data_2ZKW
# 
_entry.id   2ZKW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   2ZKW         pdb_00002zkw 10.2210/pdb2zkw/pdb 
RCSB  RCSB028100   ?            ?                   
WWPDB D_1000028100 ?            ?                   
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2012-04-04 
_pdbx_database_PDB_obs_spr.pdb_id           2ZKW 
_pdbx_database_PDB_obs_spr.replace_pdb_id   2YQV 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB      2ZKX           'human Cu-Zn superoxide dismutase mutant G85R in space group I212121' unspecified 
PDB      2ZKY           'human Cu-Zn superoxide dismutase mutant G93A'                        unspecified 
TargetDB ar_001000134.2 .                                                                     unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2ZKW 
_pdbx_database_status.recvd_initial_deposition_date   2008-03-31 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Yoshikawa, S.'                                          1  
'Kukimoto-Niino, M.'                                     2  
'Ito, K.'                                                3  
'Chen, L.'                                               4  
'Fu, Z.Q.'                                               5  
'Chrzas, J.'                                             6  
'Wang, B.C.'                                             7  
'Shirouzu, M.'                                           8  
'Urushitani, M.'                                         9  
'Takahashi, R.'                                          10 
'Yokoyama, S.'                                           11 
'RIKEN Structural Genomics/Proteomics Initiative (RSGI)' 12 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of human Cu-Zn superoxide dismutase mutant G85R in space group P21' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yoshikawa, S.'      1  ? 
primary 'Kukimoto-Niino, M.' 2  ? 
primary 'Ito, K.'            3  ? 
primary 'Chen, L.'           4  ? 
primary 'Fu, Z.Q.'           5  ? 
primary 'Chrzas, J.'         6  ? 
primary 'Wang, B.C.'         7  ? 
primary 'Shirouzu, M.'       8  ? 
primary 'Urushitani, M.'     9  ? 
primary 'Takahashi, R.'      10 ? 
primary 'Yokoyama, S.'       11 ? 
# 
_cell.entry_id           2ZKW 
_cell.length_a           48.616 
_cell.length_b           46.233 
_cell.length_c           52.818 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.42 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2ZKW 
_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 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]' 16470.348 2  1.15.1.1 G85R ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    2  ?        ?    ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    2  ?        ?    ? ? 
4 water       nat water                          18.015    46 ?        ?    ? ? 
# 
_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       
;GPLGSMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGP
KDEERHVGDLRNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGP
KDEERHVGDLRNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ar_001000134.2 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   ALA n 
1 8   THR n 
1 9   LYS n 
1 10  ALA n 
1 11  VAL n 
1 12  CYS n 
1 13  VAL n 
1 14  LEU n 
1 15  LYS n 
1 16  GLY n 
1 17  ASP n 
1 18  GLY n 
1 19  PRO n 
1 20  VAL n 
1 21  GLN n 
1 22  GLY n 
1 23  ILE n 
1 24  ILE n 
1 25  ASN n 
1 26  PHE n 
1 27  GLU n 
1 28  GLN n 
1 29  LYS n 
1 30  GLU n 
1 31  SER n 
1 32  ASN n 
1 33  GLY n 
1 34  PRO n 
1 35  VAL n 
1 36  LYS n 
1 37  VAL n 
1 38  TRP n 
1 39  GLY n 
1 40  SER n 
1 41  ILE n 
1 42  LYS n 
1 43  GLY n 
1 44  LEU n 
1 45  THR n 
1 46  GLU n 
1 47  GLY n 
1 48  LEU n 
1 49  HIS n 
1 50  GLY n 
1 51  PHE n 
1 52  HIS n 
1 53  VAL n 
1 54  HIS n 
1 55  GLU n 
1 56  PHE n 
1 57  GLY n 
1 58  ASP n 
1 59  ASN n 
1 60  THR n 
1 61  ALA n 
1 62  GLY n 
1 63  CYS n 
1 64  THR n 
1 65  SER n 
1 66  ALA n 
1 67  GLY n 
1 68  PRO n 
1 69  HIS n 
1 70  PHE n 
1 71  ASN n 
1 72  PRO n 
1 73  LEU n 
1 74  SER n 
1 75  ARG n 
1 76  LYS n 
1 77  HIS n 
1 78  GLY n 
1 79  GLY n 
1 80  PRO n 
1 81  LYS n 
1 82  ASP n 
1 83  GLU n 
1 84  GLU n 
1 85  ARG n 
1 86  HIS n 
1 87  VAL n 
1 88  GLY n 
1 89  ASP n 
1 90  LEU n 
1 91  ARG n 
1 92  ASN n 
1 93  VAL n 
1 94  THR n 
1 95  ALA n 
1 96  ASP n 
1 97  LYS n 
1 98  ASP n 
1 99  GLY n 
1 100 VAL n 
1 101 ALA n 
1 102 ASP n 
1 103 VAL n 
1 104 SER n 
1 105 ILE n 
1 106 GLU n 
1 107 ASP n 
1 108 SER n 
1 109 VAL n 
1 110 ILE n 
1 111 SER n 
1 112 LEU n 
1 113 SER n 
1 114 GLY n 
1 115 ASP n 
1 116 HIS n 
1 117 CYS n 
1 118 ILE n 
1 119 ILE n 
1 120 GLY n 
1 121 ARG n 
1 122 THR n 
1 123 LEU n 
1 124 VAL n 
1 125 VAL n 
1 126 HIS n 
1 127 GLU n 
1 128 LYS n 
1 129 ALA n 
1 130 ASP n 
1 131 ASP n 
1 132 LEU n 
1 133 GLY n 
1 134 LYS n 
1 135 GLY n 
1 136 GLY n 
1 137 ASN n 
1 138 GLU n 
1 139 GLU n 
1 140 SER n 
1 141 THR n 
1 142 LYS n 
1 143 THR n 
1 144 GLY n 
1 145 ASN n 
1 146 ALA n 
1 147 GLY n 
1 148 SER n 
1 149 ARG n 
1 150 LEU n 
1 151 ALA n 
1 152 CYS n 
1 153 GLY n 
1 154 VAL n 
1 155 ILE n 
1 156 GLY n 
1 157 ILE n 
1 158 ALA n 
1 159 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                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX6P 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2ZKW A 6 ? 159 ? P00441 1 ? 154 ? 0 153 
2 1 2ZKW B 6 ? 159 ? P00441 1 ? 154 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2ZKW GLY A 1  ? UNP P00441 ?   ?  'expression tag'      -5 1  
1 2ZKW PRO A 2  ? UNP P00441 ?   ?  'expression tag'      -4 2  
1 2ZKW LEU A 3  ? UNP P00441 ?   ?  'expression tag'      -3 3  
1 2ZKW GLY A 4  ? UNP P00441 ?   ?  'expression tag'      -2 4  
1 2ZKW SER A 5  ? UNP P00441 ?   ?  'expression tag'      -1 5  
1 2ZKW ARG A 91 ? UNP P00441 GLY 86 'engineered mutation' 85 6  
2 2ZKW GLY B 1  ? UNP P00441 ?   ?  'expression tag'      -5 7  
2 2ZKW PRO B 2  ? UNP P00441 ?   ?  'expression tag'      -4 8  
2 2ZKW LEU B 3  ? UNP P00441 ?   ?  'expression tag'      -3 9  
2 2ZKW GLY B 4  ? UNP P00441 ?   ?  'expression tag'      -2 10 
2 2ZKW SER B 5  ? UNP P00441 ?   ?  'expression tag'      -1 11 
2 2ZKW ARG B 91 ? UNP P00441 GLY 86 'engineered mutation' 85 12 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ? 'C4 H7 N O4'     133.103 
CU1 non-polymer         . 'COPPER (I) ION' ? 'Cu 1'           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 
MET 'L-peptide linking' y METHIONINE       ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'       ? 'Zn 2'           65.409  
# 
_exptl.entry_id          2ZKW 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.796609 
_exptl_crystal.density_percent_sol   31.537685 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.2 
_exptl_crystal_grow.pdbx_details    
'0.2M Ammonium iodide, 20%(w/v) PEG3350, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_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   2007-01-31 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 22-BM' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   22-BM 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.979 
# 
_reflns.entry_id                     2ZKW 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            1.90 
_reflns.number_obs                   17839 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         97.0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.104 
_reflns.pdbx_netI_over_sigmaI        10.367 
_reflns.B_iso_Wilson_estimate        17.4 
_reflns.pdbx_redundancy              3.583 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.90 
_reflns_shell.d_res_low              1.97 
_reflns_shell.percent_possible_all   92.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.264 
_reflns_shell.meanI_over_sigI_obs    4.25 
_reflns_shell.pdbx_redundancy        3.0 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      1680 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2ZKW 
_refine.ls_number_reflns_obs                     17328 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               185773.23 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             33.46 
_refine.ls_d_res_high                            1.90 
_refine.ls_percent_reflns_obs                    93.1 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.193 
_refine.ls_R_factor_R_free                       0.252 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  1707 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               36.1 
_refine.aniso_B[1][1]                            10.66 
_refine.aniso_B[2][2]                            -1.89 
_refine.aniso_B[3][3]                            -8.76 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            6.01 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.417534 
_refine.solvent_model_param_bsol                 54.2519 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1HL5' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2ZKW 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_refine_analyze.Luzzati_sigma_a_obs             0.13 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.28 
_refine_analyze.Luzzati_sigma_a_free            0.16 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2151 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             46 
_refine_hist.number_atoms_total               2201 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        33.46 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.010 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.6   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.4  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.94  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             4.44  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            5.49  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             6.83  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            8.76  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.90 
_refine_ls_shell.d_res_low                        2.02 
_refine_ls_shell.number_reflns_R_work             2226 
_refine_ls_shell.R_factor_R_work                  0.224 
_refine_ls_shell.percent_reflns_obs               79.9 
_refine_ls_shell.R_factor_R_free                  0.294 
_refine_ls_shell.R_factor_R_free_error            0.019 
_refine_ls_shell.percent_reflns_R_free            9.8 
_refine_ls_shell.number_reflns_R_free             242 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                2468 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 
2 ion.param         water.top   'X-RAY DIFFRACTION' 
3 water_rep.param   ion.top     'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2ZKW 
_struct.title                     'Crystal structure of human Cu-Zn superoxide dismutase mutant G85R in space group P21' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2ZKW 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;oxidoreductase, human Cu-Zn superoxide dismutase, ALS, FALS, metal-binding, disease mutation, E.C.1.15.1.1, Amyotrophic lateral sclerosis, Antioxidant, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI
;
# 
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 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 61  ? GLY A 67  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 GLU A 138 ? LYS A 142 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 3 CYS B 63  ? GLY B 67  ? CYS B 57  GLY B 61  5 ? 5 
HELX_P HELX_P4 4 SER B 113 ? CYS B 117 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P5 5 GLU B 138 ? LYS B 142 ? GLU B 132 LYS B 136 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 63  SG  ? ? ? 1_555 A CYS 152 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
disulf2  disulf ? ? B CYS 63  SG  ? ? ? 1_555 B CYS 152 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc1  metalc ? ? A HIS 52  ND1 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 46  A CU1 301 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc2  metalc ? ? A HIS 54  NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 48  A CU1 301 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc3  metalc ? ? A HIS 69  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  401 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc4  metalc ? ? A HIS 77  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  401 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc5  metalc ? ? A HIS 86  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  401 1_555 ? ? ? ? ? ? ? 1.929 ? ? 
metalc6  metalc ? ? A ASP 89  OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  401 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc7  metalc ? ? A ASP 89  OD2 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  401 1_555 ? ? ? ? ? ? ? 2.689 ? ? 
metalc8  metalc ? ? A HIS 126 NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 120 A CU1 301 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc9  metalc ? ? B HIS 52  ND1 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 46  B CU1 302 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc10 metalc ? ? B HIS 54  NE2 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 48  B CU1 302 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc11 metalc ? ? B HIS 69  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 63  B ZN  402 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc12 metalc ? ? B HIS 77  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 71  B ZN  402 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc13 metalc ? ? B HIS 86  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 80  B ZN  402 1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc14 metalc ? ? B ASP 89  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  402 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc15 metalc ? ? B HIS 126 NE2 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 120 B CU1 302 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 3 ? 
D ? 5 ? 
E ? 2 ? 
F ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 101 ? ASP A 107 ? ALA A 95  ASP A 101 
A 2 VAL A 35  ? LYS A 42  ? VAL A 29  LYS A 36  
A 3 GLN A 21  ? GLU A 27  ? GLN A 15  GLU A 21  
A 4 LYS A 9   ? LYS A 15  ? LYS A 3   LYS A 9   
A 5 GLY A 156 ? ILE A 157 ? GLY A 150 ILE A 151 
B 1 GLY A 47  ? HIS A 49  ? GLY A 41  HIS A 43  
B 2 VAL A 93  ? ALA A 95  ? VAL A 87  ALA A 89  
C 1 PHE A 51  ? HIS A 54  ? PHE A 45  HIS A 48  
C 2 THR A 122 ? HIS A 126 ? THR A 116 HIS A 120 
C 3 ARG A 149 ? VAL A 154 ? ARG A 143 VAL A 148 
D 1 ALA B 101 ? ASP B 107 ? ALA B 95  ASP B 101 
D 2 VAL B 35  ? LYS B 42  ? VAL B 29  LYS B 36  
D 3 GLN B 21  ? GLN B 28  ? GLN B 15  GLN B 22  
D 4 THR B 8   ? LYS B 15  ? THR B 2   LYS B 9   
D 5 GLY B 156 ? ILE B 157 ? GLY B 150 ILE B 151 
E 1 GLY B 47  ? HIS B 49  ? GLY B 41  HIS B 43  
E 2 VAL B 93  ? ALA B 95  ? VAL B 87  ALA B 89  
F 1 PHE B 51  ? HIS B 54  ? PHE B 45  HIS B 48  
F 2 THR B 122 ? HIS B 126 ? THR B 116 HIS B 120 
F 3 ARG B 149 ? VAL B 154 ? ARG B 143 VAL B 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 
A 1 2 O ILE A 105 ? O ILE A 99  N VAL A 37  ? N VAL A 31  
A 2 3 O TRP A 38  ? O TRP A 32  N ASN A 25  ? N ASN A 19  
A 3 4 O PHE A 26  ? O PHE A 20  N ALA A 10  ? N ALA A 4   
A 4 5 N VAL A 11  ? N VAL A 5   O GLY A 156 ? O GLY A 150 
B 1 2 N HIS A 49  ? N HIS A 43  O VAL A 93  ? O VAL A 87  
C 1 2 N HIS A 54  ? N HIS A 48  O THR A 122 ? O THR A 116 
C 2 3 N LEU A 123 ? N LEU A 117 O GLY A 153 ? O GLY A 147 
D 1 2 O VAL B 103 ? O VAL B 97  N GLY B 39  ? N GLY B 33  
D 2 3 O TRP B 38  ? O TRP B 32  N ASN B 25  ? N ASN B 19  
D 3 4 O PHE B 26  ? O PHE B 20  N ALA B 10  ? N ALA B 4   
D 4 5 N VAL B 11  ? N VAL B 5   O GLY B 156 ? O GLY B 150 
E 1 2 N HIS B 49  ? N HIS B 43  O VAL B 93  ? O VAL B 87  
F 1 2 N HIS B 54  ? N HIS B 48  O THR B 122 ? O THR B 116 
F 2 3 N LEU B 123 ? N LEU B 117 O GLY B 153 ? O GLY B 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A CU1 301 ? 4 'BINDING SITE FOR RESIDUE CU1 A 301' 
AC2 Software B CU1 302 ? 4 'BINDING SITE FOR RESIDUE CU1 B 302' 
AC3 Software A ZN  401 ? 4 'BINDING SITE FOR RESIDUE ZN A 401'  
AC4 Software B ZN  402 ? 4 'BINDING SITE FOR RESIDUE ZN B 402'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 52  ? HIS A 46  . ? 1_555 ? 
2  AC1 4 HIS A 54  ? HIS A 48  . ? 1_555 ? 
3  AC1 4 HIS A 69  ? HIS A 63  . ? 1_555 ? 
4  AC1 4 HIS A 126 ? HIS A 120 . ? 1_555 ? 
5  AC2 4 HIS B 52  ? HIS B 46  . ? 1_555 ? 
6  AC2 4 HIS B 54  ? HIS B 48  . ? 1_555 ? 
7  AC2 4 HIS B 69  ? HIS B 63  . ? 1_555 ? 
8  AC2 4 HIS B 126 ? HIS B 120 . ? 1_555 ? 
9  AC3 4 HIS A 69  ? HIS A 63  . ? 1_555 ? 
10 AC3 4 HIS A 77  ? HIS A 71  . ? 1_555 ? 
11 AC3 4 HIS A 86  ? HIS A 80  . ? 1_555 ? 
12 AC3 4 ASP A 89  ? ASP A 83  . ? 1_555 ? 
13 AC4 4 HIS B 69  ? HIS B 63  . ? 1_555 ? 
14 AC4 4 HIS B 77  ? HIS B 71  . ? 1_555 ? 
15 AC4 4 HIS B 86  ? HIS B 80  . ? 1_555 ? 
16 AC4 4 ASP B 89  ? ASP B 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2ZKW 
_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                    2ZKW 
_atom_sites.fract_transf_matrix[1][1]   0.020569 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001588 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021630 
_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]   0.018989 
_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   . THR A 1 8   ? -5.202  -5.727  26.072 1.00 46.78 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 8   ? -4.157  -5.442  27.102 1.00 47.78 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 8   ? -3.362  -4.212  26.669 1.00 42.79 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 8   ? -3.050  -4.054  25.489 1.00 41.51 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 8   ? -3.222  -6.655  27.295 1.00 52.97 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 8   ? -2.124  -6.291  28.145 1.00 61.40 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 8   ? -2.695  -7.131  25.972 1.00 59.57 ? 2   THR A CG2 1 
ATOM   8    N  N   . LYS A 1 9   ? -3.048  -3.343  27.629 1.00 35.40 ? 3   LYS A N   1 
ATOM   9    C  CA  . LYS A 1 9   ? -2.345  -2.080  27.375 1.00 40.70 ? 3   LYS A CA  1 
ATOM   10   C  C   . LYS A 1 9   ? -1.097  -1.853  28.226 1.00 39.93 ? 3   LYS A C   1 
ATOM   11   O  O   . LYS A 1 9   ? -1.072  -2.195  29.397 1.00 32.28 ? 3   LYS A O   1 
ATOM   12   C  CB  . LYS A 1 9   ? -3.306  -0.922  27.632 1.00 33.20 ? 3   LYS A CB  1 
ATOM   13   C  CG  . LYS A 1 9   ? -4.738  -1.227  27.220 1.00 53.61 ? 3   LYS A CG  1 
ATOM   14   C  CD  . LYS A 1 9   ? -5.652  -0.042  27.485 1.00 62.82 ? 3   LYS A CD  1 
ATOM   15   C  CE  . LYS A 1 9   ? -7.107  -0.345  27.101 1.00 69.32 ? 3   LYS A CE  1 
ATOM   16   N  NZ  . LYS A 1 9   ? -7.316  -0.509  25.629 1.00 68.17 ? 3   LYS A NZ  1 
ATOM   17   N  N   . ALA A 1 10  ? -0.077  -1.234  27.645 1.00 34.56 ? 4   ALA A N   1 
ATOM   18   C  CA  . ALA A 1 10  ? 1.142   -0.961  28.399 1.00 33.23 ? 4   ALA A CA  1 
ATOM   19   C  C   . ALA A 1 10  ? 1.605   0.431   28.040 1.00 32.54 ? 4   ALA A C   1 
ATOM   20   O  O   . ALA A 1 10  ? 1.267   0.951   26.972 1.00 32.36 ? 4   ALA A O   1 
ATOM   21   C  CB  . ALA A 1 10  ? 2.270   -2.025  28.059 1.00 28.22 ? 4   ALA A CB  1 
ATOM   22   N  N   . VAL A 1 11  ? 2.395   1.028   28.924 1.00 32.97 ? 5   VAL A N   1 
ATOM   23   C  CA  . VAL A 1 11  ? 2.907   2.360   28.709 1.00 24.41 ? 5   VAL A CA  1 
ATOM   24   C  C   . VAL A 1 11  ? 4.385   2.459   29.119 1.00 33.79 ? 5   VAL A C   1 
ATOM   25   O  O   . VAL A 1 11  ? 4.866   1.691   29.951 1.00 30.36 ? 5   VAL A O   1 
ATOM   26   C  CB  . VAL A 1 11  ? 2.084   3.400   29.502 1.00 31.01 ? 5   VAL A CB  1 
ATOM   27   C  CG1 . VAL A 1 11  ? 2.293   3.202   30.998 1.00 41.63 ? 5   VAL A CG1 1 
ATOM   28   C  CG2 . VAL A 1 11  ? 2.483   4.814   29.086 1.00 31.77 ? 5   VAL A CG2 1 
ATOM   29   N  N   . CYS A 1 12  ? 5.101   3.406   28.524 1.00 29.34 ? 6   CYS A N   1 
ATOM   30   C  CA  . CYS A 1 12  ? 6.514   3.593   28.841 1.00 27.76 ? 6   CYS A CA  1 
ATOM   31   C  C   . CYS A 1 12  ? 6.832   5.074   28.786 1.00 32.30 ? 6   CYS A C   1 
ATOM   32   O  O   . CYS A 1 12  ? 6.481   5.753   27.831 1.00 31.59 ? 6   CYS A O   1 
ATOM   33   C  CB  . CYS A 1 12  ? 7.367   2.833   27.827 1.00 35.35 ? 6   CYS A CB  1 
ATOM   34   S  SG  . CYS A 1 12  ? 9.152   2.932   28.103 1.00 34.41 ? 6   CYS A SG  1 
ATOM   35   N  N   . VAL A 1 13  ? 7.484   5.575   29.826 1.00 32.39 ? 7   VAL A N   1 
ATOM   36   C  CA  . VAL A 1 13  ? 7.857   6.972   29.900 1.00 31.07 ? 7   VAL A CA  1 
ATOM   37   C  C   . VAL A 1 13  ? 9.349   6.961   29.679 1.00 33.89 ? 7   VAL A C   1 
ATOM   38   O  O   . VAL A 1 13  ? 10.103  6.363   30.456 1.00 30.73 ? 7   VAL A O   1 
ATOM   39   C  CB  . VAL A 1 13  ? 7.545   7.575   31.297 1.00 35.20 ? 7   VAL A CB  1 
ATOM   40   C  CG1 . VAL A 1 13  ? 8.092   8.999   31.402 1.00 37.84 ? 7   VAL A CG1 1 
ATOM   41   C  CG2 . VAL A 1 13  ? 6.033   7.550   31.545 1.00 43.69 ? 7   VAL A CG2 1 
ATOM   42   N  N   . LEU A 1 14  ? 9.758   7.606   28.600 1.00 28.21 ? 8   LEU A N   1 
ATOM   43   C  CA  . LEU A 1 14  ? 11.151  7.673   28.222 1.00 31.62 ? 8   LEU A CA  1 
ATOM   44   C  C   . LEU A 1 14  ? 11.823  8.921   28.787 1.00 34.22 ? 8   LEU A C   1 
ATOM   45   O  O   . LEU A 1 14  ? 11.323  10.050  28.657 1.00 31.31 ? 8   LEU A O   1 
ATOM   46   C  CB  . LEU A 1 14  ? 11.259  7.688   26.701 1.00 29.55 ? 8   LEU A CB  1 
ATOM   47   C  CG  . LEU A 1 14  ? 10.674  6.511   25.930 1.00 33.78 ? 8   LEU A CG  1 
ATOM   48   C  CD1 . LEU A 1 14  ? 10.787  6.786   24.433 1.00 46.81 ? 8   LEU A CD1 1 
ATOM   49   C  CD2 . LEU A 1 14  ? 11.438  5.239   26.279 1.00 42.27 ? 8   LEU A CD2 1 
ATOM   50   N  N   . LYS A 1 15  ? 12.951  8.713   29.439 1.00 33.08 ? 9   LYS A N   1 
ATOM   51   C  CA  . LYS A 1 15  ? 13.703  9.839   29.971 1.00 33.26 ? 9   LYS A CA  1 
ATOM   52   C  C   . LYS A 1 15  ? 15.174  9.533   29.907 1.00 34.73 ? 9   LYS A C   1 
ATOM   53   O  O   . LYS A 1 15  ? 15.563  8.361   29.881 1.00 25.11 ? 9   LYS A O   1 
ATOM   54   C  CB  . LYS A 1 15  ? 13.274  10.176  31.402 1.00 37.81 ? 9   LYS A CB  1 
ATOM   55   C  CG  . LYS A 1 15  ? 11.973  10.983  31.409 1.00 53.24 ? 9   LYS A CG  1 
ATOM   56   C  CD  . LYS A 1 15  ? 11.737  11.761  32.686 1.00 54.80 ? 9   LYS A CD  1 
ATOM   57   C  CE  . LYS A 1 15  ? 10.403  12.500  32.595 1.00 56.62 ? 9   LYS A CE  1 
ATOM   58   N  NZ  . LYS A 1 15  ? 10.168  13.374  33.776 1.00 62.98 ? 9   LYS A NZ  1 
ATOM   59   N  N   . GLY A 1 16  ? 15.982  10.592  29.886 1.00 31.42 ? 10  GLY A N   1 
ATOM   60   C  CA  . GLY A 1 16  ? 17.429  10.433  29.810 1.00 39.34 ? 10  GLY A CA  1 
ATOM   61   C  C   . GLY A 1 16  ? 18.124  11.555  30.550 1.00 39.45 ? 10  GLY A C   1 
ATOM   62   O  O   . GLY A 1 16  ? 17.533  12.163  31.444 1.00 36.07 ? 10  GLY A O   1 
ATOM   63   N  N   . ASP A 1 17  ? 19.373  11.836  30.182 1.00 43.89 ? 11  ASP A N   1 
ATOM   64   C  CA  . ASP A 1 17  ? 20.153  12.887  30.838 1.00 41.69 ? 11  ASP A CA  1 
ATOM   65   C  C   . ASP A 1 17  ? 19.846  14.237  30.236 1.00 45.21 ? 11  ASP A C   1 
ATOM   66   O  O   . ASP A 1 17  ? 20.144  15.276  30.840 1.00 41.75 ? 11  ASP A O   1 
ATOM   67   C  CB  . ASP A 1 17  ? 21.658  12.666  30.646 1.00 53.90 ? 11  ASP A CB  1 
ATOM   68   C  CG  . ASP A 1 17  ? 22.155  11.384  31.256 1.00 55.89 ? 11  ASP A CG  1 
ATOM   69   O  OD1 . ASP A 1 17  ? 21.755  11.074  32.400 1.00 65.99 ? 11  ASP A OD1 1 
ATOM   70   O  OD2 . ASP A 1 17  ? 22.965  10.700  30.595 1.00 59.42 ? 11  ASP A OD2 1 
ATOM   71   N  N   . GLY A 1 18  ? 19.281  14.213  29.031 1.00 38.62 ? 12  GLY A N   1 
ATOM   72   C  CA  . GLY A 1 18  ? 19.012  15.451  28.325 1.00 47.76 ? 12  GLY A CA  1 
ATOM   73   C  C   . GLY A 1 18  ? 17.572  15.824  28.045 1.00 49.06 ? 12  GLY A C   1 
ATOM   74   O  O   . GLY A 1 18  ? 16.647  15.365  28.722 1.00 40.93 ? 12  GLY A O   1 
ATOM   75   N  N   . PRO A 1 19  ? 17.360  16.659  27.017 1.00 46.97 ? 13  PRO A N   1 
ATOM   76   C  CA  . PRO A 1 19  ? 16.041  17.139  26.600 1.00 48.05 ? 13  PRO A CA  1 
ATOM   77   C  C   . PRO A 1 19  ? 15.105  16.065  26.056 1.00 44.07 ? 13  PRO A C   1 
ATOM   78   O  O   . PRO A 1 19  ? 13.914  16.319  25.869 1.00 39.51 ? 13  PRO A O   1 
ATOM   79   C  CB  . PRO A 1 19  ? 16.384  18.180  25.541 1.00 51.27 ? 13  PRO A CB  1 
ATOM   80   C  CG  . PRO A 1 19  ? 17.574  17.553  24.868 1.00 50.97 ? 13  PRO A CG  1 
ATOM   81   C  CD  . PRO A 1 19  ? 18.396  17.080  26.052 1.00 52.12 ? 13  PRO A CD  1 
ATOM   82   N  N   . VAL A 1 20  ? 15.628  14.868  25.803 1.00 41.74 ? 14  VAL A N   1 
ATOM   83   C  CA  . VAL A 1 20  ? 14.788  13.818  25.237 1.00 37.90 ? 14  VAL A CA  1 
ATOM   84   C  C   . VAL A 1 20  ? 13.861  13.138  26.240 1.00 36.94 ? 14  VAL A C   1 
ATOM   85   O  O   . VAL A 1 20  ? 14.290  12.538  27.232 1.00 35.49 ? 14  VAL A O   1 
ATOM   86   C  CB  . VAL A 1 20  ? 15.638  12.731  24.522 1.00 42.20 ? 14  VAL A CB  1 
ATOM   87   C  CG1 . VAL A 1 20  ? 14.727  11.773  23.761 1.00 32.40 ? 14  VAL A CG1 1 
ATOM   88   C  CG2 . VAL A 1 20  ? 16.629  13.385  23.574 1.00 42.45 ? 14  VAL A CG2 1 
ATOM   89   N  N   . GLN A 1 21  ? 12.569  13.238  25.968 1.00 37.94 ? 15  GLN A N   1 
ATOM   90   C  CA  . GLN A 1 21  ? 11.580  12.610  26.815 1.00 36.75 ? 15  GLN A CA  1 
ATOM   91   C  C   . GLN A 1 21  ? 10.344  12.353  26.001 1.00 41.06 ? 15  GLN A C   1 
ATOM   92   O  O   . GLN A 1 21  ? 10.049  13.087  25.062 1.00 38.69 ? 15  GLN A O   1 
ATOM   93   C  CB  . GLN A 1 21  ? 11.255  13.485  28.019 1.00 40.86 ? 15  GLN A CB  1 
ATOM   94   C  CG  . GLN A 1 21  ? 10.838  14.882  27.687 1.00 54.98 ? 15  GLN A CG  1 
ATOM   95   C  CD  . GLN A 1 21  ? 10.756  15.744  28.933 1.00 64.11 ? 15  GLN A CD  1 
ATOM   96   O  OE1 . GLN A 1 21  ? 9.962   15.474  29.839 1.00 57.53 ? 15  GLN A OE1 1 
ATOM   97   N  NE2 . GLN A 1 21  ? 11.590  16.783  28.992 1.00 68.11 ? 15  GLN A NE2 1 
ATOM   98   N  N   . GLY A 1 22  ? 9.642   11.283  26.347 1.00 38.34 ? 16  GLY A N   1 
ATOM   99   C  CA  . GLY A 1 22  ? 8.439   10.954  25.628 1.00 38.99 ? 16  GLY A CA  1 
ATOM   100  C  C   . GLY A 1 22  ? 7.598   9.940   26.358 1.00 37.68 ? 16  GLY A C   1 
ATOM   101  O  O   . GLY A 1 22  ? 7.902   9.532   27.475 1.00 35.31 ? 16  GLY A O   1 
ATOM   102  N  N   . ILE A 1 23  ? 6.519   9.539   25.703 1.00 36.29 ? 17  ILE A N   1 
ATOM   103  C  CA  . ILE A 1 23  ? 5.600   8.565   26.243 1.00 41.50 ? 17  ILE A CA  1 
ATOM   104  C  C   . ILE A 1 23  ? 5.198   7.685   25.067 1.00 31.93 ? 17  ILE A C   1 
ATOM   105  O  O   . ILE A 1 23  ? 4.823   8.183   24.012 1.00 35.45 ? 17  ILE A O   1 
ATOM   106  C  CB  . ILE A 1 23  ? 4.331   9.244   26.849 1.00 46.49 ? 17  ILE A CB  1 
ATOM   107  C  CG1 . ILE A 1 23  ? 4.667   9.945   28.174 1.00 53.61 ? 17  ILE A CG1 1 
ATOM   108  C  CG2 . ILE A 1 23  ? 3.253   8.199   27.084 1.00 41.35 ? 17  ILE A CG2 1 
ATOM   109  C  CD1 . ILE A 1 23  ? 5.435   11.245  28.041 1.00 57.14 ? 17  ILE A CD1 1 
ATOM   110  N  N   . ILE A 1 24  ? 5.312   6.379   25.246 1.00 24.43 ? 18  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 24  ? 4.947   5.424   24.206 1.00 24.59 ? 18  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 24  ? 3.931   4.465   24.814 1.00 32.29 ? 18  ILE A C   1 
ATOM   113  O  O   . ILE A 1 24  ? 4.164   3.915   25.900 1.00 31.47 ? 18  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 24  ? 6.167   4.569   23.740 1.00 34.44 ? 18  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 24  ? 7.301   5.466   23.226 1.00 21.67 ? 18  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 24  ? 5.730   3.596   22.661 1.00 26.71 ? 18  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 24  ? 6.934   6.329   22.014 1.00 33.89 ? 18  ILE A CD1 1 
ATOM   118  N  N   . ASN A 1 25  ? 2.815   4.274   24.113 1.00 29.49 ? 19  ASN A N   1 
ATOM   119  C  CA  . ASN A 1 25  ? 1.750   3.371   24.535 1.00 26.54 ? 19  ASN A CA  1 
ATOM   120  C  C   . ASN A 1 25  ? 1.806   2.132   23.660 1.00 26.26 ? 19  ASN A C   1 
ATOM   121  O  O   . ASN A 1 25  ? 2.179   2.211   22.481 1.00 29.92 ? 19  ASN A O   1 
ATOM   122  C  CB  . ASN A 1 25  ? 0.374   4.037   24.338 1.00 33.07 ? 19  ASN A CB  1 
ATOM   123  C  CG  . ASN A 1 25  ? 0.280   5.378   25.010 1.00 32.28 ? 19  ASN A CG  1 
ATOM   124  O  OD1 . ASN A 1 25  ? 0.003   5.471   26.198 1.00 42.28 ? 19  ASN A OD1 1 
ATOM   125  N  ND2 . ASN A 1 25  ? 0.529   6.431   24.254 1.00 41.09 ? 19  ASN A ND2 1 
ATOM   126  N  N   . PHE A 1 26  ? 1.409   1.001   24.239 1.00 34.69 ? 20  PHE A N   1 
ATOM   127  C  CA  . PHE A 1 26  ? 1.380   -0.274  23.557 1.00 34.54 ? 20  PHE A CA  1 
ATOM   128  C  C   . PHE A 1 26  ? -0.016  -0.803  23.779 1.00 31.66 ? 20  PHE A C   1 
ATOM   129  O  O   . PHE A 1 26  ? -0.529  -0.728  24.904 1.00 38.04 ? 20  PHE A O   1 
ATOM   130  C  CB  . PHE A 1 26  ? 2.363   -1.266  24.174 1.00 28.29 ? 20  PHE A CB  1 
ATOM   131  C  CG  . PHE A 1 26  ? 3.788   -0.844  24.096 1.00 30.27 ? 20  PHE A CG  1 
ATOM   132  C  CD1 . PHE A 1 26  ? 4.281   0.122   24.951 1.00 34.13 ? 20  PHE A CD1 1 
ATOM   133  C  CD2 . PHE A 1 26  ? 4.643   -1.437  23.182 1.00 28.94 ? 20  PHE A CD2 1 
ATOM   134  C  CE1 . PHE A 1 26  ? 5.616   0.490   24.900 1.00 35.57 ? 20  PHE A CE1 1 
ATOM   135  C  CE2 . PHE A 1 26  ? 5.970   -1.077  23.120 1.00 28.44 ? 20  PHE A CE2 1 
ATOM   136  C  CZ  . PHE A 1 26  ? 6.455   -0.112  23.981 1.00 27.42 ? 20  PHE A CZ  1 
ATOM   137  N  N   . GLU A 1 27  ? -0.619  -1.340  22.719 1.00 32.63 ? 21  GLU A N   1 
ATOM   138  C  CA  . GLU A 1 27  ? -1.976  -1.885  22.789 1.00 36.74 ? 21  GLU A CA  1 
ATOM   139  C  C   . GLU A 1 27  ? -2.091  -3.104  21.893 1.00 38.27 ? 21  GLU A C   1 
ATOM   140  O  O   . GLU A 1 27  ? -1.783  -3.039  20.703 1.00 38.01 ? 21  GLU A O   1 
ATOM   141  C  CB  . GLU A 1 27  ? -2.983  -0.810  22.362 1.00 47.36 ? 21  GLU A CB  1 
ATOM   142  C  CG  . GLU A 1 27  ? -4.420  -1.290  22.182 1.00 61.69 ? 21  GLU A CG  1 
ATOM   143  C  CD  . GLU A 1 27  ? -5.423  -0.137  22.110 1.00 69.05 ? 21  GLU A CD  1 
ATOM   144  O  OE1 . GLU A 1 27  ? -5.697  0.486   23.164 1.00 65.83 ? 21  GLU A OE1 1 
ATOM   145  O  OE2 . GLU A 1 27  ? -5.930  0.148   21.000 1.00 69.22 ? 21  GLU A OE2 1 
ATOM   146  N  N   . GLN A 1 28  ? -2.547  -4.211  22.472 1.00 43.49 ? 22  GLN A N   1 
ATOM   147  C  CA  . GLN A 1 28  ? -2.673  -5.479  21.761 1.00 50.23 ? 22  GLN A CA  1 
ATOM   148  C  C   . GLN A 1 28  ? -4.072  -6.058  21.969 1.00 57.33 ? 22  GLN A C   1 
ATOM   149  O  O   . GLN A 1 28  ? -4.616  -6.004  23.071 1.00 62.78 ? 22  GLN A O   1 
ATOM   150  C  CB  . GLN A 1 28  ? -1.601  -6.457  22.283 1.00 45.78 ? 22  GLN A CB  1 
ATOM   151  C  CG  . GLN A 1 28  ? -1.597  -7.852  21.665 1.00 44.30 ? 22  GLN A CG  1 
ATOM   152  C  CD  . GLN A 1 28  ? -0.495  -8.750  22.234 1.00 51.75 ? 22  GLN A CD  1 
ATOM   153  O  OE1 . GLN A 1 28  ? -0.132  -8.646  23.409 1.00 50.11 ? 22  GLN A OE1 1 
ATOM   154  N  NE2 . GLN A 1 28  ? 0.024   -9.650  21.406 1.00 42.41 ? 22  GLN A NE2 1 
ATOM   155  N  N   . SER A 1 31  ? -3.229  -11.405 22.268 1.00 81.29 ? 25  SER A N   1 
ATOM   156  C  CA  . SER A 1 31  ? -3.103  -12.709 21.627 1.00 81.36 ? 25  SER A CA  1 
ATOM   157  C  C   . SER A 1 31  ? -1.842  -12.748 20.780 1.00 82.34 ? 25  SER A C   1 
ATOM   158  O  O   . SER A 1 31  ? -0.748  -12.454 21.258 1.00 83.72 ? 25  SER A O   1 
ATOM   159  C  CB  . SER A 1 31  ? -4.324  -12.981 20.744 1.00 82.52 ? 25  SER A CB  1 
ATOM   160  O  OG  . SER A 1 31  ? -4.230  -14.252 20.127 1.00 80.61 ? 25  SER A OG  1 
ATOM   161  N  N   . ASN A 1 32  ? -1.992  -13.140 19.523 1.00 82.95 ? 26  ASN A N   1 
ATOM   162  C  CA  . ASN A 1 32  ? -0.866  -13.182 18.607 1.00 82.38 ? 26  ASN A CA  1 
ATOM   163  C  C   . ASN A 1 32  ? -1.141  -12.043 17.645 1.00 80.83 ? 26  ASN A C   1 
ATOM   164  O  O   . ASN A 1 32  ? -0.454  -11.862 16.635 1.00 80.94 ? 26  ASN A O   1 
ATOM   165  C  CB  . ASN A 1 32  ? -0.812  -14.527 17.878 1.00 84.31 ? 26  ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 32  ? -0.518  -15.682 18.819 1.00 88.85 ? 26  ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 32  ? 0.429   -15.624 19.603 1.00 93.45 ? 26  ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 32  ? -1.322  -16.740 18.742 1.00 88.46 ? 26  ASN A ND2 1 
ATOM   169  N  N   . GLY A 1 33  ? -2.174  -11.277 17.989 1.00 77.02 ? 27  GLY A N   1 
ATOM   170  C  CA  . GLY A 1 33  ? -2.560  -10.135 17.189 1.00 71.86 ? 27  GLY A CA  1 
ATOM   171  C  C   . GLY A 1 33  ? -1.461  -9.099  17.268 1.00 64.81 ? 27  GLY A C   1 
ATOM   172  O  O   . GLY A 1 33  ? -0.696  -9.063  18.233 1.00 61.84 ? 27  GLY A O   1 
ATOM   173  N  N   . PRO A 1 34  ? -1.369  -8.221  16.274 1.00 58.11 ? 28  PRO A N   1 
ATOM   174  C  CA  . PRO A 1 34  ? -0.312  -7.214  16.318 1.00 58.09 ? 28  PRO A CA  1 
ATOM   175  C  C   . PRO A 1 34  ? -0.375  -6.301  17.545 1.00 54.18 ? 28  PRO A C   1 
ATOM   176  O  O   . PRO A 1 34  ? -1.414  -6.161  18.194 1.00 50.42 ? 28  PRO A O   1 
ATOM   177  C  CB  . PRO A 1 34  ? -0.526  -6.454  15.016 1.00 59.39 ? 28  PRO A CB  1 
ATOM   178  C  CG  . PRO A 1 34  ? -2.022  -6.456  14.900 1.00 57.69 ? 28  PRO A CG  1 
ATOM   179  C  CD  . PRO A 1 34  ? -2.380  -7.886  15.257 1.00 54.14 ? 28  PRO A CD  1 
ATOM   180  N  N   . VAL A 1 35  ? 0.758   -5.704  17.881 1.00 47.05 ? 29  VAL A N   1 
ATOM   181  C  CA  . VAL A 1 35  ? 0.804   -4.774  18.993 1.00 38.28 ? 29  VAL A CA  1 
ATOM   182  C  C   . VAL A 1 35  ? 0.925   -3.391  18.374 1.00 35.27 ? 29  VAL A C   1 
ATOM   183  O  O   . VAL A 1 35  ? 1.813   -3.138  17.559 1.00 36.73 ? 29  VAL A O   1 
ATOM   184  C  CB  . VAL A 1 35  ? 2.024   -5.004  19.899 1.00 38.48 ? 29  VAL A CB  1 
ATOM   185  C  CG1 . VAL A 1 35  ? 2.088   -3.907  20.949 1.00 44.30 ? 29  VAL A CG1 1 
ATOM   186  C  CG2 . VAL A 1 35  ? 1.939   -6.342  20.552 1.00 38.91 ? 29  VAL A CG2 1 
ATOM   187  N  N   . LYS A 1 36  ? 0.006   -2.508  18.715 1.00 27.37 ? 30  LYS A N   1 
ATOM   188  C  CA  . LYS A 1 36  ? 0.076   -1.153  18.207 1.00 39.41 ? 30  LYS A CA  1 
ATOM   189  C  C   . LYS A 1 36  ? 0.937   -0.323  19.172 1.00 38.15 ? 30  LYS A C   1 
ATOM   190  O  O   . LYS A 1 36  ? 0.706   -0.328  20.382 1.00 36.03 ? 30  LYS A O   1 
ATOM   191  C  CB  . LYS A 1 36  ? -1.330  -0.566  18.093 1.00 45.66 ? 30  LYS A CB  1 
ATOM   192  C  CG  . LYS A 1 36  ? -2.196  -1.298  17.058 1.00 50.73 ? 30  LYS A CG  1 
ATOM   193  C  CD  . LYS A 1 36  ? -3.462  -1.876  17.698 1.00 64.92 ? 30  LYS A CD  1 
ATOM   194  C  CE  . LYS A 1 36  ? -4.385  -2.524  16.664 1.00 65.79 ? 30  LYS A CE  1 
ATOM   195  N  NZ  . LYS A 1 36  ? -5.736  -2.828  17.246 1.00 55.93 ? 30  LYS A NZ  1 
ATOM   196  N  N   . VAL A 1 37  ? 1.923   0.382   18.627 1.00 32.88 ? 31  VAL A N   1 
ATOM   197  C  CA  . VAL A 1 37  ? 2.811   1.201   19.440 1.00 37.97 ? 31  VAL A CA  1 
ATOM   198  C  C   . VAL A 1 37  ? 2.712   2.636   18.961 1.00 41.88 ? 31  VAL A C   1 
ATOM   199  O  O   . VAL A 1 37  ? 2.895   2.932   17.773 1.00 37.41 ? 31  VAL A O   1 
ATOM   200  C  CB  . VAL A 1 37  ? 4.281   0.685   19.335 1.00 39.81 ? 31  VAL A CB  1 
ATOM   201  C  CG1 . VAL A 1 37  ? 5.196   1.478   20.232 1.00 29.37 ? 31  VAL A CG1 1 
ATOM   202  C  CG2 . VAL A 1 37  ? 4.337   -0.794  19.716 1.00 31.17 ? 31  VAL A CG2 1 
ATOM   203  N  N   . TRP A 1 38  ? 2.397   3.541   19.880 1.00 38.13 ? 32  TRP A N   1 
ATOM   204  C  CA  . TRP A 1 38  ? 2.274   4.932   19.491 1.00 37.50 ? 32  TRP A CA  1 
ATOM   205  C  C   . TRP A 1 38  ? 2.517   5.918   20.617 1.00 36.37 ? 32  TRP A C   1 
ATOM   206  O  O   . TRP A 1 38  ? 2.354   5.617   21.807 1.00 36.42 ? 32  TRP A O   1 
ATOM   207  C  CB  . TRP A 1 38  ? 0.884   5.179   18.877 1.00 45.96 ? 32  TRP A CB  1 
ATOM   208  C  CG  . TRP A 1 38  ? -0.187  5.398   19.880 1.00 39.47 ? 32  TRP A CG  1 
ATOM   209  C  CD1 . TRP A 1 38  ? -0.633  6.603   20.348 1.00 41.77 ? 32  TRP A CD1 1 
ATOM   210  C  CD2 . TRP A 1 38  ? -0.911  4.395   20.598 1.00 44.77 ? 32  TRP A CD2 1 
ATOM   211  N  NE1 . TRP A 1 38  ? -1.582  6.411   21.309 1.00 45.04 ? 32  TRP A NE1 1 
ATOM   212  C  CE2 . TRP A 1 38  ? -1.777  5.066   21.487 1.00 42.89 ? 32  TRP A CE2 1 
ATOM   213  C  CE3 . TRP A 1 38  ? -0.911  2.996   20.580 1.00 36.30 ? 32  TRP A CE3 1 
ATOM   214  C  CZ2 . TRP A 1 38  ? -2.640  4.387   22.354 1.00 35.91 ? 32  TRP A CZ2 1 
ATOM   215  C  CZ3 . TRP A 1 38  ? -1.769  2.322   21.443 1.00 40.91 ? 32  TRP A CZ3 1 
ATOM   216  C  CH2 . TRP A 1 38  ? -2.622  3.019   22.318 1.00 39.43 ? 32  TRP A CH2 1 
ATOM   217  N  N   . GLY A 1 39  ? 2.896   7.119   20.226 1.00 32.50 ? 33  GLY A N   1 
ATOM   218  C  CA  . GLY A 1 39  ? 3.157   8.132   21.212 1.00 34.52 ? 33  GLY A CA  1 
ATOM   219  C  C   . GLY A 1 39  ? 3.998   9.193   20.579 1.00 29.04 ? 33  GLY A C   1 
ATOM   220  O  O   . GLY A 1 39  ? 4.029   9.304   19.352 1.00 40.23 ? 33  GLY A O   1 
ATOM   221  N  N   . SER A 1 40  ? 4.687   9.976   21.399 1.00 28.39 ? 34  SER A N   1 
ATOM   222  C  CA  . SER A 1 40  ? 5.521   11.043  20.871 1.00 33.69 ? 34  SER A CA  1 
ATOM   223  C  C   . SER A 1 40  ? 6.794   11.157  21.711 1.00 36.61 ? 34  SER A C   1 
ATOM   224  O  O   . SER A 1 40  ? 6.787   10.845  22.900 1.00 36.47 ? 34  SER A O   1 
ATOM   225  C  CB  . SER A 1 40  ? 4.729   12.361  20.909 1.00 38.47 ? 34  SER A CB  1 
ATOM   226  O  OG  . SER A 1 40  ? 5.532   13.464  20.542 1.00 54.18 ? 34  SER A OG  1 
ATOM   227  N  N   . ILE A 1 41  ? 7.882   11.583  21.083 1.00 37.91 ? 35  ILE A N   1 
ATOM   228  C  CA  . ILE A 1 41  ? 9.154   11.771  21.780 1.00 36.33 ? 35  ILE A CA  1 
ATOM   229  C  C   . ILE A 1 41  ? 9.726   13.130  21.324 1.00 39.49 ? 35  ILE A C   1 
ATOM   230  O  O   . ILE A 1 41  ? 9.919   13.359  20.133 1.00 35.43 ? 35  ILE A O   1 
ATOM   231  C  CB  . ILE A 1 41  ? 10.150  10.627  21.446 1.00 30.96 ? 35  ILE A CB  1 
ATOM   232  C  CG1 . ILE A 1 41  ? 9.514   9.269   21.773 1.00 33.74 ? 35  ILE A CG1 1 
ATOM   233  C  CG2 . ILE A 1 41  ? 11.456  10.814  22.243 1.00 34.98 ? 35  ILE A CG2 1 
ATOM   234  C  CD1 . ILE A 1 41  ? 10.297  8.082   21.204 1.00 37.23 ? 35  ILE A CD1 1 
ATOM   235  N  N   . LYS A 1 42  ? 9.973   14.025  22.278 1.00 33.75 ? 36  LYS A N   1 
ATOM   236  C  CA  . LYS A 1 42  ? 10.489  15.358  21.989 1.00 35.08 ? 36  LYS A CA  1 
ATOM   237  C  C   . LYS A 1 42  ? 11.953  15.492  22.407 1.00 32.97 ? 36  LYS A C   1 
ATOM   238  O  O   . LYS A 1 42  ? 12.497  14.620  23.078 1.00 33.21 ? 36  LYS A O   1 
ATOM   239  C  CB  . LYS A 1 42  ? 9.655   16.413  22.727 1.00 47.47 ? 36  LYS A CB  1 
ATOM   240  C  CG  . LYS A 1 42  ? 9.948   16.507  24.225 1.00 58.22 ? 36  LYS A CG  1 
ATOM   241  C  CD  . LYS A 1 42  ? 9.016   17.493  24.933 1.00 65.67 ? 36  LYS A CD  1 
ATOM   242  C  CE  . LYS A 1 42  ? 9.286   17.550  26.443 1.00 65.17 ? 36  LYS A CE  1 
ATOM   243  N  NZ  . LYS A 1 42  ? 8.237   18.292  27.209 1.00 65.86 ? 36  LYS A NZ  1 
ATOM   244  N  N   . GLY A 1 43  ? 12.582  16.586  21.998 1.00 33.14 ? 37  GLY A N   1 
ATOM   245  C  CA  . GLY A 1 43  ? 13.974  16.818  22.350 1.00 39.16 ? 37  GLY A CA  1 
ATOM   246  C  C   . GLY A 1 43  ? 14.983  16.068  21.495 1.00 39.05 ? 37  GLY A C   1 
ATOM   247  O  O   . GLY A 1 43  ? 16.170  16.053  21.811 1.00 45.05 ? 37  GLY A O   1 
ATOM   248  N  N   . LEU A 1 44  ? 14.516  15.473  20.401 1.00 35.99 ? 38  LEU A N   1 
ATOM   249  C  CA  . LEU A 1 44  ? 15.372  14.710  19.492 1.00 35.61 ? 38  LEU A CA  1 
ATOM   250  C  C   . LEU A 1 44  ? 15.924  15.558  18.354 1.00 38.21 ? 38  LEU A C   1 
ATOM   251  O  O   . LEU A 1 44  ? 15.238  16.459  17.862 1.00 39.54 ? 38  LEU A O   1 
ATOM   252  C  CB  . LEU A 1 44  ? 14.572  13.548  18.886 1.00 28.74 ? 38  LEU A CB  1 
ATOM   253  C  CG  . LEU A 1 44  ? 14.265  12.341  19.779 1.00 32.87 ? 38  LEU A CG  1 
ATOM   254  C  CD1 . LEU A 1 44  ? 13.291  11.403  19.071 1.00 32.75 ? 38  LEU A CD1 1 
ATOM   255  C  CD2 . LEU A 1 44  ? 15.560  11.603  20.102 1.00 27.66 ? 38  LEU A CD2 1 
ATOM   256  N  N   . THR A 1 45  ? 17.153  15.276  17.923 1.00 38.52 ? 39  THR A N   1 
ATOM   257  C  CA  . THR A 1 45  ? 17.715  16.016  16.796 1.00 39.36 ? 39  THR A CA  1 
ATOM   258  C  C   . THR A 1 45  ? 16.912  15.564  15.587 1.00 36.63 ? 39  THR A C   1 
ATOM   259  O  O   . THR A 1 45  ? 16.479  14.413  15.531 1.00 40.28 ? 39  THR A O   1 
ATOM   260  C  CB  . THR A 1 45  ? 19.209  15.686  16.551 1.00 44.83 ? 39  THR A CB  1 
ATOM   261  O  OG1 . THR A 1 45  ? 19.359  14.283  16.340 1.00 41.65 ? 39  THR A OG1 1 
ATOM   262  C  CG2 . THR A 1 45  ? 20.057  16.106  17.739 1.00 42.46 ? 39  THR A CG2 1 
ATOM   263  N  N   . GLU A 1 46  ? 16.680  16.460  14.629 1.00 40.88 ? 40  GLU A N   1 
ATOM   264  C  CA  . GLU A 1 46  ? 15.911  16.095  13.431 1.00 48.66 ? 40  GLU A CA  1 
ATOM   265  C  C   . GLU A 1 46  ? 16.543  14.895  12.714 1.00 47.15 ? 40  GLU A C   1 
ATOM   266  O  O   . GLU A 1 46  ? 17.769  14.794  12.607 1.00 36.66 ? 40  GLU A O   1 
ATOM   267  C  CB  . GLU A 1 46  ? 15.840  17.279  12.467 1.00 51.02 ? 40  GLU A CB  1 
ATOM   268  C  CG  . GLU A 1 46  ? 14.821  17.120  11.345 1.00 57.92 ? 40  GLU A CG  1 
ATOM   269  C  CD  . GLU A 1 46  ? 14.918  18.246  10.319 1.00 72.67 ? 40  GLU A CD  1 
ATOM   270  O  OE1 . GLU A 1 46  ? 15.371  19.351  10.699 1.00 72.01 ? 40  GLU A OE1 1 
ATOM   271  O  OE2 . GLU A 1 46  ? 14.538  18.032  9.145  1.00 68.92 ? 40  GLU A OE2 1 
ATOM   272  N  N   . GLY A 1 47  ? 15.709  13.984  12.220 1.00 41.49 ? 41  GLY A N   1 
ATOM   273  C  CA  . GLY A 1 47  ? 16.257  12.821  11.541 1.00 37.94 ? 41  GLY A CA  1 
ATOM   274  C  C   . GLY A 1 47  ? 15.935  11.508  12.231 1.00 32.05 ? 41  GLY A C   1 
ATOM   275  O  O   . GLY A 1 47  ? 15.113  11.457  13.144 1.00 31.50 ? 41  GLY A O   1 
ATOM   276  N  N   . LEU A 1 48  ? 16.604  10.439  11.807 1.00 30.08 ? 42  LEU A N   1 
ATOM   277  C  CA  . LEU A 1 48  ? 16.360  9.107   12.366 1.00 33.53 ? 42  LEU A CA  1 
ATOM   278  C  C   . LEU A 1 48  ? 17.050  8.762   13.678 1.00 32.78 ? 42  LEU A C   1 
ATOM   279  O  O   . LEU A 1 48  ? 18.166  9.185   13.938 1.00 27.59 ? 42  LEU A O   1 
ATOM   280  C  CB  . LEU A 1 48  ? 16.729  8.044   11.342 1.00 32.11 ? 42  LEU A CB  1 
ATOM   281  C  CG  . LEU A 1 48  ? 15.632  7.468   10.448 1.00 39.26 ? 42  LEU A CG  1 
ATOM   282  C  CD1 . LEU A 1 48  ? 14.345  8.295   10.440 1.00 29.84 ? 42  LEU A CD1 1 
ATOM   283  C  CD2 . LEU A 1 48  ? 16.240  7.327   9.081  1.00 44.61 ? 42  LEU A CD2 1 
ATOM   284  N  N   . HIS A 1 49  ? 16.367  7.951   14.478 1.00 29.09 ? 43  HIS A N   1 
ATOM   285  C  CA  . HIS A 1 49  ? 16.869  7.496   15.784 1.00 29.93 ? 43  HIS A CA  1 
ATOM   286  C  C   . HIS A 1 49  ? 16.480  6.031   16.036 1.00 23.80 ? 43  HIS A C   1 
ATOM   287  O  O   . HIS A 1 49  ? 15.296  5.669   15.903 1.00 25.24 ? 43  HIS A O   1 
ATOM   288  C  CB  . HIS A 1 49  ? 16.285  8.375   16.892 1.00 24.06 ? 43  HIS A CB  1 
ATOM   289  C  CG  . HIS A 1 49  ? 16.755  9.788   16.834 1.00 29.28 ? 43  HIS A CG  1 
ATOM   290  N  ND1 . HIS A 1 49  ? 18.023  10.154  17.223 1.00 30.62 ? 43  HIS A ND1 1 
ATOM   291  C  CD2 . HIS A 1 49  ? 16.182  10.901  16.315 1.00 35.43 ? 43  HIS A CD2 1 
ATOM   292  C  CE1 . HIS A 1 49  ? 18.217  11.429  16.939 1.00 35.59 ? 43  HIS A CE1 1 
ATOM   293  N  NE2 . HIS A 1 49  ? 17.116  11.907  16.387 1.00 39.13 ? 43  HIS A NE2 1 
ATOM   294  N  N   . GLY A 1 50  ? 17.483  5.211   16.383 1.00 25.89 ? 44  GLY A N   1 
ATOM   295  C  CA  . GLY A 1 50  ? 17.301  3.795   16.702 1.00 31.14 ? 44  GLY A CA  1 
ATOM   296  C  C   . GLY A 1 50  ? 16.258  3.615   17.802 1.00 27.54 ? 44  GLY A C   1 
ATOM   297  O  O   . GLY A 1 50  ? 16.190  4.418   18.725 1.00 26.21 ? 44  GLY A O   1 
ATOM   298  N  N   . PHE A 1 51  ? 15.475  2.539   17.714 1.00 24.22 ? 45  PHE A N   1 
ATOM   299  C  CA  . PHE A 1 51  ? 14.354  2.300   18.625 1.00 26.56 ? 45  PHE A CA  1 
ATOM   300  C  C   . PHE A 1 51  ? 14.135  0.794   18.816 1.00 23.52 ? 45  PHE A C   1 
ATOM   301  O  O   . PHE A 1 51  ? 13.719  0.095   17.889 1.00 29.07 ? 45  PHE A O   1 
ATOM   302  C  CB  . PHE A 1 51  ? 13.109  2.958   17.991 1.00 28.60 ? 45  PHE A CB  1 
ATOM   303  C  CG  . PHE A 1 51  ? 11.916  3.082   18.911 1.00 26.30 ? 45  PHE A CG  1 
ATOM   304  C  CD1 . PHE A 1 51  ? 12.032  3.701   20.161 1.00 31.70 ? 45  PHE A CD1 1 
ATOM   305  C  CD2 . PHE A 1 51  ? 10.641  2.750   18.448 1.00 28.94 ? 45  PHE A CD2 1 
ATOM   306  C  CE1 . PHE A 1 51  ? 10.888  4.007   20.927 1.00 32.78 ? 45  PHE A CE1 1 
ATOM   307  C  CE2 . PHE A 1 51  ? 9.490   3.058   19.204 1.00 28.62 ? 45  PHE A CE2 1 
ATOM   308  C  CZ  . PHE A 1 51  ? 9.620   3.692   20.441 1.00 29.64 ? 45  PHE A CZ  1 
ATOM   309  N  N   . HIS A 1 52  ? 14.414  0.306   20.022 1.00 27.86 ? 46  HIS A N   1 
ATOM   310  C  CA  . HIS A 1 52  ? 14.327  -1.117  20.331 1.00 27.74 ? 46  HIS A CA  1 
ATOM   311  C  C   . HIS A 1 52  ? 13.876  -1.413  21.749 1.00 23.17 ? 46  HIS A C   1 
ATOM   312  O  O   . HIS A 1 52  ? 14.044  -0.585  22.631 1.00 22.38 ? 46  HIS A O   1 
ATOM   313  C  CB  . HIS A 1 52  ? 15.708  -1.773  20.242 1.00 26.55 ? 46  HIS A CB  1 
ATOM   314  C  CG  . HIS A 1 52  ? 16.634  -1.140  19.256 1.00 16.75 ? 46  HIS A CG  1 
ATOM   315  N  ND1 . HIS A 1 52  ? 17.648  -0.283  19.623 1.00 22.36 ? 46  HIS A ND1 1 
ATOM   316  C  CD2 . HIS A 1 52  ? 16.718  -1.265  17.908 1.00 21.74 ? 46  HIS A CD2 1 
ATOM   317  C  CE1 . HIS A 1 52  ? 18.316  0.090   18.549 1.00 19.44 ? 46  HIS A CE1 1 
ATOM   318  N  NE2 . HIS A 1 52  ? 17.771  -0.490  17.495 1.00 31.56 ? 46  HIS A NE2 1 
ATOM   319  N  N   . VAL A 1 53  ? 13.345  -2.622  21.955 1.00 22.33 ? 47  VAL A N   1 
ATOM   320  C  CA  . VAL A 1 53  ? 13.001  -3.079  23.286 1.00 26.37 ? 47  VAL A CA  1 
ATOM   321  C  C   . VAL A 1 53  ? 14.278  -3.850  23.678 1.00 21.96 ? 47  VAL A C   1 
ATOM   322  O  O   . VAL A 1 53  ? 14.748  -4.706  22.939 1.00 24.32 ? 47  VAL A O   1 
ATOM   323  C  CB  . VAL A 1 53  ? 11.782  -4.046  23.284 1.00 23.87 ? 47  VAL A CB  1 
ATOM   324  C  CG1 . VAL A 1 53  ? 11.602  -4.656  24.669 1.00 20.72 ? 47  VAL A CG1 1 
ATOM   325  C  CG2 . VAL A 1 53  ? 10.516  -3.251  22.921 1.00 30.93 ? 47  VAL A CG2 1 
ATOM   326  N  N   . HIS A 1 54  ? 14.863  -3.493  24.813 1.00 25.87 ? 48  HIS A N   1 
ATOM   327  C  CA  . HIS A 1 54  ? 16.075  -4.171  25.265 1.00 29.08 ? 48  HIS A CA  1 
ATOM   328  C  C   . HIS A 1 54  ? 15.692  -5.257  26.252 1.00 32.40 ? 48  HIS A C   1 
ATOM   329  O  O   . HIS A 1 54  ? 14.570  -5.279  26.771 1.00 33.38 ? 48  HIS A O   1 
ATOM   330  C  CB  . HIS A 1 54  ? 17.084  -3.145  25.852 1.00 22.69 ? 48  HIS A CB  1 
ATOM   331  C  CG  . HIS A 1 54  ? 17.805  -2.352  24.797 1.00 29.12 ? 48  HIS A CG  1 
ATOM   332  N  ND1 . HIS A 1 54  ? 19.182  -2.343  24.676 1.00 32.49 ? 48  HIS A ND1 1 
ATOM   333  C  CD2 . HIS A 1 54  ? 17.342  -1.526  23.829 1.00 33.71 ? 48  HIS A CD2 1 
ATOM   334  C  CE1 . HIS A 1 54  ? 19.536  -1.541  23.686 1.00 28.93 ? 48  HIS A CE1 1 
ATOM   335  N  NE2 . HIS A 1 54  ? 18.439  -1.031  23.155 1.00 28.24 ? 48  HIS A NE2 1 
ATOM   336  N  N   . GLU A 1 55  ? 16.621  -6.174  26.499 1.00 30.86 ? 49  GLU A N   1 
ATOM   337  C  CA  . GLU A 1 55  ? 16.357  -7.299  27.367 1.00 27.13 ? 49  GLU A CA  1 
ATOM   338  C  C   . GLU A 1 55  ? 15.942  -7.017  28.807 1.00 34.66 ? 49  GLU A C   1 
ATOM   339  O  O   . GLU A 1 55  ? 15.012  -7.650  29.289 1.00 30.60 ? 49  GLU A O   1 
ATOM   340  C  CB  . GLU A 1 55  ? 17.563  -8.237  27.377 1.00 30.25 ? 49  GLU A CB  1 
ATOM   341  C  CG  . GLU A 1 55  ? 17.212  -9.660  27.828 1.00 46.16 ? 49  GLU A CG  1 
ATOM   342  C  CD  . GLU A 1 55  ? 18.417  -10.578 27.916 1.00 59.10 ? 49  GLU A CD  1 
ATOM   343  O  OE1 . GLU A 1 55  ? 19.245  -10.579 26.978 1.00 59.64 ? 49  GLU A OE1 1 
ATOM   344  O  OE2 . GLU A 1 55  ? 18.532  -11.309 28.924 1.00 73.45 ? 49  GLU A OE2 1 
ATOM   345  N  N   . PHE A 1 56  ? 16.623  -6.091  29.495 1.00 28.25 ? 50  PHE A N   1 
ATOM   346  C  CA  . PHE A 1 56  ? 16.321  -5.825  30.905 1.00 29.01 ? 50  PHE A CA  1 
ATOM   347  C  C   . PHE A 1 56  ? 15.605  -4.513  31.217 1.00 36.95 ? 50  PHE A C   1 
ATOM   348  O  O   . PHE A 1 56  ? 15.815  -3.511  30.544 1.00 32.36 ? 50  PHE A O   1 
ATOM   349  C  CB  . PHE A 1 56  ? 17.612  -5.873  31.715 1.00 30.42 ? 50  PHE A CB  1 
ATOM   350  C  CG  . PHE A 1 56  ? 18.396  -7.143  31.521 1.00 33.10 ? 50  PHE A CG  1 
ATOM   351  C  CD1 . PHE A 1 56  ? 17.851  -8.374  31.892 1.00 22.74 ? 50  PHE A CD1 1 
ATOM   352  C  CD2 . PHE A 1 56  ? 19.653  -7.114  30.926 1.00 37.67 ? 50  PHE A CD2 1 
ATOM   353  C  CE1 . PHE A 1 56  ? 18.547  -9.574  31.666 1.00 30.57 ? 50  PHE A CE1 1 
ATOM   354  C  CE2 . PHE A 1 56  ? 20.359  -8.306  30.697 1.00 44.05 ? 50  PHE A CE2 1 
ATOM   355  C  CZ  . PHE A 1 56  ? 19.801  -9.532  31.065 1.00 35.63 ? 50  PHE A CZ  1 
ATOM   356  N  N   . GLY A 1 57  ? 14.775  -4.539  32.266 1.00 28.64 ? 51  GLY A N   1 
ATOM   357  C  CA  . GLY A 1 57  ? 14.035  -3.364  32.679 1.00 24.24 ? 51  GLY A CA  1 
ATOM   358  C  C   . GLY A 1 57  ? 14.755  -2.823  33.891 1.00 30.29 ? 51  GLY A C   1 
ATOM   359  O  O   . GLY A 1 57  ? 14.159  -2.524  34.920 1.00 30.84 ? 51  GLY A O   1 
ATOM   360  N  N   . ASP A 1 58  ? 16.060  -2.682  33.715 1.00 32.67 ? 52  ASP A N   1 
ATOM   361  C  CA  . ASP A 1 58  ? 16.981  -2.247  34.746 1.00 33.53 ? 52  ASP A CA  1 
ATOM   362  C  C   . ASP A 1 58  ? 17.589  -0.892  34.364 1.00 33.67 ? 52  ASP A C   1 
ATOM   363  O  O   . ASP A 1 58  ? 18.397  -0.796  33.431 1.00 34.17 ? 52  ASP A O   1 
ATOM   364  C  CB  . ASP A 1 58  ? 18.068  -3.333  34.875 1.00 32.95 ? 52  ASP A CB  1 
ATOM   365  C  CG  . ASP A 1 58  ? 19.125  -2.983  35.891 1.00 44.20 ? 52  ASP A CG  1 
ATOM   366  O  OD1 . ASP A 1 58  ? 19.257  -1.782  36.178 1.00 43.39 ? 52  ASP A OD1 1 
ATOM   367  O  OD2 . ASP A 1 58  ? 19.824  -3.896  36.386 1.00 36.95 ? 52  ASP A OD2 1 
ATOM   368  N  N   . ASN A 1 59  ? 17.211  0.152   35.087 1.00 26.99 ? 53  ASN A N   1 
ATOM   369  C  CA  . ASN A 1 59  ? 17.704  1.496   34.794 1.00 34.83 ? 53  ASN A CA  1 
ATOM   370  C  C   . ASN A 1 59  ? 18.660  2.003   35.898 1.00 32.74 ? 53  ASN A C   1 
ATOM   371  O  O   . ASN A 1 59  ? 18.787  3.222   36.132 1.00 28.54 ? 53  ASN A O   1 
ATOM   372  C  CB  . ASN A 1 59  ? 16.499  2.439   34.658 1.00 36.13 ? 53  ASN A CB  1 
ATOM   373  C  CG  . ASN A 1 59  ? 16.825  3.698   33.885 1.00 62.11 ? 53  ASN A CG  1 
ATOM   374  O  OD1 . ASN A 1 59  ? 16.959  3.671   32.659 1.00 70.38 ? 53  ASN A OD1 1 
ATOM   375  N  ND2 . ASN A 1 59  ? 16.962  4.813   34.597 1.00 68.32 ? 53  ASN A ND2 1 
ATOM   376  N  N   . THR A 1 60  ? 19.338  1.076   36.566 1.00 30.60 ? 54  THR A N   1 
ATOM   377  C  CA  . THR A 1 60  ? 20.226  1.449   37.673 1.00 31.45 ? 54  THR A CA  1 
ATOM   378  C  C   . THR A 1 60  ? 21.457  2.187   37.193 1.00 30.42 ? 54  THR A C   1 
ATOM   379  O  O   . THR A 1 60  ? 22.113  2.862   37.971 1.00 34.42 ? 54  THR A O   1 
ATOM   380  C  CB  . THR A 1 60  ? 20.673  0.226   38.480 1.00 32.24 ? 54  THR A CB  1 
ATOM   381  O  OG1 . THR A 1 60  ? 21.130  -0.791  37.580 1.00 37.89 ? 54  THR A OG1 1 
ATOM   382  C  CG2 . THR A 1 60  ? 19.513  -0.328  39.316 1.00 34.40 ? 54  THR A CG2 1 
ATOM   383  N  N   . ALA A 1 61  ? 21.789  2.033   35.919 1.00 30.06 ? 55  ALA A N   1 
ATOM   384  C  CA  . ALA A 1 61  ? 22.926  2.738   35.325 1.00 30.67 ? 55  ALA A CA  1 
ATOM   385  C  C   . ALA A 1 61  ? 22.359  3.496   34.122 1.00 26.07 ? 55  ALA A C   1 
ATOM   386  O  O   . ALA A 1 61  ? 22.949  3.528   33.052 1.00 32.97 ? 55  ALA A O   1 
ATOM   387  C  CB  . ALA A 1 61  ? 23.995  1.752   34.870 1.00 31.35 ? 55  ALA A CB  1 
ATOM   388  N  N   . GLY A 1 62  ? 21.221  4.143   34.322 1.00 26.40 ? 56  GLY A N   1 
ATOM   389  C  CA  . GLY A 1 62  ? 20.612  4.850   33.212 1.00 31.74 ? 56  GLY A CA  1 
ATOM   390  C  C   . GLY A 1 62  ? 20.229  3.786   32.201 1.00 33.64 ? 56  GLY A C   1 
ATOM   391  O  O   . GLY A 1 62  ? 19.957  2.632   32.572 1.00 36.50 ? 56  GLY A O   1 
ATOM   392  N  N   . CYS A 1 63  ? 20.234  4.152   30.927 1.00 29.62 ? 57  CYS A N   1 
ATOM   393  C  CA  . CYS A 1 63  ? 19.891  3.227   29.869 1.00 34.43 ? 57  CYS A CA  1 
ATOM   394  C  C   . CYS A 1 63  ? 20.945  2.157   29.643 1.00 36.77 ? 57  CYS A C   1 
ATOM   395  O  O   . CYS A 1 63  ? 20.679  1.119   29.054 1.00 32.16 ? 57  CYS A O   1 
ATOM   396  C  CB  . CYS A 1 63  ? 19.662  4.013   28.583 1.00 37.78 ? 57  CYS A CB  1 
ATOM   397  S  SG  . CYS A 1 63  ? 18.438  5.320   28.888 1.00 38.17 ? 57  CYS A SG  1 
ATOM   398  N  N   . THR A 1 64  ? 22.144  2.409   30.132 1.00 38.17 ? 58  THR A N   1 
ATOM   399  C  CA  . THR A 1 64  ? 23.242  1.483   29.947 1.00 38.81 ? 58  THR A CA  1 
ATOM   400  C  C   . THR A 1 64  ? 23.033  0.081   30.507 1.00 31.42 ? 58  THR A C   1 
ATOM   401  O  O   . THR A 1 64  ? 23.552  -0.880  29.961 1.00 37.30 ? 58  THR A O   1 
ATOM   402  C  CB  . THR A 1 64  ? 24.527  2.090   30.529 1.00 35.38 ? 58  THR A CB  1 
ATOM   403  O  OG1 . THR A 1 64  ? 24.778  3.337   29.865 1.00 42.46 ? 58  THR A OG1 1 
ATOM   404  C  CG2 . THR A 1 64  ? 25.707  1.159   30.315 1.00 52.61 ? 58  THR A CG2 1 
ATOM   405  N  N   . SER A 1 65  ? 22.274  -0.037  31.585 1.00 31.79 ? 59  SER A N   1 
ATOM   406  C  CA  . SER A 1 65  ? 22.032  -1.343  32.199 1.00 33.61 ? 59  SER A CA  1 
ATOM   407  C  C   . SER A 1 65  ? 20.840  -2.104  31.602 1.00 27.03 ? 59  SER A C   1 
ATOM   408  O  O   . SER A 1 65  ? 20.486  -3.177  32.074 1.00 28.90 ? 59  SER A O   1 
ATOM   409  C  CB  . SER A 1 65  ? 21.853  -1.162  33.706 1.00 29.11 ? 59  SER A CB  1 
ATOM   410  O  OG  . SER A 1 65  ? 21.029  -0.031  33.973 1.00 35.98 ? 59  SER A OG  1 
ATOM   411  N  N   . ALA A 1 66  ? 20.242  -1.560  30.547 1.00 33.59 ? 60  ALA A N   1 
ATOM   412  C  CA  . ALA A 1 66  ? 19.092  -2.218  29.903 1.00 33.46 ? 60  ALA A CA  1 
ATOM   413  C  C   . ALA A 1 66  ? 19.499  -3.494  29.160 1.00 30.10 ? 60  ALA A C   1 
ATOM   414  O  O   . ALA A 1 66  ? 18.659  -4.317  28.815 1.00 34.64 ? 60  ALA A O   1 
ATOM   415  C  CB  . ALA A 1 66  ? 18.409  -1.240  28.937 1.00 33.58 ? 60  ALA A CB  1 
ATOM   416  N  N   . GLY A 1 67  ? 20.794  -3.671  28.911 1.00 27.41 ? 61  GLY A N   1 
ATOM   417  C  CA  . GLY A 1 67  ? 21.228  -4.860  28.212 1.00 28.21 ? 61  GLY A CA  1 
ATOM   418  C  C   . GLY A 1 67  ? 21.103  -4.691  26.699 1.00 23.39 ? 61  GLY A C   1 
ATOM   419  O  O   . GLY A 1 67  ? 20.808  -3.596  26.211 1.00 29.91 ? 61  GLY A O   1 
ATOM   420  N  N   . PRO A 1 68  ? 21.309  -5.758  25.930 1.00 26.17 ? 62  PRO A N   1 
ATOM   421  C  CA  . PRO A 1 68  ? 21.207  -5.674  24.471 1.00 28.35 ? 62  PRO A CA  1 
ATOM   422  C  C   . PRO A 1 68  ? 19.736  -5.712  24.043 1.00 28.63 ? 62  PRO A C   1 
ATOM   423  O  O   . PRO A 1 68  ? 18.847  -5.740  24.883 1.00 28.75 ? 62  PRO A O   1 
ATOM   424  C  CB  . PRO A 1 68  ? 21.936  -6.927  24.027 1.00 26.76 ? 62  PRO A CB  1 
ATOM   425  C  CG  . PRO A 1 68  ? 21.448  -7.910  25.018 1.00 34.67 ? 62  PRO A CG  1 
ATOM   426  C  CD  . PRO A 1 68  ? 21.594  -7.145  26.344 1.00 34.26 ? 62  PRO A CD  1 
ATOM   427  N  N   . HIS A 1 69  ? 19.484  -5.756  22.738 1.00 29.10 ? 63  HIS A N   1 
ATOM   428  C  CA  . HIS A 1 69  ? 18.103  -5.815  22.246 1.00 29.92 ? 63  HIS A CA  1 
ATOM   429  C  C   . HIS A 1 69  ? 17.419  -7.133  22.671 1.00 26.16 ? 63  HIS A C   1 
ATOM   430  O  O   . HIS A 1 69  ? 18.041  -8.192  22.675 1.00 28.11 ? 63  HIS A O   1 
ATOM   431  C  CB  . HIS A 1 69  ? 18.089  -5.712  20.718 1.00 28.71 ? 63  HIS A CB  1 
ATOM   432  C  CG  . HIS A 1 69  ? 18.855  -4.549  20.162 1.00 27.68 ? 63  HIS A CG  1 
ATOM   433  N  ND1 . HIS A 1 69  ? 19.052  -4.373  18.807 1.00 24.10 ? 63  HIS A ND1 1 
ATOM   434  C  CD2 . HIS A 1 69  ? 19.423  -3.477  20.766 1.00 29.00 ? 63  HIS A CD2 1 
ATOM   435  C  CE1 . HIS A 1 69  ? 19.695  -3.238  18.600 1.00 30.13 ? 63  HIS A CE1 1 
ATOM   436  N  NE2 . HIS A 1 69  ? 19.932  -2.673  19.773 1.00 23.48 ? 63  HIS A NE2 1 
ATOM   437  N  N   . PHE A 1 70  ? 16.142  -7.070  23.046 1.00 23.87 ? 64  PHE A N   1 
ATOM   438  C  CA  . PHE A 1 70  ? 15.387  -8.277  23.424 1.00 27.72 ? 64  PHE A CA  1 
ATOM   439  C  C   . PHE A 1 70  ? 15.476  -9.297  22.268 1.00 29.56 ? 64  PHE A C   1 
ATOM   440  O  O   . PHE A 1 70  ? 15.012  -9.055  21.149 1.00 23.83 ? 64  PHE A O   1 
ATOM   441  C  CB  . PHE A 1 70  ? 13.930  -7.890  23.705 1.00 28.24 ? 64  PHE A CB  1 
ATOM   442  C  CG  . PHE A 1 70  ? 13.081  -9.016  24.238 1.00 31.07 ? 64  PHE A CG  1 
ATOM   443  C  CD1 . PHE A 1 70  ? 13.610  -9.944  25.128 1.00 32.73 ? 64  PHE A CD1 1 
ATOM   444  C  CD2 . PHE A 1 70  ? 11.727  -9.089  23.913 1.00 33.28 ? 64  PHE A CD2 1 
ATOM   445  C  CE1 . PHE A 1 70  ? 12.791  -10.941 25.698 1.00 30.58 ? 64  PHE A CE1 1 
ATOM   446  C  CE2 . PHE A 1 70  ? 10.902  -10.069 24.472 1.00 37.49 ? 64  PHE A CE2 1 
ATOM   447  C  CZ  . PHE A 1 70  ? 11.438  -10.998 25.370 1.00 33.30 ? 64  PHE A CZ  1 
ATOM   448  N  N   . ASN A 1 71  ? 16.073  -10.447 22.551 1.00 29.42 ? 65  ASN A N   1 
ATOM   449  C  CA  . ASN A 1 71  ? 16.326  -11.444 21.523 1.00 29.83 ? 65  ASN A CA  1 
ATOM   450  C  C   . ASN A 1 71  ? 16.066  -12.857 22.025 1.00 29.29 ? 65  ASN A C   1 
ATOM   451  O  O   . ASN A 1 71  ? 16.970  -13.694 22.071 1.00 33.90 ? 65  ASN A O   1 
ATOM   452  C  CB  . ASN A 1 71  ? 17.790  -11.262 21.075 1.00 33.70 ? 65  ASN A CB  1 
ATOM   453  C  CG  . ASN A 1 71  ? 18.203  -12.196 19.965 1.00 29.53 ? 65  ASN A CG  1 
ATOM   454  O  OD1 . ASN A 1 71  ? 17.373  -12.693 19.196 1.00 34.10 ? 65  ASN A OD1 1 
ATOM   455  N  ND2 . ASN A 1 71  ? 19.510  -12.401 19.835 1.00 29.29 ? 65  ASN A ND2 1 
ATOM   456  N  N   . PRO A 1 72  ? 14.819  -13.147 22.403 1.00 35.05 ? 66  PRO A N   1 
ATOM   457  C  CA  . PRO A 1 72  ? 14.531  -14.496 22.895 1.00 41.18 ? 66  PRO A CA  1 
ATOM   458  C  C   . PRO A 1 72  ? 14.786  -15.634 21.896 1.00 43.24 ? 66  PRO A C   1 
ATOM   459  O  O   . PRO A 1 72  ? 15.138  -16.734 22.304 1.00 44.92 ? 66  PRO A O   1 
ATOM   460  C  CB  . PRO A 1 72  ? 13.074  -14.405 23.341 1.00 39.05 ? 66  PRO A CB  1 
ATOM   461  C  CG  . PRO A 1 72  ? 12.489  -13.370 22.435 1.00 36.27 ? 66  PRO A CG  1 
ATOM   462  C  CD  . PRO A 1 72  ? 13.597  -12.323 22.325 1.00 32.94 ? 66  PRO A CD  1 
ATOM   463  N  N   . LEU A 1 73  ? 14.638  -15.375 20.602 1.00 42.03 ? 67  LEU A N   1 
ATOM   464  C  CA  . LEU A 1 73  ? 14.857  -16.424 19.598 1.00 46.17 ? 67  LEU A CA  1 
ATOM   465  C  C   . LEU A 1 73  ? 16.309  -16.579 19.133 1.00 43.20 ? 67  LEU A C   1 
ATOM   466  O  O   . LEU A 1 73  ? 16.583  -17.320 18.191 1.00 48.29 ? 67  LEU A O   1 
ATOM   467  C  CB  . LEU A 1 73  ? 13.941  -16.205 18.384 1.00 46.59 ? 67  LEU A CB  1 
ATOM   468  C  CG  . LEU A 1 73  ? 12.434  -16.104 18.670 1.00 54.22 ? 67  LEU A CG  1 
ATOM   469  C  CD1 . LEU A 1 73  ? 11.670  -16.030 17.359 1.00 53.63 ? 67  LEU A CD1 1 
ATOM   470  C  CD2 . LEU A 1 73  ? 11.962  -17.298 19.489 1.00 57.25 ? 67  LEU A CD2 1 
ATOM   471  N  N   . SER A 1 74  ? 17.227  -15.880 19.799 1.00 37.90 ? 68  SER A N   1 
ATOM   472  C  CA  . SER A 1 74  ? 18.651  -15.942 19.503 1.00 40.57 ? 68  SER A CA  1 
ATOM   473  C  C   . SER A 1 74  ? 18.982  -15.744 18.032 1.00 42.00 ? 68  SER A C   1 
ATOM   474  O  O   . SER A 1 74  ? 19.572  -16.622 17.401 1.00 39.80 ? 68  SER A O   1 
ATOM   475  C  CB  . SER A 1 74  ? 19.214  -17.288 19.969 1.00 36.48 ? 68  SER A CB  1 
ATOM   476  O  OG  . SER A 1 74  ? 18.796  -17.577 21.293 1.00 46.23 ? 68  SER A OG  1 
ATOM   477  N  N   . ARG A 1 75  ? 18.610  -14.585 17.495 1.00 35.54 ? 69  ARG A N   1 
ATOM   478  C  CA  . ARG A 1 75  ? 18.860  -14.257 16.098 1.00 31.80 ? 69  ARG A CA  1 
ATOM   479  C  C   . ARG A 1 75  ? 19.789  -13.054 15.960 1.00 29.99 ? 69  ARG A C   1 
ATOM   480  O  O   . ARG A 1 75  ? 20.206  -12.494 16.949 1.00 28.17 ? 69  ARG A O   1 
ATOM   481  C  CB  . ARG A 1 75  ? 17.516  -13.998 15.423 1.00 33.82 ? 69  ARG A CB  1 
ATOM   482  C  CG  . ARG A 1 75  ? 16.646  -15.249 15.559 1.00 50.33 ? 69  ARG A CG  1 
ATOM   483  C  CD  . ARG A 1 75  ? 15.416  -15.315 14.680 1.00 57.42 ? 69  ARG A CD  1 
ATOM   484  N  NE  . ARG A 1 75  ? 14.896  -16.678 14.747 1.00 68.16 ? 69  ARG A NE  1 
ATOM   485  C  CZ  . ARG A 1 75  ? 13.691  -17.061 14.339 1.00 66.89 ? 69  ARG A CZ  1 
ATOM   486  N  NH1 . ARG A 1 75  ? 12.845  -16.180 13.820 1.00 61.14 ? 69  ARG A NH1 1 
ATOM   487  N  NH2 . ARG A 1 75  ? 13.338  -18.334 14.461 1.00 48.71 ? 69  ARG A NH2 1 
ATOM   488  N  N   . LYS A 1 76  ? 20.126  -12.674 14.733 1.00 30.27 ? 70  LYS A N   1 
ATOM   489  C  CA  . LYS A 1 76  ? 20.972  -11.497 14.517 1.00 31.10 ? 70  LYS A CA  1 
ATOM   490  C  C   . LYS A 1 76  ? 20.040  -10.281 14.445 1.00 37.91 ? 70  LYS A C   1 
ATOM   491  O  O   . LYS A 1 76  ? 18.814  -10.426 14.271 1.00 25.31 ? 70  LYS A O   1 
ATOM   492  C  CB  . LYS A 1 76  ? 21.712  -11.617 13.191 1.00 41.78 ? 70  LYS A CB  1 
ATOM   493  C  CG  . LYS A 1 76  ? 22.591  -12.845 13.076 1.00 53.95 ? 70  LYS A CG  1 
ATOM   494  C  CD  . LYS A 1 76  ? 23.651  -12.836 14.152 1.00 62.99 ? 70  LYS A CD  1 
ATOM   495  C  CE  . LYS A 1 76  ? 24.705  -13.885 13.875 1.00 69.14 ? 70  LYS A CE  1 
ATOM   496  N  NZ  . LYS A 1 76  ? 25.335  -13.657 12.547 1.00 74.14 ? 70  LYS A NZ  1 
ATOM   497  N  N   . HIS A 1 77  ? 20.624  -9.092  14.573 1.00 27.25 ? 71  HIS A N   1 
ATOM   498  C  CA  . HIS A 1 77  ? 19.874  -7.852  14.499 1.00 25.25 ? 71  HIS A CA  1 
ATOM   499  C  C   . HIS A 1 77  ? 19.401  -7.611  13.045 1.00 31.38 ? 71  HIS A C   1 
ATOM   500  O  O   . HIS A 1 77  ? 20.087  -7.967  12.093 1.00 31.03 ? 71  HIS A O   1 
ATOM   501  C  CB  . HIS A 1 77  ? 20.759  -6.666  14.949 1.00 24.68 ? 71  HIS A CB  1 
ATOM   502  C  CG  . HIS A 1 77  ? 20.069  -5.338  14.844 1.00 26.12 ? 71  HIS A CG  1 
ATOM   503  N  ND1 . HIS A 1 77  ? 19.068  -4.952  15.710 1.00 26.16 ? 71  HIS A ND1 1 
ATOM   504  C  CD2 . HIS A 1 77  ? 20.196  -4.331  13.945 1.00 34.82 ? 71  HIS A CD2 1 
ATOM   505  C  CE1 . HIS A 1 77  ? 18.611  -3.764  15.350 1.00 32.69 ? 71  HIS A CE1 1 
ATOM   506  N  NE2 . HIS A 1 77  ? 19.277  -3.362  14.284 1.00 25.03 ? 71  HIS A NE2 1 
ATOM   507  N  N   . GLY A 1 78  ? 18.228  -7.015  12.875 1.00 29.11 ? 72  GLY A N   1 
ATOM   508  C  CA  . GLY A 1 78  ? 17.754  -6.731  11.531 1.00 30.63 ? 72  GLY A CA  1 
ATOM   509  C  C   . GLY A 1 78  ? 16.727  -5.626  11.574 1.00 29.33 ? 72  GLY A C   1 
ATOM   510  O  O   . GLY A 1 78  ? 16.511  -5.020  12.609 1.00 28.70 ? 72  GLY A O   1 
ATOM   511  N  N   . GLY A 1 79  ? 16.111  -5.328  10.445 1.00 36.06 ? 73  GLY A N   1 
ATOM   512  C  CA  . GLY A 1 79  ? 15.081  -4.307  10.463 1.00 28.70 ? 73  GLY A CA  1 
ATOM   513  C  C   . GLY A 1 79  ? 13.817  -5.006  10.918 1.00 35.95 ? 73  GLY A C   1 
ATOM   514  O  O   . GLY A 1 79  ? 13.746  -6.251  10.917 1.00 31.30 ? 73  GLY A O   1 
ATOM   515  N  N   . PRO A 1 80  ? 12.789  -4.245  11.294 1.00 33.93 ? 74  PRO A N   1 
ATOM   516  C  CA  . PRO A 1 80  ? 11.547  -4.862  11.750 1.00 36.43 ? 74  PRO A CA  1 
ATOM   517  C  C   . PRO A 1 80  ? 10.887  -5.753  10.712 1.00 38.74 ? 74  PRO A C   1 
ATOM   518  O  O   . PRO A 1 80  ? 10.220  -6.736  11.059 1.00 36.15 ? 74  PRO A O   1 
ATOM   519  C  CB  . PRO A 1 80  ? 10.679  -3.655  12.128 1.00 39.69 ? 74  PRO A CB  1 
ATOM   520  C  CG  . PRO A 1 80  ? 11.173  -2.577  11.242 1.00 37.36 ? 74  PRO A CG  1 
ATOM   521  C  CD  . PRO A 1 80  ? 12.671  -2.775  11.252 1.00 36.38 ? 74  PRO A CD  1 
ATOM   522  N  N   . LYS A 1 81  ? 11.085  -5.436  9.435  1.00 31.19 ? 75  LYS A N   1 
ATOM   523  C  CA  . LYS A 1 81  ? 10.426  -6.227  8.402  1.00 35.28 ? 75  LYS A CA  1 
ATOM   524  C  C   . LYS A 1 81  ? 11.342  -7.268  7.791  1.00 41.83 ? 75  LYS A C   1 
ATOM   525  O  O   . LYS A 1 81  ? 11.029  -7.844  6.752  1.00 34.33 ? 75  LYS A O   1 
ATOM   526  C  CB  . LYS A 1 81  ? 9.865   -5.319  7.297  1.00 43.62 ? 75  LYS A CB  1 
ATOM   527  C  CG  . LYS A 1 81  ? 8.925   -4.223  7.778  1.00 39.33 ? 75  LYS A CG  1 
ATOM   528  C  CD  . LYS A 1 81  ? 7.732   -4.765  8.546  1.00 53.00 ? 75  LYS A CD  1 
ATOM   529  C  CE  . LYS A 1 81  ? 6.962   -3.625  9.204  1.00 53.39 ? 75  LYS A CE  1 
ATOM   530  N  NZ  . LYS A 1 81  ? 5.677   -4.078  9.820  1.00 58.69 ? 75  LYS A NZ  1 
ATOM   531  N  N   . ASP A 1 82  ? 12.481  -7.505  8.432  1.00 41.94 ? 76  ASP A N   1 
ATOM   532  C  CA  . ASP A 1 82  ? 13.418  -8.499  7.940  1.00 42.56 ? 76  ASP A CA  1 
ATOM   533  C  C   . ASP A 1 82  ? 13.066  -9.846  8.555  1.00 40.72 ? 76  ASP A C   1 
ATOM   534  O  O   . ASP A 1 82  ? 12.489  -9.908  9.649  1.00 41.72 ? 76  ASP A O   1 
ATOM   535  C  CB  . ASP A 1 82  ? 14.860  -8.117  8.310  1.00 46.84 ? 76  ASP A CB  1 
ATOM   536  C  CG  . ASP A 1 82  ? 15.452  -7.085  7.363  1.00 54.83 ? 76  ASP A CG  1 
ATOM   537  O  OD1 . ASP A 1 82  ? 15.468  -7.348  6.143  1.00 57.26 ? 76  ASP A OD1 1 
ATOM   538  O  OD2 . ASP A 1 82  ? 15.908  -6.019  7.831  1.00 55.90 ? 76  ASP A OD2 1 
ATOM   539  N  N   . GLU A 1 83  ? 13.412  -10.916 7.843  1.00 37.54 ? 77  GLU A N   1 
ATOM   540  C  CA  . GLU A 1 83  ? 13.152  -12.282 8.300  1.00 45.94 ? 77  GLU A CA  1 
ATOM   541  C  C   . GLU A 1 83  ? 13.890  -12.498 9.610  1.00 43.93 ? 77  GLU A C   1 
ATOM   542  O  O   . GLU A 1 83  ? 13.308  -12.934 10.604 1.00 46.61 ? 77  GLU A O   1 
ATOM   543  C  CB  . GLU A 1 83  ? 13.660  -13.302 7.275  1.00 54.29 ? 77  GLU A CB  1 
ATOM   544  C  CG  . GLU A 1 83  ? 13.044  -13.195 5.878  1.00 69.33 ? 77  GLU A CG  1 
ATOM   545  C  CD  . GLU A 1 83  ? 11.641  -13.779 5.791  1.00 72.57 ? 77  GLU A CD  1 
ATOM   546  O  OE1 . GLU A 1 83  ? 10.744  -13.298 6.522  1.00 74.05 ? 77  GLU A OE1 1 
ATOM   547  O  OE2 . GLU A 1 83  ? 11.442  -14.719 4.987  1.00 68.90 ? 77  GLU A OE2 1 
ATOM   548  N  N   . GLU A 1 84  ? 15.182  -12.194 9.600  1.00 40.77 ? 78  GLU A N   1 
ATOM   549  C  CA  . GLU A 1 84  ? 16.004  -12.351 10.791 1.00 40.43 ? 78  GLU A CA  1 
ATOM   550  C  C   . GLU A 1 84  ? 16.127  -11.005 11.507 1.00 40.47 ? 78  GLU A C   1 
ATOM   551  O  O   . GLU A 1 84  ? 16.670  -10.040 10.954 1.00 30.68 ? 78  GLU A O   1 
ATOM   552  C  CB  . GLU A 1 84  ? 17.397  -12.849 10.414 1.00 44.88 ? 78  GLU A CB  1 
ATOM   553  C  CG  . GLU A 1 84  ? 17.895  -14.008 11.267 1.00 53.67 ? 78  GLU A CG  1 
ATOM   554  C  CD  . GLU A 1 84  ? 19.360  -13.870 11.611 1.00 58.34 ? 78  GLU A CD  1 
ATOM   555  O  OE1 . GLU A 1 84  ? 20.096  -13.288 10.787 1.00 60.76 ? 78  GLU A OE1 1 
ATOM   556  O  OE2 . GLU A 1 84  ? 19.783  -14.344 12.691 1.00 43.96 ? 78  GLU A OE2 1 
ATOM   557  N  N   . ARG A 1 85  ? 15.607  -10.949 12.730 1.00 33.52 ? 79  ARG A N   1 
ATOM   558  C  CA  . ARG A 1 85  ? 15.663  -9.742  13.547 1.00 33.89 ? 79  ARG A CA  1 
ATOM   559  C  C   . ARG A 1 85  ? 15.523  -10.159 14.990 1.00 33.57 ? 79  ARG A C   1 
ATOM   560  O  O   . ARG A 1 85  ? 15.162  -11.305 15.279 1.00 32.09 ? 79  ARG A O   1 
ATOM   561  C  CB  . ARG A 1 85  ? 14.500  -8.795  13.215 1.00 24.62 ? 79  ARG A CB  1 
ATOM   562  C  CG  . ARG A 1 85  ? 13.134  -9.494  13.218 1.00 33.91 ? 79  ARG A CG  1 
ATOM   563  C  CD  . ARG A 1 85  ? 11.950  -8.506  13.216 1.00 30.46 ? 79  ARG A CD  1 
ATOM   564  N  NE  . ARG A 1 85  ? 11.624  -8.037  14.561 1.00 32.29 ? 79  ARG A NE  1 
ATOM   565  C  CZ  . ARG A 1 85  ? 10.560  -7.304  14.857 1.00 38.68 ? 79  ARG A CZ  1 
ATOM   566  N  NH1 . ARG A 1 85  ? 9.722   -6.935  13.889 1.00 36.85 ? 79  ARG A NH1 1 
ATOM   567  N  NH2 . ARG A 1 85  ? 10.295  -6.998  16.126 1.00 27.77 ? 79  ARG A NH2 1 
ATOM   568  N  N   . HIS A 1 86  ? 15.788  -9.223  15.898 1.00 25.06 ? 80  HIS A N   1 
ATOM   569  C  CA  . HIS A 1 86  ? 15.623  -9.503  17.301 1.00 23.37 ? 80  HIS A CA  1 
ATOM   570  C  C   . HIS A 1 86  ? 14.149  -9.198  17.554 1.00 29.72 ? 80  HIS A C   1 
ATOM   571  O  O   . HIS A 1 86  ? 13.577  -8.341  16.873 1.00 27.01 ? 80  HIS A O   1 
ATOM   572  C  CB  . HIS A 1 86  ? 16.467  -8.519  18.131 1.00 24.96 ? 80  HIS A CB  1 
ATOM   573  C  CG  . HIS A 1 86  ? 17.940  -8.655  17.942 1.00 29.37 ? 80  HIS A CG  1 
ATOM   574  N  ND1 . HIS A 1 86  ? 18.784  -7.558  17.911 1.00 26.42 ? 80  HIS A ND1 1 
ATOM   575  C  CD2 . HIS A 1 86  ? 18.738  -9.747  17.911 1.00 22.49 ? 80  HIS A CD2 1 
ATOM   576  C  CE1 . HIS A 1 86  ? 20.038  -7.976  17.887 1.00 26.93 ? 80  HIS A CE1 1 
ATOM   577  N  NE2 . HIS A 1 86  ? 20.037  -9.298  17.887 1.00 27.75 ? 80  HIS A NE2 1 
ATOM   578  N  N   . VAL A 1 87  ? 13.521  -9.871  18.513 1.00 26.88 ? 81  VAL A N   1 
ATOM   579  C  CA  . VAL A 1 87  ? 12.127  -9.539  18.798 1.00 29.00 ? 81  VAL A CA  1 
ATOM   580  C  C   . VAL A 1 87  ? 11.991  -8.041  19.111 1.00 29.87 ? 81  VAL A C   1 
ATOM   581  O  O   . VAL A 1 87  ? 11.012  -7.400  18.728 1.00 27.64 ? 81  VAL A O   1 
ATOM   582  C  CB  . VAL A 1 87  ? 11.587  -10.346 20.002 1.00 29.88 ? 81  VAL A CB  1 
ATOM   583  C  CG1 . VAL A 1 87  ? 10.230  -9.779  20.471 1.00 27.78 ? 81  VAL A CG1 1 
ATOM   584  C  CG2 . VAL A 1 87  ? 11.416  -11.799 19.601 1.00 38.56 ? 81  VAL A CG2 1 
ATOM   585  N  N   . GLY A 1 88  ? 12.981  -7.458  19.791 1.00 26.49 ? 82  GLY A N   1 
ATOM   586  C  CA  . GLY A 1 88  ? 12.845  -6.052  20.135 1.00 28.11 ? 82  GLY A CA  1 
ATOM   587  C  C   . GLY A 1 88  ? 13.246  -5.017  19.098 1.00 26.86 ? 82  GLY A C   1 
ATOM   588  O  O   . GLY A 1 88  ? 13.361  -3.842  19.411 1.00 29.90 ? 82  GLY A O   1 
ATOM   589  N  N   . ASP A 1 89  ? 13.445  -5.437  17.856 1.00 23.62 ? 83  ASP A N   1 
ATOM   590  C  CA  . ASP A 1 89  ? 13.848  -4.514  16.828 1.00 20.06 ? 83  ASP A CA  1 
ATOM   591  C  C   . ASP A 1 89  ? 12.688  -3.768  16.190 1.00 37.76 ? 83  ASP A C   1 
ATOM   592  O  O   . ASP A 1 89  ? 11.975  -4.317  15.359 1.00 31.55 ? 83  ASP A O   1 
ATOM   593  C  CB  . ASP A 1 89  ? 14.606  -5.246  15.739 1.00 27.97 ? 83  ASP A CB  1 
ATOM   594  C  CG  . ASP A 1 89  ? 16.000  -5.659  16.186 1.00 21.54 ? 83  ASP A CG  1 
ATOM   595  O  OD1 . ASP A 1 89  ? 16.468  -5.085  17.201 1.00 25.73 ? 83  ASP A OD1 1 
ATOM   596  O  OD2 . ASP A 1 89  ? 16.598  -6.516  15.498 1.00 25.68 ? 83  ASP A OD2 1 
ATOM   597  N  N   . LEU A 1 90  ? 12.519  -2.511  16.569 1.00 27.04 ? 84  LEU A N   1 
ATOM   598  C  CA  . LEU A 1 90  ? 11.458  -1.699  15.996 1.00 35.66 ? 84  LEU A CA  1 
ATOM   599  C  C   . LEU A 1 90  ? 12.089  -0.814  14.908 1.00 39.26 ? 84  LEU A C   1 
ATOM   600  O  O   . LEU A 1 90  ? 13.321  -0.772  14.766 1.00 33.62 ? 84  LEU A O   1 
ATOM   601  C  CB  . LEU A 1 90  ? 10.831  -0.859  17.113 1.00 38.10 ? 84  LEU A CB  1 
ATOM   602  C  CG  . LEU A 1 90  ? 10.365  -1.670  18.337 1.00 38.28 ? 84  LEU A CG  1 
ATOM   603  C  CD1 . LEU A 1 90  ? 9.609   -0.768  19.269 1.00 34.34 ? 84  LEU A CD1 1 
ATOM   604  C  CD2 . LEU A 1 90  ? 9.476   -2.809  17.916 1.00 36.51 ? 84  LEU A CD2 1 
ATOM   605  N  N   . ARG A 1 91  ? 11.272  -0.120  14.120 1.00 34.45 ? 85  ARG A N   1 
ATOM   606  C  CA  . ARG A 1 91  ? 11.859  0.730   13.085 1.00 27.69 ? 85  ARG A CA  1 
ATOM   607  C  C   . ARG A 1 91  ? 12.353  2.029   13.719 1.00 20.05 ? 85  ARG A C   1 
ATOM   608  O  O   . ARG A 1 91  ? 11.878  2.422   14.789 1.00 27.74 ? 85  ARG A O   1 
ATOM   609  C  CB  . ARG A 1 91  ? 10.829  1.079   12.017 1.00 42.46 ? 85  ARG A CB  1 
ATOM   610  C  CG  . ARG A 1 91  ? 9.781   2.061   12.487 1.00 29.83 ? 85  ARG A CG  1 
ATOM   611  C  CD  . ARG A 1 91  ? 8.670   2.076   11.446 1.00 54.72 ? 85  ARG A CD  1 
ATOM   612  N  NE  . ARG A 1 91  ? 8.284   3.423   11.062 1.00 47.97 ? 85  ARG A NE  1 
ATOM   613  C  CZ  . ARG A 1 91  ? 7.461   3.702   10.052 1.00 64.04 ? 85  ARG A CZ  1 
ATOM   614  N  NH1 . ARG A 1 91  ? 6.940   2.712   9.327  1.00 56.15 ? 85  ARG A NH1 1 
ATOM   615  N  NH2 . ARG A 1 91  ? 7.162   4.969   9.759  1.00 50.34 ? 85  ARG A NH2 1 
ATOM   616  N  N   . ASN A 1 92  ? 13.305  2.681   13.056 1.00 25.06 ? 86  ASN A N   1 
ATOM   617  C  CA  . ASN A 1 92  ? 13.848  3.952   13.516 1.00 26.21 ? 86  ASN A CA  1 
ATOM   618  C  C   . ASN A 1 92  ? 12.679  4.889   13.693 1.00 35.20 ? 86  ASN A C   1 
ATOM   619  O  O   . ASN A 1 92  ? 11.694  4.783   12.944 1.00 34.13 ? 86  ASN A O   1 
ATOM   620  C  CB  . ASN A 1 92  ? 14.758  4.564   12.435 1.00 27.85 ? 86  ASN A CB  1 
ATOM   621  C  CG  . ASN A 1 92  ? 16.136  3.938   12.397 1.00 33.78 ? 86  ASN A CG  1 
ATOM   622  O  OD1 . ASN A 1 92  ? 16.998  4.274   13.205 1.00 30.64 ? 86  ASN A OD1 1 
ATOM   623  N  ND2 . ASN A 1 92  ? 16.350  3.013   11.460 1.00 36.49 ? 86  ASN A ND2 1 
ATOM   624  N  N   . VAL A 1 93  ? 12.745  5.777   14.682 1.00 25.64 ? 87  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 93  ? 11.668  6.748   14.815 1.00 32.85 ? 87  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 93  ? 12.181  7.996   14.108 1.00 30.50 ? 87  VAL A C   1 
ATOM   627  O  O   . VAL A 1 93  ? 13.402  8.193   13.952 1.00 24.86 ? 87  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 93  ? 11.276  7.051   16.296 1.00 36.45 ? 87  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 93  ? 10.679  5.799   16.944 1.00 35.53 ? 87  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 93  ? 12.468  7.566   17.076 1.00 31.48 ? 87  VAL A CG2 1 
ATOM   631  N  N   . THR A 1 94  ? 11.255  8.818   13.642 1.00 25.75 ? 88  THR A N   1 
ATOM   632  C  CA  . THR A 1 94  ? 11.617  10.009  12.885 1.00 30.97 ? 88  THR A CA  1 
ATOM   633  C  C   . THR A 1 94  ? 11.274  11.324  13.575 1.00 29.08 ? 88  THR A C   1 
ATOM   634  O  O   . THR A 1 94  ? 10.111  11.607  13.828 1.00 29.95 ? 88  THR A O   1 
ATOM   635  C  CB  . THR A 1 94  ? 10.914  9.971   11.492 1.00 34.72 ? 88  THR A CB  1 
ATOM   636  O  OG1 . THR A 1 94  ? 11.358  8.813   10.773 1.00 32.36 ? 88  THR A OG1 1 
ATOM   637  C  CG2 . THR A 1 94  ? 11.245  11.209  10.678 1.00 33.09 ? 88  THR A CG2 1 
ATOM   638  N  N   . ALA A 1 95  ? 12.285  12.138  13.855 1.00 31.91 ? 89  ALA A N   1 
ATOM   639  C  CA  . ALA A 1 95  ? 12.058  13.421  14.517 1.00 42.56 ? 89  ALA A CA  1 
ATOM   640  C  C   . ALA A 1 95  ? 11.961  14.517  13.473 1.00 44.05 ? 89  ALA A C   1 
ATOM   641  O  O   . ALA A 1 95  ? 12.771  14.545  12.529 1.00 33.92 ? 89  ALA A O   1 
ATOM   642  C  CB  . ALA A 1 95  ? 13.196  13.729  15.493 1.00 45.65 ? 89  ALA A CB  1 
ATOM   643  N  N   . ASP A 1 96  ? 10.973  15.407  13.633 1.00 39.42 ? 90  ASP A N   1 
ATOM   644  C  CA  . ASP A 1 96  ? 10.793  16.505  12.681 1.00 36.80 ? 90  ASP A CA  1 
ATOM   645  C  C   . ASP A 1 96  ? 11.675  17.697  13.023 1.00 43.94 ? 90  ASP A C   1 
ATOM   646  O  O   . ASP A 1 96  ? 12.492  17.634  13.950 1.00 34.31 ? 90  ASP A O   1 
ATOM   647  C  CB  . ASP A 1 96  ? 9.314   16.948  12.589 1.00 45.43 ? 90  ASP A CB  1 
ATOM   648  C  CG  . ASP A 1 96  ? 8.755   17.537  13.902 1.00 51.32 ? 90  ASP A CG  1 
ATOM   649  O  OD1 . ASP A 1 96  ? 9.479   18.242  14.642 1.00 52.08 ? 90  ASP A OD1 1 
ATOM   650  O  OD2 . ASP A 1 96  ? 7.555   17.319  14.176 1.00 45.79 ? 90  ASP A OD2 1 
ATOM   651  N  N   . LYS A 1 97  ? 11.502  18.774  12.258 1.00 44.62 ? 91  LYS A N   1 
ATOM   652  C  CA  . LYS A 1 97  ? 12.248  20.014  12.425 1.00 45.25 ? 91  LYS A CA  1 
ATOM   653  C  C   . LYS A 1 97  ? 12.173  20.518  13.856 1.00 44.07 ? 91  LYS A C   1 
ATOM   654  O  O   . LYS A 1 97  ? 13.139  21.074  14.371 1.00 45.89 ? 91  LYS A O   1 
ATOM   655  C  CB  . LYS A 1 97  ? 11.683  21.081  11.485 1.00 51.87 ? 91  LYS A CB  1 
ATOM   656  C  CG  . LYS A 1 97  ? 11.792  20.735  10.009 1.00 66.64 ? 91  LYS A CG  1 
ATOM   657  C  CD  . LYS A 1 97  ? 13.244  20.754  9.560  1.00 65.66 ? 91  LYS A CD  1 
ATOM   658  C  CE  . LYS A 1 97  ? 13.401  20.390  8.093  1.00 69.57 ? 91  LYS A CE  1 
ATOM   659  N  NZ  . LYS A 1 97  ? 14.843  20.398  7.678  1.00 75.47 ? 91  LYS A NZ  1 
ATOM   660  N  N   . ASP A 1 98  ? 11.023  20.331  14.500 1.00 44.27 ? 92  ASP A N   1 
ATOM   661  C  CA  . ASP A 1 98  ? 10.864  20.775  15.889 1.00 48.90 ? 92  ASP A CA  1 
ATOM   662  C  C   . ASP A 1 98  ? 11.525  19.794  16.870 1.00 49.65 ? 92  ASP A C   1 
ATOM   663  O  O   . ASP A 1 98  ? 11.525  20.022  18.083 1.00 47.02 ? 92  ASP A O   1 
ATOM   664  C  CB  . ASP A 1 98  ? 9.379   20.909  16.261 1.00 54.92 ? 92  ASP A CB  1 
ATOM   665  C  CG  . ASP A 1 98  ? 8.557   21.606  15.186 1.00 68.80 ? 92  ASP A CG  1 
ATOM   666  O  OD1 . ASP A 1 98  ? 8.963   22.697  14.727 1.00 67.62 ? 92  ASP A OD1 1 
ATOM   667  O  OD2 . ASP A 1 98  ? 7.494   21.057  14.808 1.00 72.74 ? 92  ASP A OD2 1 
ATOM   668  N  N   . GLY A 1 99  ? 12.081  18.706  16.344 1.00 40.59 ? 93  GLY A N   1 
ATOM   669  C  CA  . GLY A 1 99  ? 12.720  17.724  17.201 1.00 37.02 ? 93  GLY A CA  1 
ATOM   670  C  C   . GLY A 1 99  ? 11.705  16.773  17.816 1.00 43.54 ? 93  GLY A C   1 
ATOM   671  O  O   . GLY A 1 99  ? 11.979  16.119  18.834 1.00 44.13 ? 93  GLY A O   1 
ATOM   672  N  N   . VAL A 1 100 ? 10.531  16.682  17.196 1.00 39.05 ? 94  VAL A N   1 
ATOM   673  C  CA  . VAL A 1 100 ? 9.486   15.802  17.703 1.00 36.70 ? 94  VAL A CA  1 
ATOM   674  C  C   . VAL A 1 100 ? 9.242   14.600  16.811 1.00 35.54 ? 94  VAL A C   1 
ATOM   675  O  O   . VAL A 1 100 ? 9.116   14.726  15.596 1.00 30.22 ? 94  VAL A O   1 
ATOM   676  C  CB  . VAL A 1 100 ? 8.140   16.553  17.896 1.00 35.64 ? 94  VAL A CB  1 
ATOM   677  C  CG1 . VAL A 1 100 ? 6.990   15.554  18.055 1.00 30.95 ? 94  VAL A CG1 1 
ATOM   678  C  CG2 . VAL A 1 100 ? 8.210   17.417  19.139 1.00 42.40 ? 94  VAL A CG2 1 
ATOM   679  N  N   . ALA A 1 101 ? 9.181   13.429  17.428 1.00 33.93 ? 95  ALA A N   1 
ATOM   680  C  CA  . ALA A 1 101 ? 8.918   12.202  16.691 1.00 37.11 ? 95  ALA A CA  1 
ATOM   681  C  C   . ALA A 1 101 ? 7.564   11.682  17.134 1.00 38.18 ? 95  ALA A C   1 
ATOM   682  O  O   . ALA A 1 101 ? 7.397   11.262  18.275 1.00 42.13 ? 95  ALA A O   1 
ATOM   683  C  CB  . ALA A 1 101 ? 9.998   11.170  16.976 1.00 40.92 ? 95  ALA A CB  1 
ATOM   684  N  N   . ASP A 1 102 ? 6.586   11.738  16.243 1.00 34.09 ? 96  ASP A N   1 
ATOM   685  C  CA  . ASP A 1 102 ? 5.250   11.247  16.561 1.00 40.78 ? 96  ASP A CA  1 
ATOM   686  C  C   . ASP A 1 102 ? 5.252   9.842   16.012 1.00 43.68 ? 96  ASP A C   1 
ATOM   687  O  O   . ASP A 1 102 ? 5.272   9.641   14.798 1.00 49.38 ? 96  ASP A O   1 
ATOM   688  C  CB  . ASP A 1 102 ? 4.172   12.111  15.888 1.00 36.55 ? 96  ASP A CB  1 
ATOM   689  C  CG  . ASP A 1 102 ? 4.053   13.481  16.521 1.00 46.79 ? 96  ASP A CG  1 
ATOM   690  O  OD1 . ASP A 1 102 ? 3.814   13.551  17.747 1.00 47.00 ? 96  ASP A OD1 1 
ATOM   691  O  OD2 . ASP A 1 102 ? 4.201   14.491  15.804 1.00 62.83 ? 96  ASP A OD2 1 
ATOM   692  N  N   . VAL A 1 103 ? 5.245   8.873   16.918 1.00 37.46 ? 97  VAL A N   1 
ATOM   693  C  CA  . VAL A 1 103 ? 5.333   7.472   16.549 1.00 36.68 ? 97  VAL A CA  1 
ATOM   694  C  C   . VAL A 1 103 ? 4.015   6.738   16.415 1.00 32.99 ? 97  VAL A C   1 
ATOM   695  O  O   . VAL A 1 103 ? 3.101   6.904   17.216 1.00 34.51 ? 97  VAL A O   1 
ATOM   696  C  CB  . VAL A 1 103 ? 6.233   6.738   17.559 1.00 38.85 ? 97  VAL A CB  1 
ATOM   697  C  CG1 . VAL A 1 103 ? 6.367   5.289   17.195 1.00 38.01 ? 97  VAL A CG1 1 
ATOM   698  C  CG2 . VAL A 1 103 ? 7.604   7.425   17.601 1.00 42.79 ? 97  VAL A CG2 1 
ATOM   699  N  N   . SER A 1 104 ? 3.933   5.913   15.387 1.00 34.46 ? 98  SER A N   1 
ATOM   700  C  CA  . SER A 1 104 ? 2.732   5.133   15.154 1.00 43.99 ? 98  SER A CA  1 
ATOM   701  C  C   . SER A 1 104 ? 3.159   3.884   14.426 1.00 44.05 ? 98  SER A C   1 
ATOM   702  O  O   . SER A 1 104 ? 3.206   3.854   13.204 1.00 50.33 ? 98  SER A O   1 
ATOM   703  C  CB  . SER A 1 104 ? 1.733   5.920   14.304 1.00 49.95 ? 98  SER A CB  1 
ATOM   704  O  OG  . SER A 1 104 ? 0.553   5.161   14.091 1.00 50.92 ? 98  SER A OG  1 
ATOM   705  N  N   . ILE A 1 105 ? 3.472   2.849   15.185 1.00 38.94 ? 99  ILE A N   1 
ATOM   706  C  CA  . ILE A 1 105 ? 3.935   1.597   14.613 1.00 50.11 ? 99  ILE A CA  1 
ATOM   707  C  C   . ILE A 1 105 ? 3.070   0.410   15.002 1.00 45.14 ? 99  ILE A C   1 
ATOM   708  O  O   . ILE A 1 105 ? 2.442   0.409   16.056 1.00 43.75 ? 99  ILE A O   1 
ATOM   709  C  CB  . ILE A 1 105 ? 5.371   1.277   15.100 1.00 49.91 ? 99  ILE A CB  1 
ATOM   710  C  CG1 . ILE A 1 105 ? 6.356   2.318   14.574 1.00 55.83 ? 99  ILE A CG1 1 
ATOM   711  C  CG2 . ILE A 1 105 ? 5.777   -0.121  14.654 1.00 58.86 ? 99  ILE A CG2 1 
ATOM   712  C  CD1 . ILE A 1 105 ? 7.717   2.226   15.240 1.00 61.51 ? 99  ILE A CD1 1 
ATOM   713  N  N   . GLU A 1 106 ? 3.038   -0.592  14.137 1.00 36.18 ? 100 GLU A N   1 
ATOM   714  C  CA  . GLU A 1 106 ? 2.332   -1.824  14.442 1.00 43.50 ? 100 GLU A CA  1 
ATOM   715  C  C   . GLU A 1 106 ? 3.332   -2.978  14.281 1.00 39.71 ? 100 GLU A C   1 
ATOM   716  O  O   . GLU A 1 106 ? 3.991   -3.098  13.251 1.00 40.09 ? 100 GLU A O   1 
ATOM   717  C  CB  . GLU A 1 106 ? 1.147   -2.027  13.515 1.00 48.97 ? 100 GLU A CB  1 
ATOM   718  C  CG  . GLU A 1 106 ? 0.399   -3.300  13.825 1.00 56.98 ? 100 GLU A CG  1 
ATOM   719  C  CD  . GLU A 1 106 ? -0.807  -3.491  12.943 1.00 63.82 ? 100 GLU A CD  1 
ATOM   720  O  OE1 . GLU A 1 106 ? -1.728  -2.650  13.025 1.00 57.64 ? 100 GLU A OE1 1 
ATOM   721  O  OE2 . GLU A 1 106 ? -0.825  -4.479  12.169 1.00 61.18 ? 100 GLU A OE2 1 
ATOM   722  N  N   . ASP A 1 107 ? 3.486   -3.813  15.303 1.00 39.38 ? 101 ASP A N   1 
ATOM   723  C  CA  . ASP A 1 107 ? 4.431   -4.924  15.188 1.00 40.04 ? 101 ASP A CA  1 
ATOM   724  C  C   . ASP A 1 107 ? 3.826   -6.240  15.646 1.00 40.15 ? 101 ASP A C   1 
ATOM   725  O  O   . ASP A 1 107 ? 3.234   -6.321  16.722 1.00 45.83 ? 101 ASP A O   1 
ATOM   726  C  CB  . ASP A 1 107 ? 5.690   -4.655  16.000 1.00 37.56 ? 101 ASP A CB  1 
ATOM   727  C  CG  . ASP A 1 107 ? 6.824   -5.597  15.630 1.00 51.51 ? 101 ASP A CG  1 
ATOM   728  O  OD1 . ASP A 1 107 ? 7.480   -5.380  14.583 1.00 56.37 ? 101 ASP A OD1 1 
ATOM   729  O  OD2 . ASP A 1 107 ? 7.047   -6.569  16.371 1.00 43.13 ? 101 ASP A OD2 1 
ATOM   730  N  N   . SER A 1 108 ? 3.982   -7.275  14.829 1.00 38.30 ? 102 SER A N   1 
ATOM   731  C  CA  . SER A 1 108 ? 3.450   -8.591  15.161 1.00 45.93 ? 102 SER A CA  1 
ATOM   732  C  C   . SER A 1 108 ? 4.463   -9.538  15.795 1.00 41.60 ? 102 SER A C   1 
ATOM   733  O  O   . SER A 1 108 ? 4.167   -10.707 15.995 1.00 42.75 ? 102 SER A O   1 
ATOM   734  C  CB  . SER A 1 108 ? 2.865   -9.257  13.915 1.00 47.26 ? 102 SER A CB  1 
ATOM   735  O  OG  . SER A 1 108 ? 1.640   -8.649  13.571 1.00 56.21 ? 102 SER A OG  1 
ATOM   736  N  N   . VAL A 1 109 ? 5.656   -9.048  16.105 1.00 38.60 ? 103 VAL A N   1 
ATOM   737  C  CA  . VAL A 1 109 ? 6.658   -9.910  16.716 1.00 37.32 ? 103 VAL A CA  1 
ATOM   738  C  C   . VAL A 1 109 ? 6.635   -9.721  18.246 1.00 39.74 ? 103 VAL A C   1 
ATOM   739  O  O   . VAL A 1 109 ? 6.671   -10.688 19.004 1.00 40.55 ? 103 VAL A O   1 
ATOM   740  C  CB  . VAL A 1 109 ? 8.071   -9.590  16.162 1.00 37.61 ? 103 VAL A CB  1 
ATOM   741  C  CG1 . VAL A 1 109 ? 9.122   -10.455 16.854 1.00 39.22 ? 103 VAL A CG1 1 
ATOM   742  C  CG2 . VAL A 1 109 ? 8.101   -9.815  14.653 1.00 43.53 ? 103 VAL A CG2 1 
ATOM   743  N  N   . ILE A 1 110 ? 6.576   -8.478  18.705 1.00 36.52 ? 104 ILE A N   1 
ATOM   744  C  CA  . ILE A 1 110 ? 6.552   -8.256  20.141 1.00 36.95 ? 104 ILE A CA  1 
ATOM   745  C  C   . ILE A 1 110 ? 5.196   -8.685  20.675 1.00 42.82 ? 104 ILE A C   1 
ATOM   746  O  O   . ILE A 1 110 ? 4.291   -8.998  19.908 1.00 42.17 ? 104 ILE A O   1 
ATOM   747  C  CB  . ILE A 1 110 ? 6.783   -6.783  20.517 1.00 39.42 ? 104 ILE A CB  1 
ATOM   748  C  CG1 . ILE A 1 110 ? 5.747   -5.889  19.842 1.00 37.92 ? 104 ILE A CG1 1 
ATOM   749  C  CG2 . ILE A 1 110 ? 8.196   -6.365  20.149 1.00 43.34 ? 104 ILE A CG2 1 
ATOM   750  C  CD1 . ILE A 1 110 ? 5.804   -4.456  20.318 1.00 31.71 ? 104 ILE A CD1 1 
ATOM   751  N  N   . SER A 1 111 ? 5.053   -8.686  21.991 1.00 40.50 ? 105 SER A N   1 
ATOM   752  C  CA  . SER A 1 111 ? 3.800   -9.079  22.606 1.00 43.28 ? 105 SER A CA  1 
ATOM   753  C  C   . SER A 1 111 ? 3.721   -8.539  24.028 1.00 45.71 ? 105 SER A C   1 
ATOM   754  O  O   . SER A 1 111 ? 4.753   -8.331  24.673 1.00 44.61 ? 105 SER A O   1 
ATOM   755  C  CB  . SER A 1 111 ? 3.700   -10.607 22.628 1.00 49.80 ? 105 SER A CB  1 
ATOM   756  O  OG  . SER A 1 111 ? 2.584   -11.028 23.385 1.00 53.79 ? 105 SER A OG  1 
ATOM   757  N  N   . LEU A 1 112 ? 2.505   -8.289  24.510 1.00 43.32 ? 106 LEU A N   1 
ATOM   758  C  CA  . LEU A 1 112 ? 2.338   -7.804  25.876 1.00 45.67 ? 106 LEU A CA  1 
ATOM   759  C  C   . LEU A 1 112 ? 1.949   -8.965  26.781 1.00 50.90 ? 106 LEU A C   1 
ATOM   760  O  O   . LEU A 1 112 ? 1.590   -8.757  27.933 1.00 47.83 ? 106 LEU A O   1 
ATOM   761  C  CB  . LEU A 1 112 ? 1.260   -6.723  25.950 1.00 39.97 ? 106 LEU A CB  1 
ATOM   762  C  CG  . LEU A 1 112 ? 1.531   -5.442  25.179 1.00 34.32 ? 106 LEU A CG  1 
ATOM   763  C  CD1 . LEU A 1 112 ? 0.415   -4.458  25.443 1.00 37.32 ? 106 LEU A CD1 1 
ATOM   764  C  CD2 . LEU A 1 112 ? 2.890   -4.865  25.581 1.00 38.45 ? 106 LEU A CD2 1 
ATOM   765  N  N   . SER A 1 113 ? 2.027   -10.184 26.252 1.00 51.98 ? 107 SER A N   1 
ATOM   766  C  CA  . SER A 1 113 ? 1.665   -11.387 27.006 1.00 61.86 ? 107 SER A CA  1 
ATOM   767  C  C   . SER A 1 113 ? 2.401   -12.607 26.433 1.00 61.90 ? 107 SER A C   1 
ATOM   768  O  O   . SER A 1 113 ? 2.754   -12.622 25.255 1.00 64.51 ? 107 SER A O   1 
ATOM   769  C  CB  . SER A 1 113 ? 0.149   -11.615 26.905 1.00 62.78 ? 107 SER A CB  1 
ATOM   770  O  OG  . SER A 1 113 ? -0.434  -11.863 28.173 1.00 66.06 ? 107 SER A OG  1 
ATOM   771  N  N   . GLY A 1 114 ? 2.638   -13.622 27.261 1.00 65.69 ? 108 GLY A N   1 
ATOM   772  C  CA  . GLY A 1 114 ? 3.316   -14.819 26.779 1.00 64.84 ? 108 GLY A CA  1 
ATOM   773  C  C   . GLY A 1 114 ? 4.825   -14.852 26.948 1.00 68.28 ? 108 GLY A C   1 
ATOM   774  O  O   . GLY A 1 114 ? 5.348   -14.488 28.000 1.00 69.65 ? 108 GLY A O   1 
ATOM   775  N  N   . ASP A 1 115 ? 5.530   -15.299 25.912 1.00 69.36 ? 109 ASP A N   1 
ATOM   776  C  CA  . ASP A 1 115 ? 6.986   -15.392 25.968 1.00 69.99 ? 109 ASP A CA  1 
ATOM   777  C  C   . ASP A 1 115 ? 7.682   -14.125 25.504 1.00 68.07 ? 109 ASP A C   1 
ATOM   778  O  O   . ASP A 1 115 ? 8.520   -13.577 26.218 1.00 74.77 ? 109 ASP A O   1 
ATOM   779  C  CB  . ASP A 1 115 ? 7.485   -16.573 25.132 1.00 72.10 ? 109 ASP A CB  1 
ATOM   780  C  CG  . ASP A 1 115 ? 7.006   -17.907 25.667 1.00 76.99 ? 109 ASP A CG  1 
ATOM   781  O  OD1 . ASP A 1 115 ? 7.066   -18.107 26.900 1.00 81.10 ? 109 ASP A OD1 1 
ATOM   782  O  OD2 . ASP A 1 115 ? 6.579   -18.758 24.856 1.00 72.86 ? 109 ASP A OD2 1 
ATOM   783  N  N   . HIS A 1 116 ? 7.345   -13.664 24.306 1.00 60.15 ? 110 HIS A N   1 
ATOM   784  C  CA  . HIS A 1 116 ? 7.960   -12.450 23.780 1.00 54.88 ? 110 HIS A CA  1 
ATOM   785  C  C   . HIS A 1 116 ? 7.381   -11.217 24.463 1.00 46.86 ? 110 HIS A C   1 
ATOM   786  O  O   . HIS A 1 116 ? 7.426   -10.124 23.902 1.00 41.60 ? 110 HIS A O   1 
ATOM   787  C  CB  . HIS A 1 116 ? 7.736   -12.340 22.269 1.00 52.14 ? 110 HIS A CB  1 
ATOM   788  C  CG  . HIS A 1 116 ? 8.340   -13.461 21.484 1.00 57.13 ? 110 HIS A CG  1 
ATOM   789  N  ND1 . HIS A 1 116 ? 8.158   -13.600 20.125 1.00 54.62 ? 110 HIS A ND1 1 
ATOM   790  C  CD2 . HIS A 1 116 ? 9.109   -14.507 21.871 1.00 54.41 ? 110 HIS A CD2 1 
ATOM   791  C  CE1 . HIS A 1 116 ? 8.783   -14.687 19.708 1.00 54.30 ? 110 HIS A CE1 1 
ATOM   792  N  NE2 . HIS A 1 116 ? 9.368   -15.255 20.748 1.00 59.09 ? 110 HIS A NE2 1 
ATOM   793  N  N   . CYS A 1 117 ? 6.825   -11.406 25.662 1.00 45.56 ? 111 CYS A N   1 
ATOM   794  C  CA  . CYS A 1 117 ? 6.234   -10.310 26.430 1.00 38.96 ? 111 CYS A CA  1 
ATOM   795  C  C   . CYS A 1 117 ? 7.331   -9.282  26.738 1.00 31.72 ? 111 CYS A C   1 
ATOM   796  O  O   . CYS A 1 117 ? 8.428   -9.624  27.174 1.00 32.34 ? 111 CYS A O   1 
ATOM   797  C  CB  . CYS A 1 117 ? 5.616   -10.837 27.733 1.00 43.07 ? 111 CYS A CB  1 
ATOM   798  S  SG  . CYS A 1 117 ? 4.682   -9.609  28.707 1.00 54.70 ? 111 CYS A SG  1 
ATOM   799  N  N   . ILE A 1 118 ? 7.031   -8.019  26.497 1.00 28.42 ? 112 ILE A N   1 
ATOM   800  C  CA  . ILE A 1 118 ? 8.015   -6.968  26.729 1.00 34.29 ? 112 ILE A CA  1 
ATOM   801  C  C   . ILE A 1 118 ? 7.757   -6.192  28.014 1.00 32.39 ? 112 ILE A C   1 
ATOM   802  O  O   . ILE A 1 118 ? 8.540   -5.321  28.388 1.00 29.23 ? 112 ILE A O   1 
ATOM   803  C  CB  . ILE A 1 118 ? 8.038   -6.003  25.554 1.00 23.23 ? 112 ILE A CB  1 
ATOM   804  C  CG1 . ILE A 1 118 ? 6.640   -5.385  25.372 1.00 37.78 ? 112 ILE A CG1 1 
ATOM   805  C  CG2 . ILE A 1 118 ? 8.562   -6.745  24.323 1.00 27.47 ? 112 ILE A CG2 1 
ATOM   806  C  CD1 . ILE A 1 118 ? 6.475   -4.473  24.175 1.00 29.47 ? 112 ILE A CD1 1 
ATOM   807  N  N   . ILE A 1 119 ? 6.661   -6.506  28.699 1.00 26.32 ? 113 ILE A N   1 
ATOM   808  C  CA  . ILE A 1 119 ? 6.368   -5.782  29.927 1.00 25.52 ? 113 ILE A CA  1 
ATOM   809  C  C   . ILE A 1 119 ? 7.471   -6.108  30.916 1.00 21.49 ? 113 ILE A C   1 
ATOM   810  O  O   . ILE A 1 119 ? 7.822   -7.270  31.120 1.00 25.86 ? 113 ILE A O   1 
ATOM   811  C  CB  . ILE A 1 119 ? 4.996   -6.176  30.531 1.00 29.25 ? 113 ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 119 ? 3.867   -5.645  29.634 1.00 34.52 ? 113 ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 119 ? 4.849   -5.577  31.934 1.00 27.91 ? 113 ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 119 ? 2.489   -5.943  30.150 1.00 48.16 ? 113 ILE A CD1 1 
ATOM   815  N  N   . GLY A 1 120 ? 8.031   -5.075  31.513 1.00 24.10 ? 114 GLY A N   1 
ATOM   816  C  CA  . GLY A 1 120 ? 9.081   -5.316  32.471 1.00 31.01 ? 114 GLY A CA  1 
ATOM   817  C  C   . GLY A 1 120 ? 10.417  -5.119  31.801 1.00 26.38 ? 114 GLY A C   1 
ATOM   818  O  O   . GLY A 1 120 ? 11.448  -5.200  32.461 1.00 25.56 ? 114 GLY A O   1 
ATOM   819  N  N   . ARG A 1 121 ? 10.402  -4.863  30.489 1.00 22.11 ? 115 ARG A N   1 
ATOM   820  C  CA  . ARG A 1 121 ? 11.649  -4.635  29.769 1.00 29.44 ? 115 ARG A CA  1 
ATOM   821  C  C   . ARG A 1 121 ? 11.842  -3.159  29.442 1.00 25.76 ? 115 ARG A C   1 
ATOM   822  O  O   . ARG A 1 121 ? 10.980  -2.330  29.741 1.00 29.80 ? 115 ARG A O   1 
ATOM   823  C  CB  . ARG A 1 121 ? 11.696  -5.536  28.536 1.00 27.03 ? 115 ARG A CB  1 
ATOM   824  C  CG  . ARG A 1 121 ? 11.590  -7.024  28.978 1.00 30.18 ? 115 ARG A CG  1 
ATOM   825  C  CD  . ARG A 1 121 ? 11.704  -8.000  27.815 1.00 32.69 ? 115 ARG A CD  1 
ATOM   826  N  NE  . ARG A 1 121 ? 11.400  -9.373  28.215 1.00 30.08 ? 115 ARG A NE  1 
ATOM   827  C  CZ  . ARG A 1 121 ? 12.269  -10.194 28.786 1.00 34.89 ? 115 ARG A CZ  1 
ATOM   828  N  NH1 . ARG A 1 121 ? 13.500  -9.780  29.020 1.00 35.51 ? 115 ARG A NH1 1 
ATOM   829  N  NH2 . ARG A 1 121 ? 11.901  -11.425 29.132 1.00 37.34 ? 115 ARG A NH2 1 
ATOM   830  N  N   . THR A 1 122 ? 12.978  -2.798  28.870 1.00 26.76 ? 116 THR A N   1 
ATOM   831  C  CA  . THR A 1 122 ? 13.203  -1.382  28.592 1.00 29.06 ? 116 THR A CA  1 
ATOM   832  C  C   . THR A 1 122 ? 13.040  -0.976  27.130 1.00 28.67 ? 116 THR A C   1 
ATOM   833  O  O   . THR A 1 122 ? 13.469  -1.689  26.240 1.00 28.47 ? 116 THR A O   1 
ATOM   834  C  CB  . THR A 1 122 ? 14.632  -0.961  29.077 1.00 33.73 ? 116 THR A CB  1 
ATOM   835  O  OG1 . THR A 1 122 ? 14.664  -0.978  30.509 1.00 32.62 ? 116 THR A OG1 1 
ATOM   836  C  CG2 . THR A 1 122 ? 14.997  0.438   28.604 1.00 31.93 ? 116 THR A CG2 1 
ATOM   837  N  N   . LEU A 1 123 ? 12.377  0.152   26.894 1.00 22.84 ? 117 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 123 ? 12.262  0.694   25.543 1.00 22.23 ? 117 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 123 ? 13.395  1.748   25.517 1.00 24.88 ? 117 LEU A C   1 
ATOM   840  O  O   . LEU A 1 123 ? 13.552  2.518   26.467 1.00 25.96 ? 117 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 123 ? 10.907  1.363   25.356 1.00 26.16 ? 117 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 123 ? 10.640  1.947   23.973 1.00 30.46 ? 117 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 123 ? 10.682  0.829   22.943 1.00 26.93 ? 117 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 123 ? 9.276   2.630   23.972 1.00 27.74 ? 117 LEU A CD2 1 
ATOM   845  N  N   . VAL A 1 124 ? 14.187  1.758   24.445 1.00 21.09 ? 118 VAL A N   1 
ATOM   846  C  CA  . VAL A 1 124 ? 15.322  2.671   24.294 1.00 24.88 ? 118 VAL A CA  1 
ATOM   847  C  C   . VAL A 1 124 ? 15.318  3.438   22.988 1.00 28.07 ? 118 VAL A C   1 
ATOM   848  O  O   . VAL A 1 124 ? 15.057  2.862   21.922 1.00 24.97 ? 118 VAL A O   1 
ATOM   849  C  CB  . VAL A 1 124 ? 16.689  1.890   24.321 1.00 24.42 ? 118 VAL A CB  1 
ATOM   850  C  CG1 . VAL A 1 124 ? 17.852  2.889   24.147 1.00 26.80 ? 118 VAL A CG1 1 
ATOM   851  C  CG2 . VAL A 1 124 ? 16.832  1.076   25.621 1.00 28.73 ? 118 VAL A CG2 1 
ATOM   852  N  N   . VAL A 1 125 ? 15.637  4.732   23.050 1.00 28.13 ? 119 VAL A N   1 
ATOM   853  C  CA  . VAL A 1 125 ? 15.728  5.513   21.830 1.00 22.44 ? 119 VAL A CA  1 
ATOM   854  C  C   . VAL A 1 125 ? 17.176  5.987   21.698 1.00 28.95 ? 119 VAL A C   1 
ATOM   855  O  O   . VAL A 1 125 ? 17.773  6.468   22.672 1.00 25.75 ? 119 VAL A O   1 
ATOM   856  C  CB  . VAL A 1 125 ? 14.765  6.704   21.801 1.00 26.72 ? 119 VAL A CB  1 
ATOM   857  C  CG1 . VAL A 1 125 ? 15.133  7.715   22.855 1.00 32.93 ? 119 VAL A CG1 1 
ATOM   858  C  CG2 . VAL A 1 125 ? 14.773  7.320   20.386 1.00 32.53 ? 119 VAL A CG2 1 
ATOM   859  N  N   . HIS A 1 126 ? 17.732  5.852   20.490 1.00 26.53 ? 120 HIS A N   1 
ATOM   860  C  CA  . HIS A 1 126 ? 19.144  6.171   20.253 1.00 26.83 ? 120 HIS A CA  1 
ATOM   861  C  C   . HIS A 1 126 ? 19.567  7.474   19.604 1.00 28.86 ? 120 HIS A C   1 
ATOM   862  O  O   . HIS A 1 126 ? 18.783  8.207   19.001 1.00 28.51 ? 120 HIS A O   1 
ATOM   863  C  CB  . HIS A 1 126 ? 19.789  5.026   19.465 1.00 22.83 ? 120 HIS A CB  1 
ATOM   864  C  CG  . HIS A 1 126 ? 19.777  3.717   20.188 1.00 26.80 ? 120 HIS A CG  1 
ATOM   865  N  ND1 . HIS A 1 126 ? 20.910  3.154   20.739 1.00 27.94 ? 120 HIS A ND1 1 
ATOM   866  C  CD2 . HIS A 1 126 ? 18.770  2.848   20.435 1.00 32.50 ? 120 HIS A CD2 1 
ATOM   867  C  CE1 . HIS A 1 126 ? 20.604  1.990   21.286 1.00 27.55 ? 120 HIS A CE1 1 
ATOM   868  N  NE2 . HIS A 1 126 ? 19.311  1.780   21.116 1.00 25.82 ? 120 HIS A NE2 1 
ATOM   869  N  N   . GLU A 1 127 ? 20.866  7.724   19.724 1.00 29.79 ? 121 GLU A N   1 
ATOM   870  C  CA  . GLU A 1 127 ? 21.503  8.901   19.166 1.00 34.66 ? 121 GLU A CA  1 
ATOM   871  C  C   . GLU A 1 127 ? 21.531  8.917   17.632 1.00 33.76 ? 121 GLU A C   1 
ATOM   872  O  O   . GLU A 1 127 ? 21.298  9.955   17.023 1.00 36.70 ? 121 GLU A O   1 
ATOM   873  C  CB  . GLU A 1 127 ? 22.936  8.979   19.684 1.00 45.75 ? 121 GLU A CB  1 
ATOM   874  C  CG  . GLU A 1 127 ? 23.790  9.982   18.946 1.00 51.89 ? 121 GLU A CG  1 
ATOM   875  C  CD  . GLU A 1 127 ? 25.261  9.834   19.263 1.00 59.02 ? 121 GLU A CD  1 
ATOM   876  O  OE1 . GLU A 1 127 ? 26.087  10.406  18.519 1.00 72.11 ? 121 GLU A OE1 1 
ATOM   877  O  OE2 . GLU A 1 127 ? 25.594  9.151   20.252 1.00 46.86 ? 121 GLU A OE2 1 
ATOM   878  N  N   . LYS A 1 128 ? 21.809  7.771   17.010 1.00 34.92 ? 122 LYS A N   1 
ATOM   879  C  CA  . LYS A 1 128 ? 21.886  7.694   15.539 1.00 39.61 ? 122 LYS A CA  1 
ATOM   880  C  C   . LYS A 1 128 ? 20.819  6.753   14.969 1.00 35.26 ? 122 LYS A C   1 
ATOM   881  O  O   . LYS A 1 128 ? 20.052  6.140   15.705 1.00 38.01 ? 122 LYS A O   1 
ATOM   882  C  CB  . LYS A 1 128 ? 23.244  7.139   15.083 1.00 42.02 ? 122 LYS A CB  1 
ATOM   883  C  CG  . LYS A 1 128 ? 24.499  7.684   15.745 1.00 58.58 ? 122 LYS A CG  1 
ATOM   884  C  CD  . LYS A 1 128 ? 25.692  6.802   15.326 1.00 52.04 ? 122 LYS A CD  1 
ATOM   885  C  CE  . LYS A 1 128 ? 26.957  7.133   16.091 1.00 66.69 ? 122 LYS A CE  1 
ATOM   886  N  NZ  . LYS A 1 128 ? 28.032  6.124   15.829 1.00 71.06 ? 122 LYS A NZ  1 
ATOM   887  N  N   . ALA A 1 129 ? 20.805  6.623   13.647 1.00 34.10 ? 123 ALA A N   1 
ATOM   888  C  CA  . ALA A 1 129 ? 19.862  5.737   12.974 1.00 32.93 ? 123 ALA A CA  1 
ATOM   889  C  C   . ALA A 1 129 ? 20.296  4.299   13.165 1.00 30.72 ? 123 ALA A C   1 
ATOM   890  O  O   . ALA A 1 129 ? 21.486  4.015   13.355 1.00 32.59 ? 123 ALA A O   1 
ATOM   891  C  CB  . ALA A 1 129 ? 19.834  6.047   11.483 1.00 32.63 ? 123 ALA A CB  1 
ATOM   892  N  N   . ASP A 1 130 ? 19.329  3.393   13.122 1.00 28.29 ? 124 ASP A N   1 
ATOM   893  C  CA  . ASP A 1 130 ? 19.604  1.973   13.215 1.00 31.58 ? 124 ASP A CA  1 
ATOM   894  C  C   . ASP A 1 130 ? 19.910  1.578   11.769 1.00 35.51 ? 124 ASP A C   1 
ATOM   895  O  O   . ASP A 1 130 ? 19.090  1.858   10.900 1.00 33.20 ? 124 ASP A O   1 
ATOM   896  C  CB  . ASP A 1 130 ? 18.338  1.249   13.677 1.00 38.18 ? 124 ASP A CB  1 
ATOM   897  C  CG  . ASP A 1 130 ? 18.541  -0.239  13.873 1.00 33.86 ? 124 ASP A CG  1 
ATOM   898  O  OD1 . ASP A 1 130 ? 19.304  -0.869  13.107 1.00 38.59 ? 124 ASP A OD1 1 
ATOM   899  O  OD2 . ASP A 1 130 ? 17.901  -0.786  14.798 1.00 37.76 ? 124 ASP A OD2 1 
ATOM   900  N  N   . ASP A 1 131 ? 21.051  0.943   11.491 1.00 30.56 ? 125 ASP A N   1 
ATOM   901  C  CA  . ASP A 1 131 ? 21.327  0.561   10.106 1.00 34.75 ? 125 ASP A CA  1 
ATOM   902  C  C   . ASP A 1 131 ? 20.697  -0.768  9.678  1.00 31.85 ? 125 ASP A C   1 
ATOM   903  O  O   . ASP A 1 131 ? 20.990  -1.276  8.589  1.00 38.24 ? 125 ASP A O   1 
ATOM   904  C  CB  . ASP A 1 131 ? 22.820  0.517   9.817  1.00 32.71 ? 125 ASP A CB  1 
ATOM   905  C  CG  . ASP A 1 131 ? 23.494  -0.656  10.456 1.00 35.66 ? 125 ASP A CG  1 
ATOM   906  O  OD1 . ASP A 1 131 ? 22.827  -1.704  10.643 1.00 30.46 ? 125 ASP A OD1 1 
ATOM   907  O  OD2 . ASP A 1 131 ? 24.707  -0.535  10.746 1.00 39.32 ? 125 ASP A OD2 1 
ATOM   908  N  N   . LEU A 1 132 ? 19.862  -1.337  10.546 1.00 28.54 ? 126 LEU A N   1 
ATOM   909  C  CA  . LEU A 1 132 ? 19.125  -2.566  10.247 1.00 38.27 ? 126 LEU A CA  1 
ATOM   910  C  C   . LEU A 1 132 ? 19.960  -3.813  10.007 1.00 37.30 ? 126 LEU A C   1 
ATOM   911  O  O   . LEU A 1 132 ? 19.460  -4.820  9.491  1.00 33.72 ? 126 LEU A O   1 
ATOM   912  C  CB  . LEU A 1 132 ? 18.222  -2.325  9.033  1.00 40.57 ? 126 LEU A CB  1 
ATOM   913  C  CG  . LEU A 1 132 ? 17.492  -0.972  9.024  1.00 47.68 ? 126 LEU A CG  1 
ATOM   914  C  CD1 . LEU A 1 132 ? 16.744  -0.816  7.701  1.00 51.97 ? 126 LEU A CD1 1 
ATOM   915  C  CD2 . LEU A 1 132 ? 16.528  -0.870  10.207 1.00 41.27 ? 126 LEU A CD2 1 
ATOM   916  N  N   . GLY A 1 133 ? 21.227  -3.755  10.389 1.00 34.98 ? 127 GLY A N   1 
ATOM   917  C  CA  . GLY A 1 133 ? 22.088  -4.903  10.210 1.00 34.14 ? 127 GLY A CA  1 
ATOM   918  C  C   . GLY A 1 133 ? 22.615  -4.962  8.788  1.00 41.17 ? 127 GLY A C   1 
ATOM   919  O  O   . GLY A 1 133 ? 23.205  -5.966  8.394  1.00 47.26 ? 127 GLY A O   1 
ATOM   920  N  N   . LYS A 1 134 ? 22.389  -3.912  8.006  1.00 37.65 ? 128 LYS A N   1 
ATOM   921  C  CA  . LYS A 1 134 ? 22.887  -3.893  6.631  1.00 48.66 ? 128 LYS A CA  1 
ATOM   922  C  C   . LYS A 1 134 ? 24.221  -3.137  6.547  1.00 48.27 ? 128 LYS A C   1 
ATOM   923  O  O   . LYS A 1 134 ? 24.681  -2.810  5.459  1.00 45.88 ? 128 LYS A O   1 
ATOM   924  C  CB  . LYS A 1 134 ? 21.897  -3.214  5.682  1.00 52.55 ? 128 LYS A CB  1 
ATOM   925  C  CG  . LYS A 1 134 ? 20.505  -3.815  5.567  1.00 53.79 ? 128 LYS A CG  1 
ATOM   926  C  CD  . LYS A 1 134 ? 19.732  -2.959  4.543  1.00 65.81 ? 128 LYS A CD  1 
ATOM   927  C  CE  . LYS A 1 134 ? 18.232  -3.232  4.474  1.00 64.31 ? 128 LYS A CE  1 
ATOM   928  N  NZ  . LYS A 1 134 ? 17.547  -2.268  3.533  1.00 42.64 ? 128 LYS A NZ  1 
ATOM   929  N  N   . GLY A 1 135 ? 24.841  -2.861  7.691  1.00 41.34 ? 129 GLY A N   1 
ATOM   930  C  CA  . GLY A 1 135 ? 26.101  -2.136  7.682  1.00 38.96 ? 129 GLY A CA  1 
ATOM   931  C  C   . GLY A 1 135 ? 27.307  -2.921  7.202  1.00 45.39 ? 129 GLY A C   1 
ATOM   932  O  O   . GLY A 1 135 ? 27.203  -4.109  6.853  1.00 39.79 ? 129 GLY A O   1 
ATOM   933  N  N   . GLY A 1 136 ? 28.462  -2.258  7.175  1.00 44.49 ? 130 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 136 ? 29.682  -2.924  6.738  1.00 54.44 ? 130 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 136 ? 30.617  -3.359  7.863  1.00 57.85 ? 130 GLY A C   1 
ATOM   936  O  O   . GLY A 1 136 ? 31.835  -3.316  7.703  1.00 55.25 ? 130 GLY A O   1 
ATOM   937  N  N   . ASN A 1 137 ? 30.067  -3.796  8.993  1.00 58.51 ? 131 ASN A N   1 
ATOM   938  C  CA  . ASN A 1 137 ? 30.903  -4.213  10.116 1.00 57.21 ? 131 ASN A CA  1 
ATOM   939  C  C   . ASN A 1 137 ? 30.239  -5.210  11.059 1.00 55.70 ? 131 ASN A C   1 
ATOM   940  O  O   . ASN A 1 137 ? 29.070  -5.546  10.917 1.00 48.18 ? 131 ASN A O   1 
ATOM   941  C  CB  . ASN A 1 137 ? 31.307  -2.994  10.927 1.00 55.12 ? 131 ASN A CB  1 
ATOM   942  C  CG  . ASN A 1 137 ? 30.109  -2.239  11.432 1.00 58.58 ? 131 ASN A CG  1 
ATOM   943  O  OD1 . ASN A 1 137 ? 29.346  -1.679  10.647 1.00 61.36 ? 131 ASN A OD1 1 
ATOM   944  N  ND2 . ASN A 1 137 ? 29.919  -2.236  12.741 1.00 60.80 ? 131 ASN A ND2 1 
ATOM   945  N  N   . GLU A 1 138 ? 31.012  -5.645  12.049 1.00 58.46 ? 132 GLU A N   1 
ATOM   946  C  CA  . GLU A 1 138 ? 30.572  -6.602  13.064 1.00 62.32 ? 132 GLU A CA  1 
ATOM   947  C  C   . GLU A 1 138 ? 29.352  -6.101  13.856 1.00 61.39 ? 132 GLU A C   1 
ATOM   948  O  O   . GLU A 1 138 ? 28.286  -6.737  13.871 1.00 52.23 ? 132 GLU A O   1 
ATOM   949  C  CB  . GLU A 1 138 ? 31.737  -6.866  14.036 1.00 63.85 ? 132 GLU A CB  1 
ATOM   950  C  CG  . GLU A 1 138 ? 31.509  -7.952  15.093 1.00 68.55 ? 132 GLU A CG  1 
ATOM   951  C  CD  . GLU A 1 138 ? 31.876  -9.347  14.600 1.00 70.03 ? 132 GLU A CD  1 
ATOM   952  O  OE1 . GLU A 1 138 ? 31.162  -9.875  13.722 1.00 70.28 ? 132 GLU A OE1 1 
ATOM   953  O  OE2 . GLU A 1 138 ? 32.883  -9.913  15.084 1.00 64.66 ? 132 GLU A OE2 1 
ATOM   954  N  N   . GLU A 1 139 ? 29.530  -4.956  14.510 1.00 52.95 ? 133 GLU A N   1 
ATOM   955  C  CA  . GLU A 1 139 ? 28.494  -4.360  15.351 1.00 57.58 ? 133 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 139 ? 27.130  -4.161  14.659 1.00 48.32 ? 133 GLU A C   1 
ATOM   957  O  O   . GLU A 1 139 ? 26.093  -4.125  15.323 1.00 46.85 ? 133 GLU A O   1 
ATOM   958  C  CB  . GLU A 1 139 ? 29.010  -3.029  15.929 1.00 58.41 ? 133 GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 139 ? 28.023  -2.271  16.831 1.00 61.51 ? 133 GLU A CG  1 
ATOM   960  C  CD  . GLU A 1 139 ? 28.206  -2.541  18.327 1.00 67.51 ? 133 GLU A CD  1 
ATOM   961  O  OE1 . GLU A 1 139 ? 28.086  -3.706  18.762 1.00 64.45 ? 133 GLU A OE1 1 
ATOM   962  O  OE2 . GLU A 1 139 ? 28.463  -1.575  19.075 1.00 67.25 ? 133 GLU A OE2 1 
ATOM   963  N  N   . SER A 1 140 ? 27.120  -4.052  13.336 1.00 35.88 ? 134 SER A N   1 
ATOM   964  C  CA  . SER A 1 140 ? 25.860  -3.859  12.635 1.00 40.07 ? 134 SER A CA  1 
ATOM   965  C  C   . SER A 1 140 ? 24.876  -4.997  12.880 1.00 45.62 ? 134 SER A C   1 
ATOM   966  O  O   . SER A 1 140 ? 23.658  -4.766  12.988 1.00 34.58 ? 134 SER A O   1 
ATOM   967  C  CB  . SER A 1 140 ? 26.083  -3.726  11.136 1.00 36.89 ? 134 SER A CB  1 
ATOM   968  O  OG  . SER A 1 140 ? 24.826  -3.686  10.492 1.00 39.48 ? 134 SER A OG  1 
ATOM   969  N  N   . THR A 1 141 ? 25.415  -6.215  12.979 1.00 38.62 ? 135 THR A N   1 
ATOM   970  C  CA  . THR A 1 141 ? 24.614  -7.417  13.180 1.00 39.90 ? 135 THR A CA  1 
ATOM   971  C  C   . THR A 1 141 ? 24.167  -7.554  14.622 1.00 39.04 ? 135 THR A C   1 
ATOM   972  O  O   . THR A 1 141 ? 23.380  -8.443  14.961 1.00 36.48 ? 135 THR A O   1 
ATOM   973  C  CB  . THR A 1 141 ? 25.411  -8.694  12.788 1.00 47.55 ? 135 THR A CB  1 
ATOM   974  O  OG1 . THR A 1 141 ? 26.469  -8.920  13.732 1.00 53.74 ? 135 THR A OG1 1 
ATOM   975  C  CG2 . THR A 1 141 ? 26.026  -8.529  11.417 1.00 50.83 ? 135 THR A CG2 1 
ATOM   976  N  N   . LYS A 1 142 ? 24.667  -6.669  15.471 1.00 35.25 ? 136 LYS A N   1 
ATOM   977  C  CA  . LYS A 1 142 ? 24.316  -6.692  16.878 1.00 37.59 ? 136 LYS A CA  1 
ATOM   978  C  C   . LYS A 1 142 ? 23.467  -5.527  17.364 1.00 40.11 ? 136 LYS A C   1 
ATOM   979  O  O   . LYS A 1 142 ? 22.479  -5.730  18.052 1.00 42.19 ? 136 LYS A O   1 
ATOM   980  C  CB  . LYS A 1 142 ? 25.582  -6.750  17.733 1.00 46.15 ? 136 LYS A CB  1 
ATOM   981  C  CG  . LYS A 1 142 ? 26.385  -8.029  17.567 1.00 50.20 ? 136 LYS A CG  1 
ATOM   982  C  CD  . LYS A 1 142 ? 27.422  -8.171  18.673 1.00 51.62 ? 136 LYS A CD  1 
ATOM   983  C  CE  . LYS A 1 142 ? 26.763  -8.215  20.043 1.00 60.98 ? 136 LYS A CE  1 
ATOM   984  N  NZ  . LYS A 1 142 ? 27.742  -8.401  21.151 1.00 68.59 ? 136 LYS A NZ  1 
ATOM   985  N  N   . THR A 1 143 ? 23.851  -4.308  17.001 1.00 37.50 ? 137 THR A N   1 
ATOM   986  C  CA  . THR A 1 143 ? 23.148  -3.120  17.463 1.00 39.40 ? 137 THR A CA  1 
ATOM   987  C  C   . THR A 1 143 ? 22.638  -2.209  16.351 1.00 36.02 ? 137 THR A C   1 
ATOM   988  O  O   . THR A 1 143 ? 21.902  -1.252  16.622 1.00 29.10 ? 137 THR A O   1 
ATOM   989  C  CB  . THR A 1 143 ? 24.076  -2.249  18.345 1.00 40.13 ? 137 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 143 ? 25.128  -1.725  17.531 1.00 38.17 ? 137 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 143 ? 24.694  -3.065  19.457 1.00 41.75 ? 137 THR A CG2 1 
ATOM   992  N  N   . GLY A 1 144 ? 23.041  -2.489  15.114 1.00 33.50 ? 138 GLY A N   1 
ATOM   993  C  CA  . GLY A 1 144 ? 22.648  -1.638  14.003 1.00 33.04 ? 138 GLY A CA  1 
ATOM   994  C  C   . GLY A 1 144 ? 23.418  -0.317  14.050 1.00 28.62 ? 138 GLY A C   1 
ATOM   995  O  O   . GLY A 1 144 ? 23.079  0.634   13.352 1.00 33.02 ? 138 GLY A O   1 
ATOM   996  N  N   . ASN A 1 145 ? 24.451  -0.247  14.891 1.00 36.56 ? 139 ASN A N   1 
ATOM   997  C  CA  . ASN A 1 145 ? 25.233  0.986   15.015 1.00 30.18 ? 139 ASN A CA  1 
ATOM   998  C  C   . ASN A 1 145 ? 24.339  2.206   15.350 1.00 33.53 ? 139 ASN A C   1 
ATOM   999  O  O   . ASN A 1 145 ? 24.585  3.316   14.865 1.00 29.80 ? 139 ASN A O   1 
ATOM   1000 C  CB  . ASN A 1 145 ? 25.978  1.255   13.705 1.00 37.59 ? 139 ASN A CB  1 
ATOM   1001 C  CG  . ASN A 1 145 ? 27.057  0.232   13.434 1.00 44.93 ? 139 ASN A CG  1 
ATOM   1002 O  OD1 . ASN A 1 145 ? 28.000  0.105   14.209 1.00 35.89 ? 139 ASN A OD1 1 
ATOM   1003 N  ND2 . ASN A 1 145 ? 26.921  -0.510  12.334 1.00 36.03 ? 139 ASN A ND2 1 
ATOM   1004 N  N   . ALA A 1 146 ? 23.300  1.998   16.154 1.00 35.38 ? 140 ALA A N   1 
ATOM   1005 C  CA  . ALA A 1 146 ? 22.393  3.090   16.554 1.00 34.88 ? 140 ALA A CA  1 
ATOM   1006 C  C   . ALA A 1 146 ? 23.071  4.074   17.526 1.00 32.35 ? 140 ALA A C   1 
ATOM   1007 O  O   . ALA A 1 146 ? 22.492  5.086   17.904 1.00 33.40 ? 140 ALA A O   1 
ATOM   1008 C  CB  . ALA A 1 146 ? 21.150  2.523   17.207 1.00 31.50 ? 140 ALA A CB  1 
ATOM   1009 N  N   . GLY A 1 147 ? 24.293  3.759   17.947 1.00 37.50 ? 141 GLY A N   1 
ATOM   1010 C  CA  . GLY A 1 147 ? 25.010  4.656   18.834 1.00 38.13 ? 141 GLY A CA  1 
ATOM   1011 C  C   . GLY A 1 147 ? 24.481  4.697   20.249 1.00 36.11 ? 141 GLY A C   1 
ATOM   1012 O  O   . GLY A 1 147 ? 23.753  3.799   20.667 1.00 29.62 ? 141 GLY A O   1 
ATOM   1013 N  N   . SER A 1 148 ? 24.817  5.757   20.980 1.00 27.22 ? 142 SER A N   1 
ATOM   1014 C  CA  . SER A 1 148 ? 24.409  5.862   22.370 1.00 33.19 ? 142 SER A CA  1 
ATOM   1015 C  C   . SER A 1 148 ? 22.897  5.899   22.599 1.00 35.12 ? 142 SER A C   1 
ATOM   1016 O  O   . SER A 1 148 ? 22.093  6.167   21.701 1.00 32.72 ? 142 SER A O   1 
ATOM   1017 C  CB  . SER A 1 148 ? 25.069  7.082   23.042 1.00 41.24 ? 142 SER A CB  1 
ATOM   1018 O  OG  . SER A 1 148 ? 24.399  8.287   22.722 1.00 50.52 ? 142 SER A OG  1 
ATOM   1019 N  N   . ARG A 1 149 ? 22.532  5.621   23.835 1.00 28.18 ? 143 ARG A N   1 
ATOM   1020 C  CA  . ARG A 1 149 ? 21.147  5.588   24.239 1.00 35.71 ? 143 ARG A CA  1 
ATOM   1021 C  C   . ARG A 1 149 ? 20.783  6.946   24.813 1.00 34.38 ? 143 ARG A C   1 
ATOM   1022 O  O   . ARG A 1 149 ? 21.312  7.340   25.848 1.00 33.81 ? 143 ARG A O   1 
ATOM   1023 C  CB  . ARG A 1 149 ? 20.979  4.472   25.276 1.00 33.77 ? 143 ARG A CB  1 
ATOM   1024 C  CG  . ARG A 1 149 ? 21.406  3.118   24.718 1.00 30.60 ? 143 ARG A CG  1 
ATOM   1025 C  CD  . ARG A 1 149 ? 21.468  2.021   25.754 1.00 34.02 ? 143 ARG A CD  1 
ATOM   1026 N  NE  . ARG A 1 149 ? 22.103  0.828   25.186 1.00 26.46 ? 143 ARG A NE  1 
ATOM   1027 C  CZ  . ARG A 1 149 ? 22.080  -0.376  25.746 1.00 24.05 ? 143 ARG A CZ  1 
ATOM   1028 N  NH1 . ARG A 1 149 ? 21.451  -0.568  26.889 1.00 28.28 ? 143 ARG A NH1 1 
ATOM   1029 N  NH2 . ARG A 1 149 ? 22.704  -1.397  25.167 1.00 34.21 ? 143 ARG A NH2 1 
ATOM   1030 N  N   . LEU A 1 150 ? 19.877  7.649   24.142 1.00 27.66 ? 144 LEU A N   1 
ATOM   1031 C  CA  . LEU A 1 150 ? 19.450  8.991   24.569 1.00 30.59 ? 144 LEU A CA  1 
ATOM   1032 C  C   . LEU A 1 150 ? 18.370  9.031   25.657 1.00 30.05 ? 144 LEU A C   1 
ATOM   1033 O  O   . LEU A 1 150 ? 18.313  9.954   26.466 1.00 26.86 ? 144 LEU A O   1 
ATOM   1034 C  CB  . LEU A 1 150 ? 18.970  9.780   23.352 1.00 28.45 ? 144 LEU A CB  1 
ATOM   1035 C  CG  . LEU A 1 150 ? 20.044  10.180  22.330 1.00 29.24 ? 144 LEU A CG  1 
ATOM   1036 C  CD1 . LEU A 1 150 ? 19.371  10.966  21.193 1.00 26.67 ? 144 LEU A CD1 1 
ATOM   1037 C  CD2 . LEU A 1 150 ? 21.098  11.054  22.994 1.00 36.58 ? 144 LEU A CD2 1 
ATOM   1038 N  N   . ALA A 1 151 ? 17.505  8.031   25.675 1.00 25.46 ? 145 ALA A N   1 
ATOM   1039 C  CA  . ALA A 1 151 ? 16.466  7.987   26.673 1.00 25.20 ? 145 ALA A CA  1 
ATOM   1040 C  C   . ALA A 1 151 ? 15.877  6.613   26.668 1.00 23.45 ? 145 ALA A C   1 
ATOM   1041 O  O   . ALA A 1 151 ? 15.967  5.898   25.679 1.00 31.86 ? 145 ALA A O   1 
ATOM   1042 C  CB  . ALA A 1 151 ? 15.377  9.050   26.367 1.00 33.27 ? 145 ALA A CB  1 
ATOM   1043 N  N   . CYS A 1 152 ? 15.263  6.249   27.781 1.00 27.33 ? 146 CYS A N   1 
ATOM   1044 C  CA  . CYS A 1 152 ? 14.682  4.933   27.920 1.00 28.76 ? 146 CYS A CA  1 
ATOM   1045 C  C   . CYS A 1 152 ? 13.706  4.922   29.082 1.00 28.52 ? 146 CYS A C   1 
ATOM   1046 O  O   . CYS A 1 152 ? 13.596  5.885   29.844 1.00 27.30 ? 146 CYS A O   1 
ATOM   1047 C  CB  . CYS A 1 152 ? 15.803  3.918   28.178 1.00 29.15 ? 146 CYS A CB  1 
ATOM   1048 S  SG  . CYS A 1 152 ? 16.815  4.311   29.640 1.00 36.09 ? 146 CYS A SG  1 
ATOM   1049 N  N   . GLY A 1 153 ? 13.002  3.812   29.209 1.00 30.85 ? 147 GLY A N   1 
ATOM   1050 C  CA  . GLY A 1 153 ? 12.048  3.645   30.285 1.00 34.57 ? 147 GLY A CA  1 
ATOM   1051 C  C   . GLY A 1 153 ? 11.575  2.209   30.302 1.00 26.80 ? 147 GLY A C   1 
ATOM   1052 O  O   . GLY A 1 153 ? 11.592  1.542   29.268 1.00 27.37 ? 147 GLY A O   1 
ATOM   1053 N  N   . VAL A 1 154 ? 11.170  1.731   31.471 1.00 24.32 ? 148 VAL A N   1 
ATOM   1054 C  CA  . VAL A 1 154 ? 10.671  0.374   31.626 1.00 22.70 ? 148 VAL A CA  1 
ATOM   1055 C  C   . VAL A 1 154 ? 9.207   0.331   31.171 1.00 25.95 ? 148 VAL A C   1 
ATOM   1056 O  O   . VAL A 1 154 ? 8.394   1.168   31.564 1.00 30.69 ? 148 VAL A O   1 
ATOM   1057 C  CB  . VAL A 1 154 ? 10.750  -0.076  33.101 1.00 31.24 ? 148 VAL A CB  1 
ATOM   1058 C  CG1 . VAL A 1 154 ? 10.345  -1.553  33.241 1.00 29.02 ? 148 VAL A CG1 1 
ATOM   1059 C  CG2 . VAL A 1 154 ? 12.179  0.150   33.634 1.00 32.66 ? 148 VAL A CG2 1 
ATOM   1060 N  N   . ILE A 1 155 ? 8.880   -0.666  30.365 1.00 26.02 ? 149 ILE A N   1 
ATOM   1061 C  CA  . ILE A 1 155 ? 7.521   -0.814  29.859 1.00 33.77 ? 149 ILE A CA  1 
ATOM   1062 C  C   . ILE A 1 155 ? 6.604   -1.291  31.000 1.00 25.23 ? 149 ILE A C   1 
ATOM   1063 O  O   . ILE A 1 155 ? 6.781   -2.375  31.553 1.00 21.27 ? 149 ILE A O   1 
ATOM   1064 C  CB  . ILE A 1 155 ? 7.516   -1.805  28.657 1.00 32.17 ? 149 ILE A CB  1 
ATOM   1065 C  CG1 . ILE A 1 155 ? 8.466   -1.281  27.561 1.00 31.78 ? 149 ILE A CG1 1 
ATOM   1066 C  CG2 . ILE A 1 155 ? 6.126   -1.973  28.106 1.00 30.42 ? 149 ILE A CG2 1 
ATOM   1067 C  CD1 . ILE A 1 155 ? 8.707   -2.247  26.389 1.00 28.28 ? 149 ILE A CD1 1 
ATOM   1068 N  N   . GLY A 1 156 ? 5.607   -0.477  31.340 1.00 26.12 ? 150 GLY A N   1 
ATOM   1069 C  CA  . GLY A 1 156 ? 4.723   -0.872  32.433 1.00 32.16 ? 150 GLY A CA  1 
ATOM   1070 C  C   . GLY A 1 156 ? 3.282   -1.169  32.046 1.00 35.71 ? 150 GLY A C   1 
ATOM   1071 O  O   . GLY A 1 156 ? 2.825   -0.794  30.968 1.00 27.34 ? 150 GLY A O   1 
ATOM   1072 N  N   . ILE A 1 157 ? 2.572   -1.854  32.930 1.00 30.01 ? 151 ILE A N   1 
ATOM   1073 C  CA  . ILE A 1 157 ? 1.180   -2.208  32.680 1.00 36.63 ? 151 ILE A CA  1 
ATOM   1074 C  C   . ILE A 1 157 ? 0.314   -0.956  32.782 1.00 35.18 ? 151 ILE A C   1 
ATOM   1075 O  O   . ILE A 1 157 ? 0.540   -0.119  33.648 1.00 31.72 ? 151 ILE A O   1 
ATOM   1076 C  CB  . ILE A 1 157 ? 0.708   -3.246  33.715 1.00 39.40 ? 151 ILE A CB  1 
ATOM   1077 C  CG1 . ILE A 1 157 ? 1.330   -4.609  33.385 1.00 39.82 ? 151 ILE A CG1 1 
ATOM   1078 C  CG2 . ILE A 1 157 ? -0.830  -3.282  33.772 1.00 32.67 ? 151 ILE A CG2 1 
ATOM   1079 C  CD1 . ILE A 1 157 ? 1.212   -5.614  34.515 1.00 46.94 ? 151 ILE A CD1 1 
ATOM   1080 N  N   . ALA A 1 158 ? -0.661  -0.805  31.895 1.00 36.88 ? 152 ALA A N   1 
ATOM   1081 C  CA  . ALA A 1 158 ? -1.533  0.373   31.967 1.00 36.58 ? 152 ALA A CA  1 
ATOM   1082 C  C   . ALA A 1 158 ? -3.016  -0.018  32.054 1.00 42.73 ? 152 ALA A C   1 
ATOM   1083 O  O   . ALA A 1 158 ? -3.321  -1.203  31.839 1.00 49.64 ? 152 ALA A O   1 
ATOM   1084 C  CB  . ALA A 1 158 ? -1.298  1.263   30.769 1.00 38.84 ? 152 ALA A CB  1 
ATOM   1085 N  N   . ALA B 1 7   ? 13.929  -18.290 40.522 1.00 67.51 ? 1   ALA B N   1 
ATOM   1086 C  CA  . ALA B 1 7   ? 15.248  -17.600 40.602 1.00 67.33 ? 1   ALA B CA  1 
ATOM   1087 C  C   . ALA B 1 7   ? 15.190  -16.264 39.858 1.00 59.67 ? 1   ALA B C   1 
ATOM   1088 O  O   . ALA B 1 7   ? 16.202  -15.734 39.406 1.00 51.78 ? 1   ALA B O   1 
ATOM   1089 C  CB  . ALA B 1 7   ? 16.344  -18.498 40.004 1.00 69.47 ? 1   ALA B CB  1 
ATOM   1090 N  N   . THR B 1 8   ? 13.997  -15.710 39.738 1.00 52.99 ? 2   THR B N   1 
ATOM   1091 C  CA  . THR B 1 8   ? 13.873  -14.455 39.033 1.00 42.86 ? 2   THR B CA  1 
ATOM   1092 C  C   . THR B 1 8   ? 14.267  -13.253 39.912 1.00 32.91 ? 2   THR B C   1 
ATOM   1093 O  O   . THR B 1 8   ? 14.203  -13.278 41.152 1.00 28.81 ? 2   THR B O   1 
ATOM   1094 C  CB  . THR B 1 8   ? 12.449  -14.331 38.433 1.00 48.97 ? 2   THR B CB  1 
ATOM   1095 O  OG1 . THR B 1 8   ? 12.308  -13.072 37.765 1.00 71.15 ? 2   THR B OG1 1 
ATOM   1096 C  CG2 . THR B 1 8   ? 11.404  -14.467 39.512 1.00 62.93 ? 2   THR B CG2 1 
ATOM   1097 N  N   . LYS B 1 9   ? 14.737  -12.216 39.239 1.00 27.52 ? 3   LYS B N   1 
ATOM   1098 C  CA  . LYS B 1 9   ? 15.186  -10.991 39.876 1.00 24.60 ? 3   LYS B CA  1 
ATOM   1099 C  C   . LYS B 1 9   ? 14.505  -9.802  39.204 1.00 26.31 ? 3   LYS B C   1 
ATOM   1100 O  O   . LYS B 1 9   ? 14.251  -9.820  37.999 1.00 29.18 ? 3   LYS B O   1 
ATOM   1101 C  CB  . LYS B 1 9   ? 16.686  -10.825 39.680 1.00 31.00 ? 3   LYS B CB  1 
ATOM   1102 C  CG  . LYS B 1 9   ? 17.533  -11.921 40.242 1.00 47.83 ? 3   LYS B CG  1 
ATOM   1103 C  CD  . LYS B 1 9   ? 18.990  -11.608 39.936 1.00 59.63 ? 3   LYS B CD  1 
ATOM   1104 C  CE  . LYS B 1 9   ? 19.935  -12.561 40.624 1.00 53.68 ? 3   LYS B CE  1 
ATOM   1105 N  NZ  . LYS B 1 9   ? 21.341  -12.096 40.460 1.00 65.04 ? 3   LYS B NZ  1 
ATOM   1106 N  N   . ALA B 1 10  ? 14.262  -8.763  39.986 1.00 24.72 ? 4   ALA B N   1 
ATOM   1107 C  CA  . ALA B 1 10  ? 13.660  -7.535  39.483 1.00 26.04 ? 4   ALA B CA  1 
ATOM   1108 C  C   . ALA B 1 10  ? 14.315  -6.332  40.168 1.00 32.26 ? 4   ALA B C   1 
ATOM   1109 O  O   . ALA B 1 10  ? 14.918  -6.446  41.249 1.00 24.59 ? 4   ALA B O   1 
ATOM   1110 C  CB  . ALA B 1 10  ? 12.181  -7.536  39.749 1.00 23.29 ? 4   ALA B CB  1 
ATOM   1111 N  N   . VAL B 1 11  ? 14.208  -5.178  39.527 1.00 21.23 ? 5   VAL B N   1 
ATOM   1112 C  CA  . VAL B 1 11  ? 14.766  -3.956  40.085 1.00 21.79 ? 5   VAL B CA  1 
ATOM   1113 C  C   . VAL B 1 11  ? 13.842  -2.803  39.729 1.00 26.46 ? 5   VAL B C   1 
ATOM   1114 O  O   . VAL B 1 11  ? 13.113  -2.855  38.722 1.00 25.37 ? 5   VAL B O   1 
ATOM   1115 C  CB  . VAL B 1 11  ? 16.167  -3.692  39.531 1.00 23.31 ? 5   VAL B CB  1 
ATOM   1116 C  CG1 . VAL B 1 11  ? 16.090  -3.384  38.043 1.00 23.61 ? 5   VAL B CG1 1 
ATOM   1117 C  CG2 . VAL B 1 11  ? 16.849  -2.533  40.303 1.00 22.74 ? 5   VAL B CG2 1 
ATOM   1118 N  N   . CYS B 1 12  ? 13.872  -1.784  40.576 1.00 21.40 ? 6   CYS B N   1 
ATOM   1119 C  CA  . CYS B 1 12  ? 13.088  -0.585  40.415 1.00 22.74 ? 6   CYS B CA  1 
ATOM   1120 C  C   . CYS B 1 12  ? 13.992  0.576   40.782 1.00 27.43 ? 6   CYS B C   1 
ATOM   1121 O  O   . CYS B 1 12  ? 14.730  0.516   41.761 1.00 28.58 ? 6   CYS B O   1 
ATOM   1122 C  CB  . CYS B 1 12  ? 11.896  -0.579  41.376 1.00 21.36 ? 6   CYS B CB  1 
ATOM   1123 S  SG  . CYS B 1 12  ? 10.881  0.827   41.089 1.00 34.66 ? 6   CYS B SG  1 
ATOM   1124 N  N   . VAL B 1 13  ? 13.949  1.630   39.985 1.00 27.33 ? 7   VAL B N   1 
ATOM   1125 C  CA  . VAL B 1 13  ? 14.733  2.825   40.284 1.00 30.97 ? 7   VAL B CA  1 
ATOM   1126 C  C   . VAL B 1 13  ? 13.659  3.830   40.644 1.00 28.48 ? 7   VAL B C   1 
ATOM   1127 O  O   . VAL B 1 13  ? 12.733  4.052   39.868 1.00 26.72 ? 7   VAL B O   1 
ATOM   1128 C  CB  . VAL B 1 13  ? 15.559  3.286   39.040 1.00 27.23 ? 7   VAL B CB  1 
ATOM   1129 C  CG1 . VAL B 1 13  ? 16.110  4.685   39.234 1.00 27.88 ? 7   VAL B CG1 1 
ATOM   1130 C  CG2 . VAL B 1 13  ? 16.692  2.301   38.799 1.00 25.56 ? 7   VAL B CG2 1 
ATOM   1131 N  N   . LEU B 1 14  ? 13.748  4.396   41.841 1.00 20.38 ? 8   LEU B N   1 
ATOM   1132 C  CA  . LEU B 1 14  ? 12.763  5.376   42.282 1.00 24.47 ? 8   LEU B CA  1 
ATOM   1133 C  C   . LEU B 1 14  ? 13.199  6.811   42.059 1.00 29.55 ? 8   LEU B C   1 
ATOM   1134 O  O   . LEU B 1 14  ? 14.302  7.190   42.438 1.00 30.94 ? 8   LEU B O   1 
ATOM   1135 C  CB  . LEU B 1 14  ? 12.470  5.179   43.764 1.00 25.08 ? 8   LEU B CB  1 
ATOM   1136 C  CG  . LEU B 1 14  ? 11.795  3.863   44.157 1.00 38.99 ? 8   LEU B CG  1 
ATOM   1137 C  CD1 . LEU B 1 14  ? 12.387  3.394   45.483 1.00 32.92 ? 8   LEU B CD1 1 
ATOM   1138 C  CD2 . LEU B 1 14  ? 10.277  4.048   44.249 1.00 35.59 ? 8   LEU B CD2 1 
ATOM   1139 N  N   . LYS B 1 15  ? 12.323  7.613   41.454 1.00 28.28 ? 9   LYS B N   1 
ATOM   1140 C  CA  . LYS B 1 15  ? 12.609  9.030   41.231 1.00 33.47 ? 9   LYS B CA  1 
ATOM   1141 C  C   . LYS B 1 15  ? 11.280  9.780   41.281 1.00 33.46 ? 9   LYS B C   1 
ATOM   1142 O  O   . LYS B 1 15  ? 10.216  9.179   41.136 1.00 28.85 ? 9   LYS B O   1 
ATOM   1143 C  CB  . LYS B 1 15  ? 13.284  9.255   39.863 1.00 38.23 ? 9   LYS B CB  1 
ATOM   1144 C  CG  . LYS B 1 15  ? 14.687  8.666   39.753 1.00 43.04 ? 9   LYS B CG  1 
ATOM   1145 C  CD  . LYS B 1 15  ? 15.374  9.054   38.451 1.00 53.40 ? 9   LYS B CD  1 
ATOM   1146 C  CE  . LYS B 1 15  ? 16.779  8.456   38.390 1.00 59.27 ? 9   LYS B CE  1 
ATOM   1147 N  NZ  . LYS B 1 15  ? 17.525  8.771   37.135 1.00 55.42 ? 9   LYS B NZ  1 
ATOM   1148 N  N   . GLY B 1 16  ? 11.339  11.082  41.510 1.00 30.73 ? 10  GLY B N   1 
ATOM   1149 C  CA  . GLY B 1 16  ? 10.109  11.867  41.555 1.00 36.19 ? 10  GLY B CA  1 
ATOM   1150 C  C   . GLY B 1 16  ? 10.369  13.324  41.222 1.00 34.85 ? 10  GLY B C   1 
ATOM   1151 O  O   . GLY B 1 16  ? 11.391  13.636  40.614 1.00 31.76 ? 10  GLY B O   1 
ATOM   1152 N  N   . ASP B 1 17  ? 9.460   14.213  41.618 1.00 35.96 ? 11  ASP B N   1 
ATOM   1153 C  CA  . ASP B 1 17  ? 9.617   15.640  41.359 1.00 46.55 ? 11  ASP B CA  1 
ATOM   1154 C  C   . ASP B 1 17  ? 10.553  16.286  42.367 1.00 46.63 ? 11  ASP B C   1 
ATOM   1155 O  O   . ASP B 1 17  ? 11.170  17.322  42.104 1.00 47.17 ? 11  ASP B O   1 
ATOM   1156 C  CB  . ASP B 1 17  ? 8.255   16.331  41.392 1.00 51.53 ? 11  ASP B CB  1 
ATOM   1157 C  CG  . ASP B 1 17  ? 7.521   16.202  40.079 1.00 60.39 ? 11  ASP B CG  1 
ATOM   1158 O  OD1 . ASP B 1 17  ? 8.051   15.495  39.194 1.00 58.16 ? 11  ASP B OD1 1 
ATOM   1159 O  OD2 . ASP B 1 17  ? 6.433   16.805  39.928 1.00 67.55 ? 11  ASP B OD2 1 
ATOM   1160 N  N   . GLY B 1 18  ? 10.652  15.656  43.524 1.00 40.46 ? 12  GLY B N   1 
ATOM   1161 C  CA  . GLY B 1 18  ? 11.514  16.165  44.564 1.00 43.97 ? 12  GLY B CA  1 
ATOM   1162 C  C   . GLY B 1 18  ? 12.913  15.605  44.458 1.00 36.79 ? 12  GLY B C   1 
ATOM   1163 O  O   . GLY B 1 18  ? 13.359  15.220  43.378 1.00 39.03 ? 12  GLY B O   1 
ATOM   1164 N  N   . PRO B 1 19  ? 13.632  15.535  45.583 1.00 40.86 ? 13  PRO B N   1 
ATOM   1165 C  CA  . PRO B 1 19  ? 14.995  15.012  45.547 1.00 33.04 ? 13  PRO B CA  1 
ATOM   1166 C  C   . PRO B 1 19  ? 15.103  13.526  45.882 1.00 34.85 ? 13  PRO B C   1 
ATOM   1167 O  O   . PRO B 1 19  ? 16.201  12.988  45.898 1.00 28.77 ? 13  PRO B O   1 
ATOM   1168 C  CB  . PRO B 1 19  ? 15.693  15.864  46.588 1.00 40.41 ? 13  PRO B CB  1 
ATOM   1169 C  CG  . PRO B 1 19  ? 14.634  15.890  47.689 1.00 43.51 ? 13  PRO B CG  1 
ATOM   1170 C  CD  . PRO B 1 19  ? 13.310  16.079  46.919 1.00 39.41 ? 13  PRO B CD  1 
ATOM   1171 N  N   . VAL B 1 20  ? 13.975  12.866  46.150 1.00 29.58 ? 14  VAL B N   1 
ATOM   1172 C  CA  . VAL B 1 20  ? 14.009  11.456  46.517 1.00 31.93 ? 14  VAL B CA  1 
ATOM   1173 C  C   . VAL B 1 20  ? 14.421  10.523  45.379 1.00 34.49 ? 14  VAL B C   1 
ATOM   1174 O  O   . VAL B 1 20  ? 13.878  10.579  44.275 1.00 42.72 ? 14  VAL B O   1 
ATOM   1175 C  CB  . VAL B 1 20  ? 12.634  10.978  47.088 1.00 27.78 ? 14  VAL B CB  1 
ATOM   1176 C  CG1 . VAL B 1 20  ? 12.761  9.563   47.599 1.00 29.38 ? 14  VAL B CG1 1 
ATOM   1177 C  CG2 . VAL B 1 20  ? 12.206  11.887  48.218 1.00 36.53 ? 14  VAL B CG2 1 
ATOM   1178 N  N   . GLN B 1 21  ? 15.403  9.672   45.652 1.00 33.37 ? 15  GLN B N   1 
ATOM   1179 C  CA  . GLN B 1 21  ? 15.861  8.709   44.670 1.00 36.19 ? 15  GLN B CA  1 
ATOM   1180 C  C   . GLN B 1 21  ? 16.381  7.431   45.322 1.00 32.44 ? 15  GLN B C   1 
ATOM   1181 O  O   . GLN B 1 21  ? 16.935  7.451   46.417 1.00 30.82 ? 15  GLN B O   1 
ATOM   1182 C  CB  . GLN B 1 21  ? 16.928  9.334   43.781 1.00 41.45 ? 15  GLN B CB  1 
ATOM   1183 C  CG  . GLN B 1 21  ? 17.812  10.306  44.491 1.00 51.06 ? 15  GLN B CG  1 
ATOM   1184 C  CD  . GLN B 1 21  ? 18.694  11.062  43.528 1.00 62.69 ? 15  GLN B CD  1 
ATOM   1185 O  OE1 . GLN B 1 21  ? 18.214  11.606  42.534 1.00 63.19 ? 15  GLN B OE1 1 
ATOM   1186 N  NE2 . GLN B 1 21  ? 19.990  11.106  43.816 1.00 63.52 ? 15  GLN B NE2 1 
ATOM   1187 N  N   . GLY B 1 22  ? 16.197  6.310   44.646 1.00 27.39 ? 16  GLY B N   1 
ATOM   1188 C  CA  . GLY B 1 22  ? 16.665  5.066   45.214 1.00 29.10 ? 16  GLY B CA  1 
ATOM   1189 C  C   . GLY B 1 22  ? 16.628  3.926   44.234 1.00 23.95 ? 16  GLY B C   1 
ATOM   1190 O  O   . GLY B 1 22  ? 16.186  4.077   43.098 1.00 26.60 ? 16  GLY B O   1 
ATOM   1191 N  N   . ILE B 1 23  ? 17.096  2.773   44.689 1.00 27.37 ? 17  ILE B N   1 
ATOM   1192 C  CA  . ILE B 1 23  ? 17.123  1.555   43.899 1.00 30.99 ? 17  ILE B CA  1 
ATOM   1193 C  C   . ILE B 1 23  ? 16.613  0.483   44.819 1.00 30.10 ? 17  ILE B C   1 
ATOM   1194 O  O   . ILE B 1 23  ? 17.092  0.380   45.936 1.00 25.16 ? 17  ILE B O   1 
ATOM   1195 C  CB  . ILE B 1 23  ? 18.560  1.172   43.493 1.00 31.64 ? 17  ILE B CB  1 
ATOM   1196 C  CG1 . ILE B 1 23  ? 19.119  2.204   42.521 1.00 34.21 ? 17  ILE B CG1 1 
ATOM   1197 C  CG2 . ILE B 1 23  ? 18.570  -0.213  42.897 1.00 33.66 ? 17  ILE B CG2 1 
ATOM   1198 C  CD1 . ILE B 1 23  ? 20.575  1.928   42.144 1.00 32.59 ? 17  ILE B CD1 1 
ATOM   1199 N  N   . ILE B 1 24  ? 15.646  -0.316  44.370 1.00 18.91 ? 18  ILE B N   1 
ATOM   1200 C  CA  . ILE B 1 24  ? 15.118  -1.381  45.205 1.00 23.93 ? 18  ILE B CA  1 
ATOM   1201 C  C   . ILE B 1 24  ? 15.206  -2.674  44.398 1.00 26.04 ? 18  ILE B C   1 
ATOM   1202 O  O   . ILE B 1 24  ? 14.749  -2.719  43.251 1.00 22.57 ? 18  ILE B O   1 
ATOM   1203 C  CB  . ILE B 1 24  ? 13.644  -1.105  45.622 1.00 27.75 ? 18  ILE B CB  1 
ATOM   1204 C  CG1 . ILE B 1 24  ? 13.561  0.115   46.565 1.00 26.98 ? 18  ILE B CG1 1 
ATOM   1205 C  CG2 . ILE B 1 24  ? 13.043  -2.331  46.273 1.00 24.02 ? 18  ILE B CG2 1 
ATOM   1206 C  CD1 . ILE B 1 24  ? 14.188  -0.071  47.922 1.00 23.41 ? 18  ILE B CD1 1 
ATOM   1207 N  N   . ASN B 1 25  ? 15.822  -3.714  44.979 1.00 19.95 ? 19  ASN B N   1 
ATOM   1208 C  CA  . ASN B 1 25  ? 15.956  -4.991  44.295 1.00 22.04 ? 19  ASN B CA  1 
ATOM   1209 C  C   . ASN B 1 25  ? 14.902  -5.960  44.796 1.00 20.60 ? 19  ASN B C   1 
ATOM   1210 O  O   . ASN B 1 25  ? 14.435  -5.849  45.939 1.00 25.00 ? 19  ASN B O   1 
ATOM   1211 C  CB  . ASN B 1 25  ? 17.328  -5.614  44.571 1.00 29.54 ? 19  ASN B CB  1 
ATOM   1212 C  CG  . ASN B 1 25  ? 18.458  -4.708  44.152 1.00 35.61 ? 19  ASN B CG  1 
ATOM   1213 O  OD1 . ASN B 1 25  ? 18.756  -4.593  42.971 1.00 27.14 ? 19  ASN B OD1 1 
ATOM   1214 N  ND2 . ASN B 1 25  ? 19.073  -4.031  45.119 1.00 30.35 ? 19  ASN B ND2 1 
ATOM   1215 N  N   . PHE B 1 26  ? 14.551  -6.918  43.940 1.00 25.29 ? 20  PHE B N   1 
ATOM   1216 C  CA  . PHE B 1 26  ? 13.580  -7.964  44.286 1.00 24.49 ? 20  PHE B CA  1 
ATOM   1217 C  C   . PHE B 1 26  ? 14.146  -9.283  43.824 1.00 22.10 ? 20  PHE B C   1 
ATOM   1218 O  O   . PHE B 1 26  ? 14.621  -9.395  42.685 1.00 25.95 ? 20  PHE B O   1 
ATOM   1219 C  CB  . PHE B 1 26  ? 12.232  -7.808  43.556 1.00 27.94 ? 20  PHE B CB  1 
ATOM   1220 C  CG  . PHE B 1 26  ? 11.539  -6.501  43.805 1.00 25.72 ? 20  PHE B CG  1 
ATOM   1221 C  CD1 . PHE B 1 26  ? 11.943  -5.350  43.132 1.00 24.09 ? 20  PHE B CD1 1 
ATOM   1222 C  CD2 . PHE B 1 26  ? 10.453  -6.428  44.687 1.00 21.58 ? 20  PHE B CD2 1 
ATOM   1223 C  CE1 . PHE B 1 26  ? 11.260  -4.128  43.330 1.00 23.92 ? 20  PHE B CE1 1 
ATOM   1224 C  CE2 . PHE B 1 26  ? 9.778   -5.230  44.892 1.00 22.37 ? 20  PHE B CE2 1 
ATOM   1225 C  CZ  . PHE B 1 26  ? 10.180  -4.076  44.210 1.00 21.23 ? 20  PHE B CZ  1 
ATOM   1226 N  N   . GLU B 1 27  ? 14.075  -10.292 44.685 1.00 22.07 ? 21  GLU B N   1 
ATOM   1227 C  CA  . GLU B 1 27  ? 14.530  -11.617 44.314 1.00 28.60 ? 21  GLU B CA  1 
ATOM   1228 C  C   . GLU B 1 27  ? 13.640  -12.696 44.914 1.00 22.36 ? 21  GLU B C   1 
ATOM   1229 O  O   . GLU B 1 27  ? 13.358  -12.679 46.112 1.00 22.15 ? 21  GLU B O   1 
ATOM   1230 C  CB  . GLU B 1 27  ? 15.968  -11.865 44.756 1.00 28.39 ? 21  GLU B CB  1 
ATOM   1231 C  CG  . GLU B 1 27  ? 16.332  -13.359 44.670 1.00 37.67 ? 21  GLU B CG  1 
ATOM   1232 C  CD  . GLU B 1 27  ? 17.828  -13.647 44.632 1.00 52.71 ? 21  GLU B CD  1 
ATOM   1233 O  OE1 . GLU B 1 27  ? 18.565  -13.216 45.542 1.00 44.81 ? 21  GLU B OE1 1 
ATOM   1234 O  OE2 . GLU B 1 27  ? 18.264  -14.322 43.677 1.00 56.25 ? 21  GLU B OE2 1 
ATOM   1235 N  N   . GLN B 1 28  ? 13.238  -13.646 44.078 1.00 29.93 ? 22  GLN B N   1 
ATOM   1236 C  CA  . GLN B 1 28  ? 12.404  -14.770 44.502 1.00 22.10 ? 22  GLN B CA  1 
ATOM   1237 C  C   . GLN B 1 28  ? 13.081  -16.085 44.056 1.00 27.72 ? 22  GLN B C   1 
ATOM   1238 O  O   . GLN B 1 28  ? 13.214  -16.342 42.852 1.00 28.97 ? 22  GLN B O   1 
ATOM   1239 C  CB  . GLN B 1 28  ? 11.010  -14.632 43.885 1.00 26.44 ? 22  GLN B CB  1 
ATOM   1240 C  CG  . GLN B 1 28  ? 10.063  -15.718 44.298 1.00 25.88 ? 22  GLN B CG  1 
ATOM   1241 C  CD  . GLN B 1 28  ? 8.643   -15.484 43.816 1.00 24.41 ? 22  GLN B CD  1 
ATOM   1242 O  OE1 . GLN B 1 28  ? 8.423   -14.913 42.765 1.00 25.67 ? 22  GLN B OE1 1 
ATOM   1243 N  NE2 . GLN B 1 28  ? 7.674   -15.943 44.595 1.00 26.71 ? 22  GLN B NE2 1 
ATOM   1244 N  N   . ASN B 1 32  ? 6.733   -20.109 44.608 1.00 36.53 ? 26  ASN B N   1 
ATOM   1245 C  CA  . ASN B 1 32  ? 5.975   -19.933 45.843 1.00 35.91 ? 26  ASN B CA  1 
ATOM   1246 C  C   . ASN B 1 32  ? 6.841   -19.492 46.993 1.00 33.60 ? 26  ASN B C   1 
ATOM   1247 O  O   . ASN B 1 32  ? 6.434   -19.604 48.139 1.00 34.84 ? 26  ASN B O   1 
ATOM   1248 C  CB  . ASN B 1 32  ? 5.279   -21.230 46.271 1.00 45.31 ? 26  ASN B CB  1 
ATOM   1249 C  CG  . ASN B 1 32  ? 4.217   -21.661 45.306 1.00 55.41 ? 26  ASN B CG  1 
ATOM   1250 O  OD1 . ASN B 1 32  ? 3.357   -20.868 44.917 1.00 63.52 ? 26  ASN B OD1 1 
ATOM   1251 N  ND2 . ASN B 1 32  ? 4.256   -22.930 44.914 1.00 65.54 ? 26  ASN B ND2 1 
ATOM   1252 N  N   . GLY B 1 33  ? 8.044   -19.018 46.702 1.00 31.34 ? 27  GLY B N   1 
ATOM   1253 C  CA  . GLY B 1 33  ? 8.918   -18.574 47.770 1.00 30.38 ? 27  GLY B CA  1 
ATOM   1254 C  C   . GLY B 1 33  ? 8.704   -17.110 48.090 1.00 25.90 ? 27  GLY B C   1 
ATOM   1255 O  O   . GLY B 1 33  ? 8.115   -16.395 47.292 1.00 31.15 ? 27  GLY B O   1 
ATOM   1256 N  N   . PRO B 1 34  ? 9.138   -16.636 49.265 1.00 26.36 ? 28  PRO B N   1 
ATOM   1257 C  CA  . PRO B 1 34  ? 8.932   -15.222 49.557 1.00 31.51 ? 28  PRO B CA  1 
ATOM   1258 C  C   . PRO B 1 34  ? 9.788   -14.390 48.599 1.00 32.96 ? 28  PRO B C   1 
ATOM   1259 O  O   . PRO B 1 34  ? 10.690  -14.902 47.925 1.00 28.90 ? 28  PRO B O   1 
ATOM   1260 C  CB  . PRO B 1 34  ? 9.387   -15.100 51.016 1.00 34.82 ? 28  PRO B CB  1 
ATOM   1261 C  CG  . PRO B 1 34  ? 10.484  -16.097 51.088 1.00 35.82 ? 28  PRO B CG  1 
ATOM   1262 C  CD  . PRO B 1 34  ? 9.874   -17.292 50.357 1.00 34.30 ? 28  PRO B CD  1 
ATOM   1263 N  N   . VAL B 1 35  ? 9.481   -13.108 48.521 1.00 23.93 ? 29  VAL B N   1 
ATOM   1264 C  CA  . VAL B 1 35  ? 10.218  -12.213 47.660 1.00 25.19 ? 29  VAL B CA  1 
ATOM   1265 C  C   . VAL B 1 35  ? 11.091  -11.416 48.606 1.00 21.64 ? 29  VAL B C   1 
ATOM   1266 O  O   . VAL B 1 35  ? 10.603  -10.904 49.604 1.00 25.58 ? 29  VAL B O   1 
ATOM   1267 C  CB  . VAL B 1 35  ? 9.265   -11.241 46.870 1.00 20.62 ? 29  VAL B CB  1 
ATOM   1268 C  CG1 . VAL B 1 35  ? 10.097  -10.254 46.048 1.00 27.89 ? 29  VAL B CG1 1 
ATOM   1269 C  CG2 . VAL B 1 35  ? 8.357   -12.037 45.954 1.00 24.90 ? 29  VAL B CG2 1 
ATOM   1270 N  N   . LYS B 1 36  ? 12.394  -11.379 48.336 1.00 25.53 ? 30  LYS B N   1 
ATOM   1271 C  CA  . LYS B 1 36  ? 13.300  -10.584 49.156 1.00 28.11 ? 30  LYS B CA  1 
ATOM   1272 C  C   . LYS B 1 36  ? 13.335  -9.226  48.459 1.00 23.28 ? 30  LYS B C   1 
ATOM   1273 O  O   . LYS B 1 36  ? 13.486  -9.151  47.244 1.00 23.35 ? 30  LYS B O   1 
ATOM   1274 C  CB  . LYS B 1 36  ? 14.709  -11.180 49.182 1.00 32.57 ? 30  LYS B CB  1 
ATOM   1275 C  CG  . LYS B 1 36  ? 14.784  -12.625 49.688 1.00 36.98 ? 30  LYS B CG  1 
ATOM   1276 C  CD  . LYS B 1 36  ? 14.629  -12.737 51.198 1.00 52.12 ? 30  LYS B CD  1 
ATOM   1277 C  CE  . LYS B 1 36  ? 14.653  -14.207 51.640 1.00 55.51 ? 30  LYS B CE  1 
ATOM   1278 N  NZ  . LYS B 1 36  ? 15.809  -14.971 51.053 1.00 46.75 ? 30  LYS B NZ  1 
ATOM   1279 N  N   . VAL B 1 37  ? 13.188  -8.174  49.250 1.00 23.12 ? 31  VAL B N   1 
ATOM   1280 C  CA  . VAL B 1 37  ? 13.182  -6.797  48.792 1.00 20.08 ? 31  VAL B CA  1 
ATOM   1281 C  C   . VAL B 1 37  ? 14.223  -5.970  49.560 1.00 23.28 ? 31  VAL B C   1 
ATOM   1282 O  O   . VAL B 1 37  ? 14.132  -5.842  50.788 1.00 26.92 ? 31  VAL B O   1 
ATOM   1283 C  CB  . VAL B 1 37  ? 11.812  -6.142  49.048 1.00 24.64 ? 31  VAL B CB  1 
ATOM   1284 C  CG1 . VAL B 1 37  ? 11.805  -4.716  48.471 1.00 23.57 ? 31  VAL B CG1 1 
ATOM   1285 C  CG2 . VAL B 1 37  ? 10.691  -7.030  48.433 1.00 23.96 ? 31  VAL B CG2 1 
ATOM   1286 N  N   . TRP B 1 38  ? 15.182  -5.393  48.841 1.00 20.45 ? 32  TRP B N   1 
ATOM   1287 C  CA  . TRP B 1 38  ? 16.195  -4.582  49.532 1.00 24.04 ? 32  TRP B CA  1 
ATOM   1288 C  C   . TRP B 1 38  ? 16.810  -3.536  48.631 1.00 20.66 ? 32  TRP B C   1 
ATOM   1289 O  O   . TRP B 1 38  ? 16.809  -3.645  47.413 1.00 24.79 ? 32  TRP B O   1 
ATOM   1290 C  CB  . TRP B 1 38  ? 17.295  -5.491  50.094 1.00 25.70 ? 32  TRP B CB  1 
ATOM   1291 C  CG  . TRP B 1 38  ? 18.230  -5.983  49.024 1.00 25.24 ? 32  TRP B CG  1 
ATOM   1292 C  CD1 . TRP B 1 38  ? 19.432  -5.432  48.672 1.00 25.55 ? 32  TRP B CD1 1 
ATOM   1293 C  CD2 . TRP B 1 38  ? 18.007  -7.073  48.121 1.00 27.13 ? 32  TRP B CD2 1 
ATOM   1294 N  NE1 . TRP B 1 38  ? 19.970  -6.117  47.603 1.00 30.90 ? 32  TRP B NE1 1 
ATOM   1295 C  CE2 . TRP B 1 38  ? 19.116  -7.128  47.247 1.00 28.13 ? 32  TRP B CE2 1 
ATOM   1296 C  CE3 . TRP B 1 38  ? 16.974  -8.010  47.962 1.00 25.20 ? 32  TRP B CE3 1 
ATOM   1297 C  CZ2 . TRP B 1 38  ? 19.223  -8.086  46.229 1.00 26.54 ? 32  TRP B CZ2 1 
ATOM   1298 C  CZ3 . TRP B 1 38  ? 17.077  -8.960  46.948 1.00 29.43 ? 32  TRP B CZ3 1 
ATOM   1299 C  CH2 . TRP B 1 38  ? 18.197  -8.990  46.094 1.00 30.04 ? 32  TRP B CH2 1 
ATOM   1300 N  N   . GLY B 1 39  ? 17.347  -2.502  49.264 1.00 25.05 ? 33  GLY B N   1 
ATOM   1301 C  CA  . GLY B 1 39  ? 17.982  -1.434  48.540 1.00 23.67 ? 33  GLY B CA  1 
ATOM   1302 C  C   . GLY B 1 39  ? 18.121  -0.229  49.456 1.00 21.15 ? 33  GLY B C   1 
ATOM   1303 O  O   . GLY B 1 39  ? 18.061  -0.352  50.698 1.00 22.60 ? 33  GLY B O   1 
ATOM   1304 N  N   . SER B 1 40  ? 18.279  0.929   48.827 1.00 22.95 ? 34  SER B N   1 
ATOM   1305 C  CA  . SER B 1 40  ? 18.464  2.198   49.529 1.00 29.35 ? 34  SER B CA  1 
ATOM   1306 C  C   . SER B 1 40  ? 17.697  3.342   48.877 1.00 30.52 ? 34  SER B C   1 
ATOM   1307 O  O   . SER B 1 40  ? 17.614  3.431   47.651 1.00 34.70 ? 34  SER B O   1 
ATOM   1308 C  CB  . SER B 1 40  ? 19.952  2.571   49.547 1.00 32.17 ? 34  SER B CB  1 
ATOM   1309 O  OG  . SER B 1 40  ? 20.750  1.474   49.971 1.00 45.04 ? 34  SER B OG  1 
ATOM   1310 N  N   . ILE B 1 41  ? 17.137  4.221   49.699 1.00 22.27 ? 35  ILE B N   1 
ATOM   1311 C  CA  . ILE B 1 41  ? 16.403  5.377   49.193 1.00 26.44 ? 35  ILE B CA  1 
ATOM   1312 C  C   . ILE B 1 41  ? 16.962  6.617   49.884 1.00 27.57 ? 35  ILE B C   1 
ATOM   1313 O  O   . ILE B 1 41  ? 17.041  6.644   51.115 1.00 30.26 ? 35  ILE B O   1 
ATOM   1314 C  CB  . ILE B 1 41  ? 14.905  5.264   49.518 1.00 28.56 ? 35  ILE B CB  1 
ATOM   1315 C  CG1 . ILE B 1 41  ? 14.389  3.900   49.025 1.00 27.22 ? 35  ILE B CG1 1 
ATOM   1316 C  CG2 . ILE B 1 41  ? 14.120  6.456   48.877 1.00 27.38 ? 35  ILE B CG2 1 
ATOM   1317 C  CD1 . ILE B 1 41  ? 12.969  3.586   49.486 1.00 31.72 ? 35  ILE B CD1 1 
ATOM   1318 N  N   . LYS B 1 42  ? 17.350  7.624   49.100 1.00 26.28 ? 36  LYS B N   1 
ATOM   1319 C  CA  . LYS B 1 42  ? 17.898  8.877   49.644 1.00 30.96 ? 36  LYS B CA  1 
ATOM   1320 C  C   . LYS B 1 42  ? 16.962  10.051  49.428 1.00 35.72 ? 36  LYS B C   1 
ATOM   1321 O  O   . LYS B 1 42  ? 16.036  9.974   48.633 1.00 31.69 ? 36  LYS B O   1 
ATOM   1322 C  CB  . LYS B 1 42  ? 19.236  9.226   48.982 1.00 34.92 ? 36  LYS B CB  1 
ATOM   1323 C  CG  . LYS B 1 42  ? 20.415  8.399   49.447 1.00 54.12 ? 36  LYS B CG  1 
ATOM   1324 C  CD  . LYS B 1 42  ? 20.413  6.981   48.890 1.00 59.95 ? 36  LYS B CD  1 
ATOM   1325 C  CE  . LYS B 1 42  ? 21.758  6.308   49.191 1.00 59.77 ? 36  LYS B CE  1 
ATOM   1326 N  NZ  . LYS B 1 42  ? 21.932  5.013   48.493 1.00 54.10 ? 36  LYS B NZ  1 
ATOM   1327 N  N   . GLY B 1 43  ? 17.240  11.156  50.110 1.00 33.08 ? 37  GLY B N   1 
ATOM   1328 C  CA  . GLY B 1 43  ? 16.414  12.340  49.963 1.00 34.36 ? 37  GLY B CA  1 
ATOM   1329 C  C   . GLY B 1 43  ? 15.131  12.361  50.768 1.00 32.22 ? 37  GLY B C   1 
ATOM   1330 O  O   . GLY B 1 43  ? 14.279  13.236  50.560 1.00 29.73 ? 37  GLY B O   1 
ATOM   1331 N  N   . LEU B 1 44  ? 14.993  11.426  51.708 1.00 30.39 ? 38  LEU B N   1 
ATOM   1332 C  CA  . LEU B 1 44  ? 13.792  11.351  52.540 1.00 28.98 ? 38  LEU B CA  1 
ATOM   1333 C  C   . LEU B 1 44  ? 13.926  12.135  53.837 1.00 30.73 ? 38  LEU B C   1 
ATOM   1334 O  O   . LEU B 1 44  ? 15.020  12.293  54.366 1.00 38.69 ? 38  LEU B O   1 
ATOM   1335 C  CB  . LEU B 1 44  ? 13.493  9.887   52.907 1.00 22.53 ? 38  LEU B CB  1 
ATOM   1336 C  CG  . LEU B 1 44  ? 12.994  8.940   51.823 1.00 33.54 ? 38  LEU B CG  1 
ATOM   1337 C  CD1 . LEU B 1 44  ? 13.152  7.492   52.283 1.00 28.73 ? 38  LEU B CD1 1 
ATOM   1338 C  CD2 . LEU B 1 44  ? 11.519  9.282   51.513 1.00 33.61 ? 38  LEU B CD2 1 
ATOM   1339 N  N   . THR B 1 45  ? 12.815  12.627  54.357 1.00 29.52 ? 39  THR B N   1 
ATOM   1340 C  CA  . THR B 1 45  ? 12.873  13.305  55.637 1.00 31.62 ? 39  THR B CA  1 
ATOM   1341 C  C   . THR B 1 45  ? 12.927  12.187  56.668 1.00 34.92 ? 39  THR B C   1 
ATOM   1342 O  O   . THR B 1 45  ? 12.416  11.082  56.418 1.00 30.34 ? 39  THR B O   1 
ATOM   1343 C  CB  . THR B 1 45  ? 11.626  14.134  55.901 1.00 38.68 ? 39  THR B CB  1 
ATOM   1344 O  OG1 . THR B 1 45  ? 10.464  13.320  55.703 1.00 48.52 ? 39  THR B OG1 1 
ATOM   1345 C  CG2 . THR B 1 45  ? 11.575  15.297  54.976 1.00 30.76 ? 39  THR B CG2 1 
ATOM   1346 N  N   . GLU B 1 46  ? 13.516  12.461  57.828 1.00 27.61 ? 40  GLU B N   1 
ATOM   1347 C  CA  . GLU B 1 46  ? 13.616  11.443  58.859 1.00 25.35 ? 40  GLU B CA  1 
ATOM   1348 C  C   . GLU B 1 46  ? 12.211  11.036  59.252 1.00 31.57 ? 40  GLU B C   1 
ATOM   1349 O  O   . GLU B 1 46  ? 11.345  11.887  59.472 1.00 27.09 ? 40  GLU B O   1 
ATOM   1350 C  CB  . GLU B 1 46  ? 14.356  11.974  60.082 1.00 32.65 ? 40  GLU B CB  1 
ATOM   1351 C  CG  . GLU B 1 46  ? 14.450  10.962  61.204 1.00 32.67 ? 40  GLU B CG  1 
ATOM   1352 C  CD  . GLU B 1 46  ? 15.134  11.517  62.443 1.00 34.48 ? 40  GLU B CD  1 
ATOM   1353 O  OE1 . GLU B 1 46  ? 15.632  12.657  62.384 1.00 38.73 ? 40  GLU B OE1 1 
ATOM   1354 O  OE2 . GLU B 1 46  ? 15.177  10.815  63.469 1.00 36.61 ? 40  GLU B OE2 1 
ATOM   1355 N  N   . GLY B 1 47  ? 11.981  9.735   59.334 1.00 30.49 ? 41  GLY B N   1 
ATOM   1356 C  CA  . GLY B 1 47  ? 10.649  9.280   59.690 1.00 31.81 ? 41  GLY B CA  1 
ATOM   1357 C  C   . GLY B 1 47  ? 10.252  8.017   58.951 1.00 27.94 ? 41  GLY B C   1 
ATOM   1358 O  O   . GLY B 1 47  ? 11.046  7.450   58.179 1.00 28.61 ? 41  GLY B O   1 
ATOM   1359 N  N   . LEU B 1 48  ? 9.026   7.558   59.208 1.00 22.94 ? 42  LEU B N   1 
ATOM   1360 C  CA  . LEU B 1 48  ? 8.519   6.364   58.552 1.00 25.10 ? 42  LEU B CA  1 
ATOM   1361 C  C   . LEU B 1 48  ? 7.810   6.794   57.281 1.00 26.79 ? 42  LEU B C   1 
ATOM   1362 O  O   . LEU B 1 48  ? 7.089   7.816   57.265 1.00 25.94 ? 42  LEU B O   1 
ATOM   1363 C  CB  . LEU B 1 48  ? 7.539   5.606   59.458 1.00 27.68 ? 42  LEU B CB  1 
ATOM   1364 C  CG  . LEU B 1 48  ? 8.109   4.697   60.554 1.00 38.33 ? 42  LEU B CG  1 
ATOM   1365 C  CD1 . LEU B 1 48  ? 8.956   5.487   61.530 1.00 42.53 ? 42  LEU B CD1 1 
ATOM   1366 C  CD2 . LEU B 1 48  ? 6.954   4.040   61.280 1.00 44.50 ? 42  LEU B CD2 1 
ATOM   1367 N  N   . HIS B 1 49  ? 7.980   5.971   56.245 1.00 26.29 ? 43  HIS B N   1 
ATOM   1368 C  CA  . HIS B 1 49  ? 7.432   6.227   54.920 1.00 23.58 ? 43  HIS B CA  1 
ATOM   1369 C  C   . HIS B 1 49  ? 6.720   5.052   54.257 1.00 21.01 ? 43  HIS B C   1 
ATOM   1370 O  O   . HIS B 1 49  ? 7.315   3.984   54.059 1.00 20.24 ? 43  HIS B O   1 
ATOM   1371 C  CB  . HIS B 1 49  ? 8.562   6.657   54.022 1.00 23.05 ? 43  HIS B CB  1 
ATOM   1372 C  CG  . HIS B 1 49  ? 9.231   7.909   54.483 1.00 31.28 ? 43  HIS B CG  1 
ATOM   1373 N  ND1 . HIS B 1 49  ? 8.762   9.164   54.161 1.00 25.26 ? 43  HIS B ND1 1 
ATOM   1374 C  CD2 . HIS B 1 49  ? 10.312  8.098   55.274 1.00 30.01 ? 43  HIS B CD2 1 
ATOM   1375 C  CE1 . HIS B 1 49  ? 9.531   10.077  54.731 1.00 32.94 ? 43  HIS B CE1 1 
ATOM   1376 N  NE2 . HIS B 1 49  ? 10.479  9.455   55.413 1.00 33.27 ? 43  HIS B NE2 1 
ATOM   1377 N  N   . GLY B 1 50  ? 5.459   5.273   53.891 1.00 26.16 ? 44  GLY B N   1 
ATOM   1378 C  CA  . GLY B 1 50  ? 4.669   4.236   53.223 1.00 28.46 ? 44  GLY B CA  1 
ATOM   1379 C  C   . GLY B 1 50  ? 5.381   3.709   51.992 1.00 24.26 ? 44  GLY B C   1 
ATOM   1380 O  O   . GLY B 1 50  ? 5.980   4.464   51.226 1.00 26.74 ? 44  GLY B O   1 
ATOM   1381 N  N   . PHE B 1 51  ? 5.283   2.408   51.764 1.00 26.36 ? 45  PHE B N   1 
ATOM   1382 C  CA  . PHE B 1 51  ? 6.016   1.764   50.663 1.00 22.11 ? 45  PHE B CA  1 
ATOM   1383 C  C   . PHE B 1 51  ? 5.055   0.695   50.126 1.00 22.20 ? 45  PHE B C   1 
ATOM   1384 O  O   . PHE B 1 51  ? 4.733   -0.253  50.840 1.00 20.21 ? 45  PHE B O   1 
ATOM   1385 C  CB  . PHE B 1 51  ? 7.232   1.146   51.323 1.00 21.99 ? 45  PHE B CB  1 
ATOM   1386 C  CG  . PHE B 1 51  ? 8.294   0.618   50.398 1.00 27.00 ? 45  PHE B CG  1 
ATOM   1387 C  CD1 . PHE B 1 51  ? 8.944   1.445   49.490 1.00 26.69 ? 45  PHE B CD1 1 
ATOM   1388 C  CD2 . PHE B 1 51  ? 8.757   -0.679  50.572 1.00 23.81 ? 45  PHE B CD2 1 
ATOM   1389 C  CE1 . PHE B 1 51  ? 10.046  0.986   48.780 1.00 26.27 ? 45  PHE B CE1 1 
ATOM   1390 C  CE2 . PHE B 1 51  ? 9.855   -1.153  49.865 1.00 29.16 ? 45  PHE B CE2 1 
ATOM   1391 C  CZ  . PHE B 1 51  ? 10.506  -0.313  48.967 1.00 33.32 ? 45  PHE B CZ  1 
ATOM   1392 N  N   . HIS B 1 52  ? 4.622   0.857   48.880 1.00 22.19 ? 46  HIS B N   1 
ATOM   1393 C  CA  . HIS B 1 52  ? 3.663   -0.065  48.266 1.00 19.68 ? 46  HIS B CA  1 
ATOM   1394 C  C   . HIS B 1 52  ? 3.931   -0.292  46.783 1.00 21.65 ? 46  HIS B C   1 
ATOM   1395 O  O   . HIS B 1 52  ? 4.623   0.481   46.124 1.00 23.86 ? 46  HIS B O   1 
ATOM   1396 C  CB  . HIS B 1 52  ? 2.231   0.502   48.298 1.00 20.14 ? 46  HIS B CB  1 
ATOM   1397 C  CG  . HIS B 1 52  ? 1.887   1.281   49.524 1.00 30.50 ? 46  HIS B CG  1 
ATOM   1398 N  ND1 . HIS B 1 52  ? 1.682   2.646   49.499 1.00 28.68 ? 46  HIS B ND1 1 
ATOM   1399 C  CD2 . HIS B 1 52  ? 1.709   0.895   50.809 1.00 27.87 ? 46  HIS B CD2 1 
ATOM   1400 C  CE1 . HIS B 1 52  ? 1.399   3.063   50.721 1.00 22.09 ? 46  HIS B CE1 1 
ATOM   1401 N  NE2 . HIS B 1 52  ? 1.411   2.022   51.529 1.00 25.47 ? 46  HIS B NE2 1 
ATOM   1402 N  N   . VAL B 1 53  ? 3.347   -1.363  46.263 1.00 13.87 ? 47  VAL B N   1 
ATOM   1403 C  CA  . VAL B 1 53  ? 3.423   -1.630  44.848 1.00 20.92 ? 47  VAL B CA  1 
ATOM   1404 C  C   . VAL B 1 53  ? 2.041   -1.146  44.433 1.00 22.46 ? 47  VAL B C   1 
ATOM   1405 O  O   . VAL B 1 53  ? 1.037   -1.492  45.085 1.00 21.91 ? 47  VAL B O   1 
ATOM   1406 C  CB  . VAL B 1 53  ? 3.506   -3.105  44.523 1.00 16.11 ? 47  VAL B CB  1 
ATOM   1407 C  CG1 . VAL B 1 53  ? 3.330   -3.283  43.023 1.00 19.45 ? 47  VAL B CG1 1 
ATOM   1408 C  CG2 . VAL B 1 53  ? 4.902   -3.672  44.972 1.00 22.84 ? 47  VAL B CG2 1 
ATOM   1409 N  N   . HIS B 1 54  ? 1.992   -0.347  43.379 1.00 22.68 ? 48  HIS B N   1 
ATOM   1410 C  CA  . HIS B 1 54  ? 0.723   0.208   42.912 1.00 21.21 ? 48  HIS B CA  1 
ATOM   1411 C  C   . HIS B 1 54  ? 0.336   -0.538  41.625 1.00 27.09 ? 48  HIS B C   1 
ATOM   1412 O  O   . HIS B 1 54  ? 1.145   -1.264  41.028 1.00 28.19 ? 48  HIS B O   1 
ATOM   1413 C  CB  . HIS B 1 54  ? 0.871   1.726   42.684 1.00 18.80 ? 48  HIS B CB  1 
ATOM   1414 C  CG  . HIS B 1 54  ? 0.834   2.543   43.941 1.00 32.71 ? 48  HIS B CG  1 
ATOM   1415 N  ND1 . HIS B 1 54  ? -0.080  3.554   44.152 1.00 20.40 ? 48  HIS B ND1 1 
ATOM   1416 C  CD2 . HIS B 1 54  ? 1.622   2.513   45.044 1.00 22.18 ? 48  HIS B CD2 1 
ATOM   1417 C  CE1 . HIS B 1 54  ? 0.151   4.117   45.329 1.00 26.87 ? 48  HIS B CE1 1 
ATOM   1418 N  NE2 . HIS B 1 54  ? 1.183   3.502   45.887 1.00 18.74 ? 48  HIS B NE2 1 
ATOM   1419 N  N   . GLU B 1 55  ? -0.910  -0.350  41.208 1.00 25.78 ? 49  GLU B N   1 
ATOM   1420 C  CA  . GLU B 1 55  ? -1.489  -1.016  40.035 1.00 33.90 ? 49  GLU B CA  1 
ATOM   1421 C  C   . GLU B 1 55  ? -0.860  -0.860  38.654 1.00 26.68 ? 49  GLU B C   1 
ATOM   1422 O  O   . GLU B 1 55  ? -0.640  -1.853  37.951 1.00 32.05 ? 49  GLU B O   1 
ATOM   1423 C  CB  . GLU B 1 55  ? -2.965  -0.622  39.914 1.00 38.58 ? 49  GLU B CB  1 
ATOM   1424 C  CG  . GLU B 1 55  ? -3.785  -1.638  39.149 1.00 44.50 ? 49  GLU B CG  1 
ATOM   1425 C  CD  . GLU B 1 55  ? -4.929  -2.132  39.982 1.00 59.74 ? 49  GLU B CD  1 
ATOM   1426 O  OE1 . GLU B 1 55  ? -6.011  -1.485  39.919 1.00 49.26 ? 49  GLU B OE1 1 
ATOM   1427 O  OE2 . GLU B 1 55  ? -4.730  -3.144  40.715 1.00 44.48 ? 49  GLU B OE2 1 
ATOM   1428 N  N   . PHE B 1 56  ? -0.566  0.373   38.265 1.00 30.54 ? 50  PHE B N   1 
ATOM   1429 C  CA  . PHE B 1 56  ? -0.039  0.631   36.930 1.00 34.26 ? 50  PHE B CA  1 
ATOM   1430 C  C   . PHE B 1 56  ? 1.420   1.033   36.894 1.00 32.69 ? 50  PHE B C   1 
ATOM   1431 O  O   . PHE B 1 56  ? 1.876   1.806   37.731 1.00 41.52 ? 50  PHE B O   1 
ATOM   1432 C  CB  . PHE B 1 56  ? -0.876  1.723   36.276 1.00 25.84 ? 50  PHE B CB  1 
ATOM   1433 C  CG  . PHE B 1 56  ? -2.342  1.543   36.484 1.00 25.34 ? 50  PHE B CG  1 
ATOM   1434 C  CD1 . PHE B 1 56  ? -2.977  0.378   36.080 1.00 29.91 ? 50  PHE B CD1 1 
ATOM   1435 C  CD2 . PHE B 1 56  ? -3.093  2.540   37.098 1.00 42.20 ? 50  PHE B CD2 1 
ATOM   1436 C  CE1 . PHE B 1 56  ? -4.342  0.197   36.283 1.00 36.75 ? 50  PHE B CE1 1 
ATOM   1437 C  CE2 . PHE B 1 56  ? -4.462  2.372   37.307 1.00 46.46 ? 50  PHE B CE2 1 
ATOM   1438 C  CZ  . PHE B 1 56  ? -5.086  1.199   36.899 1.00 38.13 ? 50  PHE B CZ  1 
ATOM   1439 N  N   . GLY B 1 57  ? 2.134   0.499   35.911 1.00 30.23 ? 51  GLY B N   1 
ATOM   1440 C  CA  . GLY B 1 57  ? 3.538   0.802   35.734 1.00 26.79 ? 51  GLY B CA  1 
ATOM   1441 C  C   . GLY B 1 57  ? 3.625   2.056   34.898 1.00 39.26 ? 51  GLY B C   1 
ATOM   1442 O  O   . GLY B 1 57  ? 4.377   2.131   33.931 1.00 37.94 ? 51  GLY B O   1 
ATOM   1443 N  N   . ASP B 1 58  ? 2.807   3.031   35.263 1.00 41.52 ? 52  ASP B N   1 
ATOM   1444 C  CA  . ASP B 1 58  ? 2.761   4.316   34.593 1.00 51.45 ? 52  ASP B CA  1 
ATOM   1445 C  C   . ASP B 1 58  ? 3.553   5.239   35.515 1.00 49.83 ? 52  ASP B C   1 
ATOM   1446 O  O   . ASP B 1 58  ? 3.071   5.626   36.579 1.00 41.78 ? 52  ASP B O   1 
ATOM   1447 C  CB  . ASP B 1 58  ? 1.303   4.795   34.484 1.00 58.40 ? 52  ASP B CB  1 
ATOM   1448 C  CG  . ASP B 1 58  ? 1.120   5.930   33.479 1.00 60.49 ? 52  ASP B CG  1 
ATOM   1449 O  OD1 . ASP B 1 58  ? 2.026   6.791   33.375 1.00 51.74 ? 52  ASP B OD1 1 
ATOM   1450 O  OD2 . ASP B 1 58  ? 0.057   5.963   32.808 1.00 55.91 ? 52  ASP B OD2 1 
ATOM   1451 N  N   . ASN B 1 59  ? 4.776   5.559   35.116 1.00 52.91 ? 53  ASN B N   1 
ATOM   1452 C  CA  . ASN B 1 59  ? 5.644   6.422   35.898 1.00 57.65 ? 53  ASN B CA  1 
ATOM   1453 C  C   . ASN B 1 59  ? 5.016   7.806   36.105 1.00 64.57 ? 53  ASN B C   1 
ATOM   1454 O  O   . ASN B 1 59  ? 5.239   8.735   35.327 1.00 64.46 ? 53  ASN B O   1 
ATOM   1455 C  CB  . ASN B 1 59  ? 6.995   6.556   35.197 1.00 63.18 ? 53  ASN B CB  1 
ATOM   1456 C  CG  . ASN B 1 59  ? 7.897   7.564   35.868 1.00 73.72 ? 53  ASN B CG  1 
ATOM   1457 O  OD1 . ASN B 1 59  ? 8.270   7.400   37.032 1.00 83.00 ? 53  ASN B OD1 1 
ATOM   1458 N  ND2 . ASN B 1 59  ? 8.252   8.622   35.140 1.00 71.81 ? 53  ASN B ND2 1 
ATOM   1459 N  N   . CYS B 1 63  ? 4.120   10.435  39.832 1.00 30.80 ? 57  CYS B N   1 
ATOM   1460 C  CA  . CYS B 1 63  ? 3.651   9.209   40.436 1.00 35.24 ? 57  CYS B CA  1 
ATOM   1461 C  C   . CYS B 1 63  ? 2.122   9.152   40.552 1.00 34.58 ? 57  CYS B C   1 
ATOM   1462 O  O   . CYS B 1 63  ? 1.565   8.148   40.993 1.00 32.43 ? 57  CYS B O   1 
ATOM   1463 C  CB  . CYS B 1 63  ? 4.291   9.039   41.820 1.00 31.71 ? 57  CYS B CB  1 
ATOM   1464 S  SG  . CYS B 1 63  ? 6.107   8.989   41.752 1.00 34.98 ? 57  CYS B SG  1 
ATOM   1465 N  N   . THR B 1 64  ? 1.452   10.213  40.131 1.00 39.86 ? 58  THR B N   1 
ATOM   1466 C  CA  . THR B 1 64  ? 0.000   10.265  40.233 1.00 44.36 ? 58  THR B CA  1 
ATOM   1467 C  C   . THR B 1 64  ? -0.698  9.244   39.347 1.00 42.45 ? 58  THR B C   1 
ATOM   1468 O  O   . THR B 1 64  ? -1.784  8.799   39.675 1.00 54.14 ? 58  THR B O   1 
ATOM   1469 C  CB  . THR B 1 64  ? -0.551  11.676  39.880 1.00 49.59 ? 58  THR B CB  1 
ATOM   1470 O  OG1 . THR B 1 64  ? -0.372  11.924  38.479 1.00 62.93 ? 58  THR B OG1 1 
ATOM   1471 C  CG2 . THR B 1 64  ? 0.180   12.758  40.676 1.00 54.00 ? 58  THR B CG2 1 
ATOM   1472 N  N   . SER B 1 65  ? -0.082  8.862   38.235 1.00 37.83 ? 59  SER B N   1 
ATOM   1473 C  CA  . SER B 1 65  ? -0.701  7.902   37.316 1.00 34.67 ? 59  SER B CA  1 
ATOM   1474 C  C   . SER B 1 65  ? -0.521  6.445   37.687 1.00 31.12 ? 59  SER B C   1 
ATOM   1475 O  O   . SER B 1 65  ? -0.990  5.561   36.969 1.00 29.23 ? 59  SER B O   1 
ATOM   1476 C  CB  . SER B 1 65  ? -0.147  8.098   35.903 1.00 45.70 ? 59  SER B CB  1 
ATOM   1477 O  OG  . SER B 1 65  ? -0.365  9.423   35.438 1.00 53.62 ? 59  SER B OG  1 
ATOM   1478 N  N   . ALA B 1 66  ? 0.165   6.177   38.793 1.00 32.68 ? 60  ALA B N   1 
ATOM   1479 C  CA  . ALA B 1 66  ? 0.418   4.789   39.186 1.00 35.77 ? 60  ALA B CA  1 
ATOM   1480 C  C   . ALA B 1 66  ? -0.848  4.072   39.625 1.00 32.53 ? 60  ALA B C   1 
ATOM   1481 O  O   . ALA B 1 66  ? -0.870  2.869   39.770 1.00 29.84 ? 60  ALA B O   1 
ATOM   1482 C  CB  . ALA B 1 66  ? 1.451   4.742   40.307 1.00 32.06 ? 60  ALA B CB  1 
ATOM   1483 N  N   . GLY B 1 67  ? -1.909  4.821   39.855 1.00 33.98 ? 61  GLY B N   1 
ATOM   1484 C  CA  . GLY B 1 67  ? -3.122  4.185   40.289 1.00 28.68 ? 61  GLY B CA  1 
ATOM   1485 C  C   . GLY B 1 67  ? -3.115  3.896   41.774 1.00 26.90 ? 61  GLY B C   1 
ATOM   1486 O  O   . GLY B 1 67  ? -2.235  4.345   42.522 1.00 25.17 ? 61  GLY B O   1 
ATOM   1487 N  N   . PRO B 1 68  ? -4.108  3.144   42.236 1.00 27.27 ? 62  PRO B N   1 
ATOM   1488 C  CA  . PRO B 1 68  ? -4.213  2.792   43.655 1.00 26.12 ? 62  PRO B CA  1 
ATOM   1489 C  C   . PRO B 1 68  ? -3.206  1.687   43.982 1.00 26.16 ? 62  PRO B C   1 
ATOM   1490 O  O   . PRO B 1 68  ? -2.454  1.229   43.108 1.00 21.10 ? 62  PRO B O   1 
ATOM   1491 C  CB  . PRO B 1 68  ? -5.645  2.273   43.764 1.00 28.85 ? 62  PRO B CB  1 
ATOM   1492 C  CG  . PRO B 1 68  ? -5.750  1.475   42.468 1.00 30.07 ? 62  PRO B CG  1 
ATOM   1493 C  CD  . PRO B 1 68  ? -5.140  2.446   41.441 1.00 31.43 ? 62  PRO B CD  1 
ATOM   1494 N  N   . HIS B 1 69  ? -3.210  1.240   45.235 1.00 28.86 ? 63  HIS B N   1 
ATOM   1495 C  CA  . HIS B 1 69  ? -2.303  0.163   45.632 1.00 25.29 ? 63  HIS B CA  1 
ATOM   1496 C  C   . HIS B 1 69  ? -2.651  -1.067  44.800 1.00 29.07 ? 63  HIS B C   1 
ATOM   1497 O  O   . HIS B 1 69  ? -3.839  -1.300  44.515 1.00 22.59 ? 63  HIS B O   1 
ATOM   1498 C  CB  . HIS B 1 69  ? -2.503  -0.168  47.109 1.00 17.94 ? 63  HIS B CB  1 
ATOM   1499 C  CG  . HIS B 1 69  ? -2.142  0.949   48.050 1.00 20.76 ? 63  HIS B CG  1 
ATOM   1500 N  ND1 . HIS B 1 69  ? -2.249  0.826   49.420 1.00 26.42 ? 63  HIS B ND1 1 
ATOM   1501 C  CD2 . HIS B 1 69  ? -1.669  2.198   47.822 1.00 26.49 ? 63  HIS B CD2 1 
ATOM   1502 C  CE1 . HIS B 1 69  ? -1.856  1.952   49.993 1.00 26.42 ? 63  HIS B CE1 1 
ATOM   1503 N  NE2 . HIS B 1 69  ? -1.497  2.800   49.046 1.00 24.14 ? 63  HIS B NE2 1 
ATOM   1504 N  N   . PHE B 1 70  ? -1.646  -1.875  44.441 1.00 20.85 ? 64  PHE B N   1 
ATOM   1505 C  CA  . PHE B 1 70  ? -1.887  -3.098  43.635 1.00 23.71 ? 64  PHE B CA  1 
ATOM   1506 C  C   . PHE B 1 70  ? -2.887  -3.944  44.412 1.00 24.45 ? 64  PHE B C   1 
ATOM   1507 O  O   . PHE B 1 70  ? -2.600  -4.442  45.488 1.00 25.53 ? 64  PHE B O   1 
ATOM   1508 C  CB  . PHE B 1 70  ? -0.576  -3.859  43.416 1.00 25.73 ? 64  PHE B CB  1 
ATOM   1509 C  CG  . PHE B 1 70  ? -0.700  -5.122  42.564 1.00 23.41 ? 64  PHE B CG  1 
ATOM   1510 C  CD1 . PHE B 1 70  ? -1.593  -5.199  41.503 1.00 31.80 ? 64  PHE B CD1 1 
ATOM   1511 C  CD2 . PHE B 1 70  ? 0.116   -6.211  42.827 1.00 24.49 ? 64  PHE B CD2 1 
ATOM   1512 C  CE1 . PHE B 1 70  ? -1.665  -6.360  40.708 1.00 31.49 ? 64  PHE B CE1 1 
ATOM   1513 C  CE2 . PHE B 1 70  ? 0.058   -7.376  42.049 1.00 28.33 ? 64  PHE B CE2 1 
ATOM   1514 C  CZ  . PHE B 1 70  ? -0.834  -7.447  40.984 1.00 26.66 ? 64  PHE B CZ  1 
ATOM   1515 N  N   . ASN B 1 71  ? -4.078  -4.117  43.854 1.00 22.20 ? 65  ASN B N   1 
ATOM   1516 C  CA  . ASN B 1 71  ? -5.125  -4.818  44.571 1.00 19.25 ? 65  ASN B CA  1 
ATOM   1517 C  C   . ASN B 1 71  ? -5.914  -5.781  43.693 1.00 28.90 ? 65  ASN B C   1 
ATOM   1518 O  O   . ASN B 1 71  ? -7.135  -5.624  43.501 1.00 27.29 ? 65  ASN B O   1 
ATOM   1519 C  CB  . ASN B 1 71  ? -6.084  -3.792  45.173 1.00 32.98 ? 65  ASN B CB  1 
ATOM   1520 C  CG  . ASN B 1 71  ? -6.600  -2.806  44.143 1.00 40.29 ? 65  ASN B CG  1 
ATOM   1521 O  OD1 . ASN B 1 71  ? -7.604  -2.126  44.361 1.00 59.04 ? 65  ASN B OD1 1 
ATOM   1522 N  ND2 . ASN B 1 71  ? -5.908  -2.712  43.019 1.00 53.45 ? 65  ASN B ND2 1 
ATOM   1523 N  N   . PRO B 1 72  ? -5.237  -6.794  43.164 1.00 29.14 ? 66  PRO B N   1 
ATOM   1524 C  CA  . PRO B 1 72  ? -5.882  -7.775  42.299 1.00 30.63 ? 66  PRO B CA  1 
ATOM   1525 C  C   . PRO B 1 72  ? -7.021  -8.540  42.953 1.00 34.69 ? 66  PRO B C   1 
ATOM   1526 O  O   . PRO B 1 72  ? -7.881  -9.074  42.263 1.00 30.70 ? 66  PRO B O   1 
ATOM   1527 C  CB  . PRO B 1 72  ? -4.723  -8.676  41.881 1.00 34.68 ? 66  PRO B CB  1 
ATOM   1528 C  CG  . PRO B 1 72  ? -3.832  -8.651  43.101 1.00 33.07 ? 66  PRO B CG  1 
ATOM   1529 C  CD  . PRO B 1 72  ? -3.854  -7.202  43.501 1.00 32.34 ? 66  PRO B CD  1 
ATOM   1530 N  N   . LEU B 1 73  ? -7.058  -8.604  44.277 1.00 28.68 ? 67  LEU B N   1 
ATOM   1531 C  CA  . LEU B 1 73  ? -8.156  -9.340  44.904 1.00 33.27 ? 67  LEU B CA  1 
ATOM   1532 C  C   . LEU B 1 73  ? -9.255  -8.417  45.437 1.00 32.73 ? 67  LEU B C   1 
ATOM   1533 O  O   . LEU B 1 73  ? -10.202 -8.879  46.067 1.00 33.93 ? 67  LEU B O   1 
ATOM   1534 C  CB  . LEU B 1 73  ? -7.614  -10.213 46.033 1.00 34.68 ? 67  LEU B CB  1 
ATOM   1535 C  CG  . LEU B 1 73  ? -6.436  -11.114 45.626 1.00 36.50 ? 67  LEU B CG  1 
ATOM   1536 C  CD1 . LEU B 1 73  ? -6.075  -12.028 46.814 1.00 45.99 ? 67  LEU B CD1 1 
ATOM   1537 C  CD2 . LEU B 1 73  ? -6.796  -11.955 44.411 1.00 43.01 ? 67  LEU B CD2 1 
ATOM   1538 N  N   . SER B 1 74  ? -9.108  -7.119  45.186 1.00 30.61 ? 68  SER B N   1 
ATOM   1539 C  CA  . SER B 1 74  ? -10.060 -6.085  45.628 1.00 30.98 ? 68  SER B CA  1 
ATOM   1540 C  C   . SER B 1 74  ? -10.280 -6.039  47.135 1.00 34.93 ? 68  SER B C   1 
ATOM   1541 O  O   . SER B 1 74  ? -11.404 -5.880  47.622 1.00 32.44 ? 68  SER B O   1 
ATOM   1542 C  CB  . SER B 1 74  ? -11.411 -6.246  44.933 1.00 41.25 ? 68  SER B CB  1 
ATOM   1543 O  OG  . SER B 1 74  ? -11.261 -6.180  43.527 1.00 42.69 ? 68  SER B OG  1 
ATOM   1544 N  N   . ARG B 1 75  ? -9.189  -6.159  47.872 1.00 29.33 ? 69  ARG B N   1 
ATOM   1545 C  CA  . ARG B 1 75  ? -9.235  -6.139  49.327 1.00 26.69 ? 69  ARG B CA  1 
ATOM   1546 C  C   . ARG B 1 75  ? -9.021  -4.758  49.929 1.00 25.60 ? 69  ARG B C   1 
ATOM   1547 O  O   . ARG B 1 75  ? -8.684  -3.817  49.225 1.00 29.80 ? 69  ARG B O   1 
ATOM   1548 C  CB  . ARG B 1 75  ? -8.188  -7.107  49.860 1.00 25.40 ? 69  ARG B CB  1 
ATOM   1549 C  CG  . ARG B 1 75  ? -8.605  -8.565  49.620 1.00 34.34 ? 69  ARG B CG  1 
ATOM   1550 C  CD  . ARG B 1 75  ? -7.610  -9.538  50.205 1.00 33.46 ? 69  ARG B CD  1 
ATOM   1551 N  NE  . ARG B 1 75  ? -6.296  -9.382  49.596 1.00 31.98 ? 69  ARG B NE  1 
ATOM   1552 C  CZ  . ARG B 1 75  ? -5.262  -10.166 49.866 1.00 31.25 ? 69  ARG B CZ  1 
ATOM   1553 N  NH1 . ARG B 1 75  ? -5.407  -11.153 50.736 1.00 37.44 ? 69  ARG B NH1 1 
ATOM   1554 N  NH2 . ARG B 1 75  ? -4.093  -9.968  49.260 1.00 36.24 ? 69  ARG B NH2 1 
ATOM   1555 N  N   . LYS B 1 76  ? -9.240  -4.638  51.234 1.00 25.02 ? 70  LYS B N   1 
ATOM   1556 C  CA  . LYS B 1 76  ? -9.005  -3.381  51.917 1.00 24.90 ? 70  LYS B CA  1 
ATOM   1557 C  C   . LYS B 1 76  ? -7.524  -3.299  52.282 1.00 23.64 ? 70  LYS B C   1 
ATOM   1558 O  O   . LYS B 1 76  ? -6.831  -4.331  52.423 1.00 21.83 ? 70  LYS B O   1 
ATOM   1559 C  CB  . LYS B 1 76  ? -9.814  -3.286  53.206 1.00 32.05 ? 70  LYS B CB  1 
ATOM   1560 C  CG  . LYS B 1 76  ? -11.296 -3.484  53.030 1.00 41.42 ? 70  LYS B CG  1 
ATOM   1561 C  CD  . LYS B 1 76  ? -11.897 -2.443  52.125 1.00 49.80 ? 70  LYS B CD  1 
ATOM   1562 C  CE  . LYS B 1 76  ? -13.070 -1.756  52.818 1.00 53.98 ? 70  LYS B CE  1 
ATOM   1563 N  NZ  . LYS B 1 76  ? -14.019 -2.759  53.389 1.00 51.71 ? 70  LYS B NZ  1 
ATOM   1564 N  N   . HIS B 1 77  ? -7.056  -2.070  52.457 1.00 24.68 ? 71  HIS B N   1 
ATOM   1565 C  CA  . HIS B 1 77  ? -5.657  -1.804  52.826 1.00 23.37 ? 71  HIS B CA  1 
ATOM   1566 C  C   . HIS B 1 77  ? -5.318  -2.424  54.200 1.00 28.07 ? 71  HIS B C   1 
ATOM   1567 O  O   . HIS B 1 77  ? -6.146  -2.459  55.097 1.00 21.25 ? 71  HIS B O   1 
ATOM   1568 C  CB  . HIS B 1 77  ? -5.421  -0.288  52.853 1.00 19.00 ? 71  HIS B CB  1 
ATOM   1569 C  CG  . HIS B 1 77  ? -4.003  0.105   53.163 1.00 23.08 ? 71  HIS B CG  1 
ATOM   1570 N  ND1 . HIS B 1 77  ? -2.963  -0.061  52.271 1.00 19.33 ? 71  HIS B ND1 1 
ATOM   1571 C  CD2 . HIS B 1 77  ? -3.450  0.615   54.291 1.00 29.86 ? 71  HIS B CD2 1 
ATOM   1572 C  CE1 . HIS B 1 77  ? -1.832  0.322   52.839 1.00 23.28 ? 71  HIS B CE1 1 
ATOM   1573 N  NE2 . HIS B 1 77  ? -2.099  0.739   54.064 1.00 26.23 ? 71  HIS B NE2 1 
ATOM   1574 N  N   . GLY B 1 78  ? -4.099  -2.925  54.353 1.00 24.47 ? 72  GLY B N   1 
ATOM   1575 C  CA  . GLY B 1 78  ? -3.703  -3.469  55.630 1.00 25.26 ? 72  GLY B CA  1 
ATOM   1576 C  C   . GLY B 1 78  ? -2.201  -3.382  55.801 1.00 28.12 ? 72  GLY B C   1 
ATOM   1577 O  O   . GLY B 1 78  ? -1.498  -2.737  55.009 1.00 28.71 ? 72  GLY B O   1 
ATOM   1578 N  N   . GLY B 1 79  ? -1.708  -4.026  56.850 1.00 39.32 ? 73  GLY B N   1 
ATOM   1579 C  CA  . GLY B 1 79  ? -0.288  -4.057  57.114 1.00 32.44 ? 73  GLY B CA  1 
ATOM   1580 C  C   . GLY B 1 79  ? 0.220   -5.332  56.491 1.00 37.78 ? 73  GLY B C   1 
ATOM   1581 O  O   . GLY B 1 79  ? -0.578  -6.212  56.159 1.00 34.77 ? 73  GLY B O   1 
ATOM   1582 N  N   . PRO B 1 80  ? 1.541   -5.486  56.346 1.00 33.04 ? 74  PRO B N   1 
ATOM   1583 C  CA  . PRO B 1 80  ? 2.098   -6.693  55.732 1.00 35.71 ? 74  PRO B CA  1 
ATOM   1584 C  C   . PRO B 1 80  ? 1.782   -8.025  56.406 1.00 36.77 ? 74  PRO B C   1 
ATOM   1585 O  O   . PRO B 1 80  ? 1.766   -9.069  55.758 1.00 33.69 ? 74  PRO B O   1 
ATOM   1586 C  CB  . PRO B 1 80  ? 3.597   -6.391  55.647 1.00 35.36 ? 74  PRO B CB  1 
ATOM   1587 C  CG  . PRO B 1 80  ? 3.839   -5.400  56.760 1.00 41.50 ? 74  PRO B CG  1 
ATOM   1588 C  CD  . PRO B 1 80  ? 2.599   -4.521  56.708 1.00 44.43 ? 74  PRO B CD  1 
ATOM   1589 N  N   . LYS B 1 81  ? 1.510   -7.993  57.700 1.00 36.83 ? 75  LYS B N   1 
ATOM   1590 C  CA  . LYS B 1 81  ? 1.207   -9.227  58.390 1.00 40.42 ? 75  LYS B CA  1 
ATOM   1591 C  C   . LYS B 1 81  ? -0.293  -9.512  58.487 1.00 40.94 ? 75  LYS B C   1 
ATOM   1592 O  O   . LYS B 1 81  ? -0.699  -10.571 58.957 1.00 42.45 ? 75  LYS B O   1 
ATOM   1593 C  CB  . LYS B 1 81  ? 1.884   -9.211  59.772 1.00 38.75 ? 75  LYS B CB  1 
ATOM   1594 C  CG  . LYS B 1 81  ? 3.421   -9.292  59.688 1.00 43.62 ? 75  LYS B CG  1 
ATOM   1595 C  CD  . LYS B 1 81  ? 3.865   -10.567 58.947 1.00 56.36 ? 75  LYS B CD  1 
ATOM   1596 C  CE  . LYS B 1 81  ? 5.374   -10.629 58.664 1.00 60.50 ? 75  LYS B CE  1 
ATOM   1597 N  NZ  . LYS B 1 81  ? 5.825   -9.648  57.628 1.00 55.18 ? 75  LYS B NZ  1 
ATOM   1598 N  N   . ASP B 1 82  ? -1.116  -8.577  58.023 1.00 39.36 ? 76  ASP B N   1 
ATOM   1599 C  CA  . ASP B 1 82  ? -2.573  -8.756  58.061 1.00 43.24 ? 76  ASP B CA  1 
ATOM   1600 C  C   . ASP B 1 82  ? -3.087  -9.701  56.981 1.00 37.80 ? 76  ASP B C   1 
ATOM   1601 O  O   . ASP B 1 82  ? -2.589  -9.695  55.853 1.00 26.75 ? 76  ASP B O   1 
ATOM   1602 C  CB  . ASP B 1 82  ? -3.295  -7.412  57.875 1.00 43.85 ? 76  ASP B CB  1 
ATOM   1603 C  CG  . ASP B 1 82  ? -3.204  -6.522  59.094 1.00 60.50 ? 76  ASP B CG  1 
ATOM   1604 O  OD1 . ASP B 1 82  ? -3.381  -7.033  60.221 1.00 65.96 ? 76  ASP B OD1 1 
ATOM   1605 O  OD2 . ASP B 1 82  ? -2.972  -5.307  58.930 1.00 53.74 ? 76  ASP B OD2 1 
ATOM   1606 N  N   . GLU B 1 83  ? -4.093  -10.507 57.301 1.00 30.21 ? 77  GLU B N   1 
ATOM   1607 C  CA  . GLU B 1 83  ? -4.638  -11.386 56.272 1.00 32.66 ? 77  GLU B CA  1 
ATOM   1608 C  C   . GLU B 1 83  ? -5.324  -10.463 55.281 1.00 29.95 ? 77  GLU B C   1 
ATOM   1609 O  O   . GLU B 1 83  ? -5.316  -10.720 54.064 1.00 34.12 ? 77  GLU B O   1 
ATOM   1610 C  CB  . GLU B 1 83  ? -5.664  -12.364 56.840 1.00 39.84 ? 77  GLU B CB  1 
ATOM   1611 C  CG  . GLU B 1 83  ? -5.127  -13.311 57.880 1.00 43.80 ? 77  GLU B CG  1 
ATOM   1612 C  CD  . GLU B 1 83  ? -6.045  -14.495 58.070 1.00 56.65 ? 77  GLU B CD  1 
ATOM   1613 O  OE1 . GLU B 1 83  ? -5.683  -15.608 57.637 1.00 64.98 ? 77  GLU B OE1 1 
ATOM   1614 O  OE2 . GLU B 1 83  ? -7.137  -14.308 58.639 1.00 56.24 ? 77  GLU B OE2 1 
ATOM   1615 N  N   . GLU B 1 84  ? -5.929  -9.396  55.805 1.00 22.39 ? 78  GLU B N   1 
ATOM   1616 C  CA  . GLU B 1 84  ? -6.582  -8.412  54.918 1.00 29.91 ? 78  GLU B CA  1 
ATOM   1617 C  C   . GLU B 1 84  ? -5.628  -7.231  54.583 1.00 29.14 ? 78  GLU B C   1 
ATOM   1618 O  O   . GLU B 1 84  ? -5.336  -6.348  55.418 1.00 27.93 ? 78  GLU B O   1 
ATOM   1619 C  CB  . GLU B 1 84  ? -7.880  -7.886  55.530 1.00 30.54 ? 78  GLU B CB  1 
ATOM   1620 C  CG  . GLU B 1 84  ? -8.639  -6.843  54.651 1.00 30.78 ? 78  GLU B CG  1 
ATOM   1621 C  CD  . GLU B 1 84  ? -9.514  -7.446  53.524 1.00 36.93 ? 78  GLU B CD  1 
ATOM   1622 O  OE1 . GLU B 1 84  ? -10.178 -6.672  52.812 1.00 37.82 ? 78  GLU B OE1 1 
ATOM   1623 O  OE2 . GLU B 1 84  ? -9.559  -8.678  53.329 1.00 31.45 ? 78  GLU B OE2 1 
ATOM   1624 N  N   . ARG B 1 85  ? -5.143  -7.243  53.350 1.00 24.64 ? 79  ARG B N   1 
ATOM   1625 C  CA  . ARG B 1 85  ? -4.238  -6.214  52.859 1.00 24.89 ? 79  ARG B CA  1 
ATOM   1626 C  C   . ARG B 1 85  ? -4.259  -6.325  51.368 1.00 25.07 ? 79  ARG B C   1 
ATOM   1627 O  O   . ARG B 1 85  ? -4.757  -7.317  50.790 1.00 22.67 ? 79  ARG B O   1 
ATOM   1628 C  CB  . ARG B 1 85  ? -2.778  -6.468  53.339 1.00 26.15 ? 79  ARG B CB  1 
ATOM   1629 C  CG  . ARG B 1 85  ? -2.254  -7.858  52.984 1.00 30.73 ? 79  ARG B CG  1 
ATOM   1630 C  CD  . ARG B 1 85  ? -0.715  -8.017  53.148 1.00 24.78 ? 79  ARG B CD  1 
ATOM   1631 N  NE  . ARG B 1 85  ? -0.001  -7.647  51.919 1.00 23.73 ? 79  ARG B NE  1 
ATOM   1632 C  CZ  . ARG B 1 85  ? 1.315   -7.821  51.736 1.00 33.05 ? 79  ARG B CZ  1 
ATOM   1633 N  NH1 . ARG B 1 85  ? 2.060   -8.346  52.700 1.00 22.94 ? 79  ARG B NH1 1 
ATOM   1634 N  NH2 . ARG B 1 85  ? 1.886   -7.503  50.585 1.00 26.99 ? 79  ARG B NH2 1 
ATOM   1635 N  N   . HIS B 1 86  ? -3.740  -5.290  50.735 1.00 20.57 ? 80  HIS B N   1 
ATOM   1636 C  CA  . HIS B 1 86  ? -3.623  -5.288  49.292 1.00 19.10 ? 80  HIS B CA  1 
ATOM   1637 C  C   . HIS B 1 86  ? -2.351  -6.061  49.062 1.00 27.39 ? 80  HIS B C   1 
ATOM   1638 O  O   . HIS B 1 86  ? -1.474  -6.091  49.938 1.00 20.05 ? 80  HIS B O   1 
ATOM   1639 C  CB  . HIS B 1 86  ? -3.437  -3.880  48.797 1.00 24.15 ? 80  HIS B CB  1 
ATOM   1640 C  CG  . HIS B 1 86  ? -4.638  -3.013  49.014 1.00 20.90 ? 80  HIS B CG  1 
ATOM   1641 N  ND1 . HIS B 1 86  ? -4.545  -1.716  49.451 1.00 18.17 ? 80  HIS B ND1 1 
ATOM   1642 C  CD2 . HIS B 1 86  ? -5.953  -3.242  48.777 1.00 18.72 ? 80  HIS B CD2 1 
ATOM   1643 C  CE1 . HIS B 1 86  ? -5.745  -1.165  49.470 1.00 22.48 ? 80  HIS B CE1 1 
ATOM   1644 N  NE2 . HIS B 1 86  ? -6.621  -2.076  49.061 1.00 22.87 ? 80  HIS B NE2 1 
ATOM   1645 N  N   . VAL B 1 87  ? -2.264  -6.700  47.907 1.00 25.21 ? 81  VAL B N   1 
ATOM   1646 C  CA  . VAL B 1 87  ? -1.085  -7.462  47.571 1.00 20.83 ? 81  VAL B CA  1 
ATOM   1647 C  C   . VAL B 1 87  ? 0.092   -6.489  47.606 1.00 23.73 ? 81  VAL B C   1 
ATOM   1648 O  O   . VAL B 1 87  ? 1.178   -6.867  47.995 1.00 21.67 ? 81  VAL B O   1 
ATOM   1649 C  CB  . VAL B 1 87  ? -1.210  -8.066  46.184 1.00 22.86 ? 81  VAL B CB  1 
ATOM   1650 C  CG1 . VAL B 1 87  ? 0.152   -8.560  45.693 1.00 21.38 ? 81  VAL B CG1 1 
ATOM   1651 C  CG2 . VAL B 1 87  ? -2.213  -9.251  46.242 1.00 19.82 ? 81  VAL B CG2 1 
ATOM   1652 N  N   . GLY B 1 88  ? -0.140  -5.232  47.257 1.00 21.58 ? 82  GLY B N   1 
ATOM   1653 C  CA  . GLY B 1 88  ? 0.975   -4.286  47.240 1.00 28.70 ? 82  GLY B CA  1 
ATOM   1654 C  C   . GLY B 1 88  ? 1.411   -3.659  48.553 1.00 22.68 ? 82  GLY B C   1 
ATOM   1655 O  O   . GLY B 1 88  ? 2.384   -2.881  48.587 1.00 25.22 ? 82  GLY B O   1 
ATOM   1656 N  N   . ASP B 1 89  ? 0.732   -3.988  49.649 1.00 20.55 ? 83  ASP B N   1 
ATOM   1657 C  CA  . ASP B 1 89  ? 1.080   -3.376  50.919 1.00 21.63 ? 83  ASP B CA  1 
ATOM   1658 C  C   . ASP B 1 89  ? 2.363   -3.880  51.561 1.00 26.31 ? 83  ASP B C   1 
ATOM   1659 O  O   . ASP B 1 89  ? 2.332   -4.771  52.400 1.00 28.81 ? 83  ASP B O   1 
ATOM   1660 C  CB  . ASP B 1 89  ? -0.070  -3.501  51.915 1.00 28.49 ? 83  ASP B CB  1 
ATOM   1661 C  CG  . ASP B 1 89  ? -1.345  -2.839  51.400 1.00 24.57 ? 83  ASP B CG  1 
ATOM   1662 O  OD1 . ASP B 1 89  ? -1.214  -2.026  50.480 1.00 20.68 ? 83  ASP B OD1 1 
ATOM   1663 O  OD2 . ASP B 1 89  ? -2.436  -3.161  51.895 1.00 22.20 ? 83  ASP B OD2 1 
ATOM   1664 N  N   . LEU B 1 90  ? 3.490   -3.269  51.205 1.00 23.38 ? 84  LEU B N   1 
ATOM   1665 C  CA  . LEU B 1 90  ? 4.742   -3.701  51.818 1.00 31.34 ? 84  LEU B CA  1 
ATOM   1666 C  C   . LEU B 1 90  ? 4.772   -2.806  53.056 1.00 39.86 ? 84  LEU B C   1 
ATOM   1667 O  O   . LEU B 1 90  ? 3.791   -2.113  53.351 1.00 40.20 ? 84  LEU B O   1 
ATOM   1668 C  CB  . LEU B 1 90  ? 5.925   -3.481  50.863 1.00 23.38 ? 84  LEU B CB  1 
ATOM   1669 C  CG  . LEU B 1 90  ? 5.820   -4.215  49.520 1.00 34.53 ? 84  LEU B CG  1 
ATOM   1670 C  CD1 . LEU B 1 90  ? 6.961   -3.778  48.611 1.00 31.88 ? 84  LEU B CD1 1 
ATOM   1671 C  CD2 . LEU B 1 90  ? 5.874   -5.744  49.731 1.00 29.58 ? 84  LEU B CD2 1 
ATOM   1672 N  N   . ARG B 1 91  ? 5.854   -2.774  53.790 1.00 42.95 ? 85  ARG B N   1 
ATOM   1673 C  CA  . ARG B 1 91  ? 5.802   -1.984  54.999 1.00 42.15 ? 85  ARG B CA  1 
ATOM   1674 C  C   . ARG B 1 91  ? 6.339   -0.587  54.906 1.00 43.55 ? 85  ARG B C   1 
ATOM   1675 O  O   . ARG B 1 91  ? 6.824   -0.153  53.869 1.00 54.20 ? 85  ARG B O   1 
ATOM   1676 C  CB  . ARG B 1 91  ? 6.549   -2.708  56.093 1.00 53.96 ? 85  ARG B CB  1 
ATOM   1677 C  CG  . ARG B 1 91  ? 8.031   -2.644  55.920 1.00 41.31 ? 85  ARG B CG  1 
ATOM   1678 C  CD  . ARG B 1 91  ? 8.599   -3.788  56.657 1.00 54.22 ? 85  ARG B CD  1 
ATOM   1679 N  NE  . ARG B 1 91  ? 8.034   -5.030  56.136 1.00 50.08 ? 85  ARG B NE  1 
ATOM   1680 C  CZ  . ARG B 1 91  ? 8.465   -6.231  56.493 1.00 47.78 ? 85  ARG B CZ  1 
ATOM   1681 N  NH1 . ARG B 1 91  ? 9.449   -6.325  57.371 1.00 42.22 ? 85  ARG B NH1 1 
ATOM   1682 N  NH2 . ARG B 1 91  ? 7.942   -7.323  55.953 1.00 37.11 ? 85  ARG B NH2 1 
ATOM   1683 N  N   . ASN B 1 92  ? 6.251   0.113   56.021 1.00 26.71 ? 86  ASN B N   1 
ATOM   1684 C  CA  . ASN B 1 92  ? 6.782   1.459   56.097 1.00 23.95 ? 86  ASN B CA  1 
ATOM   1685 C  C   . ASN B 1 92  ? 8.306   1.309   56.067 1.00 28.50 ? 86  ASN B C   1 
ATOM   1686 O  O   . ASN B 1 92  ? 8.855   0.406   56.711 1.00 25.22 ? 86  ASN B O   1 
ATOM   1687 C  CB  . ASN B 1 92  ? 6.414   2.098   57.438 1.00 31.25 ? 86  ASN B CB  1 
ATOM   1688 C  CG  . ASN B 1 92  ? 5.023   2.709   57.447 1.00 27.84 ? 86  ASN B CG  1 
ATOM   1689 O  OD1 . ASN B 1 92  ? 4.704   3.548   56.627 1.00 32.55 ? 86  ASN B OD1 1 
ATOM   1690 N  ND2 . ASN B 1 92  ? 4.215   2.311   58.405 1.00 29.81 ? 86  ASN B ND2 1 
ATOM   1691 N  N   . VAL B 1 93  ? 9.004   2.141   55.313 1.00 27.63 ? 87  VAL B N   1 
ATOM   1692 C  CA  . VAL B 1 93  ? 10.457  2.027   55.398 1.00 30.70 ? 87  VAL B CA  1 
ATOM   1693 C  C   . VAL B 1 93  ? 10.869  3.142   56.350 1.00 27.63 ? 87  VAL B C   1 
ATOM   1694 O  O   . VAL B 1 93  ? 10.145  4.134   56.516 1.00 24.49 ? 87  VAL B O   1 
ATOM   1695 C  CB  . VAL B 1 93  ? 11.167  2.144   54.004 1.00 30.54 ? 87  VAL B CB  1 
ATOM   1696 C  CG1 . VAL B 1 93  ? 10.632  1.066   53.066 1.00 34.30 ? 87  VAL B CG1 1 
ATOM   1697 C  CG2 . VAL B 1 93  ? 10.964  3.511   53.400 1.00 30.37 ? 87  VAL B CG2 1 
ATOM   1698 N  N   . THR B 1 94  ? 12.008  2.973   57.005 1.00 27.77 ? 88  THR B N   1 
ATOM   1699 C  CA  . THR B 1 94  ? 12.487  3.972   57.960 1.00 31.29 ? 88  THR B CA  1 
ATOM   1700 C  C   . THR B 1 94  ? 13.681  4.740   57.414 1.00 25.31 ? 88  THR B C   1 
ATOM   1701 O  O   . THR B 1 94  ? 14.660  4.121   56.986 1.00 24.91 ? 88  THR B O   1 
ATOM   1702 C  CB  . THR B 1 94  ? 12.938  3.300   59.297 1.00 37.26 ? 88  THR B CB  1 
ATOM   1703 O  OG1 . THR B 1 94  ? 11.827  2.620   59.899 1.00 46.87 ? 88  THR B OG1 1 
ATOM   1704 C  CG2 . THR B 1 94  ? 13.461  4.340   60.254 1.00 38.86 ? 88  THR B CG2 1 
ATOM   1705 N  N   . ALA B 1 95  ? 13.598  6.068   57.440 1.00 25.32 ? 89  ALA B N   1 
ATOM   1706 C  CA  . ALA B 1 95  ? 14.683  6.917   56.981 1.00 27.99 ? 89  ALA B CA  1 
ATOM   1707 C  C   . ALA B 1 95  ? 15.307  7.592   58.207 1.00 24.68 ? 89  ALA B C   1 
ATOM   1708 O  O   . ALA B 1 95  ? 14.602  8.148   59.053 1.00 28.80 ? 89  ALA B O   1 
ATOM   1709 C  CB  . ALA B 1 95  ? 14.162  7.961   56.035 1.00 34.13 ? 89  ALA B CB  1 
ATOM   1710 N  N   . ASP B 1 96  ? 16.631  7.547   58.301 1.00 33.01 ? 90  ASP B N   1 
ATOM   1711 C  CA  . ASP B 1 96  ? 17.327  8.173   59.428 1.00 29.29 ? 90  ASP B CA  1 
ATOM   1712 C  C   . ASP B 1 96  ? 17.462  9.693   59.243 1.00 36.83 ? 90  ASP B C   1 
ATOM   1713 O  O   . ASP B 1 96  ? 16.961  10.272  58.267 1.00 29.41 ? 90  ASP B O   1 
ATOM   1714 C  CB  . ASP B 1 96  ? 18.710  7.542   59.604 1.00 39.50 ? 90  ASP B CB  1 
ATOM   1715 C  CG  . ASP B 1 96  ? 19.166  7.534   61.053 1.00 56.83 ? 90  ASP B CG  1 
ATOM   1716 O  OD1 . ASP B 1 96  ? 20.157  6.829   61.349 1.00 54.36 ? 90  ASP B OD1 1 
ATOM   1717 O  OD2 . ASP B 1 96  ? 18.540  8.231   61.895 1.00 62.52 ? 90  ASP B OD2 1 
ATOM   1718 N  N   . LYS B 1 97  ? 18.140  10.335  60.197 1.00 38.00 ? 91  LYS B N   1 
ATOM   1719 C  CA  . LYS B 1 97  ? 18.347  11.776  60.186 1.00 36.11 ? 91  LYS B CA  1 
ATOM   1720 C  C   . LYS B 1 97  ? 18.916  12.248  58.845 1.00 33.27 ? 91  LYS B C   1 
ATOM   1721 O  O   . LYS B 1 97  ? 18.523  13.295  58.301 1.00 31.36 ? 91  LYS B O   1 
ATOM   1722 C  CB  . LYS B 1 97  ? 19.297  12.137  61.330 1.00 46.55 ? 91  LYS B CB  1 
ATOM   1723 C  CG  . LYS B 1 97  ? 18.808  13.239  62.255 1.00 55.46 ? 91  LYS B CG  1 
ATOM   1724 C  CD  . LYS B 1 97  ? 18.671  14.582  61.547 1.00 48.72 ? 91  LYS B CD  1 
ATOM   1725 C  CE  . LYS B 1 97  ? 18.368  15.712  62.540 1.00 55.28 ? 91  LYS B CE  1 
ATOM   1726 N  NZ  . LYS B 1 97  ? 17.132  15.483  63.366 1.00 61.19 ? 91  LYS B NZ  1 
ATOM   1727 N  N   . ASP B 1 98  ? 19.846  11.463  58.307 1.00 36.61 ? 92  ASP B N   1 
ATOM   1728 C  CA  . ASP B 1 98  ? 20.466  11.785  57.027 1.00 36.95 ? 92  ASP B CA  1 
ATOM   1729 C  C   . ASP B 1 98  ? 19.565  11.593  55.803 1.00 33.75 ? 92  ASP B C   1 
ATOM   1730 O  O   . ASP B 1 98  ? 20.024  11.752  54.676 1.00 35.79 ? 92  ASP B O   1 
ATOM   1731 C  CB  . ASP B 1 98  ? 21.751  10.969  56.841 1.00 36.52 ? 92  ASP B CB  1 
ATOM   1732 C  CG  . ASP B 1 98  ? 21.505  9.466   56.780 1.00 47.80 ? 92  ASP B CG  1 
ATOM   1733 O  OD1 . ASP B 1 98  ? 22.503  8.713   56.802 1.00 50.22 ? 92  ASP B OD1 1 
ATOM   1734 O  OD2 . ASP B 1 98  ? 20.332  9.032   56.710 1.00 46.71 ? 92  ASP B OD2 1 
ATOM   1735 N  N   . GLY B 1 99  ? 18.302  11.233  56.022 1.00 33.18 ? 93  GLY B N   1 
ATOM   1736 C  CA  . GLY B 1 99  ? 17.366  11.057  54.911 1.00 27.88 ? 93  GLY B CA  1 
ATOM   1737 C  C   . GLY B 1 99  ? 17.491  9.789   54.064 1.00 26.80 ? 93  GLY B C   1 
ATOM   1738 O  O   . GLY B 1 99  ? 16.877  9.670   52.993 1.00 29.39 ? 93  GLY B O   1 
ATOM   1739 N  N   . VAL B 1 100 ? 18.286  8.844   54.539 1.00 29.33 ? 94  VAL B N   1 
ATOM   1740 C  CA  . VAL B 1 100 ? 18.513  7.605   53.830 1.00 23.43 ? 94  VAL B CA  1 
ATOM   1741 C  C   . VAL B 1 100 ? 17.793  6.451   54.483 1.00 29.30 ? 94  VAL B C   1 
ATOM   1742 O  O   . VAL B 1 100 ? 17.863  6.249   55.696 1.00 28.09 ? 94  VAL B O   1 
ATOM   1743 C  CB  . VAL B 1 100 ? 20.012  7.239   53.788 1.00 39.82 ? 94  VAL B CB  1 
ATOM   1744 C  CG1 . VAL B 1 100 ? 20.193  5.847   53.146 1.00 29.22 ? 94  VAL B CG1 1 
ATOM   1745 C  CG2 . VAL B 1 100 ? 20.790  8.315   53.032 1.00 33.55 ? 94  VAL B CG2 1 
ATOM   1746 N  N   . ALA B 1 101 ? 17.120  5.672   53.652 1.00 29.86 ? 95  ALA B N   1 
ATOM   1747 C  CA  . ALA B 1 101 ? 16.391  4.505   54.125 1.00 30.34 ? 95  ALA B CA  1 
ATOM   1748 C  C   . ALA B 1 101 ? 16.996  3.228   53.555 1.00 34.44 ? 95  ALA B C   1 
ATOM   1749 O  O   . ALA B 1 101 ? 16.984  2.997   52.332 1.00 31.56 ? 95  ALA B O   1 
ATOM   1750 C  CB  . ALA B 1 101 ? 14.920  4.623   53.732 1.00 31.26 ? 95  ALA B CB  1 
ATOM   1751 N  N   . ASP B 1 102 ? 17.546  2.400   54.434 1.00 30.55 ? 96  ASP B N   1 
ATOM   1752 C  CA  . ASP B 1 102 ? 18.125  1.141   53.988 1.00 31.46 ? 96  ASP B CA  1 
ATOM   1753 C  C   . ASP B 1 102 ? 16.993  0.148   54.111 1.00 32.99 ? 96  ASP B C   1 
ATOM   1754 O  O   . ASP B 1 102 ? 16.438  -0.052  55.181 1.00 43.94 ? 96  ASP B O   1 
ATOM   1755 C  CB  . ASP B 1 102 ? 19.310  0.732   54.862 1.00 42.01 ? 96  ASP B CB  1 
ATOM   1756 C  CG  . ASP B 1 102 ? 20.522  1.613   54.630 1.00 47.79 ? 96  ASP B CG  1 
ATOM   1757 O  OD1 . ASP B 1 102 ? 20.790  1.936   53.450 1.00 42.71 ? 96  ASP B OD1 1 
ATOM   1758 O  OD2 . ASP B 1 102 ? 21.203  1.980   55.615 1.00 62.89 ? 96  ASP B OD2 1 
ATOM   1759 N  N   . VAL B 1 103 ? 16.641  -0.463  52.996 1.00 31.41 ? 97  VAL B N   1 
ATOM   1760 C  CA  . VAL B 1 103 ? 15.513  -1.384  52.976 1.00 25.27 ? 97  VAL B CA  1 
ATOM   1761 C  C   . VAL B 1 103 ? 15.956  -2.824  52.909 1.00 27.14 ? 97  VAL B C   1 
ATOM   1762 O  O   . VAL B 1 103 ? 16.832  -3.161  52.108 1.00 27.36 ? 97  VAL B O   1 
ATOM   1763 C  CB  . VAL B 1 103 ? 14.637  -1.099  51.737 1.00 22.70 ? 97  VAL B CB  1 
ATOM   1764 C  CG1 . VAL B 1 103 ? 13.465  -2.098  51.670 1.00 24.80 ? 97  VAL B CG1 1 
ATOM   1765 C  CG2 . VAL B 1 103 ? 14.125  0.344   51.788 1.00 25.75 ? 97  VAL B CG2 1 
ATOM   1766 N  N   . SER B 1 104 ? 15.384  -3.665  53.774 1.00 25.84 ? 98  SER B N   1 
ATOM   1767 C  CA  . SER B 1 104 ? 15.673  -5.101  53.745 1.00 21.77 ? 98  SER B CA  1 
ATOM   1768 C  C   . SER B 1 104 ? 14.514  -5.842  54.363 1.00 30.78 ? 98  SER B C   1 
ATOM   1769 O  O   . SER B 1 104 ? 14.403  -5.943  55.586 1.00 29.86 ? 98  SER B O   1 
ATOM   1770 C  CB  . SER B 1 104 ? 16.952  -5.473  54.488 1.00 28.72 ? 98  SER B CB  1 
ATOM   1771 O  OG  . SER B 1 104 ? 17.163  -6.873  54.370 1.00 31.10 ? 98  SER B OG  1 
ATOM   1772 N  N   . ILE B 1 105 ? 13.648  -6.375  53.516 1.00 28.04 ? 99  ILE B N   1 
ATOM   1773 C  CA  . ILE B 1 105 ? 12.496  -7.080  54.020 1.00 25.88 ? 99  ILE B CA  1 
ATOM   1774 C  C   . ILE B 1 105 ? 12.220  -8.310  53.213 1.00 25.62 ? 99  ILE B C   1 
ATOM   1775 O  O   . ILE B 1 105 ? 12.810  -8.517  52.167 1.00 24.66 ? 99  ILE B O   1 
ATOM   1776 C  CB  . ILE B 1 105 ? 11.249  -6.192  53.967 1.00 35.53 ? 99  ILE B CB  1 
ATOM   1777 C  CG1 . ILE B 1 105 ? 10.893  -5.888  52.513 1.00 32.83 ? 99  ILE B CG1 1 
ATOM   1778 C  CG2 . ILE B 1 105 ? 11.505  -4.888  54.696 1.00 39.23 ? 99  ILE B CG2 1 
ATOM   1779 C  CD1 . ILE B 1 105 ? 9.705   -4.946  52.365 1.00 40.30 ? 99  ILE B CD1 1 
ATOM   1780 N  N   . GLU B 1 106 ? 11.315  -9.131  53.722 1.00 22.23 ? 100 GLU B N   1 
ATOM   1781 C  CA  . GLU B 1 106 ? 10.893  -10.330 53.023 1.00 31.67 ? 100 GLU B CA  1 
ATOM   1782 C  C   . GLU B 1 106 ? 9.355   -10.258 52.989 1.00 26.79 ? 100 GLU B C   1 
ATOM   1783 O  O   . GLU B 1 106 ? 8.749   -9.957  53.997 1.00 27.00 ? 100 GLU B O   1 
ATOM   1784 C  CB  . GLU B 1 106 ? 11.359  -11.554 53.798 1.00 44.87 ? 100 GLU B CB  1 
ATOM   1785 C  CG  . GLU B 1 106 ? 10.852  -12.877 53.278 1.00 57.21 ? 100 GLU B CG  1 
ATOM   1786 C  CD  . GLU B 1 106 ? 11.453  -14.040 54.035 1.00 58.99 ? 100 GLU B CD  1 
ATOM   1787 O  OE1 . GLU B 1 106 ? 12.688  -14.207 53.944 1.00 56.04 ? 100 GLU B OE1 1 
ATOM   1788 O  OE2 . GLU B 1 106 ? 10.697  -14.770 54.720 1.00 60.36 ? 100 GLU B OE2 1 
ATOM   1789 N  N   . ASP B 1 107 ? 8.740   -10.469 51.832 1.00 27.19 ? 101 ASP B N   1 
ATOM   1790 C  CA  . ASP B 1 107 ? 7.282   -10.440 51.757 1.00 25.79 ? 101 ASP B CA  1 
ATOM   1791 C  C   . ASP B 1 107 ? 6.738   -11.710 51.105 1.00 26.29 ? 101 ASP B C   1 
ATOM   1792 O  O   . ASP B 1 107 ? 7.228   -12.177 50.060 1.00 26.95 ? 101 ASP B O   1 
ATOM   1793 C  CB  . ASP B 1 107 ? 6.777   -9.218  50.983 1.00 27.49 ? 101 ASP B CB  1 
ATOM   1794 C  CG  . ASP B 1 107 ? 5.249   -9.026  51.125 1.00 36.49 ? 101 ASP B CG  1 
ATOM   1795 O  OD1 . ASP B 1 107 ? 4.804   -8.546  52.190 1.00 30.88 ? 101 ASP B OD1 1 
ATOM   1796 O  OD2 . ASP B 1 107 ? 4.497   -9.371  50.184 1.00 27.95 ? 101 ASP B OD2 1 
ATOM   1797 N  N   . SER B 1 108 ? 5.677   -12.225 51.712 1.00 23.01 ? 102 SER B N   1 
ATOM   1798 C  CA  . SER B 1 108 ? 5.037   -13.458 51.287 1.00 27.65 ? 102 SER B CA  1 
ATOM   1799 C  C   . SER B 1 108 ? 3.877   -13.309 50.312 1.00 25.13 ? 102 SER B C   1 
ATOM   1800 O  O   . SER B 1 108 ? 3.436   -14.287 49.711 1.00 25.73 ? 102 SER B O   1 
ATOM   1801 C  CB  . SER B 1 108 ? 4.536   -14.189 52.543 1.00 26.44 ? 102 SER B CB  1 
ATOM   1802 O  OG  . SER B 1 108 ? 5.633   -14.657 53.311 1.00 39.38 ? 102 SER B OG  1 
ATOM   1803 N  N   . VAL B 1 109 ? 3.380   -12.094 50.142 1.00 22.38 ? 103 VAL B N   1 
ATOM   1804 C  CA  . VAL B 1 109 ? 2.225   -11.920 49.266 1.00 29.20 ? 103 VAL B CA  1 
ATOM   1805 C  C   . VAL B 1 109 ? 2.549   -11.509 47.857 1.00 26.93 ? 103 VAL B C   1 
ATOM   1806 O  O   . VAL B 1 109 ? 1.919   -12.007 46.915 1.00 22.96 ? 103 VAL B O   1 
ATOM   1807 C  CB  . VAL B 1 109 ? 1.222   -10.936 49.905 1.00 24.59 ? 103 VAL B CB  1 
ATOM   1808 C  CG1 . VAL B 1 109 ? -0.027  -10.801 49.036 1.00 25.72 ? 103 VAL B CG1 1 
ATOM   1809 C  CG2 . VAL B 1 109 ? 0.862   -11.448 51.274 1.00 21.65 ? 103 VAL B CG2 1 
ATOM   1810 N  N   . ILE B 1 110 ? 3.500   -10.588 47.683 1.00 21.63 ? 104 ILE B N   1 
ATOM   1811 C  CA  . ILE B 1 110 ? 3.879   -10.233 46.320 1.00 21.68 ? 104 ILE B CA  1 
ATOM   1812 C  C   . ILE B 1 110 ? 4.648   -11.426 45.763 1.00 23.03 ? 104 ILE B C   1 
ATOM   1813 O  O   . ILE B 1 110 ? 4.979   -12.361 46.500 1.00 23.93 ? 104 ILE B O   1 
ATOM   1814 C  CB  . ILE B 1 110 ? 4.821   -8.983  46.245 1.00 24.14 ? 104 ILE B CB  1 
ATOM   1815 C  CG1 . ILE B 1 110 ? 6.075   -9.193  47.098 1.00 20.12 ? 104 ILE B CG1 1 
ATOM   1816 C  CG2 . ILE B 1 110 ? 4.098   -7.720  46.703 1.00 25.51 ? 104 ILE B CG2 1 
ATOM   1817 C  CD1 . ILE B 1 110 ? 7.146   -8.100  46.818 1.00 19.61 ? 104 ILE B CD1 1 
ATOM   1818 N  N   . SER B 1 111 ? 4.924   -11.404 44.466 1.00 24.82 ? 105 SER B N   1 
ATOM   1819 C  CA  . SER B 1 111 ? 5.701   -12.465 43.836 1.00 27.66 ? 105 SER B CA  1 
ATOM   1820 C  C   . SER B 1 111 ? 6.156   -11.944 42.508 1.00 24.28 ? 105 SER B C   1 
ATOM   1821 O  O   . SER B 1 111 ? 5.667   -10.914 42.023 1.00 25.24 ? 105 SER B O   1 
ATOM   1822 C  CB  . SER B 1 111 ? 4.855   -13.726 43.595 1.00 37.87 ? 105 SER B CB  1 
ATOM   1823 O  OG  . SER B 1 111 ? 3.832   -13.427 42.672 1.00 46.39 ? 105 SER B OG  1 
ATOM   1824 N  N   . LEU B 1 112 ? 7.073   -12.670 41.891 1.00 18.18 ? 106 LEU B N   1 
ATOM   1825 C  CA  . LEU B 1 112 ? 7.579   -12.247 40.597 1.00 26.12 ? 106 LEU B CA  1 
ATOM   1826 C  C   . LEU B 1 112 ? 7.031   -13.187 39.551 1.00 31.06 ? 106 LEU B C   1 
ATOM   1827 O  O   . LEU B 1 112 ? 7.474   -13.187 38.409 1.00 32.70 ? 106 LEU B O   1 
ATOM   1828 C  CB  . LEU B 1 112 ? 9.114   -12.252 40.569 1.00 28.57 ? 106 LEU B CB  1 
ATOM   1829 C  CG  . LEU B 1 112 ? 9.842   -11.331 41.562 1.00 36.97 ? 106 LEU B CG  1 
ATOM   1830 C  CD1 . LEU B 1 112 ? 11.364  -11.402 41.367 1.00 32.85 ? 106 LEU B CD1 1 
ATOM   1831 C  CD2 . LEU B 1 112 ? 9.357   -9.918  41.382 1.00 32.13 ? 106 LEU B CD2 1 
ATOM   1832 N  N   . SER B 1 113 ? 6.057   -13.998 39.951 1.00 38.66 ? 107 SER B N   1 
ATOM   1833 C  CA  . SER B 1 113 ? 5.418   -14.927 39.022 1.00 48.85 ? 107 SER B CA  1 
ATOM   1834 C  C   . SER B 1 113 ? 3.976   -15.169 39.449 1.00 48.69 ? 107 SER B C   1 
ATOM   1835 O  O   . SER B 1 113 ? 3.605   -14.892 40.591 1.00 47.11 ? 107 SER B O   1 
ATOM   1836 C  CB  . SER B 1 113 ? 6.192   -16.250 38.973 1.00 48.30 ? 107 SER B CB  1 
ATOM   1837 O  OG  . SER B 1 113 ? 6.357   -16.804 40.267 1.00 49.97 ? 107 SER B OG  1 
ATOM   1838 N  N   . GLY B 1 114 ? 3.147   -15.639 38.522 1.00 48.77 ? 108 GLY B N   1 
ATOM   1839 C  CA  . GLY B 1 114 ? 1.760   -15.915 38.857 1.00 48.93 ? 108 GLY B CA  1 
ATOM   1840 C  C   . GLY B 1 114 ? 0.741   -14.784 38.931 1.00 47.54 ? 108 GLY B C   1 
ATOM   1841 O  O   . GLY B 1 114 ? 0.828   -13.781 38.228 1.00 43.44 ? 108 GLY B O   1 
ATOM   1842 N  N   . ASP B 1 115 ? -0.245  -14.968 39.807 1.00 50.99 ? 109 ASP B N   1 
ATOM   1843 C  CA  . ASP B 1 115 ? -1.335  -14.013 39.981 1.00 50.98 ? 109 ASP B CA  1 
ATOM   1844 C  C   . ASP B 1 115 ? -0.924  -12.729 40.696 1.00 47.50 ? 109 ASP B C   1 
ATOM   1845 O  O   . ASP B 1 115 ? -1.497  -11.658 40.451 1.00 43.62 ? 109 ASP B O   1 
ATOM   1846 C  CB  . ASP B 1 115 ? -2.476  -14.671 40.765 1.00 56.30 ? 109 ASP B CB  1 
ATOM   1847 C  CG  . ASP B 1 115 ? -2.796  -16.080 40.277 1.00 58.34 ? 109 ASP B CG  1 
ATOM   1848 O  OD1 . ASP B 1 115 ? -2.069  -16.614 39.407 1.00 60.30 ? 109 ASP B OD1 1 
ATOM   1849 O  OD2 . ASP B 1 115 ? -3.781  -16.657 40.782 1.00 57.26 ? 109 ASP B OD2 1 
ATOM   1850 N  N   . HIS B 1 116 ? 0.056   -12.827 41.589 1.00 37.94 ? 110 HIS B N   1 
ATOM   1851 C  CA  . HIS B 1 116 ? 0.501   -11.645 42.321 1.00 41.63 ? 110 HIS B CA  1 
ATOM   1852 C  C   . HIS B 1 116 ? 1.794   -11.029 41.785 1.00 45.15 ? 110 HIS B C   1 
ATOM   1853 O  O   . HIS B 1 116 ? 2.474   -10.275 42.507 1.00 29.81 ? 110 HIS B O   1 
ATOM   1854 C  CB  . HIS B 1 116 ? 0.672   -11.961 43.814 1.00 36.12 ? 110 HIS B CB  1 
ATOM   1855 C  CG  . HIS B 1 116 ? -0.596  -12.368 44.501 1.00 50.43 ? 110 HIS B CG  1 
ATOM   1856 N  ND1 . HIS B 1 116 ? -0.697  -12.461 45.873 1.00 50.31 ? 110 HIS B ND1 1 
ATOM   1857 C  CD2 . HIS B 1 116 ? -1.807  -12.727 44.010 1.00 40.10 ? 110 HIS B CD2 1 
ATOM   1858 C  CE1 . HIS B 1 116 ? -1.916  -12.859 46.196 1.00 57.03 ? 110 HIS B CE1 1 
ATOM   1859 N  NE2 . HIS B 1 116 ? -2.608  -13.028 45.084 1.00 45.00 ? 110 HIS B NE2 1 
ATOM   1860 N  N   . CYS B 1 117 ? 2.125   -11.347 40.529 1.00 43.42 ? 111 CYS B N   1 
ATOM   1861 C  CA  . CYS B 1 117 ? 3.332   -10.815 39.886 1.00 38.93 ? 111 CYS B CA  1 
ATOM   1862 C  C   . CYS B 1 117 ? 3.325   -9.284  39.856 1.00 37.04 ? 111 CYS B C   1 
ATOM   1863 O  O   . CYS B 1 117 ? 2.359   -8.653  39.430 1.00 33.90 ? 111 CYS B O   1 
ATOM   1864 C  CB  . CYS B 1 117 ? 3.470   -11.342 38.449 1.00 42.62 ? 111 CYS B CB  1 
ATOM   1865 S  SG  . CYS B 1 117 ? 4.944   -10.677 37.617 1.00 43.49 ? 111 CYS B SG  1 
ATOM   1866 N  N   . ILE B 1 118 ? 4.429   -8.686  40.286 1.00 26.93 ? 112 ILE B N   1 
ATOM   1867 C  CA  . ILE B 1 118 ? 4.543   -7.242  40.347 1.00 27.25 ? 112 ILE B CA  1 
ATOM   1868 C  C   . ILE B 1 118 ? 5.412   -6.628  39.245 1.00 23.13 ? 112 ILE B C   1 
ATOM   1869 O  O   . ILE B 1 118 ? 5.591   -5.416  39.205 1.00 25.97 ? 112 ILE B O   1 
ATOM   1870 C  CB  . ILE B 1 118 ? 5.077   -6.809  41.735 1.00 25.66 ? 112 ILE B CB  1 
ATOM   1871 C  CG1 . ILE B 1 118 ? 6.454   -7.450  41.987 1.00 28.80 ? 112 ILE B CG1 1 
ATOM   1872 C  CG2 . ILE B 1 118 ? 4.097   -7.230  42.824 1.00 28.14 ? 112 ILE B CG2 1 
ATOM   1873 C  CD1 . ILE B 1 118 ? 7.122   -6.989  43.287 1.00 37.03 ? 112 ILE B CD1 1 
ATOM   1874 N  N   . ILE B 1 119 ? 5.948   -7.463  38.355 1.00 25.09 ? 113 ILE B N   1 
ATOM   1875 C  CA  . ILE B 1 119 ? 6.766   -6.972  37.256 1.00 24.50 ? 113 ILE B CA  1 
ATOM   1876 C  C   . ILE B 1 119 ? 5.866   -6.122  36.355 1.00 28.51 ? 113 ILE B C   1 
ATOM   1877 O  O   . ILE B 1 119 ? 4.763   -6.539  35.985 1.00 22.24 ? 113 ILE B O   1 
ATOM   1878 C  CB  . ILE B 1 119 ? 7.397   -8.168  36.497 1.00 27.40 ? 113 ILE B CB  1 
ATOM   1879 C  CG1 . ILE B 1 119 ? 8.451   -8.822  37.419 1.00 35.29 ? 113 ILE B CG1 1 
ATOM   1880 C  CG2 . ILE B 1 119 ? 8.024   -7.715  35.193 1.00 23.84 ? 113 ILE B CG2 1 
ATOM   1881 C  CD1 . ILE B 1 119 ? 9.041   -10.122 36.928 1.00 39.96 ? 113 ILE B CD1 1 
ATOM   1882 N  N   . GLY B 1 120 ? 6.331   -4.927  36.025 1.00 21.46 ? 114 GLY B N   1 
ATOM   1883 C  CA  . GLY B 1 120 ? 5.546   -4.029  35.211 1.00 30.22 ? 114 GLY B CA  1 
ATOM   1884 C  C   . GLY B 1 120 ? 4.627   -3.126  36.032 1.00 27.64 ? 114 GLY B C   1 
ATOM   1885 O  O   . GLY B 1 120 ? 3.867   -2.338  35.456 1.00 27.15 ? 114 GLY B O   1 
ATOM   1886 N  N   . ARG B 1 121 ? 4.660   -3.239  37.365 1.00 19.92 ? 115 ARG B N   1 
ATOM   1887 C  CA  . ARG B 1 121 ? 3.824   -2.374  38.216 1.00 21.19 ? 115 ARG B CA  1 
ATOM   1888 C  C   . ARG B 1 121 ? 4.769   -1.343  38.764 1.00 26.18 ? 115 ARG B C   1 
ATOM   1889 O  O   . ARG B 1 121 ? 5.972   -1.385  38.478 1.00 24.50 ? 115 ARG B O   1 
ATOM   1890 C  CB  . ARG B 1 121 ? 3.202   -3.138  39.389 1.00 19.56 ? 115 ARG B CB  1 
ATOM   1891 C  CG  . ARG B 1 121 ? 2.506   -4.455  39.011 1.00 30.78 ? 115 ARG B CG  1 
ATOM   1892 C  CD  . ARG B 1 121 ? 1.064   -4.240  38.691 1.00 34.21 ? 115 ARG B CD  1 
ATOM   1893 N  NE  . ARG B 1 121 ? 0.418   -5.463  38.212 1.00 38.28 ? 115 ARG B NE  1 
ATOM   1894 C  CZ  . ARG B 1 121 ? -0.807  -5.491  37.699 1.00 33.73 ? 115 ARG B CZ  1 
ATOM   1895 N  NH1 . ARG B 1 121 ? -1.499  -4.372  37.619 1.00 30.29 ? 115 ARG B NH1 1 
ATOM   1896 N  NH2 . ARG B 1 121 ? -1.319  -6.627  37.223 1.00 38.20 ? 115 ARG B NH2 1 
ATOM   1897 N  N   . THR B 1 122 ? 4.246   -0.417  39.549 1.00 24.16 ? 116 THR B N   1 
ATOM   1898 C  CA  . THR B 1 122 ? 5.100   0.625   40.112 1.00 24.18 ? 116 THR B CA  1 
ATOM   1899 C  C   . THR B 1 122 ? 5.299   0.456   41.585 1.00 26.74 ? 116 THR B C   1 
ATOM   1900 O  O   . THR B 1 122 ? 4.421   -0.012  42.301 1.00 24.27 ? 116 THR B O   1 
ATOM   1901 C  CB  . THR B 1 122 ? 4.520   2.049   39.925 1.00 28.18 ? 116 THR B CB  1 
ATOM   1902 O  OG1 . THR B 1 122 ? 3.170   2.064   40.405 1.00 44.21 ? 116 THR B OG1 1 
ATOM   1903 C  CG2 . THR B 1 122 ? 4.579   2.467   38.483 1.00 25.94 ? 116 THR B CG2 1 
ATOM   1904 N  N   . LEU B 1 123 ? 6.482   0.857   42.028 1.00 18.44 ? 117 LEU B N   1 
ATOM   1905 C  CA  . LEU B 1 123 ? 6.824   0.837   43.430 1.00 23.29 ? 117 LEU B CA  1 
ATOM   1906 C  C   . LEU B 1 123 ? 6.754   2.338   43.816 1.00 26.16 ? 117 LEU B C   1 
ATOM   1907 O  O   . LEU B 1 123 ? 7.257   3.200   43.089 1.00 26.63 ? 117 LEU B O   1 
ATOM   1908 C  CB  . LEU B 1 123 ? 8.252   0.272   43.605 1.00 25.32 ? 117 LEU B CB  1 
ATOM   1909 C  CG  . LEU B 1 123 ? 8.777   0.338   45.027 1.00 31.34 ? 117 LEU B CG  1 
ATOM   1910 C  CD1 . LEU B 1 123 ? 7.768   -0.371  45.906 1.00 35.47 ? 117 LEU B CD1 1 
ATOM   1911 C  CD2 . LEU B 1 123 ? 10.179  -0.308  45.131 1.00 24.31 ? 117 LEU B CD2 1 
ATOM   1912 N  N   . VAL B 1 124 ? 6.122   2.650   44.940 1.00 26.86 ? 118 VAL B N   1 
ATOM   1913 C  CA  . VAL B 1 124 ? 5.974   4.040   45.363 1.00 25.85 ? 118 VAL B CA  1 
ATOM   1914 C  C   . VAL B 1 124 ? 6.368   4.233   46.824 1.00 17.85 ? 118 VAL B C   1 
ATOM   1915 O  O   . VAL B 1 124 ? 5.990   3.436   47.666 1.00 19.42 ? 118 VAL B O   1 
ATOM   1916 C  CB  . VAL B 1 124 ? 4.479   4.503   45.204 1.00 25.47 ? 118 VAL B CB  1 
ATOM   1917 C  CG1 . VAL B 1 124 ? 4.327   5.980   45.605 1.00 25.40 ? 118 VAL B CG1 1 
ATOM   1918 C  CG2 . VAL B 1 124 ? 4.021   4.290   43.750 1.00 28.75 ? 118 VAL B CG2 1 
ATOM   1919 N  N   . VAL B 1 125 ? 7.154   5.269   47.117 1.00 20.83 ? 119 VAL B N   1 
ATOM   1920 C  CA  . VAL B 1 125 ? 7.505   5.583   48.508 1.00 21.12 ? 119 VAL B CA  1 
ATOM   1921 C  C   . VAL B 1 125 ? 6.779   6.895   48.828 1.00 15.08 ? 119 VAL B C   1 
ATOM   1922 O  O   . VAL B 1 125 ? 6.751   7.835   48.015 1.00 21.28 ? 119 VAL B O   1 
ATOM   1923 C  CB  . VAL B 1 125 ? 9.036   5.719   48.741 1.00 23.11 ? 119 VAL B CB  1 
ATOM   1924 C  CG1 . VAL B 1 125 ? 9.607   6.813   47.887 1.00 23.96 ? 119 VAL B CG1 1 
ATOM   1925 C  CG2 . VAL B 1 125 ? 9.301   5.945   50.231 1.00 21.37 ? 119 VAL B CG2 1 
ATOM   1926 N  N   . HIS B 1 126 ? 6.150   6.934   49.995 1.00 17.75 ? 120 HIS B N   1 
ATOM   1927 C  CA  . HIS B 1 126 ? 5.325   8.074   50.424 1.00 17.99 ? 120 HIS B CA  1 
ATOM   1928 C  C   . HIS B 1 126 ? 5.939   9.054   51.413 1.00 25.11 ? 120 HIS B C   1 
ATOM   1929 O  O   . HIS B 1 126 ? 6.921   8.762   52.077 1.00 23.55 ? 120 HIS B O   1 
ATOM   1930 C  CB  . HIS B 1 126 ? 4.019   7.532   51.035 1.00 19.90 ? 120 HIS B CB  1 
ATOM   1931 C  CG  . HIS B 1 126 ? 3.119   6.886   50.026 1.00 25.37 ? 120 HIS B CG  1 
ATOM   1932 N  ND1 . HIS B 1 126 ? 2.083   7.563   49.425 1.00 24.66 ? 120 HIS B ND1 1 
ATOM   1933 C  CD2 . HIS B 1 126 ? 3.171   5.667   49.430 1.00 23.43 ? 120 HIS B CD2 1 
ATOM   1934 C  CE1 . HIS B 1 126 ? 1.540   6.796   48.492 1.00 22.44 ? 120 HIS B CE1 1 
ATOM   1935 N  NE2 . HIS B 1 126 ? 2.188   5.641   48.473 1.00 26.84 ? 120 HIS B NE2 1 
ATOM   1936 N  N   . GLU B 1 127 ? 5.306   10.212  51.530 1.00 25.82 ? 121 GLU B N   1 
ATOM   1937 C  CA  . GLU B 1 127 ? 5.767   11.244  52.441 1.00 28.38 ? 121 GLU B CA  1 
ATOM   1938 C  C   . GLU B 1 127 ? 5.638   10.903  53.917 1.00 31.14 ? 121 GLU B C   1 
ATOM   1939 O  O   . GLU B 1 127 ? 6.518   11.249  54.717 1.00 27.26 ? 121 GLU B O   1 
ATOM   1940 C  CB  . GLU B 1 127 ? 5.010   12.549  52.188 1.00 27.17 ? 121 GLU B CB  1 
ATOM   1941 C  CG  . GLU B 1 127 ? 5.266   13.598  53.241 1.00 40.95 ? 121 GLU B CG  1 
ATOM   1942 C  CD  . GLU B 1 127 ? 4.537   14.889  52.944 1.00 49.02 ? 121 GLU B CD  1 
ATOM   1943 O  OE1 . GLU B 1 127 ? 5.084   15.701  52.175 1.00 55.69 ? 121 GLU B OE1 1 
ATOM   1944 O  OE2 . GLU B 1 127 ? 3.415   15.079  53.459 1.00 41.29 ? 121 GLU B OE2 1 
ATOM   1945 N  N   . LYS B 1 128 ? 4.564   10.211  54.287 1.00 19.63 ? 122 LYS B N   1 
ATOM   1946 C  CA  . LYS B 1 128 ? 4.309   9.916   55.702 1.00 28.38 ? 122 LYS B CA  1 
ATOM   1947 C  C   . LYS B 1 128 ? 4.138   8.429   55.952 1.00 25.61 ? 122 LYS B C   1 
ATOM   1948 O  O   . LYS B 1 128 ? 4.065   7.656   55.007 1.00 28.89 ? 122 LYS B O   1 
ATOM   1949 C  CB  . LYS B 1 128 ? 3.038   10.641  56.178 1.00 30.21 ? 122 LYS B CB  1 
ATOM   1950 C  CG  . LYS B 1 128 ? 3.080   12.167  56.078 1.00 24.85 ? 122 LYS B CG  1 
ATOM   1951 C  CD  . LYS B 1 128 ? 4.241   12.759  56.901 1.00 32.97 ? 122 LYS B CD  1 
ATOM   1952 C  CE  . LYS B 1 128 ? 4.175   14.286  56.936 1.00 38.00 ? 122 LYS B CE  1 
ATOM   1953 N  NZ  . LYS B 1 128 ? 5.323   14.892  57.697 1.00 30.18 ? 122 LYS B NZ  1 
ATOM   1954 N  N   . ALA B 1 129 ? 4.065   8.061   57.229 1.00 20.69 ? 123 ALA B N   1 
ATOM   1955 C  CA  . ALA B 1 129 ? 3.928   6.675   57.627 1.00 23.21 ? 123 ALA B CA  1 
ATOM   1956 C  C   . ALA B 1 129 ? 2.567   6.124   57.195 1.00 26.85 ? 123 ALA B C   1 
ATOM   1957 O  O   . ALA B 1 129 ? 1.572   6.870   57.102 1.00 24.73 ? 123 ALA B O   1 
ATOM   1958 C  CB  . ALA B 1 129 ? 4.081   6.542   59.150 1.00 24.97 ? 123 ALA B CB  1 
ATOM   1959 N  N   . ASP B 1 130 ? 2.551   4.827   56.914 1.00 26.83 ? 124 ASP B N   1 
ATOM   1960 C  CA  . ASP B 1 130 ? 1.334   4.092   56.535 1.00 25.43 ? 124 ASP B CA  1 
ATOM   1961 C  C   . ASP B 1 130 ? 0.677   3.630   57.856 1.00 26.95 ? 124 ASP B C   1 
ATOM   1962 O  O   . ASP B 1 130 ? 1.343   3.004   58.675 1.00 30.44 ? 124 ASP B O   1 
ATOM   1963 C  CB  . ASP B 1 130 ? 1.746   2.866   55.693 1.00 25.36 ? 124 ASP B CB  1 
ATOM   1964 C  CG  . ASP B 1 130 ? 0.551   2.096   55.151 1.00 29.67 ? 124 ASP B CG  1 
ATOM   1965 O  OD1 . ASP B 1 130 ? -0.548  2.180   55.754 1.00 28.55 ? 124 ASP B OD1 1 
ATOM   1966 O  OD2 . ASP B 1 130 ? 0.717   1.405   54.122 1.00 28.52 ? 124 ASP B OD2 1 
ATOM   1967 N  N   . ASP B 1 131 ? -0.607  3.933   58.092 1.00 23.94 ? 125 ASP B N   1 
ATOM   1968 C  CA  . ASP B 1 131 ? -1.249  3.489   59.345 1.00 25.48 ? 125 ASP B CA  1 
ATOM   1969 C  C   . ASP B 1 131 ? -1.752  2.037   59.329 1.00 26.53 ? 125 ASP B C   1 
ATOM   1970 O  O   . ASP B 1 131 ? -2.445  1.573   60.237 1.00 25.96 ? 125 ASP B O   1 
ATOM   1971 C  CB  . ASP B 1 131 ? -2.372  4.464   59.772 1.00 26.82 ? 125 ASP B CB  1 
ATOM   1972 C  CG  . ASP B 1 131 ? -3.581  4.461   58.852 1.00 34.17 ? 125 ASP B CG  1 
ATOM   1973 O  OD1 . ASP B 1 131 ? -3.890  3.443   58.200 1.00 31.00 ? 125 ASP B OD1 1 
ATOM   1974 O  OD2 . ASP B 1 131 ? -4.269  5.502   58.812 1.00 35.71 ? 125 ASP B OD2 1 
ATOM   1975 N  N   . LEU B 1 132 ? -1.354  1.325   58.286 1.00 23.05 ? 126 LEU B N   1 
ATOM   1976 C  CA  . LEU B 1 132 ? -1.672  -0.081  58.058 1.00 26.77 ? 126 LEU B CA  1 
ATOM   1977 C  C   . LEU B 1 132 ? -3.146  -0.491  58.171 1.00 31.03 ? 126 LEU B C   1 
ATOM   1978 O  O   . LEU B 1 132 ? -3.444  -1.634  58.507 1.00 27.13 ? 126 LEU B O   1 
ATOM   1979 C  CB  . LEU B 1 132 ? -0.810  -0.947  58.972 1.00 20.86 ? 126 LEU B CB  1 
ATOM   1980 C  CG  . LEU B 1 132 ? 0.638   -0.398  58.989 1.00 42.36 ? 126 LEU B CG  1 
ATOM   1981 C  CD1 . LEU B 1 132 ? 1.471   -1.155  60.010 1.00 40.86 ? 126 LEU B CD1 1 
ATOM   1982 C  CD2 . LEU B 1 132 ? 1.264   -0.475  57.575 1.00 28.98 ? 126 LEU B CD2 1 
ATOM   1983 N  N   . GLY B 1 133 ? -4.057  0.429   57.866 1.00 24.22 ? 127 GLY B N   1 
ATOM   1984 C  CA  . GLY B 1 133 ? -5.469  0.110   57.937 1.00 24.04 ? 127 GLY B CA  1 
ATOM   1985 C  C   . GLY B 1 133 ? -6.079  0.141   59.318 1.00 27.99 ? 127 GLY B C   1 
ATOM   1986 O  O   . GLY B 1 133 ? -7.222  -0.268  59.505 1.00 32.89 ? 127 GLY B O   1 
ATOM   1987 N  N   . LYS B 1 134 ? -5.341  0.648   60.286 1.00 33.67 ? 128 LYS B N   1 
ATOM   1988 C  CA  . LYS B 1 134 ? -5.836  0.713   61.657 1.00 38.54 ? 128 LYS B CA  1 
ATOM   1989 C  C   . LYS B 1 134 ? -6.022  2.154   62.152 1.00 45.99 ? 128 LYS B C   1 
ATOM   1990 O  O   . LYS B 1 134 ? -5.869  2.436   63.347 1.00 42.27 ? 128 LYS B O   1 
ATOM   1991 C  CB  . LYS B 1 134 ? -4.861  -0.016  62.584 1.00 35.32 ? 128 LYS B CB  1 
ATOM   1992 C  CG  . LYS B 1 134 ? -5.276  -1.449  62.879 1.00 53.42 ? 128 LYS B CG  1 
ATOM   1993 C  CD  . LYS B 1 134 ? -4.794  -2.426  61.842 1.00 48.39 ? 128 LYS B CD  1 
ATOM   1994 C  CE  . LYS B 1 134 ? -3.331  -2.750  62.067 1.00 58.92 ? 128 LYS B CE  1 
ATOM   1995 N  NZ  . LYS B 1 134 ? -2.916  -3.879  61.206 1.00 55.32 ? 128 LYS B NZ  1 
ATOM   1996 N  N   . GLY B 1 135 ? -6.371  3.060   61.242 1.00 40.09 ? 129 GLY B N   1 
ATOM   1997 C  CA  . GLY B 1 135 ? -6.522  4.450   61.628 1.00 42.88 ? 129 GLY B CA  1 
ATOM   1998 C  C   . GLY B 1 135 ? -7.855  4.912   62.178 1.00 40.83 ? 129 GLY B C   1 
ATOM   1999 O  O   . GLY B 1 135 ? -7.929  5.973   62.814 1.00 42.48 ? 129 GLY B O   1 
ATOM   2000 N  N   . GLY B 1 136 ? -8.914  4.156   61.931 1.00 36.30 ? 130 GLY B N   1 
ATOM   2001 C  CA  . GLY B 1 136 ? -10.206 4.582   62.440 1.00 37.00 ? 130 GLY B CA  1 
ATOM   2002 C  C   . GLY B 1 136 ? -11.024 5.455   61.498 1.00 33.91 ? 130 GLY B C   1 
ATOM   2003 O  O   . GLY B 1 136 ? -12.010 6.054   61.912 1.00 33.70 ? 130 GLY B O   1 
ATOM   2004 N  N   . ASN B 1 137 ? -10.624 5.539   60.236 1.00 29.24 ? 131 ASN B N   1 
ATOM   2005 C  CA  . ASN B 1 137 ? -11.372 6.329   59.256 1.00 29.38 ? 131 ASN B CA  1 
ATOM   2006 C  C   . ASN B 1 137 ? -11.418 5.546   57.972 1.00 29.07 ? 131 ASN B C   1 
ATOM   2007 O  O   . ASN B 1 137 ? -10.697 4.554   57.820 1.00 25.42 ? 131 ASN B O   1 
ATOM   2008 C  CB  . ASN B 1 137 ? -10.701 7.683   59.049 1.00 26.13 ? 131 ASN B CB  1 
ATOM   2009 C  CG  . ASN B 1 137 ? -9.213  7.559   58.938 1.00 33.82 ? 131 ASN B CG  1 
ATOM   2010 O  OD1 . ASN B 1 137 ? -8.700  7.208   57.890 1.00 21.73 ? 131 ASN B OD1 1 
ATOM   2011 N  ND2 . ASN B 1 137 ? -8.515  7.802   60.032 1.00 42.20 ? 131 ASN B ND2 1 
ATOM   2012 N  N   . GLU B 1 138 ? -12.251 5.960   57.027 1.00 22.59 ? 132 GLU B N   1 
ATOM   2013 C  CA  . GLU B 1 138 ? -12.346 5.204   55.786 1.00 29.80 ? 132 GLU B CA  1 
ATOM   2014 C  C   . GLU B 1 138 ? -11.076 5.189   54.929 1.00 25.98 ? 132 GLU B C   1 
ATOM   2015 O  O   . GLU B 1 138 ? -10.718 4.165   54.355 1.00 26.21 ? 132 GLU B O   1 
ATOM   2016 C  CB  . GLU B 1 138 ? -13.506 5.728   54.950 1.00 37.05 ? 132 GLU B CB  1 
ATOM   2017 C  CG  . GLU B 1 138 ? -13.749 4.949   53.661 1.00 42.50 ? 132 GLU B CG  1 
ATOM   2018 C  CD  . GLU B 1 138 ? -14.828 5.582   52.810 1.00 52.79 ? 132 GLU B CD  1 
ATOM   2019 O  OE1 . GLU B 1 138 ? -15.216 4.982   51.788 1.00 71.60 ? 132 GLU B OE1 1 
ATOM   2020 O  OE2 . GLU B 1 138 ? -15.287 6.685   53.162 1.00 59.53 ? 132 GLU B OE2 1 
ATOM   2021 N  N   . GLU B 1 139 ? -10.390 6.322   54.863 1.00 22.81 ? 133 GLU B N   1 
ATOM   2022 C  CA  . GLU B 1 139 ? -9.185  6.438   54.054 1.00 27.67 ? 133 GLU B CA  1 
ATOM   2023 C  C   . GLU B 1 139 ? -8.112  5.409   54.456 1.00 22.68 ? 133 GLU B C   1 
ATOM   2024 O  O   . GLU B 1 139 ? -7.337  4.918   53.610 1.00 28.30 ? 133 GLU B O   1 
ATOM   2025 C  CB  . GLU B 1 139 ? -8.626  7.860   54.182 1.00 26.74 ? 133 GLU B CB  1 
ATOM   2026 C  CG  . GLU B 1 139 ? -7.608  8.236   53.120 1.00 32.64 ? 133 GLU B CG  1 
ATOM   2027 C  CD  . GLU B 1 139 ? -8.115  8.006   51.715 1.00 37.39 ? 133 GLU B CD  1 
ATOM   2028 O  OE1 . GLU B 1 139 ? -9.306  8.267   51.443 1.00 35.83 ? 133 GLU B OE1 1 
ATOM   2029 O  OE2 . GLU B 1 139 ? -7.313  7.568   50.871 1.00 46.88 ? 133 GLU B OE2 1 
ATOM   2030 N  N   . SER B 1 140 ? -8.084  5.082   55.742 1.00 26.40 ? 134 SER B N   1 
ATOM   2031 C  CA  . SER B 1 140 ? -7.127  4.125   56.282 1.00 31.31 ? 134 SER B CA  1 
ATOM   2032 C  C   . SER B 1 140 ? -7.301  2.786   55.563 1.00 28.55 ? 134 SER B C   1 
ATOM   2033 O  O   . SER B 1 140 ? -6.327  2.089   55.274 1.00 26.13 ? 134 SER B O   1 
ATOM   2034 C  CB  . SER B 1 140 ? -7.359  3.953   57.796 1.00 29.78 ? 134 SER B CB  1 
ATOM   2035 O  OG  . SER B 1 140 ? -6.370  3.123   58.394 1.00 29.04 ? 134 SER B OG  1 
ATOM   2036 N  N   . THR B 1 141 ? -8.551  2.455   55.251 1.00 26.40 ? 135 THR B N   1 
ATOM   2037 C  CA  . THR B 1 141 ? -8.867  1.195   54.595 1.00 26.93 ? 135 THR B CA  1 
ATOM   2038 C  C   . THR B 1 141 ? -8.546  1.223   53.118 1.00 24.18 ? 135 THR B C   1 
ATOM   2039 O  O   . THR B 1 141 ? -8.682  0.195   52.422 1.00 22.86 ? 135 THR B O   1 
ATOM   2040 C  CB  . THR B 1 141 ? -10.381 0.827   54.735 1.00 24.78 ? 135 THR B CB  1 
ATOM   2041 O  OG1 . THR B 1 141 ? -11.147 1.746   53.951 1.00 27.05 ? 135 THR B OG1 1 
ATOM   2042 C  CG2 . THR B 1 141 ? -10.844 0.905   56.167 1.00 25.41 ? 135 THR B CG2 1 
ATOM   2043 N  N   . LYS B 1 142 ? -8.144  2.395   52.629 1.00 22.89 ? 136 LYS B N   1 
ATOM   2044 C  CA  . LYS B 1 142 ? -7.803  2.552   51.226 1.00 26.33 ? 136 LYS B CA  1 
ATOM   2045 C  C   . LYS B 1 142 ? -6.320  2.816   50.934 1.00 27.37 ? 136 LYS B C   1 
ATOM   2046 O  O   . LYS B 1 142 ? -5.724  2.134   50.099 1.00 28.31 ? 136 LYS B O   1 
ATOM   2047 C  CB  . LYS B 1 142 ? -8.621  3.692   50.586 1.00 30.50 ? 136 LYS B CB  1 
ATOM   2048 C  CG  . LYS B 1 142 ? -10.110 3.389   50.395 1.00 38.37 ? 136 LYS B CG  1 
ATOM   2049 C  CD  . LYS B 1 142 ? -10.901 4.670   50.165 1.00 53.48 ? 136 LYS B CD  1 
ATOM   2050 C  CE  . LYS B 1 142 ? -12.400 4.374   50.089 1.00 65.30 ? 136 LYS B CE  1 
ATOM   2051 N  NZ  . LYS B 1 142 ? -13.216 5.608   49.855 1.00 71.50 ? 136 LYS B NZ  1 
ATOM   2052 N  N   . THR B 1 143 ? -5.749  3.817   51.595 1.00 28.32 ? 137 THR B N   1 
ATOM   2053 C  CA  . THR B 1 143 ? -4.363  4.213   51.362 1.00 27.31 ? 137 THR B CA  1 
ATOM   2054 C  C   . THR B 1 143 ? -3.479  4.204   52.606 1.00 26.13 ? 137 THR B C   1 
ATOM   2055 O  O   . THR B 1 143 ? -2.254  4.369   52.508 1.00 29.05 ? 137 THR B O   1 
ATOM   2056 C  CB  . THR B 1 143 ? -4.305  5.634   50.792 1.00 27.94 ? 137 THR B CB  1 
ATOM   2057 O  OG1 . THR B 1 143 ? -4.726  6.563   51.794 1.00 26.52 ? 137 THR B OG1 1 
ATOM   2058 C  CG2 . THR B 1 143 ? -5.217  5.776   49.586 1.00 26.03 ? 137 THR B CG2 1 
ATOM   2059 N  N   . GLY B 1 144 ? -4.086  4.048   53.774 1.00 22.83 ? 138 GLY B N   1 
ATOM   2060 C  CA  . GLY B 1 144 ? -3.306  4.071   55.002 1.00 26.36 ? 138 GLY B CA  1 
ATOM   2061 C  C   . GLY B 1 144 ? -2.913  5.484   55.408 1.00 23.23 ? 138 GLY B C   1 
ATOM   2062 O  O   . GLY B 1 144 ? -2.145  5.686   56.345 1.00 23.59 ? 138 GLY B O   1 
ATOM   2063 N  N   . ASN B 1 145 ? -3.458  6.475   54.716 1.00 26.37 ? 139 ASN B N   1 
ATOM   2064 C  CA  . ASN B 1 145 ? -3.178  7.866   55.046 1.00 25.71 ? 139 ASN B CA  1 
ATOM   2065 C  C   . ASN B 1 145 ? -1.677  8.163   54.955 1.00 25.85 ? 139 ASN B C   1 
ATOM   2066 O  O   . ASN B 1 145 ? -1.148  8.910   55.777 1.00 23.06 ? 139 ASN B O   1 
ATOM   2067 C  CB  . ASN B 1 145 ? -3.684  8.169   56.477 1.00 28.05 ? 139 ASN B CB  1 
ATOM   2068 C  CG  . ASN B 1 145 ? -5.206  8.130   56.591 1.00 27.10 ? 139 ASN B CG  1 
ATOM   2069 O  OD1 . ASN B 1 145 ? -5.891  8.985   56.054 1.00 25.53 ? 139 ASN B OD1 1 
ATOM   2070 N  ND2 . ASN B 1 145 ? -5.732  7.139   57.303 1.00 27.28 ? 139 ASN B ND2 1 
ATOM   2071 N  N   . ALA B 1 146 ? -0.995  7.605   53.951 1.00 23.66 ? 140 ALA B N   1 
ATOM   2072 C  CA  . ALA B 1 146 ? 0.459   7.803   53.843 1.00 24.71 ? 140 ALA B CA  1 
ATOM   2073 C  C   . ALA B 1 146 ? 0.914   9.095   53.197 1.00 27.05 ? 140 ALA B C   1 
ATOM   2074 O  O   . ALA B 1 146 ? 2.116   9.403   53.164 1.00 26.27 ? 140 ALA B O   1 
ATOM   2075 C  CB  . ALA B 1 146 ? 1.085   6.611   53.130 1.00 24.12 ? 140 ALA B CB  1 
ATOM   2076 N  N   . GLY B 1 147 ? -0.018  9.858   52.652 1.00 23.20 ? 141 GLY B N   1 
ATOM   2077 C  CA  . GLY B 1 147 ? 0.384   11.125  52.060 1.00 25.45 ? 141 GLY B CA  1 
ATOM   2078 C  C   . GLY B 1 147 ? 0.882   11.093  50.624 1.00 26.03 ? 141 GLY B C   1 
ATOM   2079 O  O   . GLY B 1 147 ? 0.684   10.114  49.888 1.00 26.38 ? 141 GLY B O   1 
ATOM   2080 N  N   . SER B 1 148 ? 1.543   12.169  50.216 1.00 28.42 ? 142 SER B N   1 
ATOM   2081 C  CA  . SER B 1 148 ? 2.031   12.267  48.842 1.00 24.41 ? 142 SER B CA  1 
ATOM   2082 C  C   . SER B 1 148 ? 3.012   11.179  48.448 1.00 28.11 ? 142 SER B C   1 
ATOM   2083 O  O   . SER B 1 148 ? 3.743   10.625  49.291 1.00 26.29 ? 142 SER B O   1 
ATOM   2084 C  CB  . SER B 1 148 ? 2.649   13.655  48.584 1.00 35.02 ? 142 SER B CB  1 
ATOM   2085 O  OG  . SER B 1 148 ? 3.534   14.018  49.626 1.00 41.45 ? 142 SER B OG  1 
ATOM   2086 N  N   . ARG B 1 149 ? 2.981   10.862  47.156 1.00 24.97 ? 143 ARG B N   1 
ATOM   2087 C  CA  . ARG B 1 149 ? 3.854   9.870   46.530 1.00 23.95 ? 143 ARG B CA  1 
ATOM   2088 C  C   . ARG B 1 149 ? 5.100   10.684  46.213 1.00 31.21 ? 143 ARG B C   1 
ATOM   2089 O  O   . ARG B 1 149 ? 5.089   11.538  45.341 1.00 30.71 ? 143 ARG B O   1 
ATOM   2090 C  CB  . ARG B 1 149 ? 3.202   9.367   45.258 1.00 25.77 ? 143 ARG B CB  1 
ATOM   2091 C  CG  . ARG B 1 149 ? 1.749   8.889   45.508 1.00 22.19 ? 143 ARG B CG  1 
ATOM   2092 C  CD  . ARG B 1 149 ? 1.123   8.309   44.266 1.00 19.24 ? 143 ARG B CD  1 
ATOM   2093 N  NE  . ARG B 1 149 ? -0.152  7.736   44.639 1.00 25.07 ? 143 ARG B NE  1 
ATOM   2094 C  CZ  . ARG B 1 149 ? -0.977  7.130   43.801 1.00 34.22 ? 143 ARG B CZ  1 
ATOM   2095 N  NH1 . ARG B 1 149 ? -0.653  7.028   42.514 1.00 31.31 ? 143 ARG B NH1 1 
ATOM   2096 N  NH2 . ARG B 1 149 ? -2.113  6.609   44.270 1.00 25.97 ? 143 ARG B NH2 1 
ATOM   2097 N  N   . LEU B 1 150 ? 6.164   10.447  46.956 1.00 25.92 ? 144 LEU B N   1 
ATOM   2098 C  CA  . LEU B 1 150 ? 7.391   11.208  46.753 1.00 24.05 ? 144 LEU B CA  1 
ATOM   2099 C  C   . LEU B 1 150 ? 8.202   10.744  45.553 1.00 37.77 ? 144 LEU B C   1 
ATOM   2100 O  O   . LEU B 1 150 ? 8.877   11.546  44.907 1.00 32.78 ? 144 LEU B O   1 
ATOM   2101 C  CB  . LEU B 1 150 ? 8.259   11.141  48.010 1.00 28.26 ? 144 LEU B CB  1 
ATOM   2102 C  CG  . LEU B 1 150 ? 7.625   11.731  49.284 1.00 36.58 ? 144 LEU B CG  1 
ATOM   2103 C  CD1 . LEU B 1 150 ? 8.653   11.735  50.380 1.00 40.52 ? 144 LEU B CD1 1 
ATOM   2104 C  CD2 . LEU B 1 150 ? 7.115   13.161  49.052 1.00 34.15 ? 144 LEU B CD2 1 
ATOM   2105 N  N   . ALA B 1 151 ? 8.145   9.453   45.254 1.00 28.48 ? 145 ALA B N   1 
ATOM   2106 C  CA  . ALA B 1 151 ? 8.913   8.937   44.142 1.00 28.47 ? 145 ALA B CA  1 
ATOM   2107 C  C   . ALA B 1 151 ? 8.413   7.546   43.790 1.00 25.92 ? 145 ALA B C   1 
ATOM   2108 O  O   . ALA B 1 151 ? 7.894   6.842   44.642 1.00 25.36 ? 145 ALA B O   1 
ATOM   2109 C  CB  . ALA B 1 151 ? 10.391  8.887   44.515 1.00 25.84 ? 145 ALA B CB  1 
ATOM   2110 N  N   . CYS B 1 152 ? 8.578   7.162   42.535 1.00 22.21 ? 146 CYS B N   1 
ATOM   2111 C  CA  . CYS B 1 152 ? 8.126   5.871   42.061 1.00 31.12 ? 146 CYS B CA  1 
ATOM   2112 C  C   . CYS B 1 152 ? 8.996   5.380   40.919 1.00 29.92 ? 146 CYS B C   1 
ATOM   2113 O  O   . CYS B 1 152 ? 9.830   6.117   40.377 1.00 27.24 ? 146 CYS B O   1 
ATOM   2114 C  CB  . CYS B 1 152 ? 6.690   5.992   41.586 1.00 35.21 ? 146 CYS B CB  1 
ATOM   2115 S  SG  . CYS B 1 152 ? 6.503   7.409   40.478 1.00 36.93 ? 146 CYS B SG  1 
ATOM   2116 N  N   . GLY B 1 153 ? 8.806   4.117   40.570 1.00 22.84 ? 147 GLY B N   1 
ATOM   2117 C  CA  . GLY B 1 153 ? 9.570   3.532   39.493 1.00 26.12 ? 147 GLY B CA  1 
ATOM   2118 C  C   . GLY B 1 153 ? 8.882   2.266   39.045 1.00 25.79 ? 147 GLY B C   1 
ATOM   2119 O  O   . GLY B 1 153 ? 8.251   1.584   39.869 1.00 26.73 ? 147 GLY B O   1 
ATOM   2120 N  N   . VAL B 1 154 ? 8.995   1.940   37.760 1.00 20.56 ? 148 VAL B N   1 
ATOM   2121 C  CA  . VAL B 1 154 ? 8.361   0.731   37.248 1.00 22.22 ? 148 VAL B CA  1 
ATOM   2122 C  C   . VAL B 1 154 ? 9.274   -0.438  37.618 1.00 27.14 ? 148 VAL B C   1 
ATOM   2123 O  O   . VAL B 1 154 ? 10.501  -0.342  37.519 1.00 22.92 ? 148 VAL B O   1 
ATOM   2124 C  CB  . VAL B 1 154 ? 8.213   0.780   35.699 1.00 22.20 ? 148 VAL B CB  1 
ATOM   2125 C  CG1 . VAL B 1 154 ? 7.734   -0.547  35.188 1.00 21.64 ? 148 VAL B CG1 1 
ATOM   2126 C  CG2 . VAL B 1 154 ? 7.232   1.864   35.297 1.00 24.55 ? 148 VAL B CG2 1 
ATOM   2127 N  N   . ILE B 1 155 ? 8.665   -1.531  38.043 1.00 18.21 ? 149 ILE B N   1 
ATOM   2128 C  CA  . ILE B 1 155 ? 9.416   -2.706  38.421 1.00 22.46 ? 149 ILE B CA  1 
ATOM   2129 C  C   . ILE B 1 155 ? 9.796   -3.477  37.155 1.00 25.43 ? 149 ILE B C   1 
ATOM   2130 O  O   . ILE B 1 155 ? 8.930   -3.923  36.390 1.00 27.69 ? 149 ILE B O   1 
ATOM   2131 C  CB  . ILE B 1 155 ? 8.593   -3.546  39.396 1.00 24.90 ? 149 ILE B CB  1 
ATOM   2132 C  CG1 . ILE B 1 155 ? 8.236   -2.681  40.623 1.00 20.23 ? 149 ILE B CG1 1 
ATOM   2133 C  CG2 . ILE B 1 155 ? 9.381   -4.809  39.788 1.00 28.13 ? 149 ILE B CG2 1 
ATOM   2134 C  CD1 . ILE B 1 155 ? 7.309   -3.368  41.637 1.00 23.65 ? 149 ILE B CD1 1 
ATOM   2135 N  N   . GLY B 1 156 ? 11.104  -3.615  36.927 1.00 23.00 ? 150 GLY B N   1 
ATOM   2136 C  CA  . GLY B 1 156 ? 11.585  -4.279  35.728 1.00 23.12 ? 150 GLY B CA  1 
ATOM   2137 C  C   . GLY B 1 156 ? 12.409  -5.539  35.945 1.00 24.43 ? 150 GLY B C   1 
ATOM   2138 O  O   . GLY B 1 156 ? 12.880  -5.790  37.046 1.00 23.76 ? 150 GLY B O   1 
ATOM   2139 N  N   . ILE B 1 157 ? 12.561  -6.351  34.901 1.00 25.77 ? 151 ILE B N   1 
ATOM   2140 C  CA  . ILE B 1 157 ? 13.339  -7.595  34.999 1.00 31.83 ? 151 ILE B CA  1 
ATOM   2141 C  C   . ILE B 1 157 ? 14.788  -7.212  35.134 1.00 27.33 ? 151 ILE B C   1 
ATOM   2142 O  O   . ILE B 1 157 ? 15.280  -6.366  34.399 1.00 25.90 ? 151 ILE B O   1 
ATOM   2143 C  CB  . ILE B 1 157 ? 13.208  -8.488  33.734 1.00 32.34 ? 151 ILE B CB  1 
ATOM   2144 C  CG1 . ILE B 1 157 ? 11.751  -8.867  33.507 1.00 37.02 ? 151 ILE B CG1 1 
ATOM   2145 C  CG2 . ILE B 1 157 ? 14.037  -9.759  33.918 1.00 34.32 ? 151 ILE B CG2 1 
ATOM   2146 C  CD1 . ILE B 1 157 ? 11.464  -9.315  32.085 1.00 41.45 ? 151 ILE B CD1 1 
ATOM   2147 N  N   . ALA B 1 158 ? 15.475  -7.826  36.082 1.00 28.05 ? 152 ALA B N   1 
ATOM   2148 C  CA  . ALA B 1 158 ? 16.869  -7.492  36.302 1.00 35.76 ? 152 ALA B CA  1 
ATOM   2149 C  C   . ALA B 1 158 ? 17.755  -8.617  35.782 1.00 40.95 ? 152 ALA B C   1 
ATOM   2150 O  O   . ALA B 1 158 ? 17.273  -9.764  35.756 1.00 41.80 ? 152 ALA B O   1 
ATOM   2151 C  CB  . ALA B 1 158 ? 17.112  -7.269  37.800 1.00 28.90 ? 152 ALA B CB  1 
HETATM 2152 CU CU  . CU1 C 2 .   ? 18.278  -0.007  21.438 1.00 28.94 ? 301 CU1 A CU  1 
HETATM 2153 ZN ZN  . ZN  D 3 .   ? 18.375  -5.753  17.366 1.00 27.58 ? 401 ZN  A ZN  1 
HETATM 2154 CU CU  . CU1 E 2 .   ? 1.667   3.735   47.743 1.00 26.11 ? 302 CU1 B CU  1 
HETATM 2155 ZN ZN  . ZN  F 3 .   ? -2.855  -0.761  50.397 1.00 24.43 ? 402 ZN  B ZN  1 
HETATM 2156 O  O   . HOH G 4 .   ? 4.601   -5.902  7.360  1.00 30.35 ? 402 HOH A O   1 
HETATM 2157 O  O   . HOH G 4 .   ? 8.547   7.933   13.995 1.00 30.73 ? 403 HOH A O   1 
HETATM 2158 O  O   . HOH G 4 .   ? 14.726  -12.885 18.973 1.00 27.26 ? 404 HOH A O   1 
HETATM 2159 O  O   . HOH G 4 .   ? 4.233   -0.235  11.118 1.00 29.99 ? 405 HOH A O   1 
HETATM 2160 O  O   . HOH G 4 .   ? 8.290   3.928   32.189 1.00 32.14 ? 406 HOH A O   1 
HETATM 2161 O  O   . HOH G 4 .   ? 15.415  1.027   15.288 1.00 29.12 ? 407 HOH A O   1 
HETATM 2162 O  O   . HOH G 4 .   ? 6.300   -6.966  12.129 1.00 37.53 ? 408 HOH A O   1 
HETATM 2163 O  O   . HOH G 4 .   ? 26.326  1.180   18.382 1.00 34.27 ? 409 HOH A O   1 
HETATM 2164 O  O   . HOH G 4 .   ? 15.690  -2.386  14.388 1.00 31.71 ? 410 HOH A O   1 
HETATM 2165 O  O   . HOH G 4 .   ? 13.663  1.471   10.257 1.00 35.57 ? 411 HOH A O   1 
HETATM 2166 O  O   . HOH G 4 .   ? 14.875  -0.354  36.576 1.00 28.52 ? 412 HOH A O   1 
HETATM 2167 O  O   . HOH G 4 .   ? 21.185  -4.123  38.412 1.00 47.29 ? 413 HOH A O   1 
HETATM 2168 O  O   . HOH G 4 .   ? 9.928   6.651   11.362 1.00 31.69 ? 414 HOH A O   1 
HETATM 2169 O  O   . HOH G 4 .   ? 8.445   -1.533  13.964 1.00 44.59 ? 415 HOH A O   1 
HETATM 2170 O  O   . HOH G 4 .   ? 10.850  3.739   33.560 1.00 40.10 ? 416 HOH A O   1 
HETATM 2171 O  O   . HOH G 4 .   ? 17.686  19.099  14.581 1.00 42.89 ? 417 HOH A O   1 
HETATM 2172 O  O   . HOH G 4 .   ? 21.809  -5.958  20.806 1.00 35.72 ? 418 HOH A O   1 
HETATM 2173 O  O   . HOH G 4 .   ? 7.366   -0.686  10.876 1.00 42.94 ? 419 HOH A O   1 
HETATM 2174 O  O   . HOH G 4 .   ? 12.230  0.088   8.282  1.00 28.75 ? 420 HOH A O   1 
HETATM 2175 O  O   . HOH G 4 .   ? 9.298   0.075   8.137  1.00 22.87 ? 421 HOH A O   1 
HETATM 2176 O  O   . HOH G 4 .   ? 12.626  -3.006  7.810  1.00 31.50 ? 422 HOH A O   1 
HETATM 2177 O  O   . HOH G 4 .   ? 6.560   14.643  13.979 1.00 53.41 ? 423 HOH A O   1 
HETATM 2178 O  O   . HOH H 4 .   ? -5.556  -7.401  46.954 1.00 14.38 ? 403 HOH B O   1 
HETATM 2179 O  O   . HOH H 4 .   ? 10.014  13.308  52.761 1.00 19.66 ? 404 HOH B O   1 
HETATM 2180 O  O   . HOH H 4 .   ? 5.750   -14.996 47.516 1.00 27.20 ? 405 HOH B O   1 
HETATM 2181 O  O   . HOH H 4 .   ? 12.713  1.221   37.275 1.00 25.23 ? 406 HOH B O   1 
HETATM 2182 O  O   . HOH H 4 .   ? 10.681  -8.931  56.680 1.00 31.81 ? 407 HOH B O   1 
HETATM 2183 O  O   . HOH H 4 .   ? 13.443  0.439   56.587 1.00 35.75 ? 408 HOH B O   1 
HETATM 2184 O  O   . HOH H 4 .   ? -0.842  5.258   50.474 1.00 32.45 ? 409 HOH B O   1 
HETATM 2185 O  O   . HOH H 4 .   ? 11.130  3.686   36.311 1.00 31.43 ? 410 HOH B O   1 
HETATM 2186 O  O   . HOH H 4 .   ? -1.357  7.841   50.175 1.00 36.44 ? 411 HOH B O   1 
HETATM 2187 O  O   . HOH H 4 .   ? 4.587   -11.261 54.203 1.00 29.55 ? 412 HOH B O   1 
HETATM 2188 O  O   . HOH H 4 .   ? 19.395  11.638  52.085 1.00 33.90 ? 413 HOH B O   1 
HETATM 2189 O  O   . HOH H 4 .   ? 13.575  12.468  42.376 1.00 33.06 ? 414 HOH B O   1 
HETATM 2190 O  O   . HOH H 4 .   ? 6.109   -6.935  53.526 1.00 35.32 ? 415 HOH B O   1 
HETATM 2191 O  O   . HOH H 4 .   ? -2.856  -12.048 51.024 1.00 29.03 ? 416 HOH B O   1 
HETATM 2192 O  O   . HOH H 4 .   ? 12.512  5.827   37.838 1.00 47.97 ? 417 HOH B O   1 
HETATM 2193 O  O   . HOH H 4 .   ? 14.924  15.063  57.722 1.00 43.29 ? 418 HOH B O   1 
HETATM 2194 O  O   . HOH H 4 .   ? -3.257  7.321   40.509 1.00 40.07 ? 419 HOH B O   1 
HETATM 2195 O  O   . HOH H 4 .   ? 7.463   8.969   60.830 1.00 38.05 ? 420 HOH B O   1 
HETATM 2196 O  O   . HOH H 4 .   ? 4.961   10.056  59.469 1.00 40.73 ? 421 HOH B O   1 
HETATM 2197 O  O   . HOH H 4 .   ? 1.630   -15.079 42.459 1.00 36.43 ? 422 HOH B O   1 
HETATM 2198 O  O   . HOH H 4 .   ? 3.591   11.983  41.305 1.00 40.24 ? 423 HOH B O   1 
HETATM 2199 O  O   . HOH H 4 .   ? 15.641  -16.979 53.061 1.00 47.88 ? 424 HOH B O   1 
HETATM 2200 O  O   . HOH H 4 .   ? 23.050  -14.261 40.722 1.00 47.26 ? 425 HOH B O   1 
HETATM 2201 O  O   . HOH H 4 .   ? 21.270  3.465   45.924 1.00 46.82 ? 426 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -5  ?   ?   ?   A . n 
A 1 2   PRO 2   -4  ?   ?   ?   A . n 
A 1 3   LEU 3   -3  ?   ?   ?   A . n 
A 1 4   GLY 4   -2  ?   ?   ?   A . n 
A 1 5   SER 5   -1  ?   ?   ?   A . n 
A 1 6   MET 6   0   ?   ?   ?   A . n 
A 1 7   ALA 7   1   ?   ?   ?   A . n 
A 1 8   THR 8   2   2   THR THR A . n 
A 1 9   LYS 9   3   3   LYS LYS A . n 
A 1 10  ALA 10  4   4   ALA ALA A . n 
A 1 11  VAL 11  5   5   VAL VAL A . n 
A 1 12  CYS 12  6   6   CYS CYS A . n 
A 1 13  VAL 13  7   7   VAL VAL A . n 
A 1 14  LEU 14  8   8   LEU LEU A . n 
A 1 15  LYS 15  9   9   LYS LYS A . n 
A 1 16  GLY 16  10  10  GLY GLY A . n 
A 1 17  ASP 17  11  11  ASP ASP A . n 
A 1 18  GLY 18  12  12  GLY GLY A . n 
A 1 19  PRO 19  13  13  PRO PRO A . n 
A 1 20  VAL 20  14  14  VAL VAL A . n 
A 1 21  GLN 21  15  15  GLN GLN A . n 
A 1 22  GLY 22  16  16  GLY GLY A . n 
A 1 23  ILE 23  17  17  ILE ILE A . n 
A 1 24  ILE 24  18  18  ILE ILE A . n 
A 1 25  ASN 25  19  19  ASN ASN A . n 
A 1 26  PHE 26  20  20  PHE PHE A . n 
A 1 27  GLU 27  21  21  GLU GLU A . n 
A 1 28  GLN 28  22  22  GLN GLN A . n 
A 1 29  LYS 29  23  ?   ?   ?   A . n 
A 1 30  GLU 30  24  ?   ?   ?   A . n 
A 1 31  SER 31  25  25  SER SER A . n 
A 1 32  ASN 32  26  26  ASN ASN A . n 
A 1 33  GLY 33  27  27  GLY GLY A . n 
A 1 34  PRO 34  28  28  PRO PRO A . n 
A 1 35  VAL 35  29  29  VAL VAL A . n 
A 1 36  LYS 36  30  30  LYS LYS A . n 
A 1 37  VAL 37  31  31  VAL VAL A . n 
A 1 38  TRP 38  32  32  TRP TRP A . n 
A 1 39  GLY 39  33  33  GLY GLY A . n 
A 1 40  SER 40  34  34  SER SER A . n 
A 1 41  ILE 41  35  35  ILE ILE A . n 
A 1 42  LYS 42  36  36  LYS LYS A . n 
A 1 43  GLY 43  37  37  GLY GLY A . n 
A 1 44  LEU 44  38  38  LEU LEU A . n 
A 1 45  THR 45  39  39  THR THR A . n 
A 1 46  GLU 46  40  40  GLU GLU A . n 
A 1 47  GLY 47  41  41  GLY GLY A . n 
A 1 48  LEU 48  42  42  LEU LEU A . n 
A 1 49  HIS 49  43  43  HIS HIS A . n 
A 1 50  GLY 50  44  44  GLY GLY A . n 
A 1 51  PHE 51  45  45  PHE PHE A . n 
A 1 52  HIS 52  46  46  HIS HIS A . n 
A 1 53  VAL 53  47  47  VAL VAL A . n 
A 1 54  HIS 54  48  48  HIS HIS A . n 
A 1 55  GLU 55  49  49  GLU GLU A . n 
A 1 56  PHE 56  50  50  PHE PHE A . n 
A 1 57  GLY 57  51  51  GLY GLY A . n 
A 1 58  ASP 58  52  52  ASP ASP A . n 
A 1 59  ASN 59  53  53  ASN ASN A . n 
A 1 60  THR 60  54  54  THR THR A . n 
A 1 61  ALA 61  55  55  ALA ALA A . n 
A 1 62  GLY 62  56  56  GLY GLY A . n 
A 1 63  CYS 63  57  57  CYS CYS A . n 
A 1 64  THR 64  58  58  THR THR A . n 
A 1 65  SER 65  59  59  SER SER A . n 
A 1 66  ALA 66  60  60  ALA ALA A . n 
A 1 67  GLY 67  61  61  GLY GLY A . n 
A 1 68  PRO 68  62  62  PRO PRO A . n 
A 1 69  HIS 69  63  63  HIS HIS A . n 
A 1 70  PHE 70  64  64  PHE PHE A . n 
A 1 71  ASN 71  65  65  ASN ASN A . n 
A 1 72  PRO 72  66  66  PRO PRO A . n 
A 1 73  LEU 73  67  67  LEU LEU A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  ARG 75  69  69  ARG ARG A . n 
A 1 76  LYS 76  70  70  LYS LYS A . n 
A 1 77  HIS 77  71  71  HIS HIS A . n 
A 1 78  GLY 78  72  72  GLY GLY A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  PRO 80  74  74  PRO PRO A . n 
A 1 81  LYS 81  75  75  LYS LYS A . n 
A 1 82  ASP 82  76  76  ASP ASP A . n 
A 1 83  GLU 83  77  77  GLU GLU A . n 
A 1 84  GLU 84  78  78  GLU GLU A . n 
A 1 85  ARG 85  79  79  ARG ARG A . n 
A 1 86  HIS 86  80  80  HIS HIS A . n 
A 1 87  VAL 87  81  81  VAL VAL A . n 
A 1 88  GLY 88  82  82  GLY GLY A . n 
A 1 89  ASP 89  83  83  ASP ASP A . n 
A 1 90  LEU 90  84  84  LEU LEU A . n 
A 1 91  ARG 91  85  85  ARG ARG A . n 
A 1 92  ASN 92  86  86  ASN ASN A . n 
A 1 93  VAL 93  87  87  VAL VAL A . n 
A 1 94  THR 94  88  88  THR THR A . n 
A 1 95  ALA 95  89  89  ALA ALA A . n 
A 1 96  ASP 96  90  90  ASP ASP A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  ASP 98  92  92  ASP ASP A . n 
A 1 99  GLY 99  93  93  GLY GLY A . n 
A 1 100 VAL 100 94  94  VAL VAL A . n 
A 1 101 ALA 101 95  95  ALA ALA A . n 
A 1 102 ASP 102 96  96  ASP ASP A . n 
A 1 103 VAL 103 97  97  VAL VAL A . n 
A 1 104 SER 104 98  98  SER SER A . n 
A 1 105 ILE 105 99  99  ILE ILE A . n 
A 1 106 GLU 106 100 100 GLU GLU A . n 
A 1 107 ASP 107 101 101 ASP ASP A . n 
A 1 108 SER 108 102 102 SER SER A . n 
A 1 109 VAL 109 103 103 VAL VAL A . n 
A 1 110 ILE 110 104 104 ILE ILE A . n 
A 1 111 SER 111 105 105 SER SER A . n 
A 1 112 LEU 112 106 106 LEU LEU A . n 
A 1 113 SER 113 107 107 SER SER A . n 
A 1 114 GLY 114 108 108 GLY GLY A . n 
A 1 115 ASP 115 109 109 ASP ASP A . n 
A 1 116 HIS 116 110 110 HIS HIS A . n 
A 1 117 CYS 117 111 111 CYS CYS A . n 
A 1 118 ILE 118 112 112 ILE ILE A . n 
A 1 119 ILE 119 113 113 ILE ILE A . n 
A 1 120 GLY 120 114 114 GLY GLY A . n 
A 1 121 ARG 121 115 115 ARG ARG A . n 
A 1 122 THR 122 116 116 THR THR A . n 
A 1 123 LEU 123 117 117 LEU LEU A . n 
A 1 124 VAL 124 118 118 VAL VAL A . n 
A 1 125 VAL 125 119 119 VAL VAL A . n 
A 1 126 HIS 126 120 120 HIS HIS A . n 
A 1 127 GLU 127 121 121 GLU GLU A . n 
A 1 128 LYS 128 122 122 LYS LYS A . n 
A 1 129 ALA 129 123 123 ALA ALA A . n 
A 1 130 ASP 130 124 124 ASP ASP A . n 
A 1 131 ASP 131 125 125 ASP ASP A . n 
A 1 132 LEU 132 126 126 LEU LEU A . n 
A 1 133 GLY 133 127 127 GLY GLY A . n 
A 1 134 LYS 134 128 128 LYS LYS A . n 
A 1 135 GLY 135 129 129 GLY GLY A . n 
A 1 136 GLY 136 130 130 GLY GLY A . n 
A 1 137 ASN 137 131 131 ASN ASN A . n 
A 1 138 GLU 138 132 132 GLU GLU A . n 
A 1 139 GLU 139 133 133 GLU GLU A . n 
A 1 140 SER 140 134 134 SER SER A . n 
A 1 141 THR 141 135 135 THR THR A . n 
A 1 142 LYS 142 136 136 LYS LYS A . n 
A 1 143 THR 143 137 137 THR THR A . n 
A 1 144 GLY 144 138 138 GLY GLY A . n 
A 1 145 ASN 145 139 139 ASN ASN A . n 
A 1 146 ALA 146 140 140 ALA ALA A . n 
A 1 147 GLY 147 141 141 GLY GLY A . n 
A 1 148 SER 148 142 142 SER SER A . n 
A 1 149 ARG 149 143 143 ARG ARG A . n 
A 1 150 LEU 150 144 144 LEU LEU A . n 
A 1 151 ALA 151 145 145 ALA ALA A . n 
A 1 152 CYS 152 146 146 CYS CYS A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 VAL 154 148 148 VAL VAL A . n 
A 1 155 ILE 155 149 149 ILE ILE A . n 
A 1 156 GLY 156 150 150 GLY GLY A . n 
A 1 157 ILE 157 151 151 ILE ILE A . n 
A 1 158 ALA 158 152 152 ALA ALA A . n 
A 1 159 GLN 159 153 ?   ?   ?   A . n 
B 1 1   GLY 1   -5  ?   ?   ?   B . n 
B 1 2   PRO 2   -4  ?   ?   ?   B . n 
B 1 3   LEU 3   -3  ?   ?   ?   B . n 
B 1 4   GLY 4   -2  ?   ?   ?   B . n 
B 1 5   SER 5   -1  ?   ?   ?   B . n 
B 1 6   MET 6   0   ?   ?   ?   B . n 
B 1 7   ALA 7   1   1   ALA ALA B . n 
B 1 8   THR 8   2   2   THR THR B . n 
B 1 9   LYS 9   3   3   LYS LYS B . n 
B 1 10  ALA 10  4   4   ALA ALA B . n 
B 1 11  VAL 11  5   5   VAL VAL B . n 
B 1 12  CYS 12  6   6   CYS CYS B . n 
B 1 13  VAL 13  7   7   VAL VAL B . n 
B 1 14  LEU 14  8   8   LEU LEU B . n 
B 1 15  LYS 15  9   9   LYS LYS B . n 
B 1 16  GLY 16  10  10  GLY GLY B . n 
B 1 17  ASP 17  11  11  ASP ASP B . n 
B 1 18  GLY 18  12  12  GLY GLY B . n 
B 1 19  PRO 19  13  13  PRO PRO B . n 
B 1 20  VAL 20  14  14  VAL VAL B . n 
B 1 21  GLN 21  15  15  GLN GLN B . n 
B 1 22  GLY 22  16  16  GLY GLY B . n 
B 1 23  ILE 23  17  17  ILE ILE B . n 
B 1 24  ILE 24  18  18  ILE ILE B . n 
B 1 25  ASN 25  19  19  ASN ASN B . n 
B 1 26  PHE 26  20  20  PHE PHE B . n 
B 1 27  GLU 27  21  21  GLU GLU B . n 
B 1 28  GLN 28  22  22  GLN GLN B . n 
B 1 29  LYS 29  23  ?   ?   ?   B . n 
B 1 30  GLU 30  24  ?   ?   ?   B . n 
B 1 31  SER 31  25  ?   ?   ?   B . n 
B 1 32  ASN 32  26  26  ASN ASN B . n 
B 1 33  GLY 33  27  27  GLY GLY B . n 
B 1 34  PRO 34  28  28  PRO PRO B . n 
B 1 35  VAL 35  29  29  VAL VAL B . n 
B 1 36  LYS 36  30  30  LYS LYS B . n 
B 1 37  VAL 37  31  31  VAL VAL B . n 
B 1 38  TRP 38  32  32  TRP TRP B . n 
B 1 39  GLY 39  33  33  GLY GLY B . n 
B 1 40  SER 40  34  34  SER SER B . n 
B 1 41  ILE 41  35  35  ILE ILE B . n 
B 1 42  LYS 42  36  36  LYS LYS B . n 
B 1 43  GLY 43  37  37  GLY GLY B . n 
B 1 44  LEU 44  38  38  LEU LEU B . n 
B 1 45  THR 45  39  39  THR THR B . n 
B 1 46  GLU 46  40  40  GLU GLU B . n 
B 1 47  GLY 47  41  41  GLY GLY B . n 
B 1 48  LEU 48  42  42  LEU LEU B . n 
B 1 49  HIS 49  43  43  HIS HIS B . n 
B 1 50  GLY 50  44  44  GLY GLY B . n 
B 1 51  PHE 51  45  45  PHE PHE B . n 
B 1 52  HIS 52  46  46  HIS HIS B . n 
B 1 53  VAL 53  47  47  VAL VAL B . n 
B 1 54  HIS 54  48  48  HIS HIS B . n 
B 1 55  GLU 55  49  49  GLU GLU B . n 
B 1 56  PHE 56  50  50  PHE PHE B . n 
B 1 57  GLY 57  51  51  GLY GLY B . n 
B 1 58  ASP 58  52  52  ASP ASP B . n 
B 1 59  ASN 59  53  53  ASN ASN B . n 
B 1 60  THR 60  54  ?   ?   ?   B . n 
B 1 61  ALA 61  55  ?   ?   ?   B . n 
B 1 62  GLY 62  56  ?   ?   ?   B . n 
B 1 63  CYS 63  57  57  CYS CYS B . n 
B 1 64  THR 64  58  58  THR THR B . n 
B 1 65  SER 65  59  59  SER SER B . n 
B 1 66  ALA 66  60  60  ALA ALA B . n 
B 1 67  GLY 67  61  61  GLY GLY B . n 
B 1 68  PRO 68  62  62  PRO PRO B . n 
B 1 69  HIS 69  63  63  HIS HIS B . n 
B 1 70  PHE 70  64  64  PHE PHE B . n 
B 1 71  ASN 71  65  65  ASN ASN B . n 
B 1 72  PRO 72  66  66  PRO PRO B . n 
B 1 73  LEU 73  67  67  LEU LEU B . n 
B 1 74  SER 74  68  68  SER SER B . n 
B 1 75  ARG 75  69  69  ARG ARG B . n 
B 1 76  LYS 76  70  70  LYS LYS B . n 
B 1 77  HIS 77  71  71  HIS HIS B . n 
B 1 78  GLY 78  72  72  GLY GLY B . n 
B 1 79  GLY 79  73  73  GLY GLY B . n 
B 1 80  PRO 80  74  74  PRO PRO B . n 
B 1 81  LYS 81  75  75  LYS LYS B . n 
B 1 82  ASP 82  76  76  ASP ASP B . n 
B 1 83  GLU 83  77  77  GLU GLU B . n 
B 1 84  GLU 84  78  78  GLU GLU B . n 
B 1 85  ARG 85  79  79  ARG ARG B . n 
B 1 86  HIS 86  80  80  HIS HIS B . n 
B 1 87  VAL 87  81  81  VAL VAL B . n 
B 1 88  GLY 88  82  82  GLY GLY B . n 
B 1 89  ASP 89  83  83  ASP ASP B . n 
B 1 90  LEU 90  84  84  LEU LEU B . n 
B 1 91  ARG 91  85  85  ARG ARG B . n 
B 1 92  ASN 92  86  86  ASN ASN B . n 
B 1 93  VAL 93  87  87  VAL VAL B . n 
B 1 94  THR 94  88  88  THR THR B . n 
B 1 95  ALA 95  89  89  ALA ALA B . n 
B 1 96  ASP 96  90  90  ASP ASP B . n 
B 1 97  LYS 97  91  91  LYS LYS B . n 
B 1 98  ASP 98  92  92  ASP ASP B . n 
B 1 99  GLY 99  93  93  GLY GLY B . n 
B 1 100 VAL 100 94  94  VAL VAL B . n 
B 1 101 ALA 101 95  95  ALA ALA B . n 
B 1 102 ASP 102 96  96  ASP ASP B . n 
B 1 103 VAL 103 97  97  VAL VAL B . n 
B 1 104 SER 104 98  98  SER SER B . n 
B 1 105 ILE 105 99  99  ILE ILE B . n 
B 1 106 GLU 106 100 100 GLU GLU B . n 
B 1 107 ASP 107 101 101 ASP ASP B . n 
B 1 108 SER 108 102 102 SER SER B . n 
B 1 109 VAL 109 103 103 VAL VAL B . n 
B 1 110 ILE 110 104 104 ILE ILE B . n 
B 1 111 SER 111 105 105 SER SER B . n 
B 1 112 LEU 112 106 106 LEU LEU B . n 
B 1 113 SER 113 107 107 SER SER B . n 
B 1 114 GLY 114 108 108 GLY GLY B . n 
B 1 115 ASP 115 109 109 ASP ASP B . n 
B 1 116 HIS 116 110 110 HIS HIS B . n 
B 1 117 CYS 117 111 111 CYS CYS B . n 
B 1 118 ILE 118 112 112 ILE ILE B . n 
B 1 119 ILE 119 113 113 ILE ILE B . n 
B 1 120 GLY 120 114 114 GLY GLY B . n 
B 1 121 ARG 121 115 115 ARG ARG B . n 
B 1 122 THR 122 116 116 THR THR B . n 
B 1 123 LEU 123 117 117 LEU LEU B . n 
B 1 124 VAL 124 118 118 VAL VAL B . n 
B 1 125 VAL 125 119 119 VAL VAL B . n 
B 1 126 HIS 126 120 120 HIS HIS B . n 
B 1 127 GLU 127 121 121 GLU GLU B . n 
B 1 128 LYS 128 122 122 LYS LYS B . n 
B 1 129 ALA 129 123 123 ALA ALA B . n 
B 1 130 ASP 130 124 124 ASP ASP B . n 
B 1 131 ASP 131 125 125 ASP ASP B . n 
B 1 132 LEU 132 126 126 LEU LEU B . n 
B 1 133 GLY 133 127 127 GLY GLY B . n 
B 1 134 LYS 134 128 128 LYS LYS B . n 
B 1 135 GLY 135 129 129 GLY GLY B . n 
B 1 136 GLY 136 130 130 GLY GLY B . n 
B 1 137 ASN 137 131 131 ASN ASN B . n 
B 1 138 GLU 138 132 132 GLU GLU B . n 
B 1 139 GLU 139 133 133 GLU GLU B . n 
B 1 140 SER 140 134 134 SER SER B . n 
B 1 141 THR 141 135 135 THR THR B . n 
B 1 142 LYS 142 136 136 LYS LYS B . n 
B 1 143 THR 143 137 137 THR THR B . n 
B 1 144 GLY 144 138 138 GLY GLY B . n 
B 1 145 ASN 145 139 139 ASN ASN B . n 
B 1 146 ALA 146 140 140 ALA ALA B . n 
B 1 147 GLY 147 141 141 GLY GLY B . n 
B 1 148 SER 148 142 142 SER SER B . n 
B 1 149 ARG 149 143 143 ARG ARG B . n 
B 1 150 LEU 150 144 144 LEU LEU B . n 
B 1 151 ALA 151 145 145 ALA ALA B . n 
B 1 152 CYS 152 146 146 CYS CYS B . n 
B 1 153 GLY 153 147 147 GLY GLY B . n 
B 1 154 VAL 154 148 148 VAL VAL B . n 
B 1 155 ILE 155 149 149 ILE ILE B . n 
B 1 156 GLY 156 150 150 GLY GLY B . n 
B 1 157 ILE 157 151 151 ILE ILE B . n 
B 1 158 ALA 158 152 152 ALA ALA B . n 
B 1 159 GLN 159 153 ?   ?   ?   B . n 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NPPSFA, National Project on Protein Structural and Functional Analyses' 
_pdbx_SG_project.full_name_of_center   'RIKEN Structural Genomics/Proteomics Initiative' 
_pdbx_SG_project.initial_of_center     RSGI 
# 
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 CU1 1  301 301 CU1 CU1 A . 
D 3 ZN  1  401 401 ZN  ZN  A . 
E 2 CU1 1  302 302 CU1 CU1 B . 
F 3 ZN  1  402 402 ZN  ZN  B . 
G 4 HOH 1  402 3   HOH HOH A . 
G 4 HOH 2  403 6   HOH HOH A . 
G 4 HOH 3  404 7   HOH HOH A . 
G 4 HOH 4  405 8   HOH HOH A . 
G 4 HOH 5  406 10  HOH HOH A . 
G 4 HOH 6  407 14  HOH HOH A . 
G 4 HOH 7  408 15  HOH HOH A . 
G 4 HOH 8  409 16  HOH HOH A . 
G 4 HOH 9  410 17  HOH HOH A . 
G 4 HOH 10 411 18  HOH HOH A . 
G 4 HOH 11 412 20  HOH HOH A . 
G 4 HOH 12 413 21  HOH HOH A . 
G 4 HOH 13 414 23  HOH HOH A . 
G 4 HOH 14 415 24  HOH HOH A . 
G 4 HOH 15 416 33  HOH HOH A . 
G 4 HOH 16 417 35  HOH HOH A . 
G 4 HOH 17 418 36  HOH HOH A . 
G 4 HOH 18 419 40  HOH HOH A . 
G 4 HOH 19 420 42  HOH HOH A . 
G 4 HOH 20 421 44  HOH HOH A . 
G 4 HOH 21 422 45  HOH HOH A . 
G 4 HOH 22 423 46  HOH HOH A . 
H 4 HOH 1  403 1   HOH HOH B . 
H 4 HOH 2  404 2   HOH HOH B . 
H 4 HOH 3  405 4   HOH HOH B . 
H 4 HOH 4  406 5   HOH HOH B . 
H 4 HOH 5  407 9   HOH HOH B . 
H 4 HOH 6  408 11  HOH HOH B . 
H 4 HOH 7  409 12  HOH HOH B . 
H 4 HOH 8  410 13  HOH HOH B . 
H 4 HOH 9  411 19  HOH HOH B . 
H 4 HOH 10 412 22  HOH HOH B . 
H 4 HOH 11 413 25  HOH HOH B . 
H 4 HOH 12 414 26  HOH HOH B . 
H 4 HOH 13 415 27  HOH HOH B . 
H 4 HOH 14 416 28  HOH HOH B . 
H 4 HOH 15 417 29  HOH HOH B . 
H 4 HOH 16 418 30  HOH HOH B . 
H 4 HOH 17 419 31  HOH HOH B . 
H 4 HOH 18 420 32  HOH HOH B . 
H 4 HOH 19 421 34  HOH HOH B . 
H 4 HOH 20 422 37  HOH HOH B . 
H 4 HOH 21 423 38  HOH HOH B . 
H 4 HOH 22 424 39  HOH HOH B . 
H 4 HOH 23 425 41  HOH HOH B . 
H 4 HOH 24 426 43  HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1200  ? 
1 MORE         -9.1  ? 
1 'SSA (A^2)'  13450 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 52 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 301 ? 1_555 NE2 ? A HIS 54  ? A HIS 48  ? 1_555 138.9 ? 
2  ND1 ? A HIS 52 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 301 ? 1_555 NE2 ? A HIS 126 ? A HIS 120 ? 1_555 97.9  ? 
3  NE2 ? A HIS 54 ? A HIS 48 ? 1_555 CU ? C CU1 . ? A CU1 301 ? 1_555 NE2 ? A HIS 126 ? A HIS 120 ? 1_555 121.9 ? 
4  ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 ND1 ? A HIS 77  ? A HIS 71  ? 1_555 101.3 ? 
5  ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 ND1 ? A HIS 86  ? A HIS 80  ? 1_555 110.6 ? 
6  ND1 ? A HIS 77 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 ND1 ? A HIS 86  ? A HIS 80  ? 1_555 123.0 ? 
7  ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD1 ? A ASP 89  ? A ASP 83  ? 1_555 98.2  ? 
8  ND1 ? A HIS 77 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD1 ? A ASP 89  ? A ASP 83  ? 1_555 97.4  ? 
9  ND1 ? A HIS 86 ? A HIS 80 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD1 ? A ASP 89  ? A ASP 83  ? 1_555 122.1 ? 
10 ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD2 ? A ASP 89  ? A ASP 83  ? 1_555 150.9 ? 
11 ND1 ? A HIS 77 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD2 ? A ASP 89  ? A ASP 83  ? 1_555 76.3  ? 
12 ND1 ? A HIS 86 ? A HIS 80 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD2 ? A ASP 89  ? A ASP 83  ? 1_555 94.1  ? 
13 OD1 ? A ASP 89 ? A ASP 83 ? 1_555 ZN ? D ZN  . ? A ZN  401 ? 1_555 OD2 ? A ASP 89  ? A ASP 83  ? 1_555 54.2  ? 
14 ND1 ? B HIS 52 ? B HIS 46 ? 1_555 CU ? E CU1 . ? B CU1 302 ? 1_555 NE2 ? B HIS 54  ? B HIS 48  ? 1_555 139.0 ? 
15 ND1 ? B HIS 52 ? B HIS 46 ? 1_555 CU ? E CU1 . ? B CU1 302 ? 1_555 NE2 ? B HIS 126 ? B HIS 120 ? 1_555 100.4 ? 
16 NE2 ? B HIS 54 ? B HIS 48 ? 1_555 CU ? E CU1 . ? B CU1 302 ? 1_555 NE2 ? B HIS 126 ? B HIS 120 ? 1_555 120.3 ? 
17 ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 ND1 ? B HIS 77  ? B HIS 71  ? 1_555 101.5 ? 
18 ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 ND1 ? B HIS 86  ? B HIS 80  ? 1_555 112.4 ? 
19 ND1 ? B HIS 77 ? B HIS 71 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 ND1 ? B HIS 86  ? B HIS 80  ? 1_555 121.5 ? 
20 ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 OD1 ? B ASP 89  ? B ASP 83  ? 1_555 105.6 ? 
21 ND1 ? B HIS 77 ? B HIS 71 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 OD1 ? B ASP 89  ? B ASP 83  ? 1_555 102.6 ? 
22 ND1 ? B HIS 86 ? B HIS 80 ? 1_555 ZN ? F ZN  . ? B ZN  402 ? 1_555 OD1 ? B ASP 89  ? B ASP 83  ? 1_555 111.5 ? 
# 
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 2009-03-24 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-04-04 
4 'Structure model' 1 3 2021-11-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Other                       
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2         
2 4 'Structure model' struct_conn        
3 4 'Structure model' struct_ref_seq_dif 
4 4 'Structure model' struct_site        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_database_2.pdbx_DOI'                
2  4 'Structure model' '_database_2.pdbx_database_accession' 
3  4 'Structure model' '_struct_conn.pdbx_dist_value'        
4  4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  4 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  4 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  4 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
17 4 'Structure model' '_struct_ref_seq_dif.details'         
18 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
19 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
20 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement        1.1 ? 1 
HKL-2000  'data collection' .   ? 2 
DENZO     'data reduction'  .   ? 3 
SCALEPACK 'data scaling'    .   ? 4 
MOLREP    phasing           .   ? 5 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     78 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OE2 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    GLU 
_pdbx_validate_symm_contact.auth_seq_id_2     121 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_547 
_pdbx_validate_symm_contact.dist              2.16 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    HIS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     110 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -75.25 
_pdbx_validate_torsion.psi             22.51 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -5  ? A GLY 1   
2  1 Y 1 A PRO -4  ? A PRO 2   
3  1 Y 1 A LEU -3  ? A LEU 3   
4  1 Y 1 A GLY -2  ? A GLY 4   
5  1 Y 1 A SER -1  ? A SER 5   
6  1 Y 1 A MET 0   ? A MET 6   
7  1 Y 1 A ALA 1   ? A ALA 7   
8  1 Y 1 A LYS 23  ? A LYS 29  
9  1 Y 1 A GLU 24  ? A GLU 30  
10 1 Y 1 A GLN 153 ? A GLN 159 
11 1 Y 1 B GLY -5  ? B GLY 1   
12 1 Y 1 B PRO -4  ? B PRO 2   
13 1 Y 1 B LEU -3  ? B LEU 3   
14 1 Y 1 B GLY -2  ? B GLY 4   
15 1 Y 1 B SER -1  ? B SER 5   
16 1 Y 1 B MET 0   ? B MET 6   
17 1 Y 1 B LYS 23  ? B LYS 29  
18 1 Y 1 B GLU 24  ? B GLU 30  
19 1 Y 1 B SER 25  ? B SER 31  
20 1 Y 1 B THR 54  ? B THR 60  
21 1 Y 1 B ALA 55  ? B ALA 61  
22 1 Y 1 B GLY 56  ? B GLY 62  
23 1 Y 1 B GLN 153 ? B GLN 159 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (I) ION' CU1 
3 'ZINC ION'       ZN  
4 water            HOH 
# 
