.485   1.00  10.24 ? 122  LYS F O   1 
ATOM   2199 C  CB  . LYS B 1 122 ? 12.306 21.391  1.882   1.00  14.53 ? 122  LYS F CB  1 
ATOM   2200 C  CG  . LYS B 1 122 ? 10.982 21.496  2.526   1.00  17.89 ? 122  LYS F CG  1 
ATOM   2201 C  CD  . LYS B 1 122 ? 10.545 22.938  2.750   1.00  18.56 ? 122  LYS F CD  1 
ATOM   2202 C  CE  . LYS B 1 122 ? 10.996 23.544  4.009   1.00  21.25 ? 122  LYS F CE  1 
ATOM   2203 N  NZ  . LYS B 1 122 ? 10.006 24.679  4.309   1.00  22.85 ? 122  LYS F NZ  1 
ATOM   2204 N  N   . ALA B 1 123 ? 14.598 20.653  0.135   1.00  10.65 ? 123  ALA F N   1 
ATOM   2205 C  CA  . ALA B 1 123 ? 16.042 20.697  -0.064  1.00  9.59  ? 123  ALA F CA  1 
ATOM   2206 C  C   . ALA B 1 123 ? 16.780 21.165  1.155   1.00  9.77  ? 123  ALA F C   1 
ATOM   2207 O  O   . ALA B 1 123 ? 16.370 22.076  1.873   1.00  11.67 ? 123  ALA F O   1 
ATOM   2208 C  CB  . ALA B 1 123 ? 16.397 21.527  -1.275  1.00  11.38 ? 123  ALA F CB  1 
ATOM   2209 N  N   . ASP B 1 124 ? 17.886 20.509  1.396   1.00  8.65  ? 124  ASP F N   1 
ATOM   2210 C  CA  . ASP B 1 124 ? 18.861 21.037  2.343   1.00  8.68  ? 124  ASP F CA  1 
ATOM   2211 C  C   . ASP B 1 124 ? 19.591 22.153  1.571   1.00  9.42  ? 124  ASP F C   1 
ATOM   2212 O  O   . ASP B 1 124 ? 20.147 21.913  0.448   1.00  10.35 ? 124  ASP F O   1 
ATOM   2213 C  CB  . ASP B 1 124 ? 19.790 19.856  2.681   1.00  9.44  ? 124  ASP F CB  1 
ATOM   2214 C  CG  . ASP B 1 124 ? 20.900 20.198  3.653   1.00  9.48  ? 124  ASP F CG  1 
ATOM   2215 O  OD1 . ASP B 1 124 ? 21.242 21.361  3.805   1.00  9.70  ? 124  ASP F OD1 1 
ATOM   2216 O  OD2 . ASP B 1 124 ? 21.353 19.245  4.335   1.00  9.75  ? 124  ASP F OD2 1 
ATOM   2217 N  N   . ASP B 1 125 ? 19.682 23.304  2.198   1.00  8.91  ? 125  ASP F N   1 
ATOM   2218 C  CA  . ASP B 1 125 ? 20.364 24.459  1.549   1.00  9.56  ? 125  ASP F CA  1 
ATOM   2219 C  C   . ASP B 1 125 ? 21.870 24.452  1.737   1.00  9.50  ? 125  ASP F C   1 
ATOM   2220 O  O   . ASP B 1 125 ? 22.560 25.371  1.280   1.00  11.20 ? 125  ASP F O   1 
ATOM   2221 C  CB  . ASP B 1 125 ? 19.723 25.787  2.026   1.00  10.33 ? 125  ASP F CB  1 
ATOM   2222 C  CG  . ASP B 1 125 ? 19.896 26.065  3.525   1.00  10.13 ? 125  ASP F CG  1 
ATOM   2223 O  OD1 . ASP B 1 125 ? 20.893 25.594  4.084   1.00  9.28  ? 125  ASP F OD1 1 
ATOM   2224 O  OD2 . ASP B 1 125 ? 19.099 26.871  4.059   1.00  11.49 ? 125  ASP F OD2 1 
ATOM   2225 N  N   . LEU B 1 126 ? 22.395 23.391  2.380   1.00  10.20 ? 126  LEU F N   1 
ATOM   2226 C  CA  . LEU B 1 126 ? 23.819 23.159  2.417   1.00  9.98  ? 126  LEU F CA  1 
ATOM   2227 C  C   . LEU B 1 126 ? 24.585 24.225  3.191   1.00  11.15 ? 126  LEU F C   1 
ATOM   2228 O  O   . LEU B 1 126 ? 25.779 24.376  3.017   1.00  10.90 ? 126  LEU F O   1 
ATOM   2229 C  CB  . LEU B 1 126 ? 24.465 22.885  1.053   1.00  11.63 ? 126  LEU F CB  1 
ATOM   2230 C  CG  . LEU B 1 126 ? 23.626 21.902  0.215   1.00  11.27 ? 126  LEU F CG  1 
ATOM   2231 C  CD1 . LEU B 1 126 ? 24.333 21.718  -1.111  1.00  14.24 ? 126  LEU F CD1 1 
ATOM   2232 C  CD2 . LEU B 1 126 ? 23.432 20.582  0.916   1.00  10.70 ? 126  LEU F CD2 1 
ATOM   2233 N  N   . GLY B 1 127 ? 23.894 24.917  4.077   1.00  10.39 ? 127  GLY F N   1 
ATOM   2234 C  CA  . GLY B 1 127 ? 24.553 26.026  4.775   1.00  9.71  ? 127  GLY F CA  1 
ATOM   2235 C  C   . GLY B 1 127 ? 24.523 27.366  4.042   1.00  10.77 ? 127  GLY F C   1 
ATOM   2236 O  O   . GLY B 1 127 ? 25.087 28.317  4.540   1.00  13.31 ? 127  GLY F O   1 
ATOM   2237 N  N   . LYS B 1 128 ? 23.824 27.427  2.911   1.00  10.78 ? 128  LYS F N   1 
ATOM   2238 C  CA  . LYS B 1 128 ? 23.876 28.570  1.982   1.00  12.01 ? 128  LYS F CA  1 
ATOM   2239 C  C   . LYS B 1 128 ? 22.446 29.099  1.741   1.00  11.98 ? 128  LYS F C   1 
ATOM   2240 O  O   . LYS B 1 128 ? 22.045 29.433  0.612   1.00  13.85 ? 128  LYS F O   1 
ATOM   2241 C  CB  . LYS B 1 128 ? 24.514 28.199  0.637   1.00  13.15 ? 128  LYS F CB  1 
ATOM   2242 C  CG  . LYS B 1 128 ? 25.850 27.463  0.700   1.00  14.72 ? 128  LYS F CG  1 
ATOM   2243 C  CD  . LYS B 1 128 ? 27.057 28.295  1.070   0.70  18.82 ? 128  LYS F CD  1 
ATOM   2244 C  CE  . LYS B 1 128 ? 28.359 27.460  1.253   0.70  19.62 ? 128  LYS F CE  1 
ATOM   2245 N  NZ  . LYS B 1 128 ? 28.879 26.603  0.116   0.70  22.92 ? 128  LYS F NZ  1 
ATOM   2246 N  N   . GLY B 1 129 ? 21.666 29.156  2.818   1.00  10.74 ? 129  GLY F N   1 
ATOM   2247 C  CA  . GLY B 1 129 ? 20.308 29.646  2.748   1.00  10.92 ? 129  GLY F CA  1 
ATOM   2248 C  C   . GLY B 1 129 ? 20.080 31.084  3.253   1.00  10.32 ? 129  GLY F C   1 
ATOM   2249 O  O   . GLY B 1 129 ? 19.023 31.639  3.041   1.00  14.21 ? 129  GLY F O   1 
ATOM   2250 N  N   . GLY B 1 130 ? 21.029 31.623  3.998   1.00  11.26 ? 130  GLY F N   1 
ATOM   2251 C  CA  . GLY B 1 130 ? 20.955 33.026  4.422   1.00  12.30 ? 130  GLY F CA  1 
ATOM   2252 C  C   . GLY B 1 130 ? 20.281 33.308  5.739   1.00  11.87 ? 130  GLY F C   1 
ATOM   2253 O  O   . GLY B 1 130 ? 19.919 34.467  5.984   1.00  13.03 ? 130  GLY F O   1 
ATOM   2254 N  N   . ASN B 1 131 ? 20.174 32.319  6.625   1.00  11.46 ? 131  ASN F N   1 
ATOM   2255 C  CA  . ASN B 1 131 ? 19.642 32.527  7.964   1.00  11.83 ? 131  ASN F CA  1 
ATOM   2256 C  C   . ASN B 1 131 ? 20.400 31.621  8.904   1.00  12.65 ? 131  ASN F C   1 
ATOM   2257 O  O   . ASN B 1 131 ? 21.287 30.837  8.525   1.00  12.87 ? 131  ASN F O   1 
ATOM   2258 C  CB  . ASN B 1 131 ? 18.119 32.340  8.069   1.00  11.89 ? 131  ASN F CB  1 
ATOM   2259 C  CG  . ASN B 1 131 ? 17.670 30.914  7.815   1.00  12.59 ? 131  ASN F CG  1 
ATOM   2260 O  OD1 . ASN B 1 131 ? 18.479 30.000  7.653   1.00  14.49 ? 131  ASN F OD1 1 
ATOM   2261 N  ND2 . ASN B 1 131 ? 16.361 30.717  7.795   1.00  19.00 ? 131  ASN F ND2 1 
ATOM   2262 N  N   . GLU B 1 132 ? 20.136 31.797  10.190  1.00  13.41 ? 132  GLU F N   1 
ATOM   2263 C  CA  . GLU B 1 132 ? 20.911 31.073  11.181  1.00  13.63 ? 132  GLU F CA  1 
ATOM   2264 C  C   . GLU B 1 132 ? 20.616 29.561  11.114  1.00  11.68 ? 132  GLU F C   1 
ATOM   2265 O  O   . GLU B 1 132 ? 21.498 28.694  11.268  1.00  12.71 ? 132  GLU F O   1 
ATOM   2266 C  CB  . GLU B 1 132 ? 20.618 31.591  12.575  1.00  14.48 ? 132  GLU F CB  1 
ATOM   2267 C  CG  . GLU B 1 132 ? 21.229 30.692  13.731  1.00  16.08 ? 132  GLU F CG  1 
ATOM   2268 C  CD  . GLU B 1 132 ? 20.905 31.085  15.142  0.70  15.99 ? 132  GLU F CD  1 
ATOM   2269 O  OE1 . GLU B 1 132 ? 20.158 32.049  15.407  0.70  21.36 ? 132  GLU F OE1 1 
ATOM   2270 O  OE2 . GLU B 1 132 ? 21.414 30.350  16.017  0.70  20.08 ? 132  GLU F OE2 1 
ATOM   2271 N  N   . GLU B 1 133 ? 19.368 29.217  10.857  1.00  11.23 ? 133  GLU F N   1 
ATOM   2272 C  CA  . GLU B 1 133 ? 19.041 27.809  10.730  1.00  11.54 ? 133  GLU F CA  1 
ATOM   2273 C  C   . GLU B 1 133 ? 19.824 27.100  9.627   1.00  10.23 ? 133  GLU F C   1 
ATOM   2274 O  O   . GLU B 1 133 ? 20.114 25.892  9.709   1.00  12.33 ? 133  GLU F O   1 
ATOM   2275 C  CB  . GLU B 1 133 ? 17.543 27.670  10.622  1.00  12.32 ? 133  GLU F CB  1 
ATOM   2276 C  CG  . GLU B 1 133 ? 17.068 26.273  10.643  1.00  13.75 ? 133  GLU F CG  1 
ATOM   2277 C  CD  . GLU B 1 133 ? 15.536 26.124  10.621  1.00  15.67 ? 133  GLU F CD  1 
ATOM   2278 O  OE1 . GLU B 1 133 ? 14.788 27.120  10.682  1.00  18.63 ? 133  GLU F OE1 1 
ATOM   2279 O  OE2 . GLU B 1 133 ? 15.085 24.940  10.453  1.00  22.26 ? 133  GLU F OE2 1 
ATOM   2280 N  N   . SER B 1 134 ? 20.150 27.822  8.570   1.00  10.46 ? 134  SER F N   1 
ATOM   2281 C  CA  . SER B 1 134 ? 20.871 27.212  7.458   1.00  10.28 ? 134  SER F CA  1 
ATOM   2282 C  C   . SER B 1 134 ? 22.183 26.562  7.964   1.00  10.44 ? 134  SER F C   1 
ATOM   2283 O  O   . SER B 1 134 ? 22.546 25.498  7.474   1.00  11.64 ? 134  SER F O   1 
ATOM   2284 C  CB  . SER B 1 134 ? 21.129 28.303  6.435   1.00  9.78  ? 134  SER F CB  1 
ATOM   2285 O  OG  . SER B 1 134 ? 21.882 27.705  5.373   1.00  11.21 ? 134  SER F OG  1 
ATOM   2286 N  N   . THR B 1 135 ? 22.868 27.207  8.936   1.00  12.68 ? 135  THR F N   1 
ATOM   2287 C  CA  . THR B 1 135 ? 24.102 26.757  9.489   1.00  13.01 ? 135  THR F CA  1 
ATOM   2288 C  C   . THR B 1 135 ? 23.978 25.644  10.540  1.00  11.16 ? 135  THR F C   1 
ATOM   2289 O  O   . THR B 1 135 ? 25.005 25.170  11.070  1.00  12.90 ? 135  THR F O   1 
ATOM   2290 C  CB  . THR B 1 135 ? 24.777 27.971  10.247  1.00  15.09 ? 135  THR F CB  1 
ATOM   2291 O  OG1 . THR B 1 135 ? 24.074 28.230  11.507  1.00  16.21 ? 135  THR F OG1 1 
ATOM   2292 C  CG2 . THR B 1 135 ? 24.828 29.178  9.389   1.00  16.36 ? 135  THR F CG2 1 
ATOM   2293 N  N   . LYS B 1 136 ? 22.738 25.260  10.846  1.00  12.52 ? 136  LYS F N   1 
ATOM   2294 C  CA  . LYS B 1 136 ? 22.466 24.228  11.822  1.00  12.13 ? 136  LYS F CA  1 
ATOM   2295 C  C   . LYS B 1 136 ? 21.786 23.007  11.208  1.00  11.13 ? 136  LYS F C   1 
ATOM   2296 O  O   . LYS B 1 136 ? 22.243 21.883  11.401  1.00  12.20 ? 136  LYS F O   1 
ATOM   2297 C  CB  . LYS B 1 136 ? 21.583 24.797  12.953  1.00  12.95 ? 136  LYS F CB  1 
ATOM   2298 C  CG  . LYS B 1 136 ? 22.300 25.853  13.730  1.00  15.37 ? 136  LYS F CG  1 
ATOM   2299 C  CD  . LYS B 1 136 ? 21.510 26.287  14.907  1.00  18.21 ? 136  LYS F CD  1 
ATOM   2300 C  CE  . LYS B 1 136 ? 22.420 27.154  15.776  1.00  18.76 ? 136  LYS F CE  1 
ATOM   2301 N  NZ  . LYS B 1 136 ? 21.862 27.398  17.072  1.00  20.06 ? 136  LYS F NZ  1 
ATOM   2302 N  N   . THR B 1 137 ? 20.672 23.211  10.514  1.00  11.18 ? 137  THR F N   1 
ATOM   2303 C  CA  . THR B 1 137 ? 19.918 22.091  9.957   1.00  9.76  ? 137  THR F CA  1 
ATOM   2304 C  C   . THR B 1 137 ? 19.882 22.087  8.423   1.00  9.54  ? 137  THR F C   1 
ATOM   2305 O  O   . THR B 1 137 ? 19.602 21.053  7.850   1.00  9.19  ? 137  THR F O   1 
ATOM   2306 C  CB  . THR B 1 137 ? 18.474 22.064  10.417  1.00  12.11 ? 137  THR F CB  1 
ATOM   2307 O  OG1 . THR B 1 137 ? 17.763 23.140  9.796   1.00  12.47 ? 137  THR F OG1 1 
ATOM   2308 C  CG2 . THR B 1 137 ? 18.375 22.122  11.923  1.00  12.54 ? 137  THR F CG2 1 
ATOM   2309 N  N   . GLY B 1 138 ? 20.059 23.235  7.745   1.00  8.46  ? 138  GLY F N   1 
ATOM   2310 C  CA  . GLY B 1 138 ? 19.897 23.344  6.311   1.00  9.14  ? 138  GLY F CA  1 
ATOM   2311 C  C   . GLY B 1 138 ? 18.500 23.543  5.829   1.00  9.45  ? 138  GLY F C   1 
ATOM   2312 O  O   . GLY B 1 138 ? 18.244 23.547  4.649   1.00  10.00 ? 138  GLY F O   1 
ATOM   2313 N  N   . ASN B 1 139 ? 17.532 23.719  6.710   1.00  9.92  ? 139  ASN F N   1 
ATOM   2314 C  CA  . ASN B 1 139 ? 16.190 24.101  6.348   1.00  10.03 ? 139  ASN F CA  1 
ATOM   2315 C  C   . ASN B 1 139 ? 15.468 23.135  5.412   1.00  10.34 ? 139  ASN F C   1 
ATOM   2316 O  O   . ASN B 1 139 ? 14.720 23.558  4.550   1.00  11.91 ? 139  ASN F O   1 
ATOM   2317 C  CB  . ASN B 1 139 ? 16.158 25.514  5.731   1.00  10.70 ? 139  ASN F CB  1 
ATOM   2318 C  CG  . ASN B 1 139 ? 16.552 26.608  6.705   1.00  12.53 ? 139  ASN F CG  1 
ATOM   2319 O  OD1 . ASN B 1 139 ? 15.864 26.850  7.661   1.00  16.56 ? 139  ASN F OD1 1 
ATOM   2320 N  ND2 . ASN B 1 139 ? 17.644 27.277  6.430   1.00  12.00 ? 139  ASN F ND2 1 
ATOM   2321 N  N   . ALA B 1 140 ? 15.601 21.844  5.692   1.00  9.83  ? 140  ALA F N   1 
ATOM   2322 C  CA  . ALA B 1 140 ? 15.077 20.808  4.760   1.00  9.71  ? 140  ALA F CA  1 
ATOM   2323 C  C   . ALA B 1 140 ? 13.673 20.344  5.114   1.00  11.05 ? 140  ALA F C   1 
ATOM   2324 O  O   . ALA B 1 140 ? 13.129 19.471  4.530   1.00  10.93 ? 140  ALA F O   1 
ATOM   2325 C  CB  . ALA B 1 140 ? 15.988 19.631  4.640   1.00  11.68 ? 140  ALA F CB  1 
ATOM   2326 N  N   . GLY B 1 141 ? 13.057 20.959  6.112   1.00  10.65 ? 141  GLY F N   1 
ATOM   2327 C  CA  . GLY B 1 141 ? 11.676 20.685  6.366   1.00  10.88 ? 141  GLY F CA  1 
ATOM   2328 C  C   . GLY B 1 141 ? 11.469 19.357  7.055   1.00  9.59  ? 141  GLY F C   1 
ATOM   2329 O  O   . GLY B 1 141 ? 12.352 18.837  7.718   1.00  12.17 ? 141  GLY F O   1 
ATOM   2330 N  N   . SER B 1 142 ? 10.269 18.872  6.957   1.00  10.88 ? 142  SER F N   1 
ATOM   2331 C  CA  . SER B 1 142 ? 9.907  17.690  7.715   1.00  12.43 ? 142  SER F CA  1 
ATOM   2332 C  C   . SER B 1 142 ? 10.716 16.423  7.363   1.00  9.93  ? 142  SER F C   1 
ATOM   2333 O  O   . SER B 1 142 ? 11.258 16.296  6.267   1.00  11.73 ? 142  SER F O   1 
ATOM   2334 C  CB  . SER B 1 142 ? 8.409  17.448  7.601   1.00  13.53 ? 142  SER F CB  1 
ATOM   2335 O  OG  . SER B 1 142 ? 8.048  16.946  6.364   1.00  19.87 ? 142  SER F OG  1 
ATOM   2336 N  N   . ARG B 1 143 ? 10.780 15.494  8.315   1.00  10.28 ? 143  ARG F N   1 
ATOM   2337 C  CA  . ARG B 1 143 ? 11.372 14.184  8.101   1.00  9.70  ? 143  ARG F CA  1 
ATOM   2338 C  C   . ARG B 1 143 ? 10.342 13.294  7.471   1.00  10.07 ? 143  ARG F C   1 
ATOM   2339 O  O   . ARG B 1 143 ? 9.404  12.856  8.113   1.00  13.38 ? 143  ARG F O   1 
ATOM   2340 C  CB  . ARG B 1 143 ? 11.842 13.649  9.470   1.00  9.61  ? 143  ARG F CB  1 
ATOM   2341 C  CG  . ARG B 1 143 ? 12.814 14.588  10.119  1.00  9.44  ? 143  ARG F CG  1 
ATOM   2342 C  CD  . ARG B 1 143 ? 13.236 14.081  11.461  1.00  10.43 ? 143  ARG F CD  1 
ATOM   2343 N  NE  . ARG B 1 143 ? 14.089 15.080  12.068  1.00  12.75 ? 143  ARG F NE  1 
ATOM   2344 C  CZ  . ARG B 1 143 ? 14.784 14.991  13.205  1.00  11.62 ? 143  ARG F CZ  1 
ATOM   2345 N  NH1 . ARG B 1 143 ? 14.728 13.897  13.951  1.00  13.46 ? 143  ARG F NH1 1 
ATOM   2346 N  NH2 . ARG B 1 143 ? 15.527 16.020  13.609  1.00  12.20 ? 143  ARG F NH2 1 
ATOM   2347 N  N   . LEU B 1 144 ? 10.495 13.005  6.190   1.00  9.77  ? 144  LEU F N   1 
ATOM   2348 C  CA  . LEU B 1 144 ? 9.527  12.208  5.465   1.00  10.15 ? 144  LEU F CA  1 
ATOM   2349 C  C   . LEU B 1 144 ? 9.622  10.714  5.729   1.00  9.45  ? 144  LEU F C   1 
ATOM   2350 O  O   . LEU B 1 144 ? 8.602  10.031  5.742   1.00  11.65 ? 144  LEU F O   1 
ATOM   2351 C  CB  . LEU B 1 144 ? 9.600  12.396  3.939   1.00  10.62 ? 144  LEU F CB  1 
ATOM   2352 C  CG  . LEU B 1 144 ? 9.318  13.769  3.432   1.00  12.58 ? 144  LEU F CG  1 
ATOM   2353 C  CD1 . LEU B 1 144 ? 9.312  13.699  1.953   1.00  15.55 ? 144  LEU F CD1 1 
ATOM   2354 C  CD2 . LEU B 1 144 ? 8.006  14.252  3.925   1.00  18.13 ? 144  LEU F CD2 1 
ATOM   2355 N  N   . ALA B 1 145 ? 10.841 10.226  5.850   1.00  8.97  ? 145  ALA F N   1 
ATOM   2356 C  CA  . ALA B 1 145 ? 11.043 8.805   6.055   1.00  8.69  ? 145  ALA F CA  1 
ATOM   2357 C  C   . ALA B 1 145 ? 12.376 8.626   6.722   1.00  8.42  ? 145  ALA F C   1 
ATOM   2358 O  O   . ALA B 1 145 ? 13.287 9.428   6.508   1.00  9.31  ? 145  ALA F O   1 
ATOM   2359 C  CB  . ALA B 1 145 ? 10.965 8.042   4.731   1.00  9.56  ? 145  ALA F CB  1 
ATOM   2360 N  N   . CYS B 1 146 ? 12.537 7.530   7.444   1.00  8.12  ? 146  CYS F N   1 
ATOM   2361 C  CA  . CYS B 1 146 ? 13.783 7.261   8.119   1.00  7.97  ? 146  CYS F CA  1 
ATOM   2362 C  C   . CYS B 1 146 ? 13.876 5.766   8.490   1.00  7.04  ? 146  CYS F C   1 
ATOM   2363 O  O   . CYS B 1 146 ? 12.883 5.052   8.381   1.00  8.96  ? 146  CYS F O   1 
ATOM   2364 C  CB  . CYS B 1 146 ? 13.871 8.070   9.373   1.00  8.70  ? 146  CYS F CB  1 
ATOM   2365 S  SG  . CYS B 1 146 ? 12.605 7.716   10.655  1.00  13.51 ? 146  CYS F SG  1 
ATOM   2366 N  N   . GLY B 1 147 ? 15.058 5.367   8.887   1.00  7.48  ? 147  GLY F N   1 
ATOM   2367 C  CA  . GLY B 1 147 ? 15.301 4.039   9.445   1.00  6.99  ? 147  GLY F CA  1 
ATOM   2368 C  C   . GLY B 1 147 ? 16.646 3.987   10.086  1.00  6.79  ? 147  GLY F C   1 
ATOM   2369 O  O   . GLY B 1 147 ? 17.465 4.869   9.936   1.00  7.54  ? 147  GLY F O   1 
ATOM   2370 N  N   . VAL B 1 148 ? 16.852 2.938   10.881  1.00  7.86  ? 148  VAL F N   1 
ATOM   2371 C  CA  . VAL B 1 148 ? 18.091 2.754   11.584  1.00  7.35  ? 148  VAL F CA  1 
ATOM   2372 C  C   . VAL B 1 148 ? 19.078 1.983   10.664  1.00  7.53  ? 148  VAL F C   1 
ATOM   2373 O  O   . VAL B 1 148 ? 18.699 1.048   9.950   1.00  8.52  ? 148  VAL F O   1 
ATOM   2374 C  CB  . VAL B 1 148 ? 17.866 1.959   12.918  1.00  8.85  ? 148  VAL F CB  1 
ATOM   2375 C  CG1 . VAL B 1 148 ? 19.124 1.832   13.678  1.00  8.71  ? 148  VAL F CG1 1 
ATOM   2376 C  CG2 . VAL B 1 148 ? 16.838 2.701   13.829  1.00  9.69  ? 148  VAL F CG2 1 
ATOM   2377 N  N   . ILE B 1 149 ? 20.326 2.435   10.615  1.00  6.84  ? 149  ILE F N   1 
ATOM   2378 C  CA  . ILE B 1 149 ? 21.365 1.846   9.756   1.00  7.52  ? 149  ILE F CA  1 
ATOM   2379 C  C   . ILE B 1 149 ? 21.886 0.618   10.458  1.00  7.59  ? 149  ILE F C   1 
ATOM   2380 O  O   . ILE B 1 149 ? 22.411 0.692   11.603  1.00  8.89  ? 149  ILE F O   1 
ATOM   2381 C  CB  . ILE B 1 149 ? 22.456 2.904   9.503   1.00  7.63  ? 149  ILE F CB  1 
ATOM   2382 C  CG1 . ILE B 1 149 ? 21.871 4.155   8.802   1.00  8.29  ? 149  ILE F CG1 1 
ATOM   2383 C  CG2 . ILE B 1 149 ? 23.610 2.294   8.740   1.00  8.33  ? 149  ILE F CG2 1 
ATOM   2384 C  CD1 . ILE B 1 149 ? 22.884 5.302   8.762   1.00  9.63  ? 149  ILE F CD1 1 
ATOM   2385 N  N   . GLY B 1 150 ? 21.828 -0.510  9.782   1.00  7.18  ? 150  GLY F N   1 
ATOM   2386 C  CA  . GLY B 1 150 ? 22.203 -1.778  10.356  1.00  8.00  ? 150  GLY F CA  1 
ATOM   2387 C  C   . GLY B 1 150 ? 23.387 -2.424  9.680   1.00  7.66  ? 150  GLY F C   1 
ATOM   2388 O  O   . GLY B 1 150 ? 23.664 -2.127  8.487   1.00  9.46  ? 150  GLY F O   1 
ATOM   2389 N  N   . ILE B 1 151 ? 24.082 -3.281  10.362  1.00  7.93  ? 151  ILE F N   1 
ATOM   2390 C  CA  . ILE B 1 151 ? 25.139 -4.093  9.802   1.00  8.04  ? 151  ILE F CA  1 
ATOM   2391 C  C   . ILE B 1 151 ? 24.568 -5.062  8.795   1.00  8.73  ? 151  ILE F C   1 
ATOM   2392 O  O   . ILE B 1 151 ? 23.612 -5.785  9.074   1.00  9.45  ? 151  ILE F O   1 
ATOM   2393 C  CB  . ILE B 1 151 ? 25.875 -4.831  10.885  1.00  8.81  ? 151  ILE F CB  1 
ATOM   2394 C  CG1 . ILE B 1 151 ? 26.546 -3.857  11.798  1.00  11.72 ? 151  ILE F CG1 1 
ATOM   2395 C  CG2 . ILE B 1 151 ? 26.882 -5.837  10.322  1.00  13.08 ? 151  ILE F CG2 1 
ATOM   2396 C  CD1 . ILE B 1 151 ? 26.914 -4.440  13.163  1.00  12.73 ? 151  ILE F CD1 1 
ATOM   2397 N  N   . ALA B 1 152 ? 25.229 -5.144  7.631   1.00  9.11  ? 152  ALA F N   1 
ATOM   2398 C  CA  . ALA B 1 152 ? 24.835 -6.058  6.620   1.00  10.52 ? 152  ALA F CA  1 
ATOM   2399 C  C   . ALA B 1 152 ? 25.914 -7.113  6.380   1.00  9.61  ? 152  ALA F C   1 
ATOM   2400 O  O   . ALA B 1 152 ? 27.076 -6.998  6.792   1.00  11.22 ? 152  ALA F O   1 
ATOM   2401 C  CB  . ALA B 1 152 ? 24.576 -5.211  5.290   1.00  10.14 ? 152  ALA F CB  1 
ATOM   2402 N  N   . GLN B 1 153 ? 25.488 -8.164  5.692   1.00  11.21 ? 153  GLN F N   1 
ATOM   2403 C  CA  . GLN B 1 153 ? 26.356 -9.283  5.410   1.00  13.14 ? 153  GLN F CA  1 
ATOM   2404 C  C   . GLN B 1 153 ? 27.438 -8.932  4.448   1.00  15.48 ? 153  GLN F C   1 
ATOM   2405 O  O   . GLN B 1 153 ? 27.130 -8.296  3.449   1.00  17.52 ? 153  GLN F O   1 
ATOM   2406 C  CB  . GLN B 1 153 ? 25.570 -10.425 4.835   1.00  12.65 ? 153  GLN F CB  1 
ATOM   2407 C  CG  . GLN B 1 153 ? 26.361 -11.700 4.601   1.00  14.13 ? 153  GLN F CG  1 
ATOM   2408 C  CD  . GLN B 1 153 ? 25.459 -12.820 4.174   1.00  15.68 ? 153  GLN F CD  1 
ATOM   2409 O  OE1 . GLN B 1 153 ? 24.400 -13.002 4.763   1.00  17.30 ? 153  GLN F OE1 1 
ATOM   2410 N  NE2 . GLN B 1 153 ? 25.857 -13.581 3.136   1.00  17.95 ? 153  GLN F NE2 1 
ATOM   2411 O  OXT . GLN B 1 153 ? 28.563 -9.364  4.708   1.00  18.96 ? 153  GLN F OXT 1 
HETATM 2412 ZN ZN  . ZN  C 2 .   ? 15.617 -15.970 16.421  1.00  9.57  ? 1155 ZN  A ZN  1 
HETATM 2413 ZN ZN  . ZN  D 2 .   ? 21.293 -18.984 19.569  1.00  9.11  ? 1156 ZN  A ZN  1 
HETATM 2414 ZN ZN  . ZN  E 2 .   ? 7.824  -14.869 11.431  0.15  10.44 ? 1157 ZN  A ZN  1 
HETATM 2415 C  C   . ACT F 3 .   ? 18.112 -32.895 11.044  1.00  24.33 ? 1158 ACT A C   1 
HETATM 2416 O  O   . ACT F 3 .   ? 18.345 -33.976 11.607  1.00  27.39 ? 1158 ACT A O   1 
HETATM 2417 O  OXT . ACT F 3 .   ? 19.080 -32.097 10.863  1.00  28.53 ? 1158 ACT A OXT 1 
HETATM 2418 C  CH3 . ACT F 3 .   ? 16.796 -32.629 10.410  1.00  25.31 ? 1158 ACT A CH3 1 
HETATM 2419 C  C   . ACT G 3 .   ? 16.870 -34.924 14.898  1.00  27.85 ? 1159 ACT A C   1 
HETATM 2420 O  O   . ACT G 3 .   ? 17.421 -35.715 15.743  1.00  29.17 ? 1159 ACT A O   1 
HETATM 2421 O  OXT . ACT G 3 .   ? 17.516 -33.962 14.467  1.00  27.51 ? 1159 ACT A OXT 1 
HETATM 2422 C  CH3 . ACT G 3 .   ? 15.436 -35.050 14.523  1.00  28.41 ? 1159 ACT A CH3 1 
HETATM 2423 S  S   . SO4 H 4 .   ? 34.555 -18.288 24.677  0.50  14.40 ? 1160 SO4 A S   1 
HETATM 2424 O  O1  . SO4 H 4 .   ? 35.107 -19.299 23.760  0.50  15.37 ? 1160 SO4 A O1  1 
HETATM 2425 O  O2  . SO4 H 4 .   ? 33.082 -18.297 24.477  0.50  14.23 ? 1160 SO4 A O2  1 
HETATM 2426 O  O3  . SO4 H 4 .   ? 34.717 -18.658 26.104  0.50  12.67 ? 1160 SO4 A O3  1 
HETATM 2427 O  O4  . SO4 H 4 .   ? 35.199 -16.985 24.310  0.50  11.68 ? 1160 SO4 A O4  1 
HETATM 2428 S  S   . SO4 I 4 .   ? 15.616 -18.366 14.313  1.00  10.89 ? 1161 SO4 A S   1 
HETATM 2429 O  O1  . SO4 I 4 .   ? 16.869 -18.814 13.773  1.00  15.99 ? 1161 SO4 A O1  1 
HETATM 2430 O  O2  . SO4 I 4 .   ? 14.967 -17.392 13.477  1.00  11.36 ? 1161 SO4 A O2  1 
HETATM 2431 O  O3  . SO4 I 4 .   ? 14.735 -19.513 14.501  1.00  14.07 ? 1161 SO4 A O3  1 
HETATM 2432 O  O4  . SO4 I 4 .   ? 15.964 -17.840 15.618  1.00  10.57 ? 1161 SO4 A O4  1 
HETATM 2433 S  S   . SO4 J 4 .   ? 11.229 -23.517 13.489  0.50  21.92 ? 1162 SO4 A S   1 
HETATM 2434 O  O1  . SO4 J 4 .   ? 11.863 -24.784 13.170  0.50  19.45 ? 1162 SO4 A O1  1 
HETATM 2435 O  O2  . SO4 J 4 .   ? 9.796  -23.770 13.478  0.50  22.95 ? 1162 SO4 A O2  1 
HETATM 2436 O  O3  . SO4 J 4 .   ? 11.659 -23.008 14.765  0.50  12.18 ? 1162 SO4 A O3  1 
HETATM 2437 O  O4  . SO4 J 4 .   ? 11.546 -22.475 12.487  0.50  21.33 ? 1162 SO4 A O4  1 
HETATM 2438 S  S   . SO4 K 4 .   ? 10.157 -16.024 9.424   0.40  19.93 ? 1163 SO4 A S   1 
HETATM 2439 O  O1  . SO4 K 4 .   ? 11.104 -14.980 8.979   0.40  16.54 ? 1163 SO4 A O1  1 
HETATM 2440 O  O2  . SO4 K 4 .   ? 9.468  -16.622 8.267   0.40  21.61 ? 1163 SO4 A O2  1 
HETATM 2441 O  O3  . SO4 K 4 .   ? 10.802 -17.060 10.232  0.40  20.94 ? 1163 SO4 A O3  1 
HETATM 2442 O  O4  . SO4 K 4 .   ? 9.179  -15.371 10.262  0.40  13.67 ? 1163 SO4 A O4  1 
HETATM 2443 S  S   . SO4 L 4 .   ? 16.532 18.368  10.634  1.00  10.99 ? 1154 SO4 F S   1 
HETATM 2444 O  O1  . SO4 L 4 .   ? 17.507 17.783  9.676   1.00  9.72  ? 1154 SO4 F O1  1 
HETATM 2445 O  O2  . SO4 L 4 .   ? 15.888 19.528  10.003  1.00  15.26 ? 1154 SO4 F O2  1 
HETATM 2446 O  O3  . SO4 L 4 .   ? 15.530 17.407  10.987  1.00  11.62 ? 1154 SO4 F O3  1 
HETATM 2447 O  O4  . SO4 L 4 .   ? 17.320 18.744  11.736  1.00  16.13 ? 1154 SO4 F O4  1 
HETATM 2448 S  S   . SO4 M 4 .   ? 9.459  15.704  12.178  0.55  26.05 ? 1155 SO4 F S   1 
HETATM 2449 O  O1  . SO4 M 4 .   ? 9.342  15.904  10.764  0.55  17.96 ? 1155 SO4 F O1  1 
HETATM 2450 O  O2  . SO4 M 4 .   ? 10.674 16.428  12.602  0.55  26.89 ? 1155 SO4 F O2  1 
HETATM 2451 O  O3  . SO4 M 4 .   ? 8.249  16.258  12.793  0.55  25.87 ? 1155 SO4 F O3  1 
HETATM 2452 O  O4  . SO4 M 4 .   ? 9.746  14.315  12.549  0.55  20.47 ? 1155 SO4 F O4  1 
HETATM 2453 ZN ZN  . ZN  N 2 .   ? 17.691 16.000  8.851   1.00  9.72  ? 1157 ZN  F ZN  1 
HETATM 2454 ZN ZN  . ZN  O 2 .   ? 24.154 19.073  9.269   1.00  8.64  ? 1158 ZN  F ZN  1 
HETATM 2455 C  C   . ACT P 3 .   ? 23.861 18.058  -2.451  0.50  16.43 ? 1159 ACT F C   1 
HETATM 2456 O  O   . ACT P 3 .   ? 24.066 16.858  -2.531  0.50  14.08 ? 1159 ACT F O   1 
HETATM 2457 O  OXT . ACT P 3 .   ? 22.946 18.625  -3.136  0.50  19.04 ? 1159 ACT F OXT 1 
HETATM 2458 C  CH3 . ACT P 3 .   ? 24.817 18.794  -1.633  0.50  17.16 ? 1159 ACT F CH3 1 
HETATM 2459 ZN ZN  . ZN  Q 2 .   ? 8.735  14.813  8.813   0.15  12.12 ? 1160 ZN  F ZN  1 
HETATM 2460 O  O   . HOH R 5 .   ? 30.492 3.849   29.535  1.00  43.33 ? 2001 HOH A O   1 
HETATM 2461 O  O   . HOH R 5 .   ? 29.163 0.685   26.724  1.00  33.85 ? 2002 HOH A O   1 
HETATM 2462 O  O   . HOH R 5 .   ? 24.924 7.904   26.331  1.00  37.84 ? 2003 HOH A O   1 
HETATM 2463 O  O   . HOH R 5 .   ? 3.346  -12.257 11.097  1.00  35.87 ? 2004 HOH A O   1 
HETATM 2464 O  O   . HOH R 5 .   ? 11.330 -1.391  13.696  1.00  16.19 ? 2005 HOH A O   1 
HETATM 2465 O  O   . HOH R 5 .   ? 6.702  3.170   15.683  1.00  32.84 ? 2006 HOH A O   1 
HETATM 2466 O  O   . HOH R 5 .   ? 10.310 -5.223  11.098  0.50  11.41 ? 2007 HOH A O   1 
HETATM 2467 O  O   . HOH R 5 .   ? 6.163  -0.986  16.932  1.00  32.62 ? 2008 HOH A O   1 
HETATM 2468 O  O   . HOH R 5 .   ? 25.090 -2.662  36.216  1.00  39.77 ? 2009 HOH A O   1 
HETATM 2469 O  O   . HOH R 5 .   ? 26.750 -4.366  37.701  1.00  46.13 ? 2010 HOH A O   1 
HETATM 2470 O  O   . HOH R 5 .   ? 39.291 -2.665  26.291  1.00  30.63 ? 2011 HOH A O   1 
HETATM 2471 O  O   . HOH R 5 .   ? 37.468 -23.334 13.603  1.00  43.85 ? 2012 HOH A O   1 
HETATM 2472 O  O   . HOH R 5 .   ? 5.164  -3.134  10.426  1.00  39.94 ? 2013 HOH A O   1 
HETATM 2473 O  O   . HOH R 5 .   ? 21.825 -0.158  33.765  1.00  34.44 ? 2014 HOH A O   1 
HETATM 2474 O  O   . HOH R 5 .   ? 7.598  -8.853  6.355   1.00  40.97 ? 2015 HOH A O   1 
HETATM 2475 O  O   . HOH R 5 .   ? 5.882  -12.926 8.151   1.00  45.67 ? 2016 HOH A O   1 
HETATM 2476 O  O   . HOH R 5 .   ? 5.383  -10.668 11.341  0.50  12.60 ? 2017 HOH A O   1 
HETATM 2477 O  O   . HOH R 5 .   ? 13.153 1.878   37.964  1.00  38.35 ? 2018 HOH A O   1 
HETATM 2478 O  O   . HOH R 5 .   ? 1.392  -4.855  11.062  1.00  37.79 ? 2019 HOH A O   1 
HETATM 2479 O  O   . HOH R 5 .   ? -1.299 -5.689  19.377  1.00  26.65 ? 2020 HOH A O   1 
HETATM 2480 O  O   . HOH R 5 .   ? 36.756 -11.962 11.916  1.00  32.28 ? 2021 HOH A O   1 
HETATM 2481 O  O   . HOH R 5 .   ? 3.801  -5.261  14.172  1.00  20.22 ? 2022 HOH A O   1 
HETATM 2482 O  O   . HOH R 5 .   ? 1.071  -13.276 15.647  1.00  21.35 ? 2023 HOH A O   1 
HETATM 2483 O  O   . HOH R 5 .   ? 4.877  -0.704  21.469  1.00  35.04 ? 2024 HOH A O   1 
HETATM 2484 O  O   . HOH R 5 .   ? 6.342  -0.400  19.054  1.00  29.41 ? 2025 HOH A O   1 
HETATM 2485 O  O   . HOH R 5 .   ? 16.698 3.330   25.536  1.00  20.07 ? 2026 HOH A O   1 
HETATM 2486 O  O   . HOH R 5 .   ? 13.192 4.952   25.889  1.00  25.28 ? 2027 HOH A O   1 
HETATM 2487 O  O   . HOH R 5 .   ? 12.610 3.953   24.393  1.00  25.73 ? 2028 HOH A O   1 
HETATM 2488 O  O   . HOH R 5 .   ? 30.877 -10.632 14.218  1.00  26.33 ? 2029 HOH A O   1 
HETATM 2489 O  O   . HOH R 5 .   ? 18.271 2.783   27.170  1.00  25.54 ? 2030 HOH A O   1 
HETATM 2490 O  O   . HOH R 5 .   ? 8.937  -4.911  6.916   1.00  34.98 ? 2031 HOH A O   1 
HETATM 2491 O  O   . HOH R 5 .   ? 18.326 4.722   32.259  1.00  31.88 ? 2032 HOH A O   1 
HETATM 2492 O  O   . HOH R 5 .   ? 29.299 1.668   29.176  1.00  31.10 ? 2033 HOH A O   1 
HETATM 2493 O  O   . HOH R 5 .   ? 23.736 5.849   36.712  1.00  48.81 ? 2034 HOH A O   1 
HETATM 2494 O  O   . HOH R 5 .   ? 27.710 -2.124  35.731  1.00  23.47 ? 2035 HOH A O   1 
HETATM 2495 O  O   . HOH R 5 .   ? 32.450 -3.757  34.679  1.00  39.85 ? 2036 HOH A O   1 
HETATM 2496 O  O   . HOH R 5 .   ? 37.171 -20.457 19.840  1.00  30.24 ? 2037 HOH A O   1 
HETATM 2497 O  O   . HOH R 5 .   ? 36.047 -16.953 17.684  1.00  25.70 ? 2038 HOH A O   1 
HETATM 2498 O  O   . HOH R 5 .   ? 34.264 -23.433 15.836  1.00  34.22 ? 2039 HOH A O   1 
HETATM 2499 O  O   . HOH R 5 .   ? 33.388 2.427   31.550  1.00  35.95 ? 2040 HOH A O   1 
HETATM 2500 O  O   . HOH R 5 .   ? 16.789 -18.501 31.077  1.00  25.10 ? 2041 HOH A O   1 
HETATM 2501 O  O   . HOH R 5 .   ? 39.048 -2.930  29.441  1.00  37.89 ? 2042 HOH A O   1 
HETATM 2502 O  O   . HOH R 5 .   ? 36.880 -3.083  25.903  1.00  38.65 ? 2043 HOH A O   1 
HETATM 2503 O  O   . HOH R 5 .   ? 32.400 -3.995  25.476  1.00  23.77 ? 2044 HOH A O   1 
HETATM 2504 O  O   . HOH R 5 .   ? 36.695 -3.582  32.887  1.00  44.05 ? 2045 HOH A O   1 
HETATM 2505 O  O   . HOH R 5 .   ? 35.605 -4.119  23.914  1.00  31.61 ? 2046 HOH A O   1 
HETATM 2506 O  O   . HOH R 5 .   ? 29.860 -8.100  31.291  1.00  21.02 ? 2047 HOH A O   1 
HETATM 2507 O  O   . HOH R 5 .   ? 25.399 -27.211 24.803  1.00  33.29 ? 2048 HOH A O   1 
HETATM 2508 O  O   . HOH R 5 .   ? 28.134 -7.232  29.378  0.30  9.57  ? 2049 HOH A O   1 
HETATM 2509 O  O   . HOH R 5 .   ? 17.999 -13.575 31.180  1.00  14.02 ? 2050 HOH A O   1 
HETATM 2510 O  O   . HOH R 5 .   ? 27.516 -2.112  32.923  1.00  18.17 ? 2051 HOH A O   1 
HETATM 2511 O  O   . HOH R 5 .   ? 24.225 -1.597  33.144  1.00  21.02 ? 2052 HOH A O   1 
HETATM 2512 O  O   . HOH R 5 .   ? 13.379 -13.511 32.517  1.00  30.04 ? 2053 HOH A O   1 
HETATM 2513 O  O   . HOH R 5 .   ? 8.013  -12.214 33.336  1.00  40.77 ? 2054 HOH A O   1 
HETATM 2514 O  O   . HOH R 5 .   ? 17.241 -2.351  37.314  1.00  49.86 ? 2055 HOH A O   1 
HETATM 2515 O  O   . HOH R 5 .   ? 16.380 2.189   33.650  1.00  43.99 ? 2056 HOH A O   1 
HETATM 2516 O  O   . HOH R 5 .   ? 13.421 -0.628  38.318  1.00  33.07 ? 2057 HOH A O   1 
HETATM 2517 O  O   . HOH R 5 .   ? 13.654 1.169   33.787  1.00  42.60 ? 2058 HOH A O   1 
HETATM 2518 O  O   . HOH R 5 .   ? 11.640 -2.475  33.826  1.00  39.93 ? 2059 HOH A O   1 
HETATM 2519 O  O   . HOH R 5 .   ? 21.285 -14.742 33.021  1.00  39.88 ? 2060 HOH A O   1 
HETATM 2520 O  O   . HOH R 5 .   ? 19.346 -15.404 35.195  1.00  32.78 ? 2061 HOH A O   1 
HETATM 2521 O  O   . HOH R 5 .   ? 4.657  -2.018  23.537  1.00  40.80 ? 2062 HOH A O   1 
HETATM 2522 O  O   . HOH R 5 .   ? 31.718 1.685   20.530  1.00  51.66 ? 2063 HOH A O   1 
HETATM 2523 O  O   . HOH R 5 .   ? -2.884 -1.473  22.108  1.00  46.25 ? 2064 HOH A O   1 
HETATM 2524 O  O   . HOH R 5 .   ? 1.299  0.663   23.903  1.00  45.86 ? 2065 HOH A O   1 
HETATM 2525 O  O   . HOH R 5 .   ? 36.609 -13.082 14.539  1.00  29.91 ? 2066 HOH A O   1 
HETATM 2526 O  O   . HOH R 5 .   ? 0.343  -12.885 18.196  1.00  16.73 ? 2067 HOH A O   1 
HETATM 2527 O  O   . HOH R 5 .   ? -2.790 -12.537 23.189  0.50  22.26 ? 2068 HOH A O   1 
HETATM 2528 O  O   . HOH R 5 .   ? 2.273  -14.506 19.591  1.00  13.32 ? 2069 HOH A O   1 
HETATM 2529 O  O   . HOH R 5 .   ? 2.201  -18.837 23.088  1.00  30.24 ? 2070 HOH A O   1 
HETATM 2530 O  O   . HOH R 5 .   ? -0.467 -16.239 32.728  1.00  15.93 ? 2071 HOH A O   1 
HETATM 2531 O  O   . HOH R 5 .   ? -0.259 -19.711 23.673  1.00  26.57 ? 2072 HOH A O   1 
HETATM 2532 O  O   . HOH R 5 .   ? 1.025  -19.199 18.517  1.00  33.44 ? 2073 HOH A O   1 
HETATM 2533 O  O   . HOH R 5 .   ? 0.598  -22.944 17.032  1.00  31.10 ? 2074 HOH A O   1 
HETATM 2534 O  O   . HOH R 5 .   ? 1.903  -16.436 16.016  1.00  34.61 ? 2075 HOH A O   1 
HETATM 2535 O  O   . HOH R 5 .   ? 7.290  -24.924 24.206  1.00  24.35 ? 2076 HOH A O   1 
HETATM 2536 O  O   . HOH R 5 .   ? 10.041 -25.251 23.970  1.00  25.87 ? 2077 HOH A O   1 
HETATM 2537 O  O   . HOH R 5 .   ? 10.144 -28.113 18.615  1.00  31.62 ? 2078 HOH A O   1 
HETATM 2538 O  O   . HOH R 5 .   ? 12.132 -17.899 19.523  0.50  8.44  ? 2079 HOH A O   1 
HETATM 2539 O  O   . HOH R 5 .   ? 17.237 -20.373 10.058  1.00  44.13 ? 2080 HOH A O   1 
HETATM 2540 O  O   . HOH R 5 .   ? 20.648 -20.596 12.162  1.00  26.37 ? 2081 HOH A O   1 
HETATM 2541 O  O   . HOH R 5 .   ? 2.221  -16.550 13.650  1.00  33.37 ? 2082 HOH A O   1 
HETATM 2542 O  O   . HOH R 5 .   ? 28.177 -9.612  11.332  1.00  18.67 ? 2083 HOH A O   1 
HETATM 2543 O  O   . HOH R 5 .   ? 30.115 -13.213 10.869  1.00  37.59 ? 2084 HOH A O   1 
HETATM 2544 O  O   . HOH R 5 .   ? 28.416 -13.127 8.148   1.00  22.44 ? 2085 HOH A O   1 
HETATM 2545 O  O   . HOH R 5 .   ? 29.573 -12.859 13.536  1.00  23.64 ? 2086 HOH A O   1 
HETATM 2546 O  O   . HOH R 5 .   ? 2.373  -11.967 13.890  1.00  27.76 ? 2087 HOH A O   1 
HETATM 2547 O  O   . HOH R 5 .   ? 17.839 -2.640  7.647   1.00  11.06 ? 2088 HOH A O   1 
HETATM 2548 O  O   . HOH R 5 .   ? 19.167 -8.227  1.848   1.00  19.09 ? 2089 HOH A O   1 
HETATM 2549 O  O   . HOH R 5 .   ? 14.017 -0.579  9.280   1.00  15.58 ? 2090 HOH A O   1 
HETATM 2550 O  O   . HOH R 5 .   ? 12.900 -2.748  10.961  0.30  11.97 ? 2091 HOH A O   1 
HETATM 2551 O  O   . HOH R 5 .   ? 11.001 -2.621  11.272  0.70  21.28 ? 2092 HOH A O   1 
HETATM 2552 O  O   . HOH R 5 .   ? 11.763 -1.336  8.944   1.00  27.53 ? 2093 HOH A O   1 
HETATM 2553 O  O   . HOH R 5 .   ? 11.170 -3.433  6.720   1.00  24.57 ? 2094 HOH A O   1 
HETATM 2554 O  O   . HOH R 5 .   ? 10.763 -5.188  9.516   0.50  20.47 ? 2095 HOH A O   1 
HETATM 2555 O  O   . HOH R 5 .   ? 8.940  -9.462  8.824   1.00  20.70 ? 2096 HOH A O   1 
HETATM 2556 O  O   . HOH R 5 .   ? 17.469 -14.970 8.169   1.00  21.71 ? 2097 HOH A O   1 
HETATM 2557 O  O   . HOH R 5 .   ? 20.930 -9.917  5.460   1.00  22.62 ? 2098 HOH A O   1 
HETATM 2558 O  O   . HOH R 5 .   ? 16.167 -11.955 3.905   1.00  23.48 ? 2099 HOH A O   1 
HETATM 2559 O  O   . HOH R 5 .   ? 28.790 -16.110 20.164  1.00  10.43 ? 2100 HOH A O   1 
HETATM 2560 O  O   . HOH R 5 .   ? 35.195 -19.178 20.972  1.00  24.81 ? 2101 HOH A O   1 
HETATM 2561 O  O   . HOH R 5 .   ? 34.437 -21.813 19.127  0.50  18.95 ? 2102 HOH A O   1 
HETATM 2562 O  O   . HOH R 5 .   ? 34.321 -17.062 15.976  1.00  20.00 ? 2103 HOH A O   1 
HETATM 2563 O  O   . HOH R 5 .   ? 34.000 -20.394 13.397  1.00  29.27 ? 2104 HOH A O   1 
HETATM 2564 O  O   . HOH R 5 .   ? 30.914 -24.233 18.531  1.00  26.82 ? 2105 HOH A O   1 
HETATM 2565 O  O   . HOH R 5 .   ? 33.862 -22.822 18.223  0.50  22.03 ? 2106 HOH A O   1 
HETATM 2566 O  O   . HOH R 5 .   ? 29.498 -22.231 15.955  1.00  26.78 ? 2107 HOH A O   1 
HETATM 2567 O  O   . HOH R 5 .   ? 23.132 -26.520 21.999  1.00  25.45 ? 2108 HOH A O   1 
HETATM 2568 O  O   . HOH R 5 .   ? 23.890 -21.398 34.663  1.00  33.49 ? 2109 HOH A O   1 
HETATM 2569 O  O   . HOH R 5 .   ? 19.137 -19.796 30.359  1.00  16.54 ? 2110 HOH A O   1 
HETATM 2570 O  O   . HOH R 5 .   ? 26.165 -16.939 30.093  1.00  13.97 ? 2111 HOH A O   1 
HETATM 2571 O  O   . HOH R 5 .   ? 20.136 -22.029 31.742  0.50  20.23 ? 2112 HOH A O   1 
HETATM 2572 O  O   . HOH R 5 .   ? 19.078 -22.437 30.727  0.50  18.53 ? 2113 HOH A O   1 
HETATM 2573 O  O   . HOH R 5 .   ? 19.578 -24.293 28.622  1.00  23.32 ? 2114 HOH A O   1 
HETATM 2574 O  O   . HOH R 5 .   ? 33.249 -25.027 27.049  1.00  36.13 ? 2115 HOH A O   1 
HETATM 2575 O  O   . HOH R 5 .   ? 29.400 -25.268 28.687  1.00  29.13 ? 2116 HOH A O   1 
HETATM 2576 O  O   . HOH R 5 .   ? 34.404 -22.593 26.803  1.00  26.95 ? 2117 HOH A O   1 
HETATM 2577 O  O   . HOH R 5 .   ? 29.836 -17.963 27.523  1.00  16.07 ? 2118 HOH A O   1 
HETATM 2578 O  O   . HOH R 5 .   ? 23.980 -24.753 24.952  1.00  17.23 ? 2119 HOH A O   1 
HETATM 2579 O  O   . HOH R 5 .   ? 30.833 -24.685 21.051  1.00  37.15 ? 2120 HOH A O   1 
HETATM 2580 O  O   . HOH R 5 .   ? 28.979 -16.699 22.829  1.00  11.46 ? 2121 HOH A O   1 
HETATM 2581 O  O   . HOH R 5 .   ? 15.910 -13.809 29.309  1.00  15.22 ? 2122 HOH A O   1 
HETATM 2582 O  O   . HOH R 5 .   ? 14.885 -18.530 29.116  0.50  18.86 ? 2123 HOH A O   1 
HETATM 2583 O  O   . HOH R 5 .   ? 15.013 -16.696 29.450  1.00  18.64 ? 2124 HOH A O   1 
HETATM 2584 O  O   . HOH R 5 .   ? 12.737 -19.300 29.244  1.00  19.23 ? 2125 HOH A O   1 
HETATM 2585 O  O   . HOH R 5 .   ? 13.419 -12.813 29.901  1.00  19.83 ? 2126 HOH A O   1 
HETATM 2586 O  O   . HOH R 5 .   ? 10.645 -14.824 30.422  1.00  19.02 ? 2127 HOH A O   1 
HETATM 2587 O  O   . HOH R 5 .   ? 10.447 -13.525 32.330  1.00  29.11 ? 2128 HOH A O   1 
HETATM 2588 O  O   . HOH R 5 .   ? 7.887  -17.029 32.646  1.00  24.85 ? 2129 HOH A O   1 
HETATM 2589 O  O   . HOH R 5 .   ? 5.905  -10.373 31.396  1.00  18.00 ? 2130 HOH A O   1 
HETATM 2590 O  O   . HOH R 5 .   ? 0.594  -12.273 34.784  1.00  35.53 ? 2131 HOH A O   1 
HETATM 2591 O  O   . HOH R 5 .   ? -1.461 -9.346  33.264  1.00  27.73 ? 2132 HOH A O   1 
HETATM 2592 O  O   . HOH R 5 .   ? 4.360  -13.295 33.791  1.00  26.82 ? 2133 HOH A O   1 
HETATM 2593 O  O   . HOH R 5 .   ? -2.870 -11.280 31.756  1.00  31.15 ? 2134 HOH A O   1 
HETATM 2594 O  O   . HOH R 5 .   ? -4.255 -14.916 25.968  1.00  23.86 ? 2135 HOH A O   1 
HETATM 2595 O  O   . HOH R 5 .   ? -6.668 -14.272 26.152  1.00  24.04 ? 2136 HOH A O   1 
HETATM 2596 O  O   . HOH R 5 .   ? -7.114 -8.255  27.149  1.00  31.99 ? 2137 HOH A O   1 
HETATM 2597 O  O   . HOH R 5 .   ? -1.970 -8.263  23.210  0.70  13.16 ? 2138 HOH A O   1 
HETATM 2598 O  O   . HOH R 5 .   ? -7.129 -10.664 28.160  1.00  27.96 ? 2139 HOH A O   1 
HETATM 2599 O  O   . HOH R 5 .   ? -5.075 -7.374  25.771  1.00  22.00 ? 2140 HOH A O   1 
HETATM 2600 O  O   . HOH R 5 .   ? -1.352 -7.146  24.134  0.30  9.47  ? 2141 HOH A O   1 
HETATM 2601 O  O   . HOH R 5 .   ? 3.045  -8.737  31.237  1.00  25.66 ? 2142 HOH A O   1 
HETATM 2602 O  O   . HOH R 5 .   ? 9.706  -9.344  33.579  1.00  29.60 ? 2143 HOH A O   1 
HETATM 2603 O  O   . HOH R 5 .   ? 6.204  -10.814 33.985  1.00  30.63 ? 2144 HOH A O   1 
HETATM 2604 O  O   . HOH R 5 .   ? 4.144  -10.228 33.303  1.00  26.53 ? 2145 HOH A O   1 
HETATM 2605 O  O   . HOH R 5 .   ? 3.132  -2.966  30.557  1.00  25.70 ? 2146 HOH A O   1 
HETATM 2606 O  O   . HOH R 5 .   ? 5.626  -8.545  35.180  1.00  22.77 ? 2147 HOH A O   1 
HETATM 2607 O  O   . HOH R 5 .   ? 9.187  -5.526  34.588  1.00  27.67 ? 2148 HOH A O   1 
HETATM 2608 O  O   . HOH R 5 .   ? 9.254  -11.237 29.954  1.00  14.54 ? 2149 HOH A O   1 
HETATM 2609 O  O   . HOH R 5 .   ? 5.191  -5.689  34.948  1.00  24.52 ? 2150 HOH A O   1 
HETATM 2610 O  O   . HOH R 5 .   ? 8.967  -4.529  32.278  0.50  17.59 ? 2151 HOH A O   1 
HETATM 2611 O  O   . HOH R 5 .   ? 9.968  -3.927  32.270  0.50  13.78 ? 2152 HOH A O   1 
HETATM 2612 O  O   . HOH R 5 .   ? 11.770 -10.939 33.731  1.00  26.93 ? 2153 HOH A O   1 
HETATM 2613 O  O   . HOH R 5 .   ? 15.311 -11.696 33.955  1.00  30.59 ? 2154 HOH A O   1 
HETATM 2614 O  O   . HOH R 5 .   ? 16.778 -6.335  35.289  1.00  35.83 ? 2155 HOH A O   1 
HETATM 2615 O  O   . HOH R 5 .   ? 11.915 -10.610 30.467  1.00  13.82 ? 2156 HOH A O   1 
HETATM 2616 O  O   . HOH R 5 .   ? 16.095 -4.673  33.474  1.00  26.50 ? 2157 HOH A O   1 
HETATM 2617 O  O   . HOH R 5 .   ? 22.674 -12.755 33.918  1.00  29.64 ? 2158 HOH A O   1 
HETATM 2618 O  O   . HOH R 5 .   ? 21.583 -10.402 37.387  1.00  38.36 ? 2159 HOH A O   1 
HETATM 2619 O  O   . HOH R 5 .   ? 20.620 -12.789 30.918  1.00  14.05 ? 2160 HOH A O   1 
HETATM 2620 O  O   . HOH R 5 .   ? 19.852 -12.293 35.094  1.00  33.54 ? 2161 HOH A O   1 
HETATM 2621 O  O   . HOH R 5 .   ? 17.957 -11.666 33.265  1.00  17.20 ? 2162 HOH A O   1 
HETATM 2622 O  O   . HOH R 5 .   ? 24.183 -13.110 31.452  1.00  14.43 ? 2163 HOH A O   1 
HETATM 2623 O  O   . HOH R 5 .   ? 23.988 -9.909  33.925  1.00  22.69 ? 2164 HOH A O   1 
HETATM 2624 O  O   . HOH R 5 .   ? 29.099 -6.864  28.290  0.70  15.73 ? 2165 HOH A O   1 
HETATM 2625 O  O   . HOH R 5 .   ? 29.114 1.755   21.218  1.00  34.10 ? 2166 HOH A O   1 
HETATM 2626 O  O   . HOH R 5 .   ? 30.464 -1.076  26.142  1.00  32.25 ? 2167 HOH A O   1 
HETATM 2627 O  O   . HOH R 5 .   ? 32.454 -6.586  23.329  1.00  18.11 ? 2168 HOH A O   1 
HETATM 2628 O  O   . HOH R 5 .   ? 32.675 -0.571  19.254  1.00  43.25 ? 2169 HOH A O   1 
HETATM 2629 O  O   . HOH R 5 .   ? 31.425 -9.016  16.236  1.00  23.34 ? 2170 HOH A O   1 
HETATM 2630 O  O   . HOH R 5 .   ? 34.276 -12.144 16.108  1.00  35.45 ? 2171 HOH A O   1 
HETATM 2631 O  O   . HOH R 5 .   ? 35.710 -10.709 21.993  1.00  19.40 ? 2172 HOH A O   1 
HETATM 2632 O  O   . HOH R 5 .   ? 34.950 -5.108  17.329  1.00  34.83 ? 2173 HOH A O   1 
HETATM 2633 O  O   . HOH R 5 .   ? 35.871 -13.302 18.150  1.00  37.63 ? 2174 HOH A O   1 
HETATM 2634 O  O   . HOH R 5 .   ? 35.858 -5.977  21.887  1.00  18.39 ? 2175 HOH A O   1 
HETATM 2635 O  O   . HOH R 5 .   ? 33.337 -7.177  15.663  1.00  35.31 ? 2176 HOH A O   1 
HETATM 2636 O  O   . HOH R 5 .   ? 35.147 -12.817 24.328  0.50  11.68 ? 2177 HOH A O   1 
HETATM 2637 O  O   . HOH R 5 .   ? 29.698 -6.658  17.032  1.00  19.90 ? 2178 HOH A O   1 
HETATM 2638 O  O   . HOH R 5 .   ? 27.451 -4.594  16.535  1.00  22.74 ? 2179 HOH A O   1 
HETATM 2639 O  O   . HOH R 5 .   ? 31.082 -7.018  12.447  1.00  50.34 ? 2180 HOH A O   1 
HETATM 2640 O  O   . HOH R 5 .   ? 5.697  -14.855 19.114  0.50  10.31 ? 2181 HOH A O   1 
HETATM 2641 O  O   . HOH R 5 .   ? 3.611  -20.349 20.923  1.00  27.70 ? 2182 HOH A O   1 
HETATM 2642 O  O   . HOH R 5 .   ? 3.567  -21.231 12.961  1.00  28.70 ? 2183 HOH A O   1 
HETATM 2643 O  O   . HOH R 5 .   ? 6.187  -21.521 12.189  1.00  35.17 ? 2184 HOH A O   1 
HETATM 2644 O  O   . HOH R 5 .   ? 2.130  -21.019 17.067  1.00  32.71 ? 2185 HOH A O   1 
HETATM 2645 O  O   . HOH R 5 .   ? 2.676  -17.086 18.695  1.00  14.59 ? 2186 HOH A O   1 
HETATM 2646 O  O   . HOH R 5 .   ? 7.145  -26.230 20.031  1.00  39.51 ? 2187 HOH A O   1 
HETATM 2647 O  O   . HOH R 5 .   ? 9.792  -24.600 21.219  1.00  20.90 ? 2188 HOH A O   1 
HETATM 2648 O  O   . HOH R 5 .   ? 6.768  -23.316 22.156  1.00  23.31 ? 2189 HOH A O   1 
HETATM 2649 O  O   . HOH R 5 .   ? 18.264 -18.166 23.858  1.00  10.35 ? 2190 HOH A O   1 
HETATM 2650 O  O   . HOH R 5 .   ? 12.191 -23.363 27.213  1.00  17.92 ? 2191 HOH A O   1 
HETATM 2651 O  O   . HOH R 5 .   ? 11.597 -27.520 21.053  1.00  21.22 ? 2192 HOH A O   1 
HETATM 2652 O  O   . HOH R 5 .   ? 13.837 -25.392 27.414  1.00  22.93 ? 2193 HOH A O   1 
HETATM 2653 O  O   . HOH R 5 .   ? 21.657 -25.653 26.528  1.00  26.50 ? 2194 HOH A O   1 
HETATM 2654 O  O   . HOH R 5 .   ? 18.824 -32.258 25.510  1.00  41.35 ? 2195 HOH A O   1 
HETATM 2655 O  O   . HOH R 5 .   ? 24.629 -28.411 31.319  1.00  43.71 ? 2196 HOH A O   1 
HETATM 2656 O  O   . HOH R 5 .   ? 24.778 -26.401 27.994  1.00  31.78 ? 2197 HOH A O   1 
HETATM 2657 O  O   . HOH R 5 .   ? 12.088 -28.127 25.305  1.00  26.45 ? 2198 HOH A O   1 
HETATM 2658 O  O   . HOH R 5 .   ? 19.133 -30.701 22.926  1.00  28.09 ? 2199 HOH A O   1 
HETATM 2659 O  O   . HOH R 5 .   ? 20.088 -31.487 20.565  1.00  37.80 ? 2200 HOH A O   1 
HETATM 2660 O  O   . HOH R 5 .   ? 13.125 -33.104 15.208  1.00  32.01 ? 2201 HOH A O   1 
HETATM 2661 O  O   . HOH R 5 .   ? 23.540 -34.909 11.580  1.00  37.43 ? 2202 HOH A O   1 
HETATM 2662 O  O   . HOH R 5 .   ? 16.365 -30.879 14.133  1.00  16.26 ? 2203 HOH A O   1 
HETATM 2663 O  O   . HOH R 5 .   ? 13.799 -30.164 13.366  1.00  25.62 ? 2204 HOH A O   1 
HETATM 2664 O  O   . HOH R 5 .   ? 13.175 -27.962 10.979  1.00  37.45 ? 2205 HOH A O   1 
HETATM 2665 O  O   . HOH R 5 .   ? 14.827 -22.660 11.533  1.00  28.22 ? 2206 HOH A O   1 
HETATM 2666 O  O   . HOH R 5 .   ? 25.061 -28.360 16.410  1.00  38.05 ? 2207 HOH A O   1 
HETATM 2667 O  O   . HOH R 5 .   ? 21.472 -19.629 14.770  1.00  17.35 ? 2208 HOH A O   1 
HETATM 2668 O  O   . HOH R 5 .   ? 22.953 -25.297 10.570  1.00  27.55 ? 2209 HOH A O   1 
HETATM 2669 O  O   . HOH R 5 .   ? 25.309 -29.351 11.723  1.00  38.54 ? 2210 HOH A O   1 
HETATM 2670 O  O   . HOH R 5 .   ? 14.471 -20.227 17.267  1.00  13.00 ? 2211 HOH A O   1 
HETATM 2671 O  O   . HOH R 5 .   ? 11.960 -26.894 14.622  0.50  19.67 ? 2212 HOH A O   1 
HETATM 2672 O  O   . HOH R 5 .   ? 12.534 -29.024 18.311  1.00  37.98 ? 2213 HOH A O   1 
HETATM 2673 O  O   . HOH R 5 .   ? 12.469 -19.550 12.772  1.00  20.18 ? 2214 HOH A O   1 
HETATM 2674 O  O   . HOH R 5 .   ? 3.250  -17.869 11.938  1.00  39.71 ? 2215 HOH A O   1 
HETATM 2675 O  O   . HOH R 5 .   ? 4.313  -19.904 11.232  1.00  39.13 ? 2216 HOH A O   1 
HETATM 2676 O  O   . HOH R 5 .   ? 7.268  -10.631 10.727  0.50  17.67 ? 2217 HOH A O   1 
HETATM 2677 O  O   . HOH R 5 .   ? 3.427  -9.336  14.243  1.00  17.88 ? 2218 HOH A O   1 
HETATM 2678 O  O   . HOH R 5 .   ? 14.251 -0.797  13.332  1.00  14.63 ? 2219 HOH A O   1 
HETATM 2679 O  O   . HOH R 5 .   ? 14.659 0.138   16.120  1.00  7.74  ? 2220 HOH A O   1 
HETATM 2680 O  O   . HOH R 5 .   ? 24.510 5.967   24.347  1.00  18.36 ? 2221 HOH A O   1 
HETATM 2681 O  O   . HOH R 5 .   ? 24.682 8.720   22.332  1.00  18.25 ? 2222 HOH A O   1 
HETATM 2682 O  O   . HOH R 5 .   ? 22.895 8.861   28.187  1.00  39.66 ? 2223 HOH A O   1 
HETATM 2683 O  O   . HOH R 5 .   ? 18.420 7.631   25.946  1.00  26.86 ? 2224 HOH A O   1 
HETATM 2684 O  O   . HOH R 5 .   ? 24.411 11.017  24.053  1.00  20.86 ? 2225 HOH A O   1 
HETATM 2685 O  O   . HOH R 5 .   ? 19.101 9.213   28.081  1.00  36.83 ? 2226 HOH A O   1 
HETATM 2686 O  O   . HOH R 5 .   ? 19.031 15.236  26.850  1.00  27.08 ? 2227 HOH A O   1 
HETATM 2687 O  O   . HOH R 5 .   ? 16.917 10.955  22.895  0.75  21.21 ? 2228 HOH A O   1 
HETATM 2688 O  O   . HOH R 5 .   ? 6.836  -14.598 9.856   1.00  30.58 ? 2229 HOH A O   1 
HETATM 2689 O  O   . HOH R 5 .   ? 15.060 -33.769 12.092  0.50  17.91 ? 2230 HOH A O   1 
HETATM 2690 O  O   . HOH R 5 .   ? 17.301 -29.904 11.696  1.00  22.83 ? 2231 HOH A O   1 
HETATM 2691 O  O   . HOH R 5 .   ? 16.580 -37.842 13.806  1.00  22.62 ? 2232 HOH A O   1 
HETATM 2692 O  O   . HOH R 5 .   ? 16.378 -36.560 18.035  1.00  20.61 ? 2233 HOH A O   1 
HETATM 2693 O  O   . HOH R 5 .   ? 30.525 -16.611 25.175  1.00  17.92 ? 2234 HOH A O   1 
HETATM 2694 O  O   . HOH R 5 .   ? 35.334 -20.076 27.813  1.00  37.67 ? 2235 HOH A O   1 
HETATM 2695 O  O   . HOH R 5 .   ? 34.431 -21.851 22.238  1.00  39.20 ? 2236 HOH A O   1 
HETATM 2696 O  O   . HOH R 5 .   ? 14.243 -17.885 11.955  0.50  7.19  ? 2237 HOH A O   1 
HETATM 2697 O  O   . HOH R 5 .   ? 18.828 -18.819 11.580  1.00  22.40 ? 2238 HOH A O   1 
HETATM 2698 O  O   . HOH R 5 .   ? 12.301 -25.554 10.574  1.00  34.12 ? 2239 HOH A O   1 
HETATM 2699 O  O   . HOH R 5 .   ? 9.106  -20.969 11.542  0.50  23.33 ? 2240 HOH A O   1 
HETATM 2700 O  O   . HOH R 5 .   ? 11.223 -25.532 15.000  0.50  16.17 ? 2241 HOH A O   1 
HETATM 2701 O  O   . HOH R 5 .   ? 14.015 -22.121 14.072  1.00  23.30 ? 2242 HOH A O   1 
HETATM 2702 O  O   . HOH R 5 .   ? 14.033 -17.476 8.757   1.00  38.78 ? 2243 HOH A O   1 
HETATM 2703 O  O   . HOH R 5 .   ? 10.932 -16.450 6.157   1.00  40.96 ? 2244 HOH A O   1 
HETATM 2704 O  O   . HOH R 5 .   ? 9.710  -16.182 10.322  0.60  14.65 ? 2245 HOH A O   1 
HETATM 2705 O  O   . HOH R 5 .   ? 12.637 -17.576 10.704  0.50  21.38 ? 2246 HOH A O   1 
HETATM 2706 O  O   . HOH R 5 .   ? 9.788  -12.571 9.220   1.00  31.82 ? 2247 HOH A O   1 
HETATM 2707 O  O   . HOH S 5 .   ? 6.126  17.859  16.635  1.00  26.94 ? 2001 HOH F O   1 
HETATM 2708 O  O   . HOH S 5 .   ? 28.388 15.822  -3.654  1.00  31.09 ? 2002 HOH F O   1 
HETATM 2709 O  O   . HOH S 5 .   ? 34.318 -7.512  0.652   1.00  36.78 ? 2003 HOH F O   1 
HETATM 2710 O  O   . HOH S 5 .   ? 37.268 -7.851  -0.040  1.00  35.97 ? 2004 HOH F O   1 
HETATM 2711 O  O   . HOH S 5 .   ? 24.048 -5.896  -3.989  1.00  25.31 ? 2005 HOH F O   1 
HETATM 2712 O  O   . HOH S 5 .   ? 30.508 -6.226  -5.479  1.00  39.98 ? 2006 HOH F O   1 
HETATM 2713 O  O   . HOH S 5 .   ? 38.390 -7.000  2.562   1.00  39.90 ? 2007 HOH F O   1 
HETATM 2714 O  O   . HOH S 5 .   ? 34.533 -4.931  9.235   1.00  40.88 ? 2008 HOH F O   1 
HETATM 2715 O  O   . HOH S 5 .   ? 8.889  0.931   10.719  1.00  28.60 ? 2009 HOH F O   1 
HETATM 2716 O  O   . HOH S 5 .   ? 10.327 5.046   12.207  1.00  35.83 ? 2010 HOH F O   1 
HETATM 2717 O  O   . HOH S 5 .   ? 38.486 5.678   -3.630  1.00  34.33 ? 2011 HOH F O   1 
HETATM 2718 O  O   . HOH S 5 .   ? 25.658 -5.265  -1.630  1.00  27.04 ? 2012 HOH F O   1 
HETATM 2719 O  O   . HOH S 5 .   ? 30.747 -7.670  -2.478  1.00  37.08 ? 2013 HOH F O   1 
HETATM 2720 O  O   . HOH S 5 .   ? 25.725 -8.293  -1.195  1.00  29.67 ? 2014 HOH F O   1 
HETATM 2721 O  O   . HOH S 5 .   ? 1.618  11.937  1.135   1.00  28.15 ? 2015 HOH F O   1 
HETATM 2722 O  O   . HOH S 5 .   ? 4.405  15.561  2.597   1.00  29.11 ? 2016 HOH F O   1 
HETATM 2723 O  O   . HOH S 5 .   ? 11.635 -0.019  -1.279  1.00  41.32 ? 2017 HOH F O   1 
HETATM 2724 O  O   . HOH S 5 .   ? 3.530  16.832  -1.478  1.00  41.98 ? 2018 HOH F O   1 
HETATM 2725 O  O   . HOH S 5 .   ? 23.511 -5.688  1.677   1.00  33.90 ? 2019 HOH F O   1 
HETATM 2726 O  O   . HOH S 5 .   ? 12.529 1.346   8.485   1.00  21.48 ? 2020 HOH F O   1 
HETATM 2727 O  O   . HOH S 5 .   ? 36.218 2.380   -2.484  1.00  29.07 ? 2021 HOH F O   1 
HETATM 2728 O  O   . HOH S 5 .   ? 25.517 -4.747  -5.815  1.00  27.28 ? 2022 HOH F O   1 
HETATM 2729 O  O   . HOH S 5 .   ? 25.552 -1.805  -6.947  1.00  43.00 ? 2023 HOH F O   1 
HETATM 2730 O  O   . HOH S 5 .   ? 8.847  -0.992  9.765   1.00  26.78 ? 2024 HOH F O   1 
HETATM 2731 O  O   . HOH S 5 .   ? 9.902  5.198   9.952   1.00  29.01 ? 2025 HOH F O   1 
HETATM 2732 O  O   . HOH S 5 .   ? 38.114 -4.664  -3.085  1.00  37.26 ? 2026 HOH F O   1 
HETATM 2733 O  O   . HOH S 5 .   ? 31.210 27.893  9.757   1.00  37.31 ? 2027 HOH F O   1 
HETATM 2734 O  O   . HOH S 5 .   ? -1.512 7.929   9.979   1.00  32.09 ? 2028 HOH F O   1 
HETATM 2735 O  O   . HOH S 5 .   ? 4.185  11.760  12.262  1.00  44.97 ? 2029 HOH F O   1 
HETATM 2736 O  O   . HOH S 5 .   ? 4.730  12.169  1.722   1.00  24.68 ? 2030 HOH F O   1 
HETATM 2737 O  O   . HOH S 5 .   ? 35.135 14.520  -5.337  1.00  48.69 ? 2031 HOH F O   1 
HETATM 2738 O  O   . HOH S 5 .   ? 5.788  4.973   -2.720  1.00  35.02 ? 2032 HOH F O   1 
HETATM 2739 O  O   . HOH S 5 .   ? 4.199  13.810  -2.022  1.00  47.56 ? 2033 HOH F O   1 
HETATM 2740 O  O   . HOH S 5 .   ? 3.898  12.897  -4.954  1.00  42.61 ? 2034 HOH F O   1 
HETATM 2741 O  O   . HOH S 5 .   ? 1.481  9.539   -7.762  1.00  43.73 ? 2035 HOH F O   1 
HETATM 2742 O  O   . HOH S 5 .   ? 10.328 -1.849  2.606   1.00  34.63 ? 2036 HOH F O   1 
HETATM 2743 O  O   . HOH S 5 .   ? 12.295 2.246   -3.038  1.00  38.16 ? 2037 HOH F O   1 
HETATM 2744 O  O   . HOH S 5 .   ? 4.122  15.801  -6.125  1.00  39.01 ? 2038 HOH F O   1 
HETATM 2745 O  O   . HOH S 5 .   ? 11.520 0.421   1.662   1.00  32.75 ? 2039 HOH F O   1 
HETATM 2746 O  O   . HOH S 5 .   ? 20.939 -4.965  -0.459  1.00  20.61 ? 2040 HOH F O   1 
HETATM 2747 O  O   . HOH S 5 .   ? 23.840 -3.395  1.831   1.00  18.26 ? 2041 HOH F O   1 
HETATM 2748 O  O   . HOH S 5 .   ? 26.014 -2.790  1.231   1.00  26.04 ? 2042 HOH F O   1 
HETATM 2749 O  O   . HOH S 5 .   ? 10.603 1.326   13.246  1.00  20.64 ? 2043 HOH F O   1 
HETATM 2750 O  O   . HOH S 5 .   ? 27.313 -2.470  -5.260  1.00  41.05 ? 2044 HOH F O   1 
HETATM 2751 O  O   . HOH S 5 .   ? 33.568 1.425   -0.967  1.00  34.47 ? 2045 HOH F O   1 
HETATM 2752 O  O   . HOH S 5 .   ? 33.699 -2.740  -0.769  1.00  35.07 ? 2046 HOH F O   1 
HETATM 2753 O  O   . HOH S 5 .   ? 35.080 0.507   8.289   1.00  36.63 ? 2047 HOH F O   1 
HETATM 2754 O  O   . HOH S 5 .   ? 36.078 -1.494  5.551   1.00  27.36 ? 2048 HOH F O   1 
HETATM 2755 O  O   . HOH S 5 .   ? 36.062 2.878   -7.482  1.00  33.75 ? 2049 HOH F O   1 
HETATM 2756 O  O   . HOH S 5 .   ? 39.882 -2.943  -1.866  1.00  47.12 ? 2050 HOH F O   1 
HETATM 2757 O  O   . HOH S 5 .   ? 38.199 2.276   -0.779  1.00  30.31 ? 2051 HOH F O   1 
HETATM 2758 O  O   . HOH S 5 .   ? 38.394 18.185  14.970  1.00  29.15 ? 2052 HOH F O   1 
HETATM 2759 O  O   . HOH S 5 .   ? 36.522 14.431  9.018   0.50  20.55 ? 2053 HOH F O   1 
HETATM 2760 O  O   . HOH S 5 .   ? 38.729 14.141  11.923  0.50  21.46 ? 2054 HOH F O   1 
HETATM 2761 O  O   . HOH S 5 .   ? 41.475 16.678  11.962  1.00  40.48 ? 2055 HOH F O   1 
HETATM 2762 O  O   . HOH S 5 .   ? 39.882 -1.635  7.330   1.00  36.09 ? 2056 HOH F O   1 
HETATM 2763 O  O   . HOH S 5 .   ? 28.536 28.383  9.685   1.00  29.13 ? 2057 HOH F O   1 
HETATM 2764 O  O   . HOH S 5 .   ? 30.370 27.283  7.254   1.00  31.91 ? 2058 HOH F O   1 
HETATM 2765 O  O   . HOH S 5 .   ? 31.527 26.694  4.502   1.00  49.89 ? 2059 HOH F O   1 
HETATM 2766 O  O   . HOH S 5 .   ? 44.944 4.720   4.546   1.00  32.72 ? 2060 HOH F O   1 
HETATM 2767 O  O   . HOH S 5 .   ? 32.956 27.666  11.605  1.00  34.56 ? 2061 HOH F O   1 
HETATM 2768 O  O   . HOH S 5 .   ? 35.887 29.349  8.712   1.00  46.14 ? 2062 HOH F O   1 
HETATM 2769 O  O   . HOH S 5 .   ? 27.675 13.552  -2.318  1.00  16.03 ? 2063 HOH F O   1 
HETATM 2770 O  O   . HOH S 5 .   ? 36.351 2.105   0.933   1.00  23.59 ? 2064 HOH F O   1 
HETATM 2771 O  O   . HOH S 5 .   ? 22.216 13.744  -7.504  1.00  31.43 ? 2065 HOH F O   1 
HETATM 2772 O  O   . HOH S 5 .   ? 1.095  17.068  -13.221 1.00  42.82 ? 2066 HOH F O   1 
HETATM 2773 O  O   . HOH S 5 .   ? 7.491  4.486   -7.918  1.00  28.56 ? 2067 HOH F O   1 
HETATM 2774 O  O   . HOH S 5 .   ? 19.488 8.384   -12.397 1.00  25.09 ? 2068 HOH F O   1 
HETATM 2775 O  O   . HOH S 5 .   ? 22.086 5.430   -9.717  1.00  33.84 ? 2069 HOH F O   1 
HETATM 2776 O  O   . HOH S 5 .   ? 29.262 8.562   -6.889  1.00  35.52 ? 2070 HOH F O   1 
HETATM 2777 O  O   . HOH S 5 .   ? 31.380 4.735   -9.075  1.00  26.85 ? 2071 HOH F O   1 
HETATM 2778 O  O   . HOH S 5 .   ? 31.075 14.914  -1.949  1.00  30.65 ? 2072 HOH F O   1 
HETATM 2779 O  O   . HOH S 5 .   ? 32.351 14.405  -3.700  1.00  37.41 ? 2073 HOH F O   1 
HETATM 2780 O  O   . HOH S 5 .   ? 33.791 10.644  -5.511  1.00  34.18 ? 2074 HOH F O   1 
HETATM 2781 O  O   . HOH S 5 .   ? 14.707 0.573   -7.191  1.00  28.49 ? 2075 HOH F O   1 
HETATM 2782 O  O   . HOH S 5 .   ? 39.467 11.429  3.941   1.00  36.06 ? 2076 HOH F O   1 
HETATM 2783 O  O   . HOH S 5 .   ? 39.411 15.393  3.017   1.00  35.87 ? 2077 HOH F O   1 
HETATM 2784 O  O   . HOH S 5 .   ? 33.508 -1.490  14.401  1.00  40.77 ? 2078 HOH F O   1 
HETATM 2785 O  O   . HOH S 5 .   ? 29.573 4.218   17.323  1.00  40.14 ? 2079 HOH F O   1 
HETATM 2786 O  O   . HOH S 5 .   ? 29.688 5.272   19.793  1.00  34.59 ? 2080 HOH F O   1 
HETATM 2787 O  O   . HOH S 5 .   ? 4.259  9.344   -1.701  1.00  23.45 ? 2081 HOH F O   1 
HETATM 2788 O  O   . HOH S 5 .   ? 3.612  10.273  -3.745  1.00  37.99 ? 2082 HOH F O   1 
HETATM 2789 O  O   . HOH S 5 .   ? 5.996  12.509  -0.834  1.00  19.76 ? 2083 HOH F O   1 
HETATM 2790 O  O   . HOH S 5 .   ? 5.495  11.904  -6.475  1.00  35.32 ? 2084 HOH F O   1 
HETATM 2791 O  O   . HOH S 5 .   ? 8.199  14.287  -1.061  1.00  14.35 ? 2085 HOH F O   1 
HETATM 2792 O  O   . HOH S 5 .   ? 9.806  18.745  -4.259  1.00  22.67 ? 2086 HOH F O   1 
HETATM 2793 O  O   . HOH S 5 .   ? 26.503 6.323   22.692  1.00  27.63 ? 2087 HOH F O   1 
HETATM 2794 O  O   . HOH S 5 .   ? 8.048  20.077  -5.083  1.00  38.74 ? 2088 HOH F O   1 
HETATM 2795 O  O   . HOH S 5 .   ? 6.226  15.892  -7.940  1.00  26.54 ? 2089 HOH F O   1 
HETATM 2796 O  O   . HOH S 5 .   ? 8.012  18.956  -7.478  1.00  27.67 ? 2090 HOH F O   1 
HETATM 2797 O  O   . HOH S 5 .   ? 12.977 16.225  -13.562 1.00  15.39 ? 2091 HOH F O   1 
HETATM 2798 O  O   . HOH S 5 .   ? 11.121 19.799  -13.981 1.00  12.13 ? 2092 HOH F O   1 
HETATM 2799 O  O   . HOH S 5 .   ? 6.323  18.721  -0.782  1.00  29.39 ? 2093 HOH F O   1 
HETATM 2800 O  O   . HOH S 5 .   ? 5.533  16.551  1.030   1.00  36.09 ? 2094 HOH F O   1 
HETATM 2801 O  O   . HOH S 5 .   ? 6.614  20.084  9.953   1.00  46.14 ? 2095 HOH F O   1 
HETATM 2802 O  O   . HOH S 5 .   ? 17.137 25.247  -0.596  1.00  22.19 ? 2096 HOH F O   1 
HETATM 2803 O  O   . HOH S 5 .   ? 25.408 32.443  3.327   1.00  33.11 ? 2097 HOH F O   1 
HETATM 2804 O  O   . HOH S 5 .   ? 11.797 22.175  10.309  1.00  27.21 ? 2098 HOH F O   1 
HETATM 2805 O  O   . HOH S 5 .   ? 24.744 13.397  22.394  1.00  28.65 ? 2099 HOH F O   1 
HETATM 2806 O  O   . HOH S 5 .   ? 25.843 9.669   19.838  1.00  15.97 ? 2100 HOH F O   1 
HETATM 2807 O  O   . HOH S 5 .   ? 27.793 13.106  18.852  1.00  20.80 ? 2101 HOH F O   1 
HETATM 2808 O  O   . HOH S 5 .   ? 14.910 2.661   17.354  1.00  10.65 ? 2102 HOH F O   1 
HETATM 2809 O  O   . HOH S 5 .   ? 12.772 8.021   23.089  1.00  26.04 ? 2103 HOH F O   1 
HETATM 2810 O  O   . HOH S 5 .   ? 14.240 9.489   22.358  1.00  23.50 ? 2104 HOH F O   1 
HETATM 2811 O  O   . HOH S 5 .   ? 17.731 8.255   22.070  1.00  17.92 ? 2105 HOH F O   1 
HETATM 2812 O  O   . HOH S 5 .   ? 15.876 5.805   24.050  1.00  37.89 ? 2106 HOH F O   1 
HETATM 2813 O  O   . HOH S 5 .   ? 30.545 -6.243  9.493   1.00  30.03 ? 2107 HOH F O   1 
HETATM 2814 O  O   . HOH S 5 .   ? 23.442 -9.278  2.313   1.00  30.59 ? 2108 HOH F O   1 
HETATM 2815 O  O   . HOH S 5 .   ? 9.134  3.431   14.491  1.00  27.00 ? 2109 HOH F O   1 
HETATM 2816 O  O   . HOH S 5 .   ? 12.713 2.760   12.034  1.00  18.35 ? 2110 HOH F O   1 
HETATM 2817 O  O   . HOH S 5 .   ? 6.885  2.870   18.309  1.00  35.50 ? 2111 HOH F O   1 
HETATM 2818 O  O   . HOH S 5 .   ? 7.911  9.556   11.786  1.00  24.92 ? 2112 HOH F O   1 
HETATM 2819 O  O   . HOH S 5 .   ? 14.604 14.754  16.824  1.00  22.84 ? 2113 HOH F O   1 
HETATM 2820 O  O   . HOH S 5 .   ? 11.507 17.019  18.592  1.00  25.66 ? 2114 HOH F O   1 
HETATM 2821 O  O   . HOH S 5 .   ? 11.138 12.074  19.569  1.00  27.76 ? 2115 HOH F O   1 
HETATM 2822 O  O   . HOH S 5 .   ? 16.579 10.757  21.371  0.25  12.31 ? 2116 HOH F O   1 
HETATM 2823 O  O   . HOH S 5 .   ? 24.158 18.609  14.629  1.00  21.27 ? 2117 HOH F O   1 
HETATM 2824 O  O   . HOH S 5 .   ? 25.439 19.775  16.530  1.00  18.85 ? 2118 HOH F O   1 
HETATM 2825 O  O   . HOH S 5 .   ? 25.990 14.112  17.095  1.00  11.71 ? 2119 HOH F O   1 
HETATM 2826 O  O   . HOH S 5 .   ? 30.766 16.255  12.821  1.00  9.40  ? 2120 HOH F O   1 
HETATM 2827 O  O   . HOH S 5 .   ? 33.257 17.112  19.316  1.00  12.79 ? 2121 HOH F O   1 
HETATM 2828 O  O   . HOH S 5 .   ? 36.321 18.652  16.874  1.00  16.78 ? 2122 HOH F O   1 
HETATM 2829 O  O   . HOH S 5 .   ? 31.749 24.634  15.387  1.00  25.52 ? 2123 HOH F O   1 
HETATM 2830 O  O   . HOH S 5 .   ? 31.104 20.858  21.211  1.00  21.64 ? 2124 HOH F O   1 
HETATM 2831 O  O   . HOH S 5 .   ? 28.814 22.556  16.511  1.00  42.14 ? 2125 HOH F O   1 
HETATM 2832 O  O   . HOH S 5 .   ? 38.988 16.623  12.794  1.00  34.66 ? 2126 HOH F O   1 
HETATM 2833 O  O   . HOH S 5 .   ? 37.861 21.032  7.961   1.00  36.18 ? 2127 HOH F O   1 
HETATM 2834 O  O   . HOH S 5 .   ? 37.583 15.279  10.214  0.50  26.53 ? 2128 HOH F O   1 
HETATM 2835 O  O   . HOH S 5 .   ? 39.280 21.753  10.057  1.00  47.61 ? 2129 HOH F O   1 
HETATM 2836 O  O   . HOH S 5 .   ? 38.966 18.296  8.342   1.00  42.89 ? 2130 HOH F O   1 
HETATM 2837 O  O   . HOH S 5 .   ? 34.526 16.340  9.160   1.00  22.35 ? 2131 HOH F O   1 
HETATM 2838 O  O   . HOH S 5 .   ? 27.092 26.606  8.233   1.00  22.11 ? 2132 HOH F O   1 
HETATM 2839 O  O   . HOH S 5 .   ? 29.293 24.869  6.074   1.00  22.44 ? 2133 HOH F O   1 
HETATM 2840 O  O   . HOH S 5 .   ? 34.126 15.512  1.449   1.00  30.62 ? 2134 HOH F O   1 
HETATM 2841 O  O   . HOH S 5 .   ? 28.110 19.800  -1.089  1.00  20.10 ? 2135 HOH F O   1 
HETATM 2842 O  O   . HOH S 5 .   ? 35.187 17.286  -0.944  1.00  39.47 ? 2136 HOH F O   1 
HETATM 2843 O  O   . HOH S 5 .   ? 34.227 17.154  3.408   1.00  28.26 ? 2137 HOH F O   1 
HETATM 2844 O  O   . HOH S 5 .   ? 28.240 22.468  -1.192  1.00  38.90 ? 2138 HOH F O   1 
HETATM 2845 O  O   . HOH S 5 .   ? 35.099 17.715  6.900   1.00  25.32 ? 2139 HOH F O   1 
HETATM 2846 O  O   . HOH S 5 .   ? 42.441 24.003  2.842   1.00  28.90 ? 2140 HOH F O   1 
HETATM 2847 O  O   . HOH S 5 .   ? 34.844 23.749  1.850   1.00  30.82 ? 2141 HOH F O   1 
HETATM 2848 O  O   . HOH S 5 .   ? 37.841 18.863  3.553   1.00  40.91 ? 2142 HOH F O   1 
HETATM 2849 O  O   . HOH S 5 .   ? 35.330 26.885  11.014  1.00  42.63 ? 2143 HOH F O   1 
HETATM 2850 O  O   . HOH S 5 .   ? 33.026 25.511  13.077  1.00  28.95 ? 2144 HOH F O   1 
HETATM 2851 O  O   . HOH S 5 .   ? 33.790 24.625  4.190   1.00  23.71 ? 2145 HOH F O   1 
HETATM 2852 O  O   . HOH S 5 .   ? 32.372 16.862  10.745  1.00  13.26 ? 2146 HOH F O   1 
HETATM 2853 O  O   . HOH S 5 .   ? 25.626 22.789  14.187  1.00  25.07 ? 2147 HOH F O   1 
HETATM 2854 O  O   . HOH S 5 .   ? 24.918 13.932  -1.855  1.00  16.27 ? 2148 HOH F O   1 
HETATM 2855 O  O   . HOH S 5 .   ? 23.154 12.873  -3.694  1.00  18.99 ? 2149 HOH F O   1 
HETATM 2856 O  O   . HOH S 5 .   ? 19.971 16.660  -9.136  1.00  17.81 ? 2150 HOH F O   1 
HETATM 2857 O  O   . HOH S 5 .   ? 17.812 10.371  -8.888  1.00  20.35 ? 2151 HOH F O   1 
HETATM 2858 O  O   . HOH S 5 .   ? 19.657 11.253  -6.014  1.00  15.03 ? 2152 HOH F O   1 
HETATM 2859 O  O   . HOH S 5 .   ? 20.964 14.866  -5.607  1.00  17.99 ? 2153 HOH F O   1 
HETATM 2860 O  O   . HOH S 5 .   ? 12.021 13.892  -14.236 1.00  16.63 ? 2154 HOH F O   1 
HETATM 2861 O  O   . HOH S 5 .   ? 13.156 11.184  -16.151 1.00  20.18 ? 2155 HOH F O   1 
HETATM 2862 O  O   . HOH S 5 .   ? 16.024 12.185  -13.618 1.00  42.12 ? 2156 HOH F O   1 
HETATM 2863 O  O   . HOH S 5 .   ? 6.708  18.541  -9.670  1.00  33.47 ? 2157 HOH F O   1 
HETATM 2864 O  O   . HOH S 5 .   ? 3.434  17.859  -13.473 1.00  39.15 ? 2158 HOH F O   1 
HETATM 2865 O  O   . HOH S 5 .   ? 5.827  20.475  -13.876 1.00  38.77 ? 2159 HOH F O   1 
HETATM 2866 O  O   . HOH S 5 .   ? 5.051  7.881   -12.712 1.00  37.37 ? 2160 HOH F O   1 
HETATM 2867 O  O   . HOH S 5 .   ? 10.541 10.656  -14.378 1.00  32.65 ? 2161 HOH F O   1 
HETATM 2868 O  O   . HOH S 5 .   ? 5.274  7.509   -10.255 1.00  37.62 ? 2162 HOH F O   1 
HETATM 2869 O  O   . HOH S 5 .   ? 7.313  7.141   -6.709  1.00  18.44 ? 2163 HOH F O   1 
HETATM 2870 O  O   . HOH S 5 .   ? 5.382  10.744  -13.518 1.00  48.92 ? 2164 HOH F O   1 
HETATM 2871 O  O   . HOH S 5 .   ? 14.868 3.016   -9.792  1.00  30.09 ? 2165 HOH F O   1 
HETATM 2872 O  O   . HOH S 5 .   ? 21.848 9.507   -8.884  1.00  31.03 ? 2166 HOH F O   1 
HETATM 2873 O  O   . HOH S 5 .   ? 18.902 5.567   -12.449 1.00  24.76 ? 2167 HOH F O   1 
HETATM 2874 O  O   . HOH S 5 .   ? 21.392 3.951   -7.560  1.00  21.99 ? 2168 HOH F O   1 
HETATM 2875 O  O   . HOH S 5 .   ? 27.623 4.841   -5.264  1.00  29.46 ? 2169 HOH F O   1 
HETATM 2876 O  O   . HOH S 5 .   ? 26.472 11.880  -5.772  1.00  34.97 ? 2170 HOH F O   1 
HETATM 2877 O  O   . HOH S 5 .   ? 23.881 11.046  -7.698  1.00  26.64 ? 2171 HOH F O   1 
HETATM 2878 O  O   . HOH S 5 .   ? 29.031 6.189   -6.414  1.00  44.75 ? 2172 HOH F O   1 
HETATM 2879 O  O   . HOH S 5 .   ? 22.244 10.553  -4.986  1.00  15.68 ? 2173 HOH F O   1 
HETATM 2880 O  O   . HOH S 5 .   ? 28.774 11.720  -4.083  1.00  18.42 ? 2174 HOH F O   1 
HETATM 2881 O  O   . HOH S 5 .   ? 31.732 12.262  -4.117  1.00  30.11 ? 2175 HOH F O   1 
HETATM 2882 O  O   . HOH S 5 .   ? 35.403 8.857   -3.629  1.00  31.16 ? 2176 HOH F O   1 
HETATM 2883 O  O   . HOH S 5 .   ? 33.357 12.597  -2.199  1.00  28.65 ? 2177 HOH F O   1 
HETATM 2884 O  O   . HOH S 5 .   ? 29.766 12.875  -0.693  1.00  17.05 ? 2178 HOH F O   1 
HETATM 2885 O  O   . HOH S 5 .   ? 32.884 13.192  0.814   1.00  19.13 ? 2179 HOH F O   1 
HETATM 2886 O  O   . HOH S 5 .   ? 37.595 13.693  4.554   1.00  42.32 ? 2180 HOH F O   1 
HETATM 2887 O  O   . HOH S 5 .   ? 38.079 9.208   0.672   1.00  33.49 ? 2181 HOH F O   1 
HETATM 2888 O  O   . HOH S 5 .   ? 37.787 8.433   4.069   1.00  28.67 ? 2182 HOH F O   1 
HETATM 2889 O  O   . HOH S 5 .   ? 34.256 10.043  -1.329  1.00  24.24 ? 2183 HOH F O   1 
HETATM 2890 O  O   . HOH S 5 .   ? 36.787 13.466  -0.248  1.00  43.23 ? 2184 HOH F O   1 
HETATM 2891 O  O   . HOH S 5 .   ? 35.294 7.138   5.515   1.00  23.36 ? 2185 HOH F O   1 
HETATM 2892 O  O   . HOH S 5 .   ? 36.944 5.048   9.717   1.00  24.94 ? 2186 HOH F O   1 
HETATM 2893 O  O   . HOH S 5 .   ? 31.942 -1.666  12.190  1.00  36.20 ? 2187 HOH F O   1 
HETATM 2894 O  O   . HOH S 5 .   ? 35.491 6.950   12.096  1.00  18.64 ? 2188 HOH F O   1 
HETATM 2895 O  O   . HOH S 5 .   ? 31.638 5.122   17.434  1.00  44.57 ? 2189 HOH F O   1 
HETATM 2896 O  O   . HOH S 5 .   ? 34.541 0.858   15.317  1.00  39.58 ? 2190 HOH F O   1 
HETATM 2897 O  O   . HOH S 5 .   ? 34.019 5.249   18.575  1.00  31.76 ? 2191 HOH F O   1 
HETATM 2898 O  O   . HOH S 5 .   ? 35.353 12.597  15.921  1.00  25.92 ? 2192 HOH F O   1 
HETATM 2899 O  O   . HOH S 5 .   ? 35.492 9.395   20.144  1.00  16.21 ? 2193 HOH F O   1 
HETATM 2900 O  O   . HOH S 5 .   ? 30.866 9.177   17.648  1.00  22.65 ? 2194 HOH F O   1 
HETATM 2901 O  O   . HOH S 5 .   ? 37.866 6.601   15.533  1.00  38.19 ? 2195 HOH F O   1 
HETATM 2902 O  O   . HOH S 5 .   ? 38.172 12.773  12.588  0.50  18.14 ? 2196 HOH F O   1 
HETATM 2903 O  O   . HOH S 5 .   ? 35.714 10.150  8.752   1.00  36.01 ? 2197 HOH F O   1 
HETATM 2904 O  O   . HOH S 5 .   ? 27.813 4.604   15.428  1.00  25.59 ? 2198 HOH F O   1 
HETATM 2905 O  O   . HOH S 5 .   ? 30.010 6.695   15.911  1.00  18.17 ? 2199 HOH F O   1 
HETATM 2906 O  O   . HOH S 5 .   ? 28.567 10.557  18.839  1.00  18.27 ? 2200 HOH F O   1 
HETATM 2907 O  O   . HOH S 5 .   ? 28.276 7.235   20.124  1.00  27.04 ? 2201 HOH F O   1 
HETATM 2908 O  O   . HOH S 5 .   ? 10.900 14.797  1.184   0.70  9.19  ? 2202 HOH F O   1 
HETATM 2909 O  O   . HOH S 5 .   ? 7.114  21.585  0.755   1.00  45.10 ? 2203 HOH F O   1 
HETATM 2910 O  O   . HOH S 5 .   ? 7.623  21.265  7.748   1.00  34.99 ? 2204 HOH F O   1 
HETATM 2911 O  O   . HOH S 5 .   ? 8.145  16.864  -0.123  1.00  18.09 ? 2205 HOH F O   1 
HETATM 2912 O  O   . HOH S 5 .   ? 5.791  22.640  5.254   1.00  38.04 ? 2206 HOH F O   1 
HETATM 2913 O  O   . HOH S 5 .   ? 15.609 24.653  1.796   1.00  21.61 ? 2207 HOH F O   1 
HETATM 2914 O  O   . HOH S 5 .   ? 13.294 23.238  -0.810  1.00  21.20 ? 2208 HOH F O   1 
HETATM 2915 O  O   . HOH S 5 .   ? 20.849 23.339  -1.877  1.00  16.55 ? 2209 HOH F O   1 
HETATM 2916 O  O   . HOH S 5 .   ? 23.940 18.206  3.964   1.00  11.44 ? 2210 HOH F O   1 
HETATM 2917 O  O   . HOH S 5 .   ? 16.738 27.434  2.797   1.00  17.77 ? 2211 HOH F O   1 
HETATM 2918 O  O   . HOH S 5 .   ? 22.328 25.333  -1.451  1.00  18.09 ? 2212 HOH F O   1 
HETATM 2919 O  O   . HOH S 5 .   ? 28.027 25.879  3.706   1.00  24.00 ? 2213 HOH F O   1 
HETATM 2920 O  O   . HOH S 5 .   ? 27.026 28.104  6.149   1.00  34.56 ? 2214 HOH F O   1 
HETATM 2921 O  O   . HOH S 5 .   ? 23.770 30.802  4.789   1.00  21.89 ? 2215 HOH F O   1 
HETATM 2922 O  O   . HOH S 5 .   ? 19.647 28.177  -0.484  1.00  25.18 ? 2216 HOH F O   1 
HETATM 2923 O  O   . HOH S 5 .   ? 27.701 24.399  0.684   1.00  24.82 ? 2217 HOH F O   1 
HETATM 2924 O  O   . HOH S 5 .   ? 19.259 36.500  7.953   1.00  21.53 ? 2218 HOH F O   1 
HETATM 2925 O  O   . HOH S 5 .   ? 14.724 33.170  8.422   1.00  30.46 ? 2219 HOH F O   1 
HETATM 2926 O  O   . HOH S 5 .   ? 23.815 31.743  7.324   1.00  25.20 ? 2220 HOH F O   1 
HETATM 2927 O  O   . HOH S 5 .   ? 12.130 24.749  11.709  1.00  39.44 ? 2221 HOH F O   1 
HETATM 2928 O  O   . HOH S 5 .   ? 12.374 23.788  8.553   0.50  17.20 ? 2222 HOH F O   1 
HETATM 2929 O  O   . HOH S 5 .   ? 17.123 30.981  11.237  1.00  16.50 ? 2223 HOH F O   1 
HETATM 2930 O  O   . HOH S 5 .   ? 14.514 22.891  12.445  1.00  29.25 ? 2224 HOH F O   1 
HETATM 2931 O  O   . HOH S 5 .   ? 14.730 30.064  10.648  1.00  29.63 ? 2225 HOH F O   1 
HETATM 2932 O  O   . HOH S 5 .   ? 25.427 28.744  13.719  1.00  43.12 ? 2226 HOH F O   1 
HETATM 2933 O  O   . HOH S 5 .   ? 23.829 29.101  18.186  1.00  27.24 ? 2227 HOH F O   1 
HETATM 2934 O  O   . HOH S 5 .   ? 21.733 19.587  13.514  1.00  17.68 ? 2228 HOH F O   1 
HETATM 2935 O  O   . HOH S 5 .   ? 17.133 20.237  7.485   1.00  12.97 ? 2229 HOH F O   1 
HETATM 2936 O  O   . HOH S 5 .   ? 13.464 22.938  8.241   0.50  11.51 ? 2230 HOH F O   1 
HETATM 2937 O  O   . HOH S 5 .   ? 13.027 19.491  10.193  1.00  20.97 ? 2231 HOH F O   1 
HETATM 2938 O  O   . HOH S 5 .   ? 7.980  10.479  9.222   1.00  27.71 ? 2232 HOH F O   1 
HETATM 2939 O  O   . HOH S 5 .   ? 6.410  11.272  4.891   1.00  23.15 ? 2233 HOH F O   1 
HETATM 2940 O  O   . HOH S 5 .   ? 11.372 3.310   9.730   1.00  21.78 ? 2234 HOH F O   1 
HETATM 2941 O  O   . HOH S 5 .   ? 14.803 0.986   11.196  1.00  15.42 ? 2235 HOH F O   1 
HETATM 2942 O  O   . HOH S 5 .   ? 16.722 -0.167  8.565   1.00  8.66  ? 2236 HOH F O   1 
HETATM 2943 O  O   . HOH S 5 .   ? 28.569 -8.601  8.691   1.00  19.32 ? 2237 HOH F O   1 
HETATM 2944 O  O   . HOH S 5 .   ? 29.651 -5.960  6.941   1.00  20.13 ? 2238 HOH F O   1 
HETATM 2945 O  O   . HOH S 5 .   ? 28.000 -11.548 1.062   1.00  37.83 ? 2239 HOH F O   1 
HETATM 2946 O  O   . HOH S 5 .   ? 29.285 -10.899 7.067   1.00  22.52 ? 2240 HOH F O   1 
HETATM 2947 O  O   . HOH S 5 .   ? 25.304 -7.599  2.420   1.00  25.93 ? 2241 HOH F O   1 
HETATM 2948 O  O   . HOH S 5 .   ? 26.509 -15.364 1.956   1.00  28.74 ? 2242 HOH F O   1 
HETATM 2949 O  O   . HOH S 5 .   ? 22.733 -8.244  5.166   1.00  21.52 ? 2243 HOH F O   1 
HETATM 2950 O  O   . HOH S 5 .   ? 30.583 -7.770  5.494   1.00  36.42 ? 2244 HOH F O   1 
HETATM 2951 O  O   . HOH S 5 .   ? 22.530 -11.047 4.131   1.00  24.28 ? 2245 HOH F O   1 
HETATM 2952 O  O   . HOH S 5 .   ? 28.251 -13.711 1.529   1.00  32.38 ? 2246 HOH F O   1 
HETATM 2953 O  O   . HOH S 5 .   ? 27.042 -9.482  0.966   1.00  30.48 ? 2247 HOH F O   1 
HETATM 2954 O  O   . HOH S 5 .   ? 19.494 18.906  13.715  1.00  26.00 ? 2248 HOH F O   1 
HETATM 2955 O  O   . HOH S 5 .   ? 17.567 18.845  14.643  1.00  25.75 ? 2249 HOH F O   1 
HETATM 2956 O  O   . HOH S 5 .   ? 14.407 17.926  11.974  0.50  7.66  ? 2250 HOH F O   1 
HETATM 2957 O  O   . HOH S 5 .   ? 15.174 22.101  10.001  1.00  23.30 ? 2251 HOH F O   1 
HETATM 2958 O  O   . HOH S 5 .   ? 7.342  17.276  10.755  1.00  43.59 ? 2252 HOH F O   1 
HETATM 2959 O  O   . HOH S 5 .   ? 12.495 17.569  12.150  0.50  18.58 ? 2253 HOH F O   1 
HETATM 2960 O  O   . HOH S 5 .   ? 8.726  18.156  15.341  1.00  31.06 ? 2254 HOH F O   1 
HETATM 2961 O  O   . HOH S 5 .   ? 8.871  12.053  11.980  1.00  33.03 ? 2255 HOH F O   1 
HETATM 2962 O  O   . HOH S 5 .   ? 24.761 15.632  -5.494  1.00  35.34 ? 2256 HOH F O   1 
HETATM 2963 O  O   . HOH S 5 .   ? 22.105 19.424  -3.542  0.50  10.31 ? 2257 HOH F O   1 
HETATM 2964 O  O   . HOH S 5 .   ? 22.349 17.048  -5.180  1.00  29.83 ? 2258 HOH F O   1 
HETATM 2965 O  O   . HOH S 5 .   ? 26.944 18.297  -2.936  1.00  30.46 ? 2259 HOH F O   1 
HETATM 2966 O  O   . HOH S 5 .   ? 6.766  14.570  9.543   0.30  13.99 ? 2260 HOH F 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 CSO 111 111 111 CSO CSO 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 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER 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   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  CYS 57  57  57  CYS CYS F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  GLY 93  93  93  GLY GLY F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CSO 111 111 111 CSO CSO F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 ILE 113 113 113 ILE ILE F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 CYS 146 146 146 CYS CYS F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 GLN 153 153 153 GLN GLN F . 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   1155 1155 ZN  ZN  A . 
D 2 ZN  1   1156 1156 ZN  ZN  A . 
E 2 ZN  1   1157 1157 ZN  ZN  A . 
F 3 ACT 1   1158 1158 ACT ACT A . 
G 3 ACT 1   1159 1159 ACT ACT A . 
H 4 SO4 1   1160 1160 SO4 SO4 A . 
I 4 SO4 1   1161 1161 SO4 SO4 A . 
J 4 SO4 1   1162 1162 SO4 SO4 A . 
K 4 SO4 1   1163 1163 SO4 SO4 A . 
L 4 SO4 1   1154 1154 SO4 SO4 F . 
M 4 SO4 1   1155 1155 SO4 SO4 F . 
N 2 ZN  1   1157 1157 ZN  ZN  F . 
O 2 ZN  1   1158 1158 ZN  ZN  F . 
P 3 ACT 1   1159 1159 ACT ACT F . 
Q 2 ZN  1   1160 1160 ZN  ZN  F . 
R 5 HOH 1   2001 2001 HOH HOH A . 
R 5 HOH 2   2002 2002 HOH HOH A . 
R 5 HOH 3   2003 2003 HOH HOH A . 
R 5 HOH 4   2004 2004 HOH HOH A . 
R 5 HOH 5   2005 2005 HOH HOH A . 
R 5 HOH 6   2006 2006 HOH HOH A . 
R 5 HOH 7   2007 2007 HOH HOH A . 
R 5 HOH 8   2008 2008 HOH HOH A . 
R 5 HOH 9   2009 2009 HOH HOH A . 
R 5 HOH 10  2010 2010 HOH HOH A . 
R 5 HOH 11  2011 2011 HOH HOH A . 
R 5 HOH 12  2012 2012 HOH HOH A . 
R 5 HOH 13  2013 2013 HOH HOH A . 
R 5 HOH 14  2014 2014 HOH HOH A . 
R 5 HOH 15  2015 2015 HOH HOH A . 
R 5 HOH 16  2016 2016 HOH HOH A . 
R 5 HOH 17  2017 2017 HOH HOH A . 
R 5 HOH 18  2018 2018 HOH HOH A . 
R 5 HOH 19  2019 2019 HOH HOH A . 
R 5 HOH 20  2020 2020 HOH HOH A . 
R 5 HOH 21  2021 2021 HOH HOH A . 
R 5 HOH 22  2022 2022 HOH HOH A . 
R 5 HOH 23  2023 2023 HOH HOH A . 
R 5 HOH 24  2024 2024 HOH HOH A . 
R 5 HOH 25  2025 2025 HOH HOH A . 
R 5 HOH 26  2026 2026 HOH HOH A . 
R 5 HOH 27  2027 2027 HOH HOH A . 
R 5 HOH 28  2028 2028 HOH HOH A . 
R 5 HOH 29  2029 2029 HOH HOH A . 
R 5 HOH 30  2030 2030 HOH HOH A . 
R 5 HOH 31  2031 2031 HOH HOH A . 
R 5 HOH 32  2032 2032 HOH HOH A . 
R 5 HOH 33  2033 2033 HOH HOH A . 
R 5 HOH 34  2034 2034 HOH HOH A . 
R 5 HOH 35  2035 2035 HOH HOH A . 
R 5 HOH 36  2036 2036 HOH HOH A . 
R 5 HOH 37  2037 2037 HOH HOH A . 
R 5 HOH 38  2038 2038 HOH HOH A . 
R 5 HOH 39  2039 2039 HOH HOH A . 
R 5 HOH 40  2040 2040 HOH HOH A . 
R 5 HOH 41  2041 2041 HOH HOH A . 
R 5 HOH 42  2042 2042 HOH HOH A . 
R 5 HOH 43  2043 2043 HOH HOH A . 
R 5 HOH 44  2044 2044 HOH HOH A . 
R 5 HOH 45  2045 2045 HOH HOH A . 
R 5 HOH 46  2046 2046 HOH HOH A . 
R 5 HOH 47  2047 2047 HOH HOH A . 
R 5 HOH 48  2048 2048 HOH HOH A . 
R 5 HOH 49  2049 2049 HOH HOH A . 
R 5 HOH 50  2050 2050 HOH HOH A . 
R 5 HOH 51  2051 2051 HOH HOH A . 
R 5 HOH 52  2052 2052 HOH HOH A . 
R 5 HOH 53  2053 2053 HOH HOH A . 
R 5 HOH 54  2054 2054 HOH HOH A . 
R 5 HOH 55  2055 2055 HOH HOH A . 
R 5 HOH 56  2056 2056 HOH HOH A . 
R 5 HOH 57  2057 2057 HOH HOH A . 
R 5 HOH 58  2058 2058 HOH HOH A . 
R 5 HOH 59  2059 2059 HOH HOH A . 
R 5 HOH 60  2060 2060 HOH HOH A . 
R 5 HOH 61  2061 2061 HOH HOH A . 
R 5 HOH 62  2062 2062 HOH HOH A . 
R 5 HOH 63  2063 2063 HOH HOH A . 
R 5 HOH 64  2064 2064 HOH HOH A . 
R 5 HOH 65  2065 2065 HOH HOH A . 
R 5 HOH 66  2066 2066 HOH HOH A . 
R 5 HOH 67  2067 2067 HOH HOH A . 
R 5 HOH 68  2068 2068 HOH HOH A . 
R 5 HOH 69  2069 2069 HOH HOH A . 
R 5 HOH 70  2070 2070 HOH HOH A . 
R 5 HOH 71  2071 2071 HOH HOH A . 
R 5 HOH 72  2072 2072 HOH HOH A . 
R 5 HOH 73  2073 2073 HOH HOH A . 
R 5 HOH 74  2074 2074 HOH HOH A . 
R 5 HOH 75  2075 2075 HOH HOH A . 
R 5 HOH 76  2076 2076 HOH HOH A . 
R 5 HOH 77  2077 2077 HOH HOH A . 
R 5 HOH 78  2078 2078 HOH HOH A . 
R 5 HOH 79  2079 2079 HOH HOH A . 
R 5 HOH 80  2080 2080 HOH HOH A . 
R 5 HOH 81  2081 2081 HOH HOH A . 
R 5 HOH 82  2082 2082 HOH HOH A . 
R 5 HOH 83  2083 2083 HOH HOH A . 
R 5 HOH 84  2084 2084 HOH HOH A . 
R 5 HOH 85  2085 2085 HOH HOH A . 
R 5 HOH 86  2086 2086 HOH HOH A . 
R 5 HOH 87  2087 2087 HOH HOH A . 
R 5 HOH 88  2088 2088 HOH HOH A . 
R 5 HOH 89  2089 2089 HOH HOH A . 
R 5 HOH 90  2090 2090 HOH HOH A . 
R 5 HOH 91  2091 2091 HOH HOH A . 
R 5 HOH 92  2092 2092 HOH HOH A . 
R 5 HOH 93  2093 2093 HOH HOH A . 
R 5 HOH 94  2094 2094 HOH HOH A . 
R 5 HOH 95  2095 2095 HOH HOH A . 
R 5 HOH 96  2096 2096 HOH HOH A . 
R 5 HOH 97  2097 2097 HOH HOH A . 
R 5 HOH 98  2098 2098 HOH HOH A . 
R 5 HOH 99  2099 2099 HOH HOH A . 
R 5 HOH 100 2100 2100 HOH HOH A . 
R 5 HOH 101 2101 2101 HOH HOH A . 
R 5 HOH 102 2102 2102 HOH HOH A . 
R 5 HOH 103 2103 2103 HOH HOH A . 
R 5 HOH 104 2104 2104 HOH HOH A . 
R 5 HOH 105 2105 2105 HOH HOH A . 
R 5 HOH 106 2106 2106 HOH HOH A . 
R 5 HOH 107 2107 2107 HOH HOH A . 
R 5 HOH 108 2108 2108 HOH HOH A . 
R 5 HOH 109 2109 2109 HOH HOH A . 
R 5 HOH 110 2110 2110 HOH HOH A . 
R 5 HOH 111 2111 2111 HOH HOH A . 
R 5 HOH 112 2112 2112 HOH HOH A . 
R 5 HOH 113 2113 2113 HOH HOH A . 
R 5 HOH 114 2114 2114 HOH HOH A . 
R 5 HOH 115 2115 2115 HOH HOH A . 
R 5 HOH 116 2116 2116 HOH HOH A . 
R 5 HOH 117 2117 2117 HOH HOH A . 
R 5 HOH 118 2118 2118 HOH HOH A . 
R 5 HOH 119 2119 2119 HOH HOH A . 
R 5 HOH 120 2120 2120 HOH HOH A . 
R 5 HOH 121 2121 2121 HOH HOH A . 
R 5 HOH 122 2122 2122 HOH HOH A . 
R 5 HOH 123 2123 2123 HOH HOH A . 
R 5 HOH 124 2124 2124 HOH HOH A . 
R 5 HOH 125 2125 2125 HOH HOH A . 
R 5 HOH 126 2126 2126 HOH HOH A . 
R 5 HOH 127 2127 2127 HOH HOH A . 
R 5 HOH 128 2128 2128 HOH HOH A . 
R 5 HOH 129 2129 2129 HOH HOH A . 
R 5 HOH 130 2130 2130 HOH HOH A . 
R 5 HOH 131 2131 2131 HOH HOH A . 
R 5 HOH 132 2132 2132 HOH HOH A . 
R 5 HOH 133 2133 2133 HOH HOH A . 
R 5 HOH 134 2134 2134 HOH HOH A . 
R 5 HOH 135 2135 2135 HOH HOH A . 
R 5 HOH 136 2136 2136 HOH HOH A . 
R 5 HOH 137 2137 2137 HOH HOH A . 
R 5 HOH 138 2138 2138 HOH HOH A . 
R 5 HOH 139 2139 2139 HOH HOH A . 
R 5 HOH 140 2140 2140 HOH HOH A . 
R 5 HOH 141 2141 2141 HOH HOH A . 
R 5 HOH 142 2142 2142 HOH HOH A . 
R 5 HOH 143 2143 2143 HOH HOH A . 
R 5 HOH 144 2144 2144 HOH HOH A . 
R 5 HOH 145 2145 2145 HOH HOH A . 
R 5 HOH 146 2146 2146 HOH HOH A . 
R 5 HOH 147 2147 2147 HOH HOH A . 
R 5 HOH 148 2148 2148 HOH HOH A . 
R 5 HOH 149 2149 2149 HOH HOH A . 
R 5 HOH 150 2150 2150 HOH HOH A . 
R 5 HOH 151 2151 2151 HOH HOH A . 
R 5 HOH 152 2152 2152 HOH HOH A . 
R 5 HOH 153 2153 2153 HOH HOH A . 
R 5 HOH 154 2154 2154 HOH HOH A . 
R 5 HOH 155 2155 2155 HOH HOH A . 
R 5 HOH 156 2156 2156 HOH HOH A . 
R 5 HOH 157 2157 2157 HOH HOH A . 
R 5 HOH 158 2158 2158 HOH HOH A . 
R 5 HOH 159 2159 2159 HOH HOH A . 
R 5 HOH 160 2160 2160 HOH HOH A . 
R 5 HOH 161 2161 2161 HOH HOH A . 
R 5 HOH 162 2162 2162 HOH HOH A . 
R 5 HOH 163 2163 2163 HOH HOH A . 
R 5 HOH 164 2164 2164 HOH HOH A . 
R 5 HOH 165 2165 2165 HOH HOH A . 
R 5 HOH 166 2166 2166 HOH HOH A . 
R 5 HOH 167 2167 2167 HOH HOH A . 
R 5 HOH 168 2168 2168 HOH HOH A . 
R 5 HOH 169 2169 2169 HOH HOH A . 
R 5 HOH 170 2170 2170 HOH HOH A . 
R 5 HOH 171 2171 2171 HOH HOH A . 
R 5 HOH 172 2172 2172 HOH HOH A . 
R 5 HOH 173 2173 2173 HOH HOH A . 
R 5 HOH 174 2174 2174 HOH HOH A . 
R 5 HOH 175 2175 2175 HOH HOH A . 
R 5 HOH 176 2176 2176 HOH HOH A . 
R 5 HOH 177 2177 2177 HOH HOH A . 
R 5 HOH 178 2178 2178 HOH HOH A . 
R 5 HOH 179 2179 2179 HOH HOH A . 
R 5 HOH 180 2180 2180 HOH HOH A . 
R 5 HOH 181 2181 2181 HOH HOH A . 
R 5 HOH 182 2182 2182 HOH HOH A . 
R 5 HOH 183 2183 2183 HOH HOH A . 
R 5 HOH 184 2184 2184 HOH HOH A . 
R 5 HOH 185 2185 2185 HOH HOH A . 
R 5 HOH 186 2186 2186 HOH HOH A . 
R 5 HOH 187 2187 2187 HOH HOH A . 
R 5 HOH 188 2188 2188 HOH HOH A . 
R 5 HOH 189 2189 2189 HOH HOH A . 
R 5 HOH 190 2190 2190 HOH HOH A . 
R 5 HOH 191 2191 2191 HOH HOH A . 
R 5 HOH 192 2192 2192 HOH HOH A . 
R 5 HOH 193 2193 2193 HOH HOH A . 
R 5 HOH 194 2194 2194 HOH HOH A . 
R 5 HOH 195 2195 2195 HOH HOH A . 
R 5 HOH 196 2196 2196 HOH HOH A . 
R 5 HOH 197 2197 2197 HOH HOH A . 
R 5 HOH 198 2198 2198 HOH HOH A . 
R 5 HOH 199 2199 2199 HOH HOH A . 
R 5 HOH 200 2200 2200 HOH HOH A . 
R 5 HOH 201 2201 2201 HOH HOH A . 
R 5 HOH 202 2202 2202 HOH HOH A . 
R 5 HOH 203 2203 2203 HOH HOH A . 
R 5 HOH 204 2204 2204 HOH HOH A . 
R 5 HOH 205 2205 2205 HOH HOH A . 
R 5 HOH 206 2206 2206 HOH HOH A . 
R 5 HOH 207 2207 2207 HOH HOH A . 
R 5 HOH 208 2208 2208 HOH HOH A . 
R 5 HOH 209 2209 2209 HOH HOH A . 
R 5 HOH 210 2210 2210 HOH HOH A . 
R 5 HOH 211 2211 2211 HOH HOH A . 
R 5 HOH 212 2212 2212 HOH HOH A . 
R 5 HOH 213 2213 2213 HOH HOH A . 
R 5 HOH 214 2214 2214 HOH HOH A . 
R 5 HOH 215 2215 2215 HOH HOH A . 
R 5 HOH 216 2216 2216 HOH HOH A . 
R 5 HOH 217 2217 2217 HOH HOH A . 
R 5 HOH 218 2218 2218 HOH HOH A . 
R 5 HOH 219 2219 2219 HOH HOH A . 
R 5 HOH 220 2220 2220 HOH HOH A . 
R 5 HOH 221 2221 2221 HOH HOH A . 
R 5 HOH 222 2222 2222 HOH HOH A . 
R 5 HOH 223 2223 2223 HOH HOH A . 
R 5 HOH 224 2224 2224 HOH HOH A . 
R 5 HOH 225 2225 2225 HOH HOH A . 
R 5 HOH 226 2226 2226 HOH HOH A . 
R 5 HOH 227 2227 2227 HOH HOH A . 
R 5 HOH 228 2228 2228 HOH HOH A . 
R 5 HOH 229 2229 2229 HOH HOH A . 
R 5 HOH 230 2230 2230 HOH HOH A . 
R 5 HOH 231 2231 2231 HOH HOH A . 
R 5 HOH 232 2232 2232 HOH HOH A . 
R 5 HOH 233 2233 2233 HOH HOH A . 
R 5 HOH 234 2234 2234 HOH HOH A . 
R 5 HOH 235 2235 2235 HOH HOH A . 
R 5 HOH 236 2236 2236 HOH HOH A . 
R 5 HOH 237 2237 2237 HOH HOH A . 
R 5 HOH 238 2238 2238 HOH HOH A . 
R 5 HOH 239 2239 2239 HOH HOH A . 
R 5 HOH 240 2240 2240 HOH HOH A . 
R 5 HOH 241 2241 2241 HOH HOH A . 
R 5 HOH 242 2242 2242 HOH HOH A . 
R 5 HOH 243 2243 2243 HOH HOH A . 
R 5 HOH 244 2244 2244 HOH HOH A . 
R 5 HOH 245 2245 2245 HOH HOH A . 
R 5 HOH 246 2246 2246 HOH HOH A . 
R 5 HOH 247 2247 2247 HOH HOH A . 
S 5 HOH 1   2001 2001 HOH HOH F . 
S 5 HOH 2   2002 2002 HOH HOH F . 
S 5 HOH 3   2003 2003 HOH HOH F . 
S 5 HOH 4   2004 2004 HOH HOH F . 
S 5 HOH 5   2005 2005 HOH HOH F . 
S 5 HOH 6   2006 2006 HOH HOH F . 
S 5 HOH 7   2007 2007 HOH HOH F . 
S 5 HOH 8   2008 2008 HOH HOH F . 
S 5 HOH 9   2009 2009 HOH HOH F . 
S 5 HOH 10  2010 2010 HOH HOH F . 
S 5 HOH 11  2011 2011 HOH HOH F . 
S 5 HOH 12  2012 2012 HOH HOH F . 
S 5 HOH 13  2013 2013 HOH HOH F . 
S 5 HOH 14  2014 2014 HOH HOH F . 
S 5 HOH 15  2015 2015 HOH HOH F . 
S 5 HOH 16  2016 2016 HOH HOH F . 
S 5 HOH 17  2017 2017 HOH HOH F . 
S 5 HOH 18  2018 2018 HOH HOH F . 
S 5 HOH 19  2019 2019 HOH HOH F . 
S 5 HOH 20  2020 2020 HOH HOH F . 
S 5 HOH 21  2021 2021 HOH HOH F . 
S 5 HOH 22  2022 2022 HOH HOH F . 
S 5 HOH 23  2023 2023 HOH HOH F . 
S 5 HOH 24  2024 2024 HOH HOH F . 
S 5 HOH 25  2025 2025 HOH HOH F . 
S 5 HOH 26  2026 2026 HOH HOH F . 
S 5 HOH 27  2027 2027 HOH HOH F . 
S 5 HOH 28  2028 2028 HOH HOH F . 
S 5 HOH 29  2029 2029 HOH HOH F . 
S 5 HOH 30  2030 2030 HOH HOH F . 
S 5 HOH 31  2031 2031 HOH HOH F . 
S 5 HOH 32  2032 2032 HOH HOH F . 
S 5 HOH 33  2033 2033 HOH HOH F . 
S 5 HOH 34  2034 2034 HOH HOH F . 
S 5 HOH 35  2035 2035 HOH HOH F . 
S 5 HOH 36  2036 2036 HOH HOH F . 
S 5 HOH 37  2037 2037 HOH HOH F . 
S 5 HOH 38  2038 2038 HOH HOH F . 
S 5 HOH 39  2039 2039 HOH HOH F . 
S 5 HOH 40  2040 2040 HOH HOH F . 
S 5 HOH 41  2041 2041 HOH HOH F . 
S 5 HOH 42  2042 2042 HOH HOH F . 
S 5 HOH 43  2043 2043 HOH HOH F . 
S 5 HOH 44  2044 2044 HOH HOH F . 
S 5 HOH 45  2045 2045 HOH HOH F . 
S 5 HOH 46  2046 2046 HOH HOH F . 
S 5 HOH 47  2047 2047 HOH HOH F . 
S 5 HOH 48  2048 2048 HOH HOH F . 
S 5 HOH 49  2049 2049 HOH HOH F . 
S 5 HOH 50  2050 2050 HOH HOH F . 
S 5 HOH 51  2051 2051 HOH HOH F . 
S 5 HOH 52  2052 2052 HOH HOH F . 
S 5 HOH 53  2053 2053 HOH HOH F . 
S 5 HOH 54  2054 2054 HOH HOH F . 
S 5 HOH 55  2055 2055 HOH HOH F . 
S 5 HOH 56  2056 2056 HOH HOH F . 
S 5 HOH 57  2057 2057 HOH HOH F . 
S 5 HOH 58  2058 2058 HOH HOH F . 
S 5 HOH 59  2059 2059 HOH HOH F . 
S 5 HOH 60  2060 2060 HOH HOH F . 
S 5 HOH 61  2061 2061 HOH HOH F . 
S 5 HOH 62  2062 2062 HOH HOH F . 
S 5 HOH 63  2063 2063 HOH HOH F . 
S 5 HOH 64  2064 2064 HOH HOH F . 
S 5 HOH 65  2065 2065 HOH HOH F . 
S 5 HOH 66  2066 2066 HOH HOH F . 
S 5 HOH 67  2067 2067 HOH HOH F . 
S 5 HOH 68  2068 2068 HOH HOH F . 
S 5 HOH 69  2069 2069 HOH HOH F . 
S 5 HOH 70  2070 2070 HOH HOH F . 
S 5 HOH 71  2071 2071 HOH HOH F . 
S 5 HOH 72  2072 2072 HOH HOH F . 
S 5 HOH 73  2073 2073 HOH HOH F . 
S 5 HOH 74  2074 2074 HOH HOH F . 
S 5 HOH 75  2075 2075 HOH HOH F . 
S 5 HOH 76  2076 2076 HOH HOH F . 
S 5 HOH 77  2077 2077 HOH HOH F . 
S 5 HOH 78  2078 2078 HOH HOH F . 
S 5 HOH 79  2079 2079 HOH HOH F . 
S 5 HOH 80  2080 2080 HOH HOH F . 
S 5 HOH 81  2081 2081 HOH HOH F . 
S 5 HOH 82  2082 2082 HOH HOH F . 
S 5 HOH 83  2083 2083 HOH HOH F . 
S 5 HOH 84  2084 2084 HOH HOH F . 
S 5 HOH 85  2085 2085 HOH HOH F . 
S 5 HOH 86  2086 2086 HOH HOH F . 
S 5 HOH 87  2087 2087 HOH HOH F . 
S 5 HOH 88  2088 2088 HOH HOH F . 
S 5 HOH 89  2089 2089 HOH HOH F . 
S 5 HOH 90  2090 2090 HOH HOH F . 
S 5 HOH 91  2091 2091 HOH HOH F . 
S 5 HOH 92  2092 2092 HOH HOH F . 
S 5 HOH 93  2093 2093 HOH HOH F . 
S 5 HOH 94  2094 2094 HOH HOH F . 
S 5 HOH 95  2095 2095 HOH HOH F . 
S 5 HOH 96  2096 2096 HOH HOH F . 
S 5 HOH 97  2097 2097 HOH HOH F . 
S 5 HOH 98  2098 2098 HOH HOH F . 
S 5 HOH 99  2099 2099 HOH HOH F . 
S 5 HOH 100 2100 2100 HOH HOH F . 
S 5 HOH 101 2101 2101 HOH HOH F . 
S 5 HOH 102 2102 2102 HOH HOH F . 
S 5 HOH 103 2103 2103 HOH HOH F . 
S 5 HOH 104 2104 2104 HOH HOH F . 
S 5 HOH 105 2105 2105 HOH HOH F . 
S 5 HOH 106 2106 2106 HOH HOH F . 
S 5 HOH 107 2107 2107 HOH HOH F . 
S 5 HOH 108 2108 2108 HOH HOH F . 
S 5 HOH 109 2109 2109 HOH HOH F . 
S 5 HOH 110 2110 2110 HOH HOH F . 
S 5 HOH 111 2111 2111 HOH HOH F . 
S 5 HOH 112 2112 2112 HOH HOH F . 
S 5 HOH 113 2113 2113 HOH HOH F . 
S 5 HOH 114 2114 2114 HOH HOH F . 
S 5 HOH 115 2115 2115 HOH HOH F . 
S 5 HOH 116 2116 2116 HOH HOH F . 
S 5 HOH 117 2117 2117 HOH HOH F . 
S 5 HOH 118 2118 2118 HOH HOH F . 
S 5 HOH 119 2119 2119 HOH HOH F . 
S 5 HOH 120 2120 2120 HOH HOH F . 
S 5 HOH 121 2121 2121 HOH HOH F . 
S 5 HOH 122 2122 2122 HOH HOH F . 
S 5 HOH 123 2123 2123 HOH HOH F . 
S 5 HOH 124 2124 2124 HOH HOH F . 
S 5 HOH 125 2125 2125 HOH HOH F . 
S 5 HOH 126 2126 2126 HOH HOH F . 
S 5 HOH 127 2127 2127 HOH HOH F . 
S 5 HOH 128 2128 2128 HOH HOH F . 
S 5 HOH 129 2129 2129 HOH HOH F . 
S 5 HOH 130 2130 2130 HOH HOH F . 
S 5 HOH 131 2131 2131 HOH HOH F . 
S 5 HOH 132 2132 2132 HOH HOH F . 
S 5 HOH 133 2133 2133 HOH HOH F . 
S 5 HOH 134 2134 2134 HOH HOH F . 
S 5 HOH 135 2135 2135 HOH HOH F . 
S 5 HOH 136 2136 2136 HOH HOH F . 
S 5 HOH 137 2137 2137 HOH HOH F . 
S 5 HOH 138 2138 2138 HOH HOH F . 
S 5 HOH 139 2139 2139 HOH HOH F . 
S 5 HOH 140 2140 2140 HOH HOH F . 
S 5 HOH 141 2141 2141 HOH HOH F . 
S 5 HOH 142 2142 2142 HOH HOH F . 
S 5 HOH 143 2143 2143 HOH HOH F . 
S 5 HOH 144 2144 2144 HOH HOH F . 
S 5 HOH 145 2145 2145 HOH HOH F . 
S 5 HOH 146 2146 2146 HOH HOH F . 
S 5 HOH 147 2147 2147 HOH HOH F . 
S 5 HOH 148 2148 2148 HOH HOH F . 
S 5 HOH 149 2149 2149 HOH HOH F . 
S 5 HOH 150 2150 2150 HOH HOH F . 
S 5 HOH 151 2151 2151 HOH HOH F . 
S 5 HOH 152 2152 2152 HOH HOH F . 
S 5 HOH 153 2153 2153 HOH HOH F . 
S 5 HOH 154 2154 2154 HOH HOH F . 
S 5 HOH 155 2155 2155 HOH HOH F . 
S 5 HOH 156 2156 2156 HOH HOH F . 
S 5 HOH 157 2157 2157 HOH HOH F . 
S 5 HOH 158 2158 2158 HOH HOH F . 
S 5 HOH 159 2159 2159 HOH HOH F . 
S 5 HOH 160 2160 2160 HOH HOH F . 
S 5 HOH 161 2161 2161 HOH HOH F . 
S 5 HOH 162 2162 2162 HOH HOH F . 
S 5 HOH 163 2163 2163 HOH HOH F . 
S 5 HOH 164 2164 2164 HOH HOH F . 
S 5 HOH 165 2165 2165 HOH HOH F . 
S 5 HOH 166 2166 2166 HOH HOH F . 
S 5 HOH 167 2167 2167 HOH HOH F . 
S 5 HOH 168 2168 2168 HOH HOH F . 
S 5 HOH 169 2169 2169 HOH HOH F . 
S 5 HOH 170 2170 2170 HOH HOH F . 
S 5 HOH 171 2171 2171 HOH HOH F . 
S 5 HOH 172 2172 2172 HOH HOH F . 
S 5 HOH 173 2173 2173 HOH HOH F . 
S 5 HOH 174 2174 2174 HOH HOH F . 
S 5 HOH 175 2175 2175 HOH HOH F . 
S 5 HOH 176 2176 2176 HOH HOH F . 
S 5 HOH 177 2177 2177 HOH HOH F . 
S 5 HOH 178 2178 2178 HOH HOH F . 
S 5 HOH 179 2179 2179 HOH HOH F . 
S 5 HOH 180 2180 2180 HOH HOH F . 
S 5 HOH 181 2181 2181 HOH HOH F . 
S 5 HOH 182 2182 2182 HOH HOH F . 
S 5 HOH 183 2183 2183 HOH HOH F . 
S 5 HOH 184 2184 2184 HOH HOH F . 
S 5 HOH 185 2185 2185 HOH HOH F . 
S 5 HOH 186 2186 2186 HOH HOH F . 
S 5 HOH 187 2187 2187 HOH HOH F . 
S 5 HOH 188 2188 2188 HOH HOH F . 
S 5 HOH 189 2189 2189 HOH HOH F . 
S 5 HOH 190 2190 2190 HOH HOH F . 
S 5 HOH 191 2191 2191 HOH HOH F . 
S 5 HOH 192 2192 2192 HOH HOH F . 
S 5 HOH 193 2193 2193 HOH HOH F . 
S 5 HOH 194 2194 2194 HOH HOH F . 
S 5 HOH 195 2195 2195 HOH HOH F . 
S 5 HOH 196 2196 2196 HOH HOH F . 
S 5 HOH 197 2197 2197 HOH HOH F . 
S 5 HOH 198 2198 2198 HOH HOH F . 
S 5 HOH 199 2199 2199 HOH HOH F . 
S 5 HOH 200 2200 2200 HOH HOH F . 
S 5 HOH 201 2201 2201 HOH HOH F . 
S 5 HOH 202 2202 2202 HOH HOH F . 
S 5 HOH 203 2203 2203 HOH HOH F . 
S 5 HOH 204 2204 2204 HOH HOH F . 
S 5 HOH 205 2205 2205 HOH HOH F . 
S 5 HOH 206 2206 2206 HOH HOH F . 
S 5 HOH 207 2207 2207 HOH HOH F . 
S 5 HOH 208 2208 2208 HOH HOH F . 
S 5 HOH 209 2209 2209 HOH HOH F . 
S 5 HOH 210 2210 2210 HOH HOH F . 
S 5 HOH 211 2211 2211 HOH HOH F . 
S 5 HOH 212 2212 2212 HOH HOH F . 
S 5 HOH 213 2213 2213 HOH HOH F . 
S 5 HOH 214 2214 2214 HOH HOH F . 
S 5 HOH 215 2215 2215 HOH HOH F . 
S 5 HOH 216 2216 2216 HOH HOH F . 
S 5 HOH 217 2217 2217 HOH HOH F . 
S 5 HOH 218 2218 2218 HOH HOH F . 
S 5 HOH 219 2219 2219 HOH HOH F . 
S 5 HOH 220 2220 2220 HOH HOH F . 
S 5 HOH 221 2221 2221 HOH HOH F . 
S 5 HOH 222 2222 2222 HOH HOH F . 
S 5 HOH 223 2223 2223 HOH HOH F . 
S 5 HOH 224 2224 2224 HOH HOH F . 
S 5 HOH 225 2225 2225 HOH HOH F . 
S 5 HOH 226 2226 2226 HOH HOH F . 
S 5 HOH 227 2227 2227 HOH HOH F . 
S 5 HOH 228 2228 2228 HOH HOH F . 
S 5 HOH 229 2229 2229 HOH HOH F . 
S 5 HOH 230 2230 2230 HOH HOH F . 
S 5 HOH 231 2231 2231 HOH HOH F . 
S 5 HOH 232 2232 2232 HOH HOH F . 
S 5 HOH 233 2233 2233 HOH HOH F . 
S 5 HOH 234 2234 2234 HOH HOH F . 
S 5 HOH 235 2235 2235 HOH HOH F . 
S 5 HOH 236 2236 2236 HOH HOH F . 
S 5 HOH 237 2237 2237 HOH HOH F . 
S 5 HOH 238 2238 2238 HOH HOH F . 
S 5 HOH 239 2239 2239 HOH HOH F . 
S 5 HOH 240 2240 2240 HOH HOH F . 
S 5 HOH 241 2241 2241 HOH HOH F . 
S 5 HOH 242 2242 2242 HOH HOH F . 
S 5 HOH 243 2243 2243 HOH HOH F . 
S 5 HOH 244 2244 2244 HOH HOH F . 
S 5 HOH 245 2245 2245 HOH HOH F . 
S 5 HOH 246 2246 2246 HOH HOH F . 
S 5 HOH 247 2247 2247 HOH HOH F . 
S 5 HOH 248 2248 2248 HOH HOH F . 
S 5 HOH 249 2249 2249 HOH HOH F . 
S 5 HOH 250 2250 2250 HOH HOH F . 
S 5 HOH 251 2251 2251 HOH HOH F . 
S 5 HOH 252 2252 2252 HOH HOH F . 
S 5 HOH 253 2253 2253 HOH HOH F . 
S 5 HOH 254 2254 2254 HOH HOH F . 
S 5 HOH 255 2255 2255 HOH HOH F . 
S 5 HOH 256 2256 2256 HOH HOH F . 
S 5 HOH 257 2257 2257 HOH HOH F . 
S 5 HOH 258 2258 2258 HOH HOH F . 
S 5 HOH 259 2259 2259 HOH HOH F . 
S 5 HOH 260 2260 2260 HOH HOH F . 
# 
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 CSO 111 A CSO 111 ? CYS S-HYDROXYCYSTEINE 
2 B CSO 111 F CSO 111 ? CYS S-HYDROXYCYSTEINE 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_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,J,K,L,M,N,O,P,Q,R,S 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 120 ? A HIS 120  ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 O4  ? I SO4 .   ? A SO4 1161 ? 1_555 100.9 ? 
2  NE2 ? A HIS 120 ? A HIS 120  ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 NE2 ? A HIS 48  ? A HIS 48   ? 1_555 127.9 ? 
3  O4  ? I SO4 .   ? A SO4 1161 ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 NE2 ? A HIS 48  ? A HIS 48   ? 1_555 103.5 ? 
4  NE2 ? A HIS 120 ? A HIS 120  ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 100.6 ? 
5  O4  ? I SO4 .   ? A SO4 1161 ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 100.2 ? 
6  NE2 ? A HIS 48  ? A HIS 48   ? 1_555 ZN ? C ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 119.0 ? 
7  ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 105.1 ? 
8  ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 107.2 ? 
9  ND1 ? A HIS 71  ? A HIS 71   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 123.4 ? 
10 ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 108.6 ? 
11 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 97.0  ? 
12 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 ZN ? D ZN . ? A ZN 1156 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 114.5 ? 
13 O   ? R HOH .   ? A HOH 2229 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O4  ? K SO4 .   ? A SO4 1163 ? 1_555 84.0  ? 
14 O   ? R HOH .   ? A HOH 2229 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? R HOH .   ? A HOH 2245 ? 1_555 95.7  ? 
15 O4  ? K SO4 .   ? A SO4 1163 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? R HOH .   ? A HOH 2245 ? 1_555 18.0  ? 
16 O   ? R HOH .   ? A HOH 2229 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 N   ? A ARG 143 ? A ARG 143  ? 1_555 166.4 ? 
17 O4  ? K SO4 .   ? A SO4 1163 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 N   ? A ARG 143 ? A ARG 143  ? 1_555 83.0  ? 
18 O   ? R HOH .   ? A HOH 2245 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 N   ? A ARG 143 ? A ARG 143  ? 1_555 70.7  ? 
19 O   ? R HOH .   ? A HOH 2229 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? A ARG 143 ? A ARG 143  ? 1_555 110.5 ? 
20 O4  ? K SO4 .   ? A SO4 1163 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? A ARG 143 ? A ARG 143  ? 1_555 113.9 ? 
21 O   ? R HOH .   ? A HOH 2245 ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? A ARG 143 ? A ARG 143  ? 1_555 121.8 ? 
22 N   ? A ARG 143 ? A ARG 143  ? 1_555 ZN ? E ZN . ? A ZN 1157 ? 1_555 O   ? A ARG 143 ? A ARG 143  ? 1_555 78.7  ? 
23 O1  ? L SO4 .   ? F SO4 1154 ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 102.5 ? 
24 O1  ? L SO4 .   ? F SO4 1154 ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 104.4 ? 
25 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 127.2 ? 
26 O1  ? L SO4 .   ? F SO4 1154 ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 102.8 ? 
27 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 98.2  ? 
28 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 118.5 ? 
29 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 124.7 ? 
30 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 114.8 ? 
31 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 98.4  ? 
32 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 108.1 ? 
33 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 103.2 ? 
34 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 ZN ? O ZN . ? F ZN 1158 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 105.7 ? 
35 O1  ? M SO4 .   ? F SO4 1155 ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 N   ? B ARG 143 ? F ARG 143  ? 1_555 78.6  ? 
36 O1  ? M SO4 .   ? F SO4 1155 ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 O   ? B ARG 143 ? F ARG 143  ? 1_555 127.7 ? 
37 N   ? B ARG 143 ? F ARG 143  ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 O   ? B ARG 143 ? F ARG 143  ? 1_555 85.4  ? 
38 O1  ? M SO4 .   ? F SO4 1155 ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 O   ? S HOH .   ? F HOH 2260 ? 1_555 90.4  ? 
39 N   ? B ARG 143 ? F ARG 143  ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 O   ? S HOH .   ? F HOH 2260 ? 1_555 166.9 ? 
40 O   ? B ARG 143 ? F ARG 143  ? 1_555 ZN ? Q ZN . ? F ZN 1160 ? 1_555 O   ? S HOH .   ? F HOH 2260 ? 1_555 107.0 ? 
# 
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 2005-12-15 
2 'Structure model' 1 1 2011-05-08 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.2.0005 ? 1 
HKL-2000 'data reduction' .        ? 2 
HKL-2000 'data scaling'   .        ? 3 
MOLREP   phasing          .        ? 4 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY
A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD1 F ASN 26   ? ? O F HOH 2060 ? ? 1.81 
2  1 O   F GLY 12   ? B N F VAL 14   ? ? 1.89 
3  1 O   A HOH 2027 ? ? O A HOH 2028 ? ? 1.89 
4  1 OD2 F ASP 92   ? A O F HOH 2161 ? ? 1.89 
5  1 OE2 F GLU 24   ? ? O F HOH 2051 ? ? 1.93 
6  1 OD2 A ASP 96   ? B O A HOH 2147 ? ? 1.98 
7  1 O   F THR 58   ? A O F HOH 2113 ? ? 2.00 
8  1 ND2 A ASN 53   ? A O A HOH 2093 ? ? 2.07 
9  1 NE2 A GLN 153  ? ? O A HOH 2227 ? ? 2.13 
10 1 O   F HOH 2248 ? ? O F HOH 2249 ? ? 2.14 
11 1 OE2 A GLU 121  ? ? O A HOH 2183 ? ? 2.14 
12 1 O   F HOH 2009 ? ? O F HOH 2024 ? ? 2.15 
13 1 O   F HOH 2016 ? ? O F HOH 2094 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O F GLY 10   ? B 1_555 O F HOH 2060 ? ? 1_455 2.02 
2 1 O A HOH 2071 ? ? 1_555 O F HOH 2117 ? ? 2_646 2.05 
3 1 O A HOH 2028 ? ? 1_555 O A HOH 2198 ? ? 2_656 2.10 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A TRP 32  ? ? CG A TRP 32  ? B 1.383 1.498 -0.115 0.018 N 
2 1 CB A SER 102 ? ? OG A SER 102 ? B 1.337 1.418 -0.081 0.013 N 
3 1 CB F GLN 15  ? A CG F GLN 15  ? A 2.274 1.521 0.753  0.027 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  F GLY 12 ? B N  F PRO 13 ? B CA  F PRO 13 ? B 93.45  119.30 -25.85 1.50 Y 
2 1 C  F GLY 12 ? B N  F PRO 13 ? B CD  F PRO 13 ? B 151.03 128.40 22.63  2.10 Y 
3 1 CA F GLN 15 ? A CB F GLN 15 ? A CG  F GLN 15 ? A 82.32  113.40 -31.08 2.20 N 
4 1 CB F ASP 90 ? A CG F ASP 90 ? A OD1 F ASP 90 ? A 124.55 118.30 6.25   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 ASN A 26 ? B 85.64   -31.98 
2 1 SER A 98 ? B -152.40 87.20  
3 1 PRO F 13 ? A -95.35  56.06  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    12 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    13 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   B 
_pdbx_validate_peptide_omega.omega            -133.73 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2012 ? 6.54 . 
2 1 O ? A HOH 2021 ? 6.70 . 
3 1 O ? F HOH 2031 ? 6.76 . 
4 1 O ? F HOH 2035 ? 6.33 . 
5 1 O ? F HOH 2066 ? 5.85 . 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'    ZN  
3 'ACETATE ION' ACT 
4 'SULFATE ION' SO4 
5 water         HOH 
# 
