data_2C9U
# 
_entry.id   2C9U 
# 
_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   2C9U         
PDBE  EBI-26849    
WWPDB D_1290026849 
# 
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 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)
;
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2C9U 
_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           2C9U 
_cell.length_a           38.638 
_cell.length_b           67.553 
_cell.length_c           52.320 
_cell.angle_alpha        90.00 
_cell.angle_beta         106.48 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2C9U 
_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]' 15827.561 2   1.15.1.1 ? ? ? 
2 non-polymer syn 'SULFATE ION'                  96.063    3   ?        ? ? ? 
3 non-polymer syn 'COPPER (II) ION'              63.546    2   ?        ? ? ? 
4 non-polymer syn 'ZINC ION'                     65.409    4   ?        ? ? ? 
5 non-polymer syn 'ACETATE ION'                  59.044    2   ?        ? ? ? 
6 water       nat water                          18.015    389 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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 CYS 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 2C9U A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 2C9U 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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
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          2C9U 
_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              8.00 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '3.0 M AMMONIUM SULPHATE, 100 MM SODIUM CHLORITE, 50MM SODIUM ACETATE BUFFER, pH 8.00' 
# 
_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   2003-07-10 
_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   1.074 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX10.1' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX10.1 
_diffrn_source.pdbx_wavelength             1.074 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2C9U 
_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                   70045 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.3 
_reflns.pdbx_Rmerge_I_obs            0.06000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.0000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.500 
# 
_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   92.5 
_reflns_shell.Rmerge_I_obs           0.40000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.200 
_reflns_shell.pdbx_redundancy        2.20 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2C9U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     66500 
_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                             50.19 
_refine.ls_d_res_high                            1.24 
_refine.ls_percent_reflns_obs                    95.8 
_refine.ls_R_factor_obs                          0.141 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.139 
_refine.ls_R_factor_R_free                       0.176 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  3501 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_refine.B_iso_mean                               12.39 
_refine.aniso_B[1][1]                            0.43000 
_refine.aniso_B[2][2]                            -0.36000 
_refine.aniso_B[3][3]                            0.06000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.24000 
_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                       0.045 
_refine.pdbx_overall_ESU_R_Free                  0.045 
_refine.overall_SU_ML                            0.025 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.271 
_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        2214 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             389 
_refine_hist.number_atoms_total               2632 
_refine_hist.d_res_high                       1.24 
_refine_hist.d_res_low                        50.19 
# 
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             0.020  0.021  ? 2328 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 2055 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.841  1.951  ? 3138 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            2.495  3.000  ? 4845 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.798  5.000  ? 306  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       39.028 25.644 ? 101  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.843 15.000 ? 397  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       13.630 15.000 ? 9    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.119  0.200  ? 346  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 2641 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 414  'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.253  0.200  ? 474  'X-RAY DIFFRACTION' ? 
r_nbd_other                  0.203  0.200  ? 2074 'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.169  0.200  ? 1121 'X-RAY DIFFRACTION' ? 
r_nbtor_other                0.095  0.200  ? 1335 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.302  0.200  ? 301  '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       0.193  0.200  ? 24   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         0.182  0.200  ? 50   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.297  0.200  ? 47   '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                  2.417  1.500  ? 1916 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.041  2.000  ? 2408 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.718  3.000  ? 898  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.618  4.500  ? 730  '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             3900 
_refine_ls_shell.R_factor_R_work                  0.2980 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.3370 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             203 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  2C9U 
_struct.title                     '1.24 Angstroms resolution structure of as-isolated Cu-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        2C9U 
_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 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 4 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
# 
_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  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 SER A 107 ? HIS A 110 ? SER A 107 HIS A 110 5 ? 4 
HELX_P HELX_P3 3 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P4 4 ALA B 55  ? GLY B 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P5 5 ASN B 131 ? LYS B 136 ? ASN F 131 LYS F 136 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57 SG  ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57   A CYS 146  1_555 ? ? ? ? ? ? ? 2.748 ? 
disulf2  disulf ? ? B CYS 57 SG  A ? ? 1_555 B CYS 146 SG  A ? F CYS 57   F CYS 146  1_555 ? ? ? ? ? ? ? 2.584 ? 
disulf3  disulf ? ? B CYS 57 SG  B ? ? 1_555 B CYS 146 SG  B ? F CYS 57   F CYS 146  1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc1  metalc ? ? C SO4 .  O1  ? ? ? 1_555 G ZN  .   ZN  ? ? A SO4 1154 A ZN  1159 1_555 ? ? ? ? ? ? ? 1.984 ? 
metalc2  metalc ? ? E CU  .  CU  ? ? ? 1_555 A HIS 48  NE2 ? ? A CU  1157 A HIS 48   1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc3  metalc ? ? E CU  .  CU  ? ? ? 1_555 A HIS 120 NE2 ? ? A CU  1157 A HIS 120  1_555 ? ? ? ? ? ? ? 2.230 ? 
metalc4  metalc ? ? E CU  .  CU  ? ? ? 1_555 A HIS 46  ND1 ? ? A CU  1157 A HIS 46   1_555 ? ? ? ? ? ? ? 1.822 ? 
metalc5  metalc ? ? F ZN  .  ZN  ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  1158 A HIS 71   1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc6  metalc ? ? F ZN  .  ZN  ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  1158 A HIS 63   1_555 ? ? ? ? ? ? ? 2.032 ? 
metalc7  metalc ? ? F ZN  .  ZN  ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  1158 A HIS 80   1_555 ? ? ? ? ? ? ? 2.017 ? 
metalc8  metalc ? ? F ZN  .  ZN  ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  1158 A ASP 83   1_555 ? ? ? ? ? ? ? 1.973 ? 
metalc9  metalc ? ? G ZN  .  ZN  ? ? ? 1_555 A HIS 48  NE2 ? ? A ZN  1159 A HIS 48   1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc10 metalc ? ? G ZN  .  ZN  ? ? ? 1_555 A HIS 120 NE2 ? ? A ZN  1159 A HIS 120  1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc11 metalc ? ? G ZN  .  ZN  ? ? ? 1_555 N HOH .   O   ? ? A ZN  1159 A HOH 2193 1_555 ? ? ? ? ? ? ? 2.314 ? 
metalc12 metalc ? ? G ZN  .  ZN  ? ? ? 1_555 A HIS 46  ND1 ? ? A ZN  1159 A HIS 46   1_555 ? ? ? ? ? ? ? 2.220 ? 
covale1  covale ? ? B ASP 11 OD1 ? ? ? 1_555 M ACT .   OXT ? ? F ASP 11   F ACT 1159 1_555 ? ? ? ? ? ? ? 1.647 ? 
covale2  covale ? ? B ASP 11 CG  ? ? ? 1_555 M ACT .   OXT ? ? F ASP 11   F ACT 1159 1_555 ? ? ? ? ? ? ? 1.934 ? 
metalc13 metalc ? ? I ZN  .  ZN  ? ? ? 1_555 B HIS 48  NE2 ? ? F ZN  1155 F HIS 48   1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc14 metalc ? ? I ZN  .  ZN  ? ? ? 1_555 B HIS 46  ND1 ? ? F ZN  1155 F HIS 46   1_555 ? ? ? ? ? ? ? 2.283 ? 
metalc15 metalc ? ? I ZN  .  ZN  ? ? ? 1_555 B HIS 120 NE2 ? ? F ZN  1155 F HIS 120  1_555 ? ? ? ? ? ? ? 1.854 ? 
metalc16 metalc ? ? I ZN  .  ZN  ? ? ? 1_555 H SO4 .   O1  ? ? F ZN  1155 F SO4 1154 1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc17 metalc ? ? I ZN  .  ZN  ? ? ? 1_555 O HOH .   O   ? ? F ZN  1155 F HOH 2190 1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc18 metalc ? ? J CU  .  CU  ? ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120  1_555 ? ? ? ? ? ? ? 1.995 ? 
metalc19 metalc ? ? J CU  .  CU  ? ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46   1_555 ? ? ? ? ? ? ? 1.977 ? 
metalc20 metalc ? ? J CU  .  CU  ? ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48   1_555 ? ? ? ? ? ? ? 2.015 ? 
metalc21 metalc ? ? K ZN  .  ZN  ? ? ? 1_555 B HIS 80  ND1 ? ? F ZN  1157 F HIS 80   1_555 ? ? ? ? ? ? ? 1.988 ? 
metalc22 metalc ? ? K ZN  .  ZN  ? ? ? 1_555 B ASP 83  OD1 ? ? F ZN  1157 F ASP 83   1_555 ? ? ? ? ? ? ? 1.958 ? 
metalc23 metalc ? ? K ZN  .  ZN  ? ? ? 1_555 B HIS 71  ND1 ? ? F ZN  1157 F HIS 71   1_555 ? ? ? ? ? ? ? 2.072 ? 
metalc24 metalc ? ? K ZN  .  ZN  ? ? ? 1_555 B HIS 63  ND1 ? ? F ZN  1157 F HIS 63   1_555 ? ? ? ? ? ? ? 2.056 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           12 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            12 
_struct_mon_prot_cis.auth_asym_id           F 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    13 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     13 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    F 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.50 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
FA ? 5 ? 
FB ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
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 
FB 1 2 ? anti-parallel 
FB 2 3 ? anti-parallel 
FB 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
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  ? GLU A 21  ? GLN A 15  GLU A 21  
AA 4 LYS A 3   ? LYS A 9   ? LYS A 3   LYS A 9   
AA 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
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 ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
FA 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
FA 3 VAL B 14  ? GLN B 22  ? VAL F 14  GLN F 22  
FA 4 THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
FA 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
FB 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
FB 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
FB 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
FB 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 148 
# 
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 PHE A 20  ? N PHE A 20  O ALA A 4   ? O ALA A 4   
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 ASP B 101 ? N ASP F 101 O VAL B 29  ? O VAL F 29  
FA 2 3 N LYS B 36  ? N LYS F 36  O GLN B 15  ? O GLN F 15  
FA 3 4 N GLN B 22  ? N GLN F 22  O THR B 2   ? O THR F 2   
FA 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
FB 1 2 N ALA B 89  ? N ALA F 89  O GLY B 41  ? O GLY F 41  
FB 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
FB 3 4 O VAL B 119 ? O VAL F 119 N LEU B 144 ? N LEU F 144 
# 
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 ? ? ? ? 15 'BINDING SITE FOR RESIDUE SO4 A1154' 
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 A1155' 
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU A1157'  
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A1158'  
AC5 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE ZN A1159'  
AC6 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE SO4 F1154' 
AC7 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE ZN F1155'  
AC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE CU F1156'  
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F1157'  
BC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ACT F1158' 
BC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE ACT F1159' 
# 
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 15 HIS A 46  ? HIS A 46   . ? 1_555 ? 
2  AC1 15 HIS A 48  ? HIS A 48   . ? 1_555 ? 
3  AC1 15 HIS A 63  ? HIS A 63   . ? 1_555 ? 
4  AC1 15 HIS A 120 ? HIS A 120  . ? 1_555 ? 
5  AC1 15 THR A 137 ? THR A 137  . ? 1_555 ? 
6  AC1 15 ARG A 143 ? ARG A 143  . ? 1_555 ? 
7  AC1 15 CU  E .   ? CU  A 1157 . ? 1_555 ? 
8  AC1 15 ZN  G .   ? ZN  A 1159 . ? 1_555 ? 
9  AC1 15 HOH N .   ? HOH A 2177 . ? 1_555 ? 
10 AC1 15 HOH N .   ? HOH A 2178 . ? 1_555 ? 
11 AC1 15 HOH N .   ? HOH A 2191 . ? 1_555 ? 
12 AC1 15 HOH N .   ? HOH A 2192 . ? 1_555 ? 
13 AC1 15 HOH N .   ? HOH A 2193 . ? 1_555 ? 
14 AC1 15 HOH N .   ? HOH A 2194 . ? 1_555 ? 
15 AC1 15 HOH N .   ? HOH A 2196 . ? 1_555 ? 
16 AC2 6  THR A 58  ? THR A 58   . ? 1_555 ? 
17 AC2 6  ARG A 143 ? ARG A 143  . ? 1_555 ? 
18 AC2 6  HOH N .   ? HOH A 2080 . ? 1_555 ? 
19 AC2 6  HOH N .   ? HOH A 2195 . ? 1_555 ? 
20 AC2 6  HOH N .   ? HOH A 2196 . ? 1_555 ? 
21 AC2 6  HOH N .   ? HOH A 2197 . ? 1_555 ? 
22 AC3 5  HIS A 46  ? HIS A 46   . ? 1_555 ? 
23 AC3 5  HIS A 48  ? HIS A 48   . ? 1_555 ? 
24 AC3 5  HIS A 120 ? HIS A 120  . ? 1_555 ? 
25 AC3 5  SO4 C .   ? SO4 A 1154 . ? 1_555 ? 
26 AC3 5  ZN  G .   ? ZN  A 1159 . ? 1_555 ? 
27 AC4 4  HIS A 63  ? HIS A 63   . ? 1_555 ? 
28 AC4 4  HIS A 71  ? HIS A 71   . ? 1_555 ? 
29 AC4 4  HIS A 80  ? HIS A 80   . ? 1_555 ? 
30 AC4 4  ASP A 83  ? ASP A 83   . ? 1_555 ? 
31 AC5 8  HIS A 46  ? HIS A 46   . ? 1_555 ? 
32 AC5 8  HIS A 48  ? HIS A 48   . ? 1_555 ? 
33 AC5 8  HIS A 63  ? HIS A 63   . ? 1_555 ? 
34 AC5 8  HIS A 120 ? HIS A 120  . ? 1_555 ? 
35 AC5 8  SO4 C .   ? SO4 A 1154 . ? 1_555 ? 
36 AC5 8  CU  E .   ? CU  A 1157 . ? 1_555 ? 
37 AC5 8  HOH N .   ? HOH A 2191 . ? 1_555 ? 
38 AC5 8  HOH N .   ? HOH A 2193 . ? 1_555 ? 
39 AC6 16 HIS B 46  ? HIS F 46   . ? 1_555 ? 
40 AC6 16 HIS B 48  ? HIS F 48   . ? 1_555 ? 
41 AC6 16 HIS B 63  ? HIS F 63   . ? 1_555 ? 
42 AC6 16 HIS B 120 ? HIS F 120  . ? 1_555 ? 
43 AC6 16 THR B 137 ? THR F 137  . ? 1_555 ? 
44 AC6 16 ARG B 143 ? ARG F 143  . ? 1_555 ? 
45 AC6 16 ZN  I .   ? ZN  F 1155 . ? 1_555 ? 
46 AC6 16 CU  J .   ? CU  F 1156 . ? 1_555 ? 
47 AC6 16 HOH O .   ? HOH F 2172 . ? 1_555 ? 
48 AC6 16 HOH O .   ? HOH F 2173 . ? 1_555 ? 
49 AC6 16 HOH O .   ? HOH F 2185 . ? 1_555 ? 
50 AC6 16 HOH O .   ? HOH F 2186 . ? 1_555 ? 
51 AC6 16 HOH O .   ? HOH F 2187 . ? 1_555 ? 
52 AC6 16 HOH O .   ? HOH F 2188 . ? 1_555 ? 
53 AC6 16 HOH O .   ? HOH F 2189 . ? 1_555 ? 
54 AC6 16 HOH O .   ? HOH F 2190 . ? 1_555 ? 
55 AC7 8  HIS B 46  ? HIS F 46   . ? 1_555 ? 
56 AC7 8  HIS B 48  ? HIS F 48   . ? 1_555 ? 
57 AC7 8  HIS B 63  ? HIS F 63   . ? 1_555 ? 
58 AC7 8  HIS B 120 ? HIS F 120  . ? 1_555 ? 
59 AC7 8  SO4 H .   ? SO4 F 1154 . ? 1_555 ? 
60 AC7 8  CU  J .   ? CU  F 1156 . ? 1_555 ? 
61 AC7 8  HOH O .   ? HOH F 2189 . ? 1_555 ? 
62 AC7 8  HOH O .   ? HOH F 2190 . ? 1_555 ? 
63 AC8 7  HIS B 46  ? HIS F 46   . ? 1_555 ? 
64 AC8 7  HIS B 48  ? HIS F 48   . ? 1_555 ? 
65 AC8 7  HIS B 63  ? HIS F 63   . ? 1_555 ? 
66 AC8 7  HIS B 120 ? HIS F 120  . ? 1_555 ? 
67 AC8 7  SO4 H .   ? SO4 F 1154 . ? 1_555 ? 
68 AC8 7  ZN  I .   ? ZN  F 1155 . ? 1_555 ? 
69 AC8 7  HOH O .   ? HOH F 2190 . ? 1_555 ? 
70 AC9 4  HIS B 63  ? HIS F 63   . ? 1_555 ? 
71 AC9 4  HIS B 71  ? HIS F 71   . ? 1_555 ? 
72 AC9 4  HIS B 80  ? HIS F 80   . ? 1_555 ? 
73 AC9 4  ASP B 83  ? ASP F 83   . ? 1_555 ? 
74 BC1 6  GLY B 85  ? GLY F 85   . ? 1_555 ? 
75 BC1 6  ASN B 86  ? ASN F 86   . ? 1_555 ? 
76 BC1 6  LEU B 126 ? LEU F 126  . ? 1_555 ? 
77 BC1 6  HOH O .   ? HOH F 2041 . ? 1_555 ? 
78 BC1 6  HOH O .   ? HOH F 2191 . ? 1_555 ? 
79 BC1 6  HOH O .   ? HOH F 2192 . ? 1_555 ? 
80 BC2 3  GLY B 10  ? GLY F 10   . ? 1_555 ? 
81 BC2 3  ASP B 11  ? ASP F 11   . ? 1_555 ? 
82 BC2 3  HOH O .   ? HOH F 2175 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2C9U 
_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                    2C9U 
_atom_sites.fract_transf_matrix[1][1]   0.025881 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007657 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014803 
_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]   0.019932 
_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  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 29.102 2.992   23.447  1.00  30.81 ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 27.840 3.589   24.008  1.00  28.96 ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 27.600 2.971   25.365  1.00  26.43 ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 28.110 1.896   25.645  1.00  28.55 ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 26.666 3.311   23.082  1.00  29.75 ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 26.902 3.672   26.253  1.00  21.91 ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 26.453 3.018   27.415  1.00  17.09 ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 24.995 2.641   27.369  1.00  11.92 ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 24.568 1.865   28.213  1.00  12.40 ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 26.770 3.722   28.778  1.00  18.42 ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 25.958 4.927   28.922  1.00  24.64 ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 28.223 4.144   28.838  1.00  22.46 ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 24.225 3.173   26.416  1.00  10.62 ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 22.797 2.826   26.291  1.00  10.22 ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 22.440 2.535   24.841  1.00  8.83  ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 22.964 3.177   23.926  1.00  9.15  ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 21.882 3.931   26.823  1.00  12.12 ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 22.108 4.215   28.307  0.85  15.24 ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 21.306 5.375   28.781  0.85  16.57 ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 21.536 5.605   30.279  0.85  19.98 ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 20.962 6.915   30.753  0.85  24.35 ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 21.490 1.618   24.670  1.00  7.92  ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 20.981 1.290   23.370  1.00  7.98  ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 19.506 0.995   23.455  1.00  7.52  ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 18.919 0.842   24.525  1.00  7.99  ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 21.755 0.110   22.787  1.00  8.39  ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 18.834 0.966   22.294  1.00  7.34  ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 17.387 0.765   22.227  1.00  7.47  ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 17.034 0.080   20.937  1.00  7.89  ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 17.724 0.199   19.945  1.00  8.97  ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 16.642 2.111   22.402  1.00  9.33  ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 16.868 3.012   21.205  1.00  10.68 ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 15.215 1.932   22.646  1.00  10.86 ? 5    VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 15.944 -0.668  20.990  1.00  7.80  ? 6    CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 15.436 -1.355  19.807  1.00  8.28  ? 6    CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 13.936 -1.301  19.824  1.00  7.89  ? 6    CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 13.276 -1.649  20.792  1.00  9.42  ? 6    CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 15.891 -2.839  19.858  1.00  9.25  ? 6    CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 15.451 -3.797  18.473  1.00  11.17 ? 6    CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 13.380 -0.947  18.668  1.00  7.35  ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 11.939 -0.981  18.431  1.00  8.43  ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 11.662 -2.222  17.606  1.00  9.42  ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 12.139 -2.367  16.453  1.00  9.49  ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 11.474 0.266   17.670  1.00  9.72  ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 9.982  0.202   17.382  1.00  12.62 ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 11.822 1.536   18.425  1.00  13.90 ? 7    VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 10.888 -3.132  18.184  1.00  8.82  ? 8    LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 10.547 -4.377  17.532  1.00  9.68  ? 8    LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 9.248  -4.220  16.791  1.00  9.36  ? 8    LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 8.245  -3.789  17.392  1.00  10.67 ? 8    LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 10.372 -5.500  18.551  1.00  10.82 ? 8    LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 11.596 -5.903  19.376  1.00  11.81 ? 8    LEU A CG  1 
ATOM   53   C  CD1 A LEU A 1 8   ? 11.112 -6.660  20.641  0.70  14.89 ? 8    LEU A CD1 1 
ATOM   54   C  CD1 B LEU A 1 8   ? 11.308 -6.962  20.455  0.30  10.89 ? 8    LEU A CD1 1 
ATOM   55   C  CD2 A LEU A 1 8   ? 12.524 -6.735  18.567  0.70  14.48 ? 8    LEU A CD2 1 
ATOM   56   C  CD2 B LEU A 1 8   ? 12.695 -6.397  18.479  0.30  10.71 ? 8    LEU A CD2 1 
ATOM   57   N  N   . LYS A 1 9   ? 9.248  -4.583  15.500  1.00  9.88  ? 9    LYS A N   1 
ATOM   58   C  CA  . LYS A 1 9   ? 8.070  -4.564  14.663  1.00  11.82 ? 9    LYS A CA  1 
ATOM   59   C  C   . LYS A 1 9   ? 8.100  -5.741  13.721  1.00  11.40 ? 9    LYS A C   1 
ATOM   60   O  O   . LYS A 1 9   ? 9.162  -6.229  13.329  1.00  11.37 ? 9    LYS A O   1 
ATOM   61   C  CB  . LYS A 1 9   ? 7.979  -3.242  13.840  1.00  14.11 ? 9    LYS A CB  1 
ATOM   62   C  CG  . LYS A 1 9   ? 8.224  -1.962  14.597  0.10  11.09 ? 9    LYS A CG  1 
ATOM   63   C  CD  . LYS A 1 9   ? 8.000  -0.730  13.728  0.10  11.62 ? 9    LYS A CD  1 
ATOM   64   C  CE  . LYS A 1 9   ? 6.550  -0.575  13.375  0.10  11.77 ? 9    LYS A CE  1 
ATOM   65   N  NZ  . LYS A 1 9   ? 6.248  0.843   13.089  0.10  11.21 ? 9    LYS A NZ  1 
ATOM   66   N  N   . GLY A 1 10  ? 6.920  -6.164  13.257  1.00  13.15 ? 10   GLY A N   1 
ATOM   67   C  CA  . GLY A 1 10  ? 6.838  -7.210  12.214  1.00  15.26 ? 10   GLY A CA  1 
ATOM   68   C  C   . GLY A 1 10  ? 5.563  -7.092  11.402  1.00  16.81 ? 10   GLY A C   1 
ATOM   69   O  O   . GLY A 1 10  ? 4.955  -6.017  11.370  1.00  20.10 ? 10   GLY A O   1 
ATOM   70   N  N   . ASP A 1 11  ? 5.176  -8.201  10.770  1.00  17.77 ? 11   ASP A N   1 
ATOM   71   C  CA  . ASP A 1 11  ? 4.034  -8.221  9.824   1.00  17.44 ? 11   ASP A CA  1 
ATOM   72   C  C   . ASP A 1 11  ? 2.708  -8.402  10.570  0.30  16.74 ? 11   ASP A C   1 
ATOM   73   O  O   . ASP A 1 11  ? 1.635  -8.156  10.006  0.30  15.33 ? 11   ASP A O   1 
ATOM   74   C  CB  . ASP A 1 11  ? 4.226  -9.338  8.793   0.30  16.33 ? 11   ASP A CB  1 
ATOM   75   C  CG  . ASP A 1 11  ? 5.480  -9.155  7.944   0.25  15.84 ? 11   ASP A CG  1 
ATOM   76   N  N   . GLY A 1 12  ? 2.780  -8.841  11.821  1.00  18.32 ? 12   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 1.615  -9.162  12.633  1.00  18.48 ? 12   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 1.510  -8.225  13.828  1.00  17.46 ? 12   GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 1.976  -7.100  13.774  1.00  18.26 ? 12   GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 0.897  -8.676  14.928  1.00  17.26 ? 13   PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 0.600  -7.834  16.073  1.00  17.06 ? 13   PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 1.753  -7.638  17.051  1.00  16.21 ? 13   PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 1.630  -6.858  18.014  1.00  16.99 ? 13   PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -0.543 -8.617  16.763  1.00  17.68 ? 13   PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -0.228 -10.042 16.454  1.00  17.22 ? 13   PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 0.287  -10.015 15.057  1.00  19.27 ? 13   PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 2.871  -8.318  16.812  1.00  13.65 ? 14   VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 3.951  -8.273  17.804  1.00  12.83 ? 14   VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 4.756  -6.979  17.665  1.00  12.63 ? 14   VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 5.251  -6.658  16.597  1.00  13.64 ? 14   VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 4.854  -9.469  17.708  1.00  11.89 ? 14   VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 5.921  -9.405  18.745  1.00  13.03 ? 14   VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 4.073  -10.745 17.936  1.00  14.98 ? 14   VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 4.829  -6.228  18.751  1.00  11.26 ? 15   GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 5.605  -5.017  18.818  1.00  12.50 ? 15   GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 6.129  -4.731  20.196  1.00  11.71 ? 15   GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 5.513  -5.124  21.193  1.00  12.95 ? 15   GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 4.798  -3.852  18.355  1.00  15.05 ? 15   GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 3.525  -3.684  18.991  1.00  19.35 ? 15   GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 2.739  -2.571  18.292  0.50  19.19 ? 15   GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 3.095  -1.406  18.406  0.50  26.18 ? 15   GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 1.719  -2.938  17.525  0.50  23.73 ? 15   GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 7.260  -4.054  20.272  1.00  10.82 ? 16   GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 7.717  -3.647  21.573  1.00  12.00 ? 16   GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 8.914  -2.764  21.524  1.00  9.70  ? 16   GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 9.370  -2.412  20.460  1.00  10.93 ? 16   GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 9.388  -2.375  22.689  1.00  10.06 ? 17   ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 10.564 -1.516  22.841  1.00  9.84  ? 17   ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 11.441 -2.180  23.897  1.00  9.75  ? 17   ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 10.979 -2.478  25.000  1.00  10.25 ? 17   ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 10.207 -0.101  23.286  1.00  11.10 ? 17   ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 9.357  0.583   22.244  1.00  13.81 ? 17   ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 11.429 0.697   23.619  1.00  12.04 ? 17   ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 8.739  1.939   22.709  1.00  15.69 ? 17   ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 12.687 -2.403  23.531  1.00  8.23  ? 18   ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 13.680 -2.984  24.403  1.00  8.14  ? 18   ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 14.837 -2.051  24.587  1.00  8.59  ? 18   ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 15.394 -1.530  23.649  1.00  9.94  ? 18   ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 14.174 -4.367  23.860  1.00  8.98  ? 18   ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 12.977 -5.360  23.785  1.00  10.39 ? 18   ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 15.259 -4.938  24.791  1.00  9.51  ? 18   ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 12.317 -5.736  25.048  1.00  13.54 ? 18   ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 15.206 -1.822  25.830  1.00  8.11  ? 19   ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 16.318 -0.977  26.235  1.00  9.08  ? 19   ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 17.500 -1.814  26.713  1.00  9.02  ? 19   ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 17.335 -2.861  27.279  1.00  9.38  ? 19   ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 15.864 -0.089  27.427  1.00  10.97 ? 19   ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 14.656 0.675   27.112  1.00  13.52 ? 19   ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 14.748 1.632   26.380  1.00  14.93 ? 19   ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 13.503 0.265   27.600  1.00  16.57 ? 19   ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 18.681 -1.246  26.547  1.00  9.26  ? 20   PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 19.926 -1.829  26.942  1.00  9.60  ? 20   PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 20.755 -0.798  27.671  1.00  9.50  ? 20   PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 20.838 0.345   27.249  1.00  10.24 ? 20   PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 20.778 -2.319  25.742  1.00  9.94  ? 20   PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 20.078 -3.294  24.818  1.00  9.06  ? 20   PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 19.161 -2.896  23.881  1.00  11.17 ? 20   PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 20.342 -4.619  24.950  1.00  11.50 ? 20   PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 18.567 -3.825  23.061  1.00  11.44 ? 20   PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 19.758 -5.539  24.125  1.00  11.82 ? 20   PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 18.869 -5.133  23.200  1.00  10.95 ? 20   PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 21.437 -1.198  28.752  1.00  9.70  ? 21   GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 22.325 -0.294  29.478  1.00  10.53 ? 21   GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 23.522 -1.041  30.021  1.00  10.72 ? 21   GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 23.346 -2.100  30.611  1.00  11.18 ? 21   GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 21.615 0.401   30.621  1.00  13.03 ? 21   GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 22.522 1.411   31.343  1.00  15.28 ? 21   GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 21.790 2.357   32.303  0.20  12.95 ? 21   GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 20.563 2.229   32.475  0.10  11.20 ? 21   GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 22.471 3.245   32.868  0.10  12.88 ? 21   GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 24.703 -0.499  29.779  1.00  10.23 ? 22   GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 25.959 -1.059  30.261  1.00  12.12 ? 22   GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 26.713 0.062   30.952  1.00  14.42 ? 22   GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 27.285 0.901   30.312  1.00  16.37 ? 22   GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 26.739 -1.640  29.089  1.00  11.62 ? 22   GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 27.980 -2.448  29.499  1.00  13.21 ? 22   GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 28.684 -3.053  28.321  1.00  13.69 ? 22   GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 28.672 -2.487  27.240  1.00  15.85 ? 22   GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 29.314 -4.212  28.510  1.00  14.54 ? 22   GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 26.726 -0.016  32.274  1.00  17.97 ? 23   LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 27.275 1.056   33.125  1.00  21.60 ? 23   LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 28.781 1.143   33.046  1.00  23.05 ? 23   LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 29.353 2.238   33.218  1.00  25.07 ? 23   LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 26.860 0.844   34.576  1.00  24.02 ? 23   LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 25.397 0.995   34.840  1.00  25.28 ? 23   LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 25.086 0.870   36.323  0.010 23.70 ? 23   LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 23.595 0.986   36.592  0.010 24.45 ? 23   LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 23.280 0.896   38.045  0.010 24.74 ? 23   LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 29.430 0.003   32.861  1.00  23.00 ? 24   GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 30.882 -0.114  32.852  1.00  24.40 ? 24   GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 31.345 -0.912  31.650  1.00  24.73 ? 24   GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 30.699 -1.900  31.237  1.00  22.14 ? 24   GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 31.373 -0.814  34.125  1.00  26.16 ? 24   GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 31.239 0.030   35.384  0.30  25.36 ? 24   GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 29.858 0.003   36.004  0.010 25.43 ? 24   GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 29.146 -1.002  35.834  0.010 25.36 ? 24   GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 29.489 0.990   36.674  0.010 25.39 ? 24   GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 32.445 -0.475  31.053  0.80  26.08 ? 25   SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 33.062 -1.253  29.992  1.00  26.29 ? 25   SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 33.266 -2.727  30.434  1.00  26.94 ? 25   SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 33.650 -3.027  31.579  0.80  28.29 ? 25   SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 34.376 -0.585  29.489  1.00  27.22 ? 25   SER A CB  1 
ATOM   183  N  N   . ASN A 1 26  ? 32.929 -3.628  29.525  1.00  25.75 ? 26   ASN A N   1 
ATOM   184  C  CA  . ASN A 1 26  ? 32.919 -5.067  29.751  1.00  24.18 ? 26   ASN A CA  1 
ATOM   185  C  C   . ASN A 1 26  ? 32.081 -5.537  30.973  1.00  23.97 ? 26   ASN A C   1 
ATOM   186  O  O   . ASN A 1 26  ? 32.190 -6.711  31.382  1.00  25.73 ? 26   ASN A O   1 
ATOM   187  C  CB  . ASN A 1 26  ? 34.364 -5.614  29.821  0.50  24.34 ? 26   ASN A CB  1 
ATOM   188  C  CG  . ASN A 1 26  ? 35.071 -5.585  28.473  0.50  24.99 ? 26   ASN A CG  1 
ATOM   189  O  OD1 . ASN A 1 26  ? 36.209 -5.104  28.356  0.50  24.73 ? 26   ASN A OD1 1 
ATOM   190  N  ND2 . ASN A 1 26  ? 34.411 -6.117  27.448  0.50  24.35 ? 26   ASN A ND2 1 
ATOM   191  N  N   . GLY A 1 27  ? 31.211 -4.670  31.541  1.00  20.61 ? 27   GLY A N   1 
ATOM   192  C  CA  . GLY A 1 27  ? 30.349 -5.067  32.642  1.00  18.46 ? 27   GLY A CA  1 
ATOM   193  C  C   . GLY A 1 27  ? 29.005 -5.628  32.115  1.00  15.45 ? 27   GLY A C   1 
ATOM   194  O  O   . GLY A 1 27  ? 28.795 -5.711  30.900  1.00  15.71 ? 27   GLY A O   1 
ATOM   195  N  N   . PRO A 1 28  ? 28.108 -6.015  32.998  1.00  15.19 ? 28   PRO A N   1 
ATOM   196  C  CA  . PRO A 1 28  ? 26.854 -6.603  32.545  1.00  14.65 ? 28   PRO A CA  1 
ATOM   197  C  C   . PRO A 1 28  ? 26.005 -5.584  31.790  1.00  12.03 ? 28   PRO A C   1 
ATOM   198  O  O   . PRO A 1 28  ? 26.052 -4.384  32.064  1.00  13.32 ? 28   PRO A O   1 
ATOM   199  C  CB  . PRO A 1 28  ? 26.142 -7.005  33.830  1.00  16.92 ? 28   PRO A CB  1 
ATOM   200  C  CG  . PRO A 1 28  ? 27.031 -6.585  34.916  1.00  20.32 ? 28   PRO A CG  1 
ATOM   201  C  CD  . PRO A 1 28  ? 28.227 -5.976  34.468  1.00  18.05 ? 28   PRO A CD  1 
ATOM   202  N  N   . VAL A 1 29  ? 25.228 -6.105  30.862  1.00  11.10 ? 29   VAL A N   1 
ATOM   203  C  CA  . VAL A 1 29  ? 24.244 -5.342  30.161  1.00  10.08 ? 29   VAL A CA  1 
ATOM   204  C  C   . VAL A 1 29  ? 22.863 -5.658  30.701  1.00  9.13  ? 29   VAL A C   1 
ATOM   205  O  O   . VAL A 1 29  ? 22.439 -6.802  30.710  1.00  11.63 ? 29   VAL A O   1 
ATOM   206  C  CB  . VAL A 1 29  ? 24.316 -5.645  28.668  1.00  9.92  ? 29   VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 29  ? 23.349 -4.762  27.913  1.00  10.72 ? 29   VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 29  ? 25.737 -5.402  28.105  1.00  12.17 ? 29   VAL A CG2 1 
ATOM   209  N  N   . LYS A 1 30  ? 22.160 -4.641  31.159  1.00  9.72  ? 30   LYS A N   1 
ATOM   210  C  CA  . LYS A 1 30  ? 20.771 -4.753  31.580  1.00  10.63 ? 30   LYS A CA  1 
ATOM   211  C  C   . LYS A 1 30  ? 19.919 -4.600  30.322  1.00  10.37 ? 30   LYS A C   1 
ATOM   212  O  O   . LYS A 1 30  ? 20.130 -3.689  29.535  1.00  11.08 ? 30   LYS A O   1 
ATOM   213  C  CB  . LYS A 1 30  ? 20.418 -3.647  32.547  1.00  13.35 ? 30   LYS A CB  1 
ATOM   214  C  CG  A LYS A 1 30  ? 19.199 -3.834  33.366  0.50  14.83 ? 30   LYS A CG  1 
ATOM   215  C  CG  B LYS A 1 30  ? 20.701 -3.824  34.018  0.50  17.21 ? 30   LYS A CG  1 
ATOM   216  C  CD  A LYS A 1 30  ? 18.669 -2.514  33.921  0.50  17.02 ? 30   LYS A CD  1 
ATOM   217  C  CD  B LYS A 1 30  ? 20.252 -2.608  34.848  0.50  17.48 ? 30   LYS A CD  1 
ATOM   218  C  CE  A LYS A 1 30  ? 17.223 -2.641  34.453  0.50  19.71 ? 30   LYS A CE  1 
ATOM   219  C  CE  B LYS A 1 30  ? 20.822 -2.700  36.248  0.50  18.69 ? 30   LYS A CE  1 
ATOM   220  N  NZ  A LYS A 1 30  ? 16.908 -1.401  35.203  0.50  21.50 ? 30   LYS A NZ  1 
ATOM   221  N  NZ  B LYS A 1 30  ? 20.389 -1.566  37.112  0.010 18.11 ? 30   LYS A NZ  1 
ATOM   222  N  N   . VAL A 1 31  ? 18.945 -5.480  30.186  1.00  10.11 ? 31   VAL A N   1 
ATOM   223  C  CA  . VAL A 1 31  ? 18.066 -5.542  29.036  1.00  9.83  ? 31   VAL A CA  1 
ATOM   224  C  C   . VAL A 1 31  ? 16.650 -5.529  29.569  1.00  10.63 ? 31   VAL A C   1 
ATOM   225  O  O   . VAL A 1 31  ? 16.270 -6.405  30.375  1.00  12.41 ? 31   VAL A O   1 
ATOM   226  C  CB  . VAL A 1 31  ? 18.261 -6.807  28.180  1.00  11.02 ? 31   VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 31  ? 17.369 -6.820  26.938  1.00  12.56 ? 31   VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 31  ? 19.716 -6.991  27.779  1.00  12.24 ? 31   VAL A CG2 1 
ATOM   229  N  N   . TRP A 1 32  ? 15.841 -4.549  29.195  1.00  10.21 ? 32   TRP A N   1 
ATOM   230  C  CA  . TRP A 1 32  ? 14.515 -4.436  29.755  1.00  10.79 ? 32   TRP A CA  1 
ATOM   231  C  C   . TRP A 1 32  ? 13.570 -3.707  28.855  1.00  9.30  ? 32   TRP A C   1 
ATOM   232  O  O   . TRP A 1 32  ? 13.955 -2.875  28.047  1.00  10.30 ? 32   TRP A O   1 
ATOM   233  C  CB  . TRP A 1 32  ? 14.499 -3.767  31.129  1.00  12.60 ? 32   TRP A CB  1 
ATOM   234  C  CG  . TRP A 1 32  ? 14.650 -2.312  31.108  1.00  13.50 ? 32   TRP A CG  1 
ATOM   235  C  CD1 . TRP A 1 32  ? 13.623 -1.399  31.200  1.00  16.06 ? 32   TRP A CD1 1 
ATOM   236  C  CD2 . TRP A 1 32  ? 15.849 -1.538  30.908  1.00  13.62 ? 32   TRP A CD2 1 
ATOM   237  N  NE1 . TRP A 1 32  ? 14.125 -0.154  31.134  1.00  16.34 ? 32   TRP A NE1 1 
ATOM   238  C  CE2 . TRP A 1 32  ? 15.478 -0.196  30.946  1.00  14.49 ? 32   TRP A CE2 1 
ATOM   239  C  CE3 . TRP A 1 32  ? 17.189 -1.858  30.693  1.00  14.51 ? 32   TRP A CE3 1 
ATOM   240  C  CZ2 . TRP A 1 32  ? 16.392 0.828   30.812  1.00  15.31 ? 32   TRP A CZ2 1 
ATOM   241  C  CZ3 . TRP A 1 32  ? 18.089 -0.860  30.551  1.00  15.38 ? 32   TRP A CZ3 1 
ATOM   242  C  CH2 . TRP A 1 32  ? 17.693 0.488   30.614  1.00  15.49 ? 32   TRP A CH2 1 
ATOM   243  N  N   . GLY A 1 33  ? 12.314 -4.044  28.999  1.00  9.42  ? 33   GLY A N   1 
ATOM   244  C  CA  . GLY A 1 33  ? 11.271 -3.454  28.183  1.00  9.82  ? 33   GLY A CA  1 
ATOM   245  C  C   . GLY A 1 33  ? 10.051 -4.304  28.160  1.00  10.62 ? 33   GLY A C   1 
ATOM   246  O  O   . GLY A 1 33  ? 9.849  -5.145  29.037  1.00  13.87 ? 33   GLY A O   1 
ATOM   247  N  N   . SER A 1 34  ? 9.203  -4.099  27.184  1.00  11.93 ? 34   SER A N   1 
ATOM   248  C  CA  . SER A 1 34  ? 7.905  -4.766  27.031  1.00  13.46 ? 34   SER A CA  1 
ATOM   249  C  C   . SER A 1 34  ? 7.646  -5.108  25.599  1.00  12.32 ? 34   SER A C   1 
ATOM   250  O  O   . SER A 1 34  ? 8.035  -4.350  24.693  1.00  13.91 ? 34   SER A O   1 
ATOM   251  C  CB  . SER A 1 34  ? 6.805  -3.778  27.482  1.00  16.81 ? 34   SER A CB  1 
ATOM   252  O  OG  . SER A 1 34  ? 5.588  -4.449  27.711  0.50  18.85 ? 34   SER A OG  1 
ATOM   253  N  N   . ILE A 1 35  ? 7.081  -6.276  25.372  1.00  11.24 ? 35   ILE A N   1 
ATOM   254  C  CA  . ILE A 1 35  ? 6.663  -6.718  24.048  1.00  11.07 ? 35   ILE A CA  1 
ATOM   255  C  C   . ILE A 1 35  ? 5.209  -7.140  24.162  1.00  11.74 ? 35   ILE A C   1 
ATOM   256  O  O   . ILE A 1 35  ? 4.870  -7.890  25.077  1.00  13.53 ? 35   ILE A O   1 
ATOM   257  C  CB  . ILE A 1 35  ? 7.487  -7.919  23.543  1.00  10.99 ? 35   ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 35  ? 8.985  -7.605  23.662  1.00  12.27 ? 35   ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 35  ? 7.117  -8.286  22.090  1.00  12.46 ? 35   ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 35  ? 9.923  -8.790  23.322  1.00  14.34 ? 35   ILE A CD1 1 
ATOM   261  N  N   . LYS A 1 36  ? 4.355  -6.688  23.239  1.00  11.58 ? 36   LYS A N   1 
ATOM   262  C  CA  . LYS A 1 36  ? 2.950  -7.050  23.229  1.00  13.51 ? 36   LYS A CA  1 
ATOM   263  C  C   . LYS A 1 36  ? 2.600  -7.843  21.979  1.00  12.25 ? 36   LYS A C   1 
ATOM   264  O  O   . LYS A 1 36  ? 3.400  -7.878  21.034  1.00  12.84 ? 36   LYS A O   1 
ATOM   265  C  CB  . LYS A 1 36  ? 2.079  -5.814  23.403  1.00  15.88 ? 36   LYS A CB  1 
ATOM   266  C  CG  . LYS A 1 36  ? 2.088  -4.879  22.269  1.00  18.76 ? 36   LYS A CG  1 
ATOM   267  C  CD  . LYS A 1 36  ? 1.261  -3.617  22.563  1.00  20.62 ? 36   LYS A CD  1 
ATOM   268  C  CE  . LYS A 1 36  ? 1.792  -2.811  23.700  0.50  21.57 ? 36   LYS A CE  1 
ATOM   269  N  NZ  . LYS A 1 36  ? 1.305  -1.402  23.622  0.10  20.89 ? 36   LYS A NZ  1 
ATOM   270  N  N   . GLY A 1 37  ? 1.400  -8.428  21.948  1.00  12.48 ? 37   GLY A N   1 
ATOM   271  C  CA  . GLY A 1 37  ? 0.909  -9.137  20.804  1.00  13.19 ? 37   GLY A CA  1 
ATOM   272  C  C   . GLY A 1 37  ? 1.315  -10.591 20.717  1.00  13.30 ? 37   GLY A C   1 
ATOM   273  O  O   . GLY A 1 37  ? 1.109  -11.215 19.698  1.00  15.54 ? 37   GLY A O   1 
ATOM   274  N  N   . LEU A 1 38  ? 1.968  -11.127 21.768  1.00  13.15 ? 38   LEU A N   1 
ATOM   275  C  CA  . LEU A 1 38  ? 2.495  -12.486 21.756  1.00  13.37 ? 38   LEU A CA  1 
ATOM   276  C  C   . LEU A 1 38  ? 1.459  -13.494 22.253  1.00  13.69 ? 38   LEU A C   1 
ATOM   277  O  O   . LEU A 1 38  ? 0.622  -13.170 23.075  1.00  17.77 ? 38   LEU A O   1 
ATOM   278  C  CB  . LEU A 1 38  ? 3.702  -12.558 22.715  1.00  12.17 ? 38   LEU A CB  1 
ATOM   279  C  CG  . LEU A 1 38  ? 4.951  -11.788 22.205  1.00  11.96 ? 38   LEU A CG  1 
ATOM   280  C  CD1 . LEU A 1 38  ? 5.906  -11.590 23.332  1.00  13.54 ? 38   LEU A CD1 1 
ATOM   281  C  CD2 . LEU A 1 38  ? 5.626  -12.525 21.045  1.00  13.01 ? 38   LEU A CD2 1 
ATOM   282  N  N   . THR A 1 39  ? 1.593  -14.726 21.839  1.00  13.29 ? 39   THR A N   1 
ATOM   283  C  CA  . THR A 1 39  ? 0.872  -15.830 22.452  1.00  13.28 ? 39   THR A CA  1 
ATOM   284  C  C   . THR A 1 39  ? 1.431  -16.123 23.856  1.00  13.08 ? 39   THR A C   1 
ATOM   285  O  O   . THR A 1 39  ? 2.622  -15.971 24.146  1.00  13.54 ? 39   THR A O   1 
ATOM   286  C  CB  . THR A 1 39  ? 0.895  -17.089 21.570  1.00  13.94 ? 39   THR A CB  1 
ATOM   287  O  OG1 . THR A 1 39  ? 2.248  -17.470 21.295  1.00  16.02 ? 39   THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 39  ? 0.174  -16.885 20.280  1.00  16.64 ? 39   THR A CG2 1 
ATOM   289  N  N   . GLU A 1 40  ? 0.587  -16.608 24.751  1.00  12.91 ? 40   GLU A N   1 
ATOM   290  C  CA  . GLU A 1 40  ? 1.027  -16.892 26.132  1.00  11.68 ? 40   GLU A CA  1 
ATOM   291  C  C   . GLU A 1 40  ? 2.132  -17.958 26.136  1.00  12.42 ? 40   GLU A C   1 
ATOM   292  O  O   . GLU A 1 40  ? 2.096  -18.947 25.378  1.00  14.05 ? 40   GLU A O   1 
ATOM   293  C  CB  . GLU A 1 40  ? -0.188 -17.449 26.910  1.00  13.48 ? 40   GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 40  ? 0.060  -17.699 28.333  1.00  15.91 ? 40   GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 40  ? -1.111 -18.275 29.082  0.40  14.39 ? 40   GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 40  ? -1.849 -19.039 28.488  0.40  17.89 ? 40   GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 40  ? -1.278 -17.933 30.270  0.40  13.76 ? 40   GLU A OE2 1 
ATOM   298  N  N   . GLY A 1 41  ? 3.149  -17.741 26.948  1.00  10.54 ? 41   GLY A N   1 
ATOM   299  C  CA  . GLY A 1 41  ? 4.258  -18.665 27.057  1.00  10.32 ? 41   GLY A CA  1 
ATOM   300  C  C   . GLY A 1 41  ? 5.560  -18.081 26.588  1.00  9.03  ? 41   GLY A C   1 
ATOM   301  O  O   . GLY A 1 41  ? 5.715  -16.867 26.467  1.00  10.02 ? 41   GLY A O   1 
ATOM   302  N  N   . LEU A 1 42  ? 6.521  -18.969 26.374  1.00  8.84  ? 42   LEU A N   1 
ATOM   303  C  CA  . LEU A 1 42  ? 7.910  -18.597 26.086  1.00  8.40  ? 42   LEU A CA  1 
ATOM   304  C  C   . LEU A 1 42  ? 8.113  -18.362 24.619  1.00  8.39  ? 42   LEU A C   1 
ATOM   305  O  O   . LEU A 1 42  ? 7.650  -19.138 23.782  1.00  9.78  ? 42   LEU A O   1 
ATOM   306  C  CB  . LEU A 1 42  ? 8.860  -19.702 26.586  1.00  8.70  ? 42   LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 42  ? 9.237  -19.662 28.086  1.00  9.90  ? 42   LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 42  ? 8.047  -19.837 28.958  1.00  12.00 ? 42   LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 42  ? 10.302 -20.673 28.350  1.00  11.55 ? 42   LEU A CD2 1 
ATOM   310  N  N   . HIS A 1 43  ? 8.941  -17.372 24.310  1.00  8.62  ? 43   HIS A N   1 
ATOM   311  C  CA  . HIS A 1 43  ? 9.277  -17.009 22.923  1.00  8.10  ? 43   HIS A CA  1 
ATOM   312  C  C   . HIS A 1 43  ? 10.763 -16.774 22.840  1.00  7.60  ? 43   HIS A C   1 
ATOM   313  O  O   . HIS A 1 43  ? 11.327 -16.008 23.653  1.00  8.10  ? 43   HIS A O   1 
ATOM   314  C  CB  . HIS A 1 43  ? 8.550  -15.718 22.543  1.00  8.98  ? 43   HIS A CB  1 
ATOM   315  C  CG  . HIS A 1 43  ? 7.087  -15.901 22.429  1.00  9.84  ? 43   HIS A CG  1 
ATOM   316  N  ND1 . HIS A 1 43  ? 6.506  -16.288 21.238  1.00  12.66 ? 43   HIS A ND1 1 
ATOM   317  C  CD2 . HIS A 1 43  ? 6.107  -15.832 23.344  1.00  11.50 ? 43   HIS A CD2 1 
ATOM   318  C  CE1 . HIS A 1 43  ? 5.193  -16.415 21.429  1.00  13.92 ? 43   HIS A CE1 1 
ATOM   319  N  NE2 . HIS A 1 43  ? 4.927  -16.145 22.701  1.00  12.73 ? 43   HIS A NE2 1 
ATOM   320  N  N   . GLY A 1 44  ? 11.428 -17.392 21.872  1.00  7.34  ? 44   GLY A N   1 
ATOM   321  C  CA  . GLY A 1 44  ? 12.862 -17.218 21.750  1.00  7.75  ? 44   GLY A CA  1 
ATOM   322  C  C   . GLY A 1 44  ? 13.195 -15.767 21.456  1.00  7.46  ? 44   GLY A C   1 
ATOM   323  O  O   . GLY A 1 44  ? 12.486 -15.031 20.791  1.00  7.92  ? 44   GLY A O   1 
ATOM   324  N  N   . PHE A 1 45  ? 14.391 -15.399 21.903  1.00  7.52  ? 45   PHE A N   1 
ATOM   325  C  CA  . PHE A 1 45  ? 14.807 -13.996 21.935  1.00  7.46  ? 45   PHE A CA  1 
ATOM   326  C  C   . PHE A 1 45  ? 16.283 -13.960 21.661  1.00  6.78  ? 45   PHE A C   1 
ATOM   327  O  O   . PHE A 1 45  ? 17.089 -14.394 22.493  1.00  8.12  ? 45   PHE A O   1 
ATOM   328  C  CB  . PHE A 1 45  ? 14.434 -13.467 23.357  1.00  8.66  ? 45   PHE A CB  1 
ATOM   329  C  CG  . PHE A 1 45  ? 14.537 -11.977 23.564  1.00  9.63  ? 45   PHE A CG  1 
ATOM   330  C  CD1 . PHE A 1 45  ? 13.806 -11.113 22.754  1.00  11.36 ? 45   PHE A CD1 1 
ATOM   331  C  CD2 . PHE A 1 45  ? 15.275 -11.438 24.570  1.00  10.13 ? 45   PHE A CD2 1 
ATOM   332  C  CE1 . PHE A 1 45  ? 13.809 -9.749  23.030  1.00  13.44 ? 45   PHE A CE1 1 
ATOM   333  C  CE2 . PHE A 1 45  ? 15.259 -10.085 24.824  1.00  11.05 ? 45   PHE A CE2 1 
ATOM   334  C  CZ  . PHE A 1 45  ? 14.532 -9.268  24.080  1.00  12.01 ? 45   PHE A CZ  1 
ATOM   335  N  N   . HIS A 1 46  ? 16.682 -13.387 20.513  1.00  7.26  ? 46   HIS A N   1 
ATOM   336  C  CA  . HIS A 1 46  ? 18.031 -13.474 20.082  1.00  7.61  ? 46   HIS A CA  1 
ATOM   337  C  C   . HIS A 1 46  ? 18.531 -12.222 19.414  1.00  6.50  ? 46   HIS A C   1 
ATOM   338  O  O   . HIS A 1 46  ? 17.767 -11.526 18.766  1.00  7.55  ? 46   HIS A O   1 
ATOM   339  C  CB  . HIS A 1 46  ? 18.161 -14.537 18.951  1.00  11.79 ? 46   HIS A CB  1 
ATOM   340  C  CG  . HIS A 1 46  ? 17.587 -15.864 19.249  1.00  10.16 ? 46   HIS A CG  1 
ATOM   341  N  ND1 . HIS A 1 46  ? 16.846 -16.508 18.304  1.00  11.68 ? 46   HIS A ND1 1 
ATOM   342  C  CD2 . HIS A 1 46  ? 17.692 -16.675 20.323  1.00  12.17 ? 46   HIS A CD2 1 
ATOM   343  C  CE1 . HIS A 1 46  ? 16.454 -17.664 18.840  1.00  12.91 ? 46   HIS A CE1 1 
ATOM   344  N  NE2 . HIS A 1 46  ? 16.956 -17.792 20.058  1.00  10.63 ? 46   HIS A NE2 1 
ATOM   345  N  N   . VAL A 1 47  ? 19.823 -12.007 19.484  1.00  7.14  ? 47   VAL A N   1 
ATOM   346  C  CA  . VAL A 1 47  ? 20.483 -11.030 18.604  1.00  6.61  ? 47   VAL A CA  1 
ATOM   347  C  C   . VAL A 1 47  ? 20.993 -11.822 17.424  1.00  6.89  ? 47   VAL A C   1 
ATOM   348  O  O   . VAL A 1 47  ? 21.748 -12.800 17.549  1.00  7.24  ? 47   VAL A O   1 
ATOM   349  C  CB  . VAL A 1 47  ? 21.638 -10.319 19.300  1.00  7.43  ? 47   VAL A CB  1 
ATOM   350  C  CG1 . VAL A 1 47  ? 22.264 -9.271  18.343  1.00  7.89  ? 47   VAL A CG1 1 
ATOM   351  C  CG2 . VAL A 1 47  ? 21.169 -9.620  20.546  1.00  9.55  ? 47   VAL A CG2 1 
ATOM   352  N  N   . HIS A 1 48  ? 20.552 -11.390 16.256  1.00  6.88  ? 48   HIS A N   1 
ATOM   353  C  CA  . HIS A 1 48  ? 20.974 -11.965 14.967  1.00  6.96  ? 48   HIS A CA  1 
ATOM   354  C  C   . HIS A 1 48  ? 22.065 -11.068 14.367  1.00  8.21  ? 48   HIS A C   1 
ATOM   355  O  O   . HIS A 1 48  ? 22.217 -9.922  14.750  1.00  9.52  ? 48   HIS A O   1 
ATOM   356  C  CB  . HIS A 1 48  ? 19.792 -12.107 14.035  1.00  7.49  ? 48   HIS A CB  1 
ATOM   357  C  CG  . HIS A 1 48  ? 18.907 -13.270 14.364  1.00  7.86  ? 48   HIS A CG  1 
ATOM   358  N  ND1 . HIS A 1 48  ? 18.784 -14.344 13.534  1.00  9.21  ? 48   HIS A ND1 1 
ATOM   359  C  CD2 . HIS A 1 48  ? 18.135 -13.559 15.453  1.00  9.47  ? 48   HIS A CD2 1 
ATOM   360  C  CE1 . HIS A 1 48  ? 17.945 -15.221 14.071  1.00  11.19 ? 48   HIS A CE1 1 
ATOM   361  N  NE2 . HIS A 1 48  ? 17.555 -14.794 15.243  1.00  10.10 ? 48   HIS A NE2 1 
ATOM   362  N  N   . GLU A 1 49  ? 22.834 -11.627 13.436  1.00  7.43  ? 49   GLU A N   1 
ATOM   363  C  CA  . GLU A 1 49  ? 24.065 -11.058 12.990  1.00  8.19  ? 49   GLU A CA  1 
ATOM   364  C  C   . GLU A 1 49  ? 23.961 -9.717  12.295  1.00  8.48  ? 49   GLU A C   1 
ATOM   365  O  O   . GLU A 1 49  ? 24.760 -8.806  12.585  1.00  9.86  ? 49   GLU A O   1 
ATOM   366  C  CB  . GLU A 1 49  ? 24.748 -12.048 12.060  1.00  8.93  ? 49   GLU A CB  1 
ATOM   367  C  CG  A GLU A 1 49  ? 26.114 -11.590 11.725  0.80  11.92 ? 49   GLU A CG  1 
ATOM   368  C  CG  B GLU A 1 49  ? 26.132 -11.657 11.529  0.20  9.20  ? 49   GLU A CG  1 
ATOM   369  C  CD  A GLU A 1 49  ? 26.870 -12.492 10.834  0.80  13.66 ? 49   GLU A CD  1 
ATOM   370  C  CD  B GLU A 1 49  ? 27.236 -11.901 12.529  0.20  12.14 ? 49   GLU A CD  1 
ATOM   371  O  OE1 A GLU A 1 49  ? 26.315 -13.544 10.375  0.80  17.44 ? 49   GLU A OE1 1 
ATOM   372  O  OE1 B GLU A 1 49  ? 26.968 -12.610 13.499  0.20  13.08 ? 49   GLU A OE1 1 
ATOM   373  O  OE2 A GLU A 1 49  ? 28.063 -12.134 10.568  0.80  17.19 ? 49   GLU A OE2 1 
ATOM   374  O  OE2 B GLU A 1 49  ? 28.372 -11.420 12.339  0.20  15.80 ? 49   GLU A OE2 1 
ATOM   375  N  N   . PHE A 1 50  ? 23.005 -9.550  11.407  1.00  7.26  ? 50   PHE A N   1 
ATOM   376  C  CA  . PHE A 1 50  ? 22.980 -8.353  10.595  1.00  7.15  ? 50   PHE A CA  1 
ATOM   377  C  C   . PHE A 1 50  ? 21.874 -7.443  11.009  1.00  7.92  ? 50   PHE A C   1 
ATOM   378  O  O   . PHE A 1 50  ? 20.755 -7.895  11.318  1.00  9.75  ? 50   PHE A O   1 
ATOM   379  C  CB  . PHE A 1 50  ? 22.786 -8.745  9.112   1.00  8.94  ? 50   PHE A CB  1 
ATOM   380  C  CG  . PHE A 1 50  ? 23.794 -9.681  8.626   1.00  10.34 ? 50   PHE A CG  1 
ATOM   381  C  CD1 . PHE A 1 50  ? 23.384 -10.891 8.144   1.00  14.54 ? 50   PHE A CD1 1 
ATOM   382  C  CD2 . PHE A 1 50  ? 25.114 -9.393  8.710   1.00  11.77 ? 50   PHE A CD2 1 
ATOM   383  C  CE1 . PHE A 1 50  ? 24.294 -11.835 7.683   1.00  17.30 ? 50   PHE A CE1 1 
ATOM   384  C  CE2 . PHE A 1 50  ? 26.063 -10.351 8.230   1.00  17.10 ? 50   PHE A CE2 1 
ATOM   385  C  CZ  . PHE A 1 50  ? 25.602 -11.573 7.779   1.00  16.05 ? 50   PHE A CZ  1 
ATOM   386  N  N   . GLY A 1 51  ? 22.151 -6.162  10.946  1.00  8.17  ? 51   GLY A N   1 
ATOM   387  C  CA  . GLY A 1 51  ? 21.157 -5.151  11.131  1.00  8.73  ? 51   GLY A CA  1 
ATOM   388  C  C   . GLY A 1 51  ? 20.435 -4.757  9.866   1.00  9.19  ? 51   GLY A C   1 
ATOM   389  O  O   . GLY A 1 51  ? 20.337 -3.581  9.530   1.00  10.66 ? 51   GLY A O   1 
ATOM   390  N  N   . ASP A 1 52  ? 20.032 -5.754  9.090   1.00  10.50 ? 52   ASP A N   1 
ATOM   391  C  CA  . ASP A 1 52  ? 19.471 -5.615  7.739   1.00  10.41 ? 52   ASP A CA  1 
ATOM   392  C  C   . ASP A 1 52  ? 18.037 -6.069  7.826   1.00  10.89 ? 52   ASP A C   1 
ATOM   393  O  O   . ASP A 1 52  ? 17.781 -7.244  8.053   1.00  12.02 ? 52   ASP A O   1 
ATOM   394  C  CB  . ASP A 1 52  ? 20.291 -6.471  6.764   1.00  9.61  ? 52   ASP A CB  1 
ATOM   395  C  CG  . ASP A 1 52  ? 19.841 -6.336  5.384   0.80  9.26  ? 52   ASP A CG  1 
ATOM   396  O  OD1 . ASP A 1 52  ? 18.650 -6.030  5.133   0.80  10.73 ? 52   ASP A OD1 1 
ATOM   397  O  OD2 . ASP A 1 52  ? 20.662 -6.621  4.467   0.80  14.11 ? 52   ASP A OD2 1 
ATOM   398  N  N   . ASN A 1 53  ? 17.098 -5.146  7.618   1.00  11.46 ? 53   ASN A N   1 
ATOM   399  C  CA  . ASN A 1 53  ? 15.669 -5.477  7.616   1.00  12.38 ? 53   ASN A CA  1 
ATOM   400  C  C   . ASN A 1 53  ? 15.031 -5.220  6.273   1.00  11.71 ? 53   ASN A C   1 
ATOM   401  O  O   . ASN A 1 53  ? 13.836 -4.993  6.161   1.00  13.36 ? 53   ASN A O   1 
ATOM   402  C  CB  . ASN A 1 53  ? 15.038 -4.728  8.764   1.00  14.99 ? 53   ASN A CB  1 
ATOM   403  C  CG  A ASN A 1 53  ? 13.578 -5.043  8.988   0.50  14.30 ? 53   ASN A CG  1 
ATOM   404  C  CG  B ASN A 1 53  ? 15.481 -5.357  10.239  0.50  12.97 ? 53   ASN A CG  1 
ATOM   405  O  OD1 A ASN A 1 53  ? 12.699 -4.174  8.908   0.50  21.91 ? 53   ASN A OD1 1 
ATOM   406  O  OD1 B ASN A 1 53  ? 16.366 -6.283  10.382  0.50  17.24 ? 53   ASN A OD1 1 
ATOM   407  N  ND2 A ASN A 1 53  ? 13.328 -6.252  9.262   0.50  15.35 ? 53   ASN A ND2 1 
ATOM   408  N  ND2 B ASN A 1 53  ? 14.967 -4.775  11.275  0.50  13.64 ? 53   ASN A ND2 1 
ATOM   409  N  N   . THR A 1 54  ? 15.851 -5.284  5.234   1.00  10.89 ? 54   THR A N   1 
ATOM   410  C  CA  . THR A 1 54  ? 15.368 -4.924  3.902   1.00  11.72 ? 54   THR A CA  1 
ATOM   411  C  C   . THR A 1 54  ? 14.206 -5.831  3.484   1.00  13.51 ? 54   THR A C   1 
ATOM   412  O  O   . THR A 1 54  ? 13.319 -5.377  2.753   1.00  14.94 ? 54   THR A O   1 
ATOM   413  C  CB  . THR A 1 54  ? 16.486 -4.938  2.891   1.00  12.47 ? 54   THR A CB  1 
ATOM   414  O  OG1 . THR A 1 54  ? 17.175 -6.197  2.919   1.00  14.52 ? 54   THR A OG1 1 
ATOM   415  C  CG2 . THR A 1 54  ? 17.518 -3.821  3.116   1.00  13.28 ? 54   THR A CG2 1 
ATOM   416  N  N   . ALA A 1 55  ? 14.218 -7.125  3.847   1.00  12.96 ? 55   ALA A N   1 
ATOM   417  C  CA  . ALA A 1 55  ? 13.077 -7.990  3.531   1.00  13.84 ? 55   ALA A CA  1 
ATOM   418  C  C   . ALA A 1 55  ? 12.458 -8.496  4.807   1.00  13.68 ? 55   ALA A C   1 
ATOM   419  O  O   . ALA A 1 55  ? 11.924 -9.610  4.878   1.00  15.56 ? 55   ALA A O   1 
ATOM   420  C  CB  . ALA A 1 55  ? 13.529 -9.138  2.637   1.00  15.71 ? 55   ALA A CB  1 
ATOM   421  N  N   . GLY A 1 56  ? 12.421 -7.653  5.808   1.00  12.79 ? 56   GLY A N   1 
ATOM   422  C  CA  . GLY A 1 56  ? 11.914 -8.023  7.094   1.00  12.48 ? 56   GLY A CA  1 
ATOM   423  C  C   . GLY A 1 56  ? 12.934 -8.828  7.867   1.00  11.51 ? 56   GLY A C   1 
ATOM   424  O  O   . GLY A 1 56  ? 14.149 -8.773  7.625   1.00  11.98 ? 56   GLY A O   1 
ATOM   425  N  N   . CYS A 1 57  ? 12.441 -9.551  8.842   1.00  10.87 ? 57   CYS A N   1 
ATOM   426  C  CA  . CYS A 1 57  ? 13.298 -10.199 9.788   1.00  10.58 ? 57   CYS A CA  1 
ATOM   427  C  C   . CYS A 1 57  ? 14.207 -11.279 9.229   1.00  10.72 ? 57   CYS A C   1 
ATOM   428  O  O   . CYS A 1 57  ? 15.296 -11.536 9.787   1.00  11.08 ? 57   CYS A O   1 
ATOM   429  C  CB  . CYS A 1 57  ? 12.444 -10.799 10.877  1.00  12.58 ? 57   CYS A CB  1 
ATOM   430  S  SG  . CYS A 1 57  ? 11.346 -9.764  11.788  0.70  17.36 ? 57   CYS A SG  1 
ATOM   431  N  N   . THR A 1 58  ? 13.838 -11.876 8.101   1.00  11.15 ? 58   THR A N   1 
ATOM   432  C  CA  . THR A 1 58  ? 14.680 -12.888 7.476   1.00  11.78 ? 58   THR A CA  1 
ATOM   433  C  C   . THR A 1 58  ? 16.062 -12.342 7.074   1.00  11.54 ? 58   THR A C   1 
ATOM   434  O  O   . THR A 1 58  ? 17.107 -13.040 7.151   1.00  12.10 ? 58   THR A O   1 
ATOM   435  C  CB  . THR A 1 58  ? 13.932 -13.567 6.313   1.00  13.22 ? 58   THR A CB  1 
ATOM   436  O  OG1 . THR A 1 58  ? 14.683 -14.742 5.971   1.00  15.89 ? 58   THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 58  ? 13.771 -12.694 5.114   1.00  14.41 ? 58   THR A CG2 1 
ATOM   438  N  N   . SER A 1 59  ? 16.114 -11.064 6.732   1.00  9.84  ? 59   SER A N   1 
ATOM   439  C  CA  . SER A 1 59  ? 17.312 -10.438 6.322   1.00  9.96  ? 59   SER A CA  1 
ATOM   440  C  C   . SER A 1 59  ? 18.408 -10.313 7.420   1.00  9.43  ? 59   SER A C   1 
ATOM   441  O  O   . SER A 1 59  ? 19.586 -10.061 7.173   1.00  10.75 ? 59   SER A O   1 
ATOM   442  C  CB  . SER A 1 59  ? 16.922 -8.978  5.727   1.00  9.71  ? 59   SER A CB  1 
ATOM   443  O  OG  A SER A 1 59  ? 15.960 -9.092  4.668   0.72  14.23 ? 59   SER A OG  1 
ATOM   444  O  OG  B SER A 1 59  ? 15.971 -9.084  4.665   0.28  11.38 ? 59   SER A OG  1 
ATOM   445  N  N   . ALA A 1 60  ? 18.036 -10.559 8.676   1.00  8.89  ? 60   ALA A N   1 
ATOM   446  C  CA  . ALA A 1 60  ? 18.965 -10.418 9.789   1.00  9.18  ? 60   ALA A CA  1 
ATOM   447  C  C   . ALA A 1 60  ? 19.971 -11.569 9.868   1.00  8.42  ? 60   ALA A C   1 
ATOM   448  O  O   . ALA A 1 60  ? 20.933 -11.489 10.603  1.00  8.89  ? 60   ALA A O   1 
ATOM   449  C  CB  . ALA A 1 60  ? 18.200 -10.280 11.070  1.00  10.04 ? 60   ALA A CB  1 
ATOM   450  N  N   . GLY A 1 61  ? 19.734 -12.643 9.116   1.00  8.15  ? 61   GLY A N   1 
ATOM   451  C  CA  . GLY A 1 61  ? 20.704 -13.719 9.063   1.00  8.50  ? 61   GLY A CA  1 
ATOM   452  C  C   . GLY A 1 61  ? 20.663 -14.581 10.280  1.00  8.31  ? 61   GLY A C   1 
ATOM   453  O  O   . GLY A 1 61  ? 19.631 -14.673 10.941  1.00  8.02  ? 61   GLY A O   1 
ATOM   454  N  N   . PRO A 1 62  ? 21.776 -15.262 10.550  1.00  7.66  ? 62   PRO A N   1 
ATOM   455  C  CA  . PRO A 1 62  ? 21.835 -16.250 11.599  1.00  8.81  ? 62   PRO A CA  1 
ATOM   456  C  C   . PRO A 1 62  ? 22.048 -15.578 12.963  1.00  8.37  ? 62   PRO A C   1 
ATOM   457  O  O   . PRO A 1 62  ? 22.121 -14.380 13.104  1.00  7.69  ? 62   PRO A O   1 
ATOM   458  C  CB  . PRO A 1 62  ? 23.059 -17.095 11.205  1.00  11.69 ? 62   PRO A CB  1 
ATOM   459  C  CG  . PRO A 1 62  ? 23.964 -16.128 10.561  1.00  10.63 ? 62   PRO A CG  1 
ATOM   460  C  CD  . PRO A 1 62  ? 23.065 -15.146 9.812   1.00  9.83  ? 62   PRO A CD  1 
ATOM   461  N  N   . HIS A 1 63  ? 22.145 -16.388 14.006  1.00  8.97  ? 63   HIS A N   1 
ATOM   462  C  CA  . HIS A 1 63  ? 22.434 -15.884 15.371  1.00  8.69  ? 63   HIS A CA  1 
ATOM   463  C  C   . HIS A 1 63  ? 23.770 -15.192 15.379  1.00  8.44  ? 63   HIS A C   1 
ATOM   464  O  O   . HIS A 1 63  ? 24.701 -15.639 14.731  1.00  9.24  ? 63   HIS A O   1 
ATOM   465  C  CB  . HIS A 1 63  ? 22.443 -16.987 16.388  1.00  9.51  ? 63   HIS A CB  1 
ATOM   466  C  CG  . HIS A 1 63  ? 21.102 -17.602 16.575  1.00  10.89 ? 63   HIS A CG  1 
ATOM   467  N  ND1 . HIS A 1 63  ? 20.826 -18.472 17.621  1.00  9.56  ? 63   HIS A ND1 1 
ATOM   468  C  CD2 . HIS A 1 63  ? 19.972 -17.516 15.850  1.00  13.83 ? 63   HIS A CD2 1 
ATOM   469  C  CE1 . HIS A 1 63  ? 19.570 -18.871 17.514  1.00  11.65 ? 63   HIS A CE1 1 
ATOM   470  N  NE2 . HIS A 1 63  ? 19.023 -18.307 16.447  1.00  14.15 ? 63   HIS A NE2 1 
ATOM   471  N  N   . PHE A 1 64  ? 23.899 -14.112 16.119  1.00  7.98  ? 64   PHE A N   1 
ATOM   472  C  CA  . PHE A 1 64  ? 25.222 -13.469 16.278  1.00  7.17  ? 64   PHE A CA  1 
ATOM   473  C  C   . PHE A 1 64  ? 26.143 -14.401 17.046  1.00  7.16  ? 64   PHE A C   1 
ATOM   474  O  O   . PHE A 1 64  ? 25.909 -14.731 18.207  1.00  7.74  ? 64   PHE A O   1 
ATOM   475  C  CB  . PHE A 1 64  ? 25.045 -12.122 16.992  1.00  8.35  ? 64   PHE A CB  1 
ATOM   476  C  CG  . PHE A 1 64  ? 26.317 -11.343 17.167  1.00  8.62  ? 64   PHE A CG  1 
ATOM   477  C  CD1 . PHE A 1 64  ? 27.221 -11.194 16.150  1.00  9.87  ? 64   PHE A CD1 1 
ATOM   478  C  CD2 . PHE A 1 64  ? 26.575 -10.756 18.389  1.00  9.90  ? 64   PHE A CD2 1 
ATOM   479  C  CE1 . PHE A 1 64  ? 28.410 -10.459 16.353  1.00  11.02 ? 64   PHE A CE1 1 
ATOM   480  C  CE2 . PHE A 1 64  ? 27.708 -10.007 18.565  1.00  12.16 ? 64   PHE A CE2 1 
ATOM   481  C  CZ  . PHE A 1 64  ? 28.593 -9.871  17.556  1.00  11.32 ? 64   PHE A CZ  1 
ATOM   482  N  N   . ASN A 1 65  ? 27.195 -14.831 16.344  1.00  8.40  ? 65   ASN A N   1 
ATOM   483  C  CA  . ASN A 1 65  ? 28.092 -15.893 16.827  1.00  8.28  ? 65   ASN A CA  1 
ATOM   484  C  C   . ASN A 1 65  ? 29.532 -15.652 16.452  1.00  9.97  ? 65   ASN A C   1 
ATOM   485  O  O   . ASN A 1 65  ? 30.150 -16.482 15.777  1.00  11.49 ? 65   ASN A O   1 
ATOM   486  C  CB  . ASN A 1 65  ? 27.629 -17.236 16.262  1.00  9.10  ? 65   ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 65  ? 28.369 -18.437 16.839  1.00  9.66  ? 65   ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 65  ? 28.942 -18.399 17.912  1.00  10.12 ? 65   ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 65  ? 28.327 -19.548 16.101  1.00  11.18 ? 65   ASN A ND2 1 
ATOM   490  N  N   . PRO A 1 66  ? 30.114 -14.559 16.965  1.00  10.13 ? 66   PRO A N   1 
ATOM   491  C  CA  . PRO A 1 66  ? 31.504 -14.235 16.571  1.00  12.42 ? 66   PRO A CA  1 
ATOM   492  C  C   . PRO A 1 66  ? 32.502 -15.237 17.038  1.00  12.97 ? 66   PRO A C   1 
ATOM   493  O  O   . PRO A 1 66  ? 33.609 -15.287 16.461  1.00  16.15 ? 66   PRO A O   1 
ATOM   494  C  CB  . PRO A 1 66  ? 31.720 -12.862 17.186  1.00  12.60 ? 66   PRO A CB  1 
ATOM   495  C  CG  . PRO A 1 66  ? 30.797 -12.811 18.375  1.00  12.08 ? 66   PRO A CG  1 
ATOM   496  C  CD  . PRO A 1 66  ? 29.558 -13.555 17.901  1.00  10.00 ? 66   PRO A CD  1 
ATOM   497  N  N   . LEU A 1 67  ? 32.202 -15.993 18.090  1.00  12.66 ? 67   LEU A N   1 
ATOM   498  C  CA  . LEU A 1 67  ? 33.135 -16.968 18.637  1.00  13.08 ? 67   LEU A CA  1 
ATOM   499  C  C   . LEU A 1 67  ? 32.961 -18.379 18.119  1.00  13.85 ? 67   LEU A C   1 
ATOM   500  O  O   . LEU A 1 67  ? 33.646 -19.292 18.578  1.00  15.96 ? 67   LEU A O   1 
ATOM   501  C  CB  . LEU A 1 67  ? 33.073 -16.964 20.157  1.00  13.75 ? 67   LEU A CB  1 
ATOM   502  C  CG  . LEU A 1 67  ? 33.505 -15.648 20.776  1.00  16.29 ? 67   LEU A CG  1 
ATOM   503  C  CD1 . LEU A 1 67  ? 33.258 -15.631 22.255  1.00  19.16 ? 67   LEU A CD1 1 
ATOM   504  C  CD2 . LEU A 1 67  ? 35.019 -15.376 20.503  1.00  22.12 ? 67   LEU A CD2 1 
ATOM   505  N  N   . SER A 1 68  ? 32.098 -18.593 17.141  1.00  13.63 ? 68   SER A N   1 
ATOM   506  C  CA  . SER A 1 68  ? 31.914 -19.907 16.494  1.00  14.09 ? 68   SER A CA  1 
ATOM   507  C  C   . SER A 1 68  ? 31.577 -21.020 17.481  1.00  14.60 ? 68   SER A C   1 
ATOM   508  O  O   . SER A 1 68  ? 32.195 -22.101 17.456  1.00  17.37 ? 68   SER A O   1 
ATOM   509  C  CB  . SER A 1 68  ? 33.181 -20.266 15.667  1.00  15.94 ? 68   SER A CB  1 
ATOM   510  O  OG  . SER A 1 68  ? 33.430 -19.272 14.684  1.00  19.32 ? 68   SER A OG  1 
ATOM   511  N  N   . ARG A 1 69  ? 30.633 -20.771 18.383  1.00  12.59 ? 69   ARG A N   1 
ATOM   512  C  CA  . ARG A 1 69  ? 30.148 -21.725 19.369  1.00  13.34 ? 69   ARG A CA  1 
ATOM   513  C  C   . ARG A 1 69  ? 28.834 -22.312 18.916  1.00  11.93 ? 69   ARG A C   1 
ATOM   514  O  O   . ARG A 1 69  ? 28.266 -21.877 17.921  1.00  13.21 ? 69   ARG A O   1 
ATOM   515  C  CB  . ARG A 1 69  ? 29.941 -21.020 20.677  1.00  14.44 ? 69   ARG A CB  1 
ATOM   516  C  CG  . ARG A 1 69  ? 31.224 -20.386 21.274  1.00  20.45 ? 69   ARG A CG  1 
ATOM   517  C  CD  A ARG A 1 69  ? 32.191 -21.404 21.799  0.50  27.23 ? 69   ARG A CD  1 
ATOM   518  C  CD  B ARG A 1 69  ? 32.063 -21.563 21.774  0.50  25.30 ? 69   ARG A CD  1 
ATOM   519  N  NE  A ARG A 1 69  ? 32.051 -21.524 23.253  0.50  30.93 ? 69   ARG A NE  1 
ATOM   520  N  NE  B ARG A 1 69  ? 33.491 -21.318 21.896  0.50  26.40 ? 69   ARG A NE  1 
ATOM   521  C  CZ  A ARG A 1 69  ? 32.402 -20.589 24.133  0.50  32.31 ? 69   ARG A CZ  1 
ATOM   522  C  CZ  B ARG A 1 69  ? 34.399 -22.282 22.085  0.50  27.39 ? 69   ARG A CZ  1 
ATOM   523  N  NH1 A ARG A 1 69  ? 32.913 -19.419 23.739  0.50  33.40 ? 69   ARG A NH1 1 
ATOM   524  N  NH1 B ARG A 1 69  ? 34.026 -23.559 22.186  0.50  29.10 ? 69   ARG A NH1 1 
ATOM   525  N  NH2 A ARG A 1 69  ? 32.220 -20.819 25.428  0.50  31.72 ? 69   ARG A NH2 1 
ATOM   526  N  NH2 B ARG A 1 69  ? 35.683 -21.972 22.177  0.50  29.63 ? 69   ARG A NH2 1 
ATOM   527  N  N   . LYS A 1 70  ? 28.374 -23.334 19.635  1.00  12.43 ? 70   LYS A N   1 
ATOM   528  C  CA  . LYS A 1 70  ? 27.085 -23.922 19.437  1.00  12.85 ? 70   LYS A CA  1 
ATOM   529  C  C   . LYS A 1 70  ? 26.042 -23.081 20.144  1.00  9.84  ? 70   LYS A C   1 
ATOM   530  O  O   . LYS A 1 70  ? 26.320 -22.348 21.077  1.00  11.26 ? 70   LYS A O   1 
ATOM   531  C  CB  . LYS A 1 70  ? 27.058 -25.346 19.961  1.00  13.92 ? 70   LYS A CB  1 
ATOM   532  C  CG  . LYS A 1 70  ? 27.952 -26.289 19.127  0.70  16.90 ? 70   LYS A CG  1 
ATOM   533  C  CD  . LYS A 1 70  ? 27.830 -27.755 19.602  0.30  15.57 ? 70   LYS A CD  1 
ATOM   534  C  CE  . LYS A 1 70  ? 28.398 -27.962 21.006  0.30  17.74 ? 70   LYS A CE  1 
ATOM   535  N  NZ  . LYS A 1 70  ? 28.124 -29.332 21.549  0.30  19.03 ? 70   LYS A NZ  1 
ATOM   536  N  N   . HIS A 1 71  ? 24.810 -23.228 19.706  1.00  10.16 ? 71   HIS A N   1 
ATOM   537  C  CA  . HIS A 1 71  ? 23.674 -22.581 20.288  1.00  10.26 ? 71   HIS A CA  1 
ATOM   538  C  C   . HIS A 1 71  ? 23.418 -23.070 21.720  1.00  9.41  ? 71   HIS A C   1 
ATOM   539  O  O   . HIS A 1 71  ? 23.467 -24.282 21.982  1.00  11.33 ? 71   HIS A O   1 
ATOM   540  C  CB  . HIS A 1 71  ? 22.417 -22.830 19.430  1.00  9.86  ? 71   HIS A CB  1 
ATOM   541  C  CG  . HIS A 1 71  ? 21.212 -22.155 19.982  1.00  9.29  ? 71   HIS A CG  1 
ATOM   542  N  ND1 . HIS A 1 71  ? 21.011 -20.798 19.881  1.00  8.25  ? 71   HIS A ND1 1 
ATOM   543  C  CD2 . HIS A 1 71  ? 20.160 -22.637 20.674  1.00  9.04  ? 71   HIS A CD2 1 
ATOM   544  C  CE1 . HIS A 1 71  ? 19.878 -20.491 20.482  1.00  8.02  ? 71   HIS A CE1 1 
ATOM   545  N  NE2 . HIS A 1 71  ? 19.344 -21.584 20.999  1.00  9.81  ? 71   HIS A NE2 1 
ATOM   546  N  N   . GLY A 1 72  ? 23.072 -22.166 22.612  1.00  8.82  ? 72   GLY A N   1 
ATOM   547  C  CA  . GLY A 1 72  ? 22.702 -22.536 23.954  1.00  9.89  ? 72   GLY A CA  1 
ATOM   548  C  C   . GLY A 1 72  ? 21.793 -21.504 24.590  1.00  9.18  ? 72   GLY A C   1 
ATOM   549  O  O   . GLY A 1 72  ? 21.173 -20.715 23.872  1.00  11.21 ? 72   GLY A O   1 
ATOM   550  N  N   . GLY A 1 73  ? 21.590 -21.605 25.869  1.00  11.07 ? 73   GLY A N   1 
ATOM   551  C  CA  . GLY A 1 73  ? 20.848 -20.621 26.602  1.00  11.90 ? 73   GLY A CA  1 
ATOM   552  C  C   . GLY A 1 73  ? 21.758 -19.617 27.293  1.00  11.68 ? 73   GLY A C   1 
ATOM   553  O  O   . GLY A 1 73  ? 22.975 -19.783 27.390  1.00  11.70 ? 73   GLY A O   1 
ATOM   554  N  N   . PRO A 1 74  ? 21.157 -18.562 27.822  1.00  12.04 ? 74   PRO A N   1 
ATOM   555  C  CA  . PRO A 1 74  ? 21.947 -17.484 28.341  1.00  13.67 ? 74   PRO A CA  1 
ATOM   556  C  C   . PRO A 1 74  ? 22.758 -17.853 29.562  1.00  13.92 ? 74   PRO A C   1 
ATOM   557  O  O   . PRO A 1 74  ? 23.767 -17.188 29.804  1.00  16.76 ? 74   PRO A O   1 
ATOM   558  C  CB  . PRO A 1 74  ? 20.920 -16.407 28.655  1.00  14.92 ? 74   PRO A CB  1 
ATOM   559  C  CG  . PRO A 1 74  ? 19.620 -17.130 28.808  1.00  14.11 ? 74   PRO A CG  1 
ATOM   560  C  CD  . PRO A 1 74  ? 19.713 -18.272 27.856  1.00  12.99 ? 74   PRO A CD  1 
ATOM   561  N  N   . LYS A 1 75  ? 22.353 -18.890 30.298  1.00  12.63 ? 75   LYS A N   1 
ATOM   562  C  CA  . LYS A 1 75  ? 23.092 -19.359 31.460  1.00  15.03 ? 75   LYS A CA  1 
ATOM   563  C  C   . LYS A 1 75  ? 24.111 -20.430 31.163  1.00  14.39 ? 75   LYS A C   1 
ATOM   564  O  O   . LYS A 1 75  ? 24.770 -20.923 32.092  1.00  16.74 ? 75   LYS A O   1 
ATOM   565  C  CB  . LYS A 1 75  ? 22.123 -19.879 32.471  1.00  17.36 ? 75   LYS A CB  1 
ATOM   566  C  CG  . LYS A 1 75  ? 21.230 -18.782 33.058  1.00  20.41 ? 75   LYS A CG  1 
ATOM   567  C  CD  . LYS A 1 75  ? 21.916 -18.115 34.258  0.10  20.12 ? 75   LYS A CD  1 
ATOM   568  C  CE  . LYS A 1 75  ? 20.977 -17.213 35.057  0.10  19.61 ? 75   LYS A CE  1 
ATOM   569  N  NZ  . LYS A 1 75  ? 20.760 -15.891 34.408  0.10  19.57 ? 75   LYS A NZ  1 
ATOM   570  N  N   . ASP A 1 76  ? 24.314 -20.768 29.901  1.00  12.36 ? 76   ASP A N   1 
ATOM   571  C  CA  . ASP A 1 76  ? 25.299 -21.773 29.510  1.00  13.36 ? 76   ASP A CA  1 
ATOM   572  C  C   . ASP A 1 76  ? 26.598 -21.144 29.092  1.00  12.29 ? 76   ASP A C   1 
ATOM   573  O  O   . ASP A 1 76  ? 26.606 -20.075 28.498  1.00  13.10 ? 76   ASP A O   1 
ATOM   574  C  CB  . ASP A 1 76  ? 24.779 -22.593 28.305  1.00  13.70 ? 76   ASP A CB  1 
ATOM   575  C  CG  . ASP A 1 76  ? 23.504 -23.357 28.610  0.70  12.67 ? 76   ASP A CG  1 
ATOM   576  O  OD1 . ASP A 1 76  ? 23.304 -23.761 29.785  0.70  19.07 ? 76   ASP A OD1 1 
ATOM   577  O  OD2 . ASP A 1 76  ? 22.736 -23.573 27.651  0.70  15.13 ? 76   ASP A OD2 1 
ATOM   578  N  N   . GLU A 1 77  ? 27.702 -21.824 29.372  1.00  12.03 ? 77   GLU A N   1 
ATOM   579  C  CA  . GLU A 1 77  ? 28.967 -21.387 28.804  1.00  12.06 ? 77   GLU A CA  1 
ATOM   580  C  C   . GLU A 1 77  ? 29.022 -21.564 27.279  1.00  11.62 ? 77   GLU A C   1 
ATOM   581  O  O   . GLU A 1 77  ? 29.515 -20.694 26.564  1.00  12.30 ? 77   GLU A O   1 
ATOM   582  C  CB  . GLU A 1 77  ? 30.081 -22.201 29.471  1.00  12.81 ? 77   GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 77  ? 31.456 -21.721 29.131  1.00  15.53 ? 77   GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 77  ? 32.562 -22.232 30.066  1.00  17.74 ? 77   GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 77  ? 32.518 -23.424 30.416  1.00  22.48 ? 77   GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 77  ? 33.498 -21.421 30.441  1.00  23.64 ? 77   GLU A OE2 1 
ATOM   587  N  N   . GLU A 1 78  ? 28.495 -22.681 26.764  1.00  10.94 ? 78   GLU A N   1 
ATOM   588  C  CA  . GLU A 1 78  ? 28.455 -22.945 25.326  1.00  10.84 ? 78   GLU A CA  1 
ATOM   589  C  C   . GLU A 1 78  ? 27.159 -22.299 24.785  1.00  10.98 ? 78   GLU A C   1 
ATOM   590  O  O   . GLU A 1 78  ? 26.050 -22.823 24.944  1.00  11.42 ? 78   GLU A O   1 
ATOM   591  C  CB  . GLU A 1 78  ? 28.482 -24.424 25.024  1.00  12.46 ? 78   GLU A CB  1 
ATOM   592  C  CG  . GLU A 1 78  ? 28.601 -24.726 23.556  1.00  14.47 ? 78   GLU A CG  1 
ATOM   593  C  CD  . GLU A 1 78  ? 30.018 -24.455 22.975  1.00  18.66 ? 78   GLU A CD  1 
ATOM   594  O  OE1 . GLU A 1 78  ? 31.004 -24.368 23.777  1.00  23.93 ? 78   GLU A OE1 1 
ATOM   595  O  OE2 . GLU A 1 78  ? 30.168 -24.360 21.740  1.00  21.16 ? 78   GLU A OE2 1 
ATOM   596  N  N   . ARG A 1 79  ? 27.326 -21.121 24.159  1.00  8.96  ? 79   ARG A N   1 
ATOM   597  C  CA  . ARG A 1 79  ? 26.223 -20.331 23.608  1.00  8.81  ? 79   ARG A CA  1 
ATOM   598  C  C   . ARG A 1 79  ? 26.825 -19.411 22.575  1.00  7.88  ? 79   ARG A C   1 
ATOM   599  O  O   . ARG A 1 79  ? 27.984 -19.127 22.589  1.00  9.80  ? 79   ARG A O   1 
ATOM   600  C  CB  . ARG A 1 79  ? 25.505 -19.537 24.664  1.00  9.04  ? 79   ARG A CB  1 
ATOM   601  C  CG  . ARG A 1 79  ? 26.436 -18.583 25.433  1.00  10.17 ? 79   ARG A CG  1 
ATOM   602  C  CD  . ARG A 1 79  ? 25.734 -17.603 26.338  1.00  9.78  ? 79   ARG A CD  1 
ATOM   603  N  NE  . ARG A 1 79  ? 25.241 -16.431 25.608  1.00  9.51  ? 79   ARG A NE  1 
ATOM   604  C  CZ  . ARG A 1 79  ? 24.766 -15.357 26.195  1.00  9.85  ? 79   ARG A CZ  1 
ATOM   605  N  NH1 . ARG A 1 79  ? 24.594 -15.342 27.493  1.00  10.63 ? 79   ARG A NH1 1 
ATOM   606  N  NH2 . ARG A 1 79  ? 24.435 -14.283 25.493  1.00  9.72  ? 79   ARG A NH2 1 
ATOM   607  N  N   . HIS A 1 80  ? 25.980 -18.926 21.679  1.00  7.59  ? 80   HIS A N   1 
ATOM   608  C  CA  . HIS A 1 80  ? 26.266 -17.795 20.808  1.00  8.04  ? 80   HIS A CA  1 
ATOM   609  C  C   . HIS A 1 80  ? 26.179 -16.518 21.637  1.00  8.43  ? 80   HIS A C   1 
ATOM   610  O  O   . HIS A 1 80  ? 25.393 -16.435 22.561  1.00  8.57  ? 80   HIS A O   1 
ATOM   611  C  CB  . HIS A 1 80  ? 25.225 -17.729 19.678  1.00  7.58  ? 80   HIS A CB  1 
ATOM   612  C  CG  . HIS A 1 80  ? 25.100 -18.980 18.876  1.00  8.30  ? 80   HIS A CG  1 
ATOM   613  N  ND1 . HIS A 1 80  ? 23.900 -19.423 18.362  1.00  8.04  ? 80   HIS A ND1 1 
ATOM   614  C  CD2 . HIS A 1 80  ? 26.053 -19.847 18.457  1.00  10.77 ? 80   HIS A CD2 1 
ATOM   615  C  CE1 . HIS A 1 80  ? 24.153 -20.471 17.580  1.00  10.75 ? 80   HIS A CE1 1 
ATOM   616  N  NE2 . HIS A 1 80  ? 25.445 -20.758 17.644  1.00  11.92 ? 80   HIS A NE2 1 
ATOM   617  N  N   . VAL A 1 81  ? 26.920 -15.510 21.234  1.00  8.38  ? 81   VAL A N   1 
ATOM   618  C  CA  . VAL A 1 81  ? 26.785 -14.227 21.876  1.00  8.55  ? 81   VAL A CA  1 
ATOM   619  C  C   . VAL A 1 81  ? 25.342 -13.775 21.893  1.00  8.77  ? 81   VAL A C   1 
ATOM   620  O  O   . VAL A 1 81  ? 24.867 -13.225 22.865  1.00  9.43  ? 81   VAL A O   1 
ATOM   621  C  CB  . VAL A 1 81  ? 27.723 -13.157 21.276  1.00  9.79  ? 81   VAL A CB  1 
ATOM   622  C  CG1 . VAL A 1 81  ? 27.386 -11.758 21.818  1.00  10.86 ? 81   VAL A CG1 1 
ATOM   623  C  CG2 . VAL A 1 81  ? 29.196 -13.502 21.618  1.00  10.60 ? 81   VAL A CG2 1 
ATOM   624  N  N   . GLY A 1 82  ? 24.628 -13.955 20.796  1.00  8.16  ? 82   GLY A N   1 
ATOM   625  C  CA  . GLY A 1 82  ? 23.232 -13.509 20.684  1.00  8.37  ? 82   GLY A CA  1 
ATOM   626  C  C   . GLY A 1 82  ? 22.178 -14.330 21.349  1.00  8.75  ? 82   GLY A C   1 
ATOM   627  O  O   . GLY A 1 82  ? 21.026 -13.984 21.221  1.00  10.24 ? 82   GLY A O   1 
ATOM   628  N  N   . ASP A 1 83  ? 22.528 -15.341 22.120  1.00  8.06  ? 83   ASP A N   1 
ATOM   629  C  CA  . ASP A 1 83  ? 21.549 -16.210 22.733  1.00  8.44  ? 83   ASP A CA  1 
ATOM   630  C  C   . ASP A 1 83  ? 21.039 -15.678 24.042  1.00  9.17  ? 83   ASP A C   1 
ATOM   631  O  O   . ASP A 1 83  ? 21.549 -16.034 25.118  1.00  11.71 ? 83   ASP A O   1 
ATOM   632  C  CB  . ASP A 1 83  ? 22.185 -17.595 22.949  1.00  8.38  ? 83   ASP A CB  1 
ATOM   633  C  CG  . ASP A 1 83  ? 22.395 -18.368 21.671  1.00  9.04  ? 83   ASP A CG  1 
ATOM   634  O  OD1 . ASP A 1 83  ? 21.861 -17.914 20.602  1.00  8.31  ? 83   ASP A OD1 1 
ATOM   635  O  OD2 . ASP A 1 83  ? 23.198 -19.340 21.709  1.00  8.88  ? 83   ASP A OD2 1 
ATOM   636  N  N   . LEU A 1 84  ? 19.914 -14.961 24.001  1.00  8.54  ? 84   LEU A N   1 
ATOM   637  C  CA  . LEU A 1 84  ? 19.300 -14.362 25.176  1.00  9.13  ? 84   LEU A CA  1 
ATOM   638  C  C   . LEU A 1 84  ? 18.117 -15.188 25.689  1.00  10.70 ? 84   LEU A C   1 
ATOM   639  O  O   . LEU A 1 84  ? 17.380 -14.707 26.544  1.00  13.16 ? 84   LEU A O   1 
ATOM   640  C  CB  . LEU A 1 84  ? 18.890 -12.916 24.899  1.00  9.17  ? 84   LEU A CB  1 
ATOM   641  C  CG  . LEU A 1 84  ? 20.076 -11.984 24.526  1.00  11.81 ? 84   LEU A CG  1 
ATOM   642  C  CD1 . LEU A 1 84  ? 19.554 -10.608 24.221  1.00  13.90 ? 84   LEU A CD1 1 
ATOM   643  C  CD2 . LEU A 1 84  ? 21.061 -11.979 25.768  1.00  14.52 ? 84   LEU A CD2 1 
ATOM   644  N  N   . GLY A 1 85  ? 17.949 -16.403 25.233  1.00  9.36  ? 85   GLY A N   1 
ATOM   645  C  CA  . GLY A 1 85  ? 16.989 -17.322 25.836  1.00  10.50 ? 85   GLY A CA  1 
ATOM   646  C  C   . GLY A 1 85  ? 15.592 -17.073 25.356  1.00  9.38  ? 85   GLY A C   1 
ATOM   647  O  O   . GLY A 1 85  ? 15.303 -17.008 24.164  1.00  10.02 ? 85   GLY A O   1 
ATOM   648  N  N   . ASN A 1 86  ? 14.685 -16.956 26.291  1.00  8.59  ? 86   ASN A N   1 
ATOM   649  C  CA  . ASN A 1 86  ? 13.271 -16.797 26.048  1.00  9.08  ? 86   ASN A CA  1 
ATOM   650  C  C   . ASN A 1 86  ? 12.705 -15.631 26.834  1.00  9.15  ? 86   ASN A C   1 
ATOM   651  O  O   . ASN A 1 86  ? 13.157 -15.364 27.935  1.00  12.03 ? 86   ASN A O   1 
ATOM   652  C  CB  . ASN A 1 86  ? 12.485 -18.068 26.482  1.00  9.59  ? 86   ASN A CB  1 
ATOM   653  C  CG  . ASN A 1 86  ? 12.762 -19.215 25.547  1.00  9.49  ? 86   ASN A CG  1 
ATOM   654  O  OD1 . ASN A 1 86  ? 12.317 -19.164 24.388  1.00  10.06 ? 86   ASN A OD1 1 
ATOM   655  N  ND2 . ASN A 1 86  ? 13.448 -20.257 26.027  1.00  10.67 ? 86   ASN A ND2 1 
ATOM   656  N  N   . VAL A 1 87  ? 11.695 -14.977 26.299  1.00  8.56  ? 87   VAL A N   1 
ATOM   657  C  CA  . VAL A 1 87  ? 10.850 -14.065 27.038  1.00  9.31  ? 87   VAL A CA  1 
ATOM   658  C  C   . VAL A 1 87  ? 9.488  -14.725 27.288  1.00  9.11  ? 87   VAL A C   1 
ATOM   659  O  O   . VAL A 1 87  ? 9.103  -15.593 26.534  1.00  10.54 ? 87   VAL A O   1 
ATOM   660  C  CB  . VAL A 1 87  ? 10.724 -12.714 26.359  1.00  10.81 ? 87   VAL A CB  1 
ATOM   661  C  CG1 . VAL A 1 87  ? 12.116 -12.028 26.267  1.00  12.78 ? 87   VAL A CG1 1 
ATOM   662  C  CG2 . VAL A 1 87  ? 10.033 -12.815 25.035  1.00  11.76 ? 87   VAL A CG2 1 
ATOM   663  N  N   . THR A 1 88  ? 8.795  -14.354 28.350  1.00  8.84  ? 88   THR A N   1 
ATOM   664  C  CA  . THR A 1 88  ? 7.542  -15.034 28.736  1.00  9.37  ? 88   THR A CA  1 
ATOM   665  C  C   . THR A 1 88  ? 6.406  -14.046 28.654  1.00  9.83  ? 88   THR A C   1 
ATOM   666  O  O   . THR A 1 88  ? 6.421  -13.035 29.335  1.00  9.97  ? 88   THR A O   1 
ATOM   667  C  CB  . THR A 1 88  ? 7.648  -15.642 30.139  1.00  10.66 ? 88   THR A CB  1 
ATOM   668  O  OG1 . THR A 1 88  ? 8.674  -16.630 30.155  1.00  12.56 ? 88   THR A OG1 1 
ATOM   669  C  CG2 . THR A 1 88  ? 6.350  -16.302 30.549  1.00  12.39 ? 88   THR A CG2 1 
ATOM   670  N  N   . ALA A 1 89  ? 5.403  -14.380 27.856  1.00  10.13 ? 89   ALA A N   1 
ATOM   671  C  CA  . ALA A 1 89  ? 4.189  -13.567 27.723  1.00  11.20 ? 89   ALA A CA  1 
ATOM   672  C  C   . ALA A 1 89  ? 3.075  -14.178 28.595  1.00  10.06 ? 89   ALA A C   1 
ATOM   673  O  O   . ALA A 1 89  ? 2.924  -15.381 28.737  1.00  10.77 ? 89   ALA A O   1 
ATOM   674  C  CB  . ALA A 1 89  ? 3.734  -13.515 26.287  1.00  11.38 ? 89   ALA A CB  1 
ATOM   675  N  N   . ASP A 1 90  ? 2.251  -13.301 29.140  1.00  11.83 ? 90   ASP A N   1 
ATOM   676  C  CA  . ASP A 1 90  ? 1.070  -13.676 29.860  1.00  13.08 ? 90   ASP A CA  1 
ATOM   677  C  C   . ASP A 1 90  ? -0.140 -13.827 28.963  1.00  12.79 ? 90   ASP A C   1 
ATOM   678  O  O   . ASP A 1 90  ? -0.023 -13.713 27.737  1.00  13.47 ? 90   ASP A O   1 
ATOM   679  C  CB  . ASP A 1 90  ? 0.802  -12.672 30.976  1.00  15.46 ? 90   ASP A CB  1 
ATOM   680  C  CG  . ASP A 1 90  ? 0.513  -11.294 30.501  0.40  12.22 ? 90   ASP A CG  1 
ATOM   681  O  OD1 . ASP A 1 90  ? 0.170  -11.082 29.331  0.40  11.04 ? 90   ASP A OD1 1 
ATOM   682  O  OD2 . ASP A 1 90  ? 0.630  -10.379 31.354  0.40  14.15 ? 90   ASP A OD2 1 
ATOM   683  N  N   . LYS A 1 91  ? -1.334 -14.095 29.559  1.00  14.98 ? 91   LYS A N   1 
ATOM   684  C  CA  . LYS A 1 91  ? -2.549 -14.224 28.733  1.00  16.74 ? 91   LYS A CA  1 
ATOM   685  C  C   . LYS A 1 91  ? -2.908 -13.004 27.967  1.00  17.33 ? 91   LYS A C   1 
ATOM   686  O  O   . LYS A 1 91  ? -3.589 -13.107 26.963  1.00  21.57 ? 91   LYS A O   1 
ATOM   687  C  CB  . LYS A 1 91  ? -3.783 -14.509 29.617  1.00  18.76 ? 91   LYS A CB  1 
ATOM   688  C  CG  . LYS A 1 91  ? -4.000 -15.912 30.025  1.00  21.61 ? 91   LYS A CG  1 
ATOM   689  C  CD  . LYS A 1 91  ? -4.417 -16.800 28.855  1.00  22.07 ? 91   LYS A CD  1 
ATOM   690  C  CE  . LYS A 1 91  ? -5.205 -18.071 29.219  1.00  22.58 ? 91   LYS A CE  1 
ATOM   691  N  NZ  . LYS A 1 91  ? -4.353 -19.022 30.010  0.50  16.53 ? 91   LYS A NZ  1 
ATOM   692  N  N   . ASP A 1 92  ? -2.539 -11.842 28.458  1.00  16.52 ? 92   ASP A N   1 
ATOM   693  C  CA  . ASP A 1 92  ? -2.819 -10.664 27.673  1.00  17.98 ? 92   ASP A CA  1 
ATOM   694  C  C   . ASP A 1 92  ? -1.882 -10.489 26.501  1.00  16.88 ? 92   ASP A C   1 
ATOM   695  O  O   . ASP A 1 92  ? -2.083 -9.517  25.757  1.00  19.13 ? 92   ASP A O   1 
ATOM   696  C  CB  . ASP A 1 92  ? -2.807 -9.381  28.455  1.00  19.37 ? 92   ASP A CB  1 
ATOM   697  C  CG  A ASP A 1 92  ? -1.933 -9.363  29.651  0.60  20.60 ? 92   ASP A CG  1 
ATOM   698  C  CG  B ASP A 1 92  ? -3.689 -9.419  29.689  0.40  18.19 ? 92   ASP A CG  1 
ATOM   699  O  OD1 A ASP A 1 92  ? -0.677 -9.493  29.434  0.60  23.82 ? 92   ASP A OD1 1 
ATOM   700  O  OD1 B ASP A 1 92  ? -4.753 -10.058 29.534  0.40  21.41 ? 92   ASP A OD1 1 
ATOM   701  O  OD2 A ASP A 1 92  ? -2.455 -9.166  30.789  0.60  27.16 ? 92   ASP A OD2 1 
ATOM   702  O  OD2 B ASP A 1 92  ? -3.394 -8.807  30.727  0.40  18.20 ? 92   ASP A OD2 1 
ATOM   703  N  N   . GLY A 1 93  ? -0.882 -11.358 26.339  1.00  15.60 ? 93   GLY A N   1 
ATOM   704  C  CA  . GLY A 1 93  ? 0.053  -11.201 25.239  1.00  14.54 ? 93   GLY A CA  1 
ATOM   705  C  C   . GLY A 1 93  ? 1.249  -10.311 25.515  1.00  13.67 ? 93   GLY A C   1 
ATOM   706  O  O   . GLY A 1 93  ? 2.019  -10.031 24.610  1.00  14.18 ? 93   GLY A O   1 
ATOM   707  N  N   . VAL A 1 94  ? 1.437  -9.899  26.761  1.00  13.31 ? 94   VAL A N   1 
ATOM   708  C  CA  . VAL A 1 94  ? 2.514  -9.012  27.133  1.00  13.30 ? 94   VAL A CA  1 
ATOM   709  C  C   . VAL A 1 94  ? 3.637  -9.750  27.844  1.00  12.73 ? 94   VAL A C   1 
ATOM   710  O  O   . VAL A 1 94  ? 3.405  -10.510 28.769  1.00  12.75 ? 94   VAL A O   1 
ATOM   711  C  CB  . VAL A 1 94  ? 2.025  -7.877  28.054  1.00  15.41 ? 94   VAL A CB  1 
ATOM   712  C  CG1 . VAL A 1 94  ? 3.181  -6.950  28.363  1.00  18.31 ? 94   VAL A CG1 1 
ATOM   713  C  CG2 . VAL A 1 94  ? 0.887  -7.103  27.419  1.00  18.96 ? 94   VAL A CG2 1 
ATOM   714  N  N   . ALA A 1 95  ? 4.853  -9.587  27.310  1.00  11.48 ? 95   ALA A N   1 
ATOM   715  C  CA  . ALA A 1 95  ? 6.096  -10.038 27.949  1.00  12.07 ? 95   ALA A CA  1 
ATOM   716  C  C   . ALA A 1 95  ? 6.805  -8.838  28.546  1.00  13.46 ? 95   ALA A C   1 
ATOM   717  O  O   . ALA A 1 95  ? 7.207  -7.921  27.832  1.00  15.10 ? 95   ALA A O   1 
ATOM   718  C  CB  . ALA A 1 95  ? 7.009  -10.738 27.013  1.00  12.32 ? 95   ALA A CB  1 
ATOM   719  N  N   . ASP A 1 96  ? 6.992  -8.845  29.835  1.00  13.16 ? 96   ASP A N   1 
ATOM   720  C  CA  . ASP A 1 96  ? 7.835  -7.868  30.485  1.00  13.55 ? 96   ASP A CA  1 
ATOM   721  C  C   . ASP A 1 96  ? 9.223  -8.479  30.548  1.00  14.68 ? 96   ASP A C   1 
ATOM   722  O  O   . ASP A 1 96  ? 9.422  -9.592  31.070  1.00  18.48 ? 96   ASP A O   1 
ATOM   723  C  CB  . ASP A 1 96  ? 7.271  -7.507  31.877  1.00  16.40 ? 96   ASP A CB  1 
ATOM   724  C  CG  . ASP A 1 96  ? 6.051  -6.598  31.809  0.50  16.46 ? 96   ASP A CG  1 
ATOM   725  O  OD1 . ASP A 1 96  ? 5.865  -5.855  30.808  0.30  13.61 ? 96   ASP A OD1 1 
ATOM   726  O  OD2 . ASP A 1 96  ? 5.310  -6.591  32.830  0.30  17.90 ? 96   ASP A OD2 1 
ATOM   727  N  N   . VAL A 1 97  ? 10.190 -7.805  29.985  1.00  12.57 ? 97   VAL A N   1 
ATOM   728  C  CA  . VAL A 1 97  ? 11.520 -8.317  29.796  1.00  13.26 ? 97   VAL A CA  1 
ATOM   729  C  C   . VAL A 1 97  ? 12.367 -7.658  30.839  1.00  12.22 ? 97   VAL A C   1 
ATOM   730  O  O   . VAL A 1 97  ? 12.401 -6.417  30.965  1.00  11.79 ? 97   VAL A O   1 
ATOM   731  C  CB  . VAL A 1 97  ? 12.051 -8.059  28.371  1.00  14.06 ? 97   VAL A CB  1 
ATOM   732  C  CG1 . VAL A 1 97  ? 13.442 -8.630  28.196  1.00  14.84 ? 97   VAL A CG1 1 
ATOM   733  C  CG2 . VAL A 1 97  ? 11.076 -8.695  27.343  1.00  15.31 ? 97   VAL A CG2 1 
ATOM   734  N  N   . SER A 1 98  ? 13.164 -8.458  31.523  1.00  14.66 ? 98   SER A N   1 
ATOM   735  C  CA  . SER A 1 98  ? 14.135 -7.963  32.461  1.00  16.55 ? 98   SER A CA  1 
ATOM   736  C  C   . SER A 1 98  ? 15.250 -9.030  32.557  1.00  16.68 ? 98   SER A C   1 
ATOM   737  O  O   . SER A 1 98  ? 15.075 -10.101 33.190  1.00  18.86 ? 98   SER A O   1 
ATOM   738  C  CB  . SER A 1 98  ? 13.534 -7.683  33.817  1.00  20.54 ? 98   SER A CB  1 
ATOM   739  O  OG  . SER A 1 98  ? 14.472 -7.035  34.668  1.00  27.14 ? 98   SER A OG  1 
ATOM   740  N  N   . ILE A 1 99  ? 16.386 -8.760  31.954  1.00  14.97 ? 99   ILE A N   1 
ATOM   741  C  CA  . ILE A 1 99  ? 17.514 -9.722  31.790  1.00  15.48 ? 99   ILE A CA  1 
ATOM   742  C  C   . ILE A 1 99  ? 18.748 -8.913  32.259  1.00  14.12 ? 99   ILE A C   1 
ATOM   743  O  O   . ILE A 1 99  ? 18.862 -7.695  31.998  1.00  14.98 ? 99   ILE A O   1 
ATOM   744  C  CB  . ILE A 1 99  ? 17.606 -10.126 30.221  1.00  15.03 ? 99   ILE A CB  1 
ATOM   745  C  CG1 . ILE A 1 99  ? 16.363 -10.949 29.758  1.00  19.21 ? 99   ILE A CG1 1 
ATOM   746  C  CG2 . ILE A 1 99  ? 18.913 -10.793 29.837  1.00  19.99 ? 99   ILE A CG2 1 
ATOM   747  C  CD1 . ILE A 1 99  ? 16.325 -11.284 28.288  1.00  19.72 ? 99   ILE A CD1 1 
ATOM   748  N  N   . GLU A 1 100 ? 19.740 -9.562  32.842  1.00  13.30 ? 100  GLU A N   1 
ATOM   749  C  CA  . GLU A 1 100 ? 21.104 -9.047  32.859  1.00  13.17 ? 100  GLU A CA  1 
ATOM   750  C  C   . GLU A 1 100 ? 21.974 -10.072 32.142  1.00  11.45 ? 100  GLU A C   1 
ATOM   751  O  O   . GLU A 1 100 ? 21.820 -11.267 32.371  1.00  13.74 ? 100  GLU A O   1 
ATOM   752  C  CB  . GLU A 1 100 ? 21.611 -8.859  34.291  1.00  16.48 ? 100  GLU A CB  1 
ATOM   753  C  CG  . GLU A 1 100 ? 21.109 -7.610  35.011  1.00  19.97 ? 100  GLU A CG  1 
ATOM   754  C  CD  . GLU A 1 100 ? 21.986 -7.102  36.153  0.20  16.18 ? 100  GLU A CD  1 
ATOM   755  O  OE1 . GLU A 1 100 ? 23.073 -7.665  36.417  0.20  16.32 ? 100  GLU A OE1 1 
ATOM   756  O  OE2 . GLU A 1 100 ? 21.559 -6.102  36.785  0.20  16.27 ? 100  GLU A OE2 1 
ATOM   757  N  N   . ASP A 1 101 ? 22.823 -9.622  31.227  1.00  11.12 ? 101  ASP A N   1 
ATOM   758  C  CA  . ASP A 1 101 ? 23.665 -10.529 30.460  1.00  10.06 ? 101  ASP A CA  1 
ATOM   759  C  C   . ASP A 1 101 ? 25.080 -9.971  30.367  1.00  10.37 ? 101  ASP A C   1 
ATOM   760  O  O   . ASP A 1 101 ? 25.262 -8.799  30.071  1.00  11.69 ? 101  ASP A O   1 
ATOM   761  C  CB  . ASP A 1 101 ? 23.070 -10.790 29.065  1.00  12.04 ? 101  ASP A CB  1 
ATOM   762  C  CG  . ASP A 1 101 ? 23.737 -11.951 28.353  1.00  12.57 ? 101  ASP A CG  1 
ATOM   763  O  OD1 . ASP A 1 101 ? 23.312 -13.110 28.694  1.00  17.35 ? 101  ASP A OD1 1 
ATOM   764  O  OD2 . ASP A 1 101 ? 24.687 -11.777 27.569  1.00  12.86 ? 101  ASP A OD2 1 
ATOM   765  N  N   . SER A 1 102 ? 26.094 -10.819 30.562  1.00  10.35 ? 102  SER A N   1 
ATOM   766  C  CA  . SER A 1 102 ? 27.480 -10.376 30.536  1.00  10.97 ? 102  SER A CA  1 
ATOM   767  C  C   . SER A 1 102 ? 28.237 -10.873 29.345  1.00  10.43 ? 102  SER A C   1 
ATOM   768  O  O   . SER A 1 102 ? 29.415 -10.599 29.245  1.00  12.94 ? 102  SER A O   1 
ATOM   769  C  CB  . SER A 1 102 ? 28.226 -10.765 31.824  1.00  13.26 ? 102  SER A CB  1 
ATOM   770  O  OG  . SER A 1 102 ? 27.789 -9.933  32.890  1.00  16.32 ? 102  SER A OG  1 
ATOM   771  N  N   . VAL A 1 103 ? 27.597 -11.567 28.411  1.00  10.31 ? 103  VAL A N   1 
ATOM   772  C  CA  . VAL A 1 103 ? 28.231 -11.992 27.172  1.00  10.08 ? 103  VAL A CA  1 
ATOM   773  C  C   . VAL A 1 103 ? 28.027 -10.972 26.071  1.00  10.06 ? 103  VAL A C   1 
ATOM   774  O  O   . VAL A 1 103 ? 28.952 -10.658 25.340  1.00  12.04 ? 103  VAL A O   1 
ATOM   775  C  CB  . VAL A 1 103 ? 27.743 -13.403 26.767  1.00  10.96 ? 103  VAL A CB  1 
ATOM   776  C  CG1 . VAL A 1 103 ? 28.327 -13.839 25.465  1.00  12.38 ? 103  VAL A CG1 1 
ATOM   777  C  CG2 . VAL A 1 103 ? 28.095 -14.429 27.858  1.00  11.85 ? 103  VAL A CG2 1 
ATOM   778  N  N   . ILE A 1 104 ? 26.828 -10.449 25.895  1.00  9.69  ? 104  ILE A N   1 
ATOM   779  C  CA  . ILE A 1 104 ? 26.643 -9.303  25.019  1.00  9.54  ? 104  ILE A CA  1 
ATOM   780  C  C   . ILE A 1 104 ? 27.376 -8.097  25.571  1.00  9.96  ? 104  ILE A C   1 
ATOM   781  O  O   . ILE A 1 104 ? 27.667 -8.034  26.796  1.00  10.60 ? 104  ILE A O   1 
ATOM   782  C  CB  . ILE A 1 104 ? 25.150 -8.995  24.829  1.00  9.87  ? 104  ILE A CB  1 
ATOM   783  C  CG1 . ILE A 1 104 ? 24.466 -8.619  26.120  1.00  10.35 ? 104  ILE A CG1 1 
ATOM   784  C  CG2 . ILE A 1 104 ? 24.444 -10.155 24.050  1.00  10.15 ? 104  ILE A CG2 1 
ATOM   785  C  CD1 . ILE A 1 104 ? 23.039 -8.082  25.931  1.00  10.80 ? 104  ILE A CD1 1 
ATOM   786  N  N   . SER A 1 105 ? 27.650 -7.139  24.695  1.00  9.65  ? 105  SER A N   1 
ATOM   787  C  CA  . SER A 1 105 ? 28.301 -5.878  25.108  1.00  10.27 ? 105  SER A CA  1 
ATOM   788  C  C   . SER A 1 105 ? 27.750 -4.777  24.220  1.00  9.92  ? 105  SER A C   1 
ATOM   789  O  O   . SER A 1 105 ? 27.191 -5.048  23.151  1.00  9.80  ? 105  SER A O   1 
ATOM   790  C  CB  . SER A 1 105 ? 29.790 -5.994  24.938  1.00  12.08 ? 105  SER A CB  1 
ATOM   791  O  OG  . SER A 1 105 ? 30.376 -4.848  25.598  1.00  15.54 ? 105  SER A OG  1 
ATOM   792  N  N   . LEU A 1 106 ? 27.898 -3.529  24.673  1.00  11.06 ? 106  LEU A N   1 
ATOM   793  C  CA  . LEU A 1 106 ? 27.561 -2.382  23.862  1.00  12.09 ? 106  LEU A CA  1 
ATOM   794  C  C   . LEU A 1 106 ? 28.845 -1.726  23.317  1.00  13.86 ? 106  LEU A C   1 
ATOM   795  O  O   . LEU A 1 106 ? 28.770 -0.645  22.722  1.00  17.32 ? 106  LEU A O   1 
ATOM   796  C  CB  . LEU A 1 106 ? 26.685 -1.373  24.591  1.00  12.16 ? 106  LEU A CB  1 
ATOM   797  C  CG  . LEU A 1 106 ? 25.385 -1.938  25.146  1.00  12.34 ? 106  LEU A CG  1 
ATOM   798  C  CD1 . LEU A 1 106 ? 24.569 -0.854  25.865  1.00  14.31 ? 106  LEU A CD1 1 
ATOM   799  C  CD2 . LEU A 1 106 ? 24.561 -2.553  24.080  1.00  13.13 ? 106  LEU A CD2 1 
ATOM   800  N  N   . SER A 1 107 ? 29.994 -2.419  23.368  1.00  15.93 ? 107  SER A N   1 
ATOM   801  C  CA  . SER A 1 107 ? 31.250 -2.030  22.670  1.00  17.91 ? 107  SER A CA  1 
ATOM   802  C  C   . SER A 1 107 ? 32.133 -3.256  22.369  1.00  17.99 ? 107  SER A C   1 
ATOM   803  O  O   . SER A 1 107 ? 31.897 -4.339  22.873  1.00  18.60 ? 107  SER A O   1 
ATOM   804  C  CB  . SER A 1 107 ? 32.065 -1.070  23.524  0.81  20.51 ? 107  SER A CB  1 
ATOM   805  O  OG  . SER A 1 107 ? 32.648 -1.731  24.628  0.81  24.68 ? 107  SER A OG  1 
ATOM   806  N  N   . GLY A 1 108 ? 33.165 -3.080  21.552  1.00  19.90 ? 108  GLY A N   1 
ATOM   807  C  CA  . GLY A 1 108 ? 34.093 -4.171  21.249  1.00  18.75 ? 108  GLY A CA  1 
ATOM   808  C  C   . GLY A 1 108 ? 33.600 -5.316  20.374  1.00  18.83 ? 108  GLY A C   1 
ATOM   809  O  O   . GLY A 1 108 ? 32.608 -5.178  19.665  1.00  19.10 ? 108  GLY A O   1 
ATOM   810  N  N   . ASP A 1 109 ? 34.302 -6.450  20.390  1.00  19.81 ? 109  ASP A N   1 
ATOM   811  C  CA  . ASP A 1 109 ? 33.980 -7.534  19.490  1.00  19.38 ? 109  ASP A CA  1 
ATOM   812  C  C   . ASP A 1 109 ? 32.603 -8.194  19.747  1.00  18.34 ? 109  ASP A C   1 
ATOM   813  O  O   . ASP A 1 109 ? 32.021 -8.833  18.833  1.00  19.95 ? 109  ASP A O   1 
ATOM   814  C  CB  . ASP A 1 109 ? 35.085 -8.621  19.512  1.00  22.19 ? 109  ASP A CB  1 
ATOM   815  C  CG  . ASP A 1 109 ? 34.576 -9.976  18.972  0.78  24.45 ? 109  ASP A CG  1 
ATOM   816  O  OD1 . ASP A 1 109 ? 33.444 -10.383 19.305  0.78  29.83 ? 109  ASP A OD1 1 
ATOM   817  O  OD2 . ASP A 1 109 ? 35.231 -10.650 18.187  0.78  27.91 ? 109  ASP A OD2 1 
ATOM   818  N  N   . HIS A 1 110 ? 32.123 -8.110  20.972  1.00  15.13 ? 110  HIS A N   1 
ATOM   819  C  CA  . HIS A 1 110 ? 30.820 -8.683  21.293  1.00  14.52 ? 110  HIS A CA  1 
ATOM   820  C  C   . HIS A 1 110 ? 29.711 -7.657  21.180  1.00  12.47 ? 110  HIS A C   1 
ATOM   821  O  O   . HIS A 1 110 ? 28.614 -7.866  21.686  1.00  12.31 ? 110  HIS A O   1 
ATOM   822  C  CB  . HIS A 1 110 ? 30.782 -9.242  22.695  1.00  16.32 ? 110  HIS A CB  1 
ATOM   823  C  CG  . HIS A 1 110 ? 31.558 -10.495 22.848  0.71  20.13 ? 110  HIS A CG  1 
ATOM   824  N  ND1 . HIS A 1 110 ? 31.395 -11.354 23.914  0.71  19.84 ? 110  HIS A ND1 1 
ATOM   825  C  CD2 . HIS A 1 110 ? 32.418 -11.095 22.003  0.71  23.60 ? 110  HIS A CD2 1 
ATOM   826  C  CE1 . HIS A 1 110 ? 32.196 -12.394 23.749  0.71  22.13 ? 110  HIS A CE1 1 
ATOM   827  N  NE2 . HIS A 1 110 ? 32.818 -12.269 22.591  0.71  25.39 ? 110  HIS A NE2 1 
ATOM   828  N  N   . CYS A 1 111 ? 30.021 -6.522  20.575  1.00  12.47 ? 111  CYS A N   1 
ATOM   829  C  CA  . CYS A 1 111 ? 29.031 -5.455  20.484  1.00  12.17 ? 111  CYS A CA  1 
ATOM   830  C  C   . CYS A 1 111 ? 27.857 -5.819  19.607  1.00  9.77  ? 111  CYS A C   1 
ATOM   831  O  O   . CYS A 1 111 ? 27.981 -6.385  18.549  1.00  11.13 ? 111  CYS A O   1 
ATOM   832  C  CB  . CYS A 1 111 ? 29.725 -4.195  19.911  1.00  14.01 ? 111  CYS A CB  1 
ATOM   833  S  SG  . CYS A 1 111 ? 28.702 -2.766  19.882  1.00  19.14 ? 111  CYS A SG  1 
ATOM   834  N  N   . ILE A 1 112 ? 26.687 -5.479  20.117  1.00  7.87  ? 112  ILE A N   1 
ATOM   835  C  CA  . ILE A 1 112 ? 25.410 -5.800  19.473  1.00  8.11  ? 112  ILE A CA  1 
ATOM   836  C  C   . ILE A 1 112 ? 24.781 -4.569  18.806  1.00  7.76  ? 112  ILE A C   1 
ATOM   837  O  O   . ILE A 1 112 ? 23.764 -4.685  18.175  1.00  7.63  ? 112  ILE A O   1 
ATOM   838  C  CB  . ILE A 1 112 ? 24.432 -6.469  20.417  1.00  8.42  ? 112  ILE A CB  1 
ATOM   839  C  CG1 . ILE A 1 112 ? 24.031 -5.535  21.558  1.00  9.67  ? 112  ILE A CG1 1 
ATOM   840  C  CG2 . ILE A 1 112 ? 25.001 -7.846  20.893  1.00  9.76  ? 112  ILE A CG2 1 
ATOM   841  C  CD1 . ILE A 1 112 ? 22.934 -6.145  22.434  1.00  11.64 ? 112  ILE A CD1 1 
ATOM   842  N  N   . ILE A 1 113 ? 25.380 -3.404  18.967  1.00  8.36  ? 113  ILE A N   1 
ATOM   843  C  CA  . ILE A 1 113 ? 24.874 -2.194  18.269  1.00  8.86  ? 113  ILE A CA  1 
ATOM   844  C  C   . ILE A 1 113 ? 24.935 -2.406  16.775  1.00  8.53  ? 113  ILE A C   1 
ATOM   845  O  O   . ILE A 1 113 ? 25.944 -2.869  16.217  1.00  9.19  ? 113  ILE A O   1 
ATOM   846  C  CB  . ILE A 1 113 ? 25.574 -0.928  18.778  1.00  10.82 ? 113  ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 113 ? 25.129 -0.595  20.318  1.00  14.09 ? 113  ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 113 ? 25.258 0.267   17.887  1.00  11.04 ? 113  ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 113 ? 25.884 0.428   21.041  1.00  16.37 ? 113  ILE A CD1 1 
ATOM   850  N  N   . GLY A 1 114 ? 23.867 -2.081  16.092  1.00  6.43  ? 114  GLY A N   1 
ATOM   851  C  CA  . GLY A 1 114 ? 23.799 -2.272  14.641  1.00  7.75  ? 114  GLY A CA  1 
ATOM   852  C  C   . GLY A 1 114 ? 23.416 -3.651  14.198  1.00  7.88  ? 114  GLY A C   1 
ATOM   853  O  O   . GLY A 1 114 ? 23.369 -3.922  13.014  1.00  7.84  ? 114  GLY A O   1 
ATOM   854  N  N   . ARG A 1 115 ? 23.090 -4.527  15.144  1.00  6.69  ? 115  ARG A N   1 
ATOM   855  C  CA  . ARG A 1 115 ? 22.605 -5.860  14.828  1.00  6.82  ? 115  ARG A CA  1 
ATOM   856  C  C   . ARG A 1 115 ? 21.122 -5.923  15.087  1.00  6.71  ? 115  ARG A C   1 
ATOM   857  O  O   . ARG A 1 115 ? 20.556 -4.916  15.436  1.00  9.66  ? 115  ARG A O   1 
ATOM   858  C  CB  . ARG A 1 115 ? 23.429 -6.895  15.620  1.00  7.64  ? 115  ARG A CB  1 
ATOM   859  C  CG  . ARG A 1 115 ? 24.892 -6.712  15.335  1.00  9.90  ? 115  ARG A CG  1 
ATOM   860  C  CD  . ARG A 1 115 ? 25.742 -7.805  15.824  1.00  10.27 ? 115  ARG A CD  1 
ATOM   861  N  NE  . ARG A 1 115 ? 27.181 -7.521  15.606  1.00  11.34 ? 115  ARG A NE  1 
ATOM   862  C  CZ  . ARG A 1 115 ? 27.901 -7.832  14.536  1.00  9.82  ? 115  ARG A CZ  1 
ATOM   863  N  NH1 . ARG A 1 115 ? 27.391 -8.388  13.459  1.00  10.17 ? 115  ARG A NH1 1 
ATOM   864  N  NH2 . ARG A 1 115 ? 29.197 -7.559  14.570  1.00  13.22 ? 115  ARG A NH2 1 
ATOM   865  N  N   . THR A 1 116 ? 20.497 -7.068  14.915  1.00  7.39  ? 116  THR A N   1 
ATOM   866  C  CA  . THR A 1 116 ? 19.041 -7.150  14.964  1.00  7.19  ? 116  THR A CA  1 
ATOM   867  C  C   . THR A 1 116 ? 18.600 -7.968  16.168  1.00  7.32  ? 116  THR A C   1 
ATOM   868  O  O   . THR A 1 116 ? 19.048 -9.085  16.315  1.00  9.46  ? 116  THR A O   1 
ATOM   869  C  CB  . THR A 1 116 ? 18.463 -7.742  13.698  1.00  8.28  ? 116  THR A CB  1 
ATOM   870  O  OG1 . THR A 1 116 ? 18.703 -6.871  12.591  1.00  9.81  ? 116  THR A OG1 1 
ATOM   871  C  CG2 . THR A 1 116 ? 16.965 -7.927  13.761  1.00  8.49  ? 116  THR A CG2 1 
ATOM   872  N  N   . LEU A 1 117 ? 17.678 -7.453  16.952  1.00  6.56  ? 117  LEU A N   1 
ATOM   873  C  CA  . LEU A 1 117 ? 17.005 -8.224  17.981  1.00  6.88  ? 117  LEU A CA  1 
ATOM   874  C  C   . LEU A 1 117 ? 15.742 -8.821  17.400  1.00  7.01  ? 117  LEU A C   1 
ATOM   875  O  O   . LEU A 1 117 ? 14.997 -8.119  16.693  1.00  8.03  ? 117  LEU A O   1 
ATOM   876  C  CB  . LEU A 1 117 ? 16.669 -7.279  19.139  1.00  8.01  ? 117  LEU A CB  1 
ATOM   877  C  CG  . LEU A 1 117 ? 16.081 -7.924  20.350  1.00  8.79  ? 117  LEU A CG  1 
ATOM   878  C  CD1 . LEU A 1 117 ? 17.090 -8.851  21.024  1.00  10.31 ? 117  LEU A CD1 1 
ATOM   879  C  CD2 . LEU A 1 117 ? 15.648 -6.818  21.317  1.00  9.91  ? 117  LEU A CD2 1 
ATOM   880  N  N   . VAL A 1 118 ? 15.550 -10.114 17.625  1.00  7.20  ? 118  VAL A N   1 
ATOM   881  C  CA  . VAL A 1 118 ? 14.411 -10.849 17.071  1.00  7.28  ? 118  VAL A CA  1 
ATOM   882  C  C   . VAL A 1 118 ? 13.671 -11.596 18.150  1.00  7.52  ? 118  VAL A C   1 
ATOM   883  O  O   . VAL A 1 118 ? 14.264 -12.224 19.026  1.00  8.77  ? 118  VAL A O   1 
ATOM   884  C  CB  . VAL A 1 118 ? 14.881 -11.893 16.039  1.00  7.82  ? 118  VAL A CB  1 
ATOM   885  C  CG1 . VAL A 1 118 ? 13.694 -12.618 15.395  1.00  9.61  ? 118  VAL A CG1 1 
ATOM   886  C  CG2 . VAL A 1 118 ? 15.679 -11.268 14.898  1.00  8.39  ? 118  VAL A CG2 1 
ATOM   887  N  N   . VAL A 1 119 ? 12.338 -11.523 18.136  1.00  7.85  ? 119  VAL A N   1 
ATOM   888  C  CA  . VAL A 1 119 ? 11.476 -12.363 18.989  1.00  8.07  ? 119  VAL A CA  1 
ATOM   889  C  C   . VAL A 1 119 ? 10.728 -13.348 18.089  1.00  7.70  ? 119  VAL A C   1 
ATOM   890  O  O   . VAL A 1 119 ? 10.241 -13.019 16.999  1.00  9.17  ? 119  VAL A O   1 
ATOM   891  C  CB  . VAL A 1 119 ? 10.531 -11.528 19.874  1.00  9.03  ? 119  VAL A CB  1 
ATOM   892  C  CG1 . VAL A 1 119 ? 9.544  -10.732 19.106  1.00  10.65 ? 119  VAL A CG1 1 
ATOM   893  C  CG2 . VAL A 1 119 ? 9.801  -12.427 20.893  1.00  10.19 ? 119  VAL A CG2 1 
ATOM   894  N  N   . HIS A 1 120 ? 10.654 -14.600 18.563  1.00  8.20  ? 120  HIS A N   1 
ATOM   895  C  CA  . HIS A 1 120 ? 10.236 -15.719 17.770  1.00  8.07  ? 120  HIS A CA  1 
ATOM   896  C  C   . HIS A 1 120 ? 8.875  -16.264 18.166  1.00  9.27  ? 120  HIS A C   1 
ATOM   897  O  O   . HIS A 1 120 ? 8.354  -15.983 19.214  1.00  10.53 ? 120  HIS A O   1 
ATOM   898  C  CB  . HIS A 1 120 ? 11.270 -16.870 17.941  1.00  9.38  ? 120  HIS A CB  1 
ATOM   899  C  CG  . HIS A 1 120 ? 12.503 -16.663 17.168  1.00  9.01  ? 120  HIS A CG  1 
ATOM   900  N  ND1 . HIS A 1 120 ? 12.661 -17.171 15.910  1.00  10.28 ? 120  HIS A ND1 1 
ATOM   901  C  CD2 . HIS A 1 120 ? 13.660 -16.033 17.479  1.00  8.91  ? 120  HIS A CD2 1 
ATOM   902  C  CE1 . HIS A 1 120 ? 13.856 -16.829 15.458  1.00  11.43 ? 120  HIS A CE1 1 
ATOM   903  N  NE2 . HIS A 1 120 ? 14.470 -16.122 16.388  1.00  10.46 ? 120  HIS A NE2 1 
ATOM   904  N  N   . GLU A 1 121 ? 8.345  -17.060 17.242  1.00  10.66 ? 121  GLU A N   1 
ATOM   905  C  CA  . GLU A 1 121 ? 7.064  -17.741 17.399  1.00  11.50 ? 121  GLU A CA  1 
ATOM   906  C  C   . GLU A 1 121 ? 7.000  -18.750 18.523  1.00  11.78 ? 121  GLU A C   1 
ATOM   907  O  O   . GLU A 1 121 ? 5.977  -18.817 19.219  1.00  13.32 ? 121  GLU A O   1 
ATOM   908  C  CB  . GLU A 1 121 ? 6.785  -18.448 16.056  1.00  12.90 ? 121  GLU A CB  1 
ATOM   909  C  CG  . GLU A 1 121 ? 5.573  -19.320 15.938  0.50  10.36 ? 121  GLU A CG  1 
ATOM   910  C  CD  . GLU A 1 121 ? 5.679  -20.198 14.689  0.33  11.31 ? 121  GLU A CD  1 
ATOM   911  O  OE1 . GLU A 1 121 ? 6.771  -20.527 14.173  0.03  4.91  ? 121  GLU A OE1 1 
ATOM   912  O  OE2 . GLU A 1 121 ? 4.599  -20.646 14.243  0.03  4.70  ? 121  GLU A OE2 1 
ATOM   913  N  N   . LYS A 1 122 ? 8.059  -19.538 18.640  1.00  11.72 ? 122  LYS A N   1 
ATOM   914  C  CA  . LYS A 1 122 ? 8.122  -20.690 19.543  1.00  13.00 ? 122  LYS A CA  1 
ATOM   915  C  C   . LYS A 1 122 ? 9.184  -20.417 20.607  1.00  11.20 ? 122  LYS A C   1 
ATOM   916  O  O   . LYS A 1 122 ? 10.015 -19.503 20.457  1.00  10.94 ? 122  LYS A O   1 
ATOM   917  C  CB  . LYS A 1 122 ? 8.466  -21.998 18.765  1.00  14.53 ? 122  LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 122 ? 7.573  -22.336 17.610  1.00  17.99 ? 122  LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 122 ? 8.020  -23.622 16.909  1.00  19.41 ? 122  LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 122 ? 7.123  -23.926 15.723  0.10  17.15 ? 122  LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 122 ? 7.562  -25.149 15.009  0.10  17.55 ? 122  LYS A NZ  1 
ATOM   922  N  N   . ALA A 1 123 ? 9.189  -21.261 21.623  1.00  10.82 ? 123  ALA A N   1 
ATOM   923  C  CA  . ALA A 1 123 ? 10.261 -21.228 22.604  1.00  10.57 ? 123  ALA A CA  1 
ATOM   924  C  C   . ALA A 1 123 ? 11.579 -21.659 21.986  1.00  9.98  ? 123  ALA A C   1 
ATOM   925  O  O   . ALA A 1 123 ? 11.587 -22.575 21.139  1.00  12.37 ? 123  ALA A O   1 
ATOM   926  C  CB  . ALA A 1 123 ? 9.905  -22.133 23.809  1.00  12.13 ? 123  ALA A CB  1 
ATOM   927  N  N   . ASP A 1 124 ? 12.683 -21.091 22.467  1.00  9.98  ? 124  ASP A N   1 
ATOM   928  C  CA  . ASP A 1 124 ? 14.019 -21.627 22.170  1.00  10.34 ? 124  ASP A CA  1 
ATOM   929  C  C   . ASP A 1 124 ? 14.238 -22.801 23.125  1.00  10.50 ? 124  ASP A C   1 
ATOM   930  O  O   . ASP A 1 124 ? 14.107 -22.647 24.340  1.00  11.14 ? 124  ASP A O   1 
ATOM   931  C  CB  . ASP A 1 124 ? 14.967 -20.443 22.429  1.00  10.21 ? 124  ASP A CB  1 
ATOM   932  C  CG  . ASP A 1 124 ? 16.419 -20.728 22.158  1.00  10.68 ? 124  ASP A CG  1 
ATOM   933  O  OD1 . ASP A 1 124 ? 16.832 -21.870 22.149  1.00  10.78 ? 124  ASP A OD1 1 
ATOM   934  O  OD2 . ASP A 1 124 ? 17.130 -19.722 21.917  1.00  11.24 ? 124  ASP A OD2 1 
ATOM   935  N  N   . ASP A 1 125 ? 14.664 -23.935 22.598  1.00  11.01 ? 125  ASP A N   1 
ATOM   936  C  CA  . ASP A 1 125 ? 14.949 -25.119 23.395  1.00  11.66 ? 125  ASP A CA  1 
ATOM   937  C  C   . ASP A 1 125 ? 16.339 -25.126 24.004  1.00  11.79 ? 125  ASP A C   1 
ATOM   938  O  O   . ASP A 1 125 ? 16.738 -26.083 24.671  1.00  14.02 ? 125  ASP A O   1 
ATOM   939  C  CB  . ASP A 1 125 ? 14.680 -26.403 22.614  1.00  13.04 ? 125  ASP A CB  1 
ATOM   940  C  CG  . ASP A 1 125 ? 15.671 -26.671 21.504  1.00  14.53 ? 125  ASP A CG  1 
ATOM   941  O  OD1 . ASP A 1 125 ? 16.794 -26.125 21.505  1.00  15.01 ? 125  ASP A OD1 1 
ATOM   942  O  OD2 . ASP A 1 125 ? 15.308 -27.536 20.631  1.00  17.82 ? 125  ASP A OD2 1 
ATOM   943  N  N   . LEU A 1 126 ? 17.085 -24.050 23.788  1.00  11.69 ? 126  LEU A N   1 
ATOM   944  C  CA  . LEU A 1 126 ? 18.373 -23.809 24.469  1.00  12.74 ? 126  LEU A CA  1 
ATOM   945  C  C   . LEU A 1 126 ? 19.422 -24.824 24.139  1.00  12.98 ? 126  LEU A C   1 
ATOM   946  O  O   . LEU A 1 126 ? 20.379 -24.968 24.886  1.00  13.40 ? 126  LEU A O   1 
ATOM   947  C  CB  . LEU A 1 126 ? 18.229 -23.637 25.992  1.00  13.16 ? 126  LEU A CB  1 
ATOM   948  C  CG  . LEU A 1 126 ? 17.061 -22.751 26.456  1.00  13.97 ? 126  LEU A CG  1 
ATOM   949  C  CD1 . LEU A 1 126 ? 17.019 -22.696 27.963  1.00  17.61 ? 126  LEU A CD1 1 
ATOM   950  C  CD2 . LEU A 1 126 ? 17.154 -21.336 25.902  1.00  14.07 ? 126  LEU A CD2 1 
ATOM   951  N  N   . GLY A 1 127 ? 19.313 -25.474 22.993  1.00  14.05 ? 127  GLY A N   1 
ATOM   952  C  CA  . GLY A 1 127 ? 20.290 -26.498 22.641  1.00  14.88 ? 127  GLY A CA  1 
ATOM   953  C  C   . GLY A 1 127 ? 20.048 -27.864 23.234  1.00  16.37 ? 127  GLY A C   1 
ATOM   954  O  O   . GLY A 1 127 ? 20.888 -28.759 23.017  1.00  18.38 ? 127  GLY A O   1 
ATOM   955  N  N   . LYS A 1 128 ? 18.893 -28.076 23.865  1.00  16.82 ? 128  LYS A N   1 
ATOM   956  C  CA  . LYS A 1 128 ? 18.642 -29.339 24.591  1.00  20.02 ? 128  LYS A CA  1 
ATOM   957  C  C   . LYS A 1 128 ? 17.683 -30.212 23.828  1.00  20.09 ? 128  LYS A C   1 
ATOM   958  O  O   . LYS A 1 128 ? 17.274 -31.244 24.356  1.00  22.73 ? 128  LYS A O   1 
ATOM   959  C  CB  . LYS A 1 128 ? 17.977 -29.055 25.928  1.00  20.80 ? 128  LYS A CB  1 
ATOM   960  C  CG  . LYS A 1 128 ? 18.687 -28.130 26.924  1.00  23.66 ? 128  LYS A CG  1 
ATOM   961  C  CD  . LYS A 1 128 ? 17.636 -27.775 28.009  1.00  26.54 ? 128  LYS A CD  1 
ATOM   962  C  CE  . LYS A 1 128 ? 18.189 -27.253 29.304  1.00  29.61 ? 128  LYS A CE  1 
ATOM   963  N  NZ  . LYS A 1 128 ? 18.840 -25.887 29.255  1.00  32.84 ? 128  LYS A NZ  1 
ATOM   964  N  N   . GLY A 1 129 ? 17.322 -29.819 22.617  1.00  20.59 ? 129  GLY A N   1 
ATOM   965  C  CA  . GLY A 1 129 ? 16.331 -30.474 21.802  1.00  21.60 ? 129  GLY A CA  1 
ATOM   966  C  C   . GLY A 1 129 ? 16.702 -31.801 21.182  1.00  23.17 ? 129  GLY A C   1 
ATOM   967  O  O   . GLY A 1 129 ? 15.812 -32.494 20.656  1.00  26.44 ? 129  GLY A O   1 
ATOM   968  N  N   . GLY A 1 130 ? 17.966 -32.190 21.182  0.70  22.31 ? 130  GLY A N   1 
ATOM   969  C  CA  . GLY A 1 130 ? 18.286 -33.548 20.616  0.70  23.26 ? 130  GLY A CA  1 
ATOM   970  C  C   . GLY A 1 130 ? 17.963 -33.765 19.129  0.70  24.05 ? 130  GLY A C   1 
ATOM   971  O  O   . GLY A 1 130 ? 17.826 -34.905 18.647  0.70  25.33 ? 130  GLY A O   1 
ATOM   972  N  N   . ASN A 1 131 ? 17.830 -32.683 18.367  0.77  24.29 ? 131  ASN A N   1 
ATOM   973  C  CA  . ASN A 1 131 ? 17.925 -32.752 16.898  0.77  23.34 ? 131  ASN A CA  1 
ATOM   974  C  C   . ASN A 1 131 ? 19.056 -31.824 16.468  1.00  23.24 ? 131  ASN A C   1 
ATOM   975  O  O   . ASN A 1 131 ? 19.535 -31.019 17.279  1.00  23.73 ? 131  ASN A O   1 
ATOM   976  C  CB  . ASN A 1 131 ? 16.601 -32.446 16.163  0.77  23.54 ? 131  ASN A CB  1 
ATOM   977  C  CG  . ASN A 1 131 ? 16.019 -31.073 16.497  0.77  24.02 ? 131  ASN A CG  1 
ATOM   978  O  OD1 . ASN A 1 131 ? 16.723 -30.175 16.894  0.77  20.36 ? 131  ASN A OD1 1 
ATOM   979  N  ND2 . ASN A 1 131 ? 14.732 -30.911 16.301  0.77  28.49 ? 131  ASN A ND2 1 
ATOM   980  N  N   . GLU A 1 132 ? 19.472 -31.894 15.205  0.65  21.41 ? 132  GLU A N   1 
ATOM   981  C  CA  . GLU A 1 132 ? 20.626 -31.090 14.790  0.65  20.75 ? 132  GLU A CA  1 
ATOM   982  C  C   . GLU A 1 132 ? 20.377 -29.577 14.844  0.65  19.60 ? 132  GLU A C   1 
ATOM   983  O  O   . GLU A 1 132 ? 21.295 -28.790 15.183  0.65  20.47 ? 132  GLU A O   1 
ATOM   984  C  CB  . GLU A 1 132 ? 21.162 -31.534 13.428  0.65  20.80 ? 132  GLU A CB  1 
ATOM   985  C  CG  . GLU A 1 132 ? 22.129 -32.698 13.545  0.10  20.49 ? 132  GLU A CG  1 
ATOM   986  C  CD  . GLU A 1 132 ? 22.524 -33.276 12.209  0.10  20.56 ? 132  GLU A CD  1 
ATOM   987  O  OE1 . GLU A 1 132 ? 22.250 -32.633 11.178  0.10  20.58 ? 132  GLU A OE1 1 
ATOM   988  O  OE2 . GLU A 1 132 ? 23.110 -34.379 12.194  0.10  18.64 ? 132  GLU A OE2 1 
ATOM   989  N  N   . GLU A 1 133 ? 19.139 -29.166 14.572  1.00  19.19 ? 133  GLU A N   1 
ATOM   990  C  CA  . GLU A 1 133 ? 18.792 -27.723 14.570  1.00  18.13 ? 133  GLU A CA  1 
ATOM   991  C  C   . GLU A 1 133 ? 18.853 -27.136 15.976  1.00  16.83 ? 133  GLU A C   1 
ATOM   992  O  O   . GLU A 1 133 ? 19.084 -25.955 16.166  1.00  16.44 ? 133  GLU A O   1 
ATOM   993  C  CB  . GLU A 1 133 ? 17.385 -27.476 14.028  1.00  20.42 ? 133  GLU A CB  1 
ATOM   994  C  CG  . GLU A 1 133 ? 17.222 -27.612 12.518  0.10  18.57 ? 133  GLU A CG  1 
ATOM   995  C  CD  . GLU A 1 133 ? 15.756 -27.613 12.106  0.10  18.91 ? 133  GLU A CD  1 
ATOM   996  O  OE1 . GLU A 1 133 ? 14.977 -26.829 12.690  0.10  18.95 ? 133  GLU A OE1 1 
ATOM   997  O  OE2 . GLU A 1 133 ? 15.382 -28.403 11.211  0.10  19.66 ? 133  GLU A OE2 1 
ATOM   998  N  N   . SER A 1 134 ? 18.621 -27.952 16.981  1.00  16.26 ? 134  SER A N   1 
ATOM   999  C  CA  . SER A 1 134 ? 18.659 -27.464 18.383  1.00  15.54 ? 134  SER A CA  1 
ATOM   1000 C  C   . SER A 1 134 ? 19.932 -26.708 18.666  1.00  15.88 ? 134  SER A C   1 
ATOM   1001 O  O   . SER A 1 134 ? 19.920 -25.669 19.320  1.00  15.77 ? 134  SER A O   1 
ATOM   1002 C  CB  . SER A 1 134 ? 18.518 -28.608 19.366  1.00  14.90 ? 134  SER A CB  1 
ATOM   1003 O  OG  . SER A 1 134 ? 18.489 -28.088 20.663  1.00  16.54 ? 134  SER A OG  1 
ATOM   1004 N  N   . THR A 1 135 ? 21.065 -27.229 18.215  1.00  17.66 ? 135  THR A N   1 
ATOM   1005 C  CA  . THR A 1 135 ? 22.367 -26.573 18.543  1.00  18.20 ? 135  THR A CA  1 
ATOM   1006 C  C   . THR A 1 135 ? 22.822 -25.540 17.494  1.00  17.82 ? 135  THR A C   1 
ATOM   1007 O  O   . THR A 1 135 ? 23.961 -25.029 17.535  1.00  16.27 ? 135  THR A O   1 
ATOM   1008 C  CB  . THR A 1 135 ? 23.444 -27.604 18.887  1.00  21.41 ? 135  THR A CB  1 
ATOM   1009 O  OG1 . THR A 1 135 ? 23.474 -28.563 17.840  1.00  23.75 ? 135  THR A OG1 1 
ATOM   1010 C  CG2 . THR A 1 135 ? 23.144 -28.291 20.180  1.00  22.57 ? 135  THR A CG2 1 
ATOM   1011 N  N   . LYS A 1 136 ? 21.875 -25.157 16.632  1.00  17.63 ? 136  LYS A N   1 
ATOM   1012 C  CA  . LYS A 1 136 ? 22.077 -24.061 15.696  1.00  17.90 ? 136  LYS A CA  1 
ATOM   1013 C  C   . LYS A 1 136 ? 21.155 -22.905 16.021  1.00  17.72 ? 136  LYS A C   1 
ATOM   1014 O  O   . LYS A 1 136 ? 21.578 -21.756 16.200  1.00  19.44 ? 136  LYS A O   1 
ATOM   1015 C  CB  . LYS A 1 136 ? 21.899 -24.609 14.264  1.00  19.11 ? 136  LYS A CB  1 
ATOM   1016 C  CG  . LYS A 1 136 ? 22.807 -25.810 14.051  0.72  20.98 ? 136  LYS A CG  1 
ATOM   1017 C  CD  . LYS A 1 136 ? 22.805 -26.396 12.648  0.72  21.80 ? 136  LYS A CD  1 
ATOM   1018 C  CE  . LYS A 1 136 ? 23.457 -27.779 12.659  0.10  20.89 ? 136  LYS A CE  1 
ATOM   1019 N  NZ  . LYS A 1 136 ? 23.559 -28.408 11.310  0.10  20.60 ? 136  LYS A NZ  1 
ATOM   1020 N  N   . THR A 1 137 ? 19.875 -23.195 16.119  1.00  16.41 ? 137  THR A N   1 
ATOM   1021 C  CA  . THR A 1 137 ? 18.854 -22.172 16.207  1.00  16.15 ? 137  THR A CA  1 
ATOM   1022 C  C   . THR A 1 137 ? 18.051 -22.300 17.485  1.00  14.20 ? 137  THR A C   1 
ATOM   1023 O  O   . THR A 1 137 ? 17.420 -21.377 17.851  1.00  16.21 ? 137  THR A O   1 
ATOM   1024 C  CB  . THR A 1 137 ? 17.875 -22.263 15.057  1.00  18.20 ? 137  THR A CB  1 
ATOM   1025 O  OG1 . THR A 1 137 ? 17.141 -23.483 15.182  1.00  18.30 ? 137  THR A OG1 1 
ATOM   1026 C  CG2 . THR A 1 137 ? 18.605 -22.176 13.739  1.00  21.57 ? 137  THR A CG2 1 
ATOM   1027 N  N   . GLY A 1 138 ? 17.979 -23.478 18.121  1.00  12.47 ? 138  GLY A N   1 
ATOM   1028 C  CA  . GLY A 1 138 ? 17.070 -23.681 19.229  1.00  12.04 ? 138  GLY A CA  1 
ATOM   1029 C  C   . GLY A 1 138 ? 15.625 -23.986 18.854  1.00  11.99 ? 138  GLY A C   1 
ATOM   1030 O  O   . GLY A 1 138 ? 14.783 -24.091 19.741  1.00  12.03 ? 138  GLY A O   1 
ATOM   1031 N  N   . ASN A 1 139 ? 15.326 -24.149 17.568  1.00  12.46 ? 139  ASN A N   1 
ATOM   1032 C  CA  . ASN A 1 139 ? 13.989 -24.543 17.106  1.00  13.08 ? 139  ASN A CA  1 
ATOM   1033 C  C   . ASN A 1 139 ? 12.918 -23.538 17.478  1.00  12.13 ? 139  ASN A C   1 
ATOM   1034 O  O   . ASN A 1 139 ? 11.794 -23.919 17.808  1.00  13.53 ? 139  ASN A O   1 
ATOM   1035 C  CB  . ASN A 1 139 ? 13.625 -25.963 17.611  1.00  13.65 ? 139  ASN A CB  1 
ATOM   1036 C  CG  . ASN A 1 139 ? 14.465 -27.038 16.962  1.00  16.53 ? 139  ASN A CG  1 
ATOM   1037 O  OD1 . ASN A 1 139 ? 14.465 -27.196 15.739  1.00  22.33 ? 139  ASN A OD1 1 
ATOM   1038 N  ND2 . ASN A 1 139 ? 15.229 -27.735 17.767  1.00  17.26 ? 139  ASN A ND2 1 
ATOM   1039 N  N   . ALA A 1 140 ? 13.266 -22.232 17.461  1.00  11.61 ? 140  ALA A N   1 
ATOM   1040 C  CA  . ALA A 1 140 ? 12.287 -21.242 17.890  1.00  13.12 ? 140  ALA A CA  1 
ATOM   1041 C  C   . ALA A 1 140 ? 11.281 -20.801 16.827  1.00  13.05 ? 140  ALA A C   1 
ATOM   1042 O  O   . ALA A 1 140 ? 10.449 -19.934 17.062  1.00  12.00 ? 140  ALA A O   1 
ATOM   1043 C  CB  . ALA A 1 140 ? 12.984 -20.014 18.508  1.00  14.12 ? 140  ALA A CB  1 
ATOM   1044 N  N   . GLY A 1 141 ? 11.374 -21.372 15.627  1.00  14.93 ? 141  GLY A N   1 
ATOM   1045 C  CA  . GLY A 1 141 ? 10.400 -21.105 14.604  1.00  14.78 ? 141  GLY A CA  1 
ATOM   1046 C  C   . GLY A 1 141 ? 10.480 -19.697 14.030  1.00  14.49 ? 141  GLY A C   1 
ATOM   1047 O  O   . GLY A 1 141 ? 11.516 -19.068 14.007  1.00  14.22 ? 141  GLY A O   1 
ATOM   1048 N  N   . SER A 1 142 ? 9.352  -19.204 13.556  1.00  14.24 ? 142  SER A N   1 
ATOM   1049 C  CA  . SER A 1 142 ? 9.275  -18.004 12.775  1.00  13.78 ? 142  SER A CA  1 
ATOM   1050 C  C   . SER A 1 142 ? 9.694  -16.777 13.550  1.00  10.96 ? 142  SER A C   1 
ATOM   1051 O  O   . SER A 1 142 ? 9.630  -16.714 14.768  1.00  11.94 ? 142  SER A O   1 
ATOM   1052 C  CB  . SER A 1 142 ? 7.815  -17.890 12.251  1.00  15.54 ? 142  SER A CB  1 
ATOM   1053 O  OG  A SER A 1 142 ? 7.639  -18.842 11.199  0.50  17.42 ? 142  SER A OG  1 
ATOM   1054 O  OG  B SER A 1 142 ? 7.068  -17.073 13.088  0.50  19.22 ? 142  SER A OG  1 
ATOM   1055 N  N   . ARG A 1 143 ? 10.148 -15.780 12.816  1.00  10.69 ? 143  ARG A N   1 
ATOM   1056 C  CA  . ARG A 1 143 ? 10.542 -14.502 13.360  1.00  9.65  ? 143  ARG A CA  1 
ATOM   1057 C  C   . ARG A 1 143 ? 9.341  -13.598 13.398  1.00  10.91 ? 143  ARG A C   1 
ATOM   1058 O  O   . ARG A 1 143 ? 8.841  -13.240 12.331  1.00  14.79 ? 143  ARG A O   1 
ATOM   1059 C  CB  . ARG A 1 143 ? 11.677 -13.882 12.530  1.00  9.57  ? 143  ARG A CB  1 
ATOM   1060 C  CG  . ARG A 1 143 ? 12.863 -14.806 12.454  1.00  9.89  ? 143  ARG A CG  1 
ATOM   1061 C  CD  . ARG A 1 143 ? 13.977 -14.290 11.602  1.00  9.60  ? 143  ARG A CD  1 
ATOM   1062 N  NE  . ARG A 1 143 ? 15.017 -15.317 11.515  1.00  10.12 ? 143  ARG A NE  1 
ATOM   1063 C  CZ  . ARG A 1 143 ? 16.237 -15.161 11.037  1.00  9.14  ? 143  ARG A CZ  1 
ATOM   1064 N  NH1 . ARG A 1 143 ? 16.661 -13.963 10.628  1.00  10.14 ? 143  ARG A NH1 1 
ATOM   1065 N  NH2 . ARG A 1 143 ? 17.064 -16.191 11.018  1.00  11.02 ? 143  ARG A NH2 1 
ATOM   1066 N  N   . LEU A 1 144 ? 8.822  -13.233 14.531  1.00  9.63  ? 144  LEU A N   1 
ATOM   1067 C  CA  . LEU A 1 144 ? 7.602  -12.449 14.618  1.00  10.70 ? 144  LEU A CA  1 
ATOM   1068 C  C   . LEU A 1 144 ? 7.785  -10.954 14.563  1.00  9.91  ? 144  LEU A C   1 
ATOM   1069 O  O   . LEU A 1 144 ? 6.958  -10.240 14.033  1.00  11.12 ? 144  LEU A O   1 
ATOM   1070 C  CB  . LEU A 1 144 ? 6.835  -12.784 15.890  1.00  11.97 ? 144  LEU A CB  1 
ATOM   1071 C  CG  . LEU A 1 144 ? 6.392  -14.215 16.086  1.00  16.15 ? 144  LEU A CG  1 
ATOM   1072 C  CD1 . LEU A 1 144 ? 5.585  -14.335 17.392  1.00  20.86 ? 144  LEU A CD1 1 
ATOM   1073 C  CD2 . LEU A 1 144 ? 5.596  -14.683 14.910  1.00  19.13 ? 144  LEU A CD2 1 
ATOM   1074 N  N   . ALA A 1 145 ? 8.870  -10.461 15.109  1.00  8.58  ? 145  ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 145 ? 9.179  -9.049  15.086  1.00  8.66  ? 145  ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 145 ? 10.661 -8.877  15.293  1.00  8.63  ? 145  ALA A C   1 
ATOM   1077 O  O   . ALA A 1 145 ? 11.300 -9.731  15.894  1.00  9.24  ? 145  ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 145 ? 8.394  -8.277  16.163  1.00  9.16  ? 145  ALA A CB  1 
ATOM   1079 N  N   . CYS A 1 146 ? 11.165 -7.746  14.832  1.00  7.97  ? 146  CYS A N   1 
ATOM   1080 C  CA  . CYS A 1 146 ? 12.607 -7.456  14.901  1.00  8.69  ? 146  CYS A CA  1 
ATOM   1081 C  C   . CYS A 1 146 ? 12.865 -5.964  14.810  1.00  7.65  ? 146  CYS A C   1 
ATOM   1082 O  O   . CYS A 1 146 ? 11.962 -5.228  14.425  1.00  8.78  ? 146  CYS A O   1 
ATOM   1083 C  CB  . CYS A 1 146 ? 13.335 -8.227  13.849  1.00  9.59  ? 146  CYS A CB  1 
ATOM   1084 S  SG  . CYS A 1 146 ? 13.052 -7.650  12.205  1.00  14.66 ? 146  CYS A SG  1 
ATOM   1085 N  N   . GLY A 1 147 ? 14.067 -5.565  15.156  1.00  7.61  ? 147  GLY A N   1 
ATOM   1086 C  CA  . GLY A 1 147 ? 14.487 -4.207  14.971  1.00  8.22  ? 147  GLY A CA  1 
ATOM   1087 C  C   . GLY A 1 147 ? 15.993 -4.130  15.071  1.00  7.83  ? 147  GLY A C   1 
ATOM   1088 O  O   . GLY A 1 147 ? 16.637 -5.006  15.637  1.00  8.32  ? 147  GLY A O   1 
ATOM   1089 N  N   . VAL A 1 148 ? 16.543 -3.060  14.559  1.00  7.10  ? 148  VAL A N   1 
ATOM   1090 C  CA  . VAL A 1 148 ? 17.973 -2.808  14.649  1.00  7.57  ? 148  VAL A CA  1 
ATOM   1091 C  C   . VAL A 1 148 ? 18.279 -2.179  15.987  1.00  7.93  ? 148  VAL A C   1 
ATOM   1092 O  O   . VAL A 1 148 ? 17.557 -1.289  16.440  1.00  9.77  ? 148  VAL A O   1 
ATOM   1093 C  CB  . VAL A 1 148 ? 18.460 -1.888  13.498  1.00  8.66  ? 148  VAL A CB  1 
ATOM   1094 C  CG1 . VAL A 1 148 ? 19.960 -1.725  13.537  1.00  9.96  ? 148  VAL A CG1 1 
ATOM   1095 C  CG2 . VAL A 1 148 ? 18.081 -2.500  12.177  1.00  12.16 ? 148  VAL A CG2 1 
ATOM   1096 N  N   . ILE A 1 149 ? 19.334 -2.614  16.636  1.00  6.82  ? 149  ILE A N   1 
ATOM   1097 C  CA  . ILE A 1 149 ? 19.721 -2.080  17.933  1.00  7.66  ? 149  ILE A CA  1 
ATOM   1098 C  C   . ILE A 1 149 ? 20.533 -0.777  17.694  1.00  7.38  ? 149  ILE A C   1 
ATOM   1099 O  O   . ILE A 1 149 ? 21.584 -0.813  17.062  1.00  8.80  ? 149  ILE A O   1 
ATOM   1100 C  CB  . ILE A 1 149 ? 20.539 -3.112  18.699  1.00  7.75  ? 149  ILE A CB  1 
ATOM   1101 C  CG1 . ILE A 1 149 ? 19.669 -4.383  18.938  1.00  8.84  ? 149  ILE A CG1 1 
ATOM   1102 C  CG2 . ILE A 1 149 ? 21.029 -2.530  20.017  1.00  9.64  ? 149  ILE A CG2 1 
ATOM   1103 C  CD1 . ILE A 1 149 ? 20.559 -5.583  19.354  1.00  10.40 ? 149  ILE A CD1 1 
ATOM   1104 N  N   . GLY A 1 150 ? 20.006 0.322   18.212  1.00  7.11  ? 150  GLY A N   1 
ATOM   1105 C  CA  . GLY A 1 150 ? 20.576 1.631   17.977  1.00  7.41  ? 150  GLY A CA  1 
ATOM   1106 C  C   . GLY A 1 150 ? 21.127 2.250   19.241  1.00  8.36  ? 150  GLY A C   1 
ATOM   1107 O  O   . GLY A 1 150 ? 20.758 1.920   20.362  1.00  9.10  ? 150  GLY A O   1 
ATOM   1108 N  N   . ILE A 1 151 ? 22.025 3.198   19.048  1.00  7.75  ? 151  ILE A N   1 
ATOM   1109 C  CA  . ILE A 1 151 ? 22.605 3.985   20.156  1.00  7.86  ? 151  ILE A CA  1 
ATOM   1110 C  C   . ILE A 1 151 ? 21.560 4.923   20.751  1.00  7.95  ? 151  ILE A C   1 
ATOM   1111 O  O   . ILE A 1 151 ? 20.875 5.603   20.022  1.00  9.92  ? 151  ILE A O   1 
ATOM   1112 C  CB  . ILE A 1 151 ? 23.825 4.770   19.651  1.00  9.49  ? 151  ILE A CB  1 
ATOM   1113 C  CG1 . ILE A 1 151 ? 24.945 3.836   19.233  1.00  11.35 ? 151  ILE A CG1 1 
ATOM   1114 C  CG2 . ILE A 1 151 ? 24.330 5.755   20.695  1.00  12.25 ? 151  ILE A CG2 1 
ATOM   1115 C  CD1 . ILE A 1 151 ? 25.990 4.463   18.358  1.00  14.16 ? 151  ILE A CD1 1 
ATOM   1116 N  N   . ALA A 1 152 ? 21.444 4.922   22.068  1.00  7.90  ? 152  ALA A N   1 
ATOM   1117 C  CA  . ALA A 1 152 ? 20.461 5.720   22.765  1.00  9.20  ? 152  ALA A CA  1 
ATOM   1118 C  C   . ALA A 1 152 ? 21.141 6.781   23.582  1.00  10.18 ? 152  ALA A C   1 
ATOM   1119 O  O   . ALA A 1 152 ? 22.330 6.714   23.879  1.00  11.00 ? 152  ALA A O   1 
ATOM   1120 C  CB  . ALA A 1 152 ? 19.589 4.795   23.645  1.00  11.47 ? 152  ALA A CB  1 
ATOM   1121 N  N   . GLN A 1 153 ? 20.370 7.795   23.918  1.00  12.58 ? 153  GLN A N   1 
ATOM   1122 C  CA  . GLN A 1 153 ? 20.929 8.889   24.714  1.00  15.54 ? 153  GLN A CA  1 
ATOM   1123 C  C   . GLN A 1 153 ? 21.033 8.537   26.184  1.00  18.29 ? 153  GLN A C   1 
ATOM   1124 O  O   . GLN A 1 153 ? 20.315 7.673   26.699  0.50  18.39 ? 153  GLN A O   1 
ATOM   1125 C  CB  . GLN A 1 153 ? 20.121 10.168  24.492  1.00  16.78 ? 153  GLN A CB  1 
ATOM   1126 C  CG  . GLN A 1 153 ? 18.833 10.191  25.143  1.00  17.82 ? 153  GLN A CG  1 
ATOM   1127 C  CD  . GLN A 1 153 ? 18.203 11.592  24.988  1.00  16.38 ? 153  GLN A CD  1 
ATOM   1128 O  OE1 . GLN A 1 153 ? 17.911 12.035  23.876  1.00  13.82 ? 153  GLN A OE1 1 
ATOM   1129 N  NE2 . GLN A 1 153 ? 17.912 12.241  26.092  1.00  19.66 ? 153  GLN A NE2 1 
ATOM   1130 N  N   A ALA B 1 1   ? 34.732 -3.924  2.146   0.53  21.97 ? 1    ALA F N   1 
ATOM   1131 N  N   B ALA B 1 1   ? 31.946 -4.823  9.290   0.31  17.57 ? 1    ALA F N   1 
ATOM   1132 C  CA  A ALA B 1 1   ? 34.973 -4.863  3.286   0.53  21.12 ? 1    ALA F CA  1 
ATOM   1133 C  CA  B ALA B 1 1   ? 32.250 -3.378  9.492   0.31  16.11 ? 1    ALA F CA  1 
ATOM   1134 C  C   A ALA B 1 1   ? 34.333 -4.533  4.650   0.53  20.71 ? 1    ALA F C   1 
ATOM   1135 C  C   B ALA B 1 1   ? 32.732 -2.739  8.199   0.10  15.17 ? 1    ALA F C   1 
ATOM   1136 O  O   A ALA B 1 1   ? 34.390 -5.366  5.540   0.53  22.41 ? 1    ALA F O   1 
ATOM   1137 O  O   B ALA B 1 1   ? 33.280 -1.638  8.205   0.10  14.24 ? 1    ALA F O   1 
ATOM   1138 C  CB  A ALA B 1 1   ? 36.491 -5.192  3.461   0.53  21.61 ? 1    ALA F CB  1 
ATOM   1139 C  CB  B ALA B 1 1   ? 33.276 -3.173  10.621  0.31  16.74 ? 1    ALA F CB  1 
ATOM   1140 N  N   A THR B 1 2   ? 33.766 -3.334  4.854   0.53  18.07 ? 2    THR F N   1 
ATOM   1141 N  N   B THR B 1 2   ? 32.508 -3.435  7.087   0.47  14.47 ? 2    THR F N   1 
ATOM   1142 C  CA  A THR B 1 2   ? 32.688 -3.164  5.848   0.53  16.30 ? 2    THR F CA  1 
ATOM   1143 C  CA  B THR B 1 2   ? 32.765 -2.869  5.785   0.47  14.18 ? 2    THR F CA  1 
ATOM   1144 C  C   A THR B 1 2   ? 31.502 -2.585  5.114   0.53  12.88 ? 2    THR F C   1 
ATOM   1145 C  C   B THR B 1 2   ? 31.488 -2.585  4.994   0.47  12.37 ? 2    THR F C   1 
ATOM   1146 O  O   A THR B 1 2   ? 31.645 -1.723  4.271   0.53  11.02 ? 2    THR F O   1 
ATOM   1147 O  O   B THR B 1 2   ? 31.557 -1.954  3.940   0.47  11.68 ? 2    THR F O   1 
ATOM   1148 C  CB  A THR B 1 2   ? 33.035 -2.256  7.037   0.53  17.07 ? 2    THR F CB  1 
ATOM   1149 C  CB  B THR B 1 2   ? 33.664 -3.770  4.897   0.47  15.20 ? 2    THR F CB  1 
ATOM   1150 O  OG1 A THR B 1 2   ? 34.216 -2.734  7.692   0.53  22.63 ? 2    THR F OG1 1 
ATOM   1151 O  OG1 B THR B 1 2   ? 32.985 -4.990  4.545   0.47  19.00 ? 2    THR F OG1 1 
ATOM   1152 C  CG2 A THR B 1 2   ? 31.902 -2.261  8.067   0.53  19.72 ? 2    THR F CG2 1 
ATOM   1153 C  CG2 B THR B 1 2   ? 34.940 -4.147  5.617   0.47  14.90 ? 2    THR F CG2 1 
ATOM   1154 N  N   . LYS B 1 3   ? 30.344 -3.120  5.441   1.00  10.46 ? 3    LYS F N   1 
ATOM   1155 C  CA  . LYS B 1 3   ? 29.081 -2.808  4.808   1.00  10.02 ? 3    LYS F CA  1 
ATOM   1156 C  C   . LYS B 1 3   ? 28.012 -2.510  5.824   1.00  8.60  ? 3    LYS F C   1 
ATOM   1157 O  O   . LYS B 1 3   ? 27.984 -3.103  6.927   1.00  8.91  ? 3    LYS F O   1 
ATOM   1158 C  CB  . LYS B 1 3   ? 28.601 -3.928  3.849   1.00  11.82 ? 3    LYS F CB  1 
ATOM   1159 C  CG  . LYS B 1 3   ? 29.591 -4.241  2.728   1.00  17.44 ? 3    LYS F CG  1 
ATOM   1160 C  CD  . LYS B 1 3   ? 29.083 -5.381  1.833   1.00  19.72 ? 3    LYS F CD  1 
ATOM   1161 C  CE  . LYS B 1 3   ? 30.099 -5.688  0.682   0.80  21.35 ? 3    LYS F CE  1 
ATOM   1162 N  NZ  . LYS B 1 3   ? 29.411 -5.983  -0.622  0.80  23.73 ? 3    LYS F NZ  1 
ATOM   1163 N  N   . ALA B 1 4   ? 27.121 -1.591  5.484   1.00  7.84  ? 4    ALA F N   1 
ATOM   1164 C  CA  . ALA B 1 4   ? 25.978 -1.268  6.306   1.00  7.44  ? 4    ALA F CA  1 
ATOM   1165 C  C   . ALA B 1 4   ? 24.776 -1.014  5.434   1.00  7.17  ? 4    ALA F C   1 
ATOM   1166 O  O   . ALA B 1 4   ? 24.897 -0.832  4.218   1.00  7.40  ? 4    ALA F O   1 
ATOM   1167 C  CB  . ALA B 1 4   ? 26.251 -0.075  7.200   1.00  8.42  ? 4    ALA F CB  1 
ATOM   1168 N  N   . VAL B 1 5   ? 23.591 -0.959  6.047   1.00  6.63  ? 5    VAL F N   1 
ATOM   1169 C  CA  . VAL B 1 5   ? 22.335 -0.764  5.299   1.00  6.98  ? 5    VAL F CA  1 
ATOM   1170 C  C   . VAL B 1 5   ? 21.349 -0.041  6.189   1.00  7.33  ? 5    VAL F C   1 
ATOM   1171 O  O   . VAL B 1 5   ? 21.419 -0.167  7.398   1.00  8.29  ? 5    VAL F O   1 
ATOM   1172 C  CB  . VAL B 1 5   ? 21.788 -2.097  4.773   1.00  8.33  ? 5    VAL F CB  1 
ATOM   1173 C  CG1 . VAL B 1 5   ? 21.306 -2.992  5.849   1.00  9.97  ? 5    VAL F CG1 1 
ATOM   1174 C  CG2 . VAL B 1 5   ? 20.716 -1.893  3.713   1.00  10.44 ? 5    VAL F CG2 1 
ATOM   1175 N  N   . CYS B 1 6   ? 20.448 0.703   5.598   1.00  7.49  ? 6    CYS F N   1 
ATOM   1176 C  CA  . CYS B 1 6   ? 19.406 1.380   6.299   1.00  6.97  ? 6    CYS F CA  1 
ATOM   1177 C  C   . CYS B 1 6   ? 18.134 1.337   5.464   1.00  7.70  ? 6    CYS F C   1 
ATOM   1178 O  O   . CYS B 1 6   ? 18.128 1.654   4.280   1.00  8.99  ? 6    CYS F O   1 
ATOM   1179 C  CB  . CYS B 1 6   ? 19.791 2.841   6.511   1.00  9.06  ? 6    CYS F CB  1 
ATOM   1180 S  SG  . CYS B 1 6   ? 18.653 3.804   7.435   1.00  10.67 ? 6    CYS F SG  1 
ATOM   1181 N  N   . VAL B 1 7   ? 17.034 0.957   6.111   1.00  7.49  ? 7    VAL F N   1 
ATOM   1182 C  CA  . VAL B 1 7   ? 15.719 1.021   5.512   1.00  7.90  ? 7    VAL F CA  1 
ATOM   1183 C  C   . VAL B 1 7   ? 15.051 2.260   6.036   1.00  8.50  ? 7    VAL F C   1 
ATOM   1184 O  O   . VAL B 1 7   ? 14.789 2.390   7.234   1.00  9.58  ? 7    VAL F O   1 
ATOM   1185 C  CB  . VAL B 1 7   ? 14.888 -0.202  5.915   1.00  9.26  ? 7    VAL F CB  1 
ATOM   1186 C  CG1 . VAL B 1 7   ? 13.508 -0.118  5.317   1.00  12.74 ? 7    VAL F CG1 1 
ATOM   1187 C  CG2 . VAL B 1 7   ? 15.542 -1.460  5.438   1.00  12.26 ? 7    VAL F CG2 1 
ATOM   1188 N  N   . LEU B 1 8   ? 14.785 3.209   5.167   1.00  8.60  ? 8    LEU F N   1 
ATOM   1189 C  CA  . LEU B 1 8   ? 14.108 4.440   5.482   1.00  9.37  ? 8    LEU F CA  1 
ATOM   1190 C  C   . LEU B 1 8   ? 12.606 4.263   5.355   1.00  9.48  ? 8    LEU F C   1 
ATOM   1191 O  O   . LEU B 1 8   ? 12.121 3.796   4.322   1.00  10.22 ? 8    LEU F O   1 
ATOM   1192 C  CB  . LEU B 1 8   ? 14.520 5.549   4.506   1.00  10.79 ? 8    LEU F CB  1 
ATOM   1193 C  CG  . LEU B 1 8   ? 15.972 6.007   4.551   1.00  10.99 ? 8    LEU F CG  1 
ATOM   1194 C  CD1 . LEU B 1 8   ? 16.315 6.967   3.415   1.00  12.75 ? 8    LEU F CD1 1 
ATOM   1195 C  CD2 . LEU B 1 8   ? 16.274 6.659   5.860   1.00  12.88 ? 8    LEU F CD2 1 
ATOM   1196 N  N   . LYS B 1 9   ? 11.873 4.671   6.373   0.70  7.38  ? 9    LYS F N   1 
ATOM   1197 C  CA  . LYS B 1 9   ? 10.418 4.602   6.327   0.70  10.23 ? 9    LYS F CA  1 
ATOM   1198 C  C   . LYS B 1 9   ? 9.878  5.842   6.910   1.00  13.32 ? 9    LYS F C   1 
ATOM   1199 O  O   . LYS B 1 9   ? 10.365 6.310   7.931   1.00  13.31 ? 9    LYS F O   1 
ATOM   1200 C  CB  . LYS B 1 9   ? 9.897  3.377   7.096   0.70  11.20 ? 9    LYS F CB  1 
ATOM   1201 C  CG  . LYS B 1 9   ? 10.243 2.063   6.503   0.30  12.42 ? 9    LYS F CG  1 
ATOM   1202 C  CD  . LYS B 1 9   ? 9.512  0.914   7.197   0.30  12.92 ? 9    LYS F CD  1 
ATOM   1203 C  CE  . LYS B 1 9   ? 10.013 -0.453  6.746   0.30  15.77 ? 9    LYS F CE  1 
ATOM   1204 N  NZ  . LYS B 1 9   ? 9.752  -1.560  7.723   0.30  18.83 ? 9    LYS F NZ  1 
ATOM   1205 N  N   . GLY B 1 10  ? 8.811  6.343   6.250   1.00  13.91 ? 10   GLY F N   1 
ATOM   1206 C  CA  . GLY B 1 10  ? 8.026  7.449   6.728   1.00  15.61 ? 10   GLY F CA  1 
ATOM   1207 C  C   . GLY B 1 10  ? 6.716  7.575   5.995   1.00  14.92 ? 10   GLY F C   1 
ATOM   1208 O  O   . GLY B 1 10  ? 6.476  6.908   5.012   1.00  14.97 ? 10   GLY F O   1 
ATOM   1209 N  N   . ASP B 1 11  ? 5.870  8.463   6.463   1.00  15.68 ? 11   ASP F N   1 
ATOM   1210 C  CA  . ASP B 1 11  ? 4.508  8.678   5.955   1.00  16.96 ? 11   ASP F CA  1 
ATOM   1211 C  C   . ASP B 1 11  ? 4.583  9.185   4.516   1.00  17.51 ? 11   ASP F C   1 
ATOM   1212 O  O   . ASP B 1 11  ? 5.392  10.080  4.164   1.00  18.11 ? 11   ASP F O   1 
ATOM   1213 C  CB  . ASP B 1 11  ? 3.811  9.695   6.835   1.00  18.87 ? 11   ASP F CB  1 
ATOM   1214 C  CG  . ASP B 1 11  ? 3.120  9.065   8.029   0.10  16.58 ? 11   ASP F CG  1 
ATOM   1215 O  OD1 . ASP B 1 11  ? 3.123  7.823   8.146   0.10  13.56 ? 11   ASP F OD1 1 
ATOM   1216 O  OD2 . ASP B 1 11  ? 2.567  9.824   8.847   0.10  16.53 ? 11   ASP F OD2 1 
ATOM   1217 N  N   . GLY B 1 12  ? 3.812  8.570   3.636   1.00  17.41 ? 12   GLY F N   1 
ATOM   1218 C  CA  . GLY B 1 12  ? 3.738  9.000   2.237   1.00  18.51 ? 12   GLY F CA  1 
ATOM   1219 C  C   . GLY B 1 12  ? 3.124  7.936   1.341   1.00  18.54 ? 12   GLY F C   1 
ATOM   1220 O  O   . GLY B 1 12  ? 2.060  8.155   0.774   1.00  20.03 ? 12   GLY F O   1 
ATOM   1221 N  N   . PRO B 1 13  ? 3.744  6.761   1.215   1.00  17.84 ? 13   PRO F N   1 
ATOM   1222 C  CA  . PRO B 1 13  ? 4.977  6.345   1.884   1.00  17.43 ? 13   PRO F CA  1 
ATOM   1223 C  C   . PRO B 1 13  ? 6.236  7.000   1.322   1.00  15.54 ? 13   PRO F C   1 
ATOM   1224 O  O   . PRO B 1 13  ? 6.394  7.087   0.140   1.00  17.14 ? 13   PRO F O   1 
ATOM   1225 C  CB  . PRO B 1 13  ? 5.068  4.849   1.566   1.00  19.27 ? 13   PRO F CB  1 
ATOM   1226 C  CG  . PRO B 1 13  ? 3.818  4.476   1.118   1.00  22.00 ? 13   PRO F CG  1 
ATOM   1227 C  CD  . PRO B 1 13  ? 3.222  5.642   0.414   1.00  18.69 ? 13   PRO F CD  1 
ATOM   1228 N  N   . VAL B 1 14  ? 7.101  7.511   2.187   1.00  15.61 ? 14   VAL F N   1 
ATOM   1229 C  CA  . VAL B 1 14  ? 8.493  7.813   1.787   1.00  14.17 ? 14   VAL F CA  1 
ATOM   1230 C  C   . VAL B 1 14  ? 9.263  6.615   2.234   1.00  14.24 ? 14   VAL F C   1 
ATOM   1231 O  O   . VAL B 1 14  ? 9.216  6.263   3.433   1.00  16.28 ? 14   VAL F O   1 
ATOM   1232 C  CB  . VAL B 1 14  ? 9.043  9.104   2.399   1.00  13.62 ? 14   VAL F CB  1 
ATOM   1233 C  CG1 . VAL B 1 14  ? 10.482 9.306   2.060   1.00  13.45 ? 14   VAL F CG1 1 
ATOM   1234 C  CG2 . VAL B 1 14  ? 8.225  10.319  1.946   1.00  16.64 ? 14   VAL F CG2 1 
ATOM   1235 N  N   . GLN B 1 15  ? 9.966  5.995   1.327   1.00  13.51 ? 15   GLN F N   1 
ATOM   1236 C  CA  . GLN B 1 15  ? 10.669 4.789   1.673   1.00  15.04 ? 15   GLN F CA  1 
ATOM   1237 C  C   . GLN B 1 15  ? 11.808 4.500   0.757   1.00  12.25 ? 15   GLN F C   1 
ATOM   1238 O  O   . GLN B 1 15  ? 11.801 4.870   -0.405  1.00  13.51 ? 15   GLN F O   1 
ATOM   1239 C  CB  . GLN B 1 15  ? 9.691  3.654   1.704   1.00  18.11 ? 15   GLN F CB  1 
ATOM   1240 C  CG  . GLN B 1 15  ? 9.329  3.103   0.414   1.00  20.70 ? 15   GLN F CG  1 
ATOM   1241 C  CD  . GLN B 1 15  ? 8.065  2.213   0.530   0.50  20.48 ? 15   GLN F CD  1 
ATOM   1242 O  OE1 . GLN B 1 15  ? 7.642  1.853   1.635   0.50  27.91 ? 15   GLN F OE1 1 
ATOM   1243 N  NE2 . GLN B 1 15  ? 7.470  1.874   -0.607  0.50  28.06 ? 15   GLN F NE2 1 
ATOM   1244 N  N   . GLY B 1 16  ? 12.853 3.934   1.314   1.00  10.79 ? 16   GLY F N   1 
ATOM   1245 C  CA  . GLY B 1 16  ? 13.966 3.571   0.508   1.00  11.34 ? 16   GLY F CA  1 
ATOM   1246 C  C   . GLY B 1 16  ? 14.937 2.691   1.248   1.00  9.66  ? 16   GLY F C   1 
ATOM   1247 O  O   . GLY B 1 16  ? 14.786 2.423   2.417   1.00  12.57 ? 16   GLY F O   1 
ATOM   1248 N  N   . ILE B 1 17  ? 15.907 2.205   0.528   1.00  10.17 ? 17   ILE F N   1 
ATOM   1249 C  CA  . ILE B 1 17  ? 16.991 1.407   1.059   1.00  9.49  ? 17   ILE F CA  1 
ATOM   1250 C  C   . ILE B 1 17  ? 18.277 2.114   0.667   1.00  8.64  ? 17   ILE F C   1 
ATOM   1251 O  O   . ILE B 1 17  ? 18.497 2.419   -0.511  1.00  9.89  ? 17   ILE F O   1 
ATOM   1252 C  CB  . ILE B 1 17  ? 16.963 -0.027  0.477   1.00  11.20 ? 17   ILE F CB  1 
ATOM   1253 C  CG1 . ILE B 1 17  ? 15.709 -0.796  0.895   1.00  13.40 ? 17   ILE F CG1 1 
ATOM   1254 C  CG2 . ILE B 1 17  ? 18.199 -0.787  0.910   1.00  11.89 ? 17   ILE F CG2 1 
ATOM   1255 C  CD1 . ILE B 1 17  ? 15.501 -2.154  0.198   1.00  15.18 ? 17   ILE F CD1 1 
ATOM   1256 N  N   . ILE B 1 18  ? 19.086 2.381   1.672   1.00  7.64  ? 18   ILE F N   1 
ATOM   1257 C  CA  . ILE B 1 18  ? 20.389 2.983   1.476   1.00  7.86  ? 18   ILE F CA  1 
ATOM   1258 C  C   . ILE B 1 18  ? 21.484 2.049   1.948   1.00  8.12  ? 18   ILE F C   1 
ATOM   1259 O  O   . ILE B 1 18  ? 21.419 1.521   3.045   1.00  9.55  ? 18   ILE F O   1 
ATOM   1260 C  CB  . ILE B 1 18  ? 20.466 4.351   2.238   1.00  8.33  ? 18   ILE F CB  1 
ATOM   1261 C  CG1 . ILE B 1 18  ? 19.367 5.300   1.739   1.00  10.66 ? 18   ILE F CG1 1 
ATOM   1262 C  CG2 . ILE B 1 18  ? 21.823 4.951   2.045   1.00  8.77  ? 18   ILE F CG2 1 
ATOM   1263 C  CD1 . ILE B 1 18  ? 19.401 5.727   0.306   1.00  13.97 ? 18   ILE F CD1 1 
ATOM   1264 N  N   . ASN B 1 19  ? 22.446 1.821   1.081   1.00  7.77  ? 19   ASN F N   1 
ATOM   1265 C  CA  . ASN B 1 19  ? 23.605 0.977   1.340   1.00  8.02  ? 19   ASN F CA  1 
ATOM   1266 C  C   . ASN B 1 19  ? 24.826 1.809   1.591   1.00  8.43  ? 19   ASN F C   1 
ATOM   1267 O  O   . ASN B 1 19  ? 24.970 2.879   1.027   1.00  9.08  ? 19   ASN F O   1 
ATOM   1268 C  CB  . ASN B 1 19  ? 23.860 0.118   0.113   1.00  9.68  ? 19   ASN F CB  1 
ATOM   1269 C  CG  . ASN B 1 19  ? 22.681 -0.642  -0.290  1.00  13.61 ? 19   ASN F CG  1 
ATOM   1270 O  OD1 . ASN B 1 19  ? 22.342 -1.608  0.356   1.00  13.18 ? 19   ASN F OD1 1 
ATOM   1271 N  ND2 . ASN B 1 19  ? 22.018 -0.214  -1.343  1.00  16.00 ? 19   ASN F ND2 1 
ATOM   1272 N  N   . PHE B 1 20  ? 25.738 1.277   2.386   1.00  8.99  ? 20   PHE F N   1 
ATOM   1273 C  CA  . PHE B 1 20  ? 26.984 1.876   2.732   1.00  8.31  ? 20   PHE F CA  1 
ATOM   1274 C  C   . PHE B 1 20  ? 28.110 0.856   2.557   1.00  8.20  ? 20   PHE F C   1 
ATOM   1275 O  O   . PHE B 1 20  ? 27.941 -0.296  2.957   1.00  9.41  ? 20   PHE F O   1 
ATOM   1276 C  CB  . PHE B 1 20  ? 27.013 2.310   4.207   1.00  8.85  ? 20   PHE F CB  1 
ATOM   1277 C  CG  . PHE B 1 20  ? 25.935 3.283   4.590   1.00  9.52  ? 20   PHE F CG  1 
ATOM   1278 C  CD1 . PHE B 1 20  ? 24.667 2.870   4.895   1.00  10.26 ? 20   PHE F CD1 1 
ATOM   1279 C  CD2 . PHE B 1 20  ? 26.226 4.616   4.695   1.00  10.65 ? 20   PHE F CD2 1 
ATOM   1280 C  CE1 . PHE B 1 20  ? 23.696 3.775   5.286   1.00  9.79  ? 20   PHE F CE1 1 
ATOM   1281 C  CE2 . PHE B 1 20  ? 25.244 5.528   5.089   1.00  11.37 ? 20   PHE F CE2 1 
ATOM   1282 C  CZ  . PHE B 1 20  ? 23.994 5.094   5.390   1.00  10.99 ? 20   PHE F CZ  1 
ATOM   1283 N  N   . GLU B 1 21  ? 29.226 1.268   1.972   1.00  9.60  ? 21   GLU F N   1 
ATOM   1284 C  CA  . GLU B 1 21  ? 30.362 0.356   1.830   1.00  11.10 ? 21   GLU F CA  1 
ATOM   1285 C  C   . GLU B 1 21  ? 31.643 1.115   2.065   1.00  10.66 ? 21   GLU F C   1 
ATOM   1286 O  O   . GLU B 1 21  ? 31.803 2.216   1.562   1.00  11.88 ? 21   GLU F O   1 
ATOM   1287 C  CB  . GLU B 1 21  ? 30.396 -0.322  0.463   1.00  12.73 ? 21   GLU F CB  1 
ATOM   1288 C  CG  . GLU B 1 21  ? 31.584 -1.305  0.304   1.00  14.86 ? 21   GLU F CG  1 
ATOM   1289 C  CD  . GLU B 1 21  ? 31.434 -2.225  -0.892  0.50  16.40 ? 21   GLU F CD  1 
ATOM   1290 O  OE1 . GLU B 1 21  ? 30.368 -2.211  -1.529  0.50  21.12 ? 21   GLU F OE1 1 
ATOM   1291 O  OE2 . GLU B 1 21  ? 32.382 -2.976  -1.172  0.50  23.13 ? 21   GLU F OE2 1 
ATOM   1292 N  N   . GLN B 1 22  ? 32.539 0.552   2.866   1.00  10.58 ? 22   GLN F N   1 
ATOM   1293 C  CA  . GLN B 1 22  ? 33.854 1.159   3.119   1.00  12.04 ? 22   GLN F CA  1 
ATOM   1294 C  C   . GLN B 1 22  ? 34.888 0.053   2.940   1.00  14.13 ? 22   GLN F C   1 
ATOM   1295 O  O   . GLN B 1 22  ? 34.937 -0.850  3.689   1.00  15.60 ? 22   GLN F O   1 
ATOM   1296 C  CB  . GLN B 1 22  ? 33.866 1.731   4.527   1.00  11.78 ? 22   GLN F CB  1 
ATOM   1297 C  CG  . GLN B 1 22  ? 35.106 2.522   4.855   1.00  11.84 ? 22   GLN F CG  1 
ATOM   1298 C  CD  . GLN B 1 22  ? 35.053 3.117   6.250   1.00  11.48 ? 22   GLN F CD  1 
ATOM   1299 O  OE1 . GLN B 1 22  ? 34.370 2.581   7.139   1.00  14.06 ? 22   GLN F OE1 1 
ATOM   1300 N  NE2 . GLN B 1 22  ? 35.742 4.225   6.461   1.00  13.31 ? 22   GLN F NE2 1 
ATOM   1301 N  N   . LYS B 1 23  ? 35.701 0.172   1.914   1.00  17.41 ? 23   LYS F N   1 
ATOM   1302 C  CA  . LYS B 1 23  ? 36.669 -0.861  1.563   1.00  20.12 ? 23   LYS F CA  1 
ATOM   1303 C  C   . LYS B 1 23  ? 37.794 -1.021  2.568   1.00  20.44 ? 23   LYS F C   1 
ATOM   1304 O  O   . LYS B 1 23  ? 38.275 -2.131  2.801   1.00  22.61 ? 23   LYS F O   1 
ATOM   1305 C  CB  . LYS B 1 23  ? 37.249 -0.568  0.171   1.00  21.54 ? 23   LYS F CB  1 
ATOM   1306 C  CG  . LYS B 1 23  ? 36.273 -0.743  -0.965  1.00  25.21 ? 23   LYS F CG  1 
ATOM   1307 C  CD  . LYS B 1 23  ? 36.940 -0.841  -2.320  1.00  25.54 ? 23   LYS F CD  1 
ATOM   1308 C  CE  . LYS B 1 23  ? 35.961 -1.256  -3.402  0.10  24.78 ? 23   LYS F CE  1 
ATOM   1309 N  NZ  . LYS B 1 23  ? 36.649 -1.435  -4.708  0.10  25.13 ? 23   LYS F NZ  1 
ATOM   1310 N  N   . GLU B 1 24  ? 38.228 0.058   3.170   1.00  20.08 ? 24   GLU F N   1 
ATOM   1311 C  CA  . GLU B 1 24  ? 39.183 0.028   4.274   1.00  20.80 ? 24   GLU F CA  1 
ATOM   1312 C  C   . GLU B 1 24  ? 38.867 1.131   5.240   1.00  20.24 ? 24   GLU F C   1 
ATOM   1313 O  O   . GLU B 1 24  ? 38.244 2.143   4.866   1.00  18.05 ? 24   GLU F O   1 
ATOM   1314 C  CB  . GLU B 1 24  ? 40.627 0.200   3.783   1.00  21.87 ? 24   GLU F CB  1 
ATOM   1315 C  CG  . GLU B 1 24  ? 40.866 1.457   2.990   0.25  19.85 ? 24   GLU F CG  1 
ATOM   1316 C  CD  . GLU B 1 24  ? 42.081 1.333   2.090   0.10  20.06 ? 24   GLU F CD  1 
ATOM   1317 O  OE1 . GLU B 1 24  ? 43.211 1.389   2.614   0.10  19.24 ? 24   GLU F OE1 1 
ATOM   1318 O  OE2 . GLU B 1 24  ? 41.897 1.180   0.862   0.10  20.20 ? 24   GLU F OE2 1 
ATOM   1319 N  N   . SER B 1 25  ? 39.324 0.985   6.475   1.00  20.47 ? 25   SER F N   1 
ATOM   1320 C  CA  . SER B 1 25  ? 38.924 1.933   7.511   1.00  20.60 ? 25   SER F CA  1 
ATOM   1321 C  C   . SER B 1 25  ? 39.442 3.326   7.266   1.00  19.91 ? 25   SER F C   1 
ATOM   1322 O  O   . SER B 1 25  ? 38.889 4.310   7.753   1.00  21.49 ? 25   SER F O   1 
ATOM   1323 C  CB  . SER B 1 25  ? 39.376 1.466   8.884   0.70  21.37 ? 25   SER F CB  1 
ATOM   1324 O  OG  . SER B 1 25  ? 40.777 1.369   8.983   0.70  23.09 ? 25   SER F OG  1 
ATOM   1325 N  N   . ASN B 1 26  ? 40.505 3.413   6.480   1.00  18.77 ? 26   ASN F N   1 
ATOM   1326 C  CA  . ASN B 1 26  ? 41.078 4.709   6.123   1.00  18.08 ? 26   ASN F CA  1 
ATOM   1327 C  C   . ASN B 1 26  ? 40.552 5.287   4.813   1.00  17.47 ? 26   ASN F C   1 
ATOM   1328 O  O   . ASN B 1 26  ? 41.109 6.283   4.306   1.00  20.16 ? 26   ASN F O   1 
ATOM   1329 C  CB  . ASN B 1 26  ? 42.603 4.618   6.125   1.00  18.52 ? 26   ASN F CB  1 
ATOM   1330 C  CG  . ASN B 1 26  ? 43.157 3.579   5.213   0.52  19.27 ? 26   ASN F CG  1 
ATOM   1331 O  OD1 . ASN B 1 26  ? 42.606 2.487   5.019   0.52  21.12 ? 26   ASN F OD1 1 
ATOM   1332 N  ND2 . ASN B 1 26  ? 44.329 3.880   4.692   0.52  20.72 ? 26   ASN F ND2 1 
ATOM   1333 N  N   . GLY B 1 27  ? 39.471 4.719   4.291   1.00  16.23 ? 27   GLY F N   1 
ATOM   1334 C  CA  . GLY B 1 27  ? 38.943 5.155   3.059   1.00  15.75 ? 27   GLY F CA  1 
ATOM   1335 C  C   . GLY B 1 27  ? 37.563 5.757   3.190   1.00  14.99 ? 27   GLY F C   1 
ATOM   1336 O  O   . GLY B 1 27  ? 36.927 5.714   4.224   1.00  14.81 ? 27   GLY F O   1 
ATOM   1337 N  N   . PRO B 1 28  ? 37.058 6.243   2.082   1.00  14.38 ? 28   PRO F N   1 
ATOM   1338 C  CA  . PRO B 1 28  ? 35.764 6.841   2.070   1.00  13.88 ? 28   PRO F CA  1 
ATOM   1339 C  C   . PRO B 1 28  ? 34.656 5.803   2.167   1.00  11.97 ? 28   PRO F C   1 
ATOM   1340 O  O   . PRO B 1 28  ? 34.855 4.636   1.870   1.00  14.02 ? 28   PRO F O   1 
ATOM   1341 C  CB  . PRO B 1 28  ? 35.716 7.507   0.681   1.00  16.06 ? 28   PRO F CB  1 
ATOM   1342 C  CG  . PRO B 1 28  ? 36.560 6.808   -0.105  1.00  19.47 ? 28   PRO F CG  1 
ATOM   1343 C  CD  . PRO B 1 28  ? 37.674 6.276   0.746   1.00  16.32 ? 28   PRO F CD  1 
ATOM   1344 N  N   . VAL B 1 29  ? 33.490 6.265   2.564   1.00  10.94 ? 29   VAL F N   1 
ATOM   1345 C  CA  . VAL B 1 29  ? 32.297 5.486   2.538   1.00  9.67  ? 29   VAL F CA  1 
ATOM   1346 C  C   . VAL B 1 29  ? 31.489 5.847   1.287   1.00  9.76  ? 29   VAL F C   1 
ATOM   1347 O  O   . VAL B 1 29  ? 31.158 7.001   1.061   1.00  11.26 ? 29   VAL F O   1 
ATOM   1348 C  CB  . VAL B 1 29  ? 31.445 5.725   3.796   1.00  10.61 ? 29   VAL F CB  1 
ATOM   1349 C  CG1 . VAL B 1 29  ? 30.211 4.819   3.767   1.00  10.62 ? 29   VAL F CG1 1 
ATOM   1350 C  CG2 . VAL B 1 29  ? 32.280 5.469   5.068   1.00  11.16 ? 29   VAL F CG2 1 
ATOM   1351 N  N   . LYS B 1 30  ? 31.124 4.828   0.520   1.00  10.06 ? 30   LYS F N   1 
ATOM   1352 C  CA  . LYS B 1 30  ? 30.192 4.957   -0.604  1.00  11.03 ? 30   LYS F CA  1 
ATOM   1353 C  C   . LYS B 1 30  ? 28.777 4.725   -0.069  1.00  10.49 ? 30   LYS F C   1 
ATOM   1354 O  O   . LYS B 1 30  ? 28.539 3.814   0.696   1.00  11.48 ? 30   LYS F O   1 
ATOM   1355 C  CB  A LYS B 1 30  ? 30.525 3.910   -1.668  0.64  14.07 ? 30   LYS F CB  1 
ATOM   1356 C  CB  B LYS B 1 30  ? 30.496 3.902   -1.666  0.36  12.16 ? 30   LYS F CB  1 
ATOM   1357 C  CG  A LYS B 1 30  ? 31.811 4.213   -2.443  0.64  19.52 ? 30   LYS F CG  1 
ATOM   1358 C  CG  B LYS B 1 30  ? 29.636 4.045   -2.899  0.36  13.36 ? 30   LYS F CG  1 
ATOM   1359 C  CD  A LYS B 1 30  ? 33.071 3.657   -1.786  0.64  23.29 ? 30   LYS F CD  1 
ATOM   1360 C  CD  B LYS B 1 30  ? 30.019 3.088   -3.991  0.36  14.96 ? 30   LYS F CD  1 
ATOM   1361 C  CE  A LYS B 1 30  ? 34.260 3.636   -2.783  0.64  24.59 ? 30   LYS F CE  1 
ATOM   1362 C  CE  B LYS B 1 30  ? 28.929 2.977   -5.038  0.36  17.20 ? 30   LYS F CE  1 
ATOM   1363 N  NZ  A LYS B 1 30  ? 35.594 3.211   -2.211  0.64  27.12 ? 30   LYS F NZ  1 
ATOM   1364 N  NZ  B LYS B 1 30  ? 29.214 1.898   -6.047  0.36  19.24 ? 30   LYS F NZ  1 
ATOM   1365 N  N   . VAL B 1 31  ? 27.889 5.633   -0.398  1.00  10.08 ? 31   VAL F N   1 
ATOM   1366 C  CA  . VAL B 1 31  ? 26.506 5.634   0.028   1.00  10.11 ? 31   VAL F CA  1 
ATOM   1367 C  C   . VAL B 1 31  ? 25.628 5.618   -1.203  1.00  10.27 ? 31   VAL F C   1 
ATOM   1368 O  O   . VAL B 1 31  ? 25.730 6.507   -2.056  1.00  12.81 ? 31   VAL F O   1 
ATOM   1369 C  CB  . VAL B 1 31  ? 26.180 6.883   0.857   1.00  10.65 ? 31   VAL F CB  1 
ATOM   1370 C  CG1 . VAL B 1 31  ? 24.795 6.821   1.466   1.00  11.83 ? 31   VAL F CG1 1 
ATOM   1371 C  CG2 . VAL B 1 31  ? 27.205 7.079   1.997   1.00  11.16 ? 31   VAL F CG2 1 
ATOM   1372 N  N   . TRP B 1 32  ? 24.777 4.646   -1.350  1.00  9.24  ? 32   TRP F N   1 
ATOM   1373 C  CA  . TRP B 1 32  ? 23.982 4.562   -2.544  1.00  10.07 ? 32   TRP F CA  1 
ATOM   1374 C  C   . TRP B 1 32  ? 22.673 3.841   -2.294  1.00  9.50  ? 32   TRP F C   1 
ATOM   1375 O  O   . TRP B 1 32  ? 22.562 2.975   -1.442  1.00  10.75 ? 32   TRP F O   1 
ATOM   1376 C  CB  . TRP B 1 32  ? 24.744 3.880   -3.709  1.00  13.20 ? 32   TRP F CB  1 
ATOM   1377 C  CG  . TRP B 1 32  ? 24.843 2.463   -3.636  1.00  14.18 ? 32   TRP F CG  1 
ATOM   1378 C  CD1 . TRP B 1 32  ? 24.081 1.566   -4.310  1.00  16.26 ? 32   TRP F CD1 1 
ATOM   1379 C  CD2 . TRP B 1 32  ? 25.763 1.694   -2.852  1.00  13.19 ? 32   TRP F CD2 1 
ATOM   1380 N  NE1 . TRP B 1 32  ? 24.453 0.304   -4.004  1.00  17.34 ? 32   TRP F NE1 1 
ATOM   1381 C  CE2 . TRP B 1 32  ? 25.479 0.336   -3.097  1.00  15.02 ? 32   TRP F CE2 1 
ATOM   1382 C  CE3 . TRP B 1 32  ? 26.750 2.025   -1.921  1.00  14.36 ? 32   TRP F CE3 1 
ATOM   1383 C  CZ2 . TRP B 1 32  ? 26.169 -0.699  -2.481  1.00  16.28 ? 32   TRP F CZ2 1 
ATOM   1384 C  CZ3 . TRP B 1 32  ? 27.435 0.997   -1.289  1.00  16.18 ? 32   TRP F CZ3 1 
ATOM   1385 C  CH2 . TRP B 1 32  ? 27.175 -0.356  -1.623  1.00  15.92 ? 32   TRP F CH2 1 
ATOM   1386 N  N   . GLY B 1 33  ? 21.701 4.137   -3.086  1.00  9.62  ? 33   GLY F N   1 
ATOM   1387 C  CA  . GLY B 1 33  ? 20.393 3.540   -3.021  1.00  9.29  ? 33   GLY F CA  1 
ATOM   1388 C  C   . GLY B 1 33  ? 19.328 4.413   -3.622  1.00  10.79 ? 33   GLY F C   1 
ATOM   1389 O  O   . GLY B 1 33  ? 19.645 5.277   -4.448  1.00  12.05 ? 33   GLY F O   1 
ATOM   1390 N  N   . SER B 1 34  ? 18.095 4.208   -3.245  1.00  12.32 ? 34   SER F N   1 
ATOM   1391 C  CA  . SER B 1 34  ? 16.960 4.905   -3.832  1.00  13.81 ? 34   SER F CA  1 
ATOM   1392 C  C   . SER B 1 34  ? 15.965 5.220   -2.764  1.00  13.32 ? 34   SER F C   1 
ATOM   1393 O  O   . SER B 1 34  ? 15.810 4.424   -1.819  1.00  14.59 ? 34   SER F O   1 
ATOM   1394 C  CB  . SER B 1 34  ? 16.248 4.003   -4.831  1.00  16.59 ? 34   SER F CB  1 
ATOM   1395 O  OG  A SER B 1 34  ? 15.462 4.832   -5.647  0.65  19.02 ? 34   SER F OG  1 
ATOM   1396 O  OG  B SER B 1 34  ? 16.556 2.663   -4.579  0.34  18.76 ? 34   SER F OG  1 
ATOM   1397 N  N   . ILE B 1 35  ? 15.328 6.359   -2.879  1.00  11.01 ? 35   ILE F N   1 
ATOM   1398 C  CA  . ILE B 1 35  ? 14.264 6.779   -1.993  1.00  11.12 ? 35   ILE F CA  1 
ATOM   1399 C  C   . ILE B 1 35  ? 13.089 7.217   -2.861  1.00  10.95 ? 35   ILE F C   1 
ATOM   1400 O  O   . ILE B 1 35  ? 13.265 8.030   -3.749  1.00  13.47 ? 35   ILE F O   1 
ATOM   1401 C  CB  . ILE B 1 35  ? 14.664 7.935   -1.075  1.00  10.54 ? 35   ILE F CB  1 
ATOM   1402 C  CG1 . ILE B 1 35  ? 15.969 7.659   -0.368  1.00  12.77 ? 35   ILE F CG1 1 
ATOM   1403 C  CG2 . ILE B 1 35  ? 13.523 8.218   -0.106  1.00  13.03 ? 35   ILE F CG2 1 
ATOM   1404 C  CD1 . ILE B 1 35  ? 16.552 8.906   0.271   1.00  13.20 ? 35   ILE F CD1 1 
ATOM   1405 N  N   . LYS B 1 36  ? 11.887 6.704   -2.594  1.00  10.92 ? 36   LYS F N   1 
ATOM   1406 C  CA  . LYS B 1 36  ? 10.686 7.054   -3.301  1.00  11.44 ? 36   LYS F CA  1 
ATOM   1407 C  C   . LYS B 1 36  ? 9.711  7.818   -2.431  1.00  11.53 ? 36   LYS F C   1 
ATOM   1408 O  O   . LYS B 1 36  ? 9.811  7.807   -1.226  1.00  12.20 ? 36   LYS F O   1 
ATOM   1409 C  CB  . LYS B 1 36  ? 10.020 5.809   -3.877  1.00  14.12 ? 36   LYS F CB  1 
ATOM   1410 C  CG  . LYS B 1 36  ? 9.302  4.906   -2.952  0.40  12.99 ? 36   LYS F CG  1 
ATOM   1411 C  CD  . LYS B 1 36  ? 8.682  3.722   -3.757  0.40  14.65 ? 36   LYS F CD  1 
ATOM   1412 C  CE  . LYS B 1 36  ? 9.719  2.653   -4.059  0.40  17.88 ? 36   LYS F CE  1 
ATOM   1413 N  NZ  . LYS B 1 36  ? 9.172  1.433   -4.767  0.40  19.59 ? 36   LYS F NZ  1 
ATOM   1414 N  N   . GLY B 1 37  ? 8.769  8.469   -3.101  1.00  12.05 ? 37   GLY F N   1 
ATOM   1415 C  CA  . GLY B 1 37  ? 7.728  9.168   -2.405  1.00  11.79 ? 37   GLY F CA  1 
ATOM   1416 C  C   . GLY B 1 37  ? 7.993  10.603  -2.061  1.00  11.71 ? 37   GLY F C   1 
ATOM   1417 O  O   . GLY B 1 37  ? 7.257  11.189  -1.314  1.00  14.34 ? 37   GLY F O   1 
ATOM   1418 N  N   . LEU B 1 38  ? 9.075  11.167  -2.623  1.00  12.41 ? 38   LEU F N   1 
ATOM   1419 C  CA  . LEU B 1 38  ? 9.529  12.512  -2.265  1.00  12.34 ? 38   LEU F CA  1 
ATOM   1420 C  C   . LEU B 1 38  ? 8.949  13.547  -3.264  1.00  11.97 ? 38   LEU F C   1 
ATOM   1421 O  O   . LEU B 1 38  ? 8.678  13.211  -4.407  1.00  15.22 ? 38   LEU F O   1 
ATOM   1422 C  CB  . LEU B 1 38  ? 11.039 12.547  -2.346  1.00  10.99 ? 38   LEU F CB  1 
ATOM   1423 C  CG  . LEU B 1 38  ? 11.795 11.776  -1.264  1.00  10.86 ? 38   LEU F CG  1 
ATOM   1424 C  CD1 . LEU B 1 38  ? 13.278 11.673  -1.682  1.00  13.22 ? 38   LEU F CD1 1 
ATOM   1425 C  CD2 . LEU B 1 38  ? 11.627 12.388  0.130   1.00  12.02 ? 38   LEU F CD2 1 
ATOM   1426 N  N   . THR B 1 39  ? 8.803  14.799  -2.838  1.00  12.41 ? 39   THR F N   1 
ATOM   1427 C  CA  . THR B 1 39  ? 8.532  15.877  -3.755  1.00  12.37 ? 39   THR F CA  1 
ATOM   1428 C  C   . THR B 1 39  ? 9.772  16.157  -4.613  1.00  12.36 ? 39   THR F C   1 
ATOM   1429 O  O   . THR B 1 39  ? 10.932 15.991  -4.213  1.00  12.90 ? 39   THR F O   1 
ATOM   1430 C  CB  . THR B 1 39  ? 8.107  17.144  -3.042  1.00  13.67 ? 39   THR F CB  1 
ATOM   1431 O  OG1 . THR B 1 39  ? 9.131  17.571  -2.127  1.00  16.14 ? 39   THR F OG1 1 
ATOM   1432 C  CG2 . THR B 1 39  ? 6.830  16.924  -2.287  1.00  17.16 ? 39   THR F CG2 1 
ATOM   1433 N  N   . GLU B 1 40  ? 9.509  16.578  -5.847  1.00  12.50 ? 40   GLU F N   1 
ATOM   1434 C  CA  . GLU B 1 40  ? 10.606 16.889  -6.779  1.00  11.86 ? 40   GLU F CA  1 
ATOM   1435 C  C   . GLU B 1 40  ? 11.545 17.969  -6.197  1.00  11.89 ? 40   GLU F C   1 
ATOM   1436 O  O   . GLU B 1 40  ? 11.085 18.971  -5.637  1.00  15.50 ? 40   GLU F O   1 
ATOM   1437 C  CB  . GLU B 1 40  ? 9.999  17.332  -8.154  1.00  12.85 ? 40   GLU F CB  1 
ATOM   1438 C  CG  . GLU B 1 40  ? 11.008 17.633  -9.196  1.00  14.44 ? 40   GLU F CG  1 
ATOM   1439 C  CD  . GLU B 1 40  ? 10.364 18.189  -10.465 0.70  13.35 ? 40   GLU F CD  1 
ATOM   1440 O  OE1 . GLU B 1 40  ? 9.364  18.929  -10.363 0.50  14.26 ? 40   GLU F OE1 1 
ATOM   1441 O  OE2 . GLU B 1 40  ? 10.815 17.869  -11.558 0.50  11.54 ? 40   GLU F OE2 1 
ATOM   1442 N  N   . GLY B 1 41  ? 12.855 17.780  -6.288  1.00  10.59 ? 41   GLY F N   1 
ATOM   1443 C  CA  . GLY B 1 41  ? 13.834 18.745  -5.777  1.00  10.67 ? 41   GLY F CA  1 
ATOM   1444 C  C   . GLY B 1 41  ? 14.723 18.163  -4.686  1.00  9.95  ? 41   GLY F C   1 
ATOM   1445 O  O   . GLY B 1 41  ? 14.799 16.948  -4.523  1.00  10.38 ? 41   GLY F O   1 
ATOM   1446 N  N   . LEU B 1 42  ? 15.409 19.058  -4.001  1.00  9.53  ? 42   LEU F N   1 
ATOM   1447 C  CA  . LEU B 1 42  ? 16.431 18.690  -3.029  1.00  9.24  ? 42   LEU F CA  1 
ATOM   1448 C  C   . LEU B 1 42  ? 15.841 18.460  -1.662  1.00  9.63  ? 42   LEU F C   1 
ATOM   1449 O  O   . LEU B 1 42  ? 14.944 19.185  -1.213  1.00  10.54 ? 42   LEU F O   1 
ATOM   1450 C  CB  . LEU B 1 42  ? 17.506 19.762  -2.932  1.00  9.93  ? 42   LEU F CB  1 
ATOM   1451 C  CG  . LEU B 1 42  ? 18.636 19.692  -3.983  1.00  11.10 ? 42   LEU F CG  1 
ATOM   1452 C  CD1 . LEU B 1 42  ? 18.093 19.866  -5.385  1.00  12.83 ? 42   LEU F CD1 1 
ATOM   1453 C  CD2 . LEU B 1 42  ? 19.664 20.766  -3.641  1.00  12.74 ? 42   LEU F CD2 1 
ATOM   1454 N  N   . HIS B 1 43  ? 16.353 17.458  -0.975  1.00  8.94  ? 43   HIS F N   1 
ATOM   1455 C  CA  . HIS B 1 43  ? 15.922 17.075  0.376   1.00  7.77  ? 43   HIS F CA  1 
ATOM   1456 C  C   . HIS B 1 43  ? 17.155 16.859  1.247   1.00  7.51  ? 43   HIS F C   1 
ATOM   1457 O  O   . HIS B 1 43  ? 18.023 16.082  0.888   1.00  8.06  ? 43   HIS F O   1 
ATOM   1458 C  CB  . HIS B 1 43  ? 15.105 15.795  0.311   1.00  9.62  ? 43   HIS F CB  1 
ATOM   1459 C  CG  . HIS B 1 43  ? 13.791 15.966  -0.399  1.00  8.78  ? 43   HIS F CG  1 
ATOM   1460 N  ND1 . HIS B 1 43  ? 12.659 16.338  0.287   1.00  11.42 ? 43   HIS F ND1 1 
ATOM   1461 C  CD2 . HIS B 1 43  ? 13.462 15.900  -1.703  1.00  11.04 ? 43   HIS F CD2 1 
ATOM   1462 C  CE1 . HIS B 1 43  ? 11.651 16.455  -0.570  1.00  12.17 ? 43   HIS F CE1 1 
ATOM   1463 N  NE2 . HIS B 1 43  ? 12.118 16.221  -1.792  1.00  12.11 ? 43   HIS F NE2 1 
ATOM   1464 N  N   . GLY B 1 44  ? 17.148 17.472  2.437   1.00  7.77  ? 44   GLY F N   1 
ATOM   1465 C  CA  . GLY B 1 44  ? 18.253 17.312  3.355   1.00  8.19  ? 44   GLY F CA  1 
ATOM   1466 C  C   . GLY B 1 44  ? 18.406 15.846  3.742   1.00  8.07  ? 44   GLY F C   1 
ATOM   1467 O  O   . GLY B 1 44  ? 17.463 15.107  3.894   1.00  8.08  ? 44   GLY F O   1 
ATOM   1468 N  N   . PHE B 1 45  ? 19.656 15.468  3.989   1.00  7.67  ? 45   PHE F N   1 
ATOM   1469 C  CA  . PHE B 1 45  ? 20.040 14.048  4.176   1.00  7.87  ? 45   PHE F CA  1 
ATOM   1470 C  C   . PHE B 1 45  ? 21.149 14.018  5.195   1.00  6.72  ? 45   PHE F C   1 
ATOM   1471 O  O   . PHE B 1 45  ? 22.252 14.496  4.960   1.00  8.43  ? 45   PHE F O   1 
ATOM   1472 C  CB  . PHE B 1 45  ? 20.519 13.511  2.797   1.00  8.03  ? 45   PHE F CB  1 
ATOM   1473 C  CG  . PHE B 1 45  ? 20.684 12.030  2.714   1.00  8.38  ? 45   PHE F CG  1 
ATOM   1474 C  CD1 . PHE B 1 45  ? 19.600 11.187  2.899   1.00  11.76 ? 45   PHE F CD1 1 
ATOM   1475 C  CD2 . PHE B 1 45  ? 21.848 11.461  2.249   1.00  9.43  ? 45   PHE F CD2 1 
ATOM   1476 C  CE1 . PHE B 1 45  ? 19.776 9.806   2.696   1.00  10.80 ? 45   PHE F CE1 1 
ATOM   1477 C  CE2 . PHE B 1 45  ? 21.980 10.105  2.036   1.00  10.39 ? 45   PHE F CE2 1 
ATOM   1478 C  CZ  . PHE B 1 45  ? 20.942 9.309   2.281   1.00  11.72 ? 45   PHE F CZ  1 
ATOM   1479 N  N   . HIS B 1 46  ? 20.850 13.469  6.379   1.00  6.96  ? 46   HIS F N   1 
ATOM   1480 C  CA  . HIS B 1 46  ? 21.766 13.520  7.474   1.00  7.52  ? 46   HIS F CA  1 
ATOM   1481 C  C   . HIS B 1 46  ? 21.769 12.264  8.317   1.00  6.56  ? 46   HIS F C   1 
ATOM   1482 O  O   . HIS B 1 46  ? 20.786 11.562  8.424   1.00  7.37  ? 46   HIS F O   1 
ATOM   1483 C  CB  . HIS B 1 46  ? 21.385 14.609  8.519   1.00  12.26 ? 46   HIS F CB  1 
ATOM   1484 C  CG  . HIS B 1 46  ? 21.014 15.914  7.962   1.00  10.99 ? 46   HIS F CG  1 
ATOM   1485 N  ND1 . HIS B 1 46  ? 19.823 16.492  8.269   1.00  12.30 ? 46   HIS F ND1 1 
ATOM   1486 C  CD2 . HIS B 1 46  ? 21.689 16.771  7.171   1.00  11.20 ? 46   HIS F CD2 1 
ATOM   1487 C  CE1 . HIS B 1 46  ? 19.753 17.660  7.625   1.00  12.64 ? 46   HIS F CE1 1 
ATOM   1488 N  NE2 . HIS B 1 46  ? 20.873 17.845  6.945   1.00  11.49 ? 46   HIS F NE2 1 
ATOM   1489 N  N   . VAL B 1 47  ? 22.920 12.028  8.920   1.00  7.31  ? 47   VAL F N   1 
ATOM   1490 C  CA  . VAL B 1 47  ? 23.015 11.055  10.019  1.00  6.51  ? 47   VAL F CA  1 
ATOM   1491 C  C   . VAL B 1 47  ? 22.780 11.828  11.304  1.00  6.61  ? 47   VAL F C   1 
ATOM   1492 O  O   . VAL B 1 47  ? 23.474 12.809  11.584  1.00  7.29  ? 47   VAL F O   1 
ATOM   1493 C  CB  . VAL B 1 47  ? 24.353 10.341  10.047  1.00  8.05  ? 47   VAL F CB  1 
ATOM   1494 C  CG1 . VAL B 1 47  ? 24.398 9.313   11.160  1.00  8.51  ? 47   VAL F CG1 1 
ATOM   1495 C  CG2 . VAL B 1 47  ? 24.657 9.657   8.742   1.00  9.87  ? 47   VAL F CG2 1 
ATOM   1496 N  N   . HIS B 1 48  ? 21.805 11.377  12.059  1.00  6.97  ? 48   HIS F N   1 
ATOM   1497 C  CA  . HIS B 1 48  ? 21.488 11.921  13.380  1.00  7.47  ? 48   HIS F CA  1 
ATOM   1498 C  C   . HIS B 1 48  ? 22.136 11.096  14.477  1.00  8.52  ? 48   HIS F C   1 
ATOM   1499 O  O   . HIS B 1 48  ? 22.496 9.949   14.270  1.00  11.80 ? 48   HIS F O   1 
ATOM   1500 C  CB  . HIS B 1 48  ? 19.964 12.056  13.525  1.00  7.42  ? 48   HIS F CB  1 
ATOM   1501 C  CG  . HIS B 1 48  ? 19.407 13.215  12.760  1.00  8.46  ? 48   HIS F CG  1 
ATOM   1502 N  ND1 . HIS B 1 48  ? 18.753 14.250  13.382  1.00  9.79  ? 48   HIS F ND1 1 
ATOM   1503 C  CD2 . HIS B 1 48  ? 19.358 13.481  11.418  1.00  9.65  ? 48   HIS F CD2 1 
ATOM   1504 C  CE1 . HIS B 1 48  ? 18.348 15.114  12.454  1.00  11.15 ? 48   HIS F CE1 1 
ATOM   1505 N  NE2 . HIS B 1 48  ? 18.705 14.680  11.257  1.00  10.50 ? 48   HIS F NE2 1 
ATOM   1506 N  N   . GLU B 1 49  ? 22.247 11.682  15.660  1.00  8.51  ? 49   GLU F N   1 
ATOM   1507 C  CA  . GLU B 1 49  ? 23.069 11.134  16.730  1.00  9.46  ? 49   GLU F CA  1 
ATOM   1508 C  C   . GLU B 1 49  ? 22.585 9.780   17.251  1.00  9.30  ? 49   GLU F C   1 
ATOM   1509 O  O   . GLU B 1 49  ? 23.440 8.910   17.519  1.00  10.95 ? 49   GLU F O   1 
ATOM   1510 C  CB  . GLU B 1 49  ? 23.093 12.137  17.871  1.00  11.03 ? 49   GLU F CB  1 
ATOM   1511 C  CG  . GLU B 1 49  ? 23.970 11.680  18.934  1.00  13.71 ? 49   GLU F CG  1 
ATOM   1512 C  CD  . GLU B 1 49  ? 24.090 12.576  20.015  1.00  19.00 ? 49   GLU F CD  1 
ATOM   1513 O  OE1 . GLU B 1 49  ? 23.444 13.639  20.033  0.50  17.40 ? 49   GLU F OE1 1 
ATOM   1514 O  OE2 . GLU B 1 49  ? 24.912 12.178  20.879  0.50  16.09 ? 49   GLU F OE2 1 
ATOM   1515 N  N   . PHE B 1 50  ? 21.304 9.619   17.440  1.00  8.47  ? 50   PHE F N   1 
ATOM   1516 C  CA  . PHE B 1 50  ? 20.811 8.419   18.141  1.00  8.80  ? 50   PHE F CA  1 
ATOM   1517 C  C   . PHE B 1 50  ? 20.095 7.503   17.192  1.00  8.51  ? 50   PHE F C   1 
ATOM   1518 O  O   . PHE B 1 50  ? 19.395 7.963   16.286  1.00  10.85 ? 50   PHE F O   1 
ATOM   1519 C  CB  . PHE B 1 50  ? 19.892 8.851   19.298  1.00  9.97  ? 50   PHE F CB  1 
ATOM   1520 C  CG  . PHE B 1 50  ? 20.583 9.775   20.259  1.00  12.50 ? 50   PHE F CG  1 
ATOM   1521 C  CD1 . PHE B 1 50  ? 20.161 11.072  20.445  1.00  15.21 ? 50   PHE F CD1 1 
ATOM   1522 C  CD2 . PHE B 1 50  ? 21.695 9.357   20.932  1.00  14.48 ? 50   PHE F CD2 1 
ATOM   1523 C  CE1 . PHE B 1 50  ? 20.878 11.914  21.388  1.00  15.64 ? 50   PHE F CE1 1 
ATOM   1524 C  CE2 . PHE B 1 50  ? 22.367 10.169  21.806  1.00  17.05 ? 50   PHE F CE2 1 
ATOM   1525 C  CZ  . PHE B 1 50  ? 21.985 11.402  21.994  1.00  16.76 ? 50   PHE F CZ  1 
ATOM   1526 N  N   . GLY B 1 51  ? 20.246 6.217   17.390  1.00  8.69  ? 51   GLY F N   1 
ATOM   1527 C  CA  . GLY B 1 51  ? 19.527 5.206   16.662  1.00  9.52  ? 51   GLY F CA  1 
ATOM   1528 C  C   . GLY B 1 51  ? 18.259 4.820   17.373  1.00  10.13 ? 51   GLY F C   1 
ATOM   1529 O  O   . GLY B 1 51  ? 17.972 3.652   17.569  1.00  11.58 ? 51   GLY F O   1 
ATOM   1530 N  N   . ASP B 1 52  ? 17.526 5.822   17.851  1.00  11.73 ? 52   ASP F N   1 
ATOM   1531 C  CA  . ASP B 1 52  ? 16.331 5.668   18.650  1.00  11.11 ? 52   ASP F CA  1 
ATOM   1532 C  C   . ASP B 1 52  ? 15.172 6.144   17.846  1.00  12.19 ? 52   ASP F C   1 
ATOM   1533 O  O   . ASP B 1 52  ? 15.094 7.302   17.511  1.00  13.14 ? 52   ASP F O   1 
ATOM   1534 C  CB  . ASP B 1 52  ? 16.466 6.479   19.965  1.00  10.38 ? 52   ASP F CB  1 
ATOM   1535 C  CG  . ASP B 1 52  ? 15.316 6.306   20.907  1.00  12.77 ? 52   ASP F CG  1 
ATOM   1536 O  OD1 . ASP B 1 52  ? 14.190 6.051   20.480  1.00  15.00 ? 52   ASP F OD1 1 
ATOM   1537 O  OD2 . ASP B 1 52  ? 15.564 6.536   22.127  1.00  17.60 ? 52   ASP F OD2 1 
ATOM   1538 N  N   . ASN B 1 53  ? 14.290 5.230   17.506  1.00  13.46 ? 53   ASN F N   1 
ATOM   1539 C  CA  . ASN B 1 53  ? 13.101 5.548   16.717  1.00  13.59 ? 53   ASN F CA  1 
ATOM   1540 C  C   . ASN B 1 53  ? 11.815 5.242   17.499  1.00  14.04 ? 53   ASN F C   1 
ATOM   1541 O  O   . ASN B 1 53  ? 10.749 5.043   16.910  1.00  14.81 ? 53   ASN F O   1 
ATOM   1542 C  CB  A ASN B 1 53  ? 13.174 4.942   15.292  0.50  14.35 ? 53   ASN F CB  1 
ATOM   1543 C  CB  B ASN B 1 53  ? 13.071 4.646   15.470  0.30  14.88 ? 53   ASN F CB  1 
ATOM   1544 C  CG  A ASN B 1 53  ? 14.375 5.497   14.403  0.50  11.89 ? 53   ASN F CG  1 
ATOM   1545 C  CG  B ASN B 1 53  ? 11.883 4.934   14.545  0.30  14.97 ? 53   ASN F CG  1 
ATOM   1546 O  OD1 A ASN B 1 53  ? 15.123 6.452   14.761  0.50  14.19 ? 53   ASN F OD1 1 
ATOM   1547 O  OD1 B ASN B 1 53  ? 11.071 4.061   14.236  0.30  20.84 ? 53   ASN F OD1 1 
ATOM   1548 N  ND2 A ASN B 1 53  ? 14.545 4.878   13.237  0.50  12.89 ? 53   ASN F ND2 1 
ATOM   1549 N  ND2 B ASN B 1 53  ? 11.823 6.147   14.067  0.30  14.72 ? 53   ASN F ND2 1 
ATOM   1550 N  N   . THR B 1 54  ? 11.902 5.322   18.812  1.00  13.38 ? 54   THR F N   1 
ATOM   1551 C  CA  . THR B 1 54  ? 10.757 4.985   19.635  1.00  14.17 ? 54   THR F CA  1 
ATOM   1552 C  C   . THR B 1 54  ? 9.570  5.895   19.385  1.00  15.27 ? 54   THR F C   1 
ATOM   1553 O  O   . THR B 1 54  ? 8.424  5.450   19.489  1.00  17.95 ? 54   THR F O   1 
ATOM   1554 C  CB  . THR B 1 54  ? 11.139 4.972   21.092  1.00  15.18 ? 54   THR F CB  1 
ATOM   1555 O  OG1 . THR B 1 54  ? 11.736 6.213   21.462  1.00  16.14 ? 54   THR F OG1 1 
ATOM   1556 C  CG2 . THR B 1 54  ? 12.080 3.798   21.424  1.00  15.18 ? 54   THR F CG2 1 
ATOM   1557 N  N   . ALA B 1 55  ? 9.807  7.179   19.132  1.00  15.17 ? 55   ALA F N   1 
ATOM   1558 C  CA  . ALA B 1 55  ? 8.659  8.069   18.796  1.00  16.27 ? 55   ALA F CA  1 
ATOM   1559 C  C   . ALA B 1 55  ? 8.784  8.588   17.384  1.00  16.70 ? 55   ALA F C   1 
ATOM   1560 O  O   . ALA B 1 55  ? 8.413  9.742   17.062  1.00  20.30 ? 55   ALA F O   1 
ATOM   1561 C  CB  . ALA B 1 55  ? 8.535  9.208   19.815  1.00  18.42 ? 55   ALA F CB  1 
ATOM   1562 N  N   . GLY B 1 56  ? 9.317  7.768   16.514  1.00  15.04 ? 56   GLY F N   1 
ATOM   1563 C  CA  . GLY B 1 56  ? 9.569  8.153   15.155  1.00  14.77 ? 56   GLY F CA  1 
ATOM   1564 C  C   . GLY B 1 56  ? 10.886 8.878   15.003  1.00  12.71 ? 56   GLY F C   1 
ATOM   1565 O  O   . GLY B 1 56  ? 11.755 8.772   15.858  1.00  13.97 ? 56   GLY F O   1 
ATOM   1566 N  N   . CYS B 1 57  ? 11.013 9.655   13.944  1.00  12.70 ? 57   CYS F N   1 
ATOM   1567 C  CA  . CYS B 1 57  ? 12.261 10.276  13.580  1.00  12.14 ? 57   CYS F CA  1 
ATOM   1568 C  C   . CYS B 1 57  ? 12.720 11.325  14.605  1.00  11.26 ? 57   CYS F C   1 
ATOM   1569 O  O   . CYS B 1 57  ? 13.902 11.593  14.718  1.00  10.92 ? 57   CYS F O   1 
ATOM   1570 C  CB  . CYS B 1 57  ? 12.070 10.991  12.209  1.00  14.10 ? 57   CYS F CB  1 
ATOM   1571 S  SG  A CYS B 1 57  ? 11.627 9.691   10.929  0.70  19.35 ? 57   CYS F SG  1 
ATOM   1572 S  SG  B CYS B 1 57  ? 11.883 10.208  10.618  0.30  16.75 ? 57   CYS F SG  1 
ATOM   1573 N  N   . THR B 1 58  ? 11.795 11.904  15.351  1.00  11.92 ? 58   THR F N   1 
ATOM   1574 C  CA  . THR B 1 58  ? 12.171 12.901  16.344  1.00  12.55 ? 58   THR F CA  1 
ATOM   1575 C  C   . THR B 1 58  ? 13.122 12.380  17.445  1.00  11.99 ? 58   THR F C   1 
ATOM   1576 O  O   . THR B 1 58  ? 14.028 13.072  17.925  1.00  11.49 ? 58   THR F O   1 
ATOM   1577 C  CB  A THR B 1 58  ? 10.911 13.600  16.919  0.54  13.81 ? 58   THR F CB  1 
ATOM   1578 C  CB  B THR B 1 58  ? 10.950 13.578  16.983  0.46  14.87 ? 58   THR F CB  1 
ATOM   1579 O  OG1 A THR B 1 58  ? 11.312 14.633  17.813  0.54  14.02 ? 58   THR F OG1 1 
ATOM   1580 O  OG1 B THR B 1 58  ? 9.826  13.516  16.111  0.46  19.87 ? 58   THR F OG1 1 
ATOM   1581 C  CG2 A THR B 1 58  ? 10.104 12.655  17.719  0.54  12.81 ? 58   THR F CG2 1 
ATOM   1582 C  CG2 B THR B 1 58  ? 11.268 14.997  17.228  0.46  14.64 ? 58   THR F CG2 1 
ATOM   1583 N  N   . SER B 1 59  ? 12.967 11.112  17.765  1.00  11.44 ? 59   SER F N   1 
ATOM   1584 C  CA  . SER B 1 59  ? 13.747 10.464  18.767  1.00  11.89 ? 59   SER F CA  1 
ATOM   1585 C  C   . SER B 1 59  ? 15.268 10.344  18.413  1.00  10.76 ? 59   SER F C   1 
ATOM   1586 O  O   . SER B 1 59  ? 16.113 10.092  19.254  1.00  11.86 ? 59   SER F O   1 
ATOM   1587 C  CB  . SER B 1 59  ? 13.065 9.007   19.027  1.00  12.23 ? 59   SER F CB  1 
ATOM   1588 O  OG  A SER B 1 59  ? 11.664 9.165   19.296  0.58  17.41 ? 59   SER F OG  1 
ATOM   1589 O  OG  B SER B 1 59  ? 11.690 9.168   19.405  0.42  15.91 ? 59   SER F OG  1 
ATOM   1590 N  N   . ALA B 1 60  ? 15.609 10.541  17.133  1.00  9.39  ? 60   ALA F N   1 
ATOM   1591 C  CA  . ALA B 1 60  ? 16.972 10.473  16.664  1.00  9.62  ? 60   ALA F CA  1 
ATOM   1592 C  C   . ALA B 1 60  ? 17.823 11.625  17.123  1.00  9.10  ? 60   ALA F C   1 
ATOM   1593 O  O   . ALA B 1 60  ? 19.033 11.557  17.043  1.00  9.01  ? 60   ALA F O   1 
ATOM   1594 C  CB  . ALA B 1 60  ? 17.033 10.357  15.164  1.00  9.92  ? 60   ALA F CB  1 
ATOM   1595 N  N   . GLY B 1 61  ? 17.213 12.695  17.646  1.00  8.30  ? 61   GLY F N   1 
ATOM   1596 C  CA  . GLY B 1 61  ? 17.982 13.762  18.211  1.00  8.45  ? 61   GLY F CA  1 
ATOM   1597 C  C   . GLY B 1 61  ? 18.613 14.636  17.155  1.00  7.95  ? 61   GLY F C   1 
ATOM   1598 O  O   . GLY B 1 61  ? 18.135 14.693  16.009  1.00  8.52  ? 61   GLY F O   1 
ATOM   1599 N  N   . PRO B 1 62  ? 19.692 15.317  17.502  1.00  7.86  ? 62   PRO F N   1 
ATOM   1600 C  CA  . PRO B 1 62  ? 20.324 16.266  16.627  1.00  8.72  ? 62   PRO F CA  1 
ATOM   1601 C  C   . PRO B 1 62  ? 21.207 15.570  15.584  1.00  8.08  ? 62   PRO F C   1 
ATOM   1602 O  O   . PRO B 1 62  ? 21.327 14.371  15.572  1.00  7.51  ? 62   PRO F O   1 
ATOM   1603 C  CB  . PRO B 1 62  ? 21.181 17.113  17.612  1.00  11.39 ? 62   PRO F CB  1 
ATOM   1604 C  CG  . PRO B 1 62  ? 21.539 16.154  18.662  1.00  11.26 ? 62   PRO F CG  1 
ATOM   1605 C  CD  . PRO B 1 62  ? 20.367 15.259  18.823  1.00  9.14  ? 62   PRO F CD  1 
ATOM   1606 N  N   . HIS B 1 63  ? 21.849 16.353  14.732  1.00  8.86  ? 63   HIS F N   1 
ATOM   1607 C  CA  . HIS B 1 63  ? 22.807 15.784  13.770  1.00  8.25  ? 63   HIS F CA  1 
ATOM   1608 C  C   . HIS B 1 63  ? 23.928 15.103  14.495  1.00  7.26  ? 63   HIS F C   1 
ATOM   1609 O  O   . HIS B 1 63  ? 24.346 15.555  15.541  1.00  8.79  ? 63   HIS F O   1 
ATOM   1610 C  CB  . HIS B 1 63  ? 23.374 16.871  12.863  1.00  9.60  ? 63   HIS F CB  1 
ATOM   1611 C  CG  . HIS B 1 63  ? 22.319 17.497  11.999  1.00  10.71 ? 63   HIS F CG  1 
ATOM   1612 N  ND1 . HIS B 1 63  ? 22.625 18.463  11.085  1.00  8.68  ? 63   HIS F ND1 1 
ATOM   1613 C  CD2 . HIS B 1 63  ? 20.978 17.321  11.897  1.00  14.05 ? 63   HIS F CD2 1 
ATOM   1614 C  CE1 . HIS B 1 63  ? 21.526 18.877  10.483  1.00  10.36 ? 63   HIS F CE1 1 
ATOM   1615 N  NE2 . HIS B 1 63  ? 20.499 18.208  10.955  1.00  13.90 ? 63   HIS F NE2 1 
ATOM   1616 N  N   . PHE B 1 64  ? 24.457 14.029  13.940  1.00  7.46  ? 64   PHE F N   1 
ATOM   1617 C  CA  . PHE B 1 64  ? 25.628 13.371  14.553  1.00  7.57  ? 64   PHE F CA  1 
ATOM   1618 C  C   . PHE B 1 64  ? 26.833 14.297  14.471  1.00  7.51  ? 64   PHE F C   1 
ATOM   1619 O  O   . PHE B 1 64  ? 27.251 14.688  13.375  1.00  7.99  ? 64   PHE F O   1 
ATOM   1620 C  CB  . PHE B 1 64  ? 25.865 12.046  13.836  1.00  8.41  ? 64   PHE F CB  1 
ATOM   1621 C  CG  . PHE B 1 64  ? 27.084 11.304  14.321  1.00  9.27  ? 64   PHE F CG  1 
ATOM   1622 C  CD1 . PHE B 1 64  ? 27.323 11.121  15.672  1.00  10.14 ? 64   PHE F CD1 1 
ATOM   1623 C  CD2 . PHE B 1 64  ? 27.978 10.743  13.446  1.00  10.56 ? 64   PHE F CD2 1 
ATOM   1624 C  CE1 . PHE B 1 64  ? 28.465 10.448  16.113  1.00  12.38 ? 64   PHE F CE1 1 
ATOM   1625 C  CE2 . PHE B 1 64  ? 29.084 10.046  13.904  1.00  11.71 ? 64   PHE F CE2 1 
ATOM   1626 C  CZ  . PHE B 1 64  ? 29.296 9.883   15.227  1.00  11.25 ? 64   PHE F CZ  1 
ATOM   1627 N  N   . ASN B 1 65  ? 27.362 14.694  15.616  1.00  8.07  ? 65   ASN F N   1 
ATOM   1628 C  CA  . ASN B 1 65  ? 28.316 15.765  15.707  1.00  8.41  ? 65   ASN F CA  1 
ATOM   1629 C  C   . ASN B 1 65  ? 29.334 15.488  16.810  1.00  8.88  ? 65   ASN F C   1 
ATOM   1630 O  O   . ASN B 1 65  ? 29.416 16.234  17.792  1.00  10.09 ? 65   ASN F O   1 
ATOM   1631 C  CB  . ASN B 1 65  ? 27.568 17.081  15.994  1.00  8.55  ? 65   ASN F CB  1 
ATOM   1632 C  CG  . ASN B 1 65  ? 28.434 18.304  15.974  1.00  8.58  ? 65   ASN F CG  1 
ATOM   1633 O  OD1 . ASN B 1 65  ? 29.527 18.302  15.380  1.00  8.52  ? 65   ASN F OD1 1 
ATOM   1634 N  ND2 . ASN B 1 65  ? 27.937 19.387  16.599  1.00  10.59 ? 65   ASN F ND2 1 
ATOM   1635 N  N   . PRO B 1 66  ? 30.143 14.434  16.633  1.00  9.81  ? 66   PRO F N   1 
ATOM   1636 C  CA  . PRO B 1 66  ? 31.078 13.996  17.697  1.00  11.49 ? 66   PRO F CA  1 
ATOM   1637 C  C   . PRO B 1 66  ? 32.140 15.061  17.989  1.00  11.66 ? 66   PRO F C   1 
ATOM   1638 O  O   . PRO B 1 66  ? 32.642 15.016  19.113  1.00  14.20 ? 66   PRO F O   1 
ATOM   1639 C  CB  . PRO B 1 66  ? 31.710 12.754  17.109  1.00  12.83 ? 66   PRO F CB  1 
ATOM   1640 C  CG  . PRO B 1 66  ? 31.558 12.881  15.622  1.00  11.61 ? 66   PRO F CG  1 
ATOM   1641 C  CD  . PRO B 1 66  ? 30.239 13.538  15.451  1.00  9.37  ? 66   PRO F CD  1 
ATOM   1642 N  N   . LEU B 1 67  ? 32.440 15.996  17.070  1.00  11.24 ? 67   LEU F N   1 
ATOM   1643 C  CA  . LEU B 1 67  ? 33.479 17.007  17.260  1.00  13.07 ? 67   LEU F CA  1 
ATOM   1644 C  C   . LEU B 1 67  ? 32.915 18.347  17.659  1.00  11.45 ? 67   LEU F C   1 
ATOM   1645 O  O   . LEU B 1 67  ? 33.645 19.302  17.845  1.00  13.66 ? 67   LEU F O   1 
ATOM   1646 C  CB  . LEU B 1 67  ? 34.324 17.169  15.989  1.00  14.37 ? 67   LEU F CB  1 
ATOM   1647 C  CG  . LEU B 1 67  ? 35.186 15.960  15.623  1.00  16.27 ? 67   LEU F CG  1 
ATOM   1648 C  CD1 . LEU B 1 67  ? 35.753 16.082  14.256  1.00  20.27 ? 67   LEU F CD1 1 
ATOM   1649 C  CD2 . LEU B 1 67  ? 36.323 15.813  16.614  1.00  20.24 ? 67   LEU F CD2 1 
ATOM   1650 N  N   . SER B 1 68  ? 31.617 18.453  17.881  1.00  11.34 ? 68   SER F N   1 
ATOM   1651 C  CA  . SER B 1 68  ? 31.005 19.668  18.342  1.00  11.51 ? 68   SER F CA  1 
ATOM   1652 C  C   . SER B 1 68  ? 31.192 20.877  17.426  1.00  11.41 ? 68   SER F C   1 
ATOM   1653 O  O   . SER B 1 68  ? 31.255 22.023  17.873  1.00  13.74 ? 68   SER F O   1 
ATOM   1654 C  CB  . SER B 1 68  ? 31.474 19.994  19.779  1.00  13.56 ? 68   SER F CB  1 
ATOM   1655 O  OG  . SER B 1 68  ? 31.303 18.865  20.633  1.00  15.97 ? 68   SER F OG  1 
ATOM   1656 N  N   . ARG B 1 69  ? 31.166 20.658  16.109  1.00  11.63 ? 69   ARG F N   1 
ATOM   1657 C  CA  . ARG B 1 69  ? 31.275 21.707  15.130  1.00  12.07 ? 69   ARG F CA  1 
ATOM   1658 C  C   . ARG B 1 69  ? 29.917 22.263  14.692  1.00  11.83 ? 69   ARG F C   1 
ATOM   1659 O  O   . ARG B 1 69  ? 28.892 21.816  15.141  1.00  13.03 ? 69   ARG F O   1 
ATOM   1660 C  CB  . ARG B 1 69  ? 32.072 21.167  13.935  1.00  13.82 ? 69   ARG F CB  1 
ATOM   1661 C  CG  . ARG B 1 69  ? 33.547 20.896  14.349  1.00  15.44 ? 69   ARG F CG  1 
ATOM   1662 C  CD  . ARG B 1 69  ? 34.420 20.616  13.222  1.00  19.12 ? 69   ARG F CD  1 
ATOM   1663 N  NE  . ARG B 1 69  ? 35.771 20.340  13.739  1.00  20.16 ? 69   ARG F NE  1 
ATOM   1664 C  CZ  . ARG B 1 69  ? 36.695 19.677  13.066  1.00  24.51 ? 69   ARG F CZ  1 
ATOM   1665 N  NH1 . ARG B 1 69  ? 36.453 19.240  11.827  1.00  27.26 ? 69   ARG F NH1 1 
ATOM   1666 N  NH2 . ARG B 1 69  ? 37.865 19.442  13.625  1.00  25.12 ? 69   ARG F NH2 1 
ATOM   1667 N  N   . LYS B 1 70  ? 29.955 23.295  13.864  1.00  12.86 ? 70   LYS F N   1 
ATOM   1668 C  CA  . LYS B 1 70  ? 28.751 23.876  13.286  1.00  12.98 ? 70   LYS F CA  1 
ATOM   1669 C  C   . LYS B 1 70  ? 28.285 23.092  12.061  1.00  11.47 ? 70   LYS F C   1 
ATOM   1670 O  O   . LYS B 1 70  ? 29.068 22.392  11.464  1.00  11.39 ? 70   LYS F O   1 
ATOM   1671 C  CB  . LYS B 1 70  ? 29.011 25.326  12.882  1.00  14.70 ? 70   LYS F CB  1 
ATOM   1672 C  CG  . LYS B 1 70  ? 29.218 26.307  14.040  1.00  17.47 ? 70   LYS F CG  1 
ATOM   1673 C  CD  . LYS B 1 70  ? 29.100 27.764  13.652  0.10  14.41 ? 70   LYS F CD  1 
ATOM   1674 C  CE  . LYS B 1 70  ? 28.951 28.637  14.888  0.10  14.81 ? 70   LYS F CE  1 
ATOM   1675 N  NZ  . LYS B 1 70  ? 28.974 30.080  14.543  0.10  15.58 ? 70   LYS F NZ  1 
ATOM   1676 N  N   . HIS B 1 71  ? 26.999 23.256  11.756  1.00  10.37 ? 71   HIS F N   1 
ATOM   1677 C  CA  . HIS B 1 71  ? 26.427 22.618  10.601  1.00  9.97  ? 71   HIS F CA  1 
ATOM   1678 C  C   . HIS B 1 71  ? 27.044 23.176  9.295   1.00  9.11  ? 71   HIS F C   1 
ATOM   1679 O  O   . HIS B 1 71  ? 27.240 24.365  9.173   1.00  11.26 ? 71   HIS F O   1 
ATOM   1680 C  CB  . HIS B 1 71  ? 24.909 22.853  10.562  1.00  10.20 ? 71   HIS F CB  1 
ATOM   1681 C  CG  . HIS B 1 71  ? 24.231 22.207  9.408   1.00  9.59  ? 71   HIS F CG  1 
ATOM   1682 N  ND1 . HIS B 1 71  ? 24.042 20.844  9.331   1.00  8.31  ? 71   HIS F ND1 1 
ATOM   1683 C  CD2 . HIS B 1 71  ? 23.700 22.741  8.279   1.00  10.23 ? 71   HIS F CD2 1 
ATOM   1684 C  CE1 . HIS B 1 71  ? 23.426 20.574  8.193   1.00  8.85  ? 71   HIS F CE1 1 
ATOM   1685 N  NE2 . HIS B 1 71  ? 23.237 21.701  7.522   1.00  10.04 ? 71   HIS F NE2 1 
ATOM   1686 N  N   . GLY B 1 72  ? 27.273 22.293  8.341   1.00  9.82  ? 72   GLY F N   1 
ATOM   1687 C  CA  . GLY B 1 72  ? 27.688 22.698  7.022   1.00  11.16 ? 72   GLY F CA  1 
ATOM   1688 C  C   . GLY B 1 72  ? 27.247 21.741  5.946   1.00  10.42 ? 72   GLY F C   1 
ATOM   1689 O  O   . GLY B 1 72  ? 26.423 20.856  6.187   1.00  11.19 ? 72   GLY F O   1 
ATOM   1690 N  N   . GLY B 1 73  ? 27.773 21.927  4.776   1.00  12.71 ? 73   GLY F N   1 
ATOM   1691 C  CA  . GLY B 1 73  ? 27.612 20.971  3.714   1.00  11.94 ? 73   GLY F CA  1 
ATOM   1692 C  C   . GLY B 1 73  ? 28.733 19.945  3.699   1.00  12.05 ? 73   GLY F C   1 
ATOM   1693 O  O   . GLY B 1 73  ? 29.753 20.121  4.369   1.00  12.57 ? 73   GLY F O   1 
ATOM   1694 N  N   . PRO B 1 74  ? 28.572 18.890  2.910   1.00  12.53 ? 74   PRO F N   1 
ATOM   1695 C  CA  . PRO B 1 74  ? 29.506 17.815  2.969   1.00  13.26 ? 74   PRO F CA  1 
ATOM   1696 C  C   . PRO B 1 74  ? 30.910 18.211  2.524   1.00  14.38 ? 74   PRO F C   1 
ATOM   1697 O  O   . PRO B 1 74  ? 31.882 17.620  2.997   1.00  15.47 ? 74   PRO F O   1 
ATOM   1698 C  CB  . PRO B 1 74  ? 28.903 16.735  2.049   1.00  14.20 ? 74   PRO F CB  1 
ATOM   1699 C  CG  . PRO B 1 74  ? 27.899 17.449  1.202   1.00  15.05 ? 74   PRO F CG  1 
ATOM   1700 C  CD  . PRO B 1 74  ? 27.406 18.589  2.072   1.00  13.00 ? 74   PRO F CD  1 
ATOM   1701 N  N   . LYS B 1 75  ? 31.027 19.236  1.684   1.00  14.20 ? 75   LYS F N   1 
ATOM   1702 C  CA  . LYS B 1 75  ? 32.349 19.675  1.224   1.00  15.77 ? 75   LYS F CA  1 
ATOM   1703 C  C   . LYS B 1 75  ? 33.055 20.603  2.200   1.00  16.61 ? 75   LYS F C   1 
ATOM   1704 O  O   . LYS B 1 75  ? 34.230 20.945  1.990   1.00  19.53 ? 75   LYS F O   1 
ATOM   1705 C  CB  . LYS B 1 75  ? 32.231 20.424  -0.080  1.00  16.15 ? 75   LYS F CB  1 
ATOM   1706 C  CG  . LYS B 1 75  ? 31.639 19.640  -1.198  1.00  18.13 ? 75   LYS F CG  1 
ATOM   1707 C  CD  . LYS B 1 75  ? 31.663 20.522  -2.423  1.00  21.38 ? 75   LYS F CD  1 
ATOM   1708 C  CE  . LYS B 1 75  ? 33.000 20.509  -3.156  0.50  23.83 ? 75   LYS F CE  1 
ATOM   1709 N  NZ  . LYS B 1 75  ? 33.428 19.130  -3.523  0.10  23.65 ? 75   LYS F NZ  1 
ATOM   1710 N  N   . ASP B 1 76  ? 32.384 21.062  3.241   1.00  16.88 ? 76   ASP F N   1 
ATOM   1711 C  CA  . ASP B 1 76  ? 32.967 22.076  4.142   1.00  17.13 ? 76   ASP F CA  1 
ATOM   1712 C  C   . ASP B 1 76  ? 33.847 21.402  5.154   1.00  18.04 ? 76   ASP F C   1 
ATOM   1713 O  O   . ASP B 1 76  ? 33.554 20.280  5.591   1.00  19.37 ? 76   ASP F O   1 
ATOM   1714 C  CB  . ASP B 1 76  ? 31.851 22.844  4.824   1.00  16.93 ? 76   ASP F CB  1 
ATOM   1715 C  CG  . ASP B 1 76  ? 31.018 23.623  3.871   0.50  16.16 ? 76   ASP F CG  1 
ATOM   1716 O  OD1 . ASP B 1 76  ? 31.503 23.983  2.777   0.50  19.25 ? 76   ASP F OD1 1 
ATOM   1717 O  OD2 . ASP B 1 76  ? 29.891 23.928  4.255   0.50  13.94 ? 76   ASP F OD2 1 
ATOM   1718 N  N   . GLU B 1 77  ? 34.919 22.065  5.582   1.00  20.17 ? 77   GLU F N   1 
ATOM   1719 C  CA  . GLU B 1 77  ? 35.659 21.553  6.729   1.00  19.95 ? 77   GLU F CA  1 
ATOM   1720 C  C   . GLU B 1 77  ? 34.862 21.723  8.019   1.00  20.30 ? 77   GLU F C   1 
ATOM   1721 O  O   . GLU B 1 77  ? 34.814 20.794  8.859   1.00  21.28 ? 77   GLU F O   1 
ATOM   1722 C  CB  . GLU B 1 77  ? 36.997 22.263  6.886   1.00  22.61 ? 77   GLU F CB  1 
ATOM   1723 C  CG  . GLU B 1 77  ? 37.850 21.752  8.070   0.32  20.19 ? 77   GLU F CG  1 
ATOM   1724 C  CD  . GLU B 1 77  ? 39.218 22.425  8.160   0.10  20.41 ? 77   GLU F CD  1 
ATOM   1725 O  OE1 . GLU B 1 77  ? 39.581 23.201  7.247   0.10  21.46 ? 77   GLU F OE1 1 
ATOM   1726 O  OE2 . GLU B 1 77  ? 39.939 22.164  9.145   0.10  20.69 ? 77   GLU F OE2 1 
ATOM   1727 N  N   . GLU B 1 78  ? 34.174 22.857  8.174   1.00  17.27 ? 78   GLU F N   1 
ATOM   1728 C  CA  . GLU B 1 78  ? 33.304 23.041  9.324   1.00  15.89 ? 78   GLU F CA  1 
ATOM   1729 C  C   . GLU B 1 78  ? 31.958 22.429  8.956   1.00  14.66 ? 78   GLU F C   1 
ATOM   1730 O  O   . GLU B 1 78  ? 31.135 22.984  8.231   1.00  15.36 ? 78   GLU F O   1 
ATOM   1731 C  CB  . GLU B 1 78  ? 33.124 24.493  9.663   1.00  17.30 ? 78   GLU F CB  1 
ATOM   1732 C  CG  . GLU B 1 78  ? 32.407 24.709  10.990  1.00  21.64 ? 78   GLU F CG  1 
ATOM   1733 C  CD  . GLU B 1 78  ? 33.238 24.475  12.329  0.85  23.13 ? 78   GLU F CD  1 
ATOM   1734 O  OE1 . GLU B 1 78  ? 34.512 24.107  12.288  0.85  24.13 ? 78   GLU F OE1 1 
ATOM   1735 O  OE2 . GLU B 1 78  ? 32.576 24.702  13.441  0.85  18.55 ? 78   GLU F OE2 1 
ATOM   1736 N  N   . ARG B 1 79  ? 31.743 21.241  9.475   1.00  11.64 ? 79   ARG F N   1 
ATOM   1737 C  CA  . ARG B 1 79  ? 30.482 20.483  9.297   1.00  10.18 ? 79   ARG F CA  1 
ATOM   1738 C  C   . ARG B 1 79  ? 30.349 19.515  10.417  1.00  9.41  ? 79   ARG F C   1 
ATOM   1739 O  O   . ARG B 1 79  ? 31.314 19.219  11.101  1.00  11.13 ? 79   ARG F O   1 
ATOM   1740 C  CB  . ARG B 1 79  ? 30.460 19.717  7.957   1.00  10.16 ? 79   ARG F CB  1 
ATOM   1741 C  CG  . ARG B 1 79  ? 31.596 18.712  7.831   1.00  11.04 ? 79   ARG F CG  1 
ATOM   1742 C  CD  . ARG B 1 79  ? 31.540 17.823  6.641   1.00  10.49 ? 79   ARG F CD  1 
ATOM   1743 N  NE  . ARG B 1 79  ? 30.737 16.606  6.902   1.00  11.30 ? 79   ARG F NE  1 
ATOM   1744 C  CZ  . ARG B 1 79  ? 30.729 15.529  6.111   1.00  11.03 ? 79   ARG F CZ  1 
ATOM   1745 N  NH1 . ARG B 1 79  ? 31.303 15.568  4.922   1.00  12.71 ? 79   ARG F NH1 1 
ATOM   1746 N  NH2 . ARG B 1 79  ? 30.101 14.400  6.482   1.00  10.75 ? 79   ARG F NH2 1 
ATOM   1747 N  N   . HIS B 1 80  ? 29.142 19.023  10.630  1.00  8.85  ? 80   HIS F N   1 
ATOM   1748 C  CA  . HIS B 1 80  ? 28.938 17.869  11.478  1.00  8.74  ? 80   HIS F CA  1 
ATOM   1749 C  C   . HIS B 1 80  ? 29.358 16.623  10.721  1.00  8.48  ? 80   HIS F C   1 
ATOM   1750 O  O   . HIS B 1 80  ? 29.184 16.553  9.513   1.00  8.95  ? 80   HIS F O   1 
ATOM   1751 C  CB  . HIS B 1 80  ? 27.448 17.782  11.789  1.00  7.71  ? 80   HIS F CB  1 
ATOM   1752 C  CG  . HIS B 1 80  ? 26.869 18.977  12.438  1.00  9.12  ? 80   HIS F CG  1 
ATOM   1753 N  ND1 . HIS B 1 80  ? 25.571 19.390  12.186  1.00  7.85  ? 80   HIS F ND1 1 
ATOM   1754 C  CD2 . HIS B 1 80  ? 27.372 19.802  13.391  1.00  10.41 ? 80   HIS F CD2 1 
ATOM   1755 C  CE1 . HIS B 1 80  ? 25.318 20.413  13.004  1.00  10.70 ? 80   HIS F CE1 1 
ATOM   1756 N  NE2 . HIS B 1 80  ? 26.397 20.681  13.723  1.00  12.05 ? 80   HIS F NE2 1 
ATOM   1757 N  N   . VAL B 1 81  ? 29.786 15.584  11.434  1.00  8.34  ? 81   VAL F N   1 
ATOM   1758 C  CA  . VAL B 1 81  ? 30.092 14.353  10.767  1.00  9.09  ? 81   VAL F CA  1 
ATOM   1759 C  C   . VAL B 1 81  ? 28.877 13.861  9.982   1.00  8.88  ? 81   VAL F C   1 
ATOM   1760 O  O   . VAL B 1 81  ? 28.987 13.362  8.871   1.00  9.47  ? 81   VAL F O   1 
ATOM   1761 C  CB  . VAL B 1 81  ? 30.591 13.279  11.737  1.00  9.92  ? 81   VAL F CB  1 
ATOM   1762 C  CG1 . VAL B 1 81  ? 30.606 11.895  10.999  1.00  10.35 ? 81   VAL F CG1 1 
ATOM   1763 C  CG2 . VAL B 1 81  ? 32.009 13.625  12.195  1.00  11.64 ? 81   VAL F CG2 1 
ATOM   1764 N  N   . GLY B 1 82  ? 27.673 14.028  10.526  1.00  8.78  ? 82   GLY F N   1 
ATOM   1765 C  CA  . GLY B 1 82  ? 26.475 13.568  9.849   1.00  8.91  ? 82   GLY F CA  1 
ATOM   1766 C  C   . GLY B 1 82  ? 25.937 14.356  8.689   1.00  9.07  ? 82   GLY F C   1 
ATOM   1767 O  O   . GLY B 1 82  ? 24.887 13.993  8.133   1.00  10.16 ? 82   GLY F O   1 
ATOM   1768 N  N   . ASP B 1 83  ? 26.610 15.426  8.281   1.00  8.36  ? 83   ASP F N   1 
ATOM   1769 C  CA  . ASP B 1 83  ? 26.138 16.323  7.223   1.00  8.57  ? 83   ASP F CA  1 
ATOM   1770 C  C   . ASP B 1 83  ? 26.435 15.777  5.851   1.00  8.86  ? 83   ASP F C   1 
ATOM   1771 O  O   . ASP B 1 83  ? 27.452 16.072  5.263   1.00  12.80 ? 83   ASP F O   1 
ATOM   1772 C  CB  . ASP B 1 83  ? 26.762 17.691  7.426   1.00  9.10  ? 83   ASP F CB  1 
ATOM   1773 C  CG  . ASP B 1 83  ? 26.190 18.432  8.639   1.00  8.05  ? 83   ASP F CG  1 
ATOM   1774 O  OD1 . ASP B 1 83  ? 25.155 17.989  9.189   1.00  8.50  ? 83   ASP F OD1 1 
ATOM   1775 O  OD2 . ASP B 1 83  ? 26.853 19.432  9.024   1.00  8.93  ? 83   ASP F OD2 1 
ATOM   1776 N  N   . LEU B 1 84  ? 25.456 15.135  5.255   1.00  8.74  ? 84   LEU F N   1 
ATOM   1777 C  CA  . LEU B 1 84  ? 25.596 14.554  3.952   1.00  9.94  ? 84   LEU F CA  1 
ATOM   1778 C  C   . LEU B 1 84  ? 24.917 15.410  2.865   1.00  10.33 ? 84   LEU F C   1 
ATOM   1779 O  O   . LEU B 1 84  ? 24.785 14.954  1.754   1.00  14.02 ? 84   LEU F O   1 
ATOM   1780 C  CB  . LEU B 1 84  ? 25.092 13.099  3.909   1.00  10.43 ? 84   LEU F CB  1 
ATOM   1781 C  CG  . LEU B 1 84  ? 25.888 12.146  4.805   1.00  12.47 ? 84   LEU F CG  1 
ATOM   1782 C  CD1 . LEU B 1 84  ? 25.236 10.747  4.740   1.00  14.57 ? 84   LEU F CD1 1 
ATOM   1783 C  CD2 . LEU B 1 84  ? 27.406 12.123  4.375   1.00  15.08 ? 84   LEU F CD2 1 
ATOM   1784 N  N   . GLY B 1 85  ? 24.477 16.597  3.176   1.00  9.55  ? 85   GLY F N   1 
ATOM   1785 C  CA  . GLY B 1 85  ? 24.002 17.510  2.144   1.00  9.78  ? 85   GLY F CA  1 
ATOM   1786 C  C   . GLY B 1 85  ? 22.575 17.187  1.779   1.00  9.22  ? 85   GLY F C   1 
ATOM   1787 O  O   . GLY B 1 85  ? 21.684 17.120  2.640   1.00  10.26 ? 85   GLY F O   1 
ATOM   1788 N  N   . ASN B 1 86  ? 22.301 17.126  0.471   1.00  8.97  ? 86   ASN F N   1 
ATOM   1789 C  CA  . ASN B 1 86  ? 20.989 16.929  -0.074  1.00  8.32  ? 86   ASN F CA  1 
ATOM   1790 C  C   . ASN B 1 86  ? 20.964 15.753  -1.020  1.00  8.78  ? 86   ASN F C   1 
ATOM   1791 O  O   . ASN B 1 86  ? 21.934 15.484  -1.714  1.00  11.65 ? 86   ASN F O   1 
ATOM   1792 C  CB  . ASN B 1 86  ? 20.553 18.196  -0.835  1.00  9.24  ? 86   ASN F CB  1 
ATOM   1793 C  CG  . ASN B 1 86  ? 20.236 19.331  0.111   1.00  8.51  ? 86   ASN F CG  1 
ATOM   1794 O  OD1 . ASN B 1 86  ? 19.266 19.257  0.827   1.00  9.86  ? 86   ASN F OD1 1 
ATOM   1795 N  ND2 . ASN B 1 86  ? 21.056 20.381  0.094   1.00  11.16 ? 86   ASN F ND2 1 
ATOM   1796 N  N   . VAL B 1 87  ? 19.826 15.107  -1.100  1.00  8.67  ? 87   VAL F N   1 
ATOM   1797 C  CA  . VAL B 1 87  ? 19.524 14.214  -2.236  1.00  8.90  ? 87   VAL F CA  1 
ATOM   1798 C  C   . VAL B 1 87  ? 18.499 14.865  -3.140  1.00  8.82  ? 87   VAL F C   1 
ATOM   1799 O  O   . VAL B 1 87  ? 17.757 15.709  -2.696  1.00  10.44 ? 87   VAL F O   1 
ATOM   1800 C  CB  . VAL B 1 87  ? 19.087 12.836  -1.733  1.00  9.76  ? 87   VAL F CB  1 
ATOM   1801 C  CG1 . VAL B 1 87  ? 20.245 12.225  -0.931  1.00  12.05 ? 87   VAL F CG1 1 
ATOM   1802 C  CG2 . VAL B 1 87  ? 17.836 12.873  -0.954  1.00  11.09 ? 87   VAL F CG2 1 
ATOM   1803 N  N   . THR B 1 88  ? 18.482 14.480  -4.399  1.00  8.86  ? 88   THR F N   1 
ATOM   1804 C  CA  . THR B 1 88  ? 17.618 15.106  -5.392  1.00  9.76  ? 88   THR F CA  1 
ATOM   1805 C  C   . THR B 1 88  ? 16.613 14.113  -5.935  1.00  8.86  ? 88   THR F C   1 
ATOM   1806 O  O   . THR B 1 88  ? 16.958 13.089  -6.471  1.00  10.12 ? 88   THR F O   1 
ATOM   1807 C  CB  . THR B 1 88  ? 18.474 15.688  -6.522  1.00  10.02 ? 88   THR F CB  1 
ATOM   1808 O  OG1 . THR B 1 88  ? 19.314 16.707  -6.009  1.00  12.39 ? 88   THR F OG1 1 
ATOM   1809 C  CG2 . THR B 1 88  ? 17.597 16.322  -7.608  1.00  12.14 ? 88   THR F CG2 1 
ATOM   1810 N  N   . ALA B 1 89  ? 15.345 14.460  -5.792  1.00  9.74  ? 89   ALA F N   1 
ATOM   1811 C  CA  . ALA B 1 89  ? 14.268 13.658  -6.329  1.00  9.84  ? 89   ALA F CA  1 
ATOM   1812 C  C   . ALA B 1 89  ? 13.778 14.243  -7.654  1.00  10.61 ? 89   ALA F C   1 
ATOM   1813 O  O   . ALA B 1 89  ? 13.718 15.450  -7.861  1.00  10.48 ? 89   ALA F O   1 
ATOM   1814 C  CB  . ALA B 1 89  ? 13.081 13.614  -5.329  1.00  11.72 ? 89   ALA F CB  1 
ATOM   1815 N  N   . ASP B 1 90  ? 13.484 13.345  -8.575  1.00  11.29 ? 90   ASP F N   1 
ATOM   1816 C  CA  . ASP B 1 90  ? 12.975 13.694  -9.888  1.00  12.53 ? 90   ASP F CA  1 
ATOM   1817 C  C   . ASP B 1 90  ? 11.474 13.885  -9.869  1.00  13.22 ? 90   ASP F C   1 
ATOM   1818 O  O   . ASP B 1 90  ? 10.826 13.893  -8.829  1.00  13.53 ? 90   ASP F O   1 
ATOM   1819 C  CB  . ASP B 1 90  ? 13.417 12.656  -10.884 1.00  14.90 ? 90   ASP F CB  1 
ATOM   1820 C  CG  . ASP B 1 90  ? 12.736 11.346  -10.741 1.00  18.24 ? 90   ASP F CG  1 
ATOM   1821 O  OD1 . ASP B 1 90  ? 11.762 11.188  -9.962  0.85  16.96 ? 90   ASP F OD1 1 
ATOM   1822 O  OD2 . ASP B 1 90  ? 13.245 10.424  -11.432 0.85  22.22 ? 90   ASP F OD2 1 
ATOM   1823 N  N   . LYS B 1 91  ? 10.881 14.137  -11.038 1.00  13.51 ? 91   LYS F N   1 
ATOM   1824 C  CA  . LYS B 1 91  ? 9.474  14.462  -11.122 1.00  15.30 ? 91   LYS F CA  1 
ATOM   1825 C  C   . LYS B 1 91  ? 8.596  13.324  -10.625 1.00  15.12 ? 91   LYS F C   1 
ATOM   1826 O  O   . LYS B 1 91  ? 7.511  13.589  -10.115 1.00  19.67 ? 91   LYS F O   1 
ATOM   1827 C  CB  . LYS B 1 91  ? 9.169  14.819  -12.604 1.00  16.56 ? 91   LYS F CB  1 
ATOM   1828 C  CG  . LYS B 1 91  ? 7.822  15.275  -12.935 1.00  18.12 ? 91   LYS F CG  1 
ATOM   1829 C  CD  . LYS B 1 91  ? 7.476  16.559  -12.319 1.00  19.10 ? 91   LYS F CD  1 
ATOM   1830 C  CE  . LYS B 1 91  ? 6.246  17.138  -13.000 1.00  24.57 ? 91   LYS F CE  1 
ATOM   1831 N  NZ  . LYS B 1 91  ? 5.832  18.378  -12.294 1.00  30.20 ? 91   LYS F NZ  1 
ATOM   1832 N  N   . ASP B 1 92  ? 9.068  12.076  -10.757 1.00  14.53 ? 92   ASP F N   1 
ATOM   1833 C  CA  . ASP B 1 92  ? 8.385  10.914  -10.225 1.00  14.47 ? 92   ASP F CA  1 
ATOM   1834 C  C   . ASP B 1 92  ? 8.564  10.687  -8.733  1.00  14.80 ? 92   ASP F C   1 
ATOM   1835 O  O   . ASP B 1 92  ? 7.984  9.727   -8.204  1.00  16.78 ? 92   ASP F O   1 
ATOM   1836 C  CB  . ASP B 1 92  ? 8.789  9.632   -10.953 0.50  12.92 ? 92   ASP F CB  1 
ATOM   1837 C  CG  . ASP B 1 92  ? 7.850  9.296   -12.122 0.10  14.77 ? 92   ASP F CG  1 
ATOM   1838 O  OD1 . ASP B 1 92  ? 6.606  9.307   -11.943 0.10  14.64 ? 92   ASP F OD1 1 
ATOM   1839 O  OD2 . ASP B 1 92  ? 8.355  9.003   -13.219 0.10  16.18 ? 92   ASP F OD2 1 
ATOM   1840 N  N   . GLY B 1 93  ? 9.275  11.577  -8.056  1.00  14.12 ? 93   GLY F N   1 
ATOM   1841 C  CA  . GLY B 1 93  ? 9.484  11.484  -6.599  1.00  12.65 ? 93   GLY F CA  1 
ATOM   1842 C  C   . GLY B 1 93  ? 10.542 10.517  -6.154  1.00  11.82 ? 93   GLY F C   1 
ATOM   1843 O  O   . GLY B 1 93  ? 10.628 10.219  -4.953  1.00  12.13 ? 93   GLY F O   1 
ATOM   1844 N  N   . VAL B 1 94  ? 11.389 10.070  -7.064  1.00  11.62 ? 94   VAL F N   1 
ATOM   1845 C  CA  . VAL B 1 94  ? 12.470 9.154   -6.750  1.00  11.22 ? 94   VAL F CA  1 
ATOM   1846 C  C   . VAL B 1 94  ? 13.804 9.865   -6.745  1.00  10.23 ? 94   VAL F C   1 
ATOM   1847 O  O   . VAL B 1 94  ? 14.158 10.562  -7.694  1.00  11.31 ? 94   VAL F O   1 
ATOM   1848 C  CB  . VAL B 1 94  ? 12.502 7.989   -7.740  1.00  13.58 ? 94   VAL F CB  1 
ATOM   1849 C  CG1 . VAL B 1 94  ? 13.556 6.986   -7.364  1.00  16.15 ? 94   VAL F CG1 1 
ATOM   1850 C  CG2 . VAL B 1 94  ? 11.118 7.299   -7.781  1.00  15.42 ? 94   VAL F CG2 1 
ATOM   1851 N  N   . ALA B 1 95  ? 14.531 9.671   -5.665  1.00  10.51 ? 95   ALA F N   1 
ATOM   1852 C  CA  . ALA B 1 95  ? 15.934 10.149  -5.519  1.00  10.97 ? 95   ALA F CA  1 
ATOM   1853 C  C   . ALA B 1 95  ? 16.830 8.953   -5.662  1.00  11.01 ? 95   ALA F C   1 
ATOM   1854 O  O   . ALA B 1 95  ? 16.750 8.014   -4.845  1.00  13.70 ? 95   ALA F O   1 
ATOM   1855 C  CB  . ALA B 1 95  ? 16.185 10.850  -4.178  1.00  12.80 ? 95   ALA F CB  1 
ATOM   1856 N  N   . ASP B 1 96  ? 17.723 8.982   -6.608  1.00  11.53 ? 96   ASP F N   1 
ATOM   1857 C  CA  . ASP B 1 96  ? 18.801 8.030   -6.759  1.00  12.86 ? 96   ASP F CA  1 
ATOM   1858 C  C   . ASP B 1 96  ? 19.994 8.591   -6.027  1.00  13.41 ? 96   ASP F C   1 
ATOM   1859 O  O   . ASP B 1 96  ? 20.559 9.613   -6.388  1.00  17.40 ? 96   ASP F O   1 
ATOM   1860 C  CB  . ASP B 1 96  ? 19.120 7.811   -8.235  1.00  16.20 ? 96   ASP F CB  1 
ATOM   1861 C  CG  A ASP B 1 96  ? 18.285 6.686   -8.873  0.50  17.07 ? 96   ASP F CG  1 
ATOM   1862 C  CG  B ASP B 1 96  ? 19.483 6.382   -8.546  0.50  21.49 ? 96   ASP F CG  1 
ATOM   1863 O  OD1 A ASP B 1 96  ? 17.582 5.889   -8.167  0.50  19.91 ? 96   ASP F OD1 1 
ATOM   1864 O  OD1 B ASP B 1 96  ? 20.606 6.029   -8.125  0.50  25.64 ? 96   ASP F OD1 1 
ATOM   1865 O  OD2 A ASP B 1 96  ? 18.283 6.651   -10.129 0.50  22.80 ? 96   ASP F OD2 1 
ATOM   1866 O  OD2 B ASP B 1 96  ? 18.713 5.609   -9.160  0.50  28.64 ? 96   ASP F OD2 1 
ATOM   1867 N  N   . VAL B 1 97  ? 20.400 7.955   -4.959  1.00  10.88 ? 97   VAL F N   1 
ATOM   1868 C  CA  . VAL B 1 97  ? 21.448 8.454   -4.062  1.00  12.07 ? 97   VAL F CA  1 
ATOM   1869 C  C   . VAL B 1 97  ? 22.733 7.832   -4.478  1.00  11.53 ? 97   VAL F C   1 
ATOM   1870 O  O   . VAL B 1 97  ? 22.847 6.603   -4.638  1.00  11.15 ? 97   VAL F O   1 
ATOM   1871 C  CB  . VAL B 1 97  ? 21.123 8.095   -2.596  1.00  11.13 ? 97   VAL F CB  1 
ATOM   1872 C  CG1 . VAL B 1 97  ? 22.171 8.605   -1.628  1.00  13.94 ? 97   VAL F CG1 1 
ATOM   1873 C  CG2 . VAL B 1 97  ? 19.733 8.684   -2.226  1.00  12.29 ? 97   VAL F CG2 1 
ATOM   1874 N  N   . SER B 1 98  ? 23.776 8.650   -4.632  1.00  12.94 ? 98   SER F N   1 
ATOM   1875 C  CA  . SER B 1 98  ? 25.124 8.193   -4.931  1.00  13.86 ? 98   SER F CA  1 
ATOM   1876 C  C   . SER B 1 98  ? 26.064 9.250   -4.359  1.00  14.28 ? 98   SER F C   1 
ATOM   1877 O  O   . SER B 1 98  ? 26.241 10.339  -4.930  1.00  16.57 ? 98   SER F O   1 
ATOM   1878 C  CB  . SER B 1 98  ? 25.369 8.080   -6.437  1.00  17.16 ? 98   SER F CB  1 
ATOM   1879 O  OG  . SER B 1 98  ? 26.627 7.449   -6.692  1.00  23.65 ? 98   SER F OG  1 
ATOM   1880 N  N   . ILE B 1 99  ? 26.688 8.922   -3.253  1.00  12.72 ? 99   ILE F N   1 
ATOM   1881 C  CA  . ILE B 1 99  ? 27.526 9.853   -2.477  1.00  13.28 ? 99   ILE F CA  1 
ATOM   1882 C  C   . ILE B 1 99  ? 28.824 9.084   -2.150  1.00  12.59 ? 99   ILE F C   1 
ATOM   1883 O  O   . ILE B 1 99  ? 28.812 7.885   -1.853  1.00  13.92 ? 99   ILE F O   1 
ATOM   1884 C  CB  . ILE B 1 99  ? 26.784 10.266  -1.145  1.00  12.24 ? 99   ILE F CB  1 
ATOM   1885 C  CG1 . ILE B 1 99  ? 25.619 11.219  -1.412  1.00  15.50 ? 99   ILE F CG1 1 
ATOM   1886 C  CG2 . ILE B 1 99  ? 27.690 10.868  -0.118  1.00  16.89 ? 99   ILE F CG2 1 
ATOM   1887 C  CD1 . ILE B 1 99  ? 24.664 11.497  -0.244  1.00  15.57 ? 99   ILE F CD1 1 
ATOM   1888 N  N   . GLU B 1 100 ? 29.955 9.764   -2.154  1.00  13.04 ? 100  GLU F N   1 
ATOM   1889 C  CA  . GLU B 1 100 ? 31.162 9.255   -1.521  1.00  13.55 ? 100  GLU F CA  1 
ATOM   1890 C  C   . GLU B 1 100 ? 31.512 10.292  -0.466  1.00  12.92 ? 100  GLU F C   1 
ATOM   1891 O  O   . GLU B 1 100 ? 31.531 11.503  -0.744  1.00  14.12 ? 100  GLU F O   1 
ATOM   1892 C  CB  . GLU B 1 100 ? 32.311 9.109   -2.528  1.00  16.94 ? 100  GLU F CB  1 
ATOM   1893 C  CG  . GLU B 1 100 ? 32.327 7.820   -3.405  1.00  22.74 ? 100  GLU F CG  1 
ATOM   1894 C  CD  . GLU B 1 100 ? 33.679 7.533   -4.066  1.00  24.99 ? 100  GLU F CD  1 
ATOM   1895 O  OE1 . GLU B 1 100 ? 34.716 7.584   -3.349  1.00  35.31 ? 100  GLU F OE1 1 
ATOM   1896 O  OE2 . GLU B 1 100 ? 33.692 7.230   -5.283  1.00  37.65 ? 100  GLU F OE2 1 
ATOM   1897 N  N   . ASP B 1 101 ? 31.775 9.826   0.747   1.00  11.63 ? 101  ASP F N   1 
ATOM   1898 C  CA  . ASP B 1 101 ? 32.080 10.740  1.847   1.00  12.05 ? 101  ASP F CA  1 
ATOM   1899 C  C   . ASP B 1 101 ? 33.231 10.231  2.674   1.00  12.84 ? 101  ASP F C   1 
ATOM   1900 O  O   . ASP B 1 101 ? 33.287 9.059   3.021   1.00  14.41 ? 101  ASP F O   1 
ATOM   1901 C  CB  . ASP B 1 101 ? 30.835 10.991  2.742   1.00  13.26 ? 101  ASP F CB  1 
ATOM   1902 C  CG  . ASP B 1 101 ? 31.030 12.181  3.700   1.00  14.26 ? 101  ASP F CG  1 
ATOM   1903 O  OD1 . ASP B 1 101 ? 30.974 13.346  3.163   1.00  17.92 ? 101  ASP F OD1 1 
ATOM   1904 O  OD2 . ASP B 1 101 ? 31.376 11.983  4.879   1.00  13.92 ? 101  ASP F OD2 1 
ATOM   1905 N  N   . SER B 1 102 ? 34.131 11.138  2.992   1.00  13.38 ? 102  SER F N   1 
ATOM   1906 C  CA  . SER B 1 102 ? 35.366 10.817  3.691   1.00  14.23 ? 102  SER F CA  1 
ATOM   1907 C  C   . SER B 1 102 ? 35.323 11.126  5.155   1.00  14.33 ? 102  SER F C   1 
ATOM   1908 O  O   . SER B 1 102 ? 36.274 10.812  5.861   1.00  16.37 ? 102  SER F O   1 
ATOM   1909 C  CB  . SER B 1 102 ? 36.501 11.629  3.010   1.00  16.20 ? 102  SER F CB  1 
ATOM   1910 O  OG  A SER B 1 102 ? 36.826 10.858  1.877   0.64  21.16 ? 102  SER F OG  1 
ATOM   1911 O  OG  B SER B 1 102 ? 36.444 12.923  3.571   0.36  18.09 ? 102  SER F OG  1 
ATOM   1912 N  N   . VAL B 1 103 ? 34.222 11.695  5.666   1.00  11.60 ? 103  VAL F N   1 
ATOM   1913 C  CA  . VAL B 1 103 ? 34.117 12.085  7.053   1.00  11.31 ? 103  VAL F CA  1 
ATOM   1914 C  C   . VAL B 1 103 ? 33.376 11.047  7.885   1.00  11.83 ? 103  VAL F C   1 
ATOM   1915 O  O   . VAL B 1 103 ? 33.790 10.698  8.971   1.00  13.43 ? 103  VAL F O   1 
ATOM   1916 C  CB  . VAL B 1 103 ? 33.520 13.511  7.184   1.00  12.74 ? 103  VAL F CB  1 
ATOM   1917 C  CG1 . VAL B 1 103 ? 33.283 13.913  8.588   1.00  13.94 ? 103  VAL F CG1 1 
ATOM   1918 C  CG2 . VAL B 1 103 ? 34.425 14.516  6.480   1.00  13.88 ? 103  VAL F CG2 1 
ATOM   1919 N  N   . ILE B 1 104 ? 32.263 10.540  7.392   1.00  10.26 ? 104  ILE F N   1 
ATOM   1920 C  CA  . ILE B 1 104 ? 31.605 9.405   8.048   1.00  11.05 ? 104  ILE F CA  1 
ATOM   1921 C  C   . ILE B 1 104 ? 32.515 8.179   7.925   1.00  10.99 ? 104  ILE F C   1 
ATOM   1922 O  O   . ILE B 1 104 ? 33.412 8.093   7.033   1.00  10.99 ? 104  ILE F O   1 
ATOM   1923 C  CB  . ILE B 1 104 ? 30.211 9.111   7.425   1.00  9.95  ? 104  ILE F CB  1 
ATOM   1924 C  CG1 . ILE B 1 104 ? 30.281 8.811   5.922   1.00  11.28 ? 104  ILE F CG1 1 
ATOM   1925 C  CG2 . ILE B 1 104 ? 29.236 10.262  7.751   1.00  11.63 ? 104  ILE F CG2 1 
ATOM   1926 C  CD1 . ILE B 1 104 ? 29.033 8.174   5.358   1.00  11.41 ? 104  ILE F CD1 1 
ATOM   1927 N  N   . SER B 1 105 ? 32.257 7.191   8.783   1.00  10.24 ? 105  SER F N   1 
ATOM   1928 C  CA  . SER B 1 105 ? 32.977 5.911   8.757   1.00  10.25 ? 105  SER F CA  1 
ATOM   1929 C  C   . SER B 1 105 ? 32.023 4.803   9.214   1.00  9.59  ? 105  SER F C   1 
ATOM   1930 O  O   . SER B 1 105 ? 31.013 5.066   9.831   1.00  9.90  ? 105  SER F O   1 
ATOM   1931 C  CB  . SER B 1 105 ? 34.180 5.993   9.678   1.00  11.88 ? 105  SER F CB  1 
ATOM   1932 O  OG  . SER B 1 105 ? 34.972 4.844   9.403   1.00  14.81 ? 105  SER F OG  1 
ATOM   1933 N  N   . LEU B 1 106 ? 32.384 3.581   8.890   1.00  9.93  ? 106  LEU F N   1 
ATOM   1934 C  CA  . LEU B 1 106 ? 31.708 2.401   9.398   1.00  11.08 ? 106  LEU F CA  1 
ATOM   1935 C  C   . LEU B 1 106 ? 32.478 1.726   10.529  1.00  12.93 ? 106  LEU F C   1 
ATOM   1936 O  O   . LEU B 1 106 ? 32.070 0.673   10.998  1.00  15.15 ? 106  LEU F O   1 
ATOM   1937 C  CB  . LEU B 1 106 ? 31.402 1.409   8.278   1.00  11.22 ? 106  LEU F CB  1 
ATOM   1938 C  CG  . LEU B 1 106 ? 30.595 1.979   7.130   1.00  10.88 ? 106  LEU F CG  1 
ATOM   1939 C  CD1 . LEU B 1 106 ? 30.297 0.891   6.146   1.00  12.33 ? 106  LEU F CD1 1 
ATOM   1940 C  CD2 . LEU B 1 106 ? 29.279 2.618   7.587   1.00  11.38 ? 106  LEU F CD2 1 
ATOM   1941 N  N   . SER B 1 107 ? 33.516 2.390   11.007  1.00  14.94 ? 107  SER F N   1 
ATOM   1942 C  CA  . SER B 1 107 ? 34.236 1.955   12.222  1.00  17.10 ? 107  SER F CA  1 
ATOM   1943 C  C   . SER B 1 107 ? 34.899 3.192   12.880  1.00  18.10 ? 107  SER F C   1 
ATOM   1944 O  O   . SER B 1 107 ? 34.991 4.269   12.310  1.00  19.76 ? 107  SER F O   1 
ATOM   1945 C  CB  . SER B 1 107 ? 35.263 0.875   11.872  0.50  17.37 ? 107  SER F CB  1 
ATOM   1946 O  OG  . SER B 1 107 ? 36.290 1.423   11.074  0.50  19.03 ? 107  SER F OG  1 
ATOM   1947 N  N   . GLY B 1 108 ? 35.431 3.021   14.091  1.00  20.07 ? 108  GLY F N   1 
ATOM   1948 C  CA  . GLY B 1 108 ? 36.065 4.158   14.803  1.00  20.02 ? 108  GLY F CA  1 
ATOM   1949 C  C   . GLY B 1 108 ? 35.133 5.234   15.337  1.00  20.76 ? 108  GLY F C   1 
ATOM   1950 O  O   . GLY B 1 108 ? 33.928 5.051   15.423  1.00  22.19 ? 108  GLY F O   1 
ATOM   1951 N  N   . ASP B 1 109 ? 35.673 6.382   15.748  1.00  21.77 ? 109  ASP F N   1 
ATOM   1952 C  CA  . ASP B 1 109 ? 34.831 7.326   16.493  1.00  20.93 ? 109  ASP F CA  1 
ATOM   1953 C  C   . ASP B 1 109 ? 33.819 8.071   15.633  1.00  20.10 ? 109  ASP F C   1 
ATOM   1954 O  O   . ASP B 1 109 ? 32.836 8.659   16.165  1.00  21.46 ? 109  ASP F O   1 
ATOM   1955 C  CB  . ASP B 1 109 ? 35.674 8.336   17.237  1.00  21.94 ? 109  ASP F CB  1 
ATOM   1956 C  CG  . ASP B 1 109 ? 34.944 8.914   18.447  0.50  21.60 ? 109  ASP F CG  1 
ATOM   1957 O  OD1 . ASP B 1 109 ? 34.334 8.148   19.224  0.50  24.18 ? 109  ASP F OD1 1 
ATOM   1958 O  OD2 . ASP B 1 109 ? 34.987 10.129  18.623  0.50  19.71 ? 109  ASP F OD2 1 
ATOM   1959 N  N   . HIS B 1 110 ? 34.066 8.084   14.328  1.00  16.86 ? 110  HIS F N   1 
ATOM   1960 C  CA  . HIS B 1 110 ? 33.074 8.657   13.399  1.00  16.30 ? 110  HIS F CA  1 
ATOM   1961 C  C   . HIS B 1 110 ? 32.142 7.633   12.840  1.00  13.33 ? 110  HIS F C   1 
ATOM   1962 O  O   . HIS B 1 110 ? 31.469 7.877   11.843  1.00  13.57 ? 110  HIS F O   1 
ATOM   1963 C  CB  . HIS B 1 110 ? 33.718 9.432   12.264  1.00  14.95 ? 110  HIS F CB  1 
ATOM   1964 C  CG  . HIS B 1 110 ? 34.461 10.641  12.740  1.00  18.88 ? 110  HIS F CG  1 
ATOM   1965 N  ND1 . HIS B 1 110 ? 35.072 11.521  11.882  1.00  22.86 ? 110  HIS F ND1 1 
ATOM   1966 C  CD2 . HIS B 1 110 ? 34.658 11.123  13.992  1.00  20.66 ? 110  HIS F CD2 1 
ATOM   1967 C  CE1 . HIS B 1 110 ? 35.639 12.494  12.584  1.00  23.57 ? 110  HIS F CE1 1 
ATOM   1968 N  NE2 . HIS B 1 110 ? 35.401 12.276  13.866  1.00  25.27 ? 110  HIS F NE2 1 
ATOM   1969 N  N   . CYS B 1 111 ? 32.099 6.475   13.492  1.00  13.10 ? 111  CYS F N   1 
ATOM   1970 C  CA  . CYS B 1 111 ? 31.203 5.388   13.081  1.00  12.32 ? 111  CYS F CA  1 
ATOM   1971 C  C   . CYS B 1 111 ? 29.763 5.777   13.171  1.00  10.16 ? 111  CYS F C   1 
ATOM   1972 O  O   . CYS B 1 111 ? 29.317 6.324   14.167  1.00  11.27 ? 111  CYS F O   1 
ATOM   1973 C  CB  . CYS B 1 111 ? 31.499 4.097   13.936  1.00  15.26 ? 111  CYS F CB  1 
ATOM   1974 S  SG  . CYS B 1 111 ? 30.581 2.727   13.385  1.00  20.89 ? 111  CYS F SG  1 
ATOM   1975 N  N   . ILE B 1 112 ? 29.026 5.465   12.122  1.00  9.13  ? 112  ILE F N   1 
ATOM   1976 C  CA  . ILE B 1 112 ? 27.595 5.759   12.020  1.00  9.10  ? 112  ILE F CA  1 
ATOM   1977 C  C   . ILE B 1 112 ? 26.709 4.549   12.225  1.00  8.60  ? 112  ILE F C   1 
ATOM   1978 O  O   . ILE B 1 112 ? 25.518 4.690   12.219  1.00  8.20  ? 112  ILE F O   1 
ATOM   1979 C  CB  . ILE B 1 112 ? 27.266 6.467   10.683  1.00  9.22  ? 112  ILE F CB  1 
ATOM   1980 C  CG1 . ILE B 1 112 ? 27.585 5.574   9.487   1.00  9.03  ? 112  ILE F CG1 1 
ATOM   1981 C  CG2 . ILE B 1 112 ? 28.003 7.812   10.577  1.00  11.63 ? 112  ILE F CG2 1 
ATOM   1982 C  CD1 . ILE B 1 112 ? 27.109 6.136   8.146   1.00  12.18 ? 112  ILE F CD1 1 
ATOM   1983 N  N   . ILE B 1 113 ? 27.322 3.393   12.458  1.00  8.95  ? 113  ILE F N   1 
ATOM   1984 C  CA  . ILE B 1 113 ? 26.509 2.194   12.733  1.00  9.25  ? 113  ILE F CA  1 
ATOM   1985 C  C   . ILE B 1 113 ? 25.725 2.422   14.008  1.00  8.46  ? 113  ILE F C   1 
ATOM   1986 O  O   . ILE B 1 113 ? 26.264 2.868   15.025  1.00  9.19  ? 113  ILE F O   1 
ATOM   1987 C  CB  A ILE B 1 113 ? 27.331 0.866   12.598  0.70  10.43 ? 113  ILE F CB  1 
ATOM   1988 C  CB  B ILE B 1 113 ? 27.511 1.003   13.060  0.30  8.20  ? 113  ILE F CB  1 
ATOM   1989 C  CG1 A ILE B 1 113 ? 27.643 0.659   11.097  0.70  11.99 ? 113  ILE F CG1 1 
ATOM   1990 C  CG1 B ILE B 1 113 ? 28.391 0.693   11.840  0.30  6.62  ? 113  ILE F CG1 1 
ATOM   1991 C  CG2 A ILE B 1 113 ? 26.533 -0.274  13.099  0.70  10.58 ? 113  ILE F CG2 1 
ATOM   1992 C  CG2 B ILE B 1 113 ? 26.809 -0.263  13.563  0.30  8.47  ? 113  ILE F CG2 1 
ATOM   1993 C  CD1 A ILE B 1 113 ? 28.653 -0.368  10.711  0.70  12.23 ? 113  ILE F CD1 1 
ATOM   1994 C  CD1 B ILE B 1 113 ? 27.607 0.346   10.553  0.30  5.50  ? 113  ILE F CD1 1 
ATOM   1995 N  N   . GLY B 1 114 ? 24.448 2.094   14.005  1.00  7.30  ? 114  GLY F N   1 
ATOM   1996 C  CA  . GLY B 1 114 ? 23.628 2.284   15.179  1.00  8.16  ? 114  GLY F CA  1 
ATOM   1997 C  C   . GLY B 1 114 ? 23.065 3.665   15.318  1.00  7.16  ? 114  GLY F C   1 
ATOM   1998 O  O   . GLY B 1 114 ? 22.400 3.942   16.284  1.00  7.64  ? 114  GLY F O   1 
ATOM   1999 N  N   . ARG B 1 115 ? 23.281 4.552   14.342  1.00  6.83  ? 115  ARG F N   1 
ATOM   2000 C  CA  . ARG B 1 115 ? 22.705 5.890   14.370  1.00  6.77  ? 115  ARG F CA  1 
ATOM   2001 C  C   . ARG B 1 115 ? 21.578 5.914   13.358  1.00  7.05  ? 115  ARG F C   1 
ATOM   2002 O  O   . ARG B 1 115 ? 21.272 4.929   12.727  1.00  10.24 ? 115  ARG F O   1 
ATOM   2003 C  CB  . ARG B 1 115 ? 23.806 6.904   14.106  1.00  7.31  ? 115  ARG F CB  1 
ATOM   2004 C  CG  . ARG B 1 115 ? 24.915 6.752   15.133  1.00  9.27  ? 115  ARG F CG  1 
ATOM   2005 C  CD  . ARG B 1 115 ? 25.848 7.800   15.200  1.00  10.53 ? 115  ARG F CD  1 
ATOM   2006 N  NE  . ARG B 1 115 ? 26.976 7.483   16.094  1.00  11.55 ? 115  ARG F NE  1 
ATOM   2007 C  CZ  . ARG B 1 115 ? 27.068 7.777   17.386  1.00  10.40 ? 115  ARG F CZ  1 
ATOM   2008 N  NH1 . ARG B 1 115 ? 26.106 8.378   18.017  1.00  11.79 ? 115  ARG F NH1 1 
ATOM   2009 N  NH2 . ARG B 1 115 ? 28.194 7.468   18.024  1.00  13.04 ? 115  ARG F NH2 1 
ATOM   2010 N  N   . THR B 1 116 ? 20.923 7.048   13.181  1.00  7.74  ? 116  THR F N   1 
ATOM   2011 C  CA  . THR B 1 116 ? 19.723 7.155   12.340  1.00  6.89  ? 116  THR F CA  1 
ATOM   2012 C  C   . THR B 1 116 ? 19.996 7.995   11.091  1.00  6.71  ? 116  THR F C   1 
ATOM   2013 O  O   . THR B 1 116 ? 20.521 9.091   11.201  1.00  8.97  ? 116  THR F O   1 
ATOM   2014 C  CB  . THR B 1 116 ? 18.555 7.768   13.093  1.00  7.63  ? 116  THR F CB  1 
ATOM   2015 O  OG1 . THR B 1 116 ? 18.190 6.930   14.187  1.00  10.47 ? 116  THR F OG1 1 
ATOM   2016 C  CG2 . THR B 1 116 ? 17.354 7.937   12.237  1.00  7.86  ? 116  THR F CG2 1 
ATOM   2017 N  N   . LEU B 1 117 ? 19.682 7.467   9.926   1.00  5.88  ? 117  LEU F N   1 
ATOM   2018 C  CA  . LEU B 1 117 ? 19.689 8.249   8.701   1.00  6.69  ? 117  LEU F CA  1 
ATOM   2019 C  C   . LEU B 1 117 ? 18.330 8.872   8.521   1.00  6.81  ? 117  LEU F C   1 
ATOM   2020 O  O   . LEU B 1 117 ? 17.315 8.199   8.702   1.00  7.07  ? 117  LEU F O   1 
ATOM   2021 C  CB  . LEU B 1 117 ? 20.039 7.285   7.561   1.00  6.98  ? 117  LEU F CB  1 
ATOM   2022 C  CG  . LEU B 1 117 ? 20.212 7.931   6.256   1.00  8.55  ? 117  LEU F CG  1 
ATOM   2023 C  CD1 . LEU B 1 117 ? 21.462 8.868   6.186   1.00  9.74  ? 117  LEU F CD1 1 
ATOM   2024 C  CD2 . LEU B 1 117 ? 20.315 6.834   5.180   1.00  9.77  ? 117  LEU F CD2 1 
ATOM   2025 N  N   . VAL B 1 118 ? 18.309 10.160  8.193   1.00  7.01  ? 118  VAL F N   1 
ATOM   2026 C  CA  . VAL B 1 118 ? 17.059 10.919  8.062   1.00  6.95  ? 118  VAL F CA  1 
ATOM   2027 C  C   . VAL B 1 118 ? 17.049 11.659  6.729   1.00  7.16  ? 118  VAL F C   1 
ATOM   2028 O  O   . VAL B 1 118 ? 18.035 12.266  6.329   1.00  8.44  ? 118  VAL F O   1 
ATOM   2029 C  CB  . VAL B 1 118 ? 16.886 11.943  9.178   1.00  7.98  ? 118  VAL F CB  1 
ATOM   2030 C  CG1 . VAL B 1 118 ? 15.544 12.750  9.066   1.00  10.45 ? 118  VAL F CG1 1 
ATOM   2031 C  CG2 . VAL B 1 118 ? 16.931 11.295  10.550  1.00  8.38  ? 118  VAL F CG2 1 
ATOM   2032 N  N   . VAL B 1 119 ? 15.910 11.608  6.029   1.00  8.06  ? 119  VAL F N   1 
ATOM   2033 C  CA  . VAL B 1 119 ? 15.661 12.451  4.855   1.00  7.57  ? 119  VAL F CA  1 
ATOM   2034 C  C   . VAL B 1 119 ? 14.564 13.445  5.209   1.00  7.98  ? 119  VAL F C   1 
ATOM   2035 O  O   . VAL B 1 119 ? 13.566 13.111  5.860   1.00  9.01  ? 119  VAL F O   1 
ATOM   2036 C  CB  . VAL B 1 119 ? 15.351 11.618  3.609   1.00  8.45  ? 119  VAL F CB  1 
ATOM   2037 C  CG1 . VAL B 1 119 ? 14.115 10.804  3.719   1.00  10.24 ? 119  VAL F CG1 1 
ATOM   2038 C  CG2 . VAL B 1 119 ? 15.260 12.501  2.361   1.00  9.31  ? 119  VAL F CG2 1 
ATOM   2039 N  N   . HIS B 1 120 ? 14.772 14.675  4.781   1.00  7.95  ? 120  HIS F N   1 
ATOM   2040 C  CA  . HIS B 1 120 ? 13.956 15.787  5.208   1.00  8.50  ? 120  HIS F CA  1 
ATOM   2041 C  C   . HIS B 1 120 ? 12.989 16.337  4.155   1.00  9.70  ? 120  HIS F C   1 
ATOM   2042 O  O   . HIS B 1 120 ? 13.138 16.073  2.991   1.00  10.18 ? 120  HIS F O   1 
ATOM   2043 C  CB  . HIS B 1 120 ? 14.860 16.936  5.653   1.00  9.40  ? 120  HIS F CB  1 
ATOM   2044 C  CG  . HIS B 1 120 ? 15.513 16.720  6.975   1.00  9.45  ? 120  HIS F CG  1 
ATOM   2045 N  ND1 . HIS B 1 120 ? 14.975 17.201  8.143   1.00  11.25 ? 120  HIS F ND1 1 
ATOM   2046 C  CD2 . HIS B 1 120 ? 16.659 16.079  7.306   1.00  9.15  ? 120  HIS F CD2 1 
ATOM   2047 C  CE1 . HIS B 1 120 ? 15.756 16.845  9.145   1.00  10.86 ? 120  HIS F CE1 1 
ATOM   2048 N  NE2 . HIS B 1 120 ? 16.790 16.170  8.680   1.00  10.06 ? 120  HIS F NE2 1 
ATOM   2049 N  N   . GLU B 1 121 ? 12.074 17.171  4.635   1.00  11.39 ? 121  GLU F N   1 
ATOM   2050 C  CA  . GLU B 1 121 ? 11.068 17.803  3.818   1.00  12.15 ? 121  GLU F CA  1 
ATOM   2051 C  C   . GLU B 1 121 ? 11.619 18.817  2.817   1.00  12.53 ? 121  GLU F C   1 
ATOM   2052 O  O   . GLU B 1 121 ? 11.135 18.905  1.684   1.00  14.02 ? 121  GLU F O   1 
ATOM   2053 C  CB  . GLU B 1 121 ? 10.099 18.490  4.763   1.00  13.80 ? 121  GLU F CB  1 
ATOM   2054 C  CG  . GLU B 1 121 ? 8.969  19.335  4.179   0.70  14.80 ? 121  GLU F CG  1 
ATOM   2055 C  CD  . GLU B 1 121 ? 8.410  20.351  5.245   0.50  15.15 ? 121  GLU F CD  1 
ATOM   2056 O  OE1 . GLU B 1 121 ? 8.992  20.634  6.368   0.50  14.51 ? 121  GLU F OE1 1 
ATOM   2057 O  OE2 . GLU B 1 121 ? 7.368  20.947  4.922   0.50  19.44 ? 121  GLU F OE2 1 
ATOM   2058 N  N   . LYS B 1 122 ? 12.537 19.626  3.291   1.00  12.33 ? 122  LYS F N   1 
ATOM   2059 C  CA  . LYS B 1 122 ? 13.092 20.749  2.567   1.00  13.87 ? 122  LYS F CA  1 
ATOM   2060 C  C   . LYS B 1 122 ? 14.576 20.501  2.273   1.00  12.00 ? 122  LYS F C   1 
ATOM   2061 O  O   . LYS B 1 122 ? 15.211 19.598  2.845   1.00  11.59 ? 122  LYS F O   1 
ATOM   2062 C  CB  . LYS B 1 122 ? 12.922 22.049  3.415   1.00  14.71 ? 122  LYS F CB  1 
ATOM   2063 C  CG  . LYS B 1 122 ? 11.521 22.418  3.850   1.00  18.52 ? 122  LYS F CG  1 
ATOM   2064 C  CD  . LYS B 1 122 ? 11.443 23.628  4.761   1.00  21.02 ? 122  LYS F CD  1 
ATOM   2065 C  CE  . LYS B 1 122 ? 10.026 23.846  5.286   0.50  18.99 ? 122  LYS F CE  1 
ATOM   2066 N  NZ  . LYS B 1 122 ? 9.416  22.698  5.986   0.40  21.88 ? 122  LYS F NZ  1 
ATOM   2067 N  N   . ALA B 1 123 ? 15.140 21.341  1.430   1.00  11.30 ? 123  ALA F N   1 
ATOM   2068 C  CA  . ALA B 1 123 ? 16.558 21.306  1.206   1.00  10.93 ? 123  ALA F CA  1 
ATOM   2069 C  C   . ALA B 1 123 ? 17.312 21.785  2.425   1.00  10.60 ? 123  ALA F C   1 
ATOM   2070 O  O   . ALA B 1 123 ? 16.871 22.657  3.157   1.00  13.08 ? 123  ALA F O   1 
ATOM   2071 C  CB  . ALA B 1 123 ? 16.941 22.197  -0.018  1.00  11.98 ? 123  ALA F CB  1 
ATOM   2072 N  N   . ASP B 1 124 ? 18.486 21.231  2.635   1.00  9.48  ? 124  ASP F N   1 
ATOM   2073 C  CA  . ASP B 1 124 ? 19.451 21.722  3.629   1.00  9.76  ? 124  ASP F CA  1 
ATOM   2074 C  C   . ASP B 1 124 ? 20.175 22.901  2.967   1.00  10.97 ? 124  ASP F C   1 
ATOM   2075 O  O   . ASP B 1 124 ? 20.741 22.757  1.888   1.00  11.08 ? 124  ASP F O   1 
ATOM   2076 C  CB  . ASP B 1 124 ? 20.400 20.538  3.918   1.00  9.50  ? 124  ASP F CB  1 
ATOM   2077 C  CG  . ASP B 1 124 ? 21.456 20.821  4.937   1.00  10.03 ? 124  ASP F CG  1 
ATOM   2078 O  OD1 . ASP B 1 124 ? 21.783 21.955  5.200   1.00  10.88 ? 124  ASP F OD1 1 
ATOM   2079 O  OD2 . ASP B 1 124 ? 21.926 19.826  5.518   1.00  11.14 ? 124  ASP F OD2 1 
ATOM   2080 N  N   . ASP B 1 125 ? 20.183 24.044  3.664   1.00  11.42 ? 125  ASP F N   1 
ATOM   2081 C  CA  . ASP B 1 125 ? 20.880 25.229  3.184   1.00  12.63 ? 125  ASP F CA  1 
ATOM   2082 C  C   . ASP B 1 125 ? 22.379 25.277  3.453   1.00  12.46 ? 125  ASP F C   1 
ATOM   2083 O  O   . ASP B 1 125 ? 23.050 26.251  3.111   1.00  13.94 ? 125  ASP F O   1 
ATOM   2084 C  CB  . ASP B 1 125 ? 20.191 26.491  3.666   1.00  14.07 ? 125  ASP F CB  1 
ATOM   2085 C  CG  . ASP B 1 125 ? 20.398 26.795  5.146   1.00  16.36 ? 125  ASP F CG  1 
ATOM   2086 O  OD1 . ASP B 1 125 ? 21.334 26.288  5.797   1.00  16.54 ? 125  ASP F OD1 1 
ATOM   2087 O  OD2 . ASP B 1 125 ? 19.589 27.621  5.655   1.00  19.66 ? 125  ASP F OD2 1 
ATOM   2088 N  N   . LEU B 1 126 ? 22.910 24.177  3.994   1.00  11.81 ? 126  LEU F N   1 
ATOM   2089 C  CA  . LEU B 1 126 ? 24.342 23.956  4.158   1.00  13.29 ? 126  LEU F CA  1 
ATOM   2090 C  C   . LEU B 1 126 ? 25.022 24.972  5.063   1.00  14.49 ? 126  LEU F C   1 
ATOM   2091 O  O   . LEU B 1 126 ? 26.241 25.158  4.998   1.00  15.22 ? 126  LEU F O   1 
ATOM   2092 C  CB  . LEU B 1 126 ? 25.051 23.853  2.822   1.00  14.61 ? 126  LEU F CB  1 
ATOM   2093 C  CG  . LEU B 1 126 ? 24.373 22.977  1.776   1.00  13.46 ? 126  LEU F CG  1 
ATOM   2094 C  CD1 . LEU B 1 126 ? 25.182 23.042  0.495   1.00  16.96 ? 126  LEU F CD1 1 
ATOM   2095 C  CD2 . LEU B 1 126 ? 24.145 21.557  2.206   1.00  12.73 ? 126  LEU F CD2 1 
ATOM   2096 N  N   . GLY B 1 127 ? 24.250 25.600  5.926   1.00  13.75 ? 127  GLY F N   1 
ATOM   2097 C  CA  . GLY B 1 127 ? 24.827 26.577  6.847   1.00  16.11 ? 127  GLY F CA  1 
ATOM   2098 C  C   . GLY B 1 127 ? 24.977 27.946  6.232   1.00  16.53 ? 127  GLY F C   1 
ATOM   2099 O  O   . GLY B 1 127 ? 25.558 28.821  6.879   1.00  19.06 ? 127  GLY F O   1 
ATOM   2100 N  N   . LYS B 1 128 ? 24.441 28.166  5.031   1.00  16.58 ? 128  LYS F N   1 
ATOM   2101 C  CA  . LYS B 1 128 ? 24.626 29.431  4.325   1.00  19.16 ? 128  LYS F CA  1 
ATOM   2102 C  C   . LYS B 1 128 ? 23.403 30.286  4.345   1.00  20.09 ? 128  LYS F C   1 
ATOM   2103 O  O   . LYS B 1 128 ? 23.384 31.295  3.625   1.00  22.39 ? 128  LYS F O   1 
ATOM   2104 C  CB  . LYS B 1 128 ? 24.963 29.157  2.885   1.00  19.28 ? 128  LYS F CB  1 
ATOM   2105 C  CG  . LYS B 1 128 ? 26.159 28.308  2.655   0.50  19.49 ? 128  LYS F CG  1 
ATOM   2106 C  CD  . LYS B 1 128 ? 26.625 28.355  1.245   0.50  21.78 ? 128  LYS F CD  1 
ATOM   2107 C  CE  . LYS B 1 128 ? 25.582 27.864  0.281   0.50  22.99 ? 128  LYS F CE  1 
ATOM   2108 N  NZ  . LYS B 1 128 ? 26.207 27.152  -0.828  0.50  25.43 ? 128  LYS F NZ  1 
ATOM   2109 N  N   . GLY B 1 129 ? 22.407 29.952  5.156   1.00  20.67 ? 129  GLY F N   1 
ATOM   2110 C  CA  . GLY B 1 129 ? 21.110 30.625  5.201   1.00  22.41 ? 129  GLY F CA  1 
ATOM   2111 C  C   . GLY B 1 129 ? 21.054 31.909  5.996   1.00  24.97 ? 129  GLY F C   1 
ATOM   2112 O  O   . GLY B 1 129 ? 20.033 32.614  5.959   1.00  27.50 ? 129  GLY F O   1 
ATOM   2113 N  N   . GLY B 1 130 ? 22.097 32.224  6.741   1.00  25.04 ? 130  GLY F N   1 
ATOM   2114 C  CA  . GLY B 1 130 ? 22.151 33.549  7.427   0.50  24.72 ? 130  GLY F CA  1 
ATOM   2115 C  C   . GLY B 1 130 ? 21.098 33.806  8.513   0.50  25.67 ? 130  GLY F C   1 
ATOM   2116 O  O   . GLY B 1 130 ? 20.833 34.965  8.885   0.50  25.70 ? 130  GLY F O   1 
ATOM   2117 N  N   . ASN B 1 131 ? 20.472 32.747  9.015   0.50  25.66 ? 131  ASN F N   1 
ATOM   2118 C  CA  . ASN B 1 131 ? 19.719 32.805  10.273  1.00  25.98 ? 131  ASN F CA  1 
ATOM   2119 C  C   . ASN B 1 131 ? 20.390 31.869  11.270  1.00  25.86 ? 131  ASN F C   1 
ATOM   2120 O  O   . ASN B 1 131 ? 21.276 31.059  10.903  1.00  25.47 ? 131  ASN F O   1 
ATOM   2121 C  CB  . ASN B 1 131 ? 18.228 32.483  10.095  1.00  26.69 ? 131  ASN F CB  1 
ATOM   2122 C  CG  . ASN B 1 131 ? 17.985 31.159  9.392   1.00  28.37 ? 131  ASN F CG  1 
ATOM   2123 O  OD1 . ASN B 1 131 ? 18.632 30.159  9.703   1.00  28.59 ? 131  ASN F OD1 1 
ATOM   2124 N  ND2 . ASN B 1 131 ? 17.064 31.152  8.422   1.00  33.23 ? 131  ASN F ND2 1 
ATOM   2125 N  N   . GLU B 1 132 ? 19.974 31.951  12.530  1.00  25.64 ? 132  GLU F N   1 
ATOM   2126 C  CA  . GLU B 1 132 ? 20.547 31.126  13.595  1.00  25.23 ? 132  GLU F CA  1 
ATOM   2127 C  C   . GLU B 1 132 ? 20.506 29.622  13.277  1.00  24.29 ? 132  GLU F C   1 
ATOM   2128 O  O   . GLU B 1 132 ? 21.512 28.898  13.436  1.00  26.64 ? 132  GLU F O   1 
ATOM   2129 C  CB  . GLU B 1 132 ? 19.794 31.393  14.906  0.10  25.00 ? 132  GLU F CB  1 
ATOM   2130 C  CG  . GLU B 1 132 ? 20.372 30.710  16.136  0.10  25.00 ? 132  GLU F CG  1 
ATOM   2131 C  CD  . GLU B 1 132 ? 21.554 31.445  16.732  0.10  23.91 ? 132  GLU F CD  1 
ATOM   2132 O  OE1 . GLU B 1 132 ? 22.121 32.343  16.068  0.10  23.16 ? 132  GLU F OE1 1 
ATOM   2133 O  OE2 . GLU B 1 132 ? 21.917 31.121  17.879  0.10  22.82 ? 132  GLU F OE2 1 
ATOM   2134 N  N   . GLU B 1 133 ? 19.344 29.164  12.827  1.00  21.95 ? 133  GLU F N   1 
ATOM   2135 C  CA  . GLU B 1 133 ? 19.099 27.737  12.560  1.00  21.23 ? 133  GLU F CA  1 
ATOM   2136 C  C   . GLU B 1 133 ? 19.984 27.153  11.465  1.00  19.57 ? 133  GLU F C   1 
ATOM   2137 O  O   . GLU B 1 133 ? 20.275 25.934  11.445  1.00  19.74 ? 133  GLU F O   1 
ATOM   2138 C  CB  . GLU B 1 133 ? 17.638 27.549  12.151  0.30  20.44 ? 133  GLU F CB  1 
ATOM   2139 C  CG  . GLU B 1 133 ? 17.275 26.132  11.817  0.30  21.72 ? 133  GLU F CG  1 
ATOM   2140 C  CD  . GLU B 1 133 ? 15.787 25.865  11.870  0.30  22.02 ? 133  GLU F CD  1 
ATOM   2141 O  OE1 . GLU B 1 133 ? 15.399 24.689  11.644  0.30  21.62 ? 133  GLU F OE1 1 
ATOM   2142 O  OE2 . GLU B 1 133 ? 15.015 26.809  12.133  0.30  22.73 ? 133  GLU F OE2 1 
ATOM   2143 N  N   . SER B 1 134 ? 20.422 27.982  10.539  1.00  18.82 ? 134  SER F N   1 
ATOM   2144 C  CA  . SER B 1 134 ? 21.194 27.496  9.395   1.00  18.56 ? 134  SER F CA  1 
ATOM   2145 C  C   . SER B 1 134 ? 22.438 26.737  9.824   1.00  18.28 ? 134  SER F C   1 
ATOM   2146 O  O   . SER B 1 134 ? 22.782 25.740  9.239   1.00  17.71 ? 134  SER F O   1 
ATOM   2147 C  CB  . SER B 1 134 ? 21.628 28.639  8.478   1.00  18.70 ? 134  SER F CB  1 
ATOM   2148 O  OG  . SER B 1 134 ? 22.340 28.138  7.361   1.00  19.09 ? 134  SER F OG  1 
ATOM   2149 N  N   . THR B 1 135 ? 23.117 27.198  10.864  1.00  18.53 ? 135  THR F N   1 
ATOM   2150 C  CA  . THR B 1 135 ? 24.359 26.562  11.302  1.00  19.14 ? 135  THR F CA  1 
ATOM   2151 C  C   . THR B 1 135 ? 24.125 25.551  12.422  1.00  17.80 ? 135  THR F C   1 
ATOM   2152 O  O   . THR B 1 135 ? 25.104 25.046  13.002  1.00  16.80 ? 135  THR F O   1 
ATOM   2153 C  CB  . THR B 1 135 ? 25.409 27.602  11.720  0.80  19.94 ? 135  THR F CB  1 
ATOM   2154 O  OG1 . THR B 1 135 ? 24.782 28.514  12.618  0.60  21.22 ? 135  THR F OG1 1 
ATOM   2155 C  CG2 . THR B 1 135 ? 25.945 28.301  10.487  0.60  20.52 ? 135  THR F CG2 1 
ATOM   2156 N  N   . LYS B 1 136 ? 22.862 25.126  12.568  1.00  18.47 ? 136  LYS F N   1 
ATOM   2157 C  CA  . LYS B 1 136 ? 22.502 24.003  13.439  1.00  18.60 ? 136  LYS F CA  1 
ATOM   2158 C  C   . LYS B 1 136 ? 21.873 22.876  12.638  1.00  17.73 ? 136  LYS F C   1 
ATOM   2159 O  O   . LYS B 1 136 ? 22.313 21.697  12.704  1.00  18.70 ? 136  LYS F O   1 
ATOM   2160 C  CB  . LYS B 1 136 ? 21.597 24.506  14.585  1.00  19.41 ? 136  LYS F CB  1 
ATOM   2161 C  CG  . LYS B 1 136 ? 22.308 25.540  15.492  1.00  21.98 ? 136  LYS F CG  1 
ATOM   2162 C  CD  . LYS B 1 136 ? 21.317 26.177  16.442  0.10  19.76 ? 136  LYS F CD  1 
ATOM   2163 C  CE  . LYS B 1 136 ? 22.021 26.937  17.543  0.21  20.06 ? 136  LYS F CE  1 
ATOM   2164 N  NZ  . LYS B 1 136 ? 21.066 27.280  18.626  0.10  20.23 ? 136  LYS F NZ  1 
ATOM   2165 N  N   . THR B 1 137 ? 20.850 23.206  11.862  1.00  17.04 ? 137  THR F N   1 
ATOM   2166 C  CA  . THR B 1 137 ? 20.096 22.204  11.198  1.00  16.97 ? 137  THR F CA  1 
ATOM   2167 C  C   . THR B 1 137 ? 20.151 22.356  9.691   1.00  14.34 ? 137  THR F C   1 
ATOM   2168 O  O   . THR B 1 137 ? 19.783 21.446  8.964   1.00  16.69 ? 137  THR F O   1 
ATOM   2169 C  CB  . THR B 1 137 ? 18.600 22.277  11.588  1.00  18.57 ? 137  THR F CB  1 
ATOM   2170 O  OG1 . THR B 1 137 ? 18.056 23.510  11.125  1.00  20.71 ? 137  THR F OG1 1 
ATOM   2171 C  CG2 . THR B 1 137 ? 18.398 22.129  13.037  1.00  21.24 ? 137  THR F CG2 1 
ATOM   2172 N  N   . GLY B 1 138 ? 20.516 23.547  9.174   1.00  13.59 ? 138  GLY F N   1 
ATOM   2173 C  CA  . GLY B 1 138 ? 20.368 23.797  7.734   1.00  13.11 ? 138  GLY F CA  1 
ATOM   2174 C  C   . GLY B 1 138 ? 18.963 24.074  7.258   1.00  13.09 ? 138  GLY F C   1 
ATOM   2175 O  O   . GLY B 1 138 ? 18.709 24.159  6.048   1.00  13.31 ? 138  GLY F O   1 
ATOM   2176 N  N   . ASN B 1 139 ? 18.017 24.250  8.184   1.00  13.26 ? 139  ASN F N   1 
ATOM   2177 C  CA  . ASN B 1 139 ? 16.659 24.624  7.791   1.00  13.03 ? 139  ASN F CA  1 
ATOM   2178 C  C   . ASN B 1 139 ? 15.994 23.600  6.894   1.00  12.24 ? 139  ASN F C   1 
ATOM   2179 O  O   . ASN B 1 139 ? 15.180 23.961  6.023   1.00  14.46 ? 139  ASN F O   1 
ATOM   2180 C  CB  . ASN B 1 139 ? 16.629 26.024  7.140   1.00  14.41 ? 139  ASN F CB  1 
ATOM   2181 C  CG  . ASN B 1 139 ? 16.969 27.105  8.126   1.00  18.67 ? 139  ASN F CG  1 
ATOM   2182 O  OD1 . ASN B 1 139 ? 16.285 27.277  9.129   1.00  22.80 ? 139  ASN F OD1 1 
ATOM   2183 N  ND2 . ASN B 1 139 ? 18.038 27.810  7.872   1.00  19.48 ? 139  ASN F ND2 1 
ATOM   2184 N  N   . ALA B 1 140 ? 16.256 22.313  7.106   1.00  12.61 ? 140  ALA F N   1 
ATOM   2185 C  CA  . ALA B 1 140 ? 15.731 21.308  6.178   1.00  13.99 ? 140  ALA F CA  1 
ATOM   2186 C  C   . ALA B 1 140 ? 14.330 20.825  6.584   1.00  13.59 ? 140  ALA F C   1 
ATOM   2187 O  O   . ALA B 1 140 ? 13.734 19.998  5.906   1.00  13.40 ? 140  ALA F O   1 
ATOM   2188 C  CB  . ALA B 1 140 ? 16.691 20.168  6.072   1.00  14.57 ? 140  ALA F CB  1 
ATOM   2189 N  N   . GLY B 1 141 ? 13.749 21.413  7.646   1.00  15.39 ? 141  GLY F N   1 
ATOM   2190 C  CA  . GLY B 1 141 ? 12.371 21.107  7.930   1.00  15.72 ? 141  GLY F CA  1 
ATOM   2191 C  C   . GLY B 1 141 ? 12.136 19.732  8.536   1.00  15.14 ? 141  GLY F C   1 
ATOM   2192 O  O   . GLY B 1 141 ? 13.022 19.118  9.130   1.00  15.21 ? 141  GLY F O   1 
ATOM   2193 N  N   . SER B 1 142 ? 10.918 19.254  8.369   1.00  15.18 ? 142  SER F N   1 
ATOM   2194 C  CA  . SER B 1 142 ? 10.503 18.059  9.019   1.00  14.11 ? 142  SER F CA  1 
ATOM   2195 C  C   . SER B 1 142 ? 11.221 16.841  8.500   1.00  12.45 ? 142  SER F C   1 
ATOM   2196 O  O   . SER B 1 142 ? 11.803 16.789  7.396   1.00  12.29 ? 142  SER F O   1 
ATOM   2197 C  CB  . SER B 1 142 ? 9.028  17.837  8.926   1.00  16.30 ? 142  SER F CB  1 
ATOM   2198 O  OG  . SER B 1 142 ? 8.646  17.470  7.673   1.00  22.92 ? 142  SER F OG  1 
ATOM   2199 N  N   . ARG B 1 143 ? 11.183 15.825  9.336   1.00  10.78 ? 143  ARG F N   1 
ATOM   2200 C  CA  . ARG B 1 143 ? 11.825 14.554  9.061   1.00  9.86  ? 143  ARG F CA  1 
ATOM   2201 C  C   . ARG B 1 143 ? 10.825 13.677  8.394   1.00  11.22 ? 143  ARG F C   1 
ATOM   2202 O  O   . ARG B 1 143 ? 9.858  13.268  9.010   1.00  14.62 ? 143  ARG F O   1 
ATOM   2203 C  CB  . ARG B 1 143 ? 12.323 13.965  10.399  1.00  10.06 ? 143  ARG F CB  1 
ATOM   2204 C  CG  . ARG B 1 143 ? 13.300 14.865  11.112  1.00  10.26 ? 143  ARG F CG  1 
ATOM   2205 C  CD  . ARG B 1 143 ? 13.742 14.379  12.442  1.00  10.68 ? 143  ARG F CD  1 
ATOM   2206 N  NE  . ARG B 1 143 ? 14.542 15.404  13.086  1.00  10.09 ? 143  ARG F NE  1 
ATOM   2207 C  CZ  . ARG B 1 143 ? 15.344 15.239  14.139  1.00  9.85  ? 143  ARG F CZ  1 
ATOM   2208 N  NH1 . ARG B 1 143 ? 15.517 14.039  14.726  1.00  10.45 ? 143  ARG F NH1 1 
ATOM   2209 N  NH2 . ARG B 1 143 ? 16.035 16.289  14.581  1.00  11.13 ? 143  ARG F NH2 1 
ATOM   2210 N  N   . LEU B 1 144 ? 11.035 13.367  7.140   1.00  9.40  ? 144  LEU F N   1 
ATOM   2211 C  CA  . LEU B 1 144 ? 10.044 12.581  6.412   1.00  9.51  ? 144  LEU F CA  1 
ATOM   2212 C  C   . LEU B 1 144 ? 10.165 11.087  6.560   1.00  9.69  ? 144  LEU F C   1 
ATOM   2213 O  O   . LEU B 1 144 ? 9.171  10.388  6.554   1.00  12.28 ? 144  LEU F O   1 
ATOM   2214 C  CB  . LEU B 1 144 ? 10.096 12.857  4.927   1.00  10.89 ? 144  LEU F CB  1 
ATOM   2215 C  CG  . LEU B 1 144 ? 9.946  14.289  4.464   1.00  13.78 ? 144  LEU F CG  1 
ATOM   2216 C  CD1 . LEU B 1 144 ? 10.125 14.331  2.930   1.00  16.50 ? 144  LEU F CD1 1 
ATOM   2217 C  CD2 . LEU B 1 144 ? 8.626  14.821  4.911   1.00  20.18 ? 144  LEU F CD2 1 
ATOM   2218 N  N   . ALA B 1 145 ? 11.393 10.600  6.729   1.00  9.08  ? 145  ALA F N   1 
ATOM   2219 C  CA  . ALA B 1 145 ? 11.581 9.185   6.886   1.00  9.03  ? 145  ALA F CA  1 
ATOM   2220 C  C   . ALA B 1 145 ? 12.936 8.979   7.524   1.00  7.93  ? 145  ALA F C   1 
ATOM   2221 O  O   . ALA B 1 145 ? 13.842 9.807   7.381   1.00  8.76  ? 145  ALA F O   1 
ATOM   2222 C  CB  . ALA B 1 145 ? 11.541 8.456   5.508   1.00  9.68  ? 145  ALA F CB  1 
ATOM   2223 N  N   . CYS B 1 146 ? 13.086 7.850   8.193   1.00  7.86  ? 146  CYS F N   1 
ATOM   2224 C  CA  . CYS B 1 146 ? 14.330 7.542   8.895   1.00  8.66  ? 146  CYS F CA  1 
ATOM   2225 C  C   . CYS B 1 146 ? 14.454 6.013   9.071   1.00  8.35  ? 146  CYS F C   1 
ATOM   2226 O  O   . CYS B 1 146 ? 13.500 5.283   8.882   1.00  8.72  ? 146  CYS F O   1 
ATOM   2227 C  CB  . CYS B 1 146 ? 14.415 8.230   10.221  1.00  9.98  ? 146  CYS F CB  1 
ATOM   2228 S  SG  A CYS B 1 146 ? 13.178 7.685   11.429  0.70  12.24 ? 146  CYS F SG  1 
ATOM   2229 S  SG  B CYS B 1 146 ? 13.843 9.802   10.732  0.30  17.99 ? 146  CYS F SG  1 
ATOM   2230 N  N   . GLY B 1 147 ? 15.633 5.611   9.468   1.00  7.24  ? 147  GLY F N   1 
ATOM   2231 C  CA  . GLY B 1 147 ? 15.859 4.237   9.864   1.00  8.04  ? 147  GLY F CA  1 
ATOM   2232 C  C   . GLY B 1 147 ? 17.183 4.172   10.592  1.00  7.82  ? 147  GLY F C   1 
ATOM   2233 O  O   . GLY B 1 147 ? 18.041 5.036   10.419  1.00  7.86  ? 147  GLY F O   1 
ATOM   2234 N  N   . VAL B 1 148 ? 17.408 3.100   11.279  1.00  7.09  ? 148  VAL F N   1 
ATOM   2235 C  CA  . VAL B 1 148 ? 18.683 2.872   11.997  1.00  7.31  ? 148  VAL F CA  1 
ATOM   2236 C  C   . VAL B 1 148 ? 19.659 2.203   11.056  1.00  8.39  ? 148  VAL F C   1 
ATOM   2237 O  O   . VAL B 1 148 ? 19.289 1.310   10.273  1.00  9.06  ? 148  VAL F O   1 
ATOM   2238 C  CB  . VAL B 1 148 ? 18.432 2.001   13.247  1.00  9.13  ? 148  VAL F CB  1 
ATOM   2239 C  CG1 . VAL B 1 148 ? 19.721 1.817   14.004  1.00  9.98  ? 148  VAL F CG1 1 
ATOM   2240 C  CG2 . VAL B 1 148 ? 17.410 2.639   14.157  1.00  11.66 ? 148  VAL F CG2 1 
ATOM   2241 N  N   . ILE B 1 149 ? 20.898 2.655   11.064  1.00  6.98  ? 149  ILE F N   1 
ATOM   2242 C  CA  . ILE B 1 149 ? 21.924 2.105   10.226  1.00  7.54  ? 149  ILE F CA  1 
ATOM   2243 C  C   . ILE B 1 149 ? 22.477 0.814   10.857  1.00  7.12  ? 149  ILE F C   1 
ATOM   2244 O  O   . ILE B 1 149 ? 23.003 0.813   11.959  1.00  8.43  ? 149  ILE F O   1 
ATOM   2245 C  CB  . ILE B 1 149 ? 23.004 3.152   10.006  1.00  7.56  ? 149  ILE F CB  1 
ATOM   2246 C  CG1 . ILE B 1 149 ? 22.463 4.400   9.345   1.00  8.86  ? 149  ILE F CG1 1 
ATOM   2247 C  CG2 . ILE B 1 149 ? 24.176 2.584   9.181   1.00  8.78  ? 149  ILE F CG2 1 
ATOM   2248 C  CD1 . ILE B 1 149 ? 23.425 5.571   9.441   1.00  9.60  ? 149  ILE F CD1 1 
ATOM   2249 N  N   . GLY B 1 150 ? 22.363 -0.284  10.149  1.00  6.99  ? 150  GLY F N   1 
ATOM   2250 C  CA  . GLY B 1 150 ? 22.742 -1.584  10.632  1.00  7.40  ? 150  GLY F CA  1 
ATOM   2251 C  C   . GLY B 1 150 ? 23.875 -2.222  9.850   1.00  7.72  ? 150  GLY F C   1 
ATOM   2252 O  O   . GLY B 1 150 ? 24.147 -1.889  8.731   1.00  8.74  ? 150  GLY F O   1 
ATOM   2253 N  N   . ILE B 1 151 ? 24.559 -3.142  10.517  1.00  7.65  ? 151  ILE F N   1 
ATOM   2254 C  CA  . ILE B 1 151 ? 25.625 -3.903  9.903   1.00  8.26  ? 151  ILE F CA  1 
ATOM   2255 C  C   . ILE B 1 151 ? 25.078 -4.846  8.853   1.00  7.92  ? 151  ILE F C   1 
ATOM   2256 O  O   . ILE B 1 151 ? 24.107 -5.541  9.061   1.00  8.53  ? 151  ILE F O   1 
ATOM   2257 C  CB  . ILE B 1 151 ? 26.372 -4.705  11.005  1.00  9.28  ? 151  ILE F CB  1 
ATOM   2258 C  CG1 . ILE B 1 151 ? 27.072 -3.787  11.947  1.00  12.01 ? 151  ILE F CG1 1 
ATOM   2259 C  CG2 . ILE B 1 151 ? 27.356 -5.728  10.365  1.00  12.40 ? 151  ILE F CG2 1 
ATOM   2260 C  CD1 . ILE B 1 151 ? 27.507 -4.465  13.173  1.00  14.21 ? 151  ILE F CD1 1 
ATOM   2261 N  N   . ALA B 1 152 ? 25.692 -4.857  7.691   1.00  7.17  ? 152  ALA F N   1 
ATOM   2262 C  CA  . ALA B 1 152 ? 25.265 -5.669  6.556   1.00  8.31  ? 152  ALA F CA  1 
ATOM   2263 C  C   . ALA B 1 152 ? 26.287 -6.704  6.207   1.00  9.71  ? 152  ALA F C   1 
ATOM   2264 O  O   . ALA B 1 152 ? 27.455 -6.622  6.581   1.00  10.02 ? 152  ALA F O   1 
ATOM   2265 C  CB  . ALA B 1 152 ? 24.981 -4.763  5.366   1.00  9.99  ? 152  ALA F CB  1 
ATOM   2266 N  N   . GLN B 1 153 ? 25.825 -7.696  5.475   1.00  11.48 ? 153  GLN F N   1 
ATOM   2267 C  CA  . GLN B 1 153 ? 26.689 -8.744  4.972   1.00  14.23 ? 153  GLN F CA  1 
ATOM   2268 C  C   . GLN B 1 153 ? 27.525 -8.116  3.808   1.00  15.98 ? 153  GLN F C   1 
ATOM   2269 C  CB  . GLN B 1 153 ? 25.736 -9.848  4.479   1.00  15.13 ? 153  GLN F CB  1 
ATOM   2270 C  CG  . GLN B 1 153 ? 26.260 -11.119 4.020   1.00  20.00 ? 153  GLN F CG  1 
ATOM   2271 C  CD  . GLN B 1 153 ? 25.059 -11.921 3.522   1.00  19.58 ? 153  GLN F CD  1 
ATOM   2272 O  OE1 . GLN B 1 153 ? 23.907 -11.920 4.130   1.00  16.72 ? 153  GLN F OE1 1 
ATOM   2273 N  NE2 . GLN B 1 153 ? 25.271 -12.531 2.401   1.00  23.42 ? 153  GLN F NE2 1 
HETATM 2274 S  S   . SO4 C 2 .   ? 16.442 -18.594 13.963  0.45  10.11 ? 1154 SO4 A S   1 
HETATM 2275 O  O1  . SO4 C 2 .   ? 16.679 -18.038 15.322  0.45  7.16  ? 1154 SO4 A O1  1 
HETATM 2276 O  O2  . SO4 C 2 .   ? 15.776 -17.673 13.134  0.45  9.95  ? 1154 SO4 A O2  1 
HETATM 2277 O  O3  . SO4 C 2 .   ? 15.654 -19.829 14.092  0.45  14.79 ? 1154 SO4 A O3  1 
HETATM 2278 O  O4  . SO4 C 2 .   ? 17.705 -18.864 13.348  0.45  14.42 ? 1154 SO4 A O4  1 
HETATM 2279 S  S   . SO4 D 2 .   ? 10.871 -16.097 9.100   0.55  25.97 ? 1155 SO4 A S   1 
HETATM 2280 O  O1  . SO4 D 2 .   ? 11.443 -17.258 9.777   0.55  28.87 ? 1155 SO4 A O1  1 
HETATM 2281 O  O2  . SO4 D 2 .   ? 9.889  -15.600 10.002  0.55  21.99 ? 1155 SO4 A O2  1 
HETATM 2282 O  O3  . SO4 D 2 .   ? 10.360 -16.590 7.821   0.55  27.05 ? 1155 SO4 A O3  1 
HETATM 2283 O  O4  . SO4 D 2 .   ? 11.934 -15.117 8.824   0.55  27.19 ? 1155 SO4 A O4  1 
HETATM 2284 CU CU  . CU  E 3 .   ? 16.523 -15.409 16.887  0.45  10.92 ? 1157 CU  A CU  1 
HETATM 2285 ZN ZN  . ZN  F 4 .   ? 22.037 -19.174 19.094  1.00  9.12  ? 1158 ZN  A ZN  1 
HETATM 2286 ZN ZN  . ZN  G 4 .   ? 16.403 -16.253 16.144  0.55  9.03  ? 1159 ZN  A ZN  1 
HETATM 2287 S  S   . SO4 H 2 .   ? 16.968 18.609  11.831  0.55  14.50 ? 1154 SO4 F S   1 
HETATM 2288 O  O1  . SO4 H 2 .   ? 17.847 18.059  10.814  0.55  19.49 ? 1154 SO4 F O1  1 
HETATM 2289 O  O2  . SO4 H 2 .   ? 15.917 17.687  12.049  0.55  16.47 ? 1154 SO4 F O2  1 
HETATM 2290 O  O3  . SO4 H 2 .   ? 16.404 19.912  11.430  0.55  20.69 ? 1154 SO4 F O3  1 
HETATM 2291 O  O4  . SO4 H 2 .   ? 17.719 18.682  13.058  0.55  19.87 ? 1154 SO4 F O4  1 
HETATM 2292 ZN ZN  . ZN  I 4 .   ? 18.210 16.264  9.869   0.55  11.53 ? 1155 ZN  F ZN  1 
HETATM 2293 CU CU  . CU  J 3 .   ? 18.531 15.612  9.479   0.45  9.50  ? 1156 CU  F CU  1 
HETATM 2294 ZN ZN  . ZN  K 4 .   ? 24.460 19.218  10.546  1.00  9.12  ? 1157 ZN  F ZN  1 
HETATM 2295 C  C   . ACT L 5 .   ? 24.837 19.613  -1.252  0.50  12.71 ? 1158 ACT F C   1 
HETATM 2296 O  O   . ACT L 5 .   ? 24.606 18.408  -1.069  0.50  18.84 ? 1158 ACT F O   1 
HETATM 2297 O  OXT . ACT L 5 .   ? 23.730 20.193  -1.506  0.50  18.25 ? 1158 ACT F OXT 1 
HETATM 2298 C  CH3 . ACT L 5 .   ? 26.319 20.102  -1.412  0.50  5.66  ? 1158 ACT F CH3 1 
HETATM 2299 C  C   . ACT M 5 .   ? 5.691  8.164   8.897   0.50  21.07 ? 1159 ACT F C   1 
HETATM 2300 O  O   . ACT M 5 .   ? 6.189  7.094   8.425   0.50  23.16 ? 1159 ACT F O   1 
HETATM 2301 O  OXT . ACT M 5 .   ? 4.454  8.126   9.067   0.50  23.10 ? 1159 ACT F OXT 1 
HETATM 2302 C  CH3 . ACT M 5 .   ? 6.492  9.397   9.224   0.50  18.04 ? 1159 ACT F CH3 1 
HETATM 2303 O  O   . HOH N 6 .   ? 11.077 -15.462 3.429   1.00  28.72 ? 2001 HOH A O   1 
HETATM 2304 O  O   . HOH N 6 .   ? 30.259 3.884   25.283  1.00  34.61 ? 2002 HOH A O   1 
HETATM 2305 O  O   . HOH N 6 .   ? 12.007 -1.413  13.922  1.00  22.63 ? 2003 HOH A O   1 
HETATM 2306 O  O   . HOH N 6 .   ? 5.219  -1.184  21.489  1.00  43.55 ? 2004 HOH A O   1 
HETATM 2307 O  O   . HOH N 6 .   ? 6.857  -1.266  17.352  1.00  38.36 ? 2005 HOH A O   1 
HETATM 2308 O  O   . HOH N 6 .   ? 10.197 -6.792  10.634  1.00  39.29 ? 2006 HOH A O   1 
HETATM 2309 O  O   . HOH N 6 .   ? 2.324  -4.857  11.590  1.00  44.64 ? 2007 HOH A O   1 
HETATM 2310 O  O   . HOH N 6 .   ? 5.969  -3.324  10.602  1.00  44.62 ? 2008 HOH A O   1 
HETATM 2311 O  O   . HOH N 6 .   ? 6.092  -10.708 11.402  1.00  27.76 ? 2009 HOH A O   1 
HETATM 2312 O  O   . HOH N 6 .   ? -0.521 -5.830  19.435  1.00  29.70 ? 2010 HOH A O   1 
HETATM 2313 O  O   . HOH N 6 .   ? 4.384  -5.549  14.471  1.00  21.83 ? 2011 HOH A O   1 
HETATM 2314 O  O   . HOH N 6 .   ? 4.757  -2.953  23.496  1.00  37.38 ? 2012 HOH A O   1 
HETATM 2315 O  O   . HOH N 6 .   ? 7.074  -0.776  19.184  1.00  29.05 ? 2013 HOH A O   1 
HETATM 2316 O  O   . HOH N 6 .   ? -1.217 -14.291 17.861  1.00  36.02 ? 2014 HOH A O   1 
HETATM 2317 O  O   . HOH N 6 .   ? 1.761  -13.604 15.523  1.00  32.12 ? 2015 HOH A O   1 
HETATM 2318 O  O   . HOH N 6 .   ? 9.399  -0.866  26.826  1.00  21.34 ? 2016 HOH A O   1 
HETATM 2319 O  O   . HOH N 6 .   ? 13.097 3.677   25.416  1.00  26.97 ? 2017 HOH A O   1 
HETATM 2320 O  O   . HOH N 6 .   ? 17.273 2.723   25.988  1.00  22.17 ? 2018 HOH A O   1 
HETATM 2321 O  O   . HOH N 6 .   ? 10.796 1.296   27.341  1.00  29.88 ? 2019 HOH A O   1 
HETATM 2322 O  O   . HOH N 6 .   ? 18.870 2.445   27.719  1.00  26.98 ? 2020 HOH A O   1 
HETATM 2323 O  O   . HOH N 6 .   ? 31.465 -10.542 14.316  1.00  32.36 ? 2021 HOH A O   1 
HETATM 2324 O  O   . HOH N 6 .   ? 29.764 -0.139  26.777  1.00  39.19 ? 2022 HOH A O   1 
HETATM 2325 O  O   . HOH N 6 .   ? 30.028 1.121   29.238  1.00  32.48 ? 2023 HOH A O   1 
HETATM 2326 O  O   . HOH N 6 .   ? 8.627  -12.765 5.091   1.00  44.10 ? 2024 HOH A O   1 
HETATM 2327 O  O   . HOH N 6 .   ? 8.986  -11.316 8.018   1.00  45.84 ? 2025 HOH A O   1 
HETATM 2328 O  O   . HOH N 6 .   ? 28.045 -2.690  36.193  1.00  28.79 ? 2026 HOH A O   1 
HETATM 2329 O  O   . HOH N 6 .   ? 33.949 2.456   32.642  1.00  77.17 ? 2027 HOH A O   1 
HETATM 2330 O  O   . HOH N 6 .   ? 37.575 -5.876  30.577  1.00  43.56 ? 2028 HOH A O   1 
HETATM 2331 O  O   . HOH N 6 .   ? 33.049 -4.639  25.703  1.00  34.18 ? 2029 HOH A O   1 
HETATM 2332 O  O   . HOH N 6 .   ? 37.025 -17.193 17.459  1.00  32.62 ? 2030 HOH A O   1 
HETATM 2333 O  O   . HOH N 6 .   ? 36.776 -26.096 23.985  1.00  61.12 ? 2031 HOH A O   1 
HETATM 2334 O  O   . HOH N 6 .   ? 27.989 -2.634  33.258  1.00  19.58 ? 2032 HOH A O   1 
HETATM 2335 O  O   . HOH N 6 .   ? 24.613 -2.147  33.400  1.00  25.34 ? 2033 HOH A O   1 
HETATM 2336 O  O   . HOH N 6 .   ? 18.290 -3.109  37.647  1.00  43.47 ? 2034 HOH A O   1 
HETATM 2337 O  O   . HOH N 6 .   ? 14.022 -3.377  34.959  1.00  46.05 ? 2035 HOH A O   1 
HETATM 2338 O  O   . HOH N 6 .   ? 18.915 -14.292 31.056  1.00  19.72 ? 2036 HOH A O   1 
HETATM 2339 O  O   . HOH N 6 .   ? 17.016 -19.901 30.255  1.00  16.95 ? 2037 HOH A O   1 
HETATM 2340 O  O   . HOH N 6 .   ? 25.606 -26.597 27.905  1.00  33.69 ? 2038 HOH A O   1 
HETATM 2341 O  O   . HOH N 6 .   ? 4.005  -3.883  25.728  1.00  45.76 ? 2039 HOH A O   1 
HETATM 2342 O  O   . HOH N 6 .   ? 6.474  -1.622  24.274  1.00  38.69 ? 2040 HOH A O   1 
HETATM 2343 O  O   . HOH N 6 .   ? 4.667  -10.832 33.419  1.00  36.27 ? 2041 HOH A O   1 
HETATM 2344 O  O   . HOH N 6 .   ? -1.767 -5.048  24.212  1.00  53.32 ? 2042 HOH A O   1 
HETATM 2345 O  O   . HOH N 6 .   ? 1.395  -13.356 17.978  1.00  21.40 ? 2043 HOH A O   1 
HETATM 2346 O  O   . HOH N 6 .   ? -2.150 -13.163 22.943  1.00  36.28 ? 2044 HOH A O   1 
HETATM 2347 O  O   . HOH N 6 .   ? -1.818 -11.080 21.720  1.00  64.14 ? 2045 HOH A O   1 
HETATM 2348 O  O   . HOH N 6 .   ? 3.111  -19.545 22.786  1.00  22.37 ? 2046 HOH A O   1 
HETATM 2349 O  O   . HOH N 6 .   ? 3.109  -14.959 19.357  1.00  17.63 ? 2047 HOH A O   1 
HETATM 2350 O  O   . HOH N 6 .   ? -2.294 -16.669 24.117  1.00  21.54 ? 2048 HOH A O   1 
HETATM 2351 O  O   . HOH N 6 .   ? -1.204 -17.432 31.899  1.00  25.35 ? 2049 HOH A O   1 
HETATM 2352 O  O   . HOH N 6 .   ? -0.047 -20.092 23.973  1.00  33.80 ? 2050 HOH A O   1 
HETATM 2353 O  O   . HOH N 6 .   ? -3.327 -18.398 25.990  1.00  36.90 ? 2051 HOH A O   1 
HETATM 2354 O  O   . HOH N 6 .   ? 5.737  -19.478 21.884  1.00  19.58 ? 2052 HOH A O   1 
HETATM 2355 O  O   . HOH N 6 .   ? 30.657 -4.206  15.630  1.00  35.23 ? 2053 HOH A O   1 
HETATM 2356 O  O   . HOH N 6 .   ? 1.295  -18.104 17.174  1.00  37.66 ? 2054 HOH A O   1 
HETATM 2357 O  O   . HOH N 6 .   ? 7.965  -25.801 19.962  1.00  50.74 ? 2055 HOH A O   1 
HETATM 2358 O  O   . HOH N 6 .   ? 11.140 -25.765 24.120  1.00  40.36 ? 2056 HOH A O   1 
HETATM 2359 O  O   . HOH N 6 .   ? 13.412 -29.809 24.226  1.00  29.53 ? 2057 HOH A O   1 
HETATM 2360 O  O   . HOH N 6 .   ? 30.344 -12.451 13.652  1.00  34.32 ? 2058 HOH A O   1 
HETATM 2361 O  O   . HOH N 6 .   ? 28.974 -12.884 7.803   1.00  30.71 ? 2059 HOH A O   1 
HETATM 2362 O  O   . HOH N 6 .   ? 28.894 -9.401  11.191  1.00  27.99 ? 2060 HOH A O   1 
HETATM 2363 O  O   . HOH N 6 .   ? 27.821 -14.036 13.710  1.00  16.04 ? 2061 HOH A O   1 
HETATM 2364 O  O   . HOH N 6 .   ? 18.221 -2.470  7.964   1.00  12.23 ? 2062 HOH A O   1 
HETATM 2365 O  O   . HOH N 6 .   ? 23.007 -7.766  5.121   1.00  18.61 ? 2063 HOH A O   1 
HETATM 2366 O  O   . HOH N 6 .   ? 22.155 -5.547  3.470   1.00  44.80 ? 2064 HOH A O   1 
HETATM 2367 O  O   . HOH N 6 .   ? 20.487 -5.808  1.926   1.00  29.31 ? 2065 HOH A O   1 
HETATM 2368 O  O   . HOH N 6 .   ? 20.748 -9.259  2.545   1.00  41.82 ? 2066 HOH A O   1 
HETATM 2369 O  O   . HOH N 6 .   ? 16.110 -5.329  11.670  0.50  18.91 ? 2067 HOH A O   1 
HETATM 2370 O  O   . HOH N 6 .   ? 10.452 -5.237  8.645   1.00  53.08 ? 2068 HOH A O   1 
HETATM 2371 O  O   . HOH N 6 .   ? 15.833 -7.721  10.039  0.50  16.00 ? 2069 HOH A O   1 
HETATM 2372 O  O   . HOH N 6 .   ? 14.175 -2.949  11.448  1.00  26.38 ? 2070 HOH A O   1 
HETATM 2373 O  O   . HOH N 6 .   ? 11.608 -3.735  4.728   1.00  43.61 ? 2071 HOH A O   1 
HETATM 2374 O  O   . HOH N 6 .   ? 11.988 -3.148  7.041   1.00  40.11 ? 2072 HOH A O   1 
HETATM 2375 O  O   . HOH N 6 .   ? 3.058  -12.042 13.884  1.00  33.80 ? 2073 HOH A O   1 
HETATM 2376 O  O   . HOH N 6 .   ? 10.148 -5.521  3.496   1.00  56.90 ? 2074 HOH A O   1 
HETATM 2377 O  O   . HOH N 6 .   ? 12.385 -2.862  2.346   1.00  39.02 ? 2075 HOH A O   1 
HETATM 2378 O  O   . HOH N 6 .   ? 16.422 -7.794  0.937   1.00  32.34 ? 2076 HOH A O   1 
HETATM 2379 O  O   . HOH N 6 .   ? 10.651 -11.266 3.030   1.00  24.27 ? 2077 HOH A O   1 
HETATM 2380 O  O   . HOH N 6 .   ? 23.943 10.681  25.546  1.00  45.05 ? 2078 HOH A O   1 
HETATM 2381 O  O   . HOH N 6 .   ? 9.477  -9.315  8.958   1.00  28.98 ? 2079 HOH A O   1 
HETATM 2382 O  O   . HOH N 6 .   ? 14.484 -16.243 8.252   1.00  29.27 ? 2080 HOH A O   1 
HETATM 2383 O  O   . HOH N 6 .   ? 17.962 -15.543 7.859   1.00  13.35 ? 2081 HOH A O   1 
HETATM 2384 O  O   . HOH N 6 .   ? 11.098 -11.860 7.001   1.00  25.66 ? 2082 HOH A O   1 
HETATM 2385 O  O   . HOH N 6 .   ? 15.679 -15.372 3.525   1.00  18.76 ? 2083 HOH A O   1 
HETATM 2386 O  O   . HOH N 6 .   ? 21.639 -10.086 5.148   1.00  20.09 ? 2084 HOH A O   1 
HETATM 2387 O  O   . HOH N 6 .   ? 17.017 -10.551 2.643   1.00  22.02 ? 2085 HOH A O   1 
HETATM 2388 O  O   . HOH N 6 .   ? 24.779 -18.477 14.471  1.00  32.45 ? 2086 HOH A O   1 
HETATM 2389 O  O   . HOH N 6 .   ? 22.126 -19.467 13.956  1.00  26.10 ? 2087 HOH A O   1 
HETATM 2390 O  O   . HOH N 6 .   ? 26.424 -19.849 13.901  1.00  19.54 ? 2088 HOH A O   1 
HETATM 2391 O  O   . HOH N 6 .   ? 29.586 -16.442 19.665  1.00  10.45 ? 2089 HOH A O   1 
HETATM 2392 O  O   . HOH N 6 .   ? 34.138 -13.769 14.264  1.00  39.55 ? 2090 HOH A O   1 
HETATM 2393 O  O   . HOH N 6 .   ? 35.172 -17.277 15.531  1.00  23.01 ? 2091 HOH A O   1 
HETATM 2394 O  O   . HOH N 6 .   ? 36.095 -18.944 19.563  1.00  28.46 ? 2092 HOH A O   1 
HETATM 2395 O  O   . HOH N 6 .   ? 30.963 -24.621 17.240  1.00  32.45 ? 2093 HOH A O   1 
HETATM 2396 O  O   . HOH N 6 .   ? 35.610 -23.785 25.200  1.00  34.39 ? 2094 HOH A O   1 
HETATM 2397 O  O   . HOH N 6 .   ? 31.079 -16.734 24.783  1.00  21.07 ? 2095 HOH A O   1 
HETATM 2398 O  O   . HOH N 6 .   ? 28.414 -24.308 16.302  1.00  43.24 ? 2096 HOH A O   1 
HETATM 2399 O  O   . HOH N 6 .   ? 33.279 -26.206 23.219  1.00  52.67 ? 2097 HOH A O   1 
HETATM 2400 O  O   . HOH N 6 .   ? 35.936 -18.724 22.267  1.00  38.65 ? 2098 HOH A O   1 
HETATM 2401 O  O   . HOH N 6 .   ? 26.591 -27.440 23.397  1.00  38.07 ? 2099 HOH A O   1 
HETATM 2402 O  O   . HOH N 6 .   ? 24.853 -25.457 23.944  1.00  29.38 ? 2100 HOH A O   1 
HETATM 2403 O  O   . HOH N 6 .   ? 23.552 -15.223 31.900  1.00  31.64 ? 2101 HOH A O   1 
HETATM 2404 O  O   . HOH N 6 .   ? 26.535 -17.440 29.642  1.00  23.04 ? 2102 HOH A O   1 
HETATM 2405 O  O   . HOH N 6 .   ? 25.999 -15.776 31.037  1.00  44.44 ? 2103 HOH A O   1 
HETATM 2406 O  O   . HOH N 6 .   ? 21.330 -12.912 34.993  1.00  38.74 ? 2104 HOH A O   1 
HETATM 2407 O  O   . HOH N 6 .   ? 18.789 -16.319 32.759  1.00  42.77 ? 2105 HOH A O   1 
HETATM 2408 O  O   . HOH N 6 .   ? 27.163 -21.427 33.031  1.00  30.44 ? 2106 HOH A O   1 
HETATM 2409 O  O   . HOH N 6 .   ? 20.068 -20.750 29.846  1.00  16.32 ? 2107 HOH A O   1 
HETATM 2410 O  O   . HOH N 6 .   ? 20.955 -25.248 27.672  1.00  31.31 ? 2108 HOH A O   1 
HETATM 2411 O  O   . HOH N 6 .   ? 20.480 -23.392 29.980  1.00  40.87 ? 2109 HOH A O   1 
HETATM 2412 O  O   . HOH N 6 .   ? 34.678 -25.014 29.557  1.00  30.65 ? 2110 HOH A O   1 
HETATM 2413 O  O   . HOH N 6 .   ? 30.926 -24.905 31.597  1.00  30.77 ? 2111 HOH A O   1 
HETATM 2414 O  O   . HOH N 6 .   ? 30.098 -18.113 26.963  1.00  18.74 ? 2112 HOH A O   1 
HETATM 2415 O  O   . HOH N 6 .   ? 31.723 -23.986 26.524  1.00  36.87 ? 2113 HOH A O   1 
HETATM 2416 O  O   . HOH N 6 .   ? 24.689 -24.941 26.041  1.00  28.93 ? 2114 HOH A O   1 
HETATM 2417 O  O   . HOH N 6 .   ? 29.818 -17.142 22.287  1.00  13.31 ? 2115 HOH A O   1 
HETATM 2418 O  O   . HOH N 6 .   ? 25.744 -23.130 16.096  1.00  20.68 ? 2116 HOH A O   1 
HETATM 2419 O  O   . HOH N 6 .   ? 16.793 -14.740 29.285  1.00  18.20 ? 2117 HOH A O   1 
HETATM 2420 O  O   . HOH N 6 .   ? 14.291 -13.703 29.882  1.00  22.06 ? 2118 HOH A O   1 
HETATM 2421 O  O   . HOH N 6 .   ? 13.998 -20.561 28.883  1.00  19.07 ? 2119 HOH A O   1 
HETATM 2422 O  O   . HOH N 6 .   ? 15.666 -17.264 29.169  1.00  17.26 ? 2120 HOH A O   1 
HETATM 2423 O  O   . HOH N 6 .   ? 4.646  -13.398 32.103  1.00  33.17 ? 2121 HOH A O   1 
HETATM 2424 O  O   . HOH N 6 .   ? 8.759  -18.122 32.454  1.00  12.91 ? 2122 HOH A O   1 
HETATM 2425 O  O   . HOH N 6 .   ? 10.048 -12.273 29.913  1.00  17.22 ? 2123 HOH A O   1 
HETATM 2426 O  O   . HOH N 6 .   ? 7.222  -11.498 31.302  1.00  24.11 ? 2124 HOH A O   1 
HETATM 2427 O  O   . HOH N 6 .   ? 11.246 -16.011 30.079  1.00  23.32 ? 2125 HOH A O   1 
HETATM 2428 O  O   . HOH N 6 .   ? 0.406  -11.915 34.019  1.00  34.43 ? 2126 HOH A O   1 
HETATM 2429 O  O   . HOH N 6 .   ? -1.468 -14.791 32.375  1.00  23.41 ? 2127 HOH A O   1 
HETATM 2430 O  O   . HOH N 6 .   ? -3.401 -14.242 24.707  1.00  37.73 ? 2128 HOH A O   1 
HETATM 2431 O  O   . HOH N 6 .   ? -6.186 -14.636 25.437  1.00  30.09 ? 2129 HOH A O   1 
HETATM 2432 O  O   . HOH N 6 .   ? -2.556 -11.769 31.582  1.00  29.59 ? 2130 HOH A O   1 
HETATM 2433 O  O   . HOH N 6 .   ? -4.473 -8.138  25.355  1.00  46.48 ? 2131 HOH A O   1 
HETATM 2434 O  O   . HOH N 6 .   ? -0.815 -8.001  23.850  1.00  25.18 ? 2132 HOH A O   1 
HETATM 2435 O  O   . HOH N 6 .   ? -1.913 -8.554  33.559  1.00  44.45 ? 2133 HOH A O   1 
HETATM 2436 O  O   . HOH N 6 .   ? -4.722 -11.525 31.841  1.00  32.66 ? 2134 HOH A O   1 
HETATM 2437 O  O   . HOH N 6 .   ? -6.994 -9.462  30.117  1.00  37.65 ? 2135 HOH A O   1 
HETATM 2438 O  O   . HOH N 6 .   ? -6.767 -10.965 28.029  1.00  39.55 ? 2136 HOH A O   1 
HETATM 2439 O  O   . HOH N 6 .   ? 3.442  -9.395  31.281  1.00  35.73 ? 2137 HOH A O   1 
HETATM 2440 O  O   . HOH N 6 .   ? 5.655  -8.764  34.882  1.00  34.05 ? 2138 HOH A O   1 
HETATM 2441 O  O   . HOH N 6 .   ? 10.275 -10.159 33.737  1.00  40.13 ? 2139 HOH A O   1 
HETATM 2442 O  O   . HOH N 6 .   ? 10.685 -4.786  32.427  1.00  28.56 ? 2140 HOH A O   1 
HETATM 2443 O  O   . HOH N 6 .   ? 17.004 -5.534  33.658  1.00  32.72 ? 2141 HOH A O   1 
HETATM 2444 O  O   . HOH N 6 .   ? 12.719 -11.544 30.721  1.00  19.74 ? 2142 HOH A O   1 
HETATM 2445 O  O   . HOH N 6 .   ? 21.552 -13.499 30.838  1.00  19.52 ? 2143 HOH A O   1 
HETATM 2446 O  O   . HOH N 6 .   ? 18.926 -12.304 33.624  1.00  25.34 ? 2144 HOH A O   1 
HETATM 2447 O  O   . HOH N 6 .   ? 24.724 -9.572  36.327  1.00  40.14 ? 2145 HOH A O   1 
HETATM 2448 O  O   . HOH N 6 .   ? 25.545 -10.963 34.196  1.00  36.10 ? 2146 HOH A O   1 
HETATM 2449 O  O   . HOH N 6 .   ? 30.043 -8.652  33.951  1.00  22.89 ? 2147 HOH A O   1 
HETATM 2450 O  O   . HOH N 6 .   ? 29.712 -7.305  28.582  1.00  23.18 ? 2148 HOH A O   1 
HETATM 2451 O  O   . HOH N 6 .   ? 29.724 1.319   21.283  1.00  38.42 ? 2149 HOH A O   1 
HETATM 2452 O  O   . HOH N 6 .   ? 33.007 -6.894  23.383  1.00  22.22 ? 2150 HOH A O   1 
HETATM 2453 O  O   . HOH N 6 .   ? 31.677 -2.397  26.886  1.00  38.69 ? 2151 HOH A O   1 
HETATM 2454 O  O   . HOH N 6 .   ? 33.108 0.142   20.390  1.00  57.64 ? 2152 HOH A O   1 
HETATM 2455 O  O   . HOH N 6 .   ? 35.935 -5.011  17.913  1.00  44.95 ? 2153 HOH A O   1 
HETATM 2456 O  O   . HOH N 6 .   ? 32.034 -8.978  16.306  1.00  35.25 ? 2154 HOH A O   1 
HETATM 2457 O  O   . HOH N 6 .   ? 36.816 -6.523  21.802  1.00  26.08 ? 2155 HOH A O   1 
HETATM 2458 O  O   . HOH N 6 .   ? 30.364 -6.692  17.094  1.00  17.75 ? 2156 HOH A O   1 
HETATM 2459 O  O   . HOH N 6 .   ? 28.610 -2.650  16.372  1.00  31.14 ? 2157 HOH A O   1 
HETATM 2460 O  O   . HOH N 6 .   ? 28.043 -4.639  16.399  1.00  27.59 ? 2158 HOH A O   1 
HETATM 2461 O  O   . HOH N 6 .   ? 31.059 -8.867  12.281  1.00  50.99 ? 2159 HOH A O   1 
HETATM 2462 O  O   . HOH N 6 .   ? 4.245  -20.849 20.703  1.00  49.58 ? 2160 HOH A O   1 
HETATM 2463 O  O   . HOH N 6 .   ? 3.413  -17.613 18.619  1.00  22.71 ? 2161 HOH A O   1 
HETATM 2464 O  O   . HOH N 6 .   ? 7.203  -23.482 21.727  1.00  21.42 ? 2162 HOH A O   1 
HETATM 2465 O  O   . HOH N 6 .   ? 10.715 -24.995 20.226  1.00  29.61 ? 2163 HOH A O   1 
HETATM 2466 O  O   . HOH N 6 .   ? 19.121 -18.663 23.624  1.00  11.91 ? 2164 HOH A O   1 
HETATM 2467 O  O   . HOH N 6 .   ? 12.517 -24.122 26.090  1.00  30.94 ? 2165 HOH A O   1 
HETATM 2468 O  O   . HOH N 6 .   ? 13.225 -28.705 20.949  1.00  47.04 ? 2166 HOH A O   1 
HETATM 2469 O  O   . HOH N 6 .   ? 20.468 -31.131 21.682  1.00  36.91 ? 2167 HOH A O   1 
HETATM 2470 O  O   . HOH N 6 .   ? 18.641 -32.364 26.716  1.00  43.79 ? 2168 HOH A O   1 
HETATM 2471 O  O   . HOH N 6 .   ? 16.770 -33.762 24.149  1.00  27.21 ? 2169 HOH A O   1 
HETATM 2472 O  O   . HOH N 6 .   ? 13.305 -31.871 20.343  1.00  40.28 ? 2170 HOH A O   1 
HETATM 2473 O  O   . HOH N 6 .   ? 14.148 -34.826 19.419  1.00  55.11 ? 2171 HOH A O   1 
HETATM 2474 O  O   . HOH N 6 .   ? 17.063 -30.532 13.175  1.00  33.98 ? 2172 HOH A O   1 
HETATM 2475 O  O   . HOH N 6 .   ? 13.963 -23.423 13.191  0.50  11.71 ? 2173 HOH A O   1 
HETATM 2476 O  O   . HOH N 6 .   ? 15.527 -24.293 13.123  1.00  31.70 ? 2174 HOH A O   1 
HETATM 2477 O  O   . HOH N 6 .   ? 25.676 -27.738 15.960  1.00  45.92 ? 2175 HOH A O   1 
HETATM 2478 O  O   . HOH N 6 .   ? 22.895 -26.891 9.723   1.00  51.07 ? 2176 HOH A O   1 
HETATM 2479 O  O   . HOH N 6 .   ? 15.342 -20.536 16.736  0.50  13.00 ? 2177 HOH A O   1 
HETATM 2480 O  O   . HOH N 6 .   ? 13.299 -19.918 12.556  0.45  17.33 ? 2178 HOH A O   1 
HETATM 2481 O  O   . HOH N 6 .   ? 12.791 -23.263 14.075  0.50  17.52 ? 2179 HOH A O   1 
HETATM 2482 O  O   . HOH N 6 .   ? 6.621  -14.935 11.404  1.00  39.01 ? 2180 HOH A O   1 
HETATM 2483 O  O   . HOH N 6 .   ? 16.437 -17.895 8.210   1.00  35.41 ? 2181 HOH A O   1 
HETATM 2484 O  O   . HOH N 6 .   ? 8.163  -11.086 10.551  1.00  38.60 ? 2182 HOH A O   1 
HETATM 2485 O  O   . HOH N 6 .   ? 4.126  -9.823  14.348  1.00  22.46 ? 2183 HOH A O   1 
HETATM 2486 O  O   . HOH N 6 .   ? 4.916  -8.183  14.122  1.00  38.60 ? 2184 HOH A O   1 
HETATM 2487 O  O   . HOH N 6 .   ? 11.591 -3.611  12.259  1.00  25.17 ? 2185 HOH A O   1 
HETATM 2488 O  O   . HOH N 6 .   ? 15.146 0.000   16.522  1.00  8.77  ? 2186 HOH A O   1 
HETATM 2489 O  O   . HOH N 6 .   ? 14.819 -0.956  13.406  1.00  20.01 ? 2187 HOH A O   1 
HETATM 2490 O  O   . HOH N 6 .   ? 24.709 5.622   24.956  1.00  17.75 ? 2188 HOH A O   1 
HETATM 2491 O  O   . HOH N 6 .   ? 24.600 8.756   23.922  1.00  30.41 ? 2189 HOH A O   1 
HETATM 2492 O  O   . HOH N 6 .   ? 18.081 6.792   26.482  1.00  39.32 ? 2190 HOH A O   1 
HETATM 2493 O  O   . HOH N 6 .   ? 16.257 -19.282 16.475  0.50  17.24 ? 2191 HOH A O   1 
HETATM 2494 O  O   . HOH N 6 .   ? 14.680 -19.842 14.343  0.55  17.38 ? 2192 HOH A O   1 
HETATM 2495 O  O   . HOH N 6 .   ? 16.911 -18.143 14.910  0.55  27.79 ? 2193 HOH A O   1 
HETATM 2496 O  O   . HOH N 6 .   ? 19.287 -18.607 10.873  1.00  27.93 ? 2194 HOH A O   1 
HETATM 2497 O  O   . HOH N 6 .   ? 9.593  -13.138 9.449   1.00  41.95 ? 2195 HOH A O   1 
HETATM 2498 O  O   . HOH N 6 .   ? 13.620 -17.969 11.304  1.00  30.27 ? 2196 HOH A O   1 
HETATM 2499 O  O   . HOH N 6 .   ? 10.156 -14.283 5.951   1.00  37.04 ? 2197 HOH A O   1 
HETATM 2500 O  O   . HOH O 6 .   ? 31.831 -7.310  -2.687  1.00  69.27 ? 2001 HOH F O   1 
HETATM 2501 O  O   . HOH O 6 .   ? 26.980 -3.720  -0.742  1.00  42.95 ? 2002 HOH F O   1 
HETATM 2502 O  O   . HOH O 6 .   ? 27.034 -8.376  0.362   1.00  48.42 ? 2003 HOH F O   1 
HETATM 2503 O  O   . HOH O 6 .   ? 14.859 -0.812  9.913   1.00  24.78 ? 2004 HOH F O   1 
HETATM 2504 O  O   . HOH O 6 .   ? 5.520  13.410  7.071   1.00  37.22 ? 2005 HOH F O   1 
HETATM 2505 O  O   . HOH O 6 .   ? 4.935  15.283  3.765   1.00  36.84 ? 2006 HOH F O   1 
HETATM 2506 O  O   . HOH O 6 .   ? 13.244 1.256   9.132   1.00  24.68 ? 2007 HOH F O   1 
HETATM 2507 O  O   . HOH O 6 .   ? 12.337 -1.255  8.985   1.00  34.99 ? 2008 HOH F O   1 
HETATM 2508 O  O   . HOH O 6 .   ? 9.348  7.295   10.172  1.00  44.81 ? 2009 HOH F O   1 
HETATM 2509 O  O   . HOH O 6 .   ? 23.429 -5.071  1.973   1.00  33.25 ? 2010 HOH F O   1 
HETATM 2510 O  O   . HOH O 6 .   ? 4.753  7.021   4.343   1.00  35.71 ? 2011 HOH F O   1 
HETATM 2511 O  O   . HOH O 6 .   ? 7.342  5.150   4.994   1.00  41.23 ? 2012 HOH F O   1 
HETATM 2512 O  O   . HOH O 6 .   ? 5.330  12.677  2.673   1.00  33.36 ? 2013 HOH F O   1 
HETATM 2513 O  O   . HOH O 6 .   ? 6.800  11.574  5.786   1.00  23.50 ? 2014 HOH F O   1 
HETATM 2514 O  O   . HOH O 6 .   ? 0.363  9.713   1.652   1.00  40.10 ? 2015 HOH F O   1 
HETATM 2515 O  O   . HOH O 6 .   ? 1.213  7.849   -1.786  1.00  32.30 ? 2016 HOH F O   1 
HETATM 2516 O  O   . HOH O 6 .   ? 24.182 3.735   -7.628  1.00  43.19 ? 2017 HOH F O   1 
HETATM 2517 O  O   . HOH O 6 .   ? 12.346 2.988   -2.698  1.00  31.19 ? 2018 HOH F O   1 
HETATM 2518 O  O   . HOH O 6 .   ? 10.951 3.691   -7.334  1.00  39.18 ? 2019 HOH F O   1 
HETATM 2519 O  O   . HOH O 6 .   ? 29.509 16.644  -2.305  1.00  26.01 ? 2020 HOH F O   1 
HETATM 2520 O  O   . HOH O 6 .   ? 11.883 0.259   2.052   1.00  36.98 ? 2021 HOH F O   1 
HETATM 2521 O  O   . HOH O 6 .   ? 4.479  14.480  -0.923  1.00  35.80 ? 2022 HOH F O   1 
HETATM 2522 O  O   . HOH O 6 .   ? 18.119 0.924   -2.867  1.00  21.70 ? 2023 HOH F O   1 
HETATM 2523 O  O   . HOH O 6 .   ? 4.905  13.226  -3.619  1.00  60.48 ? 2024 HOH F O   1 
HETATM 2524 O  O   . HOH O 6 .   ? 6.312  17.847  1.768   1.00  43.61 ? 2025 HOH F O   1 
HETATM 2525 O  O   . HOH O 6 .   ? 24.261 -2.701  2.088   1.00  20.73 ? 2026 HOH F O   1 
HETATM 2526 O  O   . HOH O 6 .   ? 20.563 -3.700  0.218   1.00  28.08 ? 2027 HOH F O   1 
HETATM 2527 O  O   . HOH O 6 .   ? 19.594 -1.376  -2.648  1.00  26.72 ? 2028 HOH F O   1 
HETATM 2528 O  O   . HOH O 6 .   ? 26.556 -2.375  1.333   1.00  26.72 ? 2029 HOH F O   1 
HETATM 2529 O  O   . HOH O 6 .   ? 36.562 -0.944  6.373   1.00  28.87 ? 2030 HOH F O   1 
HETATM 2530 O  O   . HOH O 6 .   ? 35.275 0.350   8.289   1.00  29.82 ? 2031 HOH F O   1 
HETATM 2531 O  O   . HOH O 6 .   ? 15.815 8.685   26.005  1.00  26.48 ? 2032 HOH F O   1 
HETATM 2532 O  O   . HOH O 6 .   ? 13.523 0.787   14.286  1.00  29.80 ? 2033 HOH F O   1 
HETATM 2533 O  O   . HOH O 6 .   ? 11.140 17.894  13.137  1.00  50.26 ? 2034 HOH F O   1 
HETATM 2534 O  O   . HOH O 6 .   ? 39.119 3.124   -0.161  1.00  35.38 ? 2035 HOH F O   1 
HETATM 2535 O  O   . HOH O 6 .   ? 37.485 16.849  8.829   1.00  55.59 ? 2036 HOH F O   1 
HETATM 2536 O  O   . HOH O 6 .   ? 36.984 2.755   1.529   1.00  24.11 ? 2037 HOH F O   1 
HETATM 2537 O  O   . HOH O 6 .   ? 30.836 27.467  10.103  1.00  30.10 ? 2038 HOH F O   1 
HETATM 2538 O  O   . HOH O 6 .   ? 26.515 3.839   -6.728  1.00  49.25 ? 2039 HOH F O   1 
HETATM 2539 O  O   . HOH O 6 .   ? 34.413 2.114   -0.214  1.00  33.25 ? 2040 HOH F O   1 
HETATM 2540 O  O   . HOH O 6 .   ? 27.503 20.603  -1.625  0.50  19.03 ? 2041 HOH F O   1 
HETATM 2541 O  O   . HOH O 6 .   ? 28.416 14.532  -1.136  1.00  17.67 ? 2042 HOH F O   1 
HETATM 2542 O  O   . HOH O 6 .   ? 18.836 1.539   -5.457  1.00  40.07 ? 2043 HOH F O   1 
HETATM 2543 O  O   . HOH O 6 .   ? 12.795 3.834   -5.305  1.00  33.73 ? 2044 HOH F O   1 
HETATM 2544 O  O   . HOH O 6 .   ? 14.884 1.627   -2.381  1.00  29.36 ? 2045 HOH F O   1 
HETATM 2545 O  O   . HOH O 6 .   ? 17.707 10.696  -10.913 1.00  34.53 ? 2046 HOH F O   1 
HETATM 2546 O  O   . HOH O 6 .   ? 20.087 11.410  -9.846  1.00  52.03 ? 2047 HOH F O   1 
HETATM 2547 O  O   . HOH O 6 .   ? 8.142  5.494   -7.076  1.00  33.02 ? 2048 HOH F O   1 
HETATM 2548 O  O   . HOH O 6 .   ? 6.730  13.264  0.453   1.00  22.00 ? 2049 HOH F O   1 
HETATM 2549 O  O   . HOH O 6 .   ? 4.790  10.150  -0.660  1.00  29.72 ? 2050 HOH F O   1 
HETATM 2550 O  O   . HOH O 6 .   ? 6.492  13.403  -5.869  1.00  33.47 ? 2051 HOH F O   1 
HETATM 2551 O  O   . HOH O 6 .   ? 7.302  19.753  -0.718  1.00  44.80 ? 2052 HOH F O   1 
HETATM 2552 O  O   . HOH O 6 .   ? 10.712 19.609  -2.891  1.00  26.92 ? 2053 HOH F O   1 
HETATM 2553 O  O   . HOH O 6 .   ? 8.754  15.096  0.033   1.00  17.53 ? 2054 HOH F O   1 
HETATM 2554 O  O   . HOH O 6 .   ? 31.601 16.130  -0.453  1.00  28.98 ? 2055 HOH F O   1 
HETATM 2555 O  O   . HOH O 6 .   ? 8.004  20.601  -9.421  1.00  52.03 ? 2056 HOH F O   1 
HETATM 2556 O  O   . HOH O 6 .   ? 6.732  17.074  -6.562  1.00  24.99 ? 2057 HOH F O   1 
HETATM 2557 O  O   . HOH O 6 .   ? 9.018  20.360  -5.235  1.00  50.13 ? 2058 HOH F O   1 
HETATM 2558 O  O   . HOH O 6 .   ? 12.701 16.385  -12.897 1.00  18.21 ? 2059 HOH F O   1 
HETATM 2559 O  O   . HOH O 6 .   ? 12.440 19.537  -0.646  1.00  23.05 ? 2060 HOH F O   1 
HETATM 2560 O  O   . HOH O 6 .   ? 29.894 4.148   18.012  1.00  33.13 ? 2061 HOH F O   1 
HETATM 2561 O  O   . HOH O 6 .   ? 13.112 25.790  2.103   1.00  36.08 ? 2062 HOH F O   1 
HETATM 2562 O  O   . HOH O 6 .   ? 15.390 25.202  -1.349  1.00  25.56 ? 2063 HOH F O   1 
HETATM 2563 O  O   . HOH O 6 .   ? 16.717 25.763  0.953   1.00  39.41 ? 2064 HOH F O   1 
HETATM 2564 O  O   . HOH O 6 .   ? 18.786 26.012  0.000   1.00  44.65 ? 2065 HOH F O   1 
HETATM 2565 O  O   . HOH O 6 .   ? 20.152 29.887  1.664   1.00  31.07 ? 2066 HOH F O   1 
HETATM 2566 O  O   . HOH O 6 .   ? 25.987 9.576   20.861  1.00  34.43 ? 2067 HOH F O   1 
HETATM 2567 O  O   . HOH O 6 .   ? 26.496 11.669  19.378  1.00  23.06 ? 2068 HOH F O   1 
HETATM 2568 O  O   . HOH O 6 .   ? 26.405 31.539  0.144   1.00  50.80 ? 2069 HOH F O   1 
HETATM 2569 O  O   . HOH O 6 .   ? 15.389 2.538   17.729  1.00  13.07 ? 2070 HOH F O   1 
HETATM 2570 O  O   . HOH O 6 .   ? 16.255 5.245   24.554  1.00  40.70 ? 2071 HOH F O   1 
HETATM 2571 O  O   . HOH O 6 .   ? 13.976 5.744   24.117  1.00  28.99 ? 2072 HOH F O   1 
HETATM 2572 O  O   . HOH O 6 .   ? 17.850 7.828   22.797  1.00  17.80 ? 2073 HOH F O   1 
HETATM 2573 O  O   . HOH O 6 .   ? 14.524 9.387   23.547  1.00  31.98 ? 2074 HOH F O   1 
HETATM 2574 O  O   . HOH O 6 .   ? 9.671  3.423   14.948  0.30  19.42 ? 2075 HOH F O   1 
HETATM 2575 O  O   . HOH O 6 .   ? 14.317 7.715   14.631  0.50  18.28 ? 2076 HOH F O   1 
HETATM 2576 O  O   . HOH O 6 .   ? 10.014 6.180   12.266  0.50  30.09 ? 2077 HOH F O   1 
HETATM 2577 O  O   . HOH O 6 .   ? 11.204 1.323   13.747  1.00  27.12 ? 2078 HOH F O   1 
HETATM 2578 O  O   . HOH O 6 .   ? 13.384 2.922   12.480  1.00  23.67 ? 2079 HOH F O   1 
HETATM 2579 O  O   . HOH O 6 .   ? 15.186 19.626  16.223  1.00  42.09 ? 2080 HOH F O   1 
HETATM 2580 O  O   . HOH O 6 .   ? 7.499  2.795   19.146  1.00  38.86 ? 2081 HOH F O   1 
HETATM 2581 O  O   . HOH O 6 .   ? 10.116 7.929   22.763  1.00  34.73 ? 2082 HOH F O   1 
HETATM 2582 O  O   . HOH O 6 .   ? 6.575  11.517  17.793  1.00  27.87 ? 2083 HOH F O   1 
HETATM 2583 O  O   . HOH O 6 .   ? 29.687 -10.587 6.544   1.00  33.33 ? 2084 HOH F O   1 
HETATM 2584 O  O   . HOH O 6 .   ? 8.522  9.720   12.235  1.00  29.43 ? 2085 HOH F O   1 
HETATM 2585 O  O   . HOH O 6 .   ? 9.621  13.477  13.104  1.00  41.64 ? 2086 HOH F O   1 
HETATM 2586 O  O   . HOH O 6 .   ? 8.909  11.854  14.856  1.00  27.19 ? 2087 HOH F O   1 
HETATM 2587 O  O   . HOH O 6 .   ? 10.700 15.590  20.006  1.00  22.59 ? 2088 HOH F O   1 
HETATM 2588 O  O   . HOH O 6 .   ? 10.738 15.330  13.886  1.00  36.06 ? 2089 HOH F O   1 
HETATM 2589 O  O   . HOH O 6 .   ? 11.232 10.687  21.536  1.00  26.46 ? 2090 HOH F O   1 
HETATM 2590 O  O   . HOH O 6 .   ? 16.631 10.202  22.000  1.00  17.60 ? 2091 HOH F O   1 
HETATM 2591 O  O   . HOH O 6 .   ? 21.923 19.437  14.769  1.00  23.95 ? 2092 HOH F O   1 
HETATM 2592 O  O   . HOH O 6 .   ? 24.319 18.484  15.748  1.00  25.60 ? 2093 HOH F O   1 
HETATM 2593 O  O   . HOH O 6 .   ? 31.166 16.445  14.229  1.00  10.28 ? 2094 HOH F O   1 
HETATM 2594 O  O   . HOH O 6 .   ? 26.202 13.564  18.057  1.00  20.83 ? 2095 HOH F O   1 
HETATM 2595 O  O   . HOH O 6 .   ? 33.209 16.816  20.784  1.00  17.13 ? 2096 HOH F O   1 
HETATM 2596 O  O   . HOH O 6 .   ? 36.176 20.172  18.686  1.00  19.99 ? 2097 HOH F O   1 
HETATM 2597 O  O   . HOH O 6 .   ? 30.502 20.535  22.944  1.00  27.91 ? 2098 HOH F O   1 
HETATM 2598 O  O   . HOH O 6 .   ? 34.772 16.231  10.790  1.00  27.38 ? 2099 HOH F O   1 
HETATM 2599 O  O   . HOH O 6 .   ? 27.351 30.572  12.410  1.00  44.93 ? 2100 HOH F O   1 
HETATM 2600 O  O   . HOH O 6 .   ? 31.851 29.725  14.019  1.00  41.94 ? 2101 HOH F O   1 
HETATM 2601 O  O   . HOH O 6 .   ? 29.590 25.470  8.654   1.00  27.56 ? 2102 HOH F O   1 
HETATM 2602 O  O   . HOH O 6 .   ? 34.453 16.252  2.841   1.00  34.88 ? 2103 HOH F O   1 
HETATM 2603 O  O   . HOH O 6 .   ? 28.916 21.055  0.599   1.00  16.28 ? 2104 HOH F O   1 
HETATM 2604 O  O   . HOH O 6 .   ? 33.056 25.967  2.481   1.00  49.62 ? 2105 HOH F O   1 
HETATM 2605 O  O   . HOH O 6 .   ? 34.911 18.124  5.718   1.00  31.10 ? 2106 HOH F O   1 
HETATM 2606 O  O   . HOH O 6 .   ? 28.322 25.439  3.092   1.00  43.75 ? 2107 HOH F O   1 
HETATM 2607 O  O   . HOH O 6 .   ? 29.243 23.719  1.153   1.00  45.92 ? 2108 HOH F O   1 
HETATM 2608 O  O   . HOH O 6 .   ? 34.356 19.742  10.252  1.00  29.36 ? 2109 HOH F O   1 
HETATM 2609 O  O   . HOH O 6 .   ? 35.683 24.529  4.121   1.00  33.31 ? 2110 HOH F O   1 
HETATM 2610 O  O   . HOH O 6 .   ? 35.174 17.860  8.378   1.00  27.90 ? 2111 HOH F O   1 
HETATM 2611 O  O   . HOH O 6 .   ? 34.419 25.250  6.369   1.00  33.97 ? 2112 HOH F O   1 
HETATM 2612 O  O   . HOH O 6 .   ? 32.454 27.526  12.498  1.00  26.71 ? 2113 HOH F O   1 
HETATM 2613 O  O   . HOH O 6 .   ? 30.710 25.194  6.775   1.00  41.23 ? 2114 HOH F O   1 
HETATM 2614 O  O   . HOH O 6 .   ? 32.886 17.417  12.416  1.00  13.71 ? 2115 HOH F O   1 
HETATM 2615 O  O   . HOH O 6 .   ? 25.703 22.883  15.403  1.00  26.28 ? 2116 HOH F O   1 
HETATM 2616 O  O   . HOH O 6 .   ? 25.658 14.905  -0.851  1.00  15.78 ? 2117 HOH F O   1 
HETATM 2617 O  O   . HOH O 6 .   ? 23.953 13.933  -2.789  1.00  18.41 ? 2118 HOH F O   1 
HETATM 2618 O  O   . HOH O 6 .   ? 20.432 12.414  -5.130  1.00  17.90 ? 2119 HOH F O   1 
HETATM 2619 O  O   . HOH O 6 .   ? 18.415 11.504  -7.936  1.00  24.11 ? 2120 HOH F O   1 
HETATM 2620 O  O   . HOH O 6 .   ? 21.403 16.296  -4.452  1.00  21.10 ? 2121 HOH F O   1 
HETATM 2621 O  O   . HOH O 6 .   ? 15.440 9.406   -9.962  1.00  26.04 ? 2122 HOH F O   1 
HETATM 2622 O  O   . HOH O 6 .   ? 14.184 11.837  -14.044 1.00  31.90 ? 2123 HOH F O   1 
HETATM 2623 O  O   . HOH O 6 .   ? 7.807  19.695  -12.448 1.00  51.36 ? 2124 HOH F O   1 
HETATM 2624 O  O   . HOH O 6 .   ? 7.866  8.085   -5.931  1.00  19.75 ? 2125 HOH F O   1 
HETATM 2625 O  O   . HOH O 6 .   ? 8.913  11.572  -14.934 1.00  27.17 ? 2126 HOH F O   1 
HETATM 2626 O  O   . HOH O 6 .   ? 10.839 11.553  -13.180 1.00  28.02 ? 2127 HOH F O   1 
HETATM 2627 O  O   . HOH O 6 .   ? 5.798  8.517   -8.916  1.00  45.24 ? 2128 HOH F O   1 
HETATM 2628 O  O   . HOH O 6 .   ? 16.654 10.772  -8.816  1.00  37.81 ? 2129 HOH F O   1 
HETATM 2629 O  O   . HOH O 6 .   ? 22.668 10.469  -7.877  1.00  35.86 ? 2130 HOH F O   1 
HETATM 2630 O  O   . HOH O 6 .   ? 19.429 3.810   -7.254  1.00  39.94 ? 2131 HOH F O   1 
HETATM 2631 O  O   . HOH O 6 .   ? 16.044 3.621   -8.494  1.00  52.05 ? 2132 HOH F O   1 
HETATM 2632 O  O   . HOH O 6 .   ? 19.264 8.816   -11.711 1.00  28.60 ? 2133 HOH F O   1 
HETATM 2633 O  O   . HOH O 6 .   ? 22.303 5.057   -6.852  1.00  31.34 ? 2134 HOH F O   1 
HETATM 2634 O  O   . HOH O 6 .   ? 28.178 5.861   -4.425  1.00  37.61 ? 2135 HOH F O   1 
HETATM 2635 O  O   . HOH O 6 .   ? 23.020 11.641  -4.214  1.00  16.06 ? 2136 HOH F O   1 
HETATM 2636 O  O   . HOH O 6 .   ? 27.534 12.650  -5.032  1.00  45.11 ? 2137 HOH F O   1 
HETATM 2637 O  O   . HOH O 6 .   ? 30.205 11.980  -4.045  0.50  23.24 ? 2138 HOH F O   1 
HETATM 2638 O  O   . HOH O 6 .   ? 33.870 13.372  -0.911  1.00  37.92 ? 2139 HOH F O   1 
HETATM 2639 O  O   . HOH O 6 .   ? 29.479 12.629  -2.989  0.50  12.02 ? 2140 HOH F O   1 
HETATM 2640 O  O   . HOH O 6 .   ? 30.455 13.787  0.517   1.00  17.71 ? 2141 HOH F O   1 
HETATM 2641 O  O   . HOH O 6 .   ? 34.890 10.985  -0.241  1.00  38.44 ? 2142 HOH F O   1 
HETATM 2642 O  O   . HOH O 6 .   ? 33.812 13.842  2.069   1.00  28.01 ? 2143 HOH F O   1 
HETATM 2643 O  O   . HOH O 6 .   ? 38.510 8.937   4.270   1.00  41.05 ? 2144 HOH F O   1 
HETATM 2644 O  O   . HOH O 6 .   ? 35.974 7.585   6.198   1.00  26.83 ? 2145 HOH F O   1 
HETATM 2645 O  O   . HOH O 6 .   ? 37.468 4.950   10.447  1.00  31.72 ? 2146 HOH F O   1 
HETATM 2646 O  O   . HOH O 6 .   ? 31.855 -1.164  13.035  1.00  40.15 ? 2147 HOH F O   1 
HETATM 2647 O  O   . HOH O 6 .   ? 32.562 3.806   17.286  1.00  65.29 ? 2148 HOH F O   1 
HETATM 2648 O  O   . HOH O 6 .   ? 38.564 6.990   15.487  1.00  42.07 ? 2149 HOH F O   1 
HETATM 2649 O  O   . HOH O 6 .   ? 34.794 8.755   21.840  1.00  20.46 ? 2150 HOH F O   1 
HETATM 2650 O  O   . HOH O 6 .   ? 35.811 7.046   12.644  1.00  23.42 ? 2151 HOH F O   1 
HETATM 2651 O  O   . HOH O 6 .   ? 37.997 12.907  15.102  1.00  31.19 ? 2152 HOH F O   1 
HETATM 2652 O  O   . HOH O 6 .   ? 30.588 6.746   16.628  1.00  18.79 ? 2153 HOH F O   1 
HETATM 2653 O  O   . HOH O 6 .   ? 28.142 4.637   15.943  1.00  25.98 ? 2154 HOH F O   1 
HETATM 2654 O  O   . HOH O 6 .   ? 10.426 20.740  -0.603  1.00  34.98 ? 2155 HOH F O   1 
HETATM 2655 O  O   . HOH O 6 .   ? 8.709  17.732  0.794   1.00  23.48 ? 2156 HOH F O   1 
HETATM 2656 O  O   . HOH O 6 .   ? 15.554 25.094  3.475   1.00  27.72 ? 2157 HOH F O   1 
HETATM 2657 O  O   . HOH O 6 .   ? 13.470 23.521  0.263   1.00  21.88 ? 2158 HOH F O   1 
HETATM 2658 O  O   . HOH O 6 .   ? 24.563 18.878  5.140   1.00  12.85 ? 2159 HOH F O   1 
HETATM 2659 O  O   . HOH O 6 .   ? 20.374 24.265  -0.432  1.00  28.23 ? 2160 HOH F O   1 
HETATM 2660 O  O   . HOH O 6 .   ? 17.593 28.408  4.399   1.00  43.67 ? 2161 HOH F O   1 
HETATM 2661 O  O   . HOH O 6 .   ? 22.272 28.050  0.926   1.00  57.75 ? 2162 HOH F O   1 
HETATM 2662 O  O   . HOH O 6 .   ? 28.417 28.789  7.528   1.00  37.00 ? 2163 HOH F O   1 
HETATM 2663 O  O   . HOH O 6 .   ? 24.639 31.210  7.608   1.00  30.98 ? 2164 HOH F O   1 
HETATM 2664 O  O   . HOH O 6 .   ? 27.788 25.906  0.447   1.00  39.35 ? 2165 HOH F O   1 
HETATM 2665 O  O   . HOH O 6 .   ? 26.094 32.496  2.607   1.00  48.30 ? 2166 HOH F O   1 
HETATM 2666 O  O   . HOH O 6 .   ? 18.290 33.847  13.341  1.00  35.56 ? 2167 HOH F O   1 
HETATM 2667 O  O   . HOH O 6 .   ? 14.412 23.392  10.978  1.00  23.29 ? 2168 HOH F O   1 
HETATM 2668 O  O   . HOH O 6 .   ? 12.243 25.239  13.463  1.00  43.37 ? 2169 HOH F O   1 
HETATM 2669 O  O   . HOH O 6 .   ? 17.399 30.780  12.654  1.00  46.75 ? 2170 HOH F O   1 
HETATM 2670 O  O   . HOH O 6 .   ? 25.311 27.633  15.414  1.00  34.57 ? 2171 HOH F O   1 
HETATM 2671 O  O   . HOH O 6 .   ? 17.617 20.626  8.820   0.50  15.04 ? 2172 HOH F O   1 
HETATM 2672 O  O   . HOH O 6 .   ? 13.740 20.084  11.314  1.00  41.52 ? 2173 HOH F O   1 
HETATM 2673 O  O   . HOH O 6 .   ? 7.030  15.087  8.132   1.00  54.47 ? 2174 HOH F O   1 
HETATM 2674 O  O   . HOH O 6 .   ? 8.688  10.755  10.028  1.00  32.62 ? 2175 HOH F O   1 
HETATM 2675 O  O   . HOH O 6 .   ? 13.083 17.147  15.936  1.00  38.17 ? 2176 HOH F O   1 
HETATM 2676 O  O   . HOH O 6 .   ? 9.846  16.061  12.051  1.00  26.29 ? 2177 HOH F O   1 
HETATM 2677 O  O   . HOH O 6 .   ? 12.000 3.524   10.305  1.00  24.96 ? 2178 HOH F O   1 
HETATM 2678 O  O   . HOH O 6 .   ? 15.281 1.027   11.490  1.00  19.44 ? 2179 HOH F O   1 
HETATM 2679 O  O   . HOH O 6 .   ? 17.325 0.046   8.888   1.00  8.17  ? 2180 HOH F O   1 
HETATM 2680 O  O   . HOH O 6 .   ? 28.903 -8.460  8.304   1.00  28.01 ? 2181 HOH F O   1 
HETATM 2681 O  O   . HOH O 6 .   ? 30.031 -5.553  7.012   1.00  19.57 ? 2182 HOH F O   1 
HETATM 2682 O  O   . HOH O 6 .   ? 25.405 -6.744  2.033   1.00  35.81 ? 2183 HOH F O   1 
HETATM 2683 O  O   . HOH O 6 .   ? 22.579 -10.221 3.257   1.00  32.81 ? 2184 HOH F O   1 
HETATM 2684 O  O   . HOH O 6 .   ? 15.673 19.888  10.551  0.45  13.55 ? 2185 HOH F O   1 
HETATM 2685 O  O   . HOH O 6 .   ? 18.889 18.514  14.303  1.00  25.74 ? 2186 HOH F O   1 
HETATM 2686 O  O   . HOH O 6 .   ? 13.537 18.131  12.295  1.00  32.85 ? 2187 HOH F O   1 
HETATM 2687 O  O   . HOH O 6 .   ? 17.688 18.634  16.111  1.00  28.06 ? 2188 HOH F O   1 
HETATM 2688 O  O   . HOH O 6 .   ? 18.199 19.252  9.439   0.50  14.60 ? 2189 HOH F O   1 
HETATM 2689 O  O   . HOH O 6 .   ? 17.973 18.080  10.858  0.45  11.59 ? 2190 HOH F O   1 
HETATM 2690 O  O   . HOH O 6 .   ? 24.633 17.406  -1.381  0.50  7.37  ? 2191 HOH F O   1 
HETATM 2691 O  O   . HOH O 6 .   ? 22.996 20.755  -2.050  0.50  9.61  ? 2192 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 CYS 111 111 111 CYS CYS 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 CYS 111 111 111 CYS CYS 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 SO4 1   1154 1154 SO4 SO4 A . 
D 2 SO4 1   1155 1155 SO4 SO4 A . 
E 3 CU  1   1157 1157 CU  CU  A . 
F 4 ZN  1   1158 1158 ZN  ZN  A . 
G 4 ZN  1   1159 1159 ZN  ZN  A . 
H 2 SO4 1   1154 1154 SO4 SO4 F . 
I 4 ZN  1   1155 1155 ZN  ZN  F . 
J 3 CU  1   1156 1156 CU  CU  F . 
K 4 ZN  1   1157 1157 ZN  ZN  F . 
L 5 ACT 1   1158 1158 ACT ACT F . 
M 5 ACT 1   1159 1159 ACT ACT F . 
N 6 HOH 1   2001 2001 HOH HOH A . 
N 6 HOH 2   2002 2002 HOH HOH A . 
N 6 HOH 3   2003 2003 HOH HOH A . 
N 6 HOH 4   2004 2004 HOH HOH A . 
N 6 HOH 5   2005 2005 HOH HOH A . 
N 6 HOH 6   2006 2006 HOH HOH A . 
N 6 HOH 7   2007 2007 HOH HOH A . 
N 6 HOH 8   2008 2008 HOH HOH A . 
N 6 HOH 9   2009 2009 HOH HOH A . 
N 6 HOH 10  2010 2010 HOH HOH A . 
N 6 HOH 11  2011 2011 HOH HOH A . 
N 6 HOH 12  2012 2012 HOH HOH A . 
N 6 HOH 13  2013 2013 HOH HOH A . 
N 6 HOH 14  2014 2014 HOH HOH A . 
N 6 HOH 15  2015 2015 HOH HOH A . 
N 6 HOH 16  2016 2016 HOH HOH A . 
N 6 HOH 17  2017 2017 HOH HOH A . 
N 6 HOH 18  2018 2018 HOH HOH A . 
N 6 HOH 19  2019 2019 HOH HOH A . 
N 6 HOH 20  2020 2020 HOH HOH A . 
N 6 HOH 21  2021 2021 HOH HOH A . 
N 6 HOH 22  2022 2022 HOH HOH A . 
N 6 HOH 23  2023 2023 HOH HOH A . 
N 6 HOH 24  2024 2024 HOH HOH A . 
N 6 HOH 25  2025 2025 HOH HOH A . 
N 6 HOH 26  2026 2026 HOH HOH A . 
N 6 HOH 27  2027 2027 HOH HOH A . 
N 6 HOH 28  2028 2028 HOH HOH A . 
N 6 HOH 29  2029 2029 HOH HOH A . 
N 6 HOH 30  2030 2030 HOH HOH A . 
N 6 HOH 31  2031 2031 HOH HOH A . 
N 6 HOH 32  2032 2032 HOH HOH A . 
N 6 HOH 33  2033 2033 HOH HOH A . 
N 6 HOH 34  2034 2034 HOH HOH A . 
N 6 HOH 35  2035 2035 HOH HOH A . 
N 6 HOH 36  2036 2036 HOH HOH A . 
N 6 HOH 37  2037 2037 HOH HOH A . 
N 6 HOH 38  2038 2038 HOH HOH A . 
N 6 HOH 39  2039 2039 HOH HOH A . 
N 6 HOH 40  2040 2040 HOH HOH A . 
N 6 HOH 41  2041 2041 HOH HOH A . 
N 6 HOH 42  2042 2042 HOH HOH A . 
N 6 HOH 43  2043 2043 HOH HOH A . 
N 6 HOH 44  2044 2044 HOH HOH A . 
N 6 HOH 45  2045 2045 HOH HOH A . 
N 6 HOH 46  2046 2046 HOH HOH A . 
N 6 HOH 47  2047 2047 HOH HOH A . 
N 6 HOH 48  2048 2048 HOH HOH A . 
N 6 HOH 49  2049 2049 HOH HOH A . 
N 6 HOH 50  2050 2050 HOH HOH A . 
N 6 HOH 51  2051 2051 HOH HOH A . 
N 6 HOH 52  2052 2052 HOH HOH A . 
N 6 HOH 53  2053 2053 HOH HOH A . 
N 6 HOH 54  2054 2054 HOH HOH A . 
N 6 HOH 55  2055 2055 HOH HOH A . 
N 6 HOH 56  2056 2056 HOH HOH A . 
N 6 HOH 57  2057 2057 HOH HOH A . 
N 6 HOH 58  2058 2058 HOH HOH A . 
N 6 HOH 59  2059 2059 HOH HOH A . 
N 6 HOH 60  2060 2060 HOH HOH A . 
N 6 HOH 61  2061 2061 HOH HOH A . 
N 6 HOH 62  2062 2062 HOH HOH A . 
N 6 HOH 63  2063 2063 HOH HOH A . 
N 6 HOH 64  2064 2064 HOH HOH A . 
N 6 HOH 65  2065 2065 HOH HOH A . 
N 6 HOH 66  2066 2066 HOH HOH A . 
N 6 HOH 67  2067 2067 HOH HOH A . 
N 6 HOH 68  2068 2068 HOH HOH A . 
N 6 HOH 69  2069 2069 HOH HOH A . 
N 6 HOH 70  2070 2070 HOH HOH A . 
N 6 HOH 71  2071 2071 HOH HOH A . 
N 6 HOH 72  2072 2072 HOH HOH A . 
N 6 HOH 73  2073 2073 HOH HOH A . 
N 6 HOH 74  2074 2074 HOH HOH A . 
N 6 HOH 75  2075 2075 HOH HOH A . 
N 6 HOH 76  2076 2076 HOH HOH A . 
N 6 HOH 77  2077 2077 HOH HOH A . 
N 6 HOH 78  2078 2078 HOH HOH A . 
N 6 HOH 79  2079 2079 HOH HOH A . 
N 6 HOH 80  2080 2080 HOH HOH A . 
N 6 HOH 81  2081 2081 HOH HOH A . 
N 6 HOH 82  2082 2082 HOH HOH A . 
N 6 HOH 83  2083 2083 HOH HOH A . 
N 6 HOH 84  2084 2084 HOH HOH A . 
N 6 HOH 85  2085 2085 HOH HOH A . 
N 6 HOH 86  2086 2086 HOH HOH A . 
N 6 HOH 87  2087 2087 HOH HOH A . 
N 6 HOH 88  2088 2088 HOH HOH A . 
N 6 HOH 89  2089 2089 HOH HOH A . 
N 6 HOH 90  2090 2090 HOH HOH A . 
N 6 HOH 91  2091 2091 HOH HOH A . 
N 6 HOH 92  2092 2092 HOH HOH A . 
N 6 HOH 93  2093 2093 HOH HOH A . 
N 6 HOH 94  2094 2094 HOH HOH A . 
N 6 HOH 95  2095 2095 HOH HOH A . 
N 6 HOH 96  2096 2096 HOH HOH A . 
N 6 HOH 97  2097 2097 HOH HOH A . 
N 6 HOH 98  2098 2098 HOH HOH A . 
N 6 HOH 99  2099 2099 HOH HOH A . 
N 6 HOH 100 2100 2100 HOH HOH A . 
N 6 HOH 101 2101 2101 HOH HOH A . 
N 6 HOH 102 2102 2102 HOH HOH A . 
N 6 HOH 103 2103 2103 HOH HOH A . 
N 6 HOH 104 2104 2104 HOH HOH A . 
N 6 HOH 105 2105 2105 HOH HOH A . 
N 6 HOH 106 2106 2106 HOH HOH A . 
N 6 HOH 107 2107 2107 HOH HOH A . 
N 6 HOH 108 2108 2108 HOH HOH A . 
N 6 HOH 109 2109 2109 HOH HOH A . 
N 6 HOH 110 2110 2110 HOH HOH A . 
N 6 HOH 111 2111 2111 HOH HOH A . 
N 6 HOH 112 2112 2112 HOH HOH A . 
N 6 HOH 113 2113 2113 HOH HOH A . 
N 6 HOH 114 2114 2114 HOH HOH A . 
N 6 HOH 115 2115 2115 HOH HOH A . 
N 6 HOH 116 2116 2116 HOH HOH A . 
N 6 HOH 117 2117 2117 HOH HOH A . 
N 6 HOH 118 2118 2118 HOH HOH A . 
N 6 HOH 119 2119 2119 HOH HOH A . 
N 6 HOH 120 2120 2120 HOH HOH A . 
N 6 HOH 121 2121 2121 HOH HOH A . 
N 6 HOH 122 2122 2122 HOH HOH A . 
N 6 HOH 123 2123 2123 HOH HOH A . 
N 6 HOH 124 2124 2124 HOH HOH A . 
N 6 HOH 125 2125 2125 HOH HOH A . 
N 6 HOH 126 2126 2126 HOH HOH A . 
N 6 HOH 127 2127 2127 HOH HOH A . 
N 6 HOH 128 2128 2128 HOH HOH A . 
N 6 HOH 129 2129 2129 HOH HOH A . 
N 6 HOH 130 2130 2130 HOH HOH A . 
N 6 HOH 131 2131 2131 HOH HOH A . 
N 6 HOH 132 2132 2132 HOH HOH A . 
N 6 HOH 133 2133 2133 HOH HOH A . 
N 6 HOH 134 2134 2134 HOH HOH A . 
N 6 HOH 135 2135 2135 HOH HOH A . 
N 6 HOH 136 2136 2136 HOH HOH A . 
N 6 HOH 137 2137 2137 HOH HOH A . 
N 6 HOH 138 2138 2138 HOH HOH A . 
N 6 HOH 139 2139 2139 HOH HOH A . 
N 6 HOH 140 2140 2140 HOH HOH A . 
N 6 HOH 141 2141 2141 HOH HOH A . 
N 6 HOH 142 2142 2142 HOH HOH A . 
N 6 HOH 143 2143 2143 HOH HOH A . 
N 6 HOH 144 2144 2144 HOH HOH A . 
N 6 HOH 145 2145 2145 HOH HOH A . 
N 6 HOH 146 2146 2146 HOH HOH A . 
N 6 HOH 147 2147 2147 HOH HOH A . 
N 6 HOH 148 2148 2148 HOH HOH A . 
N 6 HOH 149 2149 2149 HOH HOH A . 
N 6 HOH 150 2150 2150 HOH HOH A . 
N 6 HOH 151 2151 2151 HOH HOH A . 
N 6 HOH 152 2152 2152 HOH HOH A . 
N 6 HOH 153 2153 2153 HOH HOH A . 
N 6 HOH 154 2154 2154 HOH HOH A . 
N 6 HOH 155 2155 2155 HOH HOH A . 
N 6 HOH 156 2156 2156 HOH HOH A . 
N 6 HOH 157 2157 2157 HOH HOH A . 
N 6 HOH 158 2158 2158 HOH HOH A . 
N 6 HOH 159 2159 2159 HOH HOH A . 
N 6 HOH 160 2160 2160 HOH HOH A . 
N 6 HOH 161 2161 2161 HOH HOH A . 
N 6 HOH 162 2162 2162 HOH HOH A . 
N 6 HOH 163 2163 2163 HOH HOH A . 
N 6 HOH 164 2164 2164 HOH HOH A . 
N 6 HOH 165 2165 2165 HOH HOH A . 
N 6 HOH 166 2166 2166 HOH HOH A . 
N 6 HOH 167 2167 2167 HOH HOH A . 
N 6 HOH 168 2168 2168 HOH HOH A . 
N 6 HOH 169 2169 2169 HOH HOH A . 
N 6 HOH 170 2170 2170 HOH HOH A . 
N 6 HOH 171 2171 2171 HOH HOH A . 
N 6 HOH 172 2172 2172 HOH HOH A . 
N 6 HOH 173 2173 2173 HOH HOH A . 
N 6 HOH 174 2174 2174 HOH HOH A . 
N 6 HOH 175 2175 2175 HOH HOH A . 
N 6 HOH 176 2176 2176 HOH HOH A . 
N 6 HOH 177 2177 2177 HOH HOH A . 
N 6 HOH 178 2178 2178 HOH HOH A . 
N 6 HOH 179 2179 2179 HOH HOH A . 
N 6 HOH 180 2180 2180 HOH HOH A . 
N 6 HOH 181 2181 2181 HOH HOH A . 
N 6 HOH 182 2182 2182 HOH HOH A . 
N 6 HOH 183 2183 2183 HOH HOH A . 
N 6 HOH 184 2184 2184 HOH HOH A . 
N 6 HOH 185 2185 2185 HOH HOH A . 
N 6 HOH 186 2186 2186 HOH HOH A . 
N 6 HOH 187 2187 2187 HOH HOH A . 
N 6 HOH 188 2188 2188 HOH HOH A . 
N 6 HOH 189 2189 2189 HOH HOH A . 
N 6 HOH 190 2190 2190 HOH HOH A . 
N 6 HOH 191 2191 2191 HOH HOH A . 
N 6 HOH 192 2192 2192 HOH HOH A . 
N 6 HOH 193 2193 2193 HOH HOH A . 
N 6 HOH 194 2194 2194 HOH HOH A . 
N 6 HOH 195 2195 2195 HOH HOH A . 
N 6 HOH 196 2196 2196 HOH HOH A . 
N 6 HOH 197 2197 2197 HOH HOH A . 
O 6 HOH 1   2001 2001 HOH HOH F . 
O 6 HOH 2   2002 2002 HOH HOH F . 
O 6 HOH 3   2003 2003 HOH HOH F . 
O 6 HOH 4   2004 2004 HOH HOH F . 
O 6 HOH 5   2005 2005 HOH HOH F . 
O 6 HOH 6   2006 2006 HOH HOH F . 
O 6 HOH 7   2007 2007 HOH HOH F . 
O 6 HOH 8   2008 2008 HOH HOH F . 
O 6 HOH 9   2009 2009 HOH HOH F . 
O 6 HOH 10  2010 2010 HOH HOH F . 
O 6 HOH 11  2011 2011 HOH HOH F . 
O 6 HOH 12  2012 2012 HOH HOH F . 
O 6 HOH 13  2013 2013 HOH HOH F . 
O 6 HOH 14  2014 2014 HOH HOH F . 
O 6 HOH 15  2015 2015 HOH HOH F . 
O 6 HOH 16  2016 2016 HOH HOH F . 
O 6 HOH 17  2017 2017 HOH HOH F . 
O 6 HOH 18  2018 2018 HOH HOH F . 
O 6 HOH 19  2019 2019 HOH HOH F . 
O 6 HOH 20  2020 2020 HOH HOH F . 
O 6 HOH 21  2021 2021 HOH HOH F . 
O 6 HOH 22  2022 2022 HOH HOH F . 
O 6 HOH 23  2023 2023 HOH HOH F . 
O 6 HOH 24  2024 2024 HOH HOH F . 
O 6 HOH 25  2025 2025 HOH HOH F . 
O 6 HOH 26  2026 2026 HOH HOH F . 
O 6 HOH 27  2027 2027 HOH HOH F . 
O 6 HOH 28  2028 2028 HOH HOH F . 
O 6 HOH 29  2029 2029 HOH HOH F . 
O 6 HOH 30  2030 2030 HOH HOH F . 
O 6 HOH 31  2031 2031 HOH HOH F . 
O 6 HOH 32  2032 2032 HOH HOH F . 
O 6 HOH 33  2033 2033 HOH HOH F . 
O 6 HOH 34  2034 2034 HOH HOH F . 
O 6 HOH 35  2035 2035 HOH HOH F . 
O 6 HOH 36  2036 2036 HOH HOH F . 
O 6 HOH 37  2037 2037 HOH HOH F . 
O 6 HOH 38  2038 2038 HOH HOH F . 
O 6 HOH 39  2039 2039 HOH HOH F . 
O 6 HOH 40  2040 2040 HOH HOH F . 
O 6 HOH 41  2041 2041 HOH HOH F . 
O 6 HOH 42  2042 2042 HOH HOH F . 
O 6 HOH 43  2043 2043 HOH HOH F . 
O 6 HOH 44  2044 2044 HOH HOH F . 
O 6 HOH 45  2045 2045 HOH HOH F . 
O 6 HOH 46  2046 2046 HOH HOH F . 
O 6 HOH 47  2047 2047 HOH HOH F . 
O 6 HOH 48  2048 2048 HOH HOH F . 
O 6 HOH 49  2049 2049 HOH HOH F . 
O 6 HOH 50  2050 2050 HOH HOH F . 
O 6 HOH 51  2051 2051 HOH HOH F . 
O 6 HOH 52  2052 2052 HOH HOH F . 
O 6 HOH 53  2053 2053 HOH HOH F . 
O 6 HOH 54  2054 2054 HOH HOH F . 
O 6 HOH 55  2055 2055 HOH HOH F . 
O 6 HOH 56  2056 2056 HOH HOH F . 
O 6 HOH 57  2057 2057 HOH HOH F . 
O 6 HOH 58  2058 2058 HOH HOH F . 
O 6 HOH 59  2059 2059 HOH HOH F . 
O 6 HOH 60  2060 2060 HOH HOH F . 
O 6 HOH 61  2061 2061 HOH HOH F . 
O 6 HOH 62  2062 2062 HOH HOH F . 
O 6 HOH 63  2063 2063 HOH HOH F . 
O 6 HOH 64  2064 2064 HOH HOH F . 
O 6 HOH 65  2065 2065 HOH HOH F . 
O 6 HOH 66  2066 2066 HOH HOH F . 
O 6 HOH 67  2067 2067 HOH HOH F . 
O 6 HOH 68  2068 2068 HOH HOH F . 
O 6 HOH 69  2069 2069 HOH HOH F . 
O 6 HOH 70  2070 2070 HOH HOH F . 
O 6 HOH 71  2071 2071 HOH HOH F . 
O 6 HOH 72  2072 2072 HOH HOH F . 
O 6 HOH 73  2073 2073 HOH HOH F . 
O 6 HOH 74  2074 2074 HOH HOH F . 
O 6 HOH 75  2075 2075 HOH HOH F . 
O 6 HOH 76  2076 2076 HOH HOH F . 
O 6 HOH 77  2077 2077 HOH HOH F . 
O 6 HOH 78  2078 2078 HOH HOH F . 
O 6 HOH 79  2079 2079 HOH HOH F . 
O 6 HOH 80  2080 2080 HOH HOH F . 
O 6 HOH 81  2081 2081 HOH HOH F . 
O 6 HOH 82  2082 2082 HOH HOH F . 
O 6 HOH 83  2083 2083 HOH HOH F . 
O 6 HOH 84  2084 2084 HOH HOH F . 
O 6 HOH 85  2085 2085 HOH HOH F . 
O 6 HOH 86  2086 2086 HOH HOH F . 
O 6 HOH 87  2087 2087 HOH HOH F . 
O 6 HOH 88  2088 2088 HOH HOH F . 
O 6 HOH 89  2089 2089 HOH HOH F . 
O 6 HOH 90  2090 2090 HOH HOH F . 
O 6 HOH 91  2091 2091 HOH HOH F . 
O 6 HOH 92  2092 2092 HOH HOH F . 
O 6 HOH 93  2093 2093 HOH HOH F . 
O 6 HOH 94  2094 2094 HOH HOH F . 
O 6 HOH 95  2095 2095 HOH HOH F . 
O 6 HOH 96  2096 2096 HOH HOH F . 
O 6 HOH 97  2097 2097 HOH HOH F . 
O 6 HOH 98  2098 2098 HOH HOH F . 
O 6 HOH 99  2099 2099 HOH HOH F . 
O 6 HOH 100 2100 2100 HOH HOH F . 
O 6 HOH 101 2101 2101 HOH HOH F . 
O 6 HOH 102 2102 2102 HOH HOH F . 
O 6 HOH 103 2103 2103 HOH HOH F . 
O 6 HOH 104 2104 2104 HOH HOH F . 
O 6 HOH 105 2105 2105 HOH HOH F . 
O 6 HOH 106 2106 2106 HOH HOH F . 
O 6 HOH 107 2107 2107 HOH HOH F . 
O 6 HOH 108 2108 2108 HOH HOH F . 
O 6 HOH 109 2109 2109 HOH HOH F . 
O 6 HOH 110 2110 2110 HOH HOH F . 
O 6 HOH 111 2111 2111 HOH HOH F . 
O 6 HOH 112 2112 2112 HOH HOH F . 
O 6 HOH 113 2113 2113 HOH HOH F . 
O 6 HOH 114 2114 2114 HOH HOH F . 
O 6 HOH 115 2115 2115 HOH HOH F . 
O 6 HOH 116 2116 2116 HOH HOH F . 
O 6 HOH 117 2117 2117 HOH HOH F . 
O 6 HOH 118 2118 2118 HOH HOH F . 
O 6 HOH 119 2119 2119 HOH HOH F . 
O 6 HOH 120 2120 2120 HOH HOH F . 
O 6 HOH 121 2121 2121 HOH HOH F . 
O 6 HOH 122 2122 2122 HOH HOH F . 
O 6 HOH 123 2123 2123 HOH HOH F . 
O 6 HOH 124 2124 2124 HOH HOH F . 
O 6 HOH 125 2125 2125 HOH HOH F . 
O 6 HOH 126 2126 2126 HOH HOH F . 
O 6 HOH 127 2127 2127 HOH HOH F . 
O 6 HOH 128 2128 2128 HOH HOH F . 
O 6 HOH 129 2129 2129 HOH HOH F . 
O 6 HOH 130 2130 2130 HOH HOH F . 
O 6 HOH 131 2131 2131 HOH HOH F . 
O 6 HOH 132 2132 2132 HOH HOH F . 
O 6 HOH 133 2133 2133 HOH HOH F . 
O 6 HOH 134 2134 2134 HOH HOH F . 
O 6 HOH 135 2135 2135 HOH HOH F . 
O 6 HOH 136 2136 2136 HOH HOH F . 
O 6 HOH 137 2137 2137 HOH HOH F . 
O 6 HOH 138 2138 2138 HOH HOH F . 
O 6 HOH 139 2139 2139 HOH HOH F . 
O 6 HOH 140 2140 2140 HOH HOH F . 
O 6 HOH 141 2141 2141 HOH HOH F . 
O 6 HOH 142 2142 2142 HOH HOH F . 
O 6 HOH 143 2143 2143 HOH HOH F . 
O 6 HOH 144 2144 2144 HOH HOH F . 
O 6 HOH 145 2145 2145 HOH HOH F . 
O 6 HOH 146 2146 2146 HOH HOH F . 
O 6 HOH 147 2147 2147 HOH HOH F . 
O 6 HOH 148 2148 2148 HOH HOH F . 
O 6 HOH 149 2149 2149 HOH HOH F . 
O 6 HOH 150 2150 2150 HOH HOH F . 
O 6 HOH 151 2151 2151 HOH HOH F . 
O 6 HOH 152 2152 2152 HOH HOH F . 
O 6 HOH 153 2153 2153 HOH HOH F . 
O 6 HOH 154 2154 2154 HOH HOH F . 
O 6 HOH 155 2155 2155 HOH HOH F . 
O 6 HOH 156 2156 2156 HOH HOH F . 
O 6 HOH 157 2157 2157 HOH HOH F . 
O 6 HOH 158 2158 2158 HOH HOH F . 
O 6 HOH 159 2159 2159 HOH HOH F . 
O 6 HOH 160 2160 2160 HOH HOH F . 
O 6 HOH 161 2161 2161 HOH HOH F . 
O 6 HOH 162 2162 2162 HOH HOH F . 
O 6 HOH 163 2163 2163 HOH HOH F . 
O 6 HOH 164 2164 2164 HOH HOH F . 
O 6 HOH 165 2165 2165 HOH HOH F . 
O 6 HOH 166 2166 2166 HOH HOH F . 
O 6 HOH 167 2167 2167 HOH HOH F . 
O 6 HOH 168 2168 2168 HOH HOH F . 
O 6 HOH 169 2169 2169 HOH HOH F . 
O 6 HOH 170 2170 2170 HOH HOH F . 
O 6 HOH 171 2171 2171 HOH HOH F . 
O 6 HOH 172 2172 2172 HOH HOH F . 
O 6 HOH 173 2173 2173 HOH HOH F . 
O 6 HOH 174 2174 2174 HOH HOH F . 
O 6 HOH 175 2175 2175 HOH HOH F . 
O 6 HOH 176 2176 2176 HOH HOH F . 
O 6 HOH 177 2177 2177 HOH HOH F . 
O 6 HOH 178 2178 2178 HOH HOH F . 
O 6 HOH 179 2179 2179 HOH HOH F . 
O 6 HOH 180 2180 2180 HOH HOH F . 
O 6 HOH 181 2181 2181 HOH HOH F . 
O 6 HOH 182 2182 2182 HOH HOH F . 
O 6 HOH 183 2183 2183 HOH HOH F . 
O 6 HOH 184 2184 2184 HOH HOH F . 
O 6 HOH 185 2185 2185 HOH HOH F . 
O 6 HOH 186 2186 2186 HOH HOH F . 
O 6 HOH 187 2187 2187 HOH HOH F . 
O 6 HOH 188 2188 2188 HOH HOH F . 
O 6 HOH 189 2189 2189 HOH HOH F . 
O 6 HOH 190 2190 2190 HOH HOH F . 
O 6 HOH 191 2191 2191 HOH HOH F . 
O 6 HOH 192 2192 2192 HOH HOH F . 
# 
_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 
# 
_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  O1  ? C SO4 .   ? A SO4 1154 ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 NE2 ? A HIS 48  ? A HIS 48   ? 1_555 112.2 ? 
2  O1  ? C SO4 .   ? A SO4 1154 ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 NE2 ? A HIS 120 ? A HIS 120  ? 1_555 104.5 ? 
3  NE2 ? A HIS 48  ? A HIS 48   ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 NE2 ? A HIS 120 ? A HIS 120  ? 1_555 124.0 ? 
4  O1  ? C SO4 .   ? A SO4 1154 ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 O   ? N HOH .   ? A HOH 2193 ? 1_555 9.5   ? 
5  NE2 ? A HIS 48  ? A HIS 48   ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 O   ? N HOH .   ? A HOH 2193 ? 1_555 102.8 ? 
6  NE2 ? A HIS 120 ? A HIS 120  ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 O   ? N HOH .   ? A HOH 2193 ? 1_555 109.8 ? 
7  O1  ? C SO4 .   ? A SO4 1154 ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 105.8 ? 
8  NE2 ? A HIS 48  ? A HIS 48   ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 113.2 ? 
9  NE2 ? A HIS 120 ? A HIS 120  ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 94.8  ? 
10 O   ? N HOH .   ? A HOH 2193 ? 1_555 ZN ? G ZN . ? A ZN 1159 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 112.4 ? 
11 NE2 ? A HIS 48  ? A HIS 48   ? 1_555 CU ? E CU . ? A CU 1157 ? 1_555 NE2 ? A HIS 120 ? A HIS 120  ? 1_555 112.5 ? 
12 NE2 ? A HIS 48  ? A HIS 48   ? 1_555 CU ? E CU . ? A CU 1157 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 136.1 ? 
13 NE2 ? A HIS 120 ? A HIS 120  ? 1_555 CU ? E CU . ? A CU 1157 ? 1_555 ND1 ? A HIS 46  ? A HIS 46   ? 1_555 98.3  ? 
14 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 63  ? A HIS 63   ? 1_555 104.5 ? 
15 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 119.8 ? 
16 ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 109.3 ? 
17 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 99.5  ? 
18 ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 106.3 ? 
19 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 ZN ? F ZN . ? A ZN 1158 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 116.0 ? 
20 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 111.2 ? 
21 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 123.3 ? 
22 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 95.5  ? 
23 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O1  ? H SO4 .   ? F SO4 1154 ? 1_555 112.6 ? 
24 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O1  ? H SO4 .   ? F SO4 1154 ? 1_555 111.0 ? 
25 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O1  ? H SO4 .   ? F SO4 1154 ? 1_555 101.7 ? 
26 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O   ? O HOH .   ? F HOH 2190 ? 1_555 111.1 ? 
27 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O   ? O HOH .   ? F HOH 2190 ? 1_555 109.0 ? 
28 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O   ? O HOH .   ? F HOH 2190 ? 1_555 105.2 ? 
29 O1  ? H SO4 .   ? F SO4 1154 ? 1_555 ZN ? I ZN . ? F ZN 1155 ? 1_555 O   ? O HOH .   ? F HOH 2190 ? 1_555 3.7   ? 
30 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 CU ? J CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 101.6 ? 
31 NE2 ? B HIS 120 ? F HIS 120  ? 1_555 CU ? J CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 123.9 ? 
32 ND1 ? B HIS 46  ? F HIS 46   ? 1_555 CU ? J CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48   ? 1_555 133.6 ? 
33 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 115.3 ? 
34 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 121.9 ? 
35 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 99.1  ? 
36 ND1 ? B HIS 80  ? F HIS 80   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 108.3 ? 
37 OD1 ? B ASP 83  ? F ASP 83   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 105.5 ? 
38 ND1 ? B HIS 71  ? F HIS 71   ? 1_555 ZN ? K ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63   ? 1_555 105.2 ? 
# 
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 2005-12-16 
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_entry_details.entry_id             2C9U 
_pdbx_entry_details.compound_details     
;ELIMINATES RADICALS WHICH ARE PRODUCED BY CELLS
 AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS.
;
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     ? 
# 
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 OE1 A GLU 49   ? B O A HOH 2061 ? ? 1.67 
2  1 OE2 A GLU 40   ? ? O A HOH 2049 ? ? 1.71 
3  1 O4  F SO4 1154 ? ? O F HOH 2186 ? ? 1.72 
4  1 OE1 F GLU 133  ? ? O F HOH 2168 ? ? 1.76 
5  1 O   F GLU 77   ? ? O F HOH 2109 ? ? 1.80 
6  1 O   A HOH 2183 ? ? O A HOH 2184 ? ? 1.83 
7  1 O   F GLY 10   ? ? O F HOH 2011 ? ? 1.85 
8  1 O   A HOH 2005 ? ? O A HOH 2013 ? ? 1.91 
9  1 N   F GLY 12   ? ? O F HOH 2011 ? ? 1.95 
10 1 O   F GLY 10   ? ? O F HOH 2012 ? ? 1.96 
11 1 ND2 A ASN 53   ? B O A HOH 2070 ? ? 2.00 
12 1 O   A HOH 2064 ? ? O F HOH 2010 ? ? 2.02 
13 1 OE1 A GLU 24   ? ? O A HOH 2026 ? ? 2.05 
14 1 O   A HOH 2157 ? ? O A HOH 2158 ? ? 2.07 
15 1 OD2 A ASP 52   ? ? O A HOH 2064 ? ? 2.09 
16 1 O   F HOH 2120 ? ? O F HOH 2129 ? ? 2.10 
17 1 O   A HOH 2084 ? ? O F HOH 2184 ? ? 2.12 
18 1 O   F HOH 2122 ? ? O F HOH 2129 ? ? 2.16 
19 1 O   A HOH 2100 ? ? O A HOH 2114 ? ? 2.17 
20 1 O   F HOH 2089 ? ? O F HOH 2177 ? ? 2.17 
21 1 O   F HOH 2186 ? ? O F HOH 2188 ? ? 2.17 
22 1 C   F ASP 11   ? ? O F HOH 2011 ? ? 2.18 
23 1 O   A HOH 2066 ? ? O F HOH 2184 ? ? 2.19 
24 1 O   F HOH 2173 ? ? O F HOH 2187 ? ? 2.19 
# 
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   A HOH 2110 ? ? 1_555 O F HOH 2067 ? ? 2_746 1.96 
2 1 O   A HOH 2058 ? ? 1_555 O F HOH 2124 ? ? 2_645 2.08 
3 1 ND2 F ASN 26   ? ? 1_555 O F HOH 2012 ? ? 1_655 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 ASN 53 ? ? CG  A ASN 53 ? B 1.664 1.506 0.158  0.023 N 
2 1 CA A SER 59 ? ? CB  A SER 59 ? ? 1.624 1.525 0.099  0.015 N 
3 1 CG F GLU 49 ? ? CD  F GLU 49 ? ? 1.409 1.515 -0.106 0.015 N 
4 1 CA F SER 59 ? ? CB  F SER 59 ? ? 1.630 1.525 0.105  0.015 N 
5 1 CD F GLU 78 ? ? OE1 F GLU 78 ? ? 1.327 1.252 0.075  0.011 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 NE A ARG 115 ? ? CZ A ARG 115 ? ? NH1 A ARG 115 ? ? 123.31 120.30 3.01  0.50 N 
2 1 CA F CYS 57  ? ? CB F CYS 57  ? ? SG  F CYS 57  ? B 126.62 114.20 12.42 1.10 N 
3 1 CA F CYS 146 ? ? CB F CYS 146 ? ? SG  F CYS 146 ? B 130.81 114.20 16.61 1.10 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     26 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             54.04 
_pdbx_validate_torsion.psi             14.33 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASP 11  ? OD1 ? A ASP 11  OD1 
2 1 Y 1 A ASP 11  ? OD2 ? A ASP 11  OD2 
3 1 Y 1 A SER 25  ? OG  ? A SER 25  OG  
4 1 Y 1 F GLN 153 ? O   ? B GLN 153 O   
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'     SO4 
3 'COPPER (II) ION' CU  
4 'ZINC ION'        ZN  
5 'ACETATE ION'     ACT 
6 water             HOH 
# 
