data_1AZV
# 
_entry.id   1AZV 
# 
_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   1AZV         pdb_00001azv 10.2210/pdb1azv/pdb 
WWPDB D_1000171458 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1AZV 
_pdbx_database_status.recvd_initial_deposition_date   1997-11-21 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Hart, P.J.'       1 
'Liu, H.'          2 
'Pellegrini, M.'   3 
'Nersissian, A.M.' 4 
'Gralla, E.B.'     5 
'Valentine, J.S.'  6 
'Eisenberg, D.'    7 
# 
_citation.id                        primary 
_citation.title                     
'Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.' 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_volume            7 
_citation.page_first                545 
_citation.page_last                 555 
_citation.year                      1998 
_citation.journal_id_ASTM           PRCIEI 
_citation.country                   US 
_citation.journal_id_ISSN           0961-8368 
_citation.journal_id_CSD            0795 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   9541385 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hart, P.J.'       1 ? 
primary 'Liu, H.'          2 ? 
primary 'Pellegrini, M.'   3 ? 
primary 'Nersissian, A.M.' 4 ? 
primary 'Gralla, E.B.'     5 ? 
primary 'Valentine, J.S.'  6 ? 
primary 'Eisenberg, D.'    7 ? 
# 
_cell.entry_id           1AZV 
_cell.length_a           67.200 
_cell.length_b           67.200 
_cell.length_c           83.800 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1AZV 
_symmetry.space_group_name_H-M             'P 41' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
# 
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 'COPPER/ZINC SUPEROXIDE DISMUTASE' 15927.703 2   1.15.1.1 G37R ? ? 
2 non-polymer syn 'COPPER (II) ION'                  63.546    2   ?        ?    ? ? 
3 non-polymer syn 'ZINC ION'                         65.409    2   ?        ?    ? ? 
4 water       nat water                              18.015    176 ?        ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CUZNSOD 
# 
_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       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKRLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKRLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  ARG n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    CYTOPLASM 
_entity_src_gen.host_org_common_name               
;baker's yeast
;
_entity_src_gen.pdbx_host_org_scientific_name      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     Saccharomyces 
_entity_src_gen.pdbx_host_org_gene                 'YEAST CUZNSOD PROMOTER' 
_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               EG118 
_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    CYTOPLASM 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               YEP351 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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 1AZV A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 1AZV B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
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 1AZV ARG A 37 ? UNP P00441 GLY 37 'engineered mutation' 37 1 
2 1AZV ARG B 37 ? UNP P00441 GLY 37 'engineered mutation' 37 2 
# 
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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
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          1AZV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.9 
_exptl_crystal.density_percent_sol   58. 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'20 MG/ML PROTEIN IN 10MM ACETATE PH 5.5 MIXED WITH PRECIPITATING SOLUTION OF 100 MM ACETATE PH 4.6, 2.0 M AMMONIUM SULFATE' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           300 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   RIGAKU 
_diffrn_detector.pdbx_collection_date   1997-01 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RUH2R' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1AZV 
_reflns.observed_criterion_sigma_I   0. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             100. 
_reflns.d_resolution_high            1.90 
_reflns.number_obs                   29129 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.065 
_reflns.pdbx_netI_over_sigmaI        17. 
_reflns.B_iso_Wilson_estimate        29.3 
_reflns.pdbx_redundancy              3.5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.90 
_reflns_shell.d_res_low              1.97 
_reflns_shell.percent_possible_all   99.6 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.383 
_reflns_shell.meanI_over_sigI_obs    1.8 
_reflns_shell.pdbx_redundancy        2.5 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1AZV 
_refine.ls_number_reflns_obs                     28975 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0. 
_refine.pdbx_data_cutoff_high_absF               100000. 
_refine.pdbx_data_cutoff_low_absF                0.0 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             10.0 
_refine.ls_d_res_high                            1.9 
_refine.ls_percent_reflns_obs                    99.3 
_refine.ls_R_factor_obs                          0.202 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.202 
_refine.ls_R_factor_R_free                       0.244 
_refine.ls_R_factor_R_free_error                 0.005 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  2889 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               29. 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1SPD' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1AZV 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           10. 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_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_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2234 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             176 
_refine_hist.number_atoms_total               2414 
_refine_hist.d_res_high                       1.9 
_refine_hist.d_res_low                        10.0 
# 
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 
x_bond_d                0.011 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             1.74  ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      26.7  ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      1.47  ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   8 
_refine_ls_shell.d_res_high                       1.90 
_refine_ls_shell.d_res_low                        1.99 
_refine_ls_shell.number_reflns_R_work             3265 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               98.6 
_refine_ls_shell.R_factor_R_free                  0.368 
_refine_ls_shell.R_factor_R_free_error            0.020 
_refine_ls_shell.percent_reflns_R_free            9.4 
_refine_ls_shell.number_reflns_R_free             343 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PARHCSDX.PRO TOPHCSDX.PRO 'X-RAY DIFFRACTION' 
2 ?            ?            'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1AZV 
_struct.title                     'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1AZV 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR, FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS MUTANT' 
# 
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 
# 
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 GLY A 56  ? ALA A 60  ? GLY A 56  ALA A 60  5 ? 5 
HELX_P HELX_P2 2 GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 1 ? 5 
HELX_P HELX_P3 3 THR B 58  ? ALA B 60  ? THR B 58  ALA B 60  5 ? 3 
HELX_P HELX_P4 4 GLU B 133 ? THR B 135 ? GLU B 133 THR B 135 5 ? 3 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc1  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 C CU  .   CU ? ? A HIS 46  A CU  154 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc2  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 48  A CU  154 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc3  metalc ? ? A HIS 63  NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 63  A CU  154 1_555 ? ? ? ? ? ? ? 2.647 ? ? 
metalc4  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  155 1_555 ? ? ? ? ? ? ? 1.911 ? ? 
metalc5  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  155 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc6  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  155 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc7  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  155 1_555 ? ? ? ? ? ? ? 1.896 ? ? 
metalc8  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 120 A CU  154 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc9  metalc ? ? B HIS 46  ND1 ? ? ? 1_555 E CU  .   CU ? ? B HIS 46  B CU  154 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc10 metalc ? ? B HIS 48  NE2 ? ? ? 1_555 E CU  .   CU ? ? B HIS 48  B CU  154 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc11 metalc ? ? B HIS 63  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 63  B ZN  155 1_555 ? ? ? ? ? ? ? 1.791 ? ? 
metalc12 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 71  B ZN  155 1_555 ? ? ? ? ? ? ? 2.232 ? ? 
metalc13 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 80  B ZN  155 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc14 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 1.844 ? ? 
metalc15 metalc ? ? B ASP 83  OD2 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 2.735 ? ? 
metalc16 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 E CU  .   CU ? ? B HIS 120 B CU  154 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
# 
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 ILE A 149 ? ILE A 151 ? ILE A 149 ILE A 151 
A 2 THR A 2   ? LYS A 9   ? THR A 2   LYS A 9   
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 5 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
B 1 GLY A 41  ? GLY A 44  ? GLY A 41  GLY A 44  
B 2 ASN A 86  ? ALA A 89  ? ASN A 86  ALA A 89  
C 1 PHE A 45  ? HIS A 48  ? PHE A 45  HIS A 48  
C 2 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
C 3 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
D 1 GLY B 150 ? ALA B 152 ? GLY B 150 ALA B 152 
D 2 THR B 2   ? LYS B 9   ? THR B 2   LYS B 9   
D 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
D 4 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
D 5 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
E 1 GLY B 41  ? GLY B 44  ? GLY B 41  GLY B 44  
E 2 ASN B 86  ? ALA B 89  ? ASN B 86  ALA B 89  
F 1 PHE B 45  ? HIS B 48  ? PHE B 45  HIS B 48  
F 2 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
F 3 ARG B 143 ? VAL B 148 ? 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 GLY A 150 ? O GLY A 150 N VAL A 5   ? N VAL A 5   
A 2 3 O THR A 2   ? O THR A 2   N GLN A 22  ? N GLN A 22  
A 3 4 O GLN A 15  ? O GLN A 15  N LYS A 36  ? N LYS A 36  
A 4 5 O VAL A 29  ? O VAL A 29  N ASP A 101 ? N ASP A 101 
B 1 2 O GLY A 41  ? O GLY A 41  N ALA A 89  ? N ALA A 89  
C 1 2 O HIS A 46  ? O HIS A 46  N VAL A 118 ? N VAL A 118 
C 2 3 O LEU A 117 ? O LEU A 117 N GLY A 147 ? N GLY A 147 
D 1 2 O GLY B 150 ? O GLY B 150 N VAL B 5   ? N VAL B 5   
D 2 3 O THR B 2   ? O THR B 2   N GLN B 22  ? N GLN B 22  
D 3 4 O GLN B 15  ? O GLN B 15  N LYS B 36  ? N LYS B 36  
D 4 5 O VAL B 29  ? O VAL B 29  N ASP B 101 ? N ASP B 101 
E 1 2 O GLY B 41  ? O GLY B 41  N ALA B 89  ? N ALA B 89  
F 1 2 O HIS B 46  ? O HIS B 46  N VAL B 118 ? N VAL B 118 
F 2 3 O LEU B 117 ? O LEU B 117 N GLY B 147 ? N 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 CU 154 ? 4 'BINDING SITE FOR RESIDUE CU A 154' 
AC2 Software A ZN 155 ? 4 'BINDING SITE FOR RESIDUE ZN A 155' 
AC3 Software B CU 154 ? 4 'BINDING SITE FOR RESIDUE CU B 154' 
AC4 Software B ZN 155 ? 4 'BINDING SITE FOR RESIDUE ZN B 155' 
# 
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 46  ? HIS A 46  . ? 1_555 ? 
2  AC1 4 HIS A 48  ? HIS A 48  . ? 1_555 ? 
3  AC1 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
4  AC1 4 HIS A 120 ? HIS A 120 . ? 1_555 ? 
5  AC2 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
6  AC2 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
7  AC2 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
8  AC2 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
9  AC3 4 HIS B 46  ? HIS B 46  . ? 1_555 ? 
10 AC3 4 HIS B 48  ? HIS B 48  . ? 1_555 ? 
11 AC3 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
12 AC3 4 HIS B 120 ? HIS B 120 . ? 1_555 ? 
13 AC4 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
14 AC4 4 HIS B 71  ? HIS B 71  . ? 1_555 ? 
15 AC4 4 HIS B 80  ? HIS B 80  . ? 1_555 ? 
16 AC4 4 ASP B 83  ? ASP B 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1AZV 
_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                    1AZV 
_atom_sites.fract_transf_matrix[1][1]   0.014881 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014881 
_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]   0.011933 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 75.174 44.840 3.494   1.00 20.92 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 74.134 43.789 3.681   1.00 22.70 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 72.764 44.335 3.286   1.00 25.56 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 72.423 45.483 3.604   1.00 26.57 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 74.096 43.302 5.122   1.00 20.68 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 72.000 43.520 2.564   1.00 25.28 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 70.665 43.872 2.108   1.00 25.12 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 69.684 43.422 3.179   1.00 23.09 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 69.874 42.383 3.807   1.00 23.23 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 70.380 43.190 0.751   1.00 28.53 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 71.328 43.680 -0.211  1.00 30.89 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 68.954 43.476 0.262   1.00 27.69 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 68.654 44.222 3.414   1.00 21.31 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 67.675 43.919 4.441   1.00 20.88 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 66.254 43.996 3.902   1.00 19.05 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 65.958 44.730 2.951   1.00 19.02 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 67.834 44.891 5.622   1.00 21.29 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 69.248 44.952 6.156   1.00 28.40 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 69.465 45.993 7.237   1.00 31.85 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 68.813 45.584 8.531   1.00 36.65 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 69.325 46.418 9.655   1.00 40.91 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 65.381 43.233 4.537   1.00 17.81 ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 63.980 43.200 4.182   1.00 17.67 ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 63.259 42.934 5.497   1.00 17.12 ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 63.890 42.540 6.495   1.00 17.87 ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 63.709 42.111 3.161   1.00 14.42 ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 61.957 43.203 5.518   1.00 17.41 ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 61.145 43.042 6.715   1.00 16.80 ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 59.742 42.645 6.300   1.00 16.11 ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 59.274 42.996 5.217   1.00 15.87 ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 61.111 44.377 7.545   1.00 14.82 ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 60.402 45.476 6.761   1.00 12.20 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 60.470 44.163 8.907   1.00 15.75 ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 59.071 41.906 7.164   1.00 16.97 ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 57.734 41.477 6.869   1.00 17.52 ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 56.895 41.576 8.123   1.00 17.72 ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 57.317 41.117 9.177   1.00 19.93 ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 57.753 40.028 6.371   1.00 17.99 ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 56.148 39.442 5.895   1.00 21.47 ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 55.747 42.238 8.027   1.00 17.48 ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 54.825 42.353 9.155   1.00 18.90 ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 53.701 41.339 8.885   1.00 19.54 ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 52.993 41.457 7.884   1.00 21.09 ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 54.225 43.767 9.260   1.00 18.42 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 53.200 43.816 10.365  1.00 22.26 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 55.315 44.790 9.508   1.00 18.67 ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 53.580 40.319 9.730   1.00 21.03 ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 52.557 39.280 9.568   1.00 23.16 ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 51.299 39.611 10.339  1.00 23.49 ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 51.350 39.880 11.527  1.00 24.66 ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 53.046 37.910 10.064  1.00 22.58 ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 54.195 37.098 9.471   1.00 23.57 ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 53.953 36.800 8.019   1.00 24.14 ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 55.472 37.834 9.641   1.00 25.66 ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 50.167 39.578 9.659   1.00 25.83 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 48.880 39.832 10.282  1.00 30.92 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 47.880 38.976 9.538   1.00 33.55 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 48.074 38.666 8.363   1.00 32.57 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 48.480 41.315 10.187  1.00 32.94 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 49.192 42.217 11.196  1.00 37.87 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 48.801 43.689 11.047  1.00 43.02 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 49.765 44.617 11.817  1.00 46.41 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 49.952 44.255 13.267  1.00 48.78 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 46.823 38.566 10.218  1.00 36.64 ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 45.830 37.755 9.559   1.00 40.57 ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 44.476 38.064 10.120  1.00 43.67 ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 44.317 39.017 10.882  1.00 42.67 ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 43.480 37.307 9.682   1.00 48.42 ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 42.125 37.481 10.194  1.00 52.97 ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 42.134 36.682 11.494  1.00 53.71 ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 41.461 35.658 11.619  1.00 56.89 ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 41.074 36.911 9.222   1.00 56.50 ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 40.874 37.779 7.977   1.00 61.55 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 40.862 39.031 8.099   1.00 65.55 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 40.713 37.200 6.876   1.00 63.85 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 42.972 37.111 12.427  1.00 52.10 ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 43.079 36.424 13.686  1.00 49.14 ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 43.999 37.219 14.565  1.00 48.29 ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 44.377 38.339 14.217  1.00 49.41 ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 44.347 36.686 15.739  1.00 46.76 ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 45.238 37.404 16.643  1.00 45.16 ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 46.719 37.113 16.375  1.00 43.73 ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 47.584 37.713 17.016  1.00 41.37 ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 44.782 36.905 18.008  1.00 45.83 ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 44.512 35.467 17.736  1.00 47.14 ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 43.782 35.493 16.396  1.00 46.90 ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 47.011 36.198 15.442  1.00 41.22 ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 48.406 35.882 15.109  1.00 38.96 ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 49.049 37.054 14.370  1.00 37.71 ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 48.530 37.538 13.355  1.00 37.77 ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 48.554 34.635 14.211  1.00 37.69 ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 50.041 34.373 13.927  1.00 34.21 ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 47.897 33.440 14.853  1.00 36.62 ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 50.185 37.499 14.884  1.00 36.15 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 50.898 38.608 14.290  1.00 34.60 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 52.355 38.449 14.638  1.00 31.60 ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 52.696 37.808 15.625  1.00 33.14 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 50.345 39.944 14.803  1.00 36.29 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 50.222 40.040 16.313  1.00 42.83 ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 49.748 41.409 16.786  1.00 48.27 ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 50.549 42.331 16.950  1.00 53.11 ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 48.452 41.541 17.032  1.00 49.44 ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 53.217 38.993 13.796  1.00 29.41 ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 54.639 38.890 14.025  1.00 27.20 ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 55.409 39.805 13.099  1.00 24.34 ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 54.828 40.440 12.227  1.00 24.07 ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 56.712 39.908 13.328  1.00 23.61 ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 57.583 40.735 12.520  1.00 21.70 ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 58.813 39.910 12.287  1.00 21.17 ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 59.404 39.396 13.241  1.00 22.40 ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 57.952 42.084 13.209  1.00 21.44 ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 56.704 42.994 13.244  1.00 24.36 ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 59.116 42.761 12.456  1.00 19.66 ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 56.850 44.341 13.971  1.00 26.13 ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 59.138 39.716 11.010  1.00 20.60 ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 60.299 38.935 10.593  1.00 19.82 ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 61.275 39.826 9.824   1.00 19.77 ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 60.879 40.607 8.953   1.00 21.62 ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 59.855 37.731 9.696   1.00 19.69 ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 58.741 36.928 10.385  1.00 19.00 ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 61.039 36.824 9.367   1.00 18.31 ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 59.139 36.238 11.668  1.00 18.17 ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 62.549 39.723 10.162  1.00 20.01 ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 63.596 40.491 9.512   1.00 19.31 ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 64.450 39.551 8.690   1.00 18.12 ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 64.650 38.397 9.055   1.00 20.67 ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 64.460 41.188 10.562  1.00 20.14 ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 63.637 42.016 11.513  1.00 23.26 ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 63.137 41.517 12.525  1.00 26.76 ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 63.432 43.269 11.165  1.00 23.57 ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 64.957 40.055 7.580   1.00 17.70 ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 65.791 39.293 6.682   1.00 17.31 ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 67.054 40.084 6.449   1.00 17.73 ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 66.996 41.294 6.263   1.00 17.59 ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 65.104 39.145 5.324   1.00 19.66 ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 63.852 38.316 5.347   1.00 20.27 ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 62.624 38.899 5.637   1.00 20.29 ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 63.905 36.957 5.062   1.00 19.86 ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 61.474 38.145 5.642   1.00 21.20 ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 62.764 36.197 5.065   1.00 19.54 ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 61.544 36.783 5.354   1.00 20.25 ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 68.190 39.408 6.429   1.00 17.17 ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 69.448 40.085 6.178   1.00 20.38 ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 70.314 39.184 5.335   1.00 19.64 ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 70.435 38.006 5.627   1.00 20.79 ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 70.180 40.435 7.485   1.00 23.82 ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 71.503 41.190 7.245   1.00 31.20 ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 72.188 41.734 8.512   1.00 35.80 ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 71.536 42.462 9.297   1.00 35.77 ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 73.403 41.456 8.698   1.00 41.17 ? 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 70.885 39.742 4.272   1.00 23.09 ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 71.763 39.010 3.358   1.00 25.54 ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 73.027 39.856 3.096   1.00 26.06 ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 72.949 40.920 2.491   1.00 25.84 ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 71.021 38.694 2.045   1.00 22.59 ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 71.755 37.723 1.132   1.00 22.96 ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 71.061 37.525 -0.183  1.00 20.88 ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 70.303 38.371 -0.612  1.00 21.33 ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 71.313 36.399 -0.827  1.00 23.09 ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 74.184 39.372 3.546   1.00 30.24 ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 75.456 40.090 3.396   1.00 35.10 ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 75.914 40.266 1.972   1.00 37.36 ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 76.389 41.338 1.607   1.00 37.24 ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 76.572 39.368 4.128   1.00 36.16 ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 76.364 39.195 5.588   1.00 38.76 ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 77.323 38.146 6.105   1.00 42.88 ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 78.745 38.507 5.730   1.00 43.22 ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 79.048 39.861 6.236   1.00 45.68 ? 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 75.821 39.184 1.199   1.00 42.04 ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 76.243 39.169 -0.207  1.00 46.66 ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 75.157 38.614 -1.124  1.00 47.09 ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 74.393 37.747 -0.704  1.00 46.74 ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 77.493 38.307 -0.354  1.00 49.45 ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 78.661 38.783 0.464   1.00 54.93 ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 79.650 37.686 0.702   1.00 58.92 ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 80.497 37.450 -0.190  1.00 61.66 ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 79.560 37.053 1.778   1.00 62.36 ? 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 75.152 39.056 -2.386  1.00 49.27 ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 74.164 38.625 -3.393  1.00 52.25 ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 73.976 37.112 -3.373  1.00 52.21 ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 72.865 36.597 -3.557  1.00 52.73 ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 74.592 39.074 -4.797  1.00 54.80 ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 73.511 38.987 -5.719  1.00 58.72 ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 75.094 36.410 -3.257  1.00 52.30 ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 75.076 34.961 -3.151  1.00 53.05 ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 75.531 34.824 -1.707  1.00 50.47 ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 76.461 35.513 -1.267  1.00 53.61 ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 76.090 34.300 -4.108  1.00 56.84 ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 77.489 34.185 -3.503  1.00 59.78 ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 77.717 33.393 -2.581  1.00 63.89 ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 78.429 34.974 -4.021  1.00 60.33 ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 74.845 34.001 -0.948  1.00 45.49 ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 75.232 33.845 0.433   1.00 39.47 ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 73.932 33.633 1.141   1.00 35.05 ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 72.873 33.986 0.616   1.00 35.58 ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 73.974 33.058 2.333   1.00 31.37 ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 72.727 32.833 3.039   1.00 30.53 ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 72.004 34.090 3.516   1.00 28.61 ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 72.585 35.173 3.666   1.00 29.49 ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 73.149 31.918 4.188   1.00 29.45 ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 74.515 32.350 4.459   1.00 30.69 ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 75.117 32.542 3.098   1.00 30.44 ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 70.706 33.921 3.690   1.00 26.89 ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 69.833 34.962 4.165   1.00 26.04 ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 69.500 34.571 5.605   1.00 25.97 ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 69.156 33.414 5.888   1.00 27.04 ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 68.525 35.017 3.307   1.00 22.15 ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 67.541 36.032 3.887   1.00 23.95 ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 68.853 35.376 1.879   1.00 20.80 ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 69.712 35.489 6.532   1.00 23.99 ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 69.371 35.213 7.908   1.00 24.80 ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 67.977 35.769 8.132   1.00 24.77 ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 67.689 36.914 7.753   1.00 24.99 ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 70.365 35.879 8.861   1.00 28.28 ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 71.747 35.234 8.869   1.00 36.82 ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 72.567 35.718 10.057  1.00 44.18 ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 73.748 34.785 10.372  1.00 49.65 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 74.446 35.145 11.666  1.00 53.54 ? 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 67.080 34.943 8.650   1.00 23.81 ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 65.725 35.405 8.944   1.00 25.30 ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 65.584 35.349 10.464  1.00 24.83 ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 65.929 34.359 11.104  1.00 25.28 ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 64.590 34.642 8.128   1.00 24.83 ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 65.156 33.494 7.310   1.00 26.51 ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 63.464 34.205 9.006   1.00 24.06 ? 31  VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? 65.211 36.472 11.049  1.00 23.72 ? 32  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? 65.099 36.571 12.491  1.00 24.25 ? 32  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? 63.823 37.305 12.841  1.00 22.36 ? 32  TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? 63.508 38.323 12.253  1.00 23.85 ? 32  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? 66.322 37.339 13.084  1.00 26.67 ? 32  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 66.237 37.316 14.552  1.00 30.51 ? 32  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 66.513 36.229 15.336  1.00 30.68 ? 32  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 65.430 38.192 15.367  1.00 29.66 ? 32  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 65.857 36.339 16.534  1.00 31.93 ? 32  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 65.192 37.534 16.587  1.00 30.67 ? 32  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? 64.866 39.460 15.169  1.00 28.49 ? 32  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 64.401 38.079 17.594  1.00 31.32 ? 32  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 64.081 40.006 16.172  1.00 27.38 ? 32  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 63.858 39.316 17.370  1.00 30.43 ? 32  TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? 63.100 36.822 13.825  1.00 21.19 ? 33  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? 61.895 37.515 14.196  1.00 21.15 ? 33  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? 61.167 36.744 15.252  1.00 21.63 ? 33  GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? 61.747 35.918 15.939  1.00 22.90 ? 33  GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? 59.887 37.023 15.384  1.00 23.81 ? 34  SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? 59.067 36.330 16.343  1.00 28.06 ? 34  SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? 57.610 36.580 15.980  1.00 27.93 ? 34  SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? 57.259 37.651 15.493  1.00 30.57 ? 34  SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? 59.365 36.830 17.758  1.00 30.35 ? 34  SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? 59.082 38.210 17.867  1.00 36.17 ? 34  SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? 56.764 35.594 16.221  1.00 28.78 ? 35  ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? 55.350 35.704 15.918  1.00 29.62 ? 35  ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? 54.663 35.321 17.219  1.00 31.26 ? 35  ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? 55.211 34.531 17.977  1.00 30.69 ? 35  ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? 54.961 34.706 14.798  1.00 29.66 ? 35  ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? 55.919 34.867 13.606  1.00 30.52 ? 35  ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? 53.521 34.946 14.347  1.00 29.46 ? 35  ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? 56.202 33.600 12.828  1.00 27.86 ? 35  ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? 53.502 35.892 17.508  1.00 34.07 ? 36  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? 52.811 35.546 18.743  1.00 38.93 ? 36  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? 51.344 35.212 18.524  1.00 39.98 ? 36  LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? 50.831 35.404 17.420  1.00 38.08 ? 36  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? 52.944 36.648 19.795  1.00 43.98 ? 36  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? 52.405 38.008 19.363  1.00 48.22 ? 36  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? 51.911 38.816 20.560  1.00 54.60 ? 36  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? 51.748 40.289 20.211  1.00 58.74 ? 36  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? 50.779 41.035 21.079  1.00 61.74 ? 36  LYS A NZ  1 
ATOM   267  N  N   . ARG A 1 37  ? 50.684 34.727 19.585  1.00 41.52 ? 37  ARG A N   1 
ATOM   268  C  CA  . ARG A 1 37  ? 49.271 34.324 19.555  1.00 42.76 ? 37  ARG A CA  1 
ATOM   269  C  C   . ARG A 1 37  ? 49.090 33.010 18.779  1.00 41.03 ? 37  ARG A C   1 
ATOM   270  O  O   . ARG A 1 37  ? 48.023 32.711 18.244  1.00 39.75 ? 37  ARG A O   1 
ATOM   271  C  CB  . ARG A 1 37  ? 48.412 35.416 18.928  1.00 48.27 ? 37  ARG A CB  1 
ATOM   272  C  CG  . ARG A 1 37  ? 48.259 36.675 19.778  1.00 57.07 ? 37  ARG A CG  1 
ATOM   273  C  CD  . ARG A 1 37  ? 47.046 36.575 20.713  1.00 64.75 ? 37  ARG A CD  1 
ATOM   274  N  NE  . ARG A 1 37  ? 47.396 36.195 22.082  1.00 71.73 ? 37  ARG A NE  1 
ATOM   275  C  CZ  . ARG A 1 37  ? 47.152 34.999 22.638  1.00 75.78 ? 37  ARG A CZ  1 
ATOM   276  N  NH1 . ARG A 1 37  ? 46.555 34.011 21.960  1.00 75.25 ? 37  ARG A NH1 1 
ATOM   277  N  NH2 . ARG A 1 37  ? 47.448 34.813 23.921  1.00 78.05 ? 37  ARG A NH2 1 
ATOM   278  N  N   . LEU A 1 38  ? 50.167 32.248 18.718  1.00 39.98 ? 38  LEU A N   1 
ATOM   279  C  CA  . LEU A 1 38  ? 50.211 30.974 18.030  1.00 40.98 ? 38  LEU A CA  1 
ATOM   280  C  C   . LEU A 1 38  ? 49.882 29.865 19.031  1.00 42.91 ? 38  LEU A C   1 
ATOM   281  O  O   . LEU A 1 38  ? 50.046 30.038 20.238  1.00 45.16 ? 38  LEU A O   1 
ATOM   282  C  CB  . LEU A 1 38  ? 51.638 30.767 17.534  1.00 37.95 ? 38  LEU A CB  1 
ATOM   283  C  CG  . LEU A 1 38  ? 52.001 30.623 16.062  1.00 38.24 ? 38  LEU A CG  1 
ATOM   284  C  CD1 . LEU A 1 38  ? 51.122 31.471 15.165  1.00 33.82 ? 38  LEU A CD1 1 
ATOM   285  C  CD2 . LEU A 1 38  ? 53.492 30.968 15.915  1.00 35.91 ? 38  LEU A CD2 1 
ATOM   286  N  N   . THR A 1 39  ? 49.425 28.723 18.535  1.00 43.86 ? 39  THR A N   1 
ATOM   287  C  CA  . THR A 1 39  ? 49.142 27.597 19.404  1.00 43.33 ? 39  THR A CA  1 
ATOM   288  C  C   . THR A 1 39  ? 50.497 26.918 19.582  1.00 44.59 ? 39  THR A C   1 
ATOM   289  O  O   . THR A 1 39  ? 51.301 26.897 18.645  1.00 45.27 ? 39  THR A O   1 
ATOM   290  C  CB  . THR A 1 39  ? 48.157 26.650 18.737  1.00 42.82 ? 39  THR A CB  1 
ATOM   291  O  OG1 . THR A 1 39  ? 48.737 26.106 17.545  1.00 44.23 ? 39  THR A OG1 1 
ATOM   292  C  CG2 . THR A 1 39  ? 46.901 27.406 18.364  1.00 42.45 ? 39  THR A CG2 1 
ATOM   293  N  N   . GLU A 1 40  ? 50.809 26.463 20.791  1.00 44.64 ? 40  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 52.090 25.809 21.003  1.00 44.71 ? 40  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 52.225 24.673 20.008  1.00 42.46 ? 40  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 51.249 23.981 19.709  1.00 41.63 ? 40  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 52.204 25.249 22.423  1.00 49.47 ? 40  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 53.403 24.307 22.591  1.00 55.15 ? 40  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 53.534 23.738 23.989  1.00 58.27 ? 40  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 52.500 23.338 24.577  1.00 59.12 ? 40  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 54.682 23.686 24.488  1.00 61.97 ? 40  GLU A OE2 1 
ATOM   302  N  N   . GLY A 1 41  ? 53.425 24.496 19.479  1.00 40.55 ? 41  GLY A N   1 
ATOM   303  C  CA  . GLY A 1 41  ? 53.642 23.432 18.523  1.00 38.83 ? 41  GLY A CA  1 
ATOM   304  C  C   . GLY A 1 41  ? 54.303 23.900 17.247  1.00 36.66 ? 41  GLY A C   1 
ATOM   305  O  O   . GLY A 1 41  ? 54.719 25.051 17.146  1.00 36.62 ? 41  GLY A O   1 
ATOM   306  N  N   . LEU A 1 42  ? 54.413 22.979 16.293  1.00 34.66 ? 42  LEU A N   1 
ATOM   307  C  CA  . LEU A 1 42  ? 55.023 23.209 14.989  1.00 31.99 ? 42  LEU A CA  1 
ATOM   308  C  C   . LEU A 1 42  ? 54.040 23.934 14.078  1.00 31.70 ? 42  LEU A C   1 
ATOM   309  O  O   . LEU A 1 42  ? 52.838 23.675 14.132  1.00 30.03 ? 42  LEU A O   1 
ATOM   310  C  CB  . LEU A 1 42  ? 55.372 21.859 14.372  1.00 33.37 ? 42  LEU A CB  1 
ATOM   311  C  CG  . LEU A 1 42  ? 56.809 21.326 14.295  1.00 36.74 ? 42  LEU A CG  1 
ATOM   312  C  CD1 . LEU A 1 42  ? 57.670 21.736 15.481  1.00 36.68 ? 42  LEU A CD1 1 
ATOM   313  C  CD2 . LEU A 1 42  ? 56.757 19.809 14.150  1.00 38.75 ? 42  LEU A CD2 1 
ATOM   314  N  N   . HIS A 1 43  ? 54.549 24.836 13.241  1.00 30.98 ? 43  HIS A N   1 
ATOM   315  C  CA  . HIS A 1 43  ? 53.713 25.600 12.303  1.00 30.43 ? 43  HIS A CA  1 
ATOM   316  C  C   . HIS A 1 43  ? 54.464 25.851 10.991  1.00 29.20 ? 43  HIS A C   1 
ATOM   317  O  O   . HIS A 1 43  ? 55.620 26.279 11.012  1.00 29.43 ? 43  HIS A O   1 
ATOM   318  C  CB  . HIS A 1 43  ? 53.301 26.947 12.903  1.00 30.26 ? 43  HIS A CB  1 
ATOM   319  C  CG  . HIS A 1 43  ? 52.280 26.850 13.993  1.00 27.23 ? 43  HIS A CG  1 
ATOM   320  N  ND1 . HIS A 1 43  ? 50.928 26.808 13.740  1.00 27.75 ? 43  HIS A ND1 1 
ATOM   321  C  CD2 . HIS A 1 43  ? 52.411 26.846 15.341  1.00 26.95 ? 43  HIS A CD2 1 
ATOM   322  C  CE1 . HIS A 1 43  ? 50.266 26.786 14.882  1.00 27.91 ? 43  HIS A CE1 1 
ATOM   323  N  NE2 . HIS A 1 43  ? 51.145 26.807 15.869  1.00 27.15 ? 43  HIS A NE2 1 
ATOM   324  N  N   . GLY A 1 44  ? 53.807 25.571 9.862   1.00 27.68 ? 44  GLY A N   1 
ATOM   325  C  CA  . GLY A 1 44  ? 54.416 25.766 8.554   1.00 23.87 ? 44  GLY A CA  1 
ATOM   326  C  C   . GLY A 1 44  ? 54.821 27.212 8.342   1.00 21.84 ? 44  GLY A C   1 
ATOM   327  O  O   . GLY A 1 44  ? 54.065 28.117 8.663   1.00 21.58 ? 44  GLY A O   1 
ATOM   328  N  N   . PHE A 1 45  ? 55.971 27.415 7.721   1.00 19.57 ? 45  PHE A N   1 
ATOM   329  C  CA  . PHE A 1 45  ? 56.521 28.748 7.492   1.00 20.67 ? 45  PHE A CA  1 
ATOM   330  C  C   . PHE A 1 45  ? 57.085 28.778 6.061   1.00 19.50 ? 45  PHE A C   1 
ATOM   331  O  O   . PHE A 1 45  ? 58.153 28.240 5.807   1.00 21.29 ? 45  PHE A O   1 
ATOM   332  C  CB  . PHE A 1 45  ? 57.650 28.943 8.523   1.00 21.81 ? 45  PHE A CB  1 
ATOM   333  C  CG  . PHE A 1 45  ? 58.185 30.342 8.614   1.00 22.01 ? 45  PHE A CG  1 
ATOM   334  C  CD1 . PHE A 1 45  ? 57.334 31.420 8.896   1.00 24.25 ? 45  PHE A CD1 1 
ATOM   335  C  CD2 . PHE A 1 45  ? 59.548 30.580 8.469   1.00 21.26 ? 45  PHE A CD2 1 
ATOM   336  C  CE1 . PHE A 1 45  ? 57.837 32.723 9.031   1.00 22.03 ? 45  PHE A CE1 1 
ATOM   337  C  CE2 . PHE A 1 45  ? 60.066 31.882 8.604   1.00 23.51 ? 45  PHE A CE2 1 
ATOM   338  C  CZ  . PHE A 1 45  ? 59.209 32.951 8.886   1.00 21.81 ? 45  PHE A CZ  1 
ATOM   339  N  N   . HIS A 1 46  ? 56.373 29.395 5.118   1.00 19.74 ? 46  HIS A N   1 
ATOM   340  C  CA  . HIS A 1 46  ? 56.838 29.412 3.732   1.00 17.47 ? 46  HIS A CA  1 
ATOM   341  C  C   . HIS A 1 46  ? 56.632 30.732 3.045   1.00 17.21 ? 46  HIS A C   1 
ATOM   342  O  O   . HIS A 1 46  ? 55.733 31.500 3.395   1.00 19.35 ? 46  HIS A O   1 
ATOM   343  C  CB  . HIS A 1 46  ? 56.065 28.403 2.868   1.00 19.25 ? 46  HIS A CB  1 
ATOM   344  C  CG  . HIS A 1 46  ? 55.746 27.121 3.559   1.00 18.31 ? 46  HIS A CG  1 
ATOM   345  N  ND1 . HIS A 1 46  ? 54.453 26.703 3.786   1.00 19.86 ? 46  HIS A ND1 1 
ATOM   346  C  CD2 . HIS A 1 46  ? 56.551 26.186 4.112   1.00 18.66 ? 46  HIS A CD2 1 
ATOM   347  C  CE1 . HIS A 1 46  ? 54.479 25.569 4.466   1.00 19.05 ? 46  HIS A CE1 1 
ATOM   348  N  NE2 . HIS A 1 46  ? 55.737 25.241 4.679   1.00 19.24 ? 46  HIS A NE2 1 
ATOM   349  N  N   . VAL A 1 47  ? 57.389 30.922 1.973   1.00 17.67 ? 47  VAL A N   1 
ATOM   350  C  CA  . VAL A 1 47  ? 57.254 32.108 1.141   1.00 18.81 ? 47  VAL A CA  1 
ATOM   351  C  C   . VAL A 1 47  ? 56.384 31.668 -0.044  1.00 19.50 ? 47  VAL A C   1 
ATOM   352  O  O   . VAL A 1 47  ? 56.664 30.656 -0.705  1.00 19.09 ? 47  VAL A O   1 
ATOM   353  C  CB  . VAL A 1 47  ? 58.612 32.635 0.626   1.00 18.39 ? 47  VAL A CB  1 
ATOM   354  C  CG1 . VAL A 1 47  ? 58.418 33.911 -0.187  1.00 17.70 ? 47  VAL A CG1 1 
ATOM   355  C  CG2 . VAL A 1 47  ? 59.535 32.908 1.789   1.00 19.20 ? 47  VAL A CG2 1 
ATOM   356  N  N   . HIS A 1 48  ? 55.240 32.330 -0.180  1.00 19.84 ? 48  HIS A N   1 
ATOM   357  C  CA  . HIS A 1 48  ? 54.314 32.090 -1.270  1.00 20.57 ? 48  HIS A CA  1 
ATOM   358  C  C   . HIS A 1 48  ? 54.637 33.057 -2.404  1.00 20.70 ? 48  HIS A C   1 
ATOM   359  O  O   . HIS A 1 48  ? 55.154 34.154 -2.179  1.00 20.80 ? 48  HIS A O   1 
ATOM   360  C  CB  . HIS A 1 48  ? 52.873 32.196 -0.795  1.00 19.62 ? 48  HIS A CB  1 
ATOM   361  C  CG  . HIS A 1 48  ? 52.449 31.041 0.055   1.00 23.62 ? 48  HIS A CG  1 
ATOM   362  N  ND1 . HIS A 1 48  ? 51.298 30.322 -0.183  1.00 25.56 ? 48  HIS A ND1 1 
ATOM   363  C  CD2 . HIS A 1 48  ? 53.031 30.471 1.137   1.00 25.86 ? 48  HIS A CD2 1 
ATOM   364  C  CE1 . HIS A 1 48  ? 51.184 29.362 0.714   1.00 26.66 ? 48  HIS A CE1 1 
ATOM   365  N  NE2 . HIS A 1 48  ? 52.223 29.428 1.531   1.00 29.35 ? 48  HIS A NE2 1 
ATOM   366  N  N   . GLU A 1 49  ? 54.306 32.643 -3.616  1.00 19.12 ? 49  GLU A N   1 
ATOM   367  C  CA  . GLU A 1 49  ? 54.625 33.376 -4.825  1.00 22.97 ? 49  GLU A CA  1 
ATOM   368  C  C   . GLU A 1 49  ? 54.220 34.835 -5.033  1.00 20.89 ? 49  GLU A C   1 
ATOM   369  O  O   . GLU A 1 49  ? 55.006 35.642 -5.542  1.00 20.84 ? 49  GLU A O   1 
ATOM   370  C  CB  . GLU A 1 49  ? 54.175 32.548 -6.031  1.00 27.14 ? 49  GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 49  ? 54.527 33.175 -7.365  1.00 32.18 ? 49  GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 49  ? 54.257 32.261 -8.543  1.00 37.42 ? 49  GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 49  ? 53.579 31.219 -8.374  1.00 38.02 ? 49  GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 49  ? 54.731 32.599 -9.651  1.00 40.76 ? 49  GLU A OE2 1 
ATOM   375  N  N   . PHE A 1 50  ? 52.992 35.163 -4.675  1.00 19.06 ? 50  PHE A N   1 
ATOM   376  C  CA  . PHE A 1 50  ? 52.516 36.500 -4.910  1.00 19.95 ? 50  PHE A CA  1 
ATOM   377  C  C   . PHE A 1 50  ? 52.433 37.382 -3.697  1.00 19.45 ? 50  PHE A C   1 
ATOM   378  O  O   . PHE A 1 50  ? 52.088 36.926 -2.621  1.00 20.71 ? 50  PHE A O   1 
ATOM   379  C  CB  . PHE A 1 50  ? 51.163 36.424 -5.614  1.00 19.44 ? 50  PHE A CB  1 
ATOM   380  C  CG  . PHE A 1 50  ? 51.219 35.667 -6.890  1.00 20.10 ? 50  PHE A CG  1 
ATOM   381  C  CD1 . PHE A 1 50  ? 52.124 36.031 -7.874  1.00 19.47 ? 50  PHE A CD1 1 
ATOM   382  C  CD2 . PHE A 1 50  ? 50.424 34.553 -7.088  1.00 22.70 ? 50  PHE A CD2 1 
ATOM   383  C  CE1 . PHE A 1 50  ? 52.249 35.292 -9.030  1.00 22.96 ? 50  PHE A CE1 1 
ATOM   384  C  CE2 . PHE A 1 50  ? 50.543 33.800 -8.248  1.00 22.09 ? 50  PHE A CE2 1 
ATOM   385  C  CZ  . PHE A 1 50  ? 51.461 34.177 -9.221  1.00 22.89 ? 50  PHE A CZ  1 
ATOM   386  N  N   . GLY A 1 51  ? 52.754 38.655 -3.888  1.00 18.71 ? 51  GLY A N   1 
ATOM   387  C  CA  . GLY A 1 51  ? 52.675 39.622 -2.813  1.00 19.41 ? 51  GLY A CA  1 
ATOM   388  C  C   . GLY A 1 51  ? 51.331 40.290 -2.942  1.00 21.62 ? 51  GLY A C   1 
ATOM   389  O  O   . GLY A 1 51  ? 51.207 41.513 -2.886  1.00 22.94 ? 51  GLY A O   1 
ATOM   390  N  N   . ASP A 1 52  ? 50.319 39.458 -3.135  1.00 22.54 ? 52  ASP A N   1 
ATOM   391  C  CA  . ASP A 1 52  ? 48.961 39.911 -3.323  1.00 24.28 ? 52  ASP A CA  1 
ATOM   392  C  C   . ASP A 1 52  ? 48.141 39.535 -2.108  1.00 26.64 ? 52  ASP A C   1 
ATOM   393  O  O   . ASP A 1 52  ? 47.898 38.362 -1.855  1.00 27.26 ? 52  ASP A O   1 
ATOM   394  C  CB  . ASP A 1 52  ? 48.390 39.218 -4.550  1.00 25.40 ? 52  ASP A CB  1 
ATOM   395  C  CG  . ASP A 1 52  ? 47.012 39.711 -4.916  1.00 27.70 ? 52  ASP A CG  1 
ATOM   396  O  OD1 . ASP A 1 52  ? 46.299 40.258 -4.057  1.00 28.76 ? 52  ASP A OD1 1 
ATOM   397  O  OD2 . ASP A 1 52  ? 46.627 39.539 -6.087  1.00 33.28 ? 52  ASP A OD2 1 
ATOM   398  N  N   . ASN A 1 53  ? 47.692 40.530 -1.364  1.00 28.66 ? 53  ASN A N   1 
ATOM   399  C  CA  . ASN A 1 53  ? 46.885 40.263 -0.188  1.00 32.18 ? 53  ASN A CA  1 
ATOM   400  C  C   . ASN A 1 53  ? 45.548 40.963 -0.312  1.00 30.71 ? 53  ASN A C   1 
ATOM   401  O  O   . ASN A 1 53  ? 44.976 41.432 0.677   1.00 30.15 ? 53  ASN A O   1 
ATOM   402  C  CB  . ASN A 1 53  ? 47.621 40.698 1.085   1.00 37.66 ? 53  ASN A CB  1 
ATOM   403  C  CG  . ASN A 1 53  ? 48.855 39.835 1.375   1.00 44.53 ? 53  ASN A CG  1 
ATOM   404  O  OD1 . ASN A 1 53  ? 49.745 40.241 2.138   1.00 46.61 ? 53  ASN A OD1 1 
ATOM   405  N  ND2 . ASN A 1 53  ? 48.914 38.639 0.772   1.00 43.53 ? 53  ASN A ND2 1 
ATOM   406  N  N   . THR A 1 54  ? 45.056 41.055 -1.542  1.00 29.63 ? 54  THR A N   1 
ATOM   407  C  CA  . THR A 1 54  ? 43.772 41.702 -1.758  1.00 31.17 ? 54  THR A CA  1 
ATOM   408  C  C   . THR A 1 54  ? 42.648 40.857 -1.125  1.00 33.45 ? 54  THR A C   1 
ATOM   409  O  O   . THR A 1 54  ? 41.653 41.394 -0.626  1.00 34.80 ? 54  THR A O   1 
ATOM   410  C  CB  . THR A 1 54  ? 43.515 41.997 -3.251  1.00 28.25 ? 54  THR A CB  1 
ATOM   411  O  OG1 . THR A 1 54  ? 43.606 40.791 -4.017  1.00 26.97 ? 54  THR A OG1 1 
ATOM   412  C  CG2 . THR A 1 54  ? 44.514 43.017 -3.765  1.00 25.64 ? 54  THR A CG2 1 
ATOM   413  N  N   . ALA A 1 55  ? 42.852 39.541 -1.092  1.00 33.66 ? 55  ALA A N   1 
ATOM   414  C  CA  . ALA A 1 55  ? 41.899 38.623 -0.493  1.00 34.00 ? 55  ALA A CA  1 
ATOM   415  C  C   . ALA A 1 55  ? 42.592 37.976 0.692   1.00 35.54 ? 55  ALA A C   1 
ATOM   416  O  O   . ALA A 1 55  ? 42.593 36.759 0.816   1.00 39.33 ? 55  ALA A O   1 
ATOM   417  C  CB  . ALA A 1 55  ? 41.483 37.558 -1.503  1.00 34.18 ? 55  ALA A CB  1 
ATOM   418  N  N   . GLY A 1 56  ? 43.209 38.780 1.553   1.00 35.24 ? 56  GLY A N   1 
ATOM   419  C  CA  . GLY A 1 56  ? 43.908 38.223 2.699   1.00 34.48 ? 56  GLY A CA  1 
ATOM   420  C  C   . GLY A 1 56  ? 45.095 37.382 2.259   1.00 34.18 ? 56  GLY A C   1 
ATOM   421  O  O   . GLY A 1 56  ? 45.745 37.668 1.245   1.00 34.84 ? 56  GLY A O   1 
ATOM   422  N  N   . CYS A 1 57  ? 45.353 36.305 2.987   1.00 34.00 ? 57  CYS A N   1 
ATOM   423  C  CA  . CYS A 1 57  ? 46.478 35.435 2.651   1.00 32.75 ? 57  CYS A CA  1 
ATOM   424  C  C   . CYS A 1 57  ? 46.145 34.514 1.492   1.00 33.21 ? 57  CYS A C   1 
ATOM   425  O  O   . CYS A 1 57  ? 47.037 33.927 0.871   1.00 31.87 ? 57  CYS A O   1 
ATOM   426  C  CB  . CYS A 1 57  ? 46.893 34.636 3.877   1.00 30.21 ? 57  CYS A CB  1 
ATOM   427  S  SG  . CYS A 1 57  ? 47.249 35.728 5.285   1.00 26.97 ? 57  CYS A SG  1 
ATOM   428  N  N   . THR A 1 58  ? 44.850 34.449 1.190   1.00 34.30 ? 58  THR A N   1 
ATOM   429  C  CA  . THR A 1 58  ? 44.273 33.633 0.123   1.00 35.76 ? 58  THR A CA  1 
ATOM   430  C  C   . THR A 1 58  ? 44.862 33.938 -1.258  1.00 33.64 ? 58  THR A C   1 
ATOM   431  O  O   . THR A 1 58  ? 45.073 33.034 -2.072  1.00 33.13 ? 58  THR A O   1 
ATOM   432  C  CB  . THR A 1 58  ? 42.737 33.870 0.055   1.00 37.22 ? 58  THR A CB  1 
ATOM   433  O  OG1 . THR A 1 58  ? 42.140 33.543 1.314   1.00 42.11 ? 58  THR A OG1 1 
ATOM   434  C  CG2 . THR A 1 58  ? 42.106 33.054 -1.038  1.00 41.43 ? 58  THR A CG2 1 
ATOM   435  N  N   . SER A 1 59  ? 45.141 35.211 -1.509  1.00 30.27 ? 59  SER A N   1 
ATOM   436  C  CA  . SER A 1 59  ? 45.669 35.627 -2.790  1.00 27.31 ? 59  SER A CA  1 
ATOM   437  C  C   . SER A 1 59  ? 47.191 35.547 -2.948  1.00 26.21 ? 59  SER A C   1 
ATOM   438  O  O   . SER A 1 59  ? 47.719 35.954 -3.974  1.00 28.12 ? 59  SER A O   1 
ATOM   439  C  CB  . SER A 1 59  ? 45.153 37.026 -3.102  1.00 27.12 ? 59  SER A CB  1 
ATOM   440  O  OG  . SER A 1 59  ? 44.801 37.696 -1.904  1.00 27.98 ? 59  SER A OG  1 
ATOM   441  N  N   . ALA A 1 60  ? 47.892 34.995 -1.957  1.00 26.51 ? 60  ALA A N   1 
ATOM   442  C  CA  . ALA A 1 60  ? 49.352 34.865 -2.019  1.00 22.89 ? 60  ALA A CA  1 
ATOM   443  C  C   . ALA A 1 60  ? 49.800 33.791 -3.009  1.00 23.59 ? 60  ALA A C   1 
ATOM   444  O  O   . ALA A 1 60  ? 50.968 33.740 -3.384  1.00 25.25 ? 60  ALA A O   1 
ATOM   445  C  CB  . ALA A 1 60  ? 49.911 34.578 -0.640  1.00 23.23 ? 60  ALA A CB  1 
ATOM   446  N  N   . GLY A 1 61  ? 48.872 32.942 -3.443  1.00 24.19 ? 61  GLY A N   1 
ATOM   447  C  CA  . GLY A 1 61  ? 49.199 31.892 -4.392  1.00 22.58 ? 61  GLY A CA  1 
ATOM   448  C  C   . GLY A 1 61  ? 49.809 30.691 -3.694  1.00 24.12 ? 61  GLY A C   1 
ATOM   449  O  O   . GLY A 1 61  ? 49.667 30.563 -2.483  1.00 26.29 ? 61  GLY A O   1 
ATOM   450  N  N   . PRO A 1 62  ? 50.465 29.778 -4.425  1.00 23.57 ? 62  PRO A N   1 
ATOM   451  C  CA  . PRO A 1 62  ? 51.097 28.579 -3.864  1.00 24.51 ? 62  PRO A CA  1 
ATOM   452  C  C   . PRO A 1 62  ? 52.524 28.906 -3.394  1.00 23.78 ? 62  PRO A C   1 
ATOM   453  O  O   . PRO A 1 62  ? 52.947 30.057 -3.494  1.00 24.89 ? 62  PRO A O   1 
ATOM   454  C  CB  . PRO A 1 62  ? 51.101 27.636 -5.061  1.00 24.14 ? 62  PRO A CB  1 
ATOM   455  C  CG  . PRO A 1 62  ? 51.440 28.572 -6.169  1.00 24.92 ? 62  PRO A CG  1 
ATOM   456  C  CD  . PRO A 1 62  ? 50.567 29.779 -5.895  1.00 24.12 ? 62  PRO A CD  1 
ATOM   457  N  N   . HIS A 1 63  ? 53.267 27.925 -2.885  1.00 21.96 ? 63  HIS A N   1 
ATOM   458  C  CA  . HIS A 1 63  ? 54.646 28.191 -2.437  1.00 22.37 ? 63  HIS A CA  1 
ATOM   459  C  C   . HIS A 1 63  ? 55.469 28.682 -3.591  1.00 21.83 ? 63  HIS A C   1 
ATOM   460  O  O   . HIS A 1 63  ? 55.264 28.246 -4.725  1.00 23.38 ? 63  HIS A O   1 
ATOM   461  C  CB  . HIS A 1 63  ? 55.323 26.953 -1.852  1.00 21.49 ? 63  HIS A CB  1 
ATOM   462  C  CG  . HIS A 1 63  ? 54.623 26.398 -0.653  1.00 23.92 ? 63  HIS A CG  1 
ATOM   463  N  ND1 . HIS A 1 63  ? 54.947 25.182 -0.084  1.00 20.78 ? 63  HIS A ND1 1 
ATOM   464  C  CD2 . HIS A 1 63  ? 53.584 26.888 0.064   1.00 24.44 ? 63  HIS A CD2 1 
ATOM   465  C  CE1 . HIS A 1 63  ? 54.131 24.947 0.927   1.00 23.82 ? 63  HIS A CE1 1 
ATOM   466  N  NE2 . HIS A 1 63  ? 53.298 25.969 1.041   1.00 28.65 ? 63  HIS A NE2 1 
ATOM   467  N  N   . PHE A 1 64  ? 56.388 29.599 -3.306  1.00 21.44 ? 64  PHE A N   1 
ATOM   468  C  CA  . PHE A 1 64  ? 57.251 30.146 -4.338  1.00 20.52 ? 64  PHE A CA  1 
ATOM   469  C  C   . PHE A 1 64  ? 58.093 28.955 -4.812  1.00 20.51 ? 64  PHE A C   1 
ATOM   470  O  O   . PHE A 1 64  ? 58.856 28.359 -4.036  1.00 19.75 ? 64  PHE A O   1 
ATOM   471  C  CB  . PHE A 1 64  ? 58.084 31.292 -3.763  1.00 18.07 ? 64  PHE A CB  1 
ATOM   472  C  CG  . PHE A 1 64  ? 58.958 31.966 -4.764  1.00 18.25 ? 64  PHE A CG  1 
ATOM   473  C  CD1 . PHE A 1 64  ? 58.514 32.179 -6.066  1.00 17.61 ? 64  PHE A CD1 1 
ATOM   474  C  CD2 . PHE A 1 64  ? 60.245 32.360 -4.416  1.00 19.91 ? 64  PHE A CD2 1 
ATOM   475  C  CE1 . PHE A 1 64  ? 59.329 32.766 -7.008  1.00 16.75 ? 64  PHE A CE1 1 
ATOM   476  C  CE2 . PHE A 1 64  ? 61.078 32.953 -5.348  1.00 21.42 ? 64  PHE A CE2 1 
ATOM   477  C  CZ  . PHE A 1 64  ? 60.621 33.158 -6.654  1.00 19.43 ? 64  PHE A CZ  1 
ATOM   478  N  N   . ASN A 1 65  ? 57.950 28.620 -6.093  1.00 20.92 ? 65  ASN A N   1 
ATOM   479  C  CA  . ASN A 1 65  ? 58.604 27.443 -6.663  1.00 23.46 ? 65  ASN A CA  1 
ATOM   480  C  C   . ASN A 1 65  ? 59.100 27.677 -8.090  1.00 23.27 ? 65  ASN A C   1 
ATOM   481  O  O   . ASN A 1 65  ? 58.723 26.954 -9.019  1.00 23.56 ? 65  ASN A O   1 
ATOM   482  C  CB  . ASN A 1 65  ? 57.575 26.301 -6.626  1.00 22.06 ? 65  ASN A CB  1 
ATOM   483  C  CG  . ASN A 1 65  ? 58.139 24.964 -7.045  1.00 23.61 ? 65  ASN A CG  1 
ATOM   484  O  OD1 . ASN A 1 65  ? 59.357 24.749 -7.059  1.00 23.93 ? 65  ASN A OD1 1 
ATOM   485  N  ND2 . ASN A 1 65  ? 57.241 24.034 -7.365  1.00 23.44 ? 65  ASN A ND2 1 
ATOM   486  N  N   . PRO A 1 66  ? 59.982 28.669 -8.282  1.00 22.39 ? 66  PRO A N   1 
ATOM   487  C  CA  . PRO A 1 66  ? 60.474 28.926 -9.631  1.00 23.46 ? 66  PRO A CA  1 
ATOM   488  C  C   . PRO A 1 66  ? 61.154 27.720 -10.318 1.00 26.73 ? 66  PRO A C   1 
ATOM   489  O  O   . PRO A 1 66  ? 61.220 27.659 -11.554 1.00 29.10 ? 66  PRO A O   1 
ATOM   490  C  CB  . PRO A 1 66  ? 61.444 30.096 -9.413  1.00 20.20 ? 66  PRO A CB  1 
ATOM   491  C  CG  . PRO A 1 66  ? 61.927 29.884 -8.057  1.00 17.28 ? 66  PRO A CG  1 
ATOM   492  C  CD  . PRO A 1 66  ? 60.679 29.528 -7.313  1.00 19.48 ? 66  PRO A CD  1 
ATOM   493  N  N   . LEU A 1 67  ? 61.587 26.732 -9.539  1.00 28.07 ? 67  LEU A N   1 
ATOM   494  C  CA  . LEU A 1 67  ? 62.273 25.574 -10.113 1.00 27.35 ? 67  LEU A CA  1 
ATOM   495  C  C   . LEU A 1 67  ? 61.415 24.342 -10.404 1.00 25.75 ? 67  LEU A C   1 
ATOM   496  O  O   . LEU A 1 67  ? 61.924 23.335 -10.892 1.00 25.99 ? 67  LEU A O   1 
ATOM   497  C  CB  . LEU A 1 67  ? 63.491 25.218 -9.262  1.00 28.67 ? 67  LEU A CB  1 
ATOM   498  C  CG  . LEU A 1 67  ? 64.500 26.368 -9.090  1.00 29.87 ? 67  LEU A CG  1 
ATOM   499  C  CD1 . LEU A 1 67  ? 65.651 25.927 -8.201  1.00 29.95 ? 67  LEU A CD1 1 
ATOM   500  C  CD2 . LEU A 1 67  ? 65.012 26.836 -10.455 1.00 28.43 ? 67  LEU A CD2 1 
ATOM   501  N  N   . SER A 1 68  ? 60.110 24.462 -10.166 1.00 25.77 ? 68  SER A N   1 
ATOM   502  C  CA  . SER A 1 68  ? 59.139 23.394 -10.413 1.00 25.87 ? 68  SER A CA  1 
ATOM   503  C  C   . SER A 1 68  ? 59.495 22.109 -9.686  1.00 26.50 ? 68  SER A C   1 
ATOM   504  O  O   . SER A 1 68  ? 59.332 20.997 -10.200 1.00 26.17 ? 68  SER A O   1 
ATOM   505  C  CB  . SER A 1 68  ? 58.995 23.145 -11.912 1.00 24.35 ? 68  SER A CB  1 
ATOM   506  O  OG  . SER A 1 68  ? 58.611 24.336 -12.580 1.00 24.60 ? 68  SER A OG  1 
ATOM   507  N  N   . ARG A 1 69  ? 59.955 22.286 -8.460  1.00 26.53 ? 69  ARG A N   1 
ATOM   508  C  CA  . ARG A 1 69  ? 60.355 21.182 -7.617  1.00 27.38 ? 69  ARG A CA  1 
ATOM   509  C  C   . ARG A 1 69  ? 59.165 20.784 -6.747  1.00 25.36 ? 69  ARG A C   1 
ATOM   510  O  O   . ARG A 1 69  ? 58.125 21.442 -6.759  1.00 24.69 ? 69  ARG A O   1 
ATOM   511  C  CB  . ARG A 1 69  ? 61.547 21.631 -6.768  1.00 31.13 ? 69  ARG A CB  1 
ATOM   512  C  CG  . ARG A 1 69  ? 62.711 20.686 -6.767  1.00 39.41 ? 69  ARG A CG  1 
ATOM   513  C  CD  . ARG A 1 69  ? 64.054 21.390 -6.985  1.00 46.23 ? 69  ARG A CD  1 
ATOM   514  N  NE  . ARG A 1 69  ? 64.288 21.729 -8.390  1.00 51.30 ? 69  ARG A NE  1 
ATOM   515  C  CZ  . ARG A 1 69  ? 64.495 20.844 -9.370  1.00 54.97 ? 69  ARG A CZ  1 
ATOM   516  N  NH1 . ARG A 1 69  ? 64.505 19.535 -9.123  1.00 57.86 ? 69  ARG A NH1 1 
ATOM   517  N  NH2 . ARG A 1 69  ? 64.673 21.269 -10.616 1.00 55.00 ? 69  ARG A NH2 1 
ATOM   518  N  N   . LYS A 1 70  ? 59.288 19.661 -6.048  1.00 26.75 ? 70  LYS A N   1 
ATOM   519  C  CA  . LYS A 1 70  ? 58.220 19.205 -5.164  1.00 27.96 ? 70  LYS A CA  1 
ATOM   520  C  C   . LYS A 1 70  ? 58.477 19.750 -3.776  1.00 25.90 ? 70  LYS A C   1 
ATOM   521  O  O   . LYS A 1 70  ? 59.570 20.213 -3.471  1.00 25.23 ? 70  LYS A O   1 
ATOM   522  C  CB  . LYS A 1 70  ? 58.127 17.680 -5.141  1.00 30.44 ? 70  LYS A CB  1 
ATOM   523  C  CG  . LYS A 1 70  ? 57.605 17.132 -6.443  1.00 35.79 ? 70  LYS A CG  1 
ATOM   524  C  CD  . LYS A 1 70  ? 57.496 15.622 -6.449  1.00 43.14 ? 70  LYS A CD  1 
ATOM   525  C  CE  . LYS A 1 70  ? 56.511 15.140 -7.543  1.00 46.86 ? 70  LYS A CE  1 
ATOM   526  N  NZ  . LYS A 1 70  ? 55.070 15.542 -7.293  1.00 47.74 ? 70  LYS A NZ  1 
ATOM   527  N  N   . HIS A 1 71  ? 57.454 19.728 -2.950  1.00 24.90 ? 71  HIS A N   1 
ATOM   528  C  CA  . HIS A 1 71  ? 57.573 20.243 -1.605  1.00 26.10 ? 71  HIS A CA  1 
ATOM   529  C  C   . HIS A 1 71  ? 58.532 19.483 -0.698  1.00 27.64 ? 71  HIS A C   1 
ATOM   530  O  O   . HIS A 1 71  ? 58.535 18.249 -0.663  1.00 27.54 ? 71  HIS A O   1 
ATOM   531  C  CB  . HIS A 1 71  ? 56.200 20.309 -0.956  1.00 25.22 ? 71  HIS A CB  1 
ATOM   532  C  CG  . HIS A 1 71  ? 56.236 20.806 0.448   1.00 26.81 ? 71  HIS A CG  1 
ATOM   533  N  ND1 . HIS A 1 71  ? 56.231 22.150 0.761   1.00 29.02 ? 71  HIS A ND1 1 
ATOM   534  C  CD2 . HIS A 1 71  ? 56.345 20.142 1.621   1.00 27.36 ? 71  HIS A CD2 1 
ATOM   535  C  CE1 . HIS A 1 71  ? 56.344 22.287 2.071   1.00 28.82 ? 71  HIS A CE1 1 
ATOM   536  N  NE2 . HIS A 1 71  ? 56.418 21.086 2.613   1.00 28.63 ? 71  HIS A NE2 1 
ATOM   537  N  N   . GLY A 1 72  ? 59.288 20.240 0.096   1.00 26.83 ? 72  GLY A N   1 
ATOM   538  C  CA  . GLY A 1 72  ? 60.232 19.641 1.011   1.00 26.68 ? 72  GLY A CA  1 
ATOM   539  C  C   . GLY A 1 72  ? 60.520 20.515 2.210   1.00 26.79 ? 72  GLY A C   1 
ATOM   540  O  O   . GLY A 1 72  ? 59.744 21.415 2.546   1.00 26.85 ? 72  GLY A O   1 
ATOM   541  N  N   . GLY A 1 73  ? 61.606 20.202 2.901   1.00 25.79 ? 73  GLY A N   1 
ATOM   542  C  CA  . GLY A 1 73  ? 61.996 20.976 4.060   1.00 25.63 ? 73  GLY A CA  1 
ATOM   543  C  C   . GLY A 1 73  ? 63.188 21.782 3.618   1.00 26.65 ? 73  GLY A C   1 
ATOM   544  O  O   . GLY A 1 73  ? 63.736 21.529 2.543   1.00 26.03 ? 73  GLY A O   1 
ATOM   545  N  N   . PRO A 1 74  ? 63.660 22.713 4.446   1.00 28.06 ? 74  PRO A N   1 
ATOM   546  C  CA  . PRO A 1 74  ? 64.809 23.590 4.180   1.00 30.36 ? 74  PRO A CA  1 
ATOM   547  C  C   . PRO A 1 74  ? 66.128 22.881 3.879   1.00 31.99 ? 74  PRO A C   1 
ATOM   548  O  O   . PRO A 1 74  ? 66.978 23.422 3.167   1.00 32.66 ? 74  PRO A O   1 
ATOM   549  C  CB  . PRO A 1 74  ? 64.941 24.393 5.476   1.00 29.44 ? 74  PRO A CB  1 
ATOM   550  C  CG  . PRO A 1 74  ? 63.588 24.374 6.038   1.00 30.53 ? 74  PRO A CG  1 
ATOM   551  C  CD  . PRO A 1 74  ? 63.084 22.990 5.772   1.00 27.53 ? 74  PRO A CD  1 
ATOM   552  N  N   . LYS A 1 75  ? 66.325 21.708 4.472   1.00 34.89 ? 75  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 75  ? 67.563 20.964 4.279   1.00 39.12 ? 75  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 75  ? 67.562 20.037 3.068   1.00 40.98 ? 75  LYS A C   1 
ATOM   555  O  O   . LYS A 1 75  ? 68.610 19.504 2.699   1.00 43.14 ? 75  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 75  ? 67.894 20.146 5.524   1.00 42.63 ? 75  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 75  ? 67.730 20.885 6.845   1.00 47.86 ? 75  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 75  ? 68.812 20.472 7.831   1.00 52.42 ? 75  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 75  ? 68.902 18.959 7.963   1.00 55.45 ? 75  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 75  ? 70.306 18.502 8.233   1.00 58.24 ? 75  LYS A NZ  1 
ATOM   561  N  N   . ASP A 1 76  ? 66.386 19.815 2.484   1.00 42.34 ? 76  ASP A N   1 
ATOM   562  C  CA  . ASP A 1 76  ? 66.236 18.952 1.315   1.00 42.21 ? 76  ASP A CA  1 
ATOM   563  C  C   . ASP A 1 76  ? 66.727 19.588 0.018   1.00 42.42 ? 76  ASP A C   1 
ATOM   564  O  O   . ASP A 1 76  ? 66.673 20.806 -0.178  1.00 41.73 ? 76  ASP A O   1 
ATOM   565  C  CB  . ASP A 1 76  ? 64.767 18.548 1.130   1.00 42.91 ? 76  ASP A CB  1 
ATOM   566  C  CG  . ASP A 1 76  ? 64.253 17.669 2.249   1.00 45.25 ? 76  ASP A CG  1 
ATOM   567  O  OD1 . ASP A 1 76  ? 65.070 16.975 2.887   1.00 50.37 ? 76  ASP A OD1 1 
ATOM   568  O  OD2 . ASP A 1 76  ? 63.028 17.656 2.491   1.00 46.80 ? 76  ASP A OD2 1 
ATOM   569  N  N   . GLU A 1 77  ? 67.211 18.727 -0.865  1.00 44.04 ? 77  GLU A N   1 
ATOM   570  C  CA  . GLU A 1 77  ? 67.684 19.129 -2.181  1.00 45.60 ? 77  GLU A CA  1 
ATOM   571  C  C   . GLU A 1 77  ? 66.450 19.514 -2.985  1.00 41.98 ? 77  GLU A C   1 
ATOM   572  O  O   . GLU A 1 77  ? 66.416 20.545 -3.661  1.00 41.87 ? 77  GLU A O   1 
ATOM   573  C  CB  . GLU A 1 77  ? 68.390 17.940 -2.846  1.00 52.94 ? 77  GLU A CB  1 
ATOM   574  C  CG  . GLU A 1 77  ? 68.467 18.001 -4.376  1.00 64.10 ? 77  GLU A CG  1 
ATOM   575  C  CD  . GLU A 1 77  ? 69.196 19.241 -4.894  1.00 69.40 ? 77  GLU A CD  1 
ATOM   576  O  OE1 . GLU A 1 77  ? 70.423 19.361 -4.640  1.00 73.62 ? 77  GLU A OE1 1 
ATOM   577  O  OE2 . GLU A 1 77  ? 68.540 20.088 -5.558  1.00 71.74 ? 77  GLU A OE2 1 
ATOM   578  N  N   . GLU A 1 78  ? 65.445 18.652 -2.896  1.00 39.25 ? 78  GLU A N   1 
ATOM   579  C  CA  . GLU A 1 78  ? 64.179 18.826 -3.584  1.00 37.02 ? 78  GLU A CA  1 
ATOM   580  C  C   . GLU A 1 78  ? 63.236 19.562 -2.645  1.00 34.00 ? 78  GLU A C   1 
ATOM   581  O  O   . GLU A 1 78  ? 62.743 18.989 -1.672  1.00 34.28 ? 78  GLU A O   1 
ATOM   582  C  CB  . GLU A 1 78  ? 63.609 17.447 -3.952  1.00 38.48 ? 78  GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 78  ? 63.423 17.209 -5.458  1.00 42.67 ? 78  GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 78  ? 62.006 17.485 -5.925  1.00 43.85 ? 78  GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 78  ? 61.109 17.553 -5.063  1.00 49.52 ? 78  GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 78  ? 61.777 17.614 -7.144  1.00 45.33 ? 78  GLU A OE2 1 
ATOM   587  N  N   . ARG A 1 79  ? 63.046 20.850 -2.899  1.00 29.25 ? 79  ARG A N   1 
ATOM   588  C  CA  . ARG A 1 79  ? 62.168 21.679 -2.083  1.00 24.85 ? 79  ARG A CA  1 
ATOM   589  C  C   . ARG A 1 79  ? 61.820 22.885 -2.917  1.00 21.47 ? 79  ARG A C   1 
ATOM   590  O  O   . ARG A 1 79  ? 62.529 23.210 -3.873  1.00 22.48 ? 79  ARG A O   1 
ATOM   591  C  CB  . ARG A 1 79  ? 62.894 22.162 -0.810  1.00 22.49 ? 79  ARG A CB  1 
ATOM   592  C  CG  . ARG A 1 79  ? 64.237 22.825 -1.099  1.00 23.38 ? 79  ARG A CG  1 
ATOM   593  C  CD  . ARG A 1 79  ? 64.794 23.605 0.084   1.00 25.46 ? 79  ARG A CD  1 
ATOM   594  N  NE  . ARG A 1 79  ? 64.350 25.001 0.113   1.00 25.49 ? 79  ARG A NE  1 
ATOM   595  C  CZ  . ARG A 1 79  ? 64.847 25.915 0.940   1.00 24.96 ? 79  ARG A CZ  1 
ATOM   596  N  NH1 . ARG A 1 79  ? 65.800 25.566 1.791   1.00 22.84 ? 79  ARG A NH1 1 
ATOM   597  N  NH2 . ARG A 1 79  ? 64.390 27.164 0.936   1.00 21.07 ? 79  ARG A NH2 1 
ATOM   598  N  N   . HIS A 1 80  ? 60.691 23.502 -2.607  1.00 20.27 ? 80  HIS A N   1 
ATOM   599  C  CA  . HIS A 1 80  ? 60.303 24.729 -3.296  1.00 21.11 ? 80  HIS A CA  1 
ATOM   600  C  C   . HIS A 1 80  ? 61.264 25.789 -2.731  1.00 21.73 ? 80  HIS A C   1 
ATOM   601  O  O   . HIS A 1 80  ? 61.794 25.607 -1.635  1.00 22.18 ? 80  HIS A O   1 
ATOM   602  C  CB  . HIS A 1 80  ? 58.888 25.139 -2.926  1.00 17.29 ? 80  HIS A CB  1 
ATOM   603  C  CG  . HIS A 1 80  ? 57.847 24.125 -3.274  1.00 18.04 ? 80  HIS A CG  1 
ATOM   604  N  ND1 . HIS A 1 80  ? 56.663 24.007 -2.577  1.00 17.15 ? 80  HIS A ND1 1 
ATOM   605  C  CD2 . HIS A 1 80  ? 57.777 23.237 -4.291  1.00 17.90 ? 80  HIS A CD2 1 
ATOM   606  C  CE1 . HIS A 1 80  ? 55.898 23.103 -3.166  1.00 16.31 ? 80  HIS A CE1 1 
ATOM   607  N  NE2 . HIS A 1 80  ? 56.553 22.622 -4.205  1.00 19.99 ? 80  HIS A NE2 1 
ATOM   608  N  N   . VAL A 1 81  ? 61.514 26.866 -3.472  1.00 23.03 ? 81  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 81  ? 62.395 27.926 -2.983  1.00 22.57 ? 81  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 81  ? 61.807 28.491 -1.676  1.00 22.46 ? 81  VAL A C   1 
ATOM   611  O  O   . VAL A 1 81  ? 62.536 28.685 -0.704  1.00 22.08 ? 81  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 81  ? 62.581 29.046 -4.064  1.00 23.87 ? 81  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 81  ? 63.229 30.314 -3.477  1.00 24.33 ? 81  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 81  ? 63.449 28.517 -5.193  1.00 22.72 ? 81  VAL A CG2 1 
ATOM   615  N  N   . GLY A 1 82  ? 60.479 28.629 -1.627  1.00 22.41 ? 82  GLY A N   1 
ATOM   616  C  CA  . GLY A 1 82  ? 59.807 29.164 -0.456  1.00 20.63 ? 82  GLY A CA  1 
ATOM   617  C  C   . GLY A 1 82  ? 59.604 28.240 0.730   1.00 22.76 ? 82  GLY A C   1 
ATOM   618  O  O   . GLY A 1 82  ? 58.911 28.621 1.677   1.00 23.46 ? 82  GLY A O   1 
ATOM   619  N  N   . ASP A 1 83  ? 60.197 27.046 0.721   1.00 22.88 ? 83  ASP A N   1 
ATOM   620  C  CA  . ASP A 1 83  ? 60.021 26.115 1.841   1.00 23.85 ? 83  ASP A CA  1 
ATOM   621  C  C   . ASP A 1 83  ? 60.984 26.359 3.001   1.00 24.70 ? 83  ASP A C   1 
ATOM   622  O  O   . ASP A 1 83  ? 62.130 25.897 2.984   1.00 25.94 ? 83  ASP A O   1 
ATOM   623  C  CB  . ASP A 1 83  ? 60.146 24.669 1.367   1.00 23.81 ? 83  ASP A CB  1 
ATOM   624  C  CG  . ASP A 1 83  ? 58.999 24.241 0.484   1.00 23.85 ? 83  ASP A CG  1 
ATOM   625  O  OD1 . ASP A 1 83  ? 57.940 24.912 0.399   1.00 24.36 ? 83  ASP A OD1 1 
ATOM   626  O  OD2 . ASP A 1 83  ? 59.120 23.182 -0.149  1.00 27.69 ? 83  ASP A OD2 1 
ATOM   627  N  N   . LEU A 1 84  ? 60.504 27.068 4.022   1.00 25.13 ? 84  LEU A N   1 
ATOM   628  C  CA  . LEU A 1 84  ? 61.315 27.378 5.202   1.00 26.40 ? 84  LEU A CA  1 
ATOM   629  C  C   . LEU A 1 84  ? 61.016 26.489 6.426   1.00 26.70 ? 84  LEU A C   1 
ATOM   630  O  O   . LEU A 1 84  ? 61.434 26.795 7.545   1.00 28.41 ? 84  LEU A O   1 
ATOM   631  C  CB  . LEU A 1 84  ? 61.221 28.876 5.560   1.00 22.66 ? 84  LEU A CB  1 
ATOM   632  C  CG  . LEU A 1 84  ? 61.808 29.827 4.519   1.00 20.74 ? 84  LEU A CG  1 
ATOM   633  C  CD1 . LEU A 1 84  ? 61.634 31.249 4.977   1.00 21.30 ? 84  LEU A CD1 1 
ATOM   634  C  CD2 . LEU A 1 84  ? 63.264 29.513 4.282   1.00 20.82 ? 84  LEU A CD2 1 
ATOM   635  N  N   . GLY A 1 85  ? 60.280 25.400 6.203   1.00 26.74 ? 85  GLY A N   1 
ATOM   636  C  CA  . GLY A 1 85  ? 59.993 24.453 7.260   1.00 25.27 ? 85  GLY A CA  1 
ATOM   637  C  C   . GLY A 1 85  ? 58.973 24.838 8.300   1.00 25.41 ? 85  GLY A C   1 
ATOM   638  O  O   . GLY A 1 85  ? 57.882 25.310 7.973   1.00 25.69 ? 85  GLY A O   1 
ATOM   639  N  N   . ASN A 1 86  ? 59.310 24.553 9.556   1.00 24.49 ? 86  ASN A N   1 
ATOM   640  C  CA  . ASN A 1 86  ? 58.426 24.831 10.670  1.00 24.95 ? 86  ASN A CA  1 
ATOM   641  C  C   . ASN A 1 86  ? 58.966 25.837 11.653  1.00 24.44 ? 86  ASN A C   1 
ATOM   642  O  O   . ASN A 1 86  ? 60.158 25.922 11.921  1.00 25.55 ? 86  ASN A O   1 
ATOM   643  C  CB  . ASN A 1 86  ? 58.089 23.557 11.439  1.00 25.65 ? 86  ASN A CB  1 
ATOM   644  C  CG  . ASN A 1 86  ? 57.140 22.662 10.703  1.00 22.78 ? 86  ASN A CG  1 
ATOM   645  O  OD1 . ASN A 1 86  ? 55.961 22.976 10.550  1.00 26.08 ? 86  ASN A OD1 1 
ATOM   646  N  ND2 . ASN A 1 86  ? 57.632 21.512 10.287  1.00 23.08 ? 86  ASN A ND2 1 
ATOM   647  N  N   . VAL A 1 87  ? 58.038 26.540 12.251  1.00 25.85 ? 87  VAL A N   1 
ATOM   648  C  CA  . VAL A 1 87  ? 58.334 27.539 13.231  1.00 28.77 ? 87  VAL A CA  1 
ATOM   649  C  C   . VAL A 1 87  ? 57.721 26.939 14.508  1.00 31.04 ? 87  VAL A C   1 
ATOM   650  O  O   . VAL A 1 87  ? 56.626 26.386 14.458  1.00 30.98 ? 87  VAL A O   1 
ATOM   651  C  CB  . VAL A 1 87  ? 57.697 28.852 12.747  1.00 25.49 ? 87  VAL A CB  1 
ATOM   652  C  CG1 . VAL A 1 87  ? 56.711 29.389 13.721  1.00 25.65 ? 87  VAL A CG1 1 
ATOM   653  C  CG2 . VAL A 1 87  ? 58.774 29.818 12.402  1.00 25.27 ? 87  VAL A CG2 1 
ATOM   654  N  N   . THR A 1 88  ? 58.456 26.970 15.621  1.00 34.75 ? 88  THR A N   1 
ATOM   655  C  CA  . THR A 1 88  ? 57.979 26.389 16.891  1.00 36.38 ? 88  THR A CA  1 
ATOM   656  C  C   . THR A 1 88  ? 57.464 27.382 17.947  1.00 36.50 ? 88  THR A C   1 
ATOM   657  O  O   . THR A 1 88  ? 58.245 28.155 18.511  1.00 36.30 ? 88  THR A O   1 
ATOM   658  C  CB  . THR A 1 88  ? 59.086 25.548 17.549  1.00 37.55 ? 88  THR A CB  1 
ATOM   659  O  OG1 . THR A 1 88  ? 59.768 24.766 16.552  1.00 38.36 ? 88  THR A OG1 1 
ATOM   660  C  CG2 . THR A 1 88  ? 58.481 24.627 18.593  1.00 39.12 ? 88  THR A CG2 1 
ATOM   661  N  N   . ALA A 1 89  ? 56.156 27.361 18.202  1.00 37.39 ? 89  ALA A N   1 
ATOM   662  C  CA  . ALA A 1 89  ? 55.536 28.240 19.191  1.00 38.16 ? 89  ALA A CA  1 
ATOM   663  C  C   . ALA A 1 89  ? 55.563 27.537 20.538  1.00 41.21 ? 89  ALA A C   1 
ATOM   664  O  O   . ALA A 1 89  ? 55.296 26.336 20.617  1.00 40.25 ? 89  ALA A O   1 
ATOM   665  C  CB  . ALA A 1 89  ? 54.109 28.558 18.802  1.00 35.17 ? 89  ALA A CB  1 
ATOM   666  N  N   . ASP A 1 90  ? 55.913 28.274 21.591  1.00 44.88 ? 90  ASP A N   1 
ATOM   667  C  CA  . ASP A 1 90  ? 55.967 27.696 22.931  1.00 48.39 ? 90  ASP A CA  1 
ATOM   668  C  C   . ASP A 1 90  ? 54.617 27.752 23.636  1.00 50.55 ? 90  ASP A C   1 
ATOM   669  O  O   . ASP A 1 90  ? 53.625 28.138 23.023  1.00 51.24 ? 90  ASP A O   1 
ATOM   670  C  CB  . ASP A 1 90  ? 57.063 28.363 23.782  1.00 48.80 ? 90  ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 90  ? 56.785 29.833 24.110  1.00 50.42 ? 90  ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 90  ? 55.633 30.320 24.021  1.00 49.92 ? 90  ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 90  ? 57.760 30.510 24.491  1.00 52.06 ? 90  ASP A OD2 1 
ATOM   674  N  N   . LYS A 1 91  ? 54.601 27.402 24.926  1.00 55.04 ? 91  LYS A N   1 
ATOM   675  C  CA  . LYS A 1 91  ? 53.389 27.403 25.766  1.00 58.35 ? 91  LYS A CA  1 
ATOM   676  C  C   . LYS A 1 91  ? 52.648 28.747 25.809  1.00 58.47 ? 91  LYS A C   1 
ATOM   677  O  O   . LYS A 1 91  ? 51.429 28.785 25.972  1.00 58.05 ? 91  LYS A O   1 
ATOM   678  C  CB  . LYS A 1 91  ? 53.730 26.967 27.204  1.00 62.02 ? 91  LYS A CB  1 
ATOM   679  C  CG  . LYS A 1 91  ? 53.722 25.463 27.487  1.00 67.40 ? 91  LYS A CG  1 
ATOM   680  C  CD  . LYS A 1 91  ? 52.304 24.869 27.372  1.00 70.41 ? 91  LYS A CD  1 
ATOM   681  C  CE  . LYS A 1 91  ? 52.224 23.450 27.976  1.00 71.12 ? 91  LYS A CE  1 
ATOM   682  N  NZ  . LYS A 1 91  ? 53.368 22.583 27.514  1.00 70.46 ? 91  LYS A NZ  1 
ATOM   683  N  N   . ASP A 1 92  ? 53.397 29.844 25.716  1.00 58.40 ? 92  ASP A N   1 
ATOM   684  C  CA  . ASP A 1 92  ? 52.814 31.186 25.726  1.00 57.60 ? 92  ASP A CA  1 
ATOM   685  C  C   . ASP A 1 92  ? 52.379 31.611 24.321  1.00 54.80 ? 92  ASP A C   1 
ATOM   686  O  O   . ASP A 1 92  ? 51.877 32.721 24.119  1.00 54.73 ? 92  ASP A O   1 
ATOM   687  C  CB  . ASP A 1 92  ? 53.809 32.192 26.323  1.00 61.26 ? 92  ASP A CB  1 
ATOM   688  C  CG  . ASP A 1 92  ? 54.146 31.886 27.791  1.00 65.20 ? 92  ASP A CG  1 
ATOM   689  O  OD1 . ASP A 1 92  ? 53.263 31.363 28.518  1.00 65.37 ? 92  ASP A OD1 1 
ATOM   690  O  OD2 . ASP A 1 92  ? 55.292 32.160 28.222  1.00 67.19 ? 92  ASP A OD2 1 
ATOM   691  N  N   . GLY A 1 93  ? 52.548 30.707 23.360  1.00 51.18 ? 93  GLY A N   1 
ATOM   692  C  CA  . GLY A 1 93  ? 52.171 30.999 21.992  1.00 47.28 ? 93  GLY A CA  1 
ATOM   693  C  C   . GLY A 1 93  ? 53.127 31.924 21.265  1.00 44.31 ? 93  GLY A C   1 
ATOM   694  O  O   . GLY A 1 93  ? 52.732 32.614 20.336  1.00 44.64 ? 93  GLY A O   1 
ATOM   695  N  N   . VAL A 1 94  ? 54.393 31.917 21.654  1.00 41.78 ? 94  VAL A N   1 
ATOM   696  C  CA  . VAL A 1 94  ? 55.373 32.776 21.017  1.00 39.37 ? 94  VAL A CA  1 
ATOM   697  C  C   . VAL A 1 94  ? 56.373 31.930 20.253  1.00 38.03 ? 94  VAL A C   1 
ATOM   698  O  O   . VAL A 1 94  ? 56.985 31.021 20.819  1.00 37.75 ? 94  VAL A O   1 
ATOM   699  C  CB  . VAL A 1 94  ? 56.114 33.658 22.057  1.00 40.24 ? 94  VAL A CB  1 
ATOM   700  C  CG1 . VAL A 1 94  ? 57.157 34.535 21.369  1.00 41.15 ? 94  VAL A CG1 1 
ATOM   701  C  CG2 . VAL A 1 94  ? 55.118 34.530 22.817  1.00 39.94 ? 94  VAL A CG2 1 
ATOM   702  N  N   . ALA A 1 95  ? 56.521 32.220 18.963  1.00 36.61 ? 95  ALA A N   1 
ATOM   703  C  CA  . ALA A 1 95  ? 57.449 31.492 18.111  1.00 35.13 ? 95  ALA A CA  1 
ATOM   704  C  C   . ALA A 1 95  ? 58.611 32.368 17.699  1.00 34.79 ? 95  ALA A C   1 
ATOM   705  O  O   . ALA A 1 95  ? 58.437 33.315 16.934  1.00 35.17 ? 95  ALA A O   1 
ATOM   706  C  CB  . ALA A 1 95  ? 56.732 30.980 16.879  1.00 35.07 ? 95  ALA A CB  1 
ATOM   707  N  N   . ASP A 1 96  ? 59.781 32.099 18.254  1.00 35.51 ? 96  ASP A N   1 
ATOM   708  C  CA  . ASP A 1 96  ? 60.970 32.858 17.895  1.00 38.28 ? 96  ASP A CA  1 
ATOM   709  C  C   . ASP A 1 96  ? 61.574 32.194 16.680  1.00 36.47 ? 96  ASP A C   1 
ATOM   710  O  O   . ASP A 1 96  ? 61.703 30.972 16.637  1.00 38.53 ? 96  ASP A O   1 
ATOM   711  C  CB  . ASP A 1 96  ? 61.978 32.918 19.034  1.00 43.75 ? 96  ASP A CB  1 
ATOM   712  C  CG  . ASP A 1 96  ? 61.883 34.210 19.808  1.00 50.30 ? 96  ASP A CG  1 
ATOM   713  O  OD1 . ASP A 1 96  ? 61.011 34.305 20.704  1.00 53.50 ? 96  ASP A OD1 1 
ATOM   714  O  OD2 . ASP A 1 96  ? 62.659 35.146 19.493  1.00 56.78 ? 96  ASP A OD2 1 
ATOM   715  N  N   . VAL A 1 97  ? 61.920 33.006 15.689  1.00 33.39 ? 97  VAL A N   1 
ATOM   716  C  CA  . VAL A 1 97  ? 62.458 32.510 14.439  1.00 28.90 ? 97  VAL A CA  1 
ATOM   717  C  C   . VAL A 1 97  ? 63.898 32.945 14.273  1.00 28.75 ? 97  VAL A C   1 
ATOM   718  O  O   . VAL A 1 97  ? 64.204 34.136 14.300  1.00 28.08 ? 97  VAL A O   1 
ATOM   719  C  CB  . VAL A 1 97  ? 61.614 33.030 13.223  1.00 28.24 ? 97  VAL A CB  1 
ATOM   720  C  CG1 . VAL A 1 97  ? 62.021 32.325 11.948  1.00 26.27 ? 97  VAL A CG1 1 
ATOM   721  C  CG2 . VAL A 1 97  ? 60.116 32.846 13.476  1.00 24.82 ? 97  VAL A CG2 1 
ATOM   722  N  N   . SER A 1 98  ? 64.779 31.970 14.115  1.00 27.85 ? 98  SER A N   1 
ATOM   723  C  CA  . SER A 1 98  ? 66.191 32.233 13.908  1.00 29.76 ? 98  SER A CA  1 
ATOM   724  C  C   . SER A 1 98  ? 66.650 31.191 12.883  1.00 30.85 ? 98  SER A C   1 
ATOM   725  O  O   . SER A 1 98  ? 67.128 30.112 13.247  1.00 34.27 ? 98  SER A O   1 
ATOM   726  C  CB  . SER A 1 98  ? 66.956 32.101 15.228  1.00 29.28 ? 98  SER A CB  1 
ATOM   727  O  OG  . SER A 1 98  ? 68.241 32.696 15.138  1.00 28.92 ? 98  SER A OG  1 
ATOM   728  N  N   . ILE A 1 99  ? 66.477 31.524 11.604  1.00 29.76 ? 99  ILE A N   1 
ATOM   729  C  CA  . ILE A 1 99  ? 66.803 30.651 10.473  1.00 28.29 ? 99  ILE A CA  1 
ATOM   730  C  C   . ILE A 1 99  ? 67.900 31.239 9.610   1.00 27.18 ? 99  ILE A C   1 
ATOM   731  O  O   . ILE A 1 99  ? 68.065 32.440 9.544   1.00 29.36 ? 99  ILE A O   1 
ATOM   732  C  CB  . ILE A 1 99  ? 65.562 30.519 9.533   1.00 28.84 ? 99  ILE A CB  1 
ATOM   733  C  CG1 . ILE A 1 99  ? 64.383 29.886 10.262  1.00 29.57 ? 99  ILE A CG1 1 
ATOM   734  C  CG2 . ILE A 1 99  ? 65.896 29.749 8.269   1.00 29.76 ? 99  ILE A CG2 1 
ATOM   735  C  CD1 . ILE A 1 99  ? 63.071 30.049 9.505   1.00 31.30 ? 99  ILE A CD1 1 
ATOM   736  N  N   . GLU A 1 100 ? 68.671 30.390 8.963   1.00 26.89 ? 100 GLU A N   1 
ATOM   737  C  CA  . GLU A 1 100 ? 69.665 30.868 8.029   1.00 27.70 ? 100 GLU A CA  1 
ATOM   738  C  C   . GLU A 1 100 ? 69.420 29.973 6.826   1.00 29.33 ? 100 GLU A C   1 
ATOM   739  O  O   . GLU A 1 100 ? 69.491 28.744 6.934   1.00 31.60 ? 100 GLU A O   1 
ATOM   740  C  CB  . GLU A 1 100 ? 71.059 30.693 8.560   1.00 27.32 ? 100 GLU A CB  1 
ATOM   741  C  CG  . GLU A 1 100 ? 72.049 31.317 7.657   1.00 32.60 ? 100 GLU A CG  1 
ATOM   742  C  CD  . GLU A 1 100 ? 73.456 31.139 8.142   1.00 38.52 ? 100 GLU A CD  1 
ATOM   743  O  OE1 . GLU A 1 100 ? 73.707 30.164 8.886   1.00 43.24 ? 100 GLU A OE1 1 
ATOM   744  O  OE2 . GLU A 1 100 ? 74.313 31.970 7.778   1.00 41.46 ? 100 GLU A OE2 1 
ATOM   745  N  N   . ASP A 1 101 ? 69.032 30.556 5.703   1.00 27.87 ? 101 ASP A N   1 
ATOM   746  C  CA  . ASP A 1 101 ? 68.735 29.741 4.541   1.00 26.93 ? 101 ASP A CA  1 
ATOM   747  C  C   . ASP A 1 101 ? 69.606 30.127 3.373   1.00 28.19 ? 101 ASP A C   1 
ATOM   748  O  O   . ASP A 1 101 ? 69.903 31.300 3.185   1.00 29.28 ? 101 ASP A O   1 
ATOM   749  C  CB  . ASP A 1 101 ? 67.256 29.877 4.183   1.00 25.42 ? 101 ASP A CB  1 
ATOM   750  C  CG  . ASP A 1 101 ? 66.788 28.800 3.219   1.00 25.81 ? 101 ASP A CG  1 
ATOM   751  O  OD1 . ASP A 1 101 ? 66.563 27.656 3.673   1.00 27.20 ? 101 ASP A OD1 1 
ATOM   752  O  OD2 . ASP A 1 101 ? 66.644 29.102 2.019   1.00 21.61 ? 101 ASP A OD2 1 
ATOM   753  N  N   . SER A 1 102 ? 69.998 29.141 2.572   1.00 27.73 ? 102 SER A N   1 
ATOM   754  C  CA  . SER A 1 102 ? 70.851 29.389 1.419   1.00 27.73 ? 102 SER A CA  1 
ATOM   755  C  C   . SER A 1 102 ? 70.154 29.358 0.053   1.00 26.98 ? 102 SER A C   1 
ATOM   756  O  O   . SER A 1 102 ? 70.764 29.694 -0.961  1.00 28.66 ? 102 SER A O   1 
ATOM   757  C  CB  . SER A 1 102 ? 72.035 28.421 1.463   1.00 31.26 ? 102 SER A CB  1 
ATOM   758  O  OG  . SER A 1 102 ? 71.663 27.222 2.130   1.00 34.83 ? 102 SER A OG  1 
ATOM   759  N  N   . VAL A 1 103 ? 68.871 28.996 0.033   1.00 24.82 ? 103 VAL A N   1 
ATOM   760  C  CA  . VAL A 1 103 ? 68.088 28.925 -1.214  1.00 23.52 ? 103 VAL A CA  1 
ATOM   761  C  C   . VAL A 1 103 ? 67.281 30.222 -1.494  1.00 23.00 ? 103 VAL A C   1 
ATOM   762  O  O   . VAL A 1 103 ? 67.143 30.642 -2.645  1.00 21.72 ? 103 VAL A O   1 
ATOM   763  C  CB  . VAL A 1 103 ? 67.139 27.678 -1.206  1.00 24.36 ? 103 VAL A CB  1 
ATOM   764  C  CG1 . VAL A 1 103 ? 66.366 27.561 -2.514  1.00 23.92 ? 103 VAL A CG1 1 
ATOM   765  C  CG2 . VAL A 1 103 ? 67.944 26.419 -0.974  1.00 24.53 ? 103 VAL A CG2 1 
ATOM   766  N  N   . ILE A 1 104 ? 66.688 30.818 -0.463  1.00 22.55 ? 104 ILE A N   1 
ATOM   767  C  CA  . ILE A 1 104 ? 65.971 32.070 -0.676  1.00 21.14 ? 104 ILE A CA  1 
ATOM   768  C  C   . ILE A 1 104 ? 67.025 33.160 -0.852  1.00 20.93 ? 104 ILE A C   1 
ATOM   769  O  O   . ILE A 1 104 ? 68.185 32.991 -0.454  1.00 22.67 ? 104 ILE A O   1 
ATOM   770  C  CB  . ILE A 1 104 ? 65.029 32.453 0.490   1.00 20.32 ? 104 ILE A CB  1 
ATOM   771  C  CG1 . ILE A 1 104 ? 65.805 32.581 1.806   1.00 19.04 ? 104 ILE A CG1 1 
ATOM   772  C  CG2 . ILE A 1 104 ? 63.847 31.513 0.543   1.00 17.70 ? 104 ILE A CG2 1 
ATOM   773  C  CD1 . ILE A 1 104 ? 64.973 33.162 2.947   1.00 21.70 ? 104 ILE A CD1 1 
ATOM   774  N  N   . SER A 1 105 ? 66.624 34.277 -1.439  1.00 19.77 ? 105 SER A N   1 
ATOM   775  C  CA  . SER A 1 105 ? 67.546 35.359 -1.675  1.00 20.35 ? 105 SER A CA  1 
ATOM   776  C  C   . SER A 1 105 ? 66.777 36.681 -1.679  1.00 21.92 ? 105 SER A C   1 
ATOM   777  O  O   . SER A 1 105 ? 65.558 36.699 -1.851  1.00 19.45 ? 105 SER A O   1 
ATOM   778  C  CB  . SER A 1 105 ? 68.237 35.134 -3.029  1.00 18.28 ? 105 SER A CB  1 
ATOM   779  O  OG  . SER A 1 105 ? 69.357 35.980 -3.234  1.00 18.32 ? 105 SER A OG  1 
ATOM   780  N  N   . LEU A 1 106 ? 67.492 37.769 -1.407  1.00 22.44 ? 106 LEU A N   1 
ATOM   781  C  CA  . LEU A 1 106 ? 66.919 39.107 -1.439  1.00 25.87 ? 106 LEU A CA  1 
ATOM   782  C  C   . LEU A 1 106 ? 67.350 39.807 -2.750  1.00 27.76 ? 106 LEU A C   1 
ATOM   783  O  O   . LEU A 1 106 ? 66.994 40.958 -2.987  1.00 28.25 ? 106 LEU A O   1 
ATOM   784  C  CB  . LEU A 1 106 ? 67.352 39.928 -0.211  1.00 22.89 ? 106 LEU A CB  1 
ATOM   785  C  CG  . LEU A 1 106 ? 67.125 39.340 1.178   1.00 21.45 ? 106 LEU A CG  1 
ATOM   786  C  CD1 . LEU A 1 106 ? 67.419 40.398 2.221   1.00 18.92 ? 106 LEU A CD1 1 
ATOM   787  C  CD2 . LEU A 1 106 ? 65.703 38.842 1.318   1.00 21.36 ? 106 LEU A CD2 1 
ATOM   788  N  N   . SER A 1 107 ? 68.087 39.085 -3.601  1.00 31.74 ? 107 SER A N   1 
ATOM   789  C  CA  . SER A 1 107 ? 68.574 39.565 -4.908  1.00 36.15 ? 107 SER A CA  1 
ATOM   790  C  C   . SER A 1 107 ? 68.433 38.422 -5.915  1.00 37.30 ? 107 SER A C   1 
ATOM   791  O  O   . SER A 1 107 ? 68.326 37.254 -5.524  1.00 38.72 ? 107 SER A O   1 
ATOM   792  C  CB  . SER A 1 107 ? 70.078 39.917 -4.858  1.00 36.44 ? 107 SER A CB  1 
ATOM   793  O  OG  . SER A 1 107 ? 70.366 40.988 -3.984  1.00 42.65 ? 107 SER A OG  1 
ATOM   794  N  N   . GLY A 1 108 ? 68.450 38.755 -7.204  1.00 39.47 ? 108 GLY A N   1 
ATOM   795  C  CA  . GLY A 1 108 ? 68.389 37.737 -8.239  1.00 39.87 ? 108 GLY A CA  1 
ATOM   796  C  C   . GLY A 1 108 ? 67.064 37.089 -8.562  1.00 41.07 ? 108 GLY A C   1 
ATOM   797  O  O   . GLY A 1 108 ? 65.997 37.641 -8.319  1.00 41.88 ? 108 GLY A O   1 
ATOM   798  N  N   . ASP A 1 109 ? 67.144 35.871 -9.072  1.00 42.68 ? 109 ASP A N   1 
ATOM   799  C  CA  . ASP A 1 109 ? 65.965 35.130 -9.485  1.00 45.54 ? 109 ASP A CA  1 
ATOM   800  C  C   . ASP A 1 109 ? 65.166 34.460 -8.382  1.00 43.43 ? 109 ASP A C   1 
ATOM   801  O  O   . ASP A 1 109 ? 63.972 34.202 -8.537  1.00 43.79 ? 109 ASP A O   1 
ATOM   802  C  CB  . ASP A 1 109 ? 66.361 34.113 -10.557 1.00 52.74 ? 109 ASP A CB  1 
ATOM   803  C  CG  . ASP A 1 109 ? 66.634 34.773 -11.914 1.00 59.27 ? 109 ASP A CG  1 
ATOM   804  O  OD1 . ASP A 1 109 ? 67.655 35.494 -12.066 1.00 61.01 ? 109 ASP A OD1 1 
ATOM   805  O  OD2 . ASP A 1 109 ? 65.804 34.583 -12.830 1.00 64.54 ? 109 ASP A OD2 1 
ATOM   806  N  N   . HIS A 1 110 ? 65.837 34.156 -7.280  1.00 40.04 ? 110 HIS A N   1 
ATOM   807  C  CA  . HIS A 1 110 ? 65.195 33.517 -6.143  1.00 35.83 ? 110 HIS A CA  1 
ATOM   808  C  C   . HIS A 1 110 ? 64.778 34.572 -5.144  1.00 31.04 ? 110 HIS A C   1 
ATOM   809  O  O   . HIS A 1 110 ? 64.492 34.268 -3.989  1.00 29.89 ? 110 HIS A O   1 
ATOM   810  C  CB  . HIS A 1 110 ? 66.166 32.543 -5.492  1.00 39.07 ? 110 HIS A CB  1 
ATOM   811  C  CG  . HIS A 1 110 ? 66.474 31.353 -6.344  1.00 44.03 ? 110 HIS A CG  1 
ATOM   812  N  ND1 . HIS A 1 110 ? 67.140 30.248 -5.868  1.00 46.06 ? 110 HIS A ND1 1 
ATOM   813  C  CD2 . HIS A 1 110 ? 66.170 31.088 -7.639  1.00 45.82 ? 110 HIS A CD2 1 
ATOM   814  C  CE1 . HIS A 1 110 ? 67.231 29.343 -6.831  1.00 47.03 ? 110 HIS A CE1 1 
ATOM   815  N  NE2 . HIS A 1 110 ? 66.651 29.829 -7.912  1.00 47.59 ? 110 HIS A NE2 1 
ATOM   816  N  N   . CYS A 1 111 ? 64.756 35.813 -5.613  1.00 27.77 ? 111 CYS A N   1 
ATOM   817  C  CA  . CYS A 1 111 ? 64.404 36.973 -4.819  1.00 26.60 ? 111 CYS A CA  1 
ATOM   818  C  C   . CYS A 1 111 ? 63.022 36.866 -4.176  1.00 23.94 ? 111 CYS A C   1 
ATOM   819  O  O   . CYS A 1 111 ? 62.029 36.682 -4.866  1.00 25.92 ? 111 CYS A O   1 
ATOM   820  C  CB  . CYS A 1 111 ? 64.458 38.198 -5.722  1.00 28.76 ? 111 CYS A CB  1 
ATOM   821  S  SG  . CYS A 1 111 ? 64.280 39.725 -4.864  1.00 38.81 ? 111 CYS A SG  1 
ATOM   822  N  N   . ILE A 1 112 ? 62.940 37.007 -2.858  1.00 22.44 ? 112 ILE A N   1 
ATOM   823  C  CA  . ILE A 1 112 ? 61.640 36.914 -2.198  1.00 21.63 ? 112 ILE A CA  1 
ATOM   824  C  C   . ILE A 1 112 ? 61.004 38.264 -1.918  1.00 21.03 ? 112 ILE A C   1 
ATOM   825  O  O   . ILE A 1 112 ? 59.935 38.328 -1.311  1.00 21.41 ? 112 ILE A O   1 
ATOM   826  C  CB  . ILE A 1 112 ? 61.710 36.133 -0.880  1.00 21.77 ? 112 ILE A CB  1 
ATOM   827  C  CG1 . ILE A 1 112 ? 62.758 36.757 0.043   1.00 21.54 ? 112 ILE A CG1 1 
ATOM   828  C  CG2 . ILE A 1 112 ? 61.999 34.662 -1.150  1.00 23.70 ? 112 ILE A CG2 1 
ATOM   829  C  CD1 . ILE A 1 112 ? 62.893 36.046 1.363   1.00 22.65 ? 112 ILE A CD1 1 
ATOM   830  N  N   . ILE A 1 113 ? 61.661 39.346 -2.323  1.00 19.02 ? 113 ILE A N   1 
ATOM   831  C  CA  . ILE A 1 113 ? 61.106 40.679 -2.098  1.00 20.02 ? 113 ILE A CA  1 
ATOM   832  C  C   . ILE A 1 113 ? 59.839 40.877 -2.939  1.00 17.61 ? 113 ILE A C   1 
ATOM   833  O  O   . ILE A 1 113 ? 59.803 40.534 -4.114  1.00 18.17 ? 113 ILE A O   1 
ATOM   834  C  CB  . ILE A 1 113 ? 62.174 41.794 -2.362  1.00 21.83 ? 113 ILE A CB  1 
ATOM   835  C  CG1 . ILE A 1 113 ? 63.211 41.778 -1.217  1.00 23.95 ? 113 ILE A CG1 1 
ATOM   836  C  CG2 . ILE A 1 113 ? 61.509 43.174 -2.486  1.00 19.44 ? 113 ILE A CG2 1 
ATOM   837  C  CD1 . ILE A 1 113 ? 64.272 42.834 -1.316  1.00 28.81 ? 113 ILE A CD1 1 
ATOM   838  N  N   . GLY A 1 114 ? 58.777 41.361 -2.307  1.00 17.01 ? 114 GLY A N   1 
ATOM   839  C  CA  . GLY A 1 114 ? 57.540 41.583 -3.021  1.00 15.63 ? 114 GLY A CA  1 
ATOM   840  C  C   . GLY A 1 114 ? 56.623 40.379 -2.997  1.00 17.81 ? 114 GLY A C   1 
ATOM   841  O  O   . GLY A 1 114 ? 55.564 40.418 -3.612  1.00 17.38 ? 114 GLY A O   1 
ATOM   842  N  N   . ARG A 1 115 ? 57.017 39.307 -2.308  1.00 17.28 ? 115 ARG A N   1 
ATOM   843  C  CA  . ARG A 1 115 ? 56.189 38.099 -2.215  1.00 17.29 ? 115 ARG A CA  1 
ATOM   844  C  C   . ARG A 1 115 ? 55.588 38.016 -0.813  1.00 17.45 ? 115 ARG A C   1 
ATOM   845  O  O   . ARG A 1 115 ? 55.802 38.919 -0.009  1.00 20.65 ? 115 ARG A O   1 
ATOM   846  C  CB  . ARG A 1 115 ? 57.006 36.855 -2.591  1.00 17.24 ? 115 ARG A CB  1 
ATOM   847  C  CG  . ARG A 1 115 ? 57.696 37.045 -3.905  1.00 18.25 ? 115 ARG A CG  1 
ATOM   848  C  CD  . ARG A 1 115 ? 58.351 35.797 -4.412  1.00 21.82 ? 115 ARG A CD  1 
ATOM   849  N  NE  . ARG A 1 115 ? 59.057 36.065 -5.657  1.00 18.73 ? 115 ARG A NE  1 
ATOM   850  C  CZ  . ARG A 1 115 ? 58.497 36.047 -6.862  1.00 18.24 ? 115 ARG A CZ  1 
ATOM   851  N  NH1 . ARG A 1 115 ? 57.206 35.768 -7.025  1.00 16.92 ? 115 ARG A NH1 1 
ATOM   852  N  NH2 . ARG A 1 115 ? 59.248 36.317 -7.915  1.00 21.47 ? 115 ARG A NH2 1 
ATOM   853  N  N   . THR A 1 116 ? 54.864 36.954 -0.500  1.00 15.63 ? 116 THR A N   1 
ATOM   854  C  CA  . THR A 1 116 ? 54.213 36.867 0.794   1.00 17.70 ? 116 THR A CA  1 
ATOM   855  C  C   . THR A 1 116 ? 54.775 35.811 1.738   1.00 18.99 ? 116 THR A C   1 
ATOM   856  O  O   . THR A 1 116 ? 54.961 34.661 1.351   1.00 21.85 ? 116 THR A O   1 
ATOM   857  C  CB  . THR A 1 116 ? 52.707 36.603 0.589   1.00 16.13 ? 116 THR A CB  1 
ATOM   858  O  OG1 . THR A 1 116 ? 52.152 37.663 -0.191  1.00 18.75 ? 116 THR A OG1 1 
ATOM   859  C  CG2 . THR A 1 116 ? 51.962 36.513 1.905   1.00 18.13 ? 116 THR A CG2 1 
ATOM   860  N  N   . LEU A 1 117 ? 55.078 36.199 2.969   1.00 18.16 ? 117 LEU A N   1 
ATOM   861  C  CA  . LEU A 1 117 ? 55.551 35.239 3.949   1.00 18.10 ? 117 LEU A CA  1 
ATOM   862  C  C   . LEU A 1 117 ? 54.270 34.809 4.669   1.00 18.68 ? 117 LEU A C   1 
ATOM   863  O  O   . LEU A 1 117 ? 53.422 35.639 4.979   1.00 19.43 ? 117 LEU A O   1 
ATOM   864  C  CB  . LEU A 1 117 ? 56.546 35.894 4.907   1.00 17.70 ? 117 LEU A CB  1 
ATOM   865  C  CG  . LEU A 1 117 ? 57.265 34.995 5.917   1.00 21.41 ? 117 LEU A CG  1 
ATOM   866  C  CD1 . LEU A 1 117 ? 58.110 33.894 5.233   1.00 19.19 ? 117 LEU A CD1 1 
ATOM   867  C  CD2 . LEU A 1 117 ? 58.142 35.881 6.780   1.00 20.44 ? 117 LEU A CD2 1 
ATOM   868  N  N   . VAL A 1 118 ? 54.105 33.511 4.880   1.00 19.62 ? 118 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 118 ? 52.904 32.969 5.517   1.00 21.57 ? 118 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 118 ? 53.220 31.943 6.616   1.00 22.92 ? 118 VAL A C   1 
ATOM   871  O  O   . VAL A 1 118 ? 54.121 31.106 6.460   1.00 23.35 ? 118 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 118 ? 51.975 32.262 4.456   1.00 21.25 ? 118 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 118 ? 50.768 31.612 5.127   1.00 19.94 ? 118 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 118 ? 51.501 33.243 3.403   1.00 20.09 ? 118 VAL A CG2 1 
ATOM   875  N  N   . VAL A 1 119 ? 52.481 32.030 7.724   1.00 25.02 ? 119 VAL A N   1 
ATOM   876  C  CA  . VAL A 1 119 ? 52.612 31.103 8.849   1.00 26.22 ? 119 VAL A CA  1 
ATOM   877  C  C   . VAL A 1 119 ? 51.331 30.280 8.840   1.00 26.32 ? 119 VAL A C   1 
ATOM   878  O  O   . VAL A 1 119 ? 50.226 30.825 8.787   1.00 25.60 ? 119 VAL A O   1 
ATOM   879  C  CB  . VAL A 1 119 ? 52.837 31.816 10.239  1.00 27.55 ? 119 VAL A CB  1 
ATOM   880  C  CG1 . VAL A 1 119 ? 51.695 32.784 10.587  1.00 28.53 ? 119 VAL A CG1 1 
ATOM   881  C  CG2 . VAL A 1 119 ? 53.008 30.771 11.344  1.00 27.45 ? 119 VAL A CG2 1 
ATOM   882  N  N   . HIS A 1 120 ? 51.494 28.963 8.843   1.00 28.47 ? 120 HIS A N   1 
ATOM   883  C  CA  . HIS A 1 120 ? 50.371 28.049 8.779   1.00 29.14 ? 120 HIS A CA  1 
ATOM   884  C  C   . HIS A 1 120 ? 49.847 27.511 10.084  1.00 31.48 ? 120 HIS A C   1 
ATOM   885  O  O   . HIS A 1 120 ? 50.561 27.379 11.081  1.00 32.20 ? 120 HIS A O   1 
ATOM   886  C  CB  . HIS A 1 120 ? 50.700 26.881 7.862   1.00 28.75 ? 120 HIS A CB  1 
ATOM   887  C  CG  . HIS A 1 120 ? 50.713 27.239 6.410   1.00 26.05 ? 120 HIS A CG  1 
ATOM   888  N  ND1 . HIS A 1 120 ? 49.579 27.226 5.632   1.00 25.92 ? 120 HIS A ND1 1 
ATOM   889  C  CD2 . HIS A 1 120 ? 51.726 27.611 5.592   1.00 24.04 ? 120 HIS A CD2 1 
ATOM   890  C  CE1 . HIS A 1 120 ? 49.888 27.573 4.397   1.00 26.16 ? 120 HIS A CE1 1 
ATOM   891  N  NE2 . HIS A 1 120 ? 51.187 27.812 4.346   1.00 26.98 ? 120 HIS A NE2 1 
ATOM   892  N  N   . GLU A 1 121 ? 48.593 27.119 10.020  1.00 32.70 ? 121 GLU A N   1 
ATOM   893  C  CA  . GLU A 1 121 ? 47.883 26.570 11.141  1.00 36.28 ? 121 GLU A CA  1 
ATOM   894  C  C   . GLU A 1 121 ? 48.479 25.271 11.688  1.00 35.67 ? 121 GLU A C   1 
ATOM   895  O  O   . GLU A 1 121 ? 48.539 25.065 12.901  1.00 36.26 ? 121 GLU A O   1 
ATOM   896  C  CB  . GLU A 1 121 ? 46.459 26.321 10.690  1.00 41.27 ? 121 GLU A CB  1 
ATOM   897  C  CG  . GLU A 1 121 ? 45.584 25.586 11.677  1.00 48.92 ? 121 GLU A CG  1 
ATOM   898  C  CD  . GLU A 1 121 ? 44.314 25.110 11.022  1.00 53.93 ? 121 GLU A CD  1 
ATOM   899  O  OE1 . GLU A 1 121 ? 44.423 24.371 10.008  1.00 55.73 ? 121 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A 1 121 ? 43.220 25.505 11.494  1.00 56.88 ? 121 GLU A OE2 1 
ATOM   901  N  N   . LYS A 1 122 ? 48.918 24.399 10.794  1.00 35.08 ? 122 LYS A N   1 
ATOM   902  C  CA  . LYS A 1 122 ? 49.445 23.118 11.211  1.00 35.51 ? 122 LYS A CA  1 
ATOM   903  C  C   . LYS A 1 122 ? 50.895 22.941 10.873  1.00 34.33 ? 122 LYS A C   1 
ATOM   904  O  O   . LYS A 1 122 ? 51.489 23.774 10.191  1.00 34.47 ? 122 LYS A O   1 
ATOM   905  C  CB  . LYS A 1 122 ? 48.661 21.995 10.549  1.00 39.58 ? 122 LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 122 ? 47.205 21.901 10.945  1.00 44.78 ? 122 LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 122 ? 46.508 20.870 10.067  1.00 50.09 ? 122 LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 122 ? 47.335 19.575 9.938   1.00 54.53 ? 122 LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 122 ? 47.503 18.822 11.235  1.00 58.01 ? 122 LYS A NZ  1 
ATOM   910  N  N   . ALA A 1 123 ? 51.451 21.831 11.345  1.00 32.35 ? 123 ALA A N   1 
ATOM   911  C  CA  . ALA A 1 123 ? 52.837 21.502 11.091  1.00 32.74 ? 123 ALA A CA  1 
ATOM   912  C  C   . ALA A 1 123 ? 52.972 21.141 9.634   1.00 32.02 ? 123 ALA A C   1 
ATOM   913  O  O   . ALA A 1 123 ? 52.027 20.674 8.999   1.00 32.74 ? 123 ALA A O   1 
ATOM   914  C  CB  . ALA A 1 123 ? 53.286 20.341 11.951  1.00 32.62 ? 123 ALA A CB  1 
ATOM   915  N  N   . ASP A 1 124 ? 54.159 21.381 9.116   1.00 30.48 ? 124 ASP A N   1 
ATOM   916  C  CA  . ASP A 1 124 ? 54.473 21.099 7.749   1.00 29.79 ? 124 ASP A CA  1 
ATOM   917  C  C   . ASP A 1 124 ? 55.215 19.774 7.821   1.00 30.32 ? 124 ASP A C   1 
ATOM   918  O  O   . ASP A 1 124 ? 56.257 19.689 8.475   1.00 30.92 ? 124 ASP A O   1 
ATOM   919  C  CB  . ASP A 1 124 ? 55.374 22.229 7.236   1.00 29.56 ? 124 ASP A CB  1 
ATOM   920  C  CG  . ASP A 1 124 ? 55.891 21.998 5.834   1.00 31.13 ? 124 ASP A CG  1 
ATOM   921  O  OD1 . ASP A 1 124 ? 55.620 20.937 5.246   1.00 33.63 ? 124 ASP A OD1 1 
ATOM   922  O  OD2 . ASP A 1 124 ? 56.602 22.881 5.315   1.00 29.89 ? 124 ASP A OD2 1 
ATOM   923  N  N   . ASP A 1 125 ? 54.696 18.746 7.144   1.00 31.78 ? 125 ASP A N   1 
ATOM   924  C  CA  . ASP A 1 125 ? 55.335 17.417 7.138   1.00 32.33 ? 125 ASP A CA  1 
ATOM   925  C  C   . ASP A 1 125 ? 56.619 17.323 6.321   1.00 31.55 ? 125 ASP A C   1 
ATOM   926  O  O   . ASP A 1 125 ? 57.165 16.240 6.141   1.00 33.98 ? 125 ASP A O   1 
ATOM   927  C  CB  . ASP A 1 125 ? 54.350 16.285 6.743   1.00 33.39 ? 125 ASP A CB  1 
ATOM   928  C  CG  . ASP A 1 125 ? 53.822 16.394 5.304   1.00 32.37 ? 125 ASP A CG  1 
ATOM   929  O  OD1 . ASP A 1 125 ? 54.546 16.838 4.387   1.00 34.32 ? 125 ASP A OD1 1 
ATOM   930  O  OD2 . ASP A 1 125 ? 52.663 15.991 5.084   1.00 31.47 ? 125 ASP A OD2 1 
ATOM   931  N  N   . LEU A 1 126 ? 57.077 18.455 5.804   1.00 29.08 ? 126 LEU A N   1 
ATOM   932  C  CA  . LEU A 1 126 ? 58.293 18.530 5.018   1.00 26.81 ? 126 LEU A CA  1 
ATOM   933  C  C   . LEU A 1 126 ? 58.262 17.679 3.749   1.00 29.15 ? 126 LEU A C   1 
ATOM   934  O  O   . LEU A 1 126 ? 59.302 17.250 3.244   1.00 29.25 ? 126 LEU A O   1 
ATOM   935  C  CB  . LEU A 1 126 ? 59.508 18.205 5.891   1.00 26.90 ? 126 LEU A CB  1 
ATOM   936  C  CG  . LEU A 1 126 ? 59.636 18.979 7.226   1.00 30.31 ? 126 LEU A CG  1 
ATOM   937  C  CD1 . LEU A 1 126 ? 61.012 18.733 7.810   1.00 29.40 ? 126 LEU A CD1 1 
ATOM   938  C  CD2 . LEU A 1 126 ? 59.429 20.506 7.063   1.00 28.34 ? 126 LEU A CD2 1 
ATOM   939  N  N   . GLY A 1 127 ? 57.064 17.481 3.209   1.00 30.85 ? 127 GLY A N   1 
ATOM   940  C  CA  . GLY A 1 127 ? 56.910 16.706 1.991   1.00 35.10 ? 127 GLY A CA  1 
ATOM   941  C  C   . GLY A 1 127 ? 57.187 15.215 2.103   1.00 38.54 ? 127 GLY A C   1 
ATOM   942  O  O   . GLY A 1 127 ? 57.285 14.527 1.091   1.00 37.67 ? 127 GLY A O   1 
ATOM   943  N  N   . LYS A 1 128 ? 57.246 14.699 3.326   1.00 41.35 ? 128 LYS A N   1 
ATOM   944  C  CA  . LYS A 1 128 ? 57.521 13.284 3.538   1.00 44.54 ? 128 LYS A CA  1 
ATOM   945  C  C   . LYS A 1 128 ? 56.268 12.547 3.991   1.00 45.98 ? 128 LYS A C   1 
ATOM   946  O  O   . LYS A 1 128 ? 56.332 11.380 4.374   1.00 46.83 ? 128 LYS A O   1 
ATOM   947  C  CB  . LYS A 1 128 ? 58.633 13.123 4.578   1.00 45.53 ? 128 LYS A CB  1 
ATOM   948  C  CG  . LYS A 1 128 ? 58.198 13.461 5.999   1.00 50.37 ? 128 LYS A CG  1 
ATOM   949  C  CD  . LYS A 1 128 ? 59.393 13.691 6.930   1.00 55.21 ? 128 LYS A CD  1 
ATOM   950  C  CE  . LYS A 1 128 ? 58.962 13.752 8.402   1.00 57.42 ? 128 LYS A CE  1 
ATOM   951  N  NZ  . LYS A 1 128 ? 58.004 14.861 8.710   1.00 56.96 ? 128 LYS A NZ  1 
ATOM   952  N  N   . GLY A 1 129 ? 55.127 13.223 3.919   1.00 46.99 ? 129 GLY A N   1 
ATOM   953  C  CA  . GLY A 1 129 ? 53.876 12.622 4.347   1.00 48.87 ? 129 GLY A CA  1 
ATOM   954  C  C   . GLY A 1 129 ? 53.375 11.455 3.518   1.00 50.47 ? 129 GLY A C   1 
ATOM   955  O  O   . GLY A 1 129 ? 52.471 10.744 3.947   1.00 50.58 ? 129 GLY A O   1 
ATOM   956  N  N   . GLY A 1 130 ? 53.907 11.297 2.308   1.00 52.79 ? 130 GLY A N   1 
ATOM   957  C  CA  . GLY A 1 130 ? 53.497 10.196 1.446   1.00 54.58 ? 130 GLY A CA  1 
ATOM   958  C  C   . GLY A 1 130 ? 52.236 10.353 0.601   1.00 54.97 ? 130 GLY A C   1 
ATOM   959  O  O   . GLY A 1 130 ? 51.771 9.373  0.018   1.00 55.63 ? 130 GLY A O   1 
ATOM   960  N  N   . ASN A 1 131 ? 51.678 11.558 0.527   1.00 55.38 ? 131 ASN A N   1 
ATOM   961  C  CA  . ASN A 1 131 ? 50.475 11.801 -0.275  1.00 55.93 ? 131 ASN A CA  1 
ATOM   962  C  C   . ASN A 1 131 ? 50.622 13.097 -1.088  1.00 56.15 ? 131 ASN A C   1 
ATOM   963  O  O   . ASN A 1 131 ? 51.465 13.939 -0.758  1.00 59.15 ? 131 ASN A O   1 
ATOM   964  C  CB  . ASN A 1 131 ? 49.197 11.793 0.602   1.00 55.66 ? 131 ASN A CB  1 
ATOM   965  C  CG  . ASN A 1 131 ? 49.065 13.018 1.510   1.00 54.29 ? 131 ASN A CG  1 
ATOM   966  O  OD1 . ASN A 1 131 ? 48.086 13.756 1.421   1.00 55.22 ? 131 ASN A OD1 1 
ATOM   967  N  ND2 . ASN A 1 131 ? 50.007 13.198 2.419   1.00 54.32 ? 131 ASN A ND2 1 
ATOM   968  N  N   . GLU A 1 132 ? 49.847 13.230 -2.168  1.00 54.90 ? 132 GLU A N   1 
ATOM   969  C  CA  . GLU A 1 132 ? 49.880 14.404 -3.060  1.00 54.06 ? 132 GLU A CA  1 
ATOM   970  C  C   . GLU A 1 132 ? 50.112 15.738 -2.328  1.00 49.92 ? 132 GLU A C   1 
ATOM   971  O  O   . GLU A 1 132 ? 51.084 16.437 -2.604  1.00 50.07 ? 132 GLU A O   1 
ATOM   972  C  CB  . GLU A 1 132 ? 48.585 14.463 -3.883  1.00 57.45 ? 132 GLU A CB  1 
ATOM   973  C  CG  . GLU A 1 132 ? 48.630 15.387 -5.101  1.00 64.04 ? 132 GLU A CG  1 
ATOM   974  C  CD  . GLU A 1 132 ? 47.251 15.610 -5.730  1.00 68.39 ? 132 GLU A CD  1 
ATOM   975  O  OE1 . GLU A 1 132 ? 46.328 16.064 -5.005  1.00 70.11 ? 132 GLU A OE1 1 
ATOM   976  O  OE2 . GLU A 1 132 ? 47.093 15.340 -6.948  1.00 70.59 ? 132 GLU A OE2 1 
ATOM   977  N  N   . GLU A 1 133 ? 49.246 16.043 -1.362  1.00 46.45 ? 133 GLU A N   1 
ATOM   978  C  CA  . GLU A 1 133 ? 49.318 17.255 -0.546  1.00 42.57 ? 133 GLU A CA  1 
ATOM   979  C  C   . GLU A 1 133 ? 50.645 17.449 0.155   1.00 39.37 ? 133 GLU A C   1 
ATOM   980  O  O   . GLU A 1 133 ? 51.081 18.574 0.379   1.00 38.53 ? 133 GLU A O   1 
ATOM   981  C  CB  . GLU A 1 133 ? 48.232 17.233 0.518   1.00 44.82 ? 133 GLU A CB  1 
ATOM   982  C  CG  . GLU A 1 133 ? 46.906 17.708 0.036   1.00 49.70 ? 133 GLU A CG  1 
ATOM   983  C  CD  . GLU A 1 133 ? 46.980 19.136 -0.418  1.00 52.36 ? 133 GLU A CD  1 
ATOM   984  O  OE1 . GLU A 1 133 ? 46.989 20.038 0.448   1.00 54.31 ? 133 GLU A OE1 1 
ATOM   985  O  OE2 . GLU A 1 133 ? 47.057 19.352 -1.644  1.00 57.31 ? 133 GLU A OE2 1 
ATOM   986  N  N   . SER A 1 134 ? 51.254 16.354 0.568   1.00 35.35 ? 134 SER A N   1 
ATOM   987  C  CA  . SER A 1 134 ? 52.516 16.451 1.235   1.00 32.47 ? 134 SER A CA  1 
ATOM   988  C  C   . SER A 1 134 ? 53.554 16.939 0.257   1.00 33.24 ? 134 SER A C   1 
ATOM   989  O  O   . SER A 1 134 ? 54.385 17.767 0.613   1.00 33.99 ? 134 SER A O   1 
ATOM   990  C  CB  . SER A 1 134 ? 52.932 15.114 1.797   1.00 30.68 ? 134 SER A CB  1 
ATOM   991  O  OG  . SER A 1 134 ? 54.275 15.189 2.220   1.00 30.79 ? 134 SER A OG  1 
ATOM   992  N  N   . THR A 1 135 ? 53.524 16.430 -0.969  1.00 32.13 ? 135 THR A N   1 
ATOM   993  C  CA  . THR A 1 135 ? 54.501 16.858 -1.970  1.00 32.07 ? 135 THR A CA  1 
ATOM   994  C  C   . THR A 1 135 ? 54.110 18.230 -2.543  1.00 33.69 ? 135 THR A C   1 
ATOM   995  O  O   . THR A 1 135 ? 54.836 18.805 -3.363  1.00 33.28 ? 135 THR A O   1 
ATOM   996  C  CB  . THR A 1 135 ? 54.634 15.844 -3.151  1.00 31.41 ? 135 THR A CB  1 
ATOM   997  O  OG1 . THR A 1 135 ? 53.417 15.816 -3.910  1.00 33.32 ? 135 THR A OG1 1 
ATOM   998  C  CG2 . THR A 1 135 ? 54.925 14.441 -2.649  1.00 31.17 ? 135 THR A CG2 1 
ATOM   999  N  N   . LYS A 1 136 ? 52.982 18.762 -2.080  1.00 33.23 ? 136 LYS A N   1 
ATOM   1000 C  CA  . LYS A 1 136 ? 52.468 20.037 -2.547  1.00 32.90 ? 136 LYS A CA  1 
ATOM   1001 C  C   . LYS A 1 136 ? 52.651 21.145 -1.531  1.00 33.44 ? 136 LYS A C   1 
ATOM   1002 O  O   . LYS A 1 136 ? 53.400 22.109 -1.759  1.00 32.86 ? 136 LYS A O   1 
ATOM   1003 C  CB  . LYS A 1 136 ? 50.980 19.897 -2.826  1.00 36.40 ? 136 LYS A CB  1 
ATOM   1004 C  CG  . LYS A 1 136 ? 50.504 20.670 -4.016  1.00 41.08 ? 136 LYS A CG  1 
ATOM   1005 C  CD  . LYS A 1 136 ? 51.028 20.035 -5.284  1.00 44.66 ? 136 LYS A CD  1 
ATOM   1006 C  CE  . LYS A 1 136 ? 50.370 18.694 -5.532  1.00 49.63 ? 136 LYS A CE  1 
ATOM   1007 N  NZ  . LYS A 1 136 ? 48.967 18.862 -6.022  1.00 54.60 ? 136 LYS A NZ  1 
ATOM   1008 N  N   . THR A 1 137 ? 51.965 20.992 -0.403  1.00 33.04 ? 137 THR A N   1 
ATOM   1009 C  CA  . THR A 1 137 ? 51.975 21.971 0.682   1.00 32.56 ? 137 THR A CA  1 
ATOM   1010 C  C   . THR A 1 137 ? 52.572 21.497 2.005   1.00 31.68 ? 137 THR A C   1 
ATOM   1011 O  O   . THR A 1 137 ? 52.797 22.309 2.905   1.00 30.77 ? 137 THR A O   1 
ATOM   1012 C  CB  . THR A 1 137 ? 50.547 22.438 0.984   1.00 33.52 ? 137 THR A CB  1 
ATOM   1013 O  OG1 . THR A 1 137 ? 49.748 21.307 1.373   1.00 34.30 ? 137 THR A OG1 1 
ATOM   1014 C  CG2 . THR A 1 137 ? 49.933 23.097 -0.249  1.00 34.85 ? 137 THR A CG2 1 
ATOM   1015 N  N   . GLY A 1 138 ? 52.831 20.198 2.123   1.00 30.67 ? 138 GLY A N   1 
ATOM   1016 C  CA  . GLY A 1 138 ? 53.362 19.660 3.357   1.00 28.48 ? 138 GLY A CA  1 
ATOM   1017 C  C   . GLY A 1 138 ? 52.245 19.504 4.375   1.00 29.77 ? 138 GLY A C   1 
ATOM   1018 O  O   . GLY A 1 138 ? 52.493 19.386 5.564   1.00 31.10 ? 138 GLY A O   1 
ATOM   1019 N  N   . ASN A 1 139 ? 51.001 19.536 3.916   1.00 31.93 ? 139 ASN A N   1 
ATOM   1020 C  CA  . ASN A 1 139 ? 49.840 19.388 4.798   1.00 32.91 ? 139 ASN A CA  1 
ATOM   1021 C  C   . ASN A 1 139 ? 49.806 20.354 5.994   1.00 33.64 ? 139 ASN A C   1 
ATOM   1022 O  O   . ASN A 1 139 ? 49.216 20.029 7.031   1.00 35.22 ? 139 ASN A O   1 
ATOM   1023 C  CB  . ASN A 1 139 ? 49.715 17.939 5.300   1.00 33.49 ? 139 ASN A CB  1 
ATOM   1024 C  CG  . ASN A 1 139 ? 49.269 16.974 4.221   1.00 32.26 ? 139 ASN A CG  1 
ATOM   1025 O  OD1 . ASN A 1 139 ? 50.079 16.235 3.652   1.00 35.11 ? 139 ASN A OD1 1 
ATOM   1026 N  ND2 . ASN A 1 139 ? 47.976 16.951 3.954   1.00 32.14 ? 139 ASN A ND2 1 
ATOM   1027 N  N   . ALA A 1 140 ? 50.357 21.561 5.815   1.00 33.14 ? 140 ALA A N   1 
ATOM   1028 C  CA  . ALA A 1 140 ? 50.404 22.602 6.867   1.00 31.77 ? 140 ALA A CA  1 
ATOM   1029 C  C   . ALA A 1 140 ? 49.079 23.331 7.192   1.00 31.34 ? 140 ALA A C   1 
ATOM   1030 O  O   . ALA A 1 140 ? 49.022 24.154 8.112   1.00 30.47 ? 140 ALA A O   1 
ATOM   1031 C  CB  . ALA A 1 140 ? 51.484 23.619 6.538   1.00 30.87 ? 140 ALA A CB  1 
ATOM   1032 N  N   . GLY A 1 141 ? 48.036 23.078 6.408   1.00 31.72 ? 141 GLY A N   1 
ATOM   1033 C  CA  . GLY A 1 141 ? 46.745 23.696 6.657   1.00 32.38 ? 141 GLY A CA  1 
ATOM   1034 C  C   . GLY A 1 141 ? 46.594 25.176 6.365   1.00 33.70 ? 141 GLY A C   1 
ATOM   1035 O  O   . GLY A 1 141 ? 47.308 25.753 5.537   1.00 33.32 ? 141 GLY A O   1 
ATOM   1036 N  N   . SER A 1 142 ? 45.652 25.788 7.075   1.00 34.98 ? 142 SER A N   1 
ATOM   1037 C  CA  . SER A 1 142 ? 45.328 27.207 6.939   1.00 36.63 ? 142 SER A CA  1 
ATOM   1038 C  C   . SER A 1 142 ? 46.513 28.166 7.059   1.00 34.71 ? 142 SER A C   1 
ATOM   1039 O  O   . SER A 1 142 ? 47.536 27.862 7.677   1.00 34.31 ? 142 SER A O   1 
ATOM   1040 C  CB  . SER A 1 142 ? 44.297 27.612 8.002   1.00 37.57 ? 142 SER A CB  1 
ATOM   1041 O  OG  . SER A 1 142 ? 43.298 26.623 8.158   1.00 46.47 ? 142 SER A OG  1 
ATOM   1042 N  N   . ARG A 1 143 ? 46.323 29.343 6.476   1.00 34.02 ? 143 ARG A N   1 
ATOM   1043 C  CA  . ARG A 1 143 ? 47.291 30.425 6.502   1.00 32.18 ? 143 ARG A CA  1 
ATOM   1044 C  C   . ARG A 1 143 ? 46.733 31.350 7.596   1.00 31.41 ? 143 ARG A C   1 
ATOM   1045 O  O   . ARG A 1 143 ? 45.706 31.993 7.402   1.00 32.52 ? 143 ARG A O   1 
ATOM   1046 C  CB  . ARG A 1 143 ? 47.296 31.126 5.137   1.00 31.41 ? 143 ARG A CB  1 
ATOM   1047 C  CG  . ARG A 1 143 ? 47.537 30.179 3.957   1.00 29.23 ? 143 ARG A CG  1 
ATOM   1048 C  CD  . ARG A 1 143 ? 47.410 30.879 2.593   1.00 28.83 ? 143 ARG A CD  1 
ATOM   1049 N  NE  . ARG A 1 143 ? 47.569 29.926 1.495   1.00 28.45 ? 143 ARG A NE  1 
ATOM   1050 C  CZ  . ARG A 1 143 ? 47.910 30.234 0.245   1.00 28.16 ? 143 ARG A CZ  1 
ATOM   1051 N  NH1 . ARG A 1 143 ? 48.133 31.491 -0.123  1.00 27.98 ? 143 ARG A NH1 1 
ATOM   1052 N  NH2 . ARG A 1 143 ? 48.103 29.258 -0.630  1.00 27.18 ? 143 ARG A NH2 1 
ATOM   1053 N  N   . LEU A 1 144 ? 47.362 31.365 8.765   1.00 30.78 ? 144 LEU A N   1 
ATOM   1054 C  CA  . LEU A 1 144 ? 46.875 32.197 9.867   1.00 30.26 ? 144 LEU A CA  1 
ATOM   1055 C  C   . LEU A 1 144 ? 47.197 33.688 9.730   1.00 29.61 ? 144 LEU A C   1 
ATOM   1056 O  O   . LEU A 1 144 ? 46.363 34.544 10.057  1.00 30.62 ? 144 LEU A O   1 
ATOM   1057 C  CB  . LEU A 1 144 ? 47.414 31.677 11.209  1.00 28.96 ? 144 LEU A CB  1 
ATOM   1058 C  CG  . LEU A 1 144 ? 47.022 30.253 11.610  1.00 29.56 ? 144 LEU A CG  1 
ATOM   1059 C  CD1 . LEU A 1 144 ? 47.668 29.875 12.928  1.00 30.85 ? 144 LEU A CD1 1 
ATOM   1060 C  CD2 . LEU A 1 144 ? 45.520 30.141 11.705  1.00 31.76 ? 144 LEU A CD2 1 
ATOM   1061 N  N   . ALA A 1 145 ? 48.422 33.983 9.292   1.00 28.97 ? 145 ALA A N   1 
ATOM   1062 C  CA  . ALA A 1 145 ? 48.911 35.354 9.134   1.00 25.51 ? 145 ALA A CA  1 
ATOM   1063 C  C   . ALA A 1 145 ? 49.892 35.403 7.975   1.00 23.62 ? 145 ALA A C   1 
ATOM   1064 O  O   . ALA A 1 145 ? 50.484 34.394 7.611   1.00 24.37 ? 145 ALA A O   1 
ATOM   1065 C  CB  . ALA A 1 145 ? 49.586 35.828 10.420  1.00 25.25 ? 145 ALA A CB  1 
ATOM   1066 N  N   . CYS A 1 146 ? 50.081 36.584 7.408   1.00 22.36 ? 146 CYS A N   1 
ATOM   1067 C  CA  . CYS A 1 146 ? 50.962 36.734 6.274   1.00 21.67 ? 146 CYS A CA  1 
ATOM   1068 C  C   . CYS A 1 146 ? 51.292 38.194 6.053   1.00 20.38 ? 146 CYS A C   1 
ATOM   1069 O  O   . CYS A 1 146 ? 50.618 39.086 6.572   1.00 20.48 ? 146 CYS A O   1 
ATOM   1070 C  CB  . CYS A 1 146 ? 50.280 36.179 5.018   1.00 23.15 ? 146 CYS A CB  1 
ATOM   1071 S  SG  . CYS A 1 146 ? 48.693 36.973 4.572   1.00 28.80 ? 146 CYS A SG  1 
ATOM   1072 N  N   . GLY A 1 147 ? 52.324 38.431 5.262   1.00 20.08 ? 147 GLY A N   1 
ATOM   1073 C  CA  . GLY A 1 147 ? 52.723 39.786 4.963   1.00 18.28 ? 147 GLY A CA  1 
ATOM   1074 C  C   . GLY A 1 147 ? 53.547 39.815 3.708   1.00 17.60 ? 147 GLY A C   1 
ATOM   1075 O  O   . GLY A 1 147 ? 54.081 38.790 3.292   1.00 19.17 ? 147 GLY A O   1 
ATOM   1076 N  N   . VAL A 1 148 ? 53.590 40.972 3.060   1.00 15.85 ? 148 VAL A N   1 
ATOM   1077 C  CA  . VAL A 1 148 ? 54.388 41.138 1.861   1.00 16.28 ? 148 VAL A CA  1 
ATOM   1078 C  C   . VAL A 1 148 ? 55.792 41.498 2.378   1.00 16.29 ? 148 VAL A C   1 
ATOM   1079 O  O   . VAL A 1 148 ? 55.932 42.249 3.348   1.00 18.39 ? 148 VAL A O   1 
ATOM   1080 C  CB  . VAL A 1 148 ? 53.810 42.269 0.937   1.00 14.19 ? 148 VAL A CB  1 
ATOM   1081 C  CG1 . VAL A 1 148 ? 54.652 42.407 -0.315  1.00 12.46 ? 148 VAL A CG1 1 
ATOM   1082 C  CG2 . VAL A 1 148 ? 52.364 41.964 0.565   1.00 14.17 ? 148 VAL A CG2 1 
ATOM   1083 N  N   . ILE A 1 149 ? 56.828 40.944 1.764   1.00 16.79 ? 149 ILE A N   1 
ATOM   1084 C  CA  . ILE A 1 149 ? 58.190 41.220 2.175   1.00 15.68 ? 149 ILE A CA  1 
ATOM   1085 C  C   . ILE A 1 149 ? 58.660 42.485 1.483   1.00 15.58 ? 149 ILE A C   1 
ATOM   1086 O  O   . ILE A 1 149 ? 58.641 42.564 0.260   1.00 17.72 ? 149 ILE A O   1 
ATOM   1087 C  CB  . ILE A 1 149 ? 59.100 40.043 1.814   1.00 15.98 ? 149 ILE A CB  1 
ATOM   1088 C  CG1 . ILE A 1 149 ? 58.579 38.781 2.526   1.00 15.32 ? 149 ILE A CG1 1 
ATOM   1089 C  CG2 . ILE A 1 149 ? 60.567 40.381 2.119   1.00 15.59 ? 149 ILE A CG2 1 
ATOM   1090 C  CD1 . ILE A 1 149 ? 59.156 37.461 2.013   1.00 15.79 ? 149 ILE A CD1 1 
ATOM   1091 N  N   . GLY A 1 150 ? 59.033 43.490 2.270   1.00 15.69 ? 150 GLY A N   1 
ATOM   1092 C  CA  . GLY A 1 150 ? 59.488 44.744 1.706   1.00 14.82 ? 150 GLY A CA  1 
ATOM   1093 C  C   . GLY A 1 150 ? 60.924 45.091 2.038   1.00 16.53 ? 150 GLY A C   1 
ATOM   1094 O  O   . GLY A 1 150 ? 61.559 44.467 2.895   1.00 17.28 ? 150 GLY A O   1 
ATOM   1095 N  N   . ILE A 1 151 ? 61.447 46.072 1.317   1.00 16.25 ? 151 ILE A N   1 
ATOM   1096 C  CA  . ILE A 1 151 ? 62.800 46.569 1.516   1.00 18.06 ? 151 ILE A CA  1 
ATOM   1097 C  C   . ILE A 1 151 ? 62.907 47.382 2.833   1.00 17.03 ? 151 ILE A C   1 
ATOM   1098 O  O   . ILE A 1 151 ? 62.001 48.134 3.199   1.00 17.01 ? 151 ILE A O   1 
ATOM   1099 C  CB  . ILE A 1 151 ? 63.240 47.397 0.281   1.00 17.61 ? 151 ILE A CB  1 
ATOM   1100 C  CG1 . ILE A 1 151 ? 63.276 46.474 -0.935  1.00 19.49 ? 151 ILE A CG1 1 
ATOM   1101 C  CG2 . ILE A 1 151 ? 64.607 48.050 0.506   1.00 17.50 ? 151 ILE A CG2 1 
ATOM   1102 C  CD1 . ILE A 1 151 ? 63.108 47.180 -2.263  1.00 19.59 ? 151 ILE A CD1 1 
ATOM   1103 N  N   . ALA A 1 152 ? 63.980 47.152 3.580   1.00 16.10 ? 152 ALA A N   1 
ATOM   1104 C  CA  . ALA A 1 152 ? 64.197 47.825 4.852   1.00 16.29 ? 152 ALA A CA  1 
ATOM   1105 C  C   . ALA A 1 152 ? 65.593 48.440 4.964   1.00 17.15 ? 152 ALA A C   1 
ATOM   1106 O  O   . ALA A 1 152 ? 66.462 48.203 4.133   1.00 18.93 ? 152 ALA A O   1 
ATOM   1107 C  CB  . ALA A 1 152 ? 63.964 46.850 6.006   1.00 11.83 ? 152 ALA A CB  1 
ATOM   1108 N  N   . GLN A 1 153 ? 65.780 49.270 5.983   1.00 20.50 ? 153 GLN A N   1 
ATOM   1109 C  CA  . GLN A 1 153 ? 67.065 49.911 6.248   1.00 21.73 ? 153 GLN A CA  1 
ATOM   1110 C  C   . GLN A 1 153 ? 67.657 49.379 7.580   1.00 23.10 ? 153 GLN A C   1 
ATOM   1111 O  O   . GLN A 1 153 ? 68.851 49.606 7.843   1.00 25.96 ? 153 GLN A O   1 
ATOM   1112 C  CB  . GLN A 1 153 ? 66.905 51.442 6.288   1.00 20.21 ? 153 GLN A CB  1 
ATOM   1113 C  CG  . GLN A 1 153 ? 65.832 51.957 7.230   1.00 17.13 ? 153 GLN A CG  1 
ATOM   1114 C  CD  . GLN A 1 153 ? 66.046 53.416 7.653   1.00 18.66 ? 153 GLN A CD  1 
ATOM   1115 O  OE1 . GLN A 1 153 ? 67.173 53.913 7.675   1.00 18.52 ? 153 GLN A OE1 1 
ATOM   1116 N  NE2 . GLN A 1 153 ? 64.972 54.080 8.046   1.00 16.35 ? 153 GLN A NE2 1 
ATOM   1117 O  OXT . GLN A 1 153 ? 66.932 48.730 8.372   1.00 24.89 ? 153 GLN A OXT 1 
ATOM   1118 N  N   . ALA B 1 1   ? 55.253 40.773 -19.342 1.00 47.94 ? 1   ALA B N   1 
ATOM   1119 C  CA  . ALA B 1 1   ? 54.365 41.738 -18.624 1.00 47.38 ? 1   ALA B CA  1 
ATOM   1120 C  C   . ALA B 1 1   ? 54.463 41.460 -17.136 1.00 45.84 ? 1   ALA B C   1 
ATOM   1121 O  O   . ALA B 1 1   ? 54.463 40.302 -16.721 1.00 47.47 ? 1   ALA B O   1 
ATOM   1122 C  CB  . ALA B 1 1   ? 52.914 41.577 -19.081 1.00 48.44 ? 1   ALA B CB  1 
ATOM   1123 N  N   . THR B 1 2   ? 54.586 42.515 -16.344 1.00 43.57 ? 2   THR B N   1 
ATOM   1124 C  CA  . THR B 1 2   ? 54.664 42.367 -14.902 1.00 39.67 ? 2   THR B CA  1 
ATOM   1125 C  C   . THR B 1 2   ? 53.487 43.116 -14.303 1.00 35.09 ? 2   THR B C   1 
ATOM   1126 O  O   . THR B 1 2   ? 53.030 44.119 -14.843 1.00 34.27 ? 2   THR B O   1 
ATOM   1127 C  CB  . THR B 1 2   ? 55.969 42.942 -14.327 1.00 41.08 ? 2   THR B CB  1 
ATOM   1128 O  OG1 . THR B 1 2   ? 57.007 42.863 -15.308 1.00 46.32 ? 2   THR B OG1 1 
ATOM   1129 C  CG2 . THR B 1 2   ? 56.391 42.160 -13.090 1.00 43.87 ? 2   THR B CG2 1 
ATOM   1130 N  N   . LYS B 1 3   ? 52.953 42.566 -13.232 1.00 31.45 ? 3   LYS B N   1 
ATOM   1131 C  CA  . LYS B 1 3   ? 51.841 43.163 -12.532 1.00 29.85 ? 3   LYS B CA  1 
ATOM   1132 C  C   . LYS B 1 3   ? 52.315 43.297 -11.099 1.00 25.42 ? 3   LYS B C   1 
ATOM   1133 O  O   . LYS B 1 3   ? 53.172 42.524 -10.639 1.00 22.45 ? 3   LYS B O   1 
ATOM   1134 C  CB  . LYS B 1 3   ? 50.627 42.233 -12.558 1.00 33.64 ? 3   LYS B CB  1 
ATOM   1135 C  CG  . LYS B 1 3   ? 49.471 42.731 -13.384 1.00 43.41 ? 3   LYS B CG  1 
ATOM   1136 C  CD  . LYS B 1 3   ? 49.834 42.689 -14.844 1.00 47.49 ? 3   LYS B CD  1 
ATOM   1137 C  CE  . LYS B 1 3   ? 49.991 41.252 -15.309 1.00 51.81 ? 3   LYS B CE  1 
ATOM   1138 N  NZ  . LYS B 1 3   ? 48.687 40.509 -15.260 1.00 55.09 ? 3   LYS B NZ  1 
ATOM   1139 N  N   . ALA B 1 4   ? 51.753 44.265 -10.398 1.00 21.30 ? 4   ALA B N   1 
ATOM   1140 C  CA  . ALA B 1 4   ? 52.081 44.488 -9.003  1.00 20.20 ? 4   ALA B CA  1 
ATOM   1141 C  C   . ALA B 1 4   ? 50.772 44.962 -8.409  1.00 18.31 ? 4   ALA B C   1 
ATOM   1142 O  O   . ALA B 1 4   ? 49.903 45.427 -9.138  1.00 19.17 ? 4   ALA B O   1 
ATOM   1143 C  CB  . ALA B 1 4   ? 53.181 45.546 -8.865  1.00 20.82 ? 4   ALA B CB  1 
ATOM   1144 N  N   . VAL B 1 5   ? 50.587 44.768 -7.114  1.00 16.64 ? 5   VAL B N   1 
ATOM   1145 C  CA  . VAL B 1 5   ? 49.355 45.177 -6.473  1.00 17.88 ? 5   VAL B CA  1 
ATOM   1146 C  C   . VAL B 1 5   ? 49.718 45.757 -5.126  1.00 18.19 ? 5   VAL B C   1 
ATOM   1147 O  O   . VAL B 1 5   ? 50.768 45.426 -4.571  1.00 19.87 ? 5   VAL B O   1 
ATOM   1148 C  CB  . VAL B 1 5   ? 48.347 43.987 -6.328  1.00 17.73 ? 5   VAL B CB  1 
ATOM   1149 C  CG1 . VAL B 1 5   ? 48.842 42.948 -5.338  1.00 16.05 ? 5   VAL B CG1 1 
ATOM   1150 C  CG2 . VAL B 1 5   ? 46.979 44.504 -5.932  1.00 18.75 ? 5   VAL B CG2 1 
ATOM   1151 N  N   . CYS B 1 6   ? 48.880 46.648 -4.621  1.00 18.06 ? 6   CYS B N   1 
ATOM   1152 C  CA  . CYS B 1 6   ? 49.126 47.282 -3.335  1.00 17.15 ? 6   CYS B CA  1 
ATOM   1153 C  C   . CYS B 1 6   ? 47.806 47.468 -2.626  1.00 15.74 ? 6   CYS B C   1 
ATOM   1154 O  O   . CYS B 1 6   ? 46.856 47.952 -3.227  1.00 16.65 ? 6   CYS B O   1 
ATOM   1155 C  CB  . CYS B 1 6   ? 49.770 48.654 -3.555  1.00 16.68 ? 6   CYS B CB  1 
ATOM   1156 S  SG  . CYS B 1 6   ? 50.219 49.424 -2.055  1.00 20.83 ? 6   CYS B SG  1 
ATOM   1157 N  N   . VAL B 1 7   ? 47.740 47.066 -1.365  1.00 16.24 ? 7   VAL B N   1 
ATOM   1158 C  CA  . VAL B 1 7   ? 46.535 47.225 -0.567  1.00 15.40 ? 7   VAL B CA  1 
ATOM   1159 C  C   . VAL B 1 7   ? 46.877 48.310 0.433   1.00 15.22 ? 7   VAL B C   1 
ATOM   1160 O  O   . VAL B 1 7   ? 47.812 48.168 1.195   1.00 15.12 ? 7   VAL B O   1 
ATOM   1161 C  CB  . VAL B 1 7   ? 46.169 45.935 0.169   1.00 16.89 ? 7   VAL B CB  1 
ATOM   1162 C  CG1 . VAL B 1 7   ? 44.921 46.147 1.012   1.00 19.10 ? 7   VAL B CG1 1 
ATOM   1163 C  CG2 . VAL B 1 7   ? 45.948 44.823 -0.819  1.00 17.13 ? 7   VAL B CG2 1 
ATOM   1164 N  N   . LEU B 1 8   ? 46.162 49.426 0.348   1.00 16.61 ? 8   LEU B N   1 
ATOM   1165 C  CA  . LEU B 1 8   ? 46.364 50.594 1.199   1.00 17.05 ? 8   LEU B CA  1 
ATOM   1166 C  C   . LEU B 1 8   ? 45.500 50.551 2.442   1.00 16.85 ? 8   LEU B C   1 
ATOM   1167 O  O   . LEU B 1 8   ? 44.289 50.375 2.365   1.00 17.53 ? 8   LEU B O   1 
ATOM   1168 C  CB  . LEU B 1 8   ? 46.056 51.865 0.418   1.00 16.45 ? 8   LEU B CB  1 
ATOM   1169 C  CG  . LEU B 1 8   ? 46.949 52.126 -0.789  1.00 18.29 ? 8   LEU B CG  1 
ATOM   1170 C  CD1 . LEU B 1 8   ? 46.352 53.158 -1.684  1.00 20.72 ? 8   LEU B CD1 1 
ATOM   1171 C  CD2 . LEU B 1 8   ? 48.267 52.601 -0.309  1.00 18.36 ? 8   LEU B CD2 1 
ATOM   1172 N  N   . LYS B 1 9   ? 46.131 50.772 3.584   1.00 16.04 ? 9   LYS B N   1 
ATOM   1173 C  CA  . LYS B 1 9   ? 45.444 50.750 4.853   1.00 20.80 ? 9   LYS B CA  1 
ATOM   1174 C  C   . LYS B 1 9   ? 46.217 51.726 5.732   1.00 18.76 ? 9   LYS B C   1 
ATOM   1175 O  O   . LYS B 1 9   ? 47.393 51.964 5.482   1.00 17.60 ? 9   LYS B O   1 
ATOM   1176 C  CB  . LYS B 1 9   ? 45.479 49.311 5.386   1.00 25.87 ? 9   LYS B CB  1 
ATOM   1177 C  CG  . LYS B 1 9   ? 44.939 49.092 6.789   1.00 39.39 ? 9   LYS B CG  1 
ATOM   1178 C  CD  . LYS B 1 9   ? 46.050 49.204 7.893   1.00 47.97 ? 9   LYS B CD  1 
ATOM   1179 C  CE  . LYS B 1 9   ? 45.581 48.677 9.266   1.00 48.09 ? 9   LYS B CE  1 
ATOM   1180 N  NZ  . LYS B 1 9   ? 44.256 49.265 9.690   1.00 50.84 ? 9   LYS B NZ  1 
ATOM   1181 N  N   . GLY B 1 10  ? 45.560 52.329 6.717   1.00 20.01 ? 10  GLY B N   1 
ATOM   1182 C  CA  . GLY B 1 10  ? 46.235 53.285 7.584   1.00 18.23 ? 10  GLY B CA  1 
ATOM   1183 C  C   . GLY B 1 10  ? 45.685 53.299 8.997   1.00 20.00 ? 10  GLY B C   1 
ATOM   1184 O  O   . GLY B 1 10  ? 45.060 52.344 9.433   1.00 21.31 ? 10  GLY B O   1 
ATOM   1185 N  N   . ASP B 1 11  ? 45.941 54.372 9.733   1.00 21.45 ? 11  ASP B N   1 
ATOM   1186 C  CA  . ASP B 1 11  ? 45.461 54.483 11.110  1.00 25.97 ? 11  ASP B CA  1 
ATOM   1187 C  C   . ASP B 1 11  ? 43.989 54.857 11.180  1.00 25.82 ? 11  ASP B C   1 
ATOM   1188 O  O   . ASP B 1 11  ? 43.334 54.651 12.209  1.00 26.66 ? 11  ASP B O   1 
ATOM   1189 C  CB  . ASP B 1 11  ? 46.294 55.510 11.893  1.00 28.32 ? 11  ASP B CB  1 
ATOM   1190 C  CG  . ASP B 1 11  ? 47.714 55.039 12.136  1.00 31.72 ? 11  ASP B CG  1 
ATOM   1191 O  OD1 . ASP B 1 11  ? 47.888 53.899 12.630  1.00 35.08 ? 11  ASP B OD1 1 
ATOM   1192 O  OD2 . ASP B 1 11  ? 48.653 55.791 11.795  1.00 34.32 ? 11  ASP B OD2 1 
ATOM   1193 N  N   . GLY B 1 12  ? 43.490 55.428 10.085  1.00 24.40 ? 12  GLY B N   1 
ATOM   1194 C  CA  . GLY B 1 12  ? 42.112 55.847 10.023  1.00 21.79 ? 12  GLY B CA  1 
ATOM   1195 C  C   . GLY B 1 12  ? 41.298 54.967 9.107   1.00 19.51 ? 12  GLY B C   1 
ATOM   1196 O  O   . GLY B 1 12  ? 41.640 53.810 8.888   1.00 19.87 ? 12  GLY B O   1 
ATOM   1197 N  N   . PRO B 1 13  ? 40.220 55.512 8.539   1.00 19.02 ? 13  PRO B N   1 
ATOM   1198 C  CA  . PRO B 1 13  ? 39.303 54.812 7.635   1.00 20.50 ? 13  PRO B CA  1 
ATOM   1199 C  C   . PRO B 1 13  ? 39.713 54.650 6.161   1.00 19.90 ? 13  PRO B C   1 
ATOM   1200 O  O   . PRO B 1 13  ? 39.074 53.910 5.405   1.00 20.18 ? 13  PRO B O   1 
ATOM   1201 C  CB  . PRO B 1 13  ? 38.043 55.639 7.778   1.00 17.77 ? 13  PRO B CB  1 
ATOM   1202 C  CG  . PRO B 1 13  ? 38.600 57.023 7.848   1.00 19.39 ? 13  PRO B CG  1 
ATOM   1203 C  CD  . PRO B 1 13  ? 39.753 56.882 8.803   1.00 17.55 ? 13  PRO B CD  1 
ATOM   1204 N  N   . VAL B 1 14  ? 40.762 55.348 5.746   1.00 19.41 ? 14  VAL B N   1 
ATOM   1205 C  CA  . VAL B 1 14  ? 41.215 55.277 4.362   1.00 20.88 ? 14  VAL B CA  1 
ATOM   1206 C  C   . VAL B 1 14  ? 41.716 53.893 3.940   1.00 21.79 ? 14  VAL B C   1 
ATOM   1207 O  O   . VAL B 1 14  ? 42.536 53.280 4.622   1.00 20.80 ? 14  VAL B O   1 
ATOM   1208 C  CB  . VAL B 1 14  ? 42.315 56.332 4.098   1.00 18.18 ? 14  VAL B CB  1 
ATOM   1209 C  CG1 . VAL B 1 14  ? 42.743 56.307 2.650   1.00 17.16 ? 14  VAL B CG1 1 
ATOM   1210 C  CG2 . VAL B 1 14  ? 41.803 57.701 4.488   1.00 14.45 ? 14  VAL B CG2 1 
ATOM   1211 N  N   . GLN B 1 15  ? 41.184 53.386 2.834   1.00 23.46 ? 15  GLN B N   1 
ATOM   1212 C  CA  . GLN B 1 15  ? 41.614 52.097 2.301   1.00 26.63 ? 15  GLN B CA  1 
ATOM   1213 C  C   . GLN B 1 15  ? 41.431 52.028 0.797   1.00 24.37 ? 15  GLN B C   1 
ATOM   1214 O  O   . GLN B 1 15  ? 40.588 52.712 0.238   1.00 26.65 ? 15  GLN B O   1 
ATOM   1215 C  CB  . GLN B 1 15  ? 40.865 50.953 2.964   1.00 33.66 ? 15  GLN B CB  1 
ATOM   1216 C  CG  . GLN B 1 15  ? 39.368 51.068 2.861   1.00 43.69 ? 15  GLN B CG  1 
ATOM   1217 C  CD  . GLN B 1 15  ? 38.692 49.773 3.222   1.00 51.84 ? 15  GLN B CD  1 
ATOM   1218 O  OE1 . GLN B 1 15  ? 38.098 49.102 2.368   1.00 56.91 ? 15  GLN B OE1 1 
ATOM   1219 N  NE2 . GLN B 1 15  ? 38.815 49.384 4.490   1.00 53.50 ? 15  GLN B NE2 1 
ATOM   1220 N  N   . GLY B 1 16  ? 42.210 51.194 0.130   1.00 23.15 ? 16  GLY B N   1 
ATOM   1221 C  CA  . GLY B 1 16  ? 42.072 51.096 -1.306  1.00 20.99 ? 16  GLY B CA  1 
ATOM   1222 C  C   . GLY B 1 16  ? 42.939 50.005 -1.872  1.00 20.81 ? 16  GLY B C   1 
ATOM   1223 O  O   . GLY B 1 16  ? 43.666 49.348 -1.130  1.00 19.70 ? 16  GLY B O   1 
ATOM   1224 N  N   . ILE B 1 17  ? 42.850 49.806 -3.184  1.00 22.51 ? 17  ILE B N   1 
ATOM   1225 C  CA  . ILE B 1 17  ? 43.628 48.793 -3.904  1.00 22.85 ? 17  ILE B CA  1 
ATOM   1226 C  C   . ILE B 1 17  ? 44.144 49.461 -5.183  1.00 21.28 ? 17  ILE B C   1 
ATOM   1227 O  O   . ILE B 1 17  ? 43.359 50.038 -5.936  1.00 22.84 ? 17  ILE B O   1 
ATOM   1228 C  CB  . ILE B 1 17  ? 42.756 47.559 -4.333  1.00 23.32 ? 17  ILE B CB  1 
ATOM   1229 C  CG1 . ILE B 1 17  ? 41.930 47.026 -3.171  1.00 24.99 ? 17  ILE B CG1 1 
ATOM   1230 C  CG2 . ILE B 1 17  ? 43.648 46.429 -4.837  1.00 23.67 ? 17  ILE B CG2 1 
ATOM   1231 C  CD1 . ILE B 1 17  ? 42.737 46.304 -2.135  1.00 30.60 ? 17  ILE B CD1 1 
ATOM   1232 N  N   . ILE B 1 18  ? 45.460 49.439 -5.390  1.00 19.83 ? 18  ILE B N   1 
ATOM   1233 C  CA  . ILE B 1 18  ? 46.084 50.017 -6.571  1.00 19.47 ? 18  ILE B CA  1 
ATOM   1234 C  C   . ILE B 1 18  ? 46.842 48.894 -7.279  1.00 20.75 ? 18  ILE B C   1 
ATOM   1235 O  O   . ILE B 1 18  ? 47.559 48.121 -6.640  1.00 21.09 ? 18  ILE B O   1 
ATOM   1236 C  CB  . ILE B 1 18  ? 47.068 51.181 -6.225  1.00 17.85 ? 18  ILE B CB  1 
ATOM   1237 C  CG1 . ILE B 1 18  ? 46.342 52.518 -6.137  1.00 21.76 ? 18  ILE B CG1 1 
ATOM   1238 C  CG2 . ILE B 1 18  ? 47.988 51.436 -7.386  1.00 15.89 ? 18  ILE B CG2 1 
ATOM   1239 C  CD1 . ILE B 1 18  ? 45.232 52.569 -5.231  1.00 24.21 ? 18  ILE B CD1 1 
ATOM   1240 N  N   . ASN B 1 19  ? 46.592 48.760 -8.582  1.00 21.39 ? 19  ASN B N   1 
ATOM   1241 C  CA  . ASN B 1 19  ? 47.223 47.765 -9.444  1.00 19.67 ? 19  ASN B CA  1 
ATOM   1242 C  C   . ASN B 1 19  ? 48.218 48.460 -10.341 1.00 18.45 ? 19  ASN B C   1 
ATOM   1243 O  O   . ASN B 1 19  ? 48.024 49.613 -10.715 1.00 20.44 ? 19  ASN B O   1 
ATOM   1244 C  CB  . ASN B 1 19  ? 46.191 47.090 -10.335 1.00 21.86 ? 19  ASN B CB  1 
ATOM   1245 C  CG  . ASN B 1 19  ? 45.101 46.421 -9.556  1.00 22.52 ? 19  ASN B CG  1 
ATOM   1246 O  OD1 . ASN B 1 19  ? 44.022 46.988 -9.372  1.00 26.98 ? 19  ASN B OD1 1 
ATOM   1247 N  ND2 . ASN B 1 19  ? 45.365 45.206 -9.093  1.00 25.76 ? 19  ASN B ND2 1 
ATOM   1248 N  N   . PHE B 1 20  ? 49.258 47.732 -10.723 1.00 17.77 ? 20  PHE B N   1 
ATOM   1249 C  CA  . PHE B 1 20  ? 50.310 48.247 -11.571 1.00 16.59 ? 20  PHE B CA  1 
ATOM   1250 C  C   . PHE B 1 20  ? 50.517 47.227 -12.667 1.00 20.16 ? 20  PHE B C   1 
ATOM   1251 O  O   . PHE B 1 20  ? 50.501 46.027 -12.412 1.00 21.92 ? 20  PHE B O   1 
ATOM   1252 C  CB  . PHE B 1 20  ? 51.638 48.358 -10.797 1.00 15.87 ? 20  PHE B CB  1 
ATOM   1253 C  CG  . PHE B 1 20  ? 51.580 49.215 -9.553  1.00 15.40 ? 20  PHE B CG  1 
ATOM   1254 C  CD1 . PHE B 1 20  ? 50.994 48.738 -8.384  1.00 16.29 ? 20  PHE B CD1 1 
ATOM   1255 C  CD2 . PHE B 1 20  ? 52.136 50.487 -9.553  1.00 15.59 ? 20  PHE B CD2 1 
ATOM   1256 C  CE1 . PHE B 1 20  ? 50.962 49.511 -7.223  1.00 17.98 ? 20  PHE B CE1 1 
ATOM   1257 C  CE2 . PHE B 1 20  ? 52.114 51.277 -8.396  1.00 18.46 ? 20  PHE B CE2 1 
ATOM   1258 C  CZ  . PHE B 1 20  ? 51.526 50.787 -7.227  1.00 17.11 ? 20  PHE B CZ  1 
ATOM   1259 N  N   . GLU B 1 21  ? 50.735 47.688 -13.884 1.00 22.73 ? 21  GLU B N   1 
ATOM   1260 C  CA  . GLU B 1 21  ? 50.997 46.778 -14.979 1.00 25.84 ? 21  GLU B CA  1 
ATOM   1261 C  C   . GLU B 1 21  ? 52.029 47.392 -15.882 1.00 26.59 ? 21  GLU B C   1 
ATOM   1262 O  O   . GLU B 1 21  ? 51.916 48.553 -16.265 1.00 27.34 ? 21  GLU B O   1 
ATOM   1263 C  CB  . GLU B 1 21  ? 49.746 46.507 -15.780 1.00 28.76 ? 21  GLU B CB  1 
ATOM   1264 C  CG  . GLU B 1 21  ? 50.009 45.577 -16.931 1.00 39.44 ? 21  GLU B CG  1 
ATOM   1265 C  CD  . GLU B 1 21  ? 48.802 45.410 -17.828 1.00 46.06 ? 21  GLU B CD  1 
ATOM   1266 O  OE1 . GLU B 1 21  ? 47.776 44.861 -17.350 1.00 47.89 ? 21  GLU B OE1 1 
ATOM   1267 O  OE2 . GLU B 1 21  ? 48.889 45.835 -19.007 1.00 49.91 ? 21  GLU B OE2 1 
ATOM   1268 N  N   . GLN B 1 22  ? 53.071 46.636 -16.169 1.00 28.95 ? 22  GLN B N   1 
ATOM   1269 C  CA  . GLN B 1 22  ? 54.114 47.100 -17.055 1.00 32.50 ? 22  GLN B CA  1 
ATOM   1270 C  C   . GLN B 1 22  ? 54.203 46.087 -18.182 1.00 38.37 ? 22  GLN B C   1 
ATOM   1271 O  O   . GLN B 1 22  ? 54.782 45.012 -18.032 1.00 36.82 ? 22  GLN B O   1 
ATOM   1272 C  CB  . GLN B 1 22  ? 55.445 47.228 -16.325 1.00 28.11 ? 22  GLN B CB  1 
ATOM   1273 C  CG  . GLN B 1 22  ? 56.547 47.834 -17.176 1.00 24.91 ? 22  GLN B CG  1 
ATOM   1274 C  CD  . GLN B 1 22  ? 57.802 48.124 -16.398 1.00 22.71 ? 22  GLN B CD  1 
ATOM   1275 O  OE1 . GLN B 1 22  ? 58.441 49.134 -16.611 1.00 25.29 ? 22  GLN B OE1 1 
ATOM   1276 N  NE2 . GLN B 1 22  ? 58.168 47.234 -15.496 1.00 24.34 ? 22  GLN B NE2 1 
ATOM   1277 N  N   . LYS B 1 23  ? 53.543 46.424 -19.284 1.00 48.43 ? 23  LYS B N   1 
ATOM   1278 C  CA  . LYS B 1 23  ? 53.484 45.599 -20.488 1.00 56.67 ? 23  LYS B CA  1 
ATOM   1279 C  C   . LYS B 1 23  ? 54.866 45.085 -20.863 1.00 61.15 ? 23  LYS B C   1 
ATOM   1280 O  O   . LYS B 1 23  ? 55.842 45.833 -20.813 1.00 59.43 ? 23  LYS B O   1 
ATOM   1281 C  CB  . LYS B 1 23  ? 52.913 46.415 -21.651 1.00 59.27 ? 23  LYS B CB  1 
ATOM   1282 C  CG  . LYS B 1 23  ? 52.506 45.606 -22.879 1.00 63.80 ? 23  LYS B CG  1 
ATOM   1283 C  CD  . LYS B 1 23  ? 51.149 44.929 -22.685 1.00 66.32 ? 23  LYS B CD  1 
ATOM   1284 C  CE  . LYS B 1 23  ? 51.280 43.410 -22.579 1.00 68.27 ? 23  LYS B CE  1 
ATOM   1285 N  NZ  . LYS B 1 23  ? 52.067 42.988 -21.388 1.00 67.83 ? 23  LYS B NZ  1 
ATOM   1286 N  N   . GLU B 1 24  ? 54.911 43.797 -21.214 1.00 67.60 ? 24  GLU B N   1 
ATOM   1287 C  CA  . GLU B 1 24  ? 56.120 43.055 -21.613 1.00 74.59 ? 24  GLU B CA  1 
ATOM   1288 C  C   . GLU B 1 24  ? 57.253 43.926 -22.192 1.00 75.85 ? 24  GLU B C   1 
ATOM   1289 O  O   . GLU B 1 24  ? 57.578 43.864 -23.387 1.00 76.98 ? 24  GLU B O   1 
ATOM   1290 C  CB  . GLU B 1 24  ? 55.720 41.914 -22.588 1.00 78.60 ? 24  GLU B CB  1 
ATOM   1291 C  CG  . GLU B 1 24  ? 56.812 40.870 -22.931 1.00 82.95 ? 24  GLU B CG  1 
ATOM   1292 C  CD  . GLU B 1 24  ? 57.544 41.170 -24.245 1.00 85.37 ? 24  GLU B CD  1 
ATOM   1293 O  OE1 . GLU B 1 24  ? 56.878 41.194 -25.311 1.00 86.52 ? 24  GLU B OE1 1 
ATOM   1294 O  OE2 . GLU B 1 24  ? 58.783 41.390 -24.206 1.00 86.47 ? 24  GLU B OE2 1 
ATOM   1295 N  N   . SER B 1 25  ? 57.851 44.726 -21.315 1.00 75.33 ? 25  SER B N   1 
ATOM   1296 C  CA  . SER B 1 25  ? 58.928 45.620 -21.682 1.00 73.84 ? 25  SER B CA  1 
ATOM   1297 C  C   . SER B 1 25  ? 59.200 46.504 -20.486 1.00 72.33 ? 25  SER B C   1 
ATOM   1298 O  O   . SER B 1 25  ? 58.480 46.466 -19.480 1.00 72.33 ? 25  SER B O   1 
ATOM   1299 C  CB  . SER B 1 25  ? 58.514 46.498 -22.882 1.00 74.75 ? 25  SER B CB  1 
ATOM   1300 O  OG  . SER B 1 25  ? 57.303 47.202 -22.633 1.00 74.47 ? 25  SER B OG  1 
ATOM   1301 N  N   . ASN B 1 26  ? 60.267 47.277 -20.598 1.00 70.20 ? 26  ASN B N   1 
ATOM   1302 C  CA  . ASN B 1 26  ? 60.649 48.220 -19.570 1.00 66.93 ? 26  ASN B CA  1 
ATOM   1303 C  C   . ASN B 1 26  ? 60.124 49.561 -20.112 1.00 61.92 ? 26  ASN B C   1 
ATOM   1304 O  O   . ASN B 1 26  ? 60.887 50.473 -20.437 1.00 60.46 ? 26  ASN B O   1 
ATOM   1305 C  CB  . ASN B 1 26  ? 62.170 48.205 -19.424 1.00 73.19 ? 26  ASN B CB  1 
ATOM   1306 C  CG  . ASN B 1 26  ? 62.678 49.120 -18.315 1.00 77.98 ? 26  ASN B CG  1 
ATOM   1307 O  OD1 . ASN B 1 26  ? 63.622 49.895 -18.529 1.00 80.90 ? 26  ASN B OD1 1 
ATOM   1308 N  ND2 . ASN B 1 26  ? 62.106 48.996 -17.115 1.00 79.56 ? 26  ASN B ND2 1 
ATOM   1309 N  N   . GLY B 1 27  ? 58.809 49.603 -20.322 1.00 55.80 ? 27  GLY B N   1 
ATOM   1310 C  CA  . GLY B 1 27  ? 58.154 50.795 -20.829 1.00 48.06 ? 27  GLY B CA  1 
ATOM   1311 C  C   . GLY B 1 27  ? 57.399 51.487 -19.711 1.00 42.57 ? 27  GLY B C   1 
ATOM   1312 O  O   . GLY B 1 27  ? 57.816 51.416 -18.559 1.00 43.17 ? 27  GLY B O   1 
ATOM   1313 N  N   . PRO B 1 28  ? 56.284 52.167 -20.004 1.00 38.22 ? 28  PRO B N   1 
ATOM   1314 C  CA  . PRO B 1 28  ? 55.545 52.844 -18.939 1.00 34.69 ? 28  PRO B CA  1 
ATOM   1315 C  C   . PRO B 1 28  ? 54.776 51.869 -18.061 1.00 31.08 ? 28  PRO B C   1 
ATOM   1316 O  O   . PRO B 1 28  ? 54.471 50.738 -18.469 1.00 29.58 ? 28  PRO B O   1 
ATOM   1317 C  CB  . PRO B 1 28  ? 54.602 53.760 -19.714 1.00 35.89 ? 28  PRO B CB  1 
ATOM   1318 C  CG  . PRO B 1 28  ? 54.273 52.951 -20.895 1.00 37.36 ? 28  PRO B CG  1 
ATOM   1319 C  CD  . PRO B 1 28  ? 55.618 52.368 -21.302 1.00 38.49 ? 28  PRO B CD  1 
ATOM   1320 N  N   . VAL B 1 29  ? 54.494 52.313 -16.845 1.00 26.69 ? 29  VAL B N   1 
ATOM   1321 C  CA  . VAL B 1 29  ? 53.748 51.522 -15.896 1.00 23.55 ? 29  VAL B CA  1 
ATOM   1322 C  C   . VAL B 1 29  ? 52.364 52.140 -15.784 1.00 21.71 ? 29  VAL B C   1 
ATOM   1323 O  O   . VAL B 1 29  ? 52.222 53.364 -15.661 1.00 23.27 ? 29  VAL B O   1 
ATOM   1324 C  CB  . VAL B 1 29  ? 54.443 51.513 -14.500 1.00 21.99 ? 29  VAL B CB  1 
ATOM   1325 C  CG1 . VAL B 1 29  ? 53.717 50.537 -13.554 1.00 20.43 ? 29  VAL B CG1 1 
ATOM   1326 C  CG2 . VAL B 1 29  ? 55.894 51.117 -14.637 1.00 20.44 ? 29  VAL B CG2 1 
ATOM   1327 N  N   . LYS B 1 30  ? 51.344 51.309 -15.903 1.00 21.45 ? 30  LYS B N   1 
ATOM   1328 C  CA  . LYS B 1 30  ? 49.971 51.776 -15.768 1.00 24.43 ? 30  LYS B CA  1 
ATOM   1329 C  C   . LYS B 1 30  ? 49.554 51.517 -14.333 1.00 22.80 ? 30  LYS B C   1 
ATOM   1330 O  O   . LYS B 1 30  ? 49.703 50.404 -13.842 1.00 24.21 ? 30  LYS B O   1 
ATOM   1331 C  CB  . LYS B 1 30  ? 49.056 51.032 -16.733 1.00 26.64 ? 30  LYS B CB  1 
ATOM   1332 C  CG  . LYS B 1 30  ? 49.402 51.313 -18.185 1.00 35.40 ? 30  LYS B CG  1 
ATOM   1333 C  CD  . LYS B 1 30  ? 48.995 50.164 -19.118 1.00 42.50 ? 30  LYS B CD  1 
ATOM   1334 C  CE  . LYS B 1 30  ? 50.021 49.010 -19.096 1.00 44.36 ? 30  LYS B CE  1 
ATOM   1335 N  NZ  . LYS B 1 30  ? 51.398 49.465 -19.475 1.00 42.45 ? 30  LYS B NZ  1 
ATOM   1336 N  N   . VAL B 1 31  ? 49.105 52.562 -13.646 1.00 22.45 ? 31  VAL B N   1 
ATOM   1337 C  CA  . VAL B 1 31  ? 48.675 52.470 -12.250 1.00 20.31 ? 31  VAL B CA  1 
ATOM   1338 C  C   . VAL B 1 31  ? 47.187 52.777 -12.219 1.00 20.55 ? 31  VAL B C   1 
ATOM   1339 O  O   . VAL B 1 31  ? 46.761 53.811 -12.735 1.00 21.02 ? 31  VAL B O   1 
ATOM   1340 C  CB  . VAL B 1 31  ? 49.384 53.534 -11.385 1.00 19.82 ? 31  VAL B CB  1 
ATOM   1341 C  CG1 . VAL B 1 31  ? 49.115 53.287 -9.920  1.00 21.85 ? 31  VAL B CG1 1 
ATOM   1342 C  CG2 . VAL B 1 31  ? 50.872 53.586 -11.684 1.00 17.73 ? 31  VAL B CG2 1 
ATOM   1343 N  N   . TRP B 1 32  ? 46.393 51.918 -11.596 1.00 19.48 ? 32  TRP B N   1 
ATOM   1344 C  CA  . TRP B 1 32  ? 44.952 52.161 -11.539 1.00 22.68 ? 32  TRP B CA  1 
ATOM   1345 C  C   . TRP B 1 32  ? 44.280 51.448 -10.375 1.00 22.15 ? 32  TRP B C   1 
ATOM   1346 O  O   . TRP B 1 32  ? 44.787 50.452 -9.887  1.00 24.79 ? 32  TRP B O   1 
ATOM   1347 C  CB  . TRP B 1 32  ? 44.302 51.725 -12.858 1.00 25.93 ? 32  TRP B CB  1 
ATOM   1348 C  CG  . TRP B 1 32  ? 44.768 50.381 -13.284 1.00 32.28 ? 32  TRP B CG  1 
ATOM   1349 C  CD1 . TRP B 1 32  ? 45.991 50.051 -13.841 1.00 34.64 ? 32  TRP B CD1 1 
ATOM   1350 C  CD2 . TRP B 1 32  ? 44.080 49.153 -13.069 1.00 32.80 ? 32  TRP B CD2 1 
ATOM   1351 N  NE1 . TRP B 1 32  ? 46.105 48.682 -13.960 1.00 34.68 ? 32  TRP B NE1 1 
ATOM   1352 C  CE2 . TRP B 1 32  ? 44.953 48.110 -13.499 1.00 34.46 ? 32  TRP B CE2 1 
ATOM   1353 C  CE3 . TRP B 1 32  ? 42.827 48.832 -12.551 1.00 31.98 ? 32  TRP B CE3 1 
ATOM   1354 C  CZ2 . TRP B 1 32  ? 44.590 46.770 -13.418 1.00 33.65 ? 32  TRP B CZ2 1 
ATOM   1355 C  CZ3 . TRP B 1 32  ? 42.472 47.507 -12.469 1.00 34.48 ? 32  TRP B CZ3 1 
ATOM   1356 C  CH2 . TRP B 1 32  ? 43.352 46.484 -12.901 1.00 36.67 ? 32  TRP B CH2 1 
ATOM   1357 N  N   . GLY B 1 33  ? 43.145 51.965 -9.928  1.00 20.85 ? 33  GLY B N   1 
ATOM   1358 C  CA  . GLY B 1 33  ? 42.417 51.351 -8.836  1.00 19.43 ? 33  GLY B CA  1 
ATOM   1359 C  C   . GLY B 1 33  ? 41.599 52.410 -8.138  1.00 19.11 ? 33  GLY B C   1 
ATOM   1360 O  O   . GLY B 1 33  ? 41.279 53.435 -8.728  1.00 20.47 ? 33  GLY B O   1 
ATOM   1361 N  N   . SER B 1 34  ? 41.275 52.198 -6.876  1.00 19.52 ? 34  SER B N   1 
ATOM   1362 C  CA  . SER B 1 34  ? 40.496 53.187 -6.151  1.00 22.41 ? 34  SER B CA  1 
ATOM   1363 C  C   . SER B 1 34  ? 40.832 53.227 -4.671  1.00 21.57 ? 34  SER B C   1 
ATOM   1364 O  O   . SER B 1 34  ? 41.269 52.229 -4.100  1.00 23.51 ? 34  SER B O   1 
ATOM   1365 C  CB  . SER B 1 34  ? 38.994 52.940 -6.338  1.00 23.80 ? 34  SER B CB  1 
ATOM   1366 O  OG  . SER B 1 34  ? 38.664 51.619 -5.960  1.00 32.56 ? 34  SER B OG  1 
ATOM   1367 N  N   . ILE B 1 35  ? 40.599 54.382 -4.060  1.00 20.04 ? 35  ILE B N   1 
ATOM   1368 C  CA  . ILE B 1 35  ? 40.863 54.594 -2.652  1.00 19.40 ? 35  ILE B CA  1 
ATOM   1369 C  C   . ILE B 1 35  ? 39.581 55.212 -2.113  1.00 20.46 ? 35  ILE B C   1 
ATOM   1370 O  O   . ILE B 1 35  ? 38.998 56.084 -2.749  1.00 21.60 ? 35  ILE B O   1 
ATOM   1371 C  CB  . ILE B 1 35  ? 42.018 55.568 -2.480  1.00 18.31 ? 35  ILE B CB  1 
ATOM   1372 C  CG1 . ILE B 1 35  ? 43.174 55.149 -3.396  1.00 19.04 ? 35  ILE B CG1 1 
ATOM   1373 C  CG2 . ILE B 1 35  ? 42.446 55.614 -1.030  1.00 18.26 ? 35  ILE B CG2 1 
ATOM   1374 C  CD1 . ILE B 1 35  ? 44.352 56.094 -3.414  1.00 21.83 ? 35  ILE B CD1 1 
ATOM   1375 N  N   . LYS B 1 36  ? 39.123 54.737 -0.965  1.00 21.63 ? 36  LYS B N   1 
ATOM   1376 C  CA  . LYS B 1 36  ? 37.891 55.221 -0.365  1.00 23.23 ? 36  LYS B CA  1 
ATOM   1377 C  C   . LYS B 1 36  ? 38.090 55.852 0.995   1.00 23.40 ? 36  LYS B C   1 
ATOM   1378 O  O   . LYS B 1 36  ? 39.148 55.700 1.614   1.00 21.27 ? 36  LYS B O   1 
ATOM   1379 C  CB  . LYS B 1 36  ? 36.906 54.068 -0.246  1.00 27.39 ? 36  LYS B CB  1 
ATOM   1380 C  CG  . LYS B 1 36  ? 36.558 53.461 -1.584  1.00 35.13 ? 36  LYS B CG  1 
ATOM   1381 C  CD  . LYS B 1 36  ? 36.644 51.956 -1.549  1.00 42.38 ? 36  LYS B CD  1 
ATOM   1382 C  CE  . LYS B 1 36  ? 36.231 51.388 -2.894  1.00 47.84 ? 36  LYS B CE  1 
ATOM   1383 N  NZ  . LYS B 1 36  ? 36.485 49.918 -3.030  1.00 53.12 ? 36  LYS B NZ  1 
ATOM   1384 N  N   . ARG B 1 37  ? 37.046 56.554 1.445   1.00 24.28 ? 37  ARG B N   1 
ATOM   1385 C  CA  . ARG B 1 37  ? 36.989 57.247 2.738   1.00 25.39 ? 37  ARG B CA  1 
ATOM   1386 C  C   . ARG B 1 37  ? 37.990 58.388 2.841   1.00 24.81 ? 37  ARG B C   1 
ATOM   1387 O  O   . ARG B 1 37  ? 38.424 58.782 3.924   1.00 24.03 ? 37  ARG B O   1 
ATOM   1388 C  CB  . ARG B 1 37  ? 37.157 56.250 3.884   1.00 27.84 ? 37  ARG B CB  1 
ATOM   1389 C  CG  . ARG B 1 37  ? 36.196 55.086 3.770   1.00 35.79 ? 37  ARG B CG  1 
ATOM   1390 C  CD  . ARG B 1 37  ? 35.490 54.779 5.075   1.00 44.45 ? 37  ARG B CD  1 
ATOM   1391 N  NE  . ARG B 1 37  ? 34.285 53.965 4.876   1.00 52.81 ? 37  ARG B NE  1 
ATOM   1392 C  CZ  . ARG B 1 37  ? 34.265 52.635 4.751   1.00 54.60 ? 37  ARG B CZ  1 
ATOM   1393 N  NH1 . ARG B 1 37  ? 35.395 51.929 4.797   1.00 55.34 ? 37  ARG B NH1 1 
ATOM   1394 N  NH2 . ARG B 1 37  ? 33.099 52.007 4.608   1.00 56.06 ? 37  ARG B NH2 1 
ATOM   1395 N  N   . LEU B 1 38  ? 38.262 58.979 1.692   1.00 24.16 ? 38  LEU B N   1 
ATOM   1396 C  CA  . LEU B 1 38  ? 39.207 60.061 1.567   1.00 24.14 ? 38  LEU B CA  1 
ATOM   1397 C  C   . LEU B 1 38  ? 38.426 61.381 1.642   1.00 25.23 ? 38  LEU B C   1 
ATOM   1398 O  O   . LEU B 1 38  ? 37.263 61.447 1.241   1.00 28.69 ? 38  LEU B O   1 
ATOM   1399 C  CB  . LEU B 1 38  ? 39.895 59.880 0.206   1.00 22.64 ? 38  LEU B CB  1 
ATOM   1400 C  CG  . LEU B 1 38  ? 41.386 60.005 -0.118  1.00 22.64 ? 38  LEU B CG  1 
ATOM   1401 C  CD1 . LEU B 1 38  ? 42.265 59.611 1.009   1.00 21.25 ? 38  LEU B CD1 1 
ATOM   1402 C  CD2 . LEU B 1 38  ? 41.657 59.181 -1.363  1.00 17.75 ? 38  LEU B CD2 1 
ATOM   1403 N  N   . THR B 1 39  ? 38.998 62.407 2.255   1.00 25.41 ? 39  THR B N   1 
ATOM   1404 C  CA  . THR B 1 39  ? 38.289 63.671 2.285   1.00 26.45 ? 39  THR B CA  1 
ATOM   1405 C  C   . THR B 1 39  ? 38.334 64.197 0.857   1.00 26.28 ? 39  THR B C   1 
ATOM   1406 O  O   . THR B 1 39  ? 39.261 63.901 0.106   1.00 23.98 ? 39  THR B O   1 
ATOM   1407 C  CB  . THR B 1 39  ? 38.936 64.712 3.224   1.00 30.52 ? 39  THR B CB  1 
ATOM   1408 O  OG1 . THR B 1 39  ? 40.331 64.842 2.924   1.00 34.92 ? 39  THR B OG1 1 
ATOM   1409 C  CG2 . THR B 1 39  ? 38.750 64.328 4.692   1.00 32.29 ? 39  THR B CG2 1 
ATOM   1410 N  N   . GLU B 1 40  ? 37.290 64.919 0.477   1.00 26.37 ? 40  GLU B N   1 
ATOM   1411 C  CA  . GLU B 1 40  ? 37.168 65.516 -0.839  1.00 27.45 ? 40  GLU B CA  1 
ATOM   1412 C  C   . GLU B 1 40  ? 38.364 66.455 -1.139  1.00 25.88 ? 40  GLU B C   1 
ATOM   1413 O  O   . GLU B 1 40  ? 38.756 67.272 -0.301  1.00 27.87 ? 40  GLU B O   1 
ATOM   1414 C  CB  . GLU B 1 40  ? 35.848 66.287 -0.872  1.00 29.23 ? 40  GLU B CB  1 
ATOM   1415 C  CG  . GLU B 1 40  ? 35.524 66.957 -2.181  1.00 33.99 ? 40  GLU B CG  1 
ATOM   1416 C  CD  . GLU B 1 40  ? 34.251 67.809 -2.136  1.00 35.82 ? 40  GLU B CD  1 
ATOM   1417 O  OE1 . GLU B 1 40  ? 33.715 68.073 -1.034  1.00 38.54 ? 40  GLU B OE1 1 
ATOM   1418 O  OE2 . GLU B 1 40  ? 33.786 68.218 -3.216  1.00 37.21 ? 40  GLU B OE2 1 
ATOM   1419 N  N   . GLY B 1 41  ? 38.942 66.345 -2.327  1.00 23.19 ? 41  GLY B N   1 
ATOM   1420 C  CA  . GLY B 1 41  ? 40.067 67.195 -2.649  1.00 20.71 ? 41  GLY B CA  1 
ATOM   1421 C  C   . GLY B 1 41  ? 41.250 66.421 -3.182  1.00 20.22 ? 41  GLY B C   1 
ATOM   1422 O  O   . GLY B 1 41  ? 41.146 65.219 -3.417  1.00 18.90 ? 41  GLY B O   1 
ATOM   1423 N  N   . LEU B 1 42  ? 42.384 67.107 -3.330  1.00 19.72 ? 42  LEU B N   1 
ATOM   1424 C  CA  . LEU B 1 42  ? 43.611 66.507 -3.864  1.00 19.03 ? 42  LEU B CA  1 
ATOM   1425 C  C   . LEU B 1 42  ? 44.424 65.859 -2.764  1.00 18.36 ? 42  LEU B C   1 
ATOM   1426 O  O   . LEU B 1 42  ? 44.499 66.387 -1.657  1.00 18.86 ? 42  LEU B O   1 
ATOM   1427 C  CB  . LEU B 1 42  ? 44.493 67.568 -4.530  1.00 19.20 ? 42  LEU B CB  1 
ATOM   1428 C  CG  . LEU B 1 42  ? 43.954 68.359 -5.715  1.00 20.91 ? 42  LEU B CG  1 
ATOM   1429 C  CD1 . LEU B 1 42  ? 44.903 69.471 -6.060  1.00 20.21 ? 42  LEU B CD1 1 
ATOM   1430 C  CD2 . LEU B 1 42  ? 43.769 67.472 -6.887  1.00 24.55 ? 42  LEU B CD2 1 
ATOM   1431 N  N   . HIS B 1 43  ? 45.047 64.725 -3.078  1.00 17.98 ? 43  HIS B N   1 
ATOM   1432 C  CA  . HIS B 1 43  ? 45.887 64.015 -2.118  1.00 17.59 ? 43  HIS B CA  1 
ATOM   1433 C  C   . HIS B 1 43  ? 47.193 63.559 -2.757  1.00 14.78 ? 43  HIS B C   1 
ATOM   1434 O  O   . HIS B 1 43  ? 47.162 62.903 -3.799  1.00 16.57 ? 43  HIS B O   1 
ATOM   1435 C  CB  . HIS B 1 43  ? 45.148 62.794 -1.586  1.00 18.73 ? 43  HIS B CB  1 
ATOM   1436 C  CG  . HIS B 1 43  ? 43.927 63.133 -0.808  1.00 18.54 ? 43  HIS B CG  1 
ATOM   1437 N  ND1 . HIS B 1 43  ? 43.978 63.529 0.509   1.00 20.15 ? 43  HIS B ND1 1 
ATOM   1438 C  CD2 . HIS B 1 43  ? 42.632 63.232 -1.186  1.00 17.98 ? 43  HIS B CD2 1 
ATOM   1439 C  CE1 . HIS B 1 43  ? 42.766 63.870 0.908   1.00 19.76 ? 43  HIS B CE1 1 
ATOM   1440 N  NE2 . HIS B 1 43  ? 41.933 63.698 -0.103  1.00 19.97 ? 43  HIS B NE2 1 
ATOM   1441 N  N   . GLY B 1 44  ? 48.328 63.932 -2.160  1.00 15.34 ? 44  GLY B N   1 
ATOM   1442 C  CA  . GLY B 1 44  ? 49.637 63.522 -2.674  1.00 14.17 ? 44  GLY B CA  1 
ATOM   1443 C  C   . GLY B 1 44  ? 49.693 62.002 -2.765  1.00 13.93 ? 44  GLY B C   1 
ATOM   1444 O  O   . GLY B 1 44  ? 49.192 61.313 -1.884  1.00 13.49 ? 44  GLY B O   1 
ATOM   1445 N  N   . PHE B 1 45  ? 50.356 61.478 -3.785  1.00 14.63 ? 45  PHE B N   1 
ATOM   1446 C  CA  . PHE B 1 45  ? 50.401 60.034 -4.042  1.00 14.59 ? 45  PHE B CA  1 
ATOM   1447 C  C   . PHE B 1 45  ? 51.841 59.715 -4.434  1.00 14.84 ? 45  PHE B C   1 
ATOM   1448 O  O   . PHE B 1 45  ? 52.301 60.161 -5.471  1.00 15.44 ? 45  PHE B O   1 
ATOM   1449 C  CB  . PHE B 1 45  ? 49.442 59.785 -5.214  1.00 14.04 ? 45  PHE B CB  1 
ATOM   1450 C  CG  . PHE B 1 45  ? 49.111 58.354 -5.463  1.00 14.11 ? 45  PHE B CG  1 
ATOM   1451 C  CD1 . PHE B 1 45  ? 48.495 57.591 -4.491  1.00 16.15 ? 45  PHE B CD1 1 
ATOM   1452 C  CD2 . PHE B 1 45  ? 49.331 57.798 -6.719  1.00 16.98 ? 45  PHE B CD2 1 
ATOM   1453 C  CE1 . PHE B 1 45  ? 48.092 56.292 -4.772  1.00 19.29 ? 45  PHE B CE1 1 
ATOM   1454 C  CE2 . PHE B 1 45  ? 48.932 56.501 -7.005  1.00 16.64 ? 45  PHE B CE2 1 
ATOM   1455 C  CZ  . PHE B 1 45  ? 48.312 55.750 -6.035  1.00 16.03 ? 45  PHE B CZ  1 
ATOM   1456 N  N   . HIS B 1 46  ? 52.578 58.995 -3.593  1.00 14.91 ? 46  HIS B N   1 
ATOM   1457 C  CA  . HIS B 1 46  ? 53.977 58.732 -3.898  1.00 14.35 ? 46  HIS B CA  1 
ATOM   1458 C  C   . HIS B 1 46  ? 54.449 57.358 -3.481  1.00 15.05 ? 46  HIS B C   1 
ATOM   1459 O  O   . HIS B 1 46  ? 53.890 56.737 -2.586  1.00 14.91 ? 46  HIS B O   1 
ATOM   1460 C  CB  . HIS B 1 46  ? 54.907 59.718 -3.162  1.00 13.83 ? 46  HIS B CB  1 
ATOM   1461 C  CG  . HIS B 1 46  ? 54.363 61.110 -3.000  1.00 17.07 ? 46  HIS B CG  1 
ATOM   1462 N  ND1 . HIS B 1 46  ? 54.132 61.675 -1.760  1.00 18.94 ? 46  HIS B ND1 1 
ATOM   1463 C  CD2 . HIS B 1 46  ? 54.094 62.075 -3.907  1.00 17.14 ? 46  HIS B CD2 1 
ATOM   1464 C  CE1 . HIS B 1 46  ? 53.750 62.930 -1.919  1.00 17.13 ? 46  HIS B CE1 1 
ATOM   1465 N  NE2 . HIS B 1 46  ? 53.716 63.196 -3.207  1.00 17.32 ? 46  HIS B NE2 1 
ATOM   1466 N  N   . VAL B 1 47  ? 55.576 56.953 -4.046  1.00 14.39 ? 47  VAL B N   1 
ATOM   1467 C  CA  . VAL B 1 47  ? 56.193 55.700 -3.675  1.00 14.28 ? 47  VAL B CA  1 
ATOM   1468 C  C   . VAL B 1 47  ? 57.339 56.094 -2.753  1.00 14.96 ? 47  VAL B C   1 
ATOM   1469 O  O   . VAL B 1 47  ? 58.156 56.960 -3.089  1.00 14.48 ? 47  VAL B O   1 
ATOM   1470 C  CB  . VAL B 1 47  ? 56.758 54.929 -4.879  1.00 14.52 ? 47  VAL B CB  1 
ATOM   1471 C  CG1 . VAL B 1 47  ? 57.513 53.686 -4.407  1.00 14.05 ? 47  VAL B CG1 1 
ATOM   1472 C  CG2 . VAL B 1 47  ? 55.632 54.535 -5.812  1.00 14.48 ? 47  VAL B CG2 1 
ATOM   1473 N  N   . HIS B 1 48  ? 57.279 55.583 -1.529  1.00 16.11 ? 48  HIS B N   1 
ATOM   1474 C  CA  . HIS B 1 48  ? 58.314 55.813 -0.533  1.00 15.73 ? 48  HIS B CA  1 
ATOM   1475 C  C   . HIS B 1 48  ? 59.334 54.690 -0.601  1.00 15.75 ? 48  HIS B C   1 
ATOM   1476 O  O   . HIS B 1 48  ? 59.043 53.603 -1.082  1.00 17.43 ? 48  HIS B O   1 
ATOM   1477 C  CB  . HIS B 1 48  ? 57.714 55.990 0.854   1.00 12.47 ? 48  HIS B CB  1 
ATOM   1478 C  CG  . HIS B 1 48  ? 57.000 57.295 1.017   1.00 13.82 ? 48  HIS B CG  1 
ATOM   1479 N  ND1 . HIS B 1 48  ? 57.320 58.204 2.002   1.00 15.02 ? 48  HIS B ND1 1 
ATOM   1480 C  CD2 . HIS B 1 48  ? 56.034 57.883 0.271   1.00 12.57 ? 48  HIS B CD2 1 
ATOM   1481 C  CE1 . HIS B 1 48  ? 56.594 59.293 1.851   1.00 12.81 ? 48  HIS B CE1 1 
ATOM   1482 N  NE2 . HIS B 1 48  ? 55.800 59.124 0.804   1.00 12.37 ? 48  HIS B NE2 1 
ATOM   1483 N  N   . GLU B 1 49  ? 60.547 54.985 -0.163  1.00 17.07 ? 49  GLU B N   1 
ATOM   1484 C  CA  . GLU B 1 49  ? 61.658 54.061 -0.242  1.00 17.68 ? 49  GLU B CA  1 
ATOM   1485 C  C   . GLU B 1 49  ? 61.593 52.682 0.429   1.00 16.60 ? 49  GLU B C   1 
ATOM   1486 O  O   . GLU B 1 49  ? 61.937 51.683 -0.185  1.00 16.55 ? 49  GLU B O   1 
ATOM   1487 C  CB  . GLU B 1 49  ? 62.918 54.797 0.191   1.00 20.33 ? 49  GLU B CB  1 
ATOM   1488 C  CG  . GLU B 1 49  ? 64.192 54.164 -0.329  1.00 25.00 ? 49  GLU B CG  1 
ATOM   1489 C  CD  . GLU B 1 49  ? 65.423 54.809 0.231   1.00 26.24 ? 49  GLU B CD  1 
ATOM   1490 O  OE1 . GLU B 1 49  ? 65.365 55.979 0.687   1.00 26.52 ? 49  GLU B OE1 1 
ATOM   1491 O  OE2 . GLU B 1 49  ? 66.455 54.122 0.217   1.00 30.46 ? 49  GLU B OE2 1 
ATOM   1492 N  N   . PHE B 1 50  ? 61.143 52.606 1.669   1.00 15.89 ? 50  PHE B N   1 
ATOM   1493 C  CA  . PHE B 1 50  ? 61.128 51.329 2.351   1.00 14.95 ? 50  PHE B CA  1 
ATOM   1494 C  C   . PHE B 1 50  ? 59.777 50.669 2.388   1.00 15.81 ? 50  PHE B C   1 
ATOM   1495 O  O   . PHE B 1 50  ? 58.768 51.341 2.469   1.00 17.57 ? 50  PHE B O   1 
ATOM   1496 C  CB  . PHE B 1 50  ? 61.659 51.506 3.776   1.00 14.81 ? 50  PHE B CB  1 
ATOM   1497 C  CG  . PHE B 1 50  ? 62.954 52.270 3.837   1.00 18.97 ? 50  PHE B CG  1 
ATOM   1498 C  CD1 . PHE B 1 50  ? 64.089 51.800 3.170   1.00 20.95 ? 50  PHE B CD1 1 
ATOM   1499 C  CD2 . PHE B 1 50  ? 63.022 53.500 4.493   1.00 20.08 ? 50  PHE B CD2 1 
ATOM   1500 C  CE1 . PHE B 1 50  ? 65.264 52.552 3.150   1.00 20.01 ? 50  PHE B CE1 1 
ATOM   1501 C  CE2 . PHE B 1 50  ? 64.192 54.251 4.476   1.00 18.62 ? 50  PHE B CE2 1 
ATOM   1502 C  CZ  . PHE B 1 50  ? 65.305 53.776 3.803   1.00 17.81 ? 50  PHE B CZ  1 
ATOM   1503 N  N   . GLY B 1 51  ? 59.767 49.345 2.291   1.00 13.94 ? 51  GLY B N   1 
ATOM   1504 C  CA  . GLY B 1 51  ? 58.535 48.579 2.367   1.00 16.56 ? 51  GLY B CA  1 
ATOM   1505 C  C   . GLY B 1 51  ? 58.439 48.047 3.786   1.00 17.89 ? 51  GLY B C   1 
ATOM   1506 O  O   . GLY B 1 51  ? 58.157 46.874 4.044   1.00 19.77 ? 51  GLY B O   1 
ATOM   1507 N  N   . ASP B 1 52  ? 58.706 48.943 4.719   1.00 19.69 ? 52  ASP B N   1 
ATOM   1508 C  CA  . ASP B 1 52  ? 58.699 48.633 6.128   1.00 19.52 ? 52  ASP B CA  1 
ATOM   1509 C  C   . ASP B 1 52  ? 57.459 49.266 6.738   1.00 20.59 ? 52  ASP B C   1 
ATOM   1510 O  O   . ASP B 1 52  ? 57.325 50.486 6.767   1.00 19.10 ? 52  ASP B O   1 
ATOM   1511 C  CB  . ASP B 1 52  ? 59.968 49.219 6.747   1.00 19.76 ? 52  ASP B CB  1 
ATOM   1512 C  CG  . ASP B 1 52  ? 60.072 48.958 8.236   1.00 22.12 ? 52  ASP B CG  1 
ATOM   1513 O  OD1 . ASP B 1 52  ? 59.067 48.611 8.879   1.00 19.90 ? 52  ASP B OD1 1 
ATOM   1514 O  OD2 . ASP B 1 52  ? 61.189 49.103 8.770   1.00 23.16 ? 52  ASP B OD2 1 
ATOM   1515 N  N   . ASN B 1 53  ? 56.537 48.436 7.207   1.00 22.06 ? 53  ASN B N   1 
ATOM   1516 C  CA  . ASN B 1 53  ? 55.324 48.954 7.825   1.00 24.40 ? 53  ASN B CA  1 
ATOM   1517 C  C   . ASN B 1 53  ? 55.239 48.548 9.290   1.00 22.52 ? 53  ASN B C   1 
ATOM   1518 O  O   . ASN B 1 53  ? 54.148 48.388 9.836   1.00 21.76 ? 53  ASN B O   1 
ATOM   1519 C  CB  . ASN B 1 53  ? 54.061 48.546 7.034   1.00 28.71 ? 53  ASN B CB  1 
ATOM   1520 C  CG  . ASN B 1 53  ? 53.820 49.415 5.752   1.00 34.83 ? 53  ASN B CG  1 
ATOM   1521 O  OD1 . ASN B 1 53  ? 52.914 49.124 4.964   1.00 38.79 ? 53  ASN B OD1 1 
ATOM   1522 N  ND2 . ASN B 1 53  ? 54.625 50.473 5.556   1.00 34.59 ? 53  ASN B ND2 1 
ATOM   1523 N  N   . THR B 1 54  ? 56.401 48.425 9.944   1.00 24.46 ? 54  THR B N   1 
ATOM   1524 C  CA  . THR B 1 54  ? 56.466 48.055 11.373  1.00 22.76 ? 54  THR B CA  1 
ATOM   1525 C  C   . THR B 1 54  ? 55.930 49.176 12.288  1.00 23.75 ? 54  THR B C   1 
ATOM   1526 O  O   . THR B 1 54  ? 55.388 48.901 13.355  1.00 25.89 ? 54  THR B O   1 
ATOM   1527 C  CB  . THR B 1 54  ? 57.894 47.593 11.837  1.00 20.74 ? 54  THR B CB  1 
ATOM   1528 O  OG1 . THR B 1 54  ? 58.839 48.643 11.639  1.00 20.33 ? 54  THR B OG1 1 
ATOM   1529 C  CG2 . THR B 1 54  ? 58.353 46.325 11.088  1.00 18.44 ? 54  THR B CG2 1 
ATOM   1530 N  N   . ALA B 1 55  ? 56.061 50.430 11.854  1.00 23.49 ? 55  ALA B N   1 
ATOM   1531 C  CA  . ALA B 1 55  ? 55.548 51.576 12.606  1.00 21.02 ? 55  ALA B CA  1 
ATOM   1532 C  C   . ALA B 1 55  ? 54.513 52.248 11.700  1.00 20.83 ? 55  ALA B C   1 
ATOM   1533 O  O   . ALA B 1 55  ? 54.472 53.469 11.562  1.00 22.80 ? 55  ALA B O   1 
ATOM   1534 C  CB  . ALA B 1 55  ? 56.677 52.550 12.957  1.00 17.77 ? 55  ALA B CB  1 
ATOM   1535 N  N   . GLY B 1 56  ? 53.696 51.432 11.045  1.00 20.58 ? 56  GLY B N   1 
ATOM   1536 C  CA  . GLY B 1 56  ? 52.684 51.968 10.152  1.00 20.95 ? 56  GLY B CA  1 
ATOM   1537 C  C   . GLY B 1 56  ? 53.303 52.591 8.911   1.00 21.56 ? 56  GLY B C   1 
ATOM   1538 O  O   . GLY B 1 56  ? 54.317 52.098 8.386   1.00 21.68 ? 56  GLY B O   1 
ATOM   1539 N  N   . CYS B 1 57  ? 52.739 53.709 8.464   1.00 19.09 ? 57  CYS B N   1 
ATOM   1540 C  CA  . CYS B 1 57  ? 53.256 54.378 7.272   1.00 18.11 ? 57  CYS B CA  1 
ATOM   1541 C  C   . CYS B 1 57  ? 54.519 55.218 7.516   1.00 17.95 ? 57  CYS B C   1 
ATOM   1542 O  O   . CYS B 1 57  ? 55.254 55.534 6.575   1.00 18.46 ? 57  CYS B O   1 
ATOM   1543 C  CB  . CYS B 1 57  ? 52.150 55.205 6.611   1.00 17.91 ? 57  CYS B CB  1 
ATOM   1544 S  SG  . CYS B 1 57  ? 50.668 54.219 6.234   1.00 16.23 ? 57  CYS B SG  1 
ATOM   1545 N  N   . THR B 1 58  ? 54.793 55.514 8.785   1.00 18.28 ? 58  THR B N   1 
ATOM   1546 C  CA  . THR B 1 58  ? 55.954 56.314 9.199   1.00 20.14 ? 58  THR B CA  1 
ATOM   1547 C  C   . THR B 1 58  ? 57.284 55.636 8.859   1.00 17.85 ? 58  THR B C   1 
ATOM   1548 O  O   . THR B 1 58  ? 58.225 56.288 8.428   1.00 19.35 ? 58  THR B O   1 
ATOM   1549 C  CB  . THR B 1 58  ? 55.896 56.581 10.718  1.00 21.31 ? 58  THR B CB  1 
ATOM   1550 O  OG1 . THR B 1 58  ? 54.567 56.978 11.071  1.00 22.84 ? 58  THR B OG1 1 
ATOM   1551 C  CG2 . THR B 1 58  ? 56.875 57.671 11.108  1.00 23.95 ? 58  THR B CG2 1 
ATOM   1552 N  N   . SER B 1 59  ? 57.343 54.320 9.023   1.00 19.05 ? 59  SER B N   1 
ATOM   1553 C  CA  . SER B 1 59  ? 58.556 53.568 8.718   1.00 17.94 ? 59  SER B CA  1 
ATOM   1554 C  C   . SER B 1 59  ? 58.881 53.424 7.221   1.00 17.74 ? 59  SER B C   1 
ATOM   1555 O  O   . SER B 1 59  ? 59.962 52.955 6.867   1.00 19.68 ? 59  SER B O   1 
ATOM   1556 C  CB  . SER B 1 59  ? 58.547 52.200 9.430   1.00 15.69 ? 59  SER B CB  1 
ATOM   1557 O  OG  . SER B 1 59  ? 57.247 51.647 9.541   1.00 17.48 ? 59  SER B OG  1 
ATOM   1558 N  N   . ALA B 1 60  ? 57.999 53.912 6.346   1.00 17.46 ? 60  ALA B N   1 
ATOM   1559 C  CA  . ALA B 1 60  ? 58.219 53.824 4.905   1.00 16.98 ? 60  ALA B CA  1 
ATOM   1560 C  C   . ALA B 1 60  ? 59.336 54.758 4.417   1.00 17.66 ? 60  ALA B C   1 
ATOM   1561 O  O   . ALA B 1 60  ? 59.784 54.669 3.268   1.00 17.31 ? 60  ALA B O   1 
ATOM   1562 C  CB  . ALA B 1 60  ? 56.930 54.075 4.152   1.00 15.70 ? 60  ALA B CB  1 
ATOM   1563 N  N   . GLY B 1 61  ? 59.805 55.633 5.300   1.00 18.67 ? 61  GLY B N   1 
ATOM   1564 C  CA  . GLY B 1 61  ? 60.884 56.528 4.942   1.00 18.76 ? 61  GLY B CA  1 
ATOM   1565 C  C   . GLY B 1 61  ? 60.468 57.640 3.996   1.00 20.17 ? 61  GLY B C   1 
ATOM   1566 O  O   . GLY B 1 61  ? 59.280 57.930 3.875   1.00 19.18 ? 61  GLY B O   1 
ATOM   1567 N  N   . PRO B 1 62  ? 61.438 58.260 3.294   1.00 20.91 ? 62  PRO B N   1 
ATOM   1568 C  CA  . PRO B 1 62  ? 61.240 59.355 2.342   1.00 19.90 ? 62  PRO B CA  1 
ATOM   1569 C  C   . PRO B 1 62  ? 60.811 58.861 0.970   1.00 19.50 ? 62  PRO B C   1 
ATOM   1570 O  O   . PRO B 1 62  ? 60.711 57.661 0.748   1.00 18.39 ? 62  PRO B O   1 
ATOM   1571 C  CB  . PRO B 1 62  ? 62.627 59.983 2.297   1.00 21.53 ? 62  PRO B CB  1 
ATOM   1572 C  CG  . PRO B 1 62  ? 63.523 58.785 2.350   1.00 20.07 ? 62  PRO B CG  1 
ATOM   1573 C  CD  . PRO B 1 62  ? 62.867 57.897 3.387   1.00 21.91 ? 62  PRO B CD  1 
ATOM   1574 N  N   . HIS B 1 63  ? 60.553 59.784 0.046   1.00 19.02 ? 63  HIS B N   1 
ATOM   1575 C  CA  . HIS B 1 63  ? 60.160 59.399 -1.302  1.00 19.26 ? 63  HIS B CA  1 
ATOM   1576 C  C   . HIS B 1 63  ? 61.284 58.582 -1.887  1.00 19.54 ? 63  HIS B C   1 
ATOM   1577 O  O   . HIS B 1 63  ? 62.440 58.809 -1.551  1.00 20.97 ? 63  HIS B O   1 
ATOM   1578 C  CB  . HIS B 1 63  ? 59.986 60.625 -2.174  1.00 18.99 ? 63  HIS B CB  1 
ATOM   1579 C  CG  . HIS B 1 63  ? 58.867 61.503 -1.748  1.00 21.68 ? 63  HIS B CG  1 
ATOM   1580 N  ND1 . HIS B 1 63  ? 58.535 62.664 -2.409  1.00 20.32 ? 63  HIS B ND1 1 
ATOM   1581 C  CD2 . HIS B 1 63  ? 57.984 61.377 -0.734  1.00 24.65 ? 63  HIS B CD2 1 
ATOM   1582 C  CE1 . HIS B 1 63  ? 57.489 63.216 -1.819  1.00 25.92 ? 63  HIS B CE1 1 
ATOM   1583 N  NE2 . HIS B 1 63  ? 57.138 62.453 -0.803  1.00 28.72 ? 63  HIS B NE2 1 
ATOM   1584 N  N   . PHE B 1 64  ? 60.947 57.629 -2.743  1.00 19.83 ? 64  PHE B N   1 
ATOM   1585 C  CA  . PHE B 1 64  ? 61.953 56.802 -3.406  1.00 19.76 ? 64  PHE B CA  1 
ATOM   1586 C  C   . PHE B 1 64  ? 62.710 57.793 -4.317  1.00 19.96 ? 64  PHE B C   1 
ATOM   1587 O  O   . PHE B 1 64  ? 62.131 58.407 -5.224  1.00 19.92 ? 64  PHE B O   1 
ATOM   1588 C  CB  . PHE B 1 64  ? 61.235 55.705 -4.200  1.00 18.04 ? 64  PHE B CB  1 
ATOM   1589 C  CG  . PHE B 1 64  ? 62.150 54.775 -4.941  1.00 17.42 ? 64  PHE B CG  1 
ATOM   1590 C  CD1 . PHE B 1 64  ? 63.359 54.364 -4.387  1.00 17.32 ? 64  PHE B CD1 1 
ATOM   1591 C  CD2 . PHE B 1 64  ? 61.808 54.339 -6.214  1.00 15.84 ? 64  PHE B CD2 1 
ATOM   1592 C  CE1 . PHE B 1 64  ? 64.217 53.533 -5.107  1.00 18.84 ? 64  PHE B CE1 1 
ATOM   1593 C  CE2 . PHE B 1 64  ? 62.646 53.517 -6.935  1.00 17.73 ? 64  PHE B CE2 1 
ATOM   1594 C  CZ  . PHE B 1 64  ? 63.863 53.110 -6.388  1.00 17.83 ? 64  PHE B CZ  1 
ATOM   1595 N  N   . ASN B 1 65  ? 63.997 57.971 -4.065  1.00 20.60 ? 65  ASN B N   1 
ATOM   1596 C  CA  . ASN B 1 65  ? 64.772 58.959 -4.813  1.00 22.81 ? 65  ASN B CA  1 
ATOM   1597 C  C   . ASN B 1 65  ? 66.186 58.456 -5.105  1.00 24.54 ? 65  ASN B C   1 
ATOM   1598 O  O   . ASN B 1 65  ? 67.164 59.006 -4.594  1.00 25.08 ? 65  ASN B O   1 
ATOM   1599 C  CB  . ASN B 1 65  ? 64.805 60.250 -3.973  1.00 19.34 ? 65  ASN B CB  1 
ATOM   1600 C  CG  . ASN B 1 65  ? 65.504 61.402 -4.658  1.00 17.66 ? 65  ASN B CG  1 
ATOM   1601 O  OD1 . ASN B 1 65  ? 65.635 61.450 -5.883  1.00 19.83 ? 65  ASN B OD1 1 
ATOM   1602 N  ND2 . ASN B 1 65  ? 65.904 62.379 -3.864  1.00 19.68 ? 65  ASN B ND2 1 
ATOM   1603 N  N   . PRO B 1 66  ? 66.311 57.419 -5.949  1.00 25.38 ? 66  PRO B N   1 
ATOM   1604 C  CA  . PRO B 1 66  ? 67.621 56.857 -6.287  1.00 27.73 ? 66  PRO B CA  1 
ATOM   1605 C  C   . PRO B 1 66  ? 68.593 57.828 -6.952  1.00 30.56 ? 66  PRO B C   1 
ATOM   1606 O  O   . PRO B 1 66  ? 69.810 57.712 -6.754  1.00 32.32 ? 66  PRO B O   1 
ATOM   1607 C  CB  . PRO B 1 66  ? 67.262 55.676 -7.202  1.00 26.01 ? 66  PRO B CB  1 
ATOM   1608 C  CG  . PRO B 1 66  ? 65.960 56.069 -7.798  1.00 25.24 ? 66  PRO B CG  1 
ATOM   1609 C  CD  . PRO B 1 66  ? 65.236 56.685 -6.637  1.00 24.10 ? 66  PRO B CD  1 
ATOM   1610 N  N   . LEU B 1 67  ? 68.055 58.801 -7.693  1.00 32.24 ? 67  LEU B N   1 
ATOM   1611 C  CA  . LEU B 1 67  ? 68.880 59.782 -8.414  1.00 33.16 ? 67  LEU B CA  1 
ATOM   1612 C  C   . LEU B 1 67  ? 69.160 61.102 -7.699  1.00 34.18 ? 67  LEU B C   1 
ATOM   1613 O  O   . LEU B 1 67  ? 69.705 62.029 -8.307  1.00 35.88 ? 67  LEU B O   1 
ATOM   1614 C  CB  . LEU B 1 67  ? 68.278 60.095 -9.783  1.00 32.19 ? 67  LEU B CB  1 
ATOM   1615 C  CG  . LEU B 1 67  ? 68.106 58.994 -10.819 1.00 32.39 ? 67  LEU B CG  1 
ATOM   1616 C  CD1 . LEU B 1 67  ? 69.404 58.246 -10.970 1.00 35.04 ? 67  LEU B CD1 1 
ATOM   1617 C  CD2 . LEU B 1 67  ? 67.008 58.064 -10.403 1.00 34.53 ? 67  LEU B CD2 1 
ATOM   1618 N  N   . SER B 1 68  ? 68.745 61.197 -6.438  1.00 34.99 ? 68  SER B N   1 
ATOM   1619 C  CA  . SER B 1 68  ? 68.941 62.384 -5.603  1.00 35.24 ? 68  SER B CA  1 
ATOM   1620 C  C   . SER B 1 68  ? 68.575 63.748 -6.205  1.00 34.41 ? 68  SER B C   1 
ATOM   1621 O  O   . SER B 1 68  ? 69.346 64.710 -6.163  1.00 34.84 ? 68  SER B O   1 
ATOM   1622 C  CB  . SER B 1 68  ? 70.349 62.382 -5.010  1.00 37.87 ? 68  SER B CB  1 
ATOM   1623 O  OG  . SER B 1 68  ? 70.526 61.229 -4.186  1.00 44.65 ? 68  SER B OG  1 
ATOM   1624 N  N   . ARG B 1 69  ? 67.353 63.827 -6.712  1.00 33.27 ? 69  ARG B N   1 
ATOM   1625 C  CA  . ARG B 1 69  ? 66.831 65.051 -7.290  1.00 32.11 ? 69  ARG B CA  1 
ATOM   1626 C  C   . ARG B 1 69  ? 65.919 65.694 -6.259  1.00 30.56 ? 69  ARG B C   1 
ATOM   1627 O  O   . ARG B 1 69  ? 65.742 65.189 -5.146  1.00 30.11 ? 69  ARG B O   1 
ATOM   1628 C  CB  . ARG B 1 69  ? 65.977 64.735 -8.507  1.00 32.39 ? 69  ARG B CB  1 
ATOM   1629 C  CG  . ARG B 1 69  ? 66.586 63.771 -9.446  1.00 37.93 ? 69  ARG B CG  1 
ATOM   1630 C  CD  . ARG B 1 69  ? 67.775 64.360 -10.153 1.00 45.26 ? 69  ARG B CD  1 
ATOM   1631 N  NE  . ARG B 1 69  ? 68.116 63.530 -11.305 1.00 51.96 ? 69  ARG B NE  1 
ATOM   1632 C  CZ  . ARG B 1 69  ? 67.344 63.396 -12.385 1.00 54.88 ? 69  ARG B CZ  1 
ATOM   1633 N  NH1 . ARG B 1 69  ? 66.188 64.056 -12.474 1.00 55.14 ? 69  ARG B NH1 1 
ATOM   1634 N  NH2 . ARG B 1 69  ? 67.697 62.547 -13.352 1.00 55.87 ? 69  ARG B NH2 1 
ATOM   1635 N  N   . LYS B 1 70  ? 65.286 66.780 -6.666  1.00 29.73 ? 70  LYS B N   1 
ATOM   1636 C  CA  . LYS B 1 70  ? 64.360 67.476 -5.804  1.00 29.55 ? 70  LYS B CA  1 
ATOM   1637 C  C   . LYS B 1 70  ? 62.973 66.969 -6.157  1.00 24.89 ? 70  LYS B C   1 
ATOM   1638 O  O   . LYS B 1 70  ? 62.762 66.372 -7.208  1.00 22.06 ? 70  LYS B O   1 
ATOM   1639 C  CB  . LYS B 1 70  ? 64.434 68.999 -6.011  1.00 34.78 ? 70  LYS B CB  1 
ATOM   1640 C  CG  . LYS B 1 70  ? 65.695 69.671 -5.448  1.00 43.65 ? 70  LYS B CG  1 
ATOM   1641 C  CD  . LYS B 1 70  ? 66.927 69.313 -6.293  1.00 54.51 ? 70  LYS B CD  1 
ATOM   1642 C  CE  . LYS B 1 70  ? 68.269 69.494 -5.541  1.00 59.39 ? 70  LYS B CE  1 
ATOM   1643 N  NZ  . LYS B 1 70  ? 69.444 68.855 -6.255  1.00 59.67 ? 70  LYS B NZ  1 
ATOM   1644 N  N   . HIS B 1 71  ? 62.049 67.163 -5.233  1.00 21.30 ? 71  HIS B N   1 
ATOM   1645 C  CA  . HIS B 1 71  ? 60.675 66.756 -5.419  1.00 20.32 ? 71  HIS B CA  1 
ATOM   1646 C  C   . HIS B 1 71  ? 60.042 67.528 -6.591  1.00 20.10 ? 71  HIS B C   1 
ATOM   1647 O  O   . HIS B 1 71  ? 60.390 68.681 -6.833  1.00 22.50 ? 71  HIS B O   1 
ATOM   1648 C  CB  . HIS B 1 71  ? 59.903 67.031 -4.120  1.00 17.69 ? 71  HIS B CB  1 
ATOM   1649 C  CG  . HIS B 1 71  ? 58.441 66.733 -4.215  1.00 17.66 ? 71  HIS B CG  1 
ATOM   1650 N  ND1 . HIS B 1 71  ? 57.931 65.459 -4.083  1.00 17.16 ? 71  HIS B ND1 1 
ATOM   1651 C  CD2 . HIS B 1 71  ? 57.388 67.535 -4.495  1.00 15.63 ? 71  HIS B CD2 1 
ATOM   1652 C  CE1 . HIS B 1 71  ? 56.627 65.494 -4.286  1.00 15.96 ? 71  HIS B CE1 1 
ATOM   1653 N  NE2 . HIS B 1 71  ? 56.278 66.740 -4.542  1.00 17.02 ? 71  HIS B NE2 1 
ATOM   1654 N  N   . GLY B 1 72  ? 59.136 66.892 -7.320  1.00 18.31 ? 72  GLY B N   1 
ATOM   1655 C  CA  . GLY B 1 72  ? 58.473 67.588 -8.398  1.00 16.83 ? 72  GLY B CA  1 
ATOM   1656 C  C   . GLY B 1 72  ? 57.207 66.861 -8.737  1.00 17.69 ? 72  GLY B C   1 
ATOM   1657 O  O   . GLY B 1 72  ? 56.809 65.961 -8.018  1.00 19.10 ? 72  GLY B O   1 
ATOM   1658 N  N   . GLY B 1 73  ? 56.528 67.315 -9.777  1.00 18.72 ? 73  GLY B N   1 
ATOM   1659 C  CA  . GLY B 1 73  ? 55.316 66.668 -10.227 1.00 18.58 ? 73  GLY B CA  1 
ATOM   1660 C  C   . GLY B 1 73  ? 55.718 65.535 -11.143 1.00 19.69 ? 73  GLY B C   1 
ATOM   1661 O  O   . GLY B 1 73  ? 56.870 65.486 -11.580 1.00 20.21 ? 73  GLY B O   1 
ATOM   1662 N  N   . PRO B 1 74  ? 54.782 64.646 -11.513 1.00 20.79 ? 74  PRO B N   1 
ATOM   1663 C  CA  . PRO B 1 74  ? 55.075 63.504 -12.388 1.00 21.65 ? 74  PRO B CA  1 
ATOM   1664 C  C   . PRO B 1 74  ? 55.616 63.834 -13.782 1.00 24.97 ? 74  PRO B C   1 
ATOM   1665 O  O   . PRO B 1 74  ? 56.398 63.056 -14.347 1.00 23.50 ? 74  PRO B O   1 
ATOM   1666 C  CB  . PRO B 1 74  ? 53.735 62.750 -12.428 1.00 20.75 ? 74  PRO B CB  1 
ATOM   1667 C  CG  . PRO B 1 74  ? 52.732 63.817 -12.207 1.00 18.30 ? 74  PRO B CG  1 
ATOM   1668 C  CD  . PRO B 1 74  ? 53.354 64.674 -11.151 1.00 18.76 ? 74  PRO B CD  1 
ATOM   1669 N  N   . LYS B 1 75  ? 55.233 64.995 -14.318 1.00 27.39 ? 75  LYS B N   1 
ATOM   1670 C  CA  . LYS B 1 75  ? 55.666 65.423 -15.654 1.00 27.96 ? 75  LYS B CA  1 
ATOM   1671 C  C   . LYS B 1 75  ? 56.803 66.437 -15.631 1.00 27.48 ? 75  LYS B C   1 
ATOM   1672 O  O   . LYS B 1 75  ? 57.142 67.030 -16.651 1.00 28.85 ? 75  LYS B O   1 
ATOM   1673 C  CB  . LYS B 1 75  ? 54.482 66.016 -16.428 1.00 30.16 ? 75  LYS B CB  1 
ATOM   1674 C  CG  . LYS B 1 75  ? 53.222 65.159 -16.481 1.00 33.29 ? 75  LYS B CG  1 
ATOM   1675 C  CD  . LYS B 1 75  ? 53.486 63.836 -17.138 1.00 36.72 ? 75  LYS B CD  1 
ATOM   1676 C  CE  . LYS B 1 75  ? 52.236 62.992 -17.184 1.00 41.17 ? 75  LYS B CE  1 
ATOM   1677 N  NZ  . LYS B 1 75  ? 52.520 61.654 -17.801 1.00 46.91 ? 75  LYS B NZ  1 
ATOM   1678 N  N   . ASP B 1 76  ? 57.355 66.683 -14.455 1.00 29.03 ? 76  ASP B N   1 
ATOM   1679 C  CA  . ASP B 1 76  ? 58.435 67.632 -14.344 1.00 30.24 ? 76  ASP B CA  1 
ATOM   1680 C  C   . ASP B 1 76  ? 59.729 66.941 -14.730 1.00 33.79 ? 76  ASP B C   1 
ATOM   1681 O  O   . ASP B 1 76  ? 59.815 65.707 -14.713 1.00 32.44 ? 76  ASP B O   1 
ATOM   1682 C  CB  . ASP B 1 76  ? 58.527 68.179 -12.922 1.00 30.64 ? 76  ASP B CB  1 
ATOM   1683 C  CG  . ASP B 1 76  ? 57.558 69.323 -12.666 1.00 30.34 ? 76  ASP B CG  1 
ATOM   1684 O  OD1 . ASP B 1 76  ? 57.517 70.269 -13.472 1.00 32.76 ? 76  ASP B OD1 1 
ATOM   1685 O  OD2 . ASP B 1 76  ? 56.857 69.300 -11.644 1.00 27.33 ? 76  ASP B OD2 1 
ATOM   1686 N  N   . GLU B 1 77  ? 60.716 67.747 -15.121 1.00 38.08 ? 77  GLU B N   1 
ATOM   1687 C  CA  . GLU B 1 77  ? 62.044 67.243 -15.503 1.00 42.02 ? 77  GLU B CA  1 
ATOM   1688 C  C   . GLU B 1 77  ? 62.720 66.647 -14.265 1.00 38.59 ? 77  GLU B C   1 
ATOM   1689 O  O   . GLU B 1 77  ? 63.257 65.543 -14.292 1.00 39.10 ? 77  GLU B O   1 
ATOM   1690 C  CB  . GLU B 1 77  ? 62.916 68.390 -16.065 1.00 49.10 ? 77  GLU B CB  1 
ATOM   1691 C  CG  . GLU B 1 77  ? 62.768 68.688 -17.578 1.00 58.18 ? 77  GLU B CG  1 
ATOM   1692 C  CD  . GLU B 1 77  ? 63.943 68.167 -18.439 1.00 63.17 ? 77  GLU B CD  1 
ATOM   1693 O  OE1 . GLU B 1 77  ? 65.022 67.823 -17.883 1.00 65.61 ? 77  GLU B OE1 1 
ATOM   1694 O  OE2 . GLU B 1 77  ? 63.782 68.112 -19.685 1.00 65.64 ? 77  GLU B OE2 1 
ATOM   1695 N  N   . GLU B 1 78  ? 62.672 67.406 -13.177 1.00 35.58 ? 78  GLU B N   1 
ATOM   1696 C  CA  . GLU B 1 78  ? 63.259 66.998 -11.925 1.00 32.44 ? 78  GLU B CA  1 
ATOM   1697 C  C   . GLU B 1 78  ? 62.187 66.547 -10.954 1.00 28.42 ? 78  GLU B C   1 
ATOM   1698 O  O   . GLU B 1 78  ? 61.316 67.316 -10.567 1.00 28.10 ? 78  GLU B O   1 
ATOM   1699 C  CB  . GLU B 1 78  ? 64.031 68.164 -11.324 1.00 35.76 ? 78  GLU B CB  1 
ATOM   1700 C  CG  . GLU B 1 78  ? 64.630 67.871 -9.969  1.00 40.54 ? 78  GLU B CG  1 
ATOM   1701 C  CD  . GLU B 1 78  ? 66.070 68.266 -9.897  1.00 42.32 ? 78  GLU B CD  1 
ATOM   1702 O  OE1 . GLU B 1 78  ? 66.508 69.039 -10.771 1.00 46.58 ? 78  GLU B OE1 1 
ATOM   1703 O  OE2 . GLU B 1 78  ? 66.770 67.794 -8.986  1.00 43.21 ? 78  GLU B OE2 1 
ATOM   1704 N  N   . ARG B 1 79  ? 62.294 65.308 -10.524 1.00 24.04 ? 79  ARG B N   1 
ATOM   1705 C  CA  . ARG B 1 79  ? 61.350 64.751 -9.587  1.00 21.89 ? 79  ARG B CA  1 
ATOM   1706 C  C   . ARG B 1 79  ? 62.031 63.536 -9.000  1.00 20.64 ? 79  ARG B C   1 
ATOM   1707 O  O   . ARG B 1 79  ? 63.069 63.092 -9.494  1.00 20.80 ? 79  ARG B O   1 
ATOM   1708 C  CB  . ARG B 1 79  ? 60.075 64.312 -10.322 1.00 18.84 ? 79  ARG B CB  1 
ATOM   1709 C  CG  . ARG B 1 79  ? 60.357 63.486 -11.562 1.00 17.55 ? 79  ARG B CG  1 
ATOM   1710 C  CD  . ARG B 1 79  ? 59.129 62.806 -12.134 1.00 19.14 ? 79  ARG B CD  1 
ATOM   1711 N  NE  . ARG B 1 79  ? 58.801 61.558 -11.447 1.00 18.31 ? 79  ARG B NE  1 
ATOM   1712 C  CZ  . ARG B 1 79  ? 57.944 60.652 -11.906 1.00 18.37 ? 79  ARG B CZ  1 
ATOM   1713 N  NH1 . ARG B 1 79  ? 57.317 60.854 -13.051 1.00 16.03 ? 79  ARG B NH1 1 
ATOM   1714 N  NH2 . ARG B 1 79  ? 57.750 59.514 -11.246 1.00 18.28 ? 79  ARG B NH2 1 
ATOM   1715 N  N   . HIS B 1 80  ? 61.456 63.020 -7.929  1.00 20.07 ? 80  HIS B N   1 
ATOM   1716 C  CA  . HIS B 1 80  ? 61.952 61.809 -7.300  1.00 18.85 ? 80  HIS B CA  1 
ATOM   1717 C  C   . HIS B 1 80  ? 61.310 60.703 -8.135  1.00 18.96 ? 80  HIS B C   1 
ATOM   1718 O  O   . HIS B 1 80  ? 60.242 60.931 -8.691  1.00 20.79 ? 80  HIS B O   1 
ATOM   1719 C  CB  . HIS B 1 80  ? 61.416 61.727 -5.877  1.00 17.56 ? 80  HIS B CB  1 
ATOM   1720 C  CG  . HIS B 1 80  ? 61.895 62.819 -4.981  1.00 15.42 ? 80  HIS B CG  1 
ATOM   1721 N  ND1 . HIS B 1 80  ? 61.135 63.328 -3.951  1.00 16.62 ? 80  HIS B ND1 1 
ATOM   1722 C  CD2 . HIS B 1 80  ? 63.099 63.427 -4.896  1.00 16.00 ? 80  HIS B CD2 1 
ATOM   1723 C  CE1 . HIS B 1 80  ? 61.863 64.188 -3.256  1.00 18.92 ? 80  HIS B CE1 1 
ATOM   1724 N  NE2 . HIS B 1 80  ? 63.056 64.264 -3.812  1.00 16.94 ? 80  HIS B NE2 1 
ATOM   1725 N  N   . VAL B 1 81  ? 61.930 59.529 -8.258  1.00 18.42 ? 81  VAL B N   1 
ATOM   1726 C  CA  . VAL B 1 81  ? 61.313 58.442 -9.030  1.00 17.89 ? 81  VAL B CA  1 
ATOM   1727 C  C   . VAL B 1 81  ? 59.883 58.145 -8.512  1.00 18.77 ? 81  VAL B C   1 
ATOM   1728 O  O   . VAL B 1 81  ? 58.953 57.893 -9.293  1.00 18.67 ? 81  VAL B O   1 
ATOM   1729 C  CB  . VAL B 1 81  ? 62.172 57.126 -8.950  1.00 20.28 ? 81  VAL B CB  1 
ATOM   1730 C  CG1 . VAL B 1 81  ? 61.360 55.909 -9.402  1.00 19.53 ? 81  VAL B CG1 1 
ATOM   1731 C  CG2 . VAL B 1 81  ? 63.428 57.253 -9.810  1.00 21.12 ? 81  VAL B CG2 1 
ATOM   1732 N  N   . GLY B 1 82  ? 59.709 58.217 -7.195  1.00 17.11 ? 82  GLY B N   1 
ATOM   1733 C  CA  . GLY B 1 82  ? 58.412 57.924 -6.618  1.00 17.16 ? 82  GLY B CA  1 
ATOM   1734 C  C   . GLY B 1 82  ? 57.368 59.020 -6.635  1.00 15.20 ? 82  GLY B C   1 
ATOM   1735 O  O   . GLY B 1 82  ? 56.315 58.835 -6.049  1.00 15.35 ? 82  GLY B O   1 
ATOM   1736 N  N   . ASP B 1 83  ? 57.622 60.133 -7.315  1.00 15.11 ? 83  ASP B N   1 
ATOM   1737 C  CA  . ASP B 1 83  ? 56.660 61.236 -7.345  1.00 16.98 ? 83  ASP B CA  1 
ATOM   1738 C  C   . ASP B 1 83  ? 55.549 61.025 -8.358  1.00 16.51 ? 83  ASP B C   1 
ATOM   1739 O  O   . ASP B 1 83  ? 55.732 61.304 -9.540  1.00 18.96 ? 83  ASP B O   1 
ATOM   1740 C  CB  . ASP B 1 83  ? 57.365 62.566 -7.619  1.00 16.34 ? 83  ASP B CB  1 
ATOM   1741 C  CG  . ASP B 1 83  ? 58.222 63.050 -6.436  1.00 17.80 ? 83  ASP B CG  1 
ATOM   1742 O  OD1 . ASP B 1 83  ? 58.135 62.534 -5.291  1.00 16.09 ? 83  ASP B OD1 1 
ATOM   1743 O  OD2 . ASP B 1 83  ? 59.012 63.994 -6.630  1.00 20.20 ? 83  ASP B OD2 1 
ATOM   1744 N  N   . LEU B 1 84  ? 54.388 60.563 -7.887  1.00 15.96 ? 84  LEU B N   1 
ATOM   1745 C  CA  . LEU B 1 84  ? 53.252 60.310 -8.769  1.00 16.48 ? 84  LEU B CA  1 
ATOM   1746 C  C   . LEU B 1 84  ? 52.150 61.388 -8.779  1.00 16.07 ? 84  LEU B C   1 
ATOM   1747 O  O   . LEU B 1 84  ? 51.096 61.226 -9.397  1.00 18.41 ? 84  LEU B O   1 
ATOM   1748 C  CB  . LEU B 1 84  ? 52.673 58.919 -8.507  1.00 16.04 ? 84  LEU B CB  1 
ATOM   1749 C  CG  . LEU B 1 84  ? 53.629 57.762 -8.826  1.00 17.98 ? 84  LEU B CG  1 
ATOM   1750 C  CD1 . LEU B 1 84  ? 53.032 56.469 -8.341  1.00 19.22 ? 84  LEU B CD1 1 
ATOM   1751 C  CD2 . LEU B 1 84  ? 53.933 57.684 -10.331 1.00 18.85 ? 84  LEU B CD2 1 
ATOM   1752 N  N   . GLY B 1 85  ? 52.413 62.511 -8.133  1.00 15.73 ? 85  GLY B N   1 
ATOM   1753 C  CA  . GLY B 1 85  ? 51.450 63.592 -8.123  1.00 17.37 ? 85  GLY B CA  1 
ATOM   1754 C  C   . GLY B 1 85  ? 50.321 63.514 -7.120  1.00 16.46 ? 85  GLY B C   1 
ATOM   1755 O  O   . GLY B 1 85  ? 50.524 63.164 -5.958  1.00 16.82 ? 85  GLY B O   1 
ATOM   1756 N  N   . ASN B 1 86  ? 49.130 63.866 -7.588  1.00 14.99 ? 86  ASN B N   1 
ATOM   1757 C  CA  . ASN B 1 86  ? 47.936 63.881 -6.766  1.00 15.58 ? 86  ASN B CA  1 
ATOM   1758 C  C   . ASN B 1 86  ? 46.871 63.019 -7.347  1.00 16.11 ? 86  ASN B C   1 
ATOM   1759 O  O   . ASN B 1 86  ? 46.782 62.862 -8.561  1.00 17.92 ? 86  ASN B O   1 
ATOM   1760 C  CB  . ASN B 1 86  ? 47.305 65.282 -6.710  1.00 16.27 ? 86  ASN B CB  1 
ATOM   1761 C  CG  . ASN B 1 86  ? 48.153 66.288 -5.989  1.00 16.33 ? 86  ASN B CG  1 
ATOM   1762 O  OD1 . ASN B 1 86  ? 48.690 67.202 -6.601  1.00 20.19 ? 86  ASN B OD1 1 
ATOM   1763 N  ND2 . ASN B 1 86  ? 48.271 66.138 -4.691  1.00 14.34 ? 86  ASN B ND2 1 
ATOM   1764 N  N   . VAL B 1 87  ? 46.062 62.451 -6.466  1.00 17.56 ? 87  VAL B N   1 
ATOM   1765 C  CA  . VAL B 1 87  ? 44.890 61.684 -6.877  1.00 18.04 ? 87  VAL B CA  1 
ATOM   1766 C  C   . VAL B 1 87  ? 43.750 62.594 -6.372  1.00 18.76 ? 87  VAL B C   1 
ATOM   1767 O  O   . VAL B 1 87  ? 43.959 63.394 -5.438  1.00 19.07 ? 87  VAL B O   1 
ATOM   1768 C  CB  . VAL B 1 87  ? 44.828 60.268 -6.244  1.00 17.64 ? 87  VAL B CB  1 
ATOM   1769 C  CG1 . VAL B 1 87  ? 45.946 59.376 -6.815  1.00 14.11 ? 87  VAL B CG1 1 
ATOM   1770 C  CG2 . VAL B 1 87  ? 44.906 60.358 -4.723  1.00 17.85 ? 87  VAL B CG2 1 
ATOM   1771 N  N   . THR B 1 88  ? 42.578 62.544 -6.995  1.00 20.66 ? 88  THR B N   1 
ATOM   1772 C  CA  . THR B 1 88  ? 41.499 63.421 -6.536  1.00 24.18 ? 88  THR B CA  1 
ATOM   1773 C  C   . THR B 1 88  ? 40.298 62.665 -6.007  1.00 22.40 ? 88  THR B C   1 
ATOM   1774 O  O   . THR B 1 88  ? 39.811 61.735 -6.649  1.00 23.39 ? 88  THR B O   1 
ATOM   1775 C  CB  . THR B 1 88  ? 41.038 64.454 -7.622  1.00 27.16 ? 88  THR B CB  1 
ATOM   1776 O  OG1 . THR B 1 88  ? 40.174 63.822 -8.575  1.00 35.50 ? 88  THR B OG1 1 
ATOM   1777 C  CG2 . THR B 1 88  ? 42.232 65.044 -8.360  1.00 28.20 ? 88  THR B CG2 1 
ATOM   1778 N  N   . ALA B 1 89  ? 39.886 63.012 -4.795  1.00 20.95 ? 89  ALA B N   1 
ATOM   1779 C  CA  . ALA B 1 89  ? 38.730 62.386 -4.178  1.00 21.90 ? 89  ALA B CA  1 
ATOM   1780 C  C   . ALA B 1 89  ? 37.528 63.305 -4.407  1.00 22.87 ? 89  ALA B C   1 
ATOM   1781 O  O   . ALA B 1 89  ? 37.650 64.525 -4.296  1.00 20.87 ? 89  ALA B O   1 
ATOM   1782 C  CB  . ALA B 1 89  ? 38.970 62.191 -2.685  1.00 18.58 ? 89  ALA B CB  1 
ATOM   1783 N  N   . ASP B 1 90  ? 36.379 62.729 -4.751  1.00 24.42 ? 90  ASP B N   1 
ATOM   1784 C  CA  . ASP B 1 90  ? 35.182 63.535 -4.975  1.00 25.91 ? 90  ASP B CA  1 
ATOM   1785 C  C   . ASP B 1 90  ? 34.446 63.780 -3.654  1.00 27.57 ? 90  ASP B C   1 
ATOM   1786 O  O   . ASP B 1 90  ? 34.958 63.428 -2.587  1.00 26.80 ? 90  ASP B O   1 
ATOM   1787 C  CB  . ASP B 1 90  ? 34.273 62.871 -6.009  1.00 25.79 ? 90  ASP B CB  1 
ATOM   1788 C  CG  . ASP B 1 90  ? 33.928 61.441 -5.653  1.00 28.65 ? 90  ASP B CG  1 
ATOM   1789 O  OD1 . ASP B 1 90  ? 33.804 61.125 -4.453  1.00 27.81 ? 90  ASP B OD1 1 
ATOM   1790 O  OD2 . ASP B 1 90  ? 33.793 60.611 -6.579  1.00 33.85 ? 90  ASP B OD2 1 
ATOM   1791 N  N   . LYS B 1 91  ? 33.242 64.352 -3.725  1.00 29.95 ? 91  LYS B N   1 
ATOM   1792 C  CA  . LYS B 1 91  ? 32.443 64.648 -2.536  1.00 30.53 ? 91  LYS B CA  1 
ATOM   1793 C  C   . LYS B 1 91  ? 32.084 63.416 -1.711  1.00 29.80 ? 91  LYS B C   1 
ATOM   1794 O  O   . LYS B 1 91  ? 31.752 63.540 -0.539  1.00 30.42 ? 91  LYS B O   1 
ATOM   1795 C  CB  . LYS B 1 91  ? 31.182 65.419 -2.911  1.00 32.88 ? 91  LYS B CB  1 
ATOM   1796 C  CG  . LYS B 1 91  ? 30.301 64.706 -3.907  1.00 38.55 ? 91  LYS B CG  1 
ATOM   1797 C  CD  . LYS B 1 91  ? 29.089 65.567 -4.218  1.00 45.21 ? 91  LYS B CD  1 
ATOM   1798 C  CE  . LYS B 1 91  ? 28.132 64.867 -5.177  1.00 50.49 ? 91  LYS B CE  1 
ATOM   1799 N  NZ  . LYS B 1 91  ? 26.947 65.717 -5.556  1.00 52.96 ? 91  LYS B NZ  1 
ATOM   1800 N  N   . ASP B 1 92  ? 32.139 62.239 -2.329  1.00 29.67 ? 92  ASP B N   1 
ATOM   1801 C  CA  . ASP B 1 92  ? 31.860 60.970 -1.651  1.00 30.23 ? 92  ASP B CA  1 
ATOM   1802 C  C   . ASP B 1 92  ? 33.118 60.339 -1.037  1.00 28.27 ? 92  ASP B C   1 
ATOM   1803 O  O   . ASP B 1 92  ? 33.055 59.245 -0.455  1.00 28.87 ? 92  ASP B O   1 
ATOM   1804 C  CB  . ASP B 1 92  ? 31.244 59.964 -2.624  1.00 34.28 ? 92  ASP B CB  1 
ATOM   1805 C  CG  . ASP B 1 92  ? 29.904 60.414 -3.164  1.00 40.03 ? 92  ASP B CG  1 
ATOM   1806 O  OD1 . ASP B 1 92  ? 29.113 61.017 -2.395  1.00 42.05 ? 92  ASP B OD1 1 
ATOM   1807 O  OD2 . ASP B 1 92  ? 29.652 60.160 -4.363  1.00 42.29 ? 92  ASP B OD2 1 
ATOM   1808 N  N   . GLY B 1 93  ? 34.256 61.001 -1.207  1.00 24.74 ? 93  GLY B N   1 
ATOM   1809 C  CA  . GLY B 1 93  ? 35.503 60.493 -0.667  1.00 23.84 ? 93  GLY B CA  1 
ATOM   1810 C  C   . GLY B 1 93  ? 36.166 59.387 -1.465  1.00 22.35 ? 93  GLY B C   1 
ATOM   1811 O  O   . GLY B 1 93  ? 37.066 58.722 -0.965  1.00 22.18 ? 93  GLY B O   1 
ATOM   1812 N  N   . VAL B 1 94  ? 35.725 59.189 -2.705  1.00 22.62 ? 94  VAL B N   1 
ATOM   1813 C  CA  . VAL B 1 94  ? 36.278 58.165 -3.584  1.00 21.51 ? 94  VAL B CA  1 
ATOM   1814 C  C   . VAL B 1 94  ? 37.231 58.792 -4.586  1.00 23.68 ? 94  VAL B C   1 
ATOM   1815 O  O   . VAL B 1 94  ? 36.912 59.810 -5.200  1.00 22.65 ? 94  VAL B O   1 
ATOM   1816 C  CB  . VAL B 1 94  ? 35.186 57.435 -4.360  1.00 19.23 ? 94  VAL B CB  1 
ATOM   1817 C  CG1 . VAL B 1 94  ? 35.806 56.493 -5.352  1.00 18.99 ? 94  VAL B CG1 1 
ATOM   1818 C  CG2 . VAL B 1 94  ? 34.325 56.667 -3.408  1.00 18.40 ? 94  VAL B CG2 1 
ATOM   1819 N  N   . ALA B 1 95  ? 38.412 58.198 -4.711  1.00 24.89 ? 95  ALA B N   1 
ATOM   1820 C  CA  . ALA B 1 95  ? 39.438 58.663 -5.637  1.00 26.17 ? 95  ALA B CA  1 
ATOM   1821 C  C   . ALA B 1 95  ? 39.670 57.581 -6.686  1.00 28.00 ? 95  ALA B C   1 
ATOM   1822 O  O   . ALA B 1 95  ? 39.974 56.427 -6.369  1.00 29.11 ? 95  ALA B O   1 
ATOM   1823 C  CB  . ALA B 1 95  ? 40.748 58.987 -4.892  1.00 23.43 ? 95  ALA B CB  1 
ATOM   1824 N  N   . ASP B 1 96  ? 39.470 57.957 -7.939  1.00 29.24 ? 96  ASP B N   1 
ATOM   1825 C  CA  . ASP B 1 96  ? 39.649 57.060 -9.055  1.00 29.35 ? 96  ASP B CA  1 
ATOM   1826 C  C   . ASP B 1 96  ? 41.035 57.275 -9.557  1.00 27.30 ? 96  ASP B C   1 
ATOM   1827 O  O   . ASP B 1 96  ? 41.355 58.342 -10.061 1.00 29.53 ? 96  ASP B O   1 
ATOM   1828 C  CB  . ASP B 1 96  ? 38.680 57.421 -10.152 1.00 35.66 ? 96  ASP B CB  1 
ATOM   1829 C  CG  . ASP B 1 96  ? 37.884 56.265 -10.570 1.00 41.63 ? 96  ASP B CG  1 
ATOM   1830 O  OD1 . ASP B 1 96  ? 38.410 55.459 -11.375 1.00 44.29 ? 96  ASP B OD1 1 
ATOM   1831 O  OD2 . ASP B 1 96  ? 36.756 56.138 -10.040 1.00 48.64 ? 96  ASP B OD2 1 
ATOM   1832 N  N   . VAL B 1 97  ? 41.850 56.246 -9.479  1.00 24.02 ? 97  VAL B N   1 
ATOM   1833 C  CA  . VAL B 1 97  ? 43.219 56.398 -9.894  1.00 23.27 ? 97  VAL B CA  1 
ATOM   1834 C  C   . VAL B 1 97  ? 43.491 55.812 -11.268 1.00 24.68 ? 97  VAL B C   1 
ATOM   1835 O  O   . VAL B 1 97  ? 43.200 54.645 -11.523 1.00 23.92 ? 97  VAL B O   1 
ATOM   1836 C  CB  . VAL B 1 97  ? 44.173 55.776 -8.832  1.00 23.72 ? 97  VAL B CB  1 
ATOM   1837 C  CG1 . VAL B 1 97  ? 45.637 55.977 -9.231  1.00 22.31 ? 97  VAL B CG1 1 
ATOM   1838 C  CG2 . VAL B 1 97  ? 43.882 56.398 -7.438  1.00 22.62 ? 97  VAL B CG2 1 
ATOM   1839 N  N   . SER B 1 98  ? 44.024 56.650 -12.153 1.00 24.38 ? 98  SER B N   1 
ATOM   1840 C  CA  . SER B 1 98  ? 44.399 56.254 -13.503 1.00 24.25 ? 98  SER B CA  1 
ATOM   1841 C  C   . SER B 1 98  ? 45.631 57.075 -13.869 1.00 23.61 ? 98  SER B C   1 
ATOM   1842 O  O   . SER B 1 98  ? 45.544 58.257 -14.207 1.00 25.26 ? 98  SER B O   1 
ATOM   1843 C  CB  . SER B 1 98  ? 43.263 56.499 -14.494 1.00 24.79 ? 98  SER B CB  1 
ATOM   1844 O  OG  . SER B 1 98  ? 43.570 55.839 -15.710 1.00 28.92 ? 98  SER B OG  1 
ATOM   1845 N  N   . ILE B 1 99  ? 46.788 56.443 -13.789 1.00 21.65 ? 99  ILE B N   1 
ATOM   1846 C  CA  . ILE B 1 99  ? 48.044 57.115 -14.048 1.00 21.54 ? 99  ILE B CA  1 
ATOM   1847 C  C   . ILE B 1 99  ? 48.863 56.246 -14.981 1.00 24.03 ? 99  ILE B C   1 
ATOM   1848 O  O   . ILE B 1 99  ? 48.702 55.024 -14.997 1.00 24.28 ? 99  ILE B O   1 
ATOM   1849 C  CB  . ILE B 1 99  ? 48.876 57.255 -12.710 1.00 20.68 ? 99  ILE B CB  1 
ATOM   1850 C  CG1 . ILE B 1 99  ? 48.150 58.128 -11.688 1.00 20.95 ? 99  ILE B CG1 1 
ATOM   1851 C  CG2 . ILE B 1 99  ? 50.270 57.827 -12.973 1.00 21.02 ? 99  ILE B CG2 1 
ATOM   1852 C  CD1 . ILE B 1 99  ? 48.886 58.245 -10.364 1.00 19.54 ? 99  ILE B CD1 1 
ATOM   1853 N  N   . GLU B 1 100 ? 49.664 56.882 -15.826 1.00 23.63 ? 100 GLU B N   1 
ATOM   1854 C  CA  . GLU B 1 100 ? 50.581 56.151 -16.677 1.00 25.64 ? 100 GLU B CA  1 
ATOM   1855 C  C   . GLU B 1 100 ? 51.892 56.872 -16.466 1.00 24.26 ? 100 GLU B C   1 
ATOM   1856 O  O   . GLU B 1 100 ? 52.001 58.081 -16.689 1.00 23.22 ? 100 GLU B O   1 
ATOM   1857 C  CB  . GLU B 1 100 ? 50.189 56.165 -18.138 1.00 30.32 ? 100 GLU B CB  1 
ATOM   1858 C  CG  . GLU B 1 100 ? 51.108 55.262 -18.921 1.00 40.06 ? 100 GLU B CG  1 
ATOM   1859 C  CD  . GLU B 1 100 ? 50.720 55.125 -20.365 1.00 46.18 ? 100 GLU B CD  1 
ATOM   1860 O  OE1 . GLU B 1 100 ? 50.355 56.149 -20.988 1.00 52.55 ? 100 GLU B OE1 1 
ATOM   1861 O  OE2 . GLU B 1 100 ? 50.790 53.987 -20.876 1.00 51.81 ? 100 GLU B OE2 1 
ATOM   1862 N  N   . ASP B 1 101 ? 52.881 56.150 -15.985 1.00 21.61 ? 101 ASP B N   1 
ATOM   1863 C  CA  . ASP B 1 101 ? 54.129 56.784 -15.699 1.00 22.43 ? 101 ASP B CA  1 
ATOM   1864 C  C   . ASP B 1 101 ? 55.271 56.029 -16.333 1.00 25.35 ? 101 ASP B C   1 
ATOM   1865 O  O   . ASP B 1 101 ? 55.292 54.813 -16.307 1.00 28.67 ? 101 ASP B O   1 
ATOM   1866 C  CB  . ASP B 1 101 ? 54.291 56.824 -14.193 1.00 21.91 ? 101 ASP B CB  1 
ATOM   1867 C  CG  . ASP B 1 101 ? 55.406 57.721 -13.764 1.00 24.28 ? 101 ASP B CG  1 
ATOM   1868 O  OD1 . ASP B 1 101 ? 55.289 58.952 -13.980 1.00 28.40 ? 101 ASP B OD1 1 
ATOM   1869 O  OD2 . ASP B 1 101 ? 56.397 57.198 -13.218 1.00 23.61 ? 101 ASP B OD2 1 
ATOM   1870 N  N   . SER B 1 102 ? 56.231 56.743 -16.893 1.00 26.04 ? 102 SER B N   1 
ATOM   1871 C  CA  . SER B 1 102 ? 57.367 56.087 -17.520 1.00 28.82 ? 102 SER B CA  1 
ATOM   1872 C  C   . SER B 1 102 ? 58.680 56.174 -16.730 1.00 28.99 ? 102 SER B C   1 
ATOM   1873 O  O   . SER B 1 102 ? 59.721 55.743 -17.225 1.00 30.95 ? 102 SER B O   1 
ATOM   1874 C  CB  . SER B 1 102 ? 57.552 56.644 -18.921 1.00 31.48 ? 102 SER B CB  1 
ATOM   1875 O  OG  . SER B 1 102 ? 57.374 58.049 -18.886 1.00 40.45 ? 102 SER B OG  1 
ATOM   1876 N  N   . VAL B 1 103 ? 58.638 56.773 -15.535 1.00 27.82 ? 103 VAL B N   1 
ATOM   1877 C  CA  . VAL B 1 103 ? 59.821 56.887 -14.669 1.00 26.20 ? 103 VAL B CA  1 
ATOM   1878 C  C   . VAL B 1 103 ? 59.905 55.710 -13.690 1.00 26.23 ? 103 VAL B C   1 
ATOM   1879 O  O   . VAL B 1 103 ? 60.995 55.173 -13.467 1.00 26.90 ? 103 VAL B O   1 
ATOM   1880 C  CB  . VAL B 1 103 ? 59.865 58.241 -13.910 1.00 23.95 ? 103 VAL B CB  1 
ATOM   1881 C  CG1 . VAL B 1 103 ? 61.085 58.332 -12.992 1.00 23.40 ? 103 VAL B CG1 1 
ATOM   1882 C  CG2 . VAL B 1 103 ? 59.881 59.366 -14.907 1.00 25.74 ? 103 VAL B CG2 1 
ATOM   1883 N  N   . ILE B 1 104 ? 58.776 55.325 -13.088 1.00 23.04 ? 104 ILE B N   1 
ATOM   1884 C  CA  . ILE B 1 104 ? 58.771 54.172 -12.187 1.00 22.80 ? 104 ILE B CA  1 
ATOM   1885 C  C   . ILE B 1 104 ? 58.850 52.915 -13.063 1.00 21.99 ? 104 ILE B C   1 
ATOM   1886 O  O   . ILE B 1 104 ? 58.541 52.947 -14.255 1.00 24.06 ? 104 ILE B O   1 
ATOM   1887 C  CB  . ILE B 1 104 ? 57.507 54.092 -11.273 1.00 20.24 ? 104 ILE B CB  1 
ATOM   1888 C  CG1 . ILE B 1 104 ? 56.228 54.074 -12.115 1.00 19.07 ? 104 ILE B CG1 1 
ATOM   1889 C  CG2 . ILE B 1 104 ? 57.512 55.218 -10.239 1.00 20.84 ? 104 ILE B CG2 1 
ATOM   1890 C  CD1 . ILE B 1 104 ? 54.995 53.747 -11.331 1.00 17.76 ? 104 ILE B CD1 1 
ATOM   1891 N  N   . SER B 1 105 ? 59.258 51.808 -12.470 1.00 22.41 ? 105 SER B N   1 
ATOM   1892 C  CA  . SER B 1 105 ? 59.380 50.578 -13.200 1.00 21.67 ? 105 SER B CA  1 
ATOM   1893 C  C   . SER B 1 105 ? 59.037 49.449 -12.277 1.00 21.41 ? 105 SER B C   1 
ATOM   1894 O  O   . SER B 1 105 ? 59.045 49.614 -11.067 1.00 21.20 ? 105 SER B O   1 
ATOM   1895 C  CB  . SER B 1 105 ? 60.816 50.407 -13.672 1.00 20.91 ? 105 SER B CB  1 
ATOM   1896 O  OG  . SER B 1 105 ? 60.902 49.265 -14.486 1.00 24.64 ? 105 SER B OG  1 
ATOM   1897 N  N   . LEU B 1 106 ? 58.657 48.317 -12.843 1.00 23.60 ? 106 LEU B N   1 
ATOM   1898 C  CA  . LEU B 1 106 ? 58.353 47.140 -12.054 1.00 25.58 ? 106 LEU B CA  1 
ATOM   1899 C  C   . LEU B 1 106 ? 59.527 46.176 -12.094 1.00 27.84 ? 106 LEU B C   1 
ATOM   1900 O  O   . LEU B 1 106 ? 59.462 45.081 -11.543 1.00 27.53 ? 106 LEU B O   1 
ATOM   1901 C  CB  . LEU B 1 106 ? 57.075 46.461 -12.533 1.00 23.57 ? 106 LEU B CB  1 
ATOM   1902 C  CG  . LEU B 1 106 ? 55.788 47.259 -12.310 1.00 23.74 ? 106 LEU B CG  1 
ATOM   1903 C  CD1 . LEU B 1 106 ? 54.590 46.427 -12.711 1.00 23.60 ? 106 LEU B CD1 1 
ATOM   1904 C  CD2 . LEU B 1 106 ? 55.673 47.662 -10.844 1.00 21.69 ? 106 LEU B CD2 1 
ATOM   1905 N  N   . SER B 1 107 ? 60.615 46.609 -12.724 1.00 32.74 ? 107 SER B N   1 
ATOM   1906 C  CA  . SER B 1 107 ? 61.836 45.814 -12.852 1.00 38.14 ? 107 SER B CA  1 
ATOM   1907 C  C   . SER B 1 107 ? 63.128 46.674 -12.938 1.00 40.97 ? 107 SER B C   1 
ATOM   1908 O  O   . SER B 1 107 ? 63.122 47.766 -13.514 1.00 42.32 ? 107 SER B O   1 
ATOM   1909 C  CB  . SER B 1 107 ? 61.731 44.858 -14.049 1.00 37.77 ? 107 SER B CB  1 
ATOM   1910 O  OG  . SER B 1 107 ? 61.222 45.517 -15.212 1.00 43.78 ? 107 SER B OG  1 
ATOM   1911 N  N   . GLY B 1 108 ? 64.144 46.213 -12.208 1.00 43.91 ? 108 GLY B N   1 
ATOM   1912 C  CA  . GLY B 1 108 ? 65.475 46.802 -12.163 1.00 47.25 ? 108 GLY B CA  1 
ATOM   1913 C  C   . GLY B 1 108 ? 65.804 48.276 -11.980 1.00 50.06 ? 108 GLY B C   1 
ATOM   1914 O  O   . GLY B 1 108 ? 65.607 49.075 -12.906 1.00 54.10 ? 108 GLY B O   1 
ATOM   1915 N  N   . ASP B 1 109 ? 66.376 48.622 -10.825 1.00 50.71 ? 109 ASP B N   1 
ATOM   1916 C  CA  . ASP B 1 109 ? 66.815 49.994 -10.471 1.00 50.82 ? 109 ASP B CA  1 
ATOM   1917 C  C   . ASP B 1 109 ? 65.763 50.992 -9.986  1.00 47.65 ? 109 ASP B C   1 
ATOM   1918 O  O   . ASP B 1 109 ? 65.820 51.480 -8.858  1.00 47.97 ? 109 ASP B O   1 
ATOM   1919 C  CB  . ASP B 1 109 ? 67.613 50.639 -11.622 1.00 55.89 ? 109 ASP B CB  1 
ATOM   1920 C  CG  . ASP B 1 109 ? 68.825 49.827 -12.034 1.00 60.93 ? 109 ASP B CG  1 
ATOM   1921 O  OD1 . ASP B 1 109 ? 69.487 49.196 -11.155 1.00 61.69 ? 109 ASP B OD1 1 
ATOM   1922 O  OD2 . ASP B 1 109 ? 69.109 49.821 -13.265 1.00 63.33 ? 109 ASP B OD2 1 
ATOM   1923 N  N   . HIS B 1 110 ? 64.860 51.373 -10.878 1.00 43.48 ? 110 HIS B N   1 
ATOM   1924 C  CA  . HIS B 1 110 ? 63.791 52.289 -10.544 1.00 40.18 ? 110 HIS B CA  1 
ATOM   1925 C  C   . HIS B 1 110 ? 62.604 51.430 -10.160 1.00 35.75 ? 110 HIS B C   1 
ATOM   1926 O  O   . HIS B 1 110 ? 61.444 51.866 -10.229 1.00 34.96 ? 110 HIS B O   1 
ATOM   1927 C  CB  . HIS B 1 110 ? 63.439 53.159 -11.741 1.00 41.98 ? 110 HIS B CB  1 
ATOM   1928 C  CG  . HIS B 1 110 ? 64.507 54.148 -12.092 1.00 45.97 ? 110 HIS B CG  1 
ATOM   1929 N  ND1 . HIS B 1 110 ? 64.281 55.221 -12.924 1.00 48.04 ? 110 HIS B ND1 1 
ATOM   1930 C  CD2 . HIS B 1 110 ? 65.808 54.231 -11.719 1.00 46.93 ? 110 HIS B CD2 1 
ATOM   1931 C  CE1 . HIS B 1 110 ? 65.395 55.922 -13.050 1.00 48.77 ? 110 HIS B CE1 1 
ATOM   1932 N  NE2 . HIS B 1 110 ? 66.338 55.343 -12.329 1.00 49.14 ? 110 HIS B NE2 1 
ATOM   1933 N  N   . CYS B 1 111 ? 62.931 50.202 -9.757  1.00 30.60 ? 111 CYS B N   1 
ATOM   1934 C  CA  . CYS B 1 111 ? 62.005 49.162 -9.376  1.00 25.98 ? 111 CYS B CA  1 
ATOM   1935 C  C   . CYS B 1 111 ? 61.303 49.535 -8.087  1.00 21.67 ? 111 CYS B C   1 
ATOM   1936 O  O   . CYS B 1 111 ? 61.961 49.799 -7.087  1.00 20.83 ? 111 CYS B O   1 
ATOM   1937 C  CB  . CYS B 1 111 ? 62.796 47.880 -9.177  1.00 29.05 ? 111 CYS B CB  1 
ATOM   1938 S  SG  . CYS B 1 111 ? 61.830 46.476 -8.735  1.00 37.19 ? 111 CYS B SG  1 
ATOM   1939 N  N   . ILE B 1 112 ? 59.972 49.488 -8.092  1.00 20.10 ? 112 ILE B N   1 
ATOM   1940 C  CA  . ILE B 1 112 ? 59.192 49.844 -6.916  1.00 16.96 ? 112 ILE B CA  1 
ATOM   1941 C  C   . ILE B 1 112 ? 58.615 48.667 -6.155  1.00 15.05 ? 112 ILE B C   1 
ATOM   1942 O  O   . ILE B 1 112 ? 57.903 48.846 -5.175  1.00 15.01 ? 112 ILE B O   1 
ATOM   1943 C  CB  . ILE B 1 112 ? 58.088 50.855 -7.283  1.00 17.15 ? 112 ILE B CB  1 
ATOM   1944 C  CG1 . ILE B 1 112 ? 57.086 50.245 -8.274  1.00 19.62 ? 112 ILE B CG1 1 
ATOM   1945 C  CG2 . ILE B 1 112 ? 58.716 52.112 -7.897  1.00 19.75 ? 112 ILE B CG2 1 
ATOM   1946 C  CD1 . ILE B 1 112 ? 55.864 51.114 -8.525  1.00 15.61 ? 112 ILE B CD1 1 
ATOM   1947 N  N   . ILE B 1 113 ? 58.922 47.456 -6.598  1.00 15.36 ? 113 ILE B N   1 
ATOM   1948 C  CA  . ILE B 1 113 ? 58.430 46.256 -5.923  1.00 15.74 ? 113 ILE B CA  1 
ATOM   1949 C  C   . ILE B 1 113 ? 59.060 46.189 -4.537  1.00 14.90 ? 113 ILE B C   1 
ATOM   1950 O  O   . ILE B 1 113 ? 60.256 46.396 -4.393  1.00 15.63 ? 113 ILE B O   1 
ATOM   1951 C  CB  . ILE B 1 113 ? 58.818 44.971 -6.703  1.00 17.65 ? 113 ILE B CB  1 
ATOM   1952 C  CG1 . ILE B 1 113 ? 58.159 44.963 -8.083  1.00 19.36 ? 113 ILE B CG1 1 
ATOM   1953 C  CG2 . ILE B 1 113 ? 58.435 43.734 -5.894  1.00 16.42 ? 113 ILE B CG2 1 
ATOM   1954 C  CD1 . ILE B 1 113 ? 56.705 44.631 -8.065  1.00 21.46 ? 113 ILE B CD1 1 
ATOM   1955 N  N   . GLY B 1 114 ? 58.250 45.895 -3.526  1.00 14.46 ? 114 GLY B N   1 
ATOM   1956 C  CA  . GLY B 1 114 ? 58.745 45.815 -2.169  1.00 13.30 ? 114 GLY B CA  1 
ATOM   1957 C  C   . GLY B 1 114 ? 58.918 47.170 -1.513  1.00 14.80 ? 114 GLY B C   1 
ATOM   1958 O  O   . GLY B 1 114 ? 59.570 47.270 -0.475  1.00 14.65 ? 114 GLY B O   1 
ATOM   1959 N  N   . ARG B 1 115 ? 58.400 48.223 -2.140  1.00 15.30 ? 115 ARG B N   1 
ATOM   1960 C  CA  . ARG B 1 115 ? 58.475 49.562 -1.567  1.00 15.87 ? 115 ARG B CA  1 
ATOM   1961 C  C   . ARG B 1 115 ? 57.069 49.975 -1.134  1.00 15.68 ? 115 ARG B C   1 
ATOM   1962 O  O   . ARG B 1 115 ? 56.137 49.189 -1.290  1.00 16.36 ? 115 ARG B O   1 
ATOM   1963 C  CB  . ARG B 1 115 ? 59.126 50.535 -2.546  1.00 14.22 ? 115 ARG B CB  1 
ATOM   1964 C  CG  . ARG B 1 115 ? 60.577 50.134 -2.801  1.00 16.12 ? 115 ARG B CG  1 
ATOM   1965 C  CD  . ARG B 1 115 ? 61.280 51.105 -3.669  1.00 16.44 ? 115 ARG B CD  1 
ATOM   1966 N  NE  . ARG B 1 115 ? 62.579 50.597 -4.107  1.00 21.88 ? 115 ARG B NE  1 
ATOM   1967 C  CZ  . ARG B 1 115 ? 63.711 50.628 -3.399  1.00 22.23 ? 115 ARG B CZ  1 
ATOM   1968 N  NH1 . ARG B 1 115 ? 63.761 51.136 -2.175  1.00 22.13 ? 115 ARG B NH1 1 
ATOM   1969 N  NH2 . ARG B 1 115 ? 64.828 50.195 -3.953  1.00 21.50 ? 115 ARG B NH2 1 
ATOM   1970 N  N   . THR B 1 116 ? 56.916 51.155 -0.538  1.00 16.69 ? 116 THR B N   1 
ATOM   1971 C  CA  . THR B 1 116 ? 55.607 51.579 -0.031  1.00 16.62 ? 116 THR B CA  1 
ATOM   1972 C  C   . THR B 1 116 ? 54.914 52.682 -0.819  1.00 16.48 ? 116 THR B C   1 
ATOM   1973 O  O   . THR B 1 116 ? 55.494 53.707 -1.134  1.00 16.97 ? 116 THR B O   1 
ATOM   1974 C  CB  . THR B 1 116 ? 55.690 51.997 1.485   1.00 16.06 ? 116 THR B CB  1 
ATOM   1975 O  OG1 . THR B 1 116 ? 56.145 50.892 2.271   1.00 17.31 ? 116 THR B OG1 1 
ATOM   1976 C  CG2 . THR B 1 116 ? 54.330 52.426 2.038   1.00 16.26 ? 116 THR B CG2 1 
ATOM   1977 N  N   . LEU B 1 117 ? 53.671 52.431 -1.185  1.00 15.85 ? 117 LEU B N   1 
ATOM   1978 C  CA  . LEU B 1 117 ? 52.885 53.421 -1.884  1.00 13.93 ? 117 LEU B CA  1 
ATOM   1979 C  C   . LEU B 1 117 ? 52.090 54.113 -0.774  1.00 16.84 ? 117 LEU B C   1 
ATOM   1980 O  O   . LEU B 1 117 ? 51.525 53.434 0.092   1.00 17.25 ? 117 LEU B O   1 
ATOM   1981 C  CB  . LEU B 1 117 ? 51.930 52.741 -2.857  1.00 14.72 ? 117 LEU B CB  1 
ATOM   1982 C  CG  . LEU B 1 117 ? 50.999 53.637 -3.670  1.00 17.63 ? 117 LEU B CG  1 
ATOM   1983 C  CD1 . LEU B 1 117 ? 51.810 54.497 -4.630  1.00 18.06 ? 117 LEU B CD1 1 
ATOM   1984 C  CD2 . LEU B 1 117 ? 49.998 52.768 -4.425  1.00 15.72 ? 117 LEU B CD2 1 
ATOM   1985 N  N   . VAL B 1 118 ? 52.083 55.447 -0.752  1.00 15.36 ? 118 VAL B N   1 
ATOM   1986 C  CA  . VAL B 1 118 ? 51.334 56.161 0.265   1.00 15.26 ? 118 VAL B CA  1 
ATOM   1987 C  C   . VAL B 1 118 ? 50.481 57.288 -0.311  1.00 15.14 ? 118 VAL B C   1 
ATOM   1988 O  O   . VAL B 1 118 ? 50.815 57.877 -1.336  1.00 14.64 ? 118 VAL B O   1 
ATOM   1989 C  CB  . VAL B 1 118 ? 52.230 56.658 1.506   1.00 18.83 ? 118 VAL B CB  1 
ATOM   1990 C  CG1 . VAL B 1 118 ? 53.606 56.019 1.523   1.00 14.06 ? 118 VAL B CG1 1 
ATOM   1991 C  CG2 . VAL B 1 118 ? 52.282 58.164 1.620   1.00 18.65 ? 118 VAL B CG2 1 
ATOM   1992 N  N   . VAL B 1 119 ? 49.311 57.472 0.288   1.00 15.77 ? 119 VAL B N   1 
ATOM   1993 C  CA  . VAL B 1 119 ? 48.386 58.532 -0.084  1.00 16.37 ? 119 VAL B CA  1 
ATOM   1994 C  C   . VAL B 1 119 ? 48.390 59.468 1.129   1.00 14.82 ? 119 VAL B C   1 
ATOM   1995 O  O   . VAL B 1 119 ? 48.301 59.037 2.279   1.00 15.28 ? 119 VAL B O   1 
ATOM   1996 C  CB  . VAL B 1 119 ? 46.951 58.006 -0.467  1.00 17.62 ? 119 VAL B CB  1 
ATOM   1997 C  CG1 . VAL B 1 119 ? 46.262 57.353 0.698   1.00 20.02 ? 119 VAL B CG1 1 
ATOM   1998 C  CG2 . VAL B 1 119 ? 46.098 59.136 -0.986  1.00 17.41 ? 119 VAL B CG2 1 
ATOM   1999 N  N   . HIS B 1 120 ? 48.549 60.749 0.844   1.00 15.92 ? 120 HIS B N   1 
ATOM   2000 C  CA  . HIS B 1 120 ? 48.653 61.787 1.836   1.00 14.30 ? 120 HIS B CA  1 
ATOM   2001 C  C   . HIS B 1 120 ? 47.427 62.574 2.172   1.00 15.15 ? 120 HIS B C   1 
ATOM   2002 O  O   . HIS B 1 120 ? 46.487 62.664 1.395   1.00 17.96 ? 120 HIS B O   1 
ATOM   2003 C  CB  . HIS B 1 120 ? 49.718 62.768 1.402   1.00 13.29 ? 120 HIS B CB  1 
ATOM   2004 C  CG  . HIS B 1 120 ? 51.088 62.198 1.417   1.00 15.94 ? 120 HIS B CG  1 
ATOM   2005 N  ND1 . HIS B 1 120 ? 51.872 62.188 2.546   1.00 15.02 ? 120 HIS B ND1 1 
ATOM   2006 C  CD2 . HIS B 1 120 ? 51.823 61.615 0.442   1.00 16.04 ? 120 HIS B CD2 1 
ATOM   2007 C  CE1 . HIS B 1 120 ? 53.030 61.626 2.271   1.00 14.59 ? 120 HIS B CE1 1 
ATOM   2008 N  NE2 . HIS B 1 120 ? 53.026 61.268 0.998   1.00 16.92 ? 120 HIS B NE2 1 
ATOM   2009 N  N   . GLU B 1 121 ? 47.565 63.287 3.275   1.00 16.91 ? 121 GLU B N   1 
ATOM   2010 C  CA  . GLU B 1 121 ? 46.555 64.151 3.852   1.00 18.62 ? 121 GLU B CA  1 
ATOM   2011 C  C   . GLU B 1 121 ? 46.164 65.351 2.996   1.00 20.17 ? 121 GLU B C   1 
ATOM   2012 O  O   . GLU B 1 121 ? 44.975 65.628 2.800   1.00 19.39 ? 121 GLU B O   1 
ATOM   2013 C  CB  . GLU B 1 121 ? 47.094 64.640 5.178   1.00 21.56 ? 121 GLU B CB  1 
ATOM   2014 C  CG  . GLU B 1 121 ? 46.320 65.746 5.818   1.00 28.06 ? 121 GLU B CG  1 
ATOM   2015 C  CD  . GLU B 1 121 ? 46.939 66.160 7.142   1.00 32.88 ? 121 GLU B CD  1 
ATOM   2016 O  OE1 . GLU B 1 121 ? 48.174 66.383 7.195   1.00 34.78 ? 121 GLU B OE1 1 
ATOM   2017 O  OE2 . GLU B 1 121 ? 46.192 66.250 8.136   1.00 38.12 ? 121 GLU B OE2 1 
ATOM   2018 N  N   . LYS B 1 122 ? 47.173 66.072 2.517   1.00 21.43 ? 122 LYS B N   1 
ATOM   2019 C  CA  . LYS B 1 122 ? 46.959 67.267 1.721   1.00 22.17 ? 122 LYS B CA  1 
ATOM   2020 C  C   . LYS B 1 122 ? 47.446 67.080 0.310   1.00 20.52 ? 122 LYS B C   1 
ATOM   2021 O  O   . LYS B 1 122 ? 48.063 66.071 -0.030  1.00 19.95 ? 122 LYS B O   1 
ATOM   2022 C  CB  . LYS B 1 122 ? 47.716 68.471 2.328   1.00 25.79 ? 122 LYS B CB  1 
ATOM   2023 C  CG  . LYS B 1 122 ? 47.314 68.862 3.730   1.00 30.79 ? 122 LYS B CG  1 
ATOM   2024 C  CD  . LYS B 1 122 ? 45.790 68.818 3.838   1.00 42.61 ? 122 LYS B CD  1 
ATOM   2025 C  CE  . LYS B 1 122 ? 45.255 69.356 5.176   1.00 49.06 ? 122 LYS B CE  1 
ATOM   2026 N  NZ  . LYS B 1 122 ? 43.827 68.943 5.448   1.00 49.84 ? 122 LYS B NZ  1 
ATOM   2027 N  N   . ALA B 1 123 ? 47.228 68.112 -0.490  1.00 18.96 ? 123 ALA B N   1 
ATOM   2028 C  CA  . ALA B 1 123 ? 47.661 68.123 -1.868  1.00 17.84 ? 123 ALA B CA  1 
ATOM   2029 C  C   . ALA B 1 123 ? 49.166 68.313 -1.955  1.00 19.36 ? 123 ALA B C   1 
ATOM   2030 O  O   . ALA B 1 123 ? 49.779 68.990 -1.128  1.00 19.85 ? 123 ALA B O   1 
ATOM   2031 C  CB  . ALA B 1 123 ? 46.981 69.253 -2.618  1.00 16.19 ? 123 ALA B CB  1 
ATOM   2032 N  N   . ASP B 1 124 ? 49.762 67.657 -2.936  1.00 18.53 ? 124 ASP B N   1 
ATOM   2033 C  CA  . ASP B 1 124 ? 51.177 67.792 -3.232  1.00 17.20 ? 124 ASP B CA  1 
ATOM   2034 C  C   . ASP B 1 124 ? 51.280 69.085 -4.090  1.00 15.97 ? 124 ASP B C   1 
ATOM   2035 O  O   . ASP B 1 124 ? 50.582 69.222 -5.075  1.00 14.40 ? 124 ASP B O   1 
ATOM   2036 C  CB  . ASP B 1 124 ? 51.589 66.550 -4.038  1.00 17.22 ? 124 ASP B CB  1 
ATOM   2037 C  CG  . ASP B 1 124 ? 53.066 66.506 -4.381  1.00 18.89 ? 124 ASP B CG  1 
ATOM   2038 O  OD1 . ASP B 1 124 ? 53.758 67.540 -4.320  1.00 20.07 ? 124 ASP B OD1 1 
ATOM   2039 O  OD2 . ASP B 1 124 ? 53.541 65.413 -4.737  1.00 19.32 ? 124 ASP B OD2 1 
ATOM   2040 N  N   . ASP B 1 125 ? 52.143 70.026 -3.722  1.00 16.92 ? 125 ASP B N   1 
ATOM   2041 C  CA  . ASP B 1 125 ? 52.273 71.261 -4.499  1.00 19.43 ? 125 ASP B CA  1 
ATOM   2042 C  C   . ASP B 1 125 ? 53.198 71.098 -5.711  1.00 21.02 ? 125 ASP B C   1 
ATOM   2043 O  O   . ASP B 1 125 ? 53.480 72.046 -6.442  1.00 19.32 ? 125 ASP B O   1 
ATOM   2044 C  CB  . ASP B 1 125 ? 52.699 72.453 -3.618  1.00 18.83 ? 125 ASP B CB  1 
ATOM   2045 C  CG  . ASP B 1 125 ? 54.054 72.263 -2.942  1.00 16.68 ? 125 ASP B CG  1 
ATOM   2046 O  OD1 . ASP B 1 125 ? 54.927 71.546 -3.459  1.00 17.51 ? 125 ASP B OD1 1 
ATOM   2047 O  OD2 . ASP B 1 125 ? 54.257 72.874 -1.877  1.00 20.24 ? 125 ASP B OD2 1 
ATOM   2048 N  N   . LEU B 1 126 ? 53.686 69.874 -5.887  1.00 19.74 ? 126 LEU B N   1 
ATOM   2049 C  CA  . LEU B 1 126 ? 54.552 69.500 -6.989  1.00 17.45 ? 126 LEU B CA  1 
ATOM   2050 C  C   . LEU B 1 126 ? 55.886 70.234 -7.014  1.00 17.87 ? 126 LEU B C   1 
ATOM   2051 O  O   . LEU B 1 126 ? 56.494 70.380 -8.063  1.00 18.86 ? 126 LEU B O   1 
ATOM   2052 C  CB  . LEU B 1 126 ? 53.794 69.665 -8.314  1.00 17.43 ? 126 LEU B CB  1 
ATOM   2053 C  CG  . LEU B 1 126 ? 52.378 69.064 -8.387  1.00 18.02 ? 126 LEU B CG  1 
ATOM   2054 C  CD1 . LEU B 1 126 ? 51.845 69.345 -9.774  1.00 17.20 ? 126 LEU B CD1 1 
ATOM   2055 C  CD2 . LEU B 1 126 ? 52.339 67.544 -8.086  1.00 12.71 ? 126 LEU B CD2 1 
ATOM   2056 N  N   . GLY B 1 127 ? 56.346 70.663 -5.850  1.00 20.74 ? 127 GLY B N   1 
ATOM   2057 C  CA  . GLY B 1 127 ? 57.607 71.375 -5.753  1.00 25.01 ? 127 GLY B CA  1 
ATOM   2058 C  C   . GLY B 1 127 ? 57.539 72.878 -6.009  1.00 28.52 ? 127 GLY B C   1 
ATOM   2059 O  O   . GLY B 1 127 ? 58.495 73.594 -5.697  1.00 32.38 ? 127 GLY B O   1 
ATOM   2060 N  N   . LYS B 1 128 ? 56.386 73.368 -6.470  1.00 28.75 ? 128 LYS B N   1 
ATOM   2061 C  CA  . LYS B 1 128 ? 56.185 74.785 -6.808  1.00 27.83 ? 128 LYS B CA  1 
ATOM   2062 C  C   . LYS B 1 128 ? 55.817 75.679 -5.644  1.00 29.12 ? 128 LYS B C   1 
ATOM   2063 O  O   . LYS B 1 128 ? 55.605 76.869 -5.839  1.00 29.29 ? 128 LYS B O   1 
ATOM   2064 C  CB  . LYS B 1 128 ? 55.057 74.951 -7.839  1.00 25.63 ? 128 LYS B CB  1 
ATOM   2065 C  CG  . LYS B 1 128 ? 54.934 73.886 -8.913  1.00 22.81 ? 128 LYS B CG  1 
ATOM   2066 C  CD  . LYS B 1 128 ? 56.176 73.721 -9.739  1.00 23.21 ? 128 LYS B CD  1 
ATOM   2067 C  CE  . LYS B 1 128 ? 55.937 72.663 -10.790 1.00 24.40 ? 128 LYS B CE  1 
ATOM   2068 N  NZ  . LYS B 1 128 ? 57.147 72.410 -11.591 1.00 29.56 ? 128 LYS B NZ  1 
ATOM   2069 N  N   . GLY B 1 129 ? 55.743 75.109 -4.449  1.00 29.53 ? 129 GLY B N   1 
ATOM   2070 C  CA  . GLY B 1 129 ? 55.336 75.850 -3.265  1.00 32.92 ? 129 GLY B CA  1 
ATOM   2071 C  C   . GLY B 1 129 ? 56.196 76.982 -2.742  1.00 33.87 ? 129 GLY B C   1 
ATOM   2072 O  O   . GLY B 1 129 ? 55.774 77.721 -1.847  1.00 33.71 ? 129 GLY B O   1 
ATOM   2073 N  N   . GLY B 1 130 ? 57.425 77.075 -3.226  1.00 36.25 ? 130 GLY B N   1 
ATOM   2074 C  CA  . GLY B 1 130 ? 58.285 78.156 -2.787  1.00 40.32 ? 130 GLY B CA  1 
ATOM   2075 C  C   . GLY B 1 130 ? 58.823 78.151 -1.364  1.00 42.37 ? 130 GLY B C   1 
ATOM   2076 O  O   . GLY B 1 130 ? 59.142 79.214 -0.833  1.00 43.85 ? 130 GLY B O   1 
ATOM   2077 N  N   . ASN B 1 131 ? 58.939 76.979 -0.747  1.00 43.31 ? 131 ASN B N   1 
ATOM   2078 C  CA  . ASN B 1 131 ? 59.500 76.867 0.602   1.00 43.19 ? 131 ASN B CA  1 
ATOM   2079 C  C   . ASN B 1 131 ? 60.363 75.601 0.635   1.00 43.98 ? 131 ASN B C   1 
ATOM   2080 O  O   . ASN B 1 131 ? 60.410 74.859 -0.354  1.00 43.95 ? 131 ASN B O   1 
ATOM   2081 C  CB  . ASN B 1 131 ? 58.418 76.907 1.708   1.00 41.72 ? 131 ASN B CB  1 
ATOM   2082 C  CG  . ASN B 1 131 ? 57.619 75.628 1.824   1.00 40.51 ? 131 ASN B CG  1 
ATOM   2083 O  OD1 . ASN B 1 131 ? 57.506 75.073 2.902   1.00 41.80 ? 131 ASN B OD1 1 
ATOM   2084 N  ND2 . ASN B 1 131 ? 57.031 75.184 0.734   1.00 40.33 ? 131 ASN B ND2 1 
ATOM   2085 N  N   . GLU B 1 132 ? 61.097 75.388 1.722   1.00 44.70 ? 132 GLU B N   1 
ATOM   2086 C  CA  . GLU B 1 132 ? 61.980 74.225 1.843   1.00 46.29 ? 132 GLU B CA  1 
ATOM   2087 C  C   . GLU B 1 132 ? 61.265 72.899 1.606   1.00 42.70 ? 132 GLU B C   1 
ATOM   2088 O  O   . GLU B 1 132 ? 61.590 72.169 0.676   1.00 41.28 ? 132 GLU B O   1 
ATOM   2089 C  CB  . GLU B 1 132 ? 62.624 74.182 3.231   1.00 53.95 ? 132 GLU B CB  1 
ATOM   2090 C  CG  . GLU B 1 132 ? 63.330 75.467 3.659   1.00 67.14 ? 132 GLU B CG  1 
ATOM   2091 C  CD  . GLU B 1 132 ? 64.595 75.746 2.853   1.00 73.59 ? 132 GLU B CD  1 
ATOM   2092 O  OE1 . GLU B 1 132 ? 65.658 75.174 3.207   1.00 76.79 ? 132 GLU B OE1 1 
ATOM   2093 O  OE2 . GLU B 1 132 ? 64.524 76.532 1.874   1.00 75.64 ? 132 GLU B OE2 1 
ATOM   2094 N  N   . GLU B 1 133 ? 60.269 72.619 2.441   1.00 39.39 ? 133 GLU B N   1 
ATOM   2095 C  CA  . GLU B 1 133 ? 59.490 71.384 2.383   1.00 37.17 ? 133 GLU B CA  1 
ATOM   2096 C  C   . GLU B 1 133 ? 58.897 71.040 1.016   1.00 34.01 ? 133 GLU B C   1 
ATOM   2097 O  O   . GLU B 1 133 ? 58.710 69.864 0.683   1.00 30.73 ? 133 GLU B O   1 
ATOM   2098 C  CB  . GLU B 1 133 ? 58.381 71.440 3.434   1.00 38.45 ? 133 GLU B CB  1 
ATOM   2099 C  CG  . GLU B 1 133 ? 57.651 70.124 3.660   1.00 43.85 ? 133 GLU B CG  1 
ATOM   2100 C  CD  . GLU B 1 133 ? 58.510 69.065 4.335   1.00 45.64 ? 133 GLU B CD  1 
ATOM   2101 O  OE1 . GLU B 1 133 ? 59.729 69.284 4.515   1.00 48.83 ? 133 GLU B OE1 1 
ATOM   2102 O  OE2 . GLU B 1 133 ? 57.957 68.009 4.702   1.00 48.31 ? 133 GLU B OE2 1 
ATOM   2103 N  N   . SER B 1 134 ? 58.604 72.068 0.233   1.00 29.98 ? 134 SER B N   1 
ATOM   2104 C  CA  . SER B 1 134 ? 58.035 71.879 -1.082  1.00 29.21 ? 134 SER B CA  1 
ATOM   2105 C  C   . SER B 1 134 ? 58.923 71.001 -1.954  1.00 27.73 ? 134 SER B C   1 
ATOM   2106 O  O   . SER B 1 134 ? 58.425 70.095 -2.638  1.00 25.51 ? 134 SER B O   1 
ATOM   2107 C  CB  . SER B 1 134 ? 57.801 73.229 -1.754  1.00 27.41 ? 134 SER B CB  1 
ATOM   2108 O  OG  . SER B 1 134 ? 57.323 73.050 -3.068  1.00 27.95 ? 134 SER B OG  1 
ATOM   2109 N  N   . THR B 1 135 ? 60.231 71.248 -1.908  1.00 26.38 ? 135 THR B N   1 
ATOM   2110 C  CA  . THR B 1 135 ? 61.182 70.478 -2.700  1.00 27.16 ? 135 THR B CA  1 
ATOM   2111 C  C   . THR B 1 135 ? 61.557 69.110 -2.104  1.00 26.96 ? 135 THR B C   1 
ATOM   2112 O  O   . THR B 1 135 ? 62.351 68.374 -2.691  1.00 27.30 ? 135 THR B O   1 
ATOM   2113 C  CB  . THR B 1 135 ? 62.474 71.290 -2.986  1.00 28.44 ? 135 THR B CB  1 
ATOM   2114 O  OG1 . THR B 1 135 ? 63.153 71.593 -1.760  1.00 32.06 ? 135 THR B OG1 1 
ATOM   2115 C  CG2 . THR B 1 135 ? 62.131 72.574 -3.700  1.00 30.53 ? 135 THR B CG2 1 
ATOM   2116 N  N   . LYS B 1 136 ? 60.948 68.740 -0.979  1.00 27.48 ? 136 LYS B N   1 
ATOM   2117 C  CA  . LYS B 1 136 ? 61.233 67.463 -0.321  1.00 27.41 ? 136 LYS B CA  1 
ATOM   2118 C  C   . LYS B 1 136 ? 60.035 66.527 -0.335  1.00 25.41 ? 136 LYS B C   1 
ATOM   2119 O  O   . LYS B 1 136 ? 60.135 65.383 -0.808  1.00 24.24 ? 136 LYS B O   1 
ATOM   2120 C  CB  . LYS B 1 136 ? 61.666 67.690 1.126   1.00 28.79 ? 136 LYS B CB  1 
ATOM   2121 C  CG  . LYS B 1 136 ? 63.133 68.057 1.283   1.00 37.11 ? 136 LYS B CG  1 
ATOM   2122 C  CD  . LYS B 1 136 ? 63.438 68.658 2.657   1.00 43.65 ? 136 LYS B CD  1 
ATOM   2123 C  CE  . LYS B 1 136 ? 62.553 68.075 3.784   1.00 50.13 ? 136 LYS B CE  1 
ATOM   2124 N  NZ  . LYS B 1 136 ? 62.680 66.591 4.008   1.00 55.42 ? 136 LYS B NZ  1 
ATOM   2125 N  N   . THR B 1 137 ? 58.895 67.047 0.119   1.00 23.17 ? 137 THR B N   1 
ATOM   2126 C  CA  . THR B 1 137 ? 57.654 66.285 0.218   1.00 23.67 ? 137 THR B CA  1 
ATOM   2127 C  C   . THR B 1 137 ? 56.508 66.897 -0.552  1.00 22.78 ? 137 THR B C   1 
ATOM   2128 O  O   . THR B 1 137 ? 55.428 66.294 -0.646  1.00 22.54 ? 137 THR B O   1 
ATOM   2129 C  CB  . THR B 1 137 ? 57.170 66.210 1.674   1.00 25.17 ? 137 THR B CB  1 
ATOM   2130 O  OG1 . THR B 1 137 ? 56.842 67.531 2.135   1.00 27.10 ? 137 THR B OG1 1 
ATOM   2131 C  CG2 . THR B 1 137 ? 58.239 65.601 2.578   1.00 26.53 ? 137 THR B CG2 1 
ATOM   2132 N  N   . GLY B 1 138 ? 56.736 68.094 -1.087  1.00 22.58 ? 138 GLY B N   1 
ATOM   2133 C  CA  . GLY B 1 138 ? 55.691 68.793 -1.807  1.00 21.05 ? 138 GLY B CA  1 
ATOM   2134 C  C   . GLY B 1 138 ? 54.612 69.275 -0.846  1.00 22.30 ? 138 GLY B C   1 
ATOM   2135 O  O   . GLY B 1 138 ? 53.507 69.581 -1.280  1.00 23.12 ? 138 GLY B O   1 
ATOM   2136 N  N   . ASN B 1 139 ? 54.915 69.320 0.455   1.00 22.92 ? 139 ASN B N   1 
ATOM   2137 C  CA  . ASN B 1 139 ? 53.964 69.763 1.482   1.00 22.15 ? 139 ASN B CA  1 
ATOM   2138 C  C   . ASN B 1 139 ? 52.665 68.946 1.523   1.00 23.30 ? 139 ASN B C   1 
ATOM   2139 O  O   . ASN B 1 139 ? 51.620 69.458 1.929   1.00 22.54 ? 139 ASN B O   1 
ATOM   2140 C  CB  . ASN B 1 139 ? 53.616 71.246 1.286   1.00 23.92 ? 139 ASN B CB  1 
ATOM   2141 C  CG  . ASN B 1 139 ? 54.763 72.166 1.619   1.00 21.94 ? 139 ASN B CG  1 
ATOM   2142 O  OD1 . ASN B 1 139 ? 55.374 72.759 0.737   1.00 25.95 ? 139 ASN B OD1 1 
ATOM   2143 N  ND2 . ASN B 1 139 ? 55.059 72.297 2.899   1.00 27.48 ? 139 ASN B ND2 1 
ATOM   2144 N  N   . ALA B 1 140 ? 52.745 67.657 1.189   1.00 22.34 ? 140 ALA B N   1 
ATOM   2145 C  CA  . ALA B 1 140 ? 51.563 66.806 1.165   1.00 21.02 ? 140 ALA B CA  1 
ATOM   2146 C  C   . ALA B 1 140 ? 51.005 66.379 2.539   1.00 20.25 ? 140 ALA B C   1 
ATOM   2147 O  O   . ALA B 1 140 ? 49.963 65.729 2.606   1.00 22.04 ? 140 ALA B O   1 
ATOM   2148 C  CB  . ALA B 1 140 ? 51.818 65.601 0.272   1.00 19.55 ? 140 ALA B CB  1 
ATOM   2149 N  N   . GLY B 1 141 ? 51.702 66.714 3.623   1.00 20.15 ? 141 GLY B N   1 
ATOM   2150 C  CA  . GLY B 1 141 ? 51.219 66.387 4.955   1.00 19.80 ? 141 GLY B CA  1 
ATOM   2151 C  C   . GLY B 1 141 ? 51.379 64.952 5.414   1.00 20.57 ? 141 GLY B C   1 
ATOM   2152 O  O   . GLY B 1 141 ? 52.212 64.224 4.898   1.00 21.46 ? 141 GLY B O   1 
ATOM   2153 N  N   . SER B 1 142 ? 50.541 64.529 6.354   1.00 21.57 ? 142 SER B N   1 
ATOM   2154 C  CA  . SER B 1 142 ? 50.608 63.177 6.912   1.00 20.24 ? 142 SER B CA  1 
ATOM   2155 C  C   . SER B 1 142 ? 50.261 62.063 5.914   1.00 19.20 ? 142 SER B C   1 
ATOM   2156 O  O   . SER B 1 142 ? 49.745 62.317 4.828   1.00 19.29 ? 142 SER B O   1 
ATOM   2157 C  CB  . SER B 1 142 ? 49.754 63.076 8.204   1.00 22.01 ? 142 SER B CB  1 
ATOM   2158 O  OG  . SER B 1 142 ? 48.357 63.207 7.956   1.00 25.79 ? 142 SER B OG  1 
ATOM   2159 N  N   . ARG B 1 143 ? 50.597 60.834 6.293   1.00 17.58 ? 143 ARG B N   1 
ATOM   2160 C  CA  . ARG B 1 143 ? 50.359 59.637 5.487   1.00 15.99 ? 143 ARG B CA  1 
ATOM   2161 C  C   . ARG B 1 143 ? 49.069 59.017 5.982   1.00 14.24 ? 143 ARG B C   1 
ATOM   2162 O  O   . ARG B 1 143 ? 48.995 58.581 7.125   1.00 18.16 ? 143 ARG B O   1 
ATOM   2163 C  CB  . ARG B 1 143 ? 51.539 58.690 5.679   1.00 14.09 ? 143 ARG B CB  1 
ATOM   2164 C  CG  . ARG B 1 143 ? 52.856 59.428 5.449   1.00 13.93 ? 143 ARG B CG  1 
ATOM   2165 C  CD  . ARG B 1 143 ? 54.102 58.597 5.713   1.00 17.71 ? 143 ARG B CD  1 
ATOM   2166 N  NE  . ARG B 1 143 ? 55.283 59.423 5.494   1.00 15.58 ? 143 ARG B NE  1 
ATOM   2167 C  CZ  . ARG B 1 143 ? 56.528 58.974 5.371   1.00 16.65 ? 143 ARG B CZ  1 
ATOM   2168 N  NH1 . ARG B 1 143 ? 56.801 57.671 5.444   1.00 17.08 ? 143 ARG B NH1 1 
ATOM   2169 N  NH2 . ARG B 1 143 ? 57.507 59.843 5.148   1.00 14.25 ? 143 ARG B NH2 1 
ATOM   2170 N  N   . LEU B 1 144 ? 48.036 59.042 5.149   1.00 15.28 ? 144 LEU B N   1 
ATOM   2171 C  CA  . LEU B 1 144 ? 46.734 58.504 5.535   1.00 13.19 ? 144 LEU B CA  1 
ATOM   2172 C  C   . LEU B 1 144 ? 46.609 56.993 5.440   1.00 14.71 ? 144 LEU B C   1 
ATOM   2173 O  O   . LEU B 1 144 ? 45.967 56.371 6.284   1.00 15.56 ? 144 LEU B O   1 
ATOM   2174 C  CB  . LEU B 1 144 ? 45.634 59.128 4.697   1.00 12.81 ? 144 LEU B CB  1 
ATOM   2175 C  CG  . LEU B 1 144 ? 45.505 60.640 4.679   1.00 13.21 ? 144 LEU B CG  1 
ATOM   2176 C  CD1 . LEU B 1 144 ? 44.352 60.989 3.740   1.00 13.94 ? 144 LEU B CD1 1 
ATOM   2177 C  CD2 . LEU B 1 144 ? 45.251 61.158 6.082   1.00 14.77 ? 144 LEU B CD2 1 
ATOM   2178 N  N   . ALA B 1 145 ? 47.183 56.414 4.388   1.00 15.11 ? 145 ALA B N   1 
ATOM   2179 C  CA  . ALA B 1 145 ? 47.136 54.975 4.150   1.00 12.36 ? 145 ALA B CA  1 
ATOM   2180 C  C   . ALA B 1 145 ? 48.354 54.613 3.316   1.00 12.96 ? 145 ALA B C   1 
ATOM   2181 O  O   . ALA B 1 145 ? 48.916 55.466 2.622   1.00 14.83 ? 145 ALA B O   1 
ATOM   2182 C  CB  . ALA B 1 145 ? 45.860 54.609 3.417   1.00 11.95 ? 145 ALA B CB  1 
ATOM   2183 N  N   . CYS B 1 146 ? 48.785 53.366 3.408   1.00 12.23 ? 146 CYS B N   1 
ATOM   2184 C  CA  . CYS B 1 146 ? 49.943 52.903 2.671   1.00 13.33 ? 146 CYS B CA  1 
ATOM   2185 C  C   . CYS B 1 146 ? 49.911 51.392 2.567   1.00 12.36 ? 146 CYS B C   1 
ATOM   2186 O  O   . CYS B 1 146 ? 49.128 50.740 3.255   1.00 13.36 ? 146 CYS B O   1 
ATOM   2187 C  CB  . CYS B 1 146 ? 51.222 53.325 3.391   1.00 11.34 ? 146 CYS B CB  1 
ATOM   2188 S  SG  . CYS B 1 146 ? 51.368 52.695 5.090   1.00 16.30 ? 146 CYS B SG  1 
ATOM   2189 N  N   . GLY B 1 147 ? 50.763 50.846 1.705   1.00 11.91 ? 147 GLY B N   1 
ATOM   2190 C  CA  . GLY B 1 147 ? 50.859 49.410 1.555   1.00 12.43 ? 147 GLY B CA  1 
ATOM   2191 C  C   . GLY B 1 147 ? 52.159 49.042 0.869   1.00 13.34 ? 147 GLY B C   1 
ATOM   2192 O  O   . GLY B 1 147 ? 52.738 49.876 0.190   1.00 13.92 ? 147 GLY B O   1 
ATOM   2193 N  N   . VAL B 1 148 ? 52.650 47.820 1.076   1.00 14.72 ? 148 VAL B N   1 
ATOM   2194 C  CA  . VAL B 1 148 ? 53.873 47.354 0.422   1.00 14.35 ? 148 VAL B CA  1 
ATOM   2195 C  C   . VAL B 1 148 ? 53.495 46.836 -0.973  1.00 14.85 ? 148 VAL B C   1 
ATOM   2196 O  O   . VAL B 1 148 ? 52.537 46.075 -1.112  1.00 15.73 ? 148 VAL B O   1 
ATOM   2197 C  CB  . VAL B 1 148 ? 54.546 46.213 1.211   1.00 13.58 ? 148 VAL B CB  1 
ATOM   2198 C  CG1 . VAL B 1 148 ? 55.785 45.744 0.491   1.00 10.80 ? 148 VAL B CG1 1 
ATOM   2199 C  CG2 . VAL B 1 148 ? 54.888 46.683 2.606   1.00 13.93 ? 148 VAL B CG2 1 
ATOM   2200 N  N   . ILE B 1 149 ? 54.216 47.281 -2.000  1.00 14.73 ? 149 ILE B N   1 
ATOM   2201 C  CA  . ILE B 1 149 ? 53.959 46.866 -3.382  1.00 16.11 ? 149 ILE B CA  1 
ATOM   2202 C  C   . ILE B 1 149 ? 54.452 45.423 -3.598  1.00 15.52 ? 149 ILE B C   1 
ATOM   2203 O  O   . ILE B 1 149 ? 55.645 45.143 -3.484  1.00 15.17 ? 149 ILE B O   1 
ATOM   2204 C  CB  . ILE B 1 149 ? 54.634 47.851 -4.387  1.00 14.30 ? 149 ILE B CB  1 
ATOM   2205 C  CG1 . ILE B 1 149 ? 54.101 49.267 -4.147  1.00 16.37 ? 149 ILE B CG1 1 
ATOM   2206 C  CG2 . ILE B 1 149 ? 54.357 47.448 -5.847  1.00 15.28 ? 149 ILE B CG2 1 
ATOM   2207 C  CD1 . ILE B 1 149 ? 54.926 50.369 -4.827  1.00 16.92 ? 149 ILE B CD1 1 
ATOM   2208 N  N   . GLY B 1 150 ? 53.522 44.516 -3.889  1.00 16.79 ? 150 GLY B N   1 
ATOM   2209 C  CA  . GLY B 1 150 ? 53.876 43.125 -4.092  1.00 17.08 ? 150 GLY B CA  1 
ATOM   2210 C  C   . GLY B 1 150 ? 53.679 42.635 -5.515  1.00 19.05 ? 150 GLY B C   1 
ATOM   2211 O  O   . GLY B 1 150 ? 52.983 43.274 -6.297  1.00 20.07 ? 150 GLY B O   1 
ATOM   2212 N  N   . ILE B 1 151 ? 54.300 41.502 -5.848  1.00 21.49 ? 151 ILE B N   1 
ATOM   2213 C  CA  . ILE B 1 151 ? 54.197 40.870 -7.170  1.00 21.79 ? 151 ILE B CA  1 
ATOM   2214 C  C   . ILE B 1 151 ? 52.821 40.238 -7.285  1.00 22.68 ? 151 ILE B C   1 
ATOM   2215 O  O   . ILE B 1 151 ? 52.336 39.613 -6.345  1.00 23.08 ? 151 ILE B O   1 
ATOM   2216 C  CB  . ILE B 1 151 ? 55.235 39.711 -7.362  1.00 23.27 ? 151 ILE B CB  1 
ATOM   2217 C  CG1 . ILE B 1 151 ? 56.657 40.254 -7.379  1.00 23.62 ? 151 ILE B CG1 1 
ATOM   2218 C  CG2 . ILE B 1 151 ? 54.962 38.929 -8.664  1.00 19.77 ? 151 ILE B CG2 1 
ATOM   2219 C  CD1 . ILE B 1 151 ? 56.948 41.120 -8.578  1.00 32.72 ? 151 ILE B CD1 1 
ATOM   2220 N  N   . ALA B 1 152 ? 52.194 40.394 -8.441  1.00 24.24 ? 152 ALA B N   1 
ATOM   2221 C  CA  . ALA B 1 152 ? 50.889 39.807 -8.666  1.00 27.98 ? 152 ALA B CA  1 
ATOM   2222 C  C   . ALA B 1 152 ? 50.957 39.003 -9.970  1.00 30.36 ? 152 ALA B C   1 
ATOM   2223 O  O   . ALA B 1 152 ? 51.964 39.058 -10.694 1.00 28.63 ? 152 ALA B O   1 
ATOM   2224 C  CB  . ALA B 1 152 ? 49.829 40.896 -8.737  1.00 27.35 ? 152 ALA B CB  1 
ATOM   2225 N  N   . GLN B 1 153 ? 49.942 38.176 -10.209 1.00 36.62 ? 153 GLN B N   1 
ATOM   2226 C  CA  . GLN B 1 153 ? 49.901 37.386 -11.433 1.00 43.19 ? 153 GLN B CA  1 
ATOM   2227 C  C   . GLN B 1 153 ? 48.891 37.968 -12.422 1.00 44.70 ? 153 GLN B C   1 
ATOM   2228 O  O   . GLN B 1 153 ? 49.128 37.784 -13.631 1.00 50.58 ? 153 GLN B O   1 
ATOM   2229 C  CB  . GLN B 1 153 ? 49.611 35.901 -11.154 1.00 45.33 ? 153 GLN B CB  1 
ATOM   2230 C  CG  . GLN B 1 153 ? 48.139 35.494 -11.009 1.00 49.40 ? 153 GLN B CG  1 
ATOM   2231 C  CD  . GLN B 1 153 ? 47.944 33.973 -10.886 1.00 51.86 ? 153 GLN B CD  1 
ATOM   2232 O  OE1 . GLN B 1 153 ? 47.132 33.510 -10.077 1.00 54.41 ? 153 GLN B OE1 1 
ATOM   2233 N  NE2 . GLN B 1 153 ? 48.691 33.196 -11.684 1.00 51.99 ? 153 GLN B NE2 1 
ATOM   2234 O  OXT . GLN B 1 153 ? 47.909 38.625 -11.994 1.00 44.70 ? 153 GLN B OXT 1 
HETATM 2235 CU CU  . CU  C 2 .   ? 52.705 27.705 2.949   1.00 40.14 ? 154 CU  A CU  1 
HETATM 2236 ZN ZN  . ZN  D 3 .   ? 56.469 24.093 -0.472  1.00 26.93 ? 155 ZN  A ZN  1 
HETATM 2237 CU CU  . CU  E 2 .   ? 54.668 60.724 -0.015  1.00 28.39 ? 154 CU  B CU  1 
HETATM 2238 ZN ZN  . ZN  F 3 .   ? 58.961 63.484 -3.943  1.00 20.97 ? 155 ZN  B ZN  1 
HETATM 2239 O  O   . HOH G 4 .   ? 46.659 39.404 12.966  1.00 27.28 ? 365 HOH A O   1 
HETATM 2240 O  O   . HOH G 4 .   ? 55.031 43.559 5.471   1.00 19.17 ? 366 HOH A O   1 
HETATM 2241 O  O   . HOH G 4 .   ? 52.161 43.523 4.250   1.00 26.54 ? 367 HOH A O   1 
HETATM 2242 O  O   . HOH G 4 .   ? 55.944 35.375 -10.044 1.00 35.09 ? 372 HOH A O   1 
HETATM 2243 O  O   . HOH G 4 .   ? 56.413 29.690 -8.465  1.00 32.35 ? 373 HOH A O   1 
HETATM 2244 O  O   . HOH G 4 .   ? 70.867 32.838 -1.287  1.00 31.95 ? 374 HOH A O   1 
HETATM 2245 O  O   . HOH G 4 .   ? 43.569 29.833 4.250   1.00 40.89 ? 382 HOH A O   1 
HETATM 2246 O  O   . HOH G 4 .   ? 63.826 25.079 -5.626  1.00 28.87 ? 388 HOH A O   1 
HETATM 2247 O  O   . HOH G 4 .   ? 61.245 28.414 15.798  1.00 48.34 ? 389 HOH A O   1 
HETATM 2248 O  O   . HOH G 4 .   ? 61.491 26.042 -6.788  1.00 21.63 ? 390 HOH A O   1 
HETATM 2249 O  O   . HOH G 4 .   ? 58.922 23.521 4.385   1.00 22.55 ? 391 HOH A O   1 
HETATM 2250 O  O   . HOH G 4 .   ? 52.668 20.162 16.909  1.00 59.96 ? 392 HOH A O   1 
HETATM 2251 O  O   . HOH G 4 .   ? 59.973 15.041 -3.470  1.00 57.88 ? 393 HOH A O   1 
HETATM 2252 O  O   . HOH G 4 .   ? 57.741 15.974 -1.733  1.00 53.69 ? 394 HOH A O   1 
HETATM 2253 O  O   . HOH G 4 .   ? 68.313 47.142 2.392   1.00 27.10 ? 395 HOH A O   1 
HETATM 2254 O  O   . HOH G 4 .   ? 65.482 44.176 8.615   1.00 41.75 ? 399 HOH A O   1 
HETATM 2255 O  O   . HOH G 4 .   ? 61.403 41.916 14.699  1.00 46.04 ? 400 HOH A O   1 
HETATM 2256 O  O   . HOH G 4 .   ? 74.569 49.155 5.069   1.00 34.87 ? 401 HOH A O   1 
HETATM 2257 O  O   . HOH G 4 .   ? 72.437 49.111 9.550   1.00 29.80 ? 403 HOH A O   1 
HETATM 2258 O  O   . HOH G 4 .   ? 66.930 47.958 11.443  1.00 28.94 ? 404 HOH A O   1 
HETATM 2259 O  O   . HOH G 4 .   ? 69.320 49.407 10.541  1.00 29.68 ? 406 HOH A O   1 
HETATM 2260 O  O   . HOH G 4 .   ? 68.661 47.566 -0.351  1.00 42.16 ? 407 HOH A O   1 
HETATM 2261 O  O   . HOH G 4 .   ? 70.545 49.815 6.019   1.00 27.61 ? 409 HOH A O   1 
HETATM 2262 O  O   . HOH G 4 .   ? 73.140 50.687 7.259   1.00 28.14 ? 410 HOH A O   1 
HETATM 2263 O  O   . HOH G 4 .   ? 52.299 25.122 -2.645  1.00 32.76 ? 418 HOH A O   1 
HETATM 2264 O  O   . HOH G 4 .   ? 42.391 32.010 12.093  1.00 63.72 ? 419 HOH A O   1 
HETATM 2265 O  O   . HOH G 4 .   ? 46.564 30.898 16.446  1.00 47.33 ? 420 HOH A O   1 
HETATM 2266 O  O   . HOH G 4 .   ? 50.854 18.055 9.019   1.00 47.68 ? 421 HOH A O   1 
HETATM 2267 O  O   . HOH G 4 .   ? 56.988 18.223 10.822  1.00 54.28 ? 422 HOH A O   1 
HETATM 2268 O  O   . HOH G 4 .   ? 60.120 20.532 12.011  1.00 42.58 ? 423 HOH A O   1 
HETATM 2269 O  O   . HOH G 4 .   ? 63.309 25.890 9.733   1.00 40.91 ? 424 HOH A O   1 
HETATM 2270 O  O   . HOH G 4 .   ? 62.282 22.876 9.775   1.00 44.18 ? 425 HOH A O   1 
HETATM 2271 O  O   . HOH G 4 .   ? 54.279 25.392 -5.253  1.00 46.78 ? 427 HOH A O   1 
HETATM 2272 O  O   . HOH G 4 .   ? 48.973 26.343 1.560   1.00 40.50 ? 428 HOH A O   1 
HETATM 2273 O  O   . HOH G 4 .   ? 45.223 34.837 12.742  1.00 41.61 ? 429 HOH A O   1 
HETATM 2274 O  O   . HOH G 4 .   ? 41.675 28.355 10.270  1.00 62.46 ? 430 HOH A O   1 
HETATM 2275 O  O   . HOH G 4 .   ? 49.250 43.189 -1.801  1.00 22.82 ? 431 HOH A O   1 
HETATM 2276 O  O   . HOH G 4 .   ? 64.469 47.184 9.654   1.00 41.91 ? 434 HOH A O   1 
HETATM 2277 O  O   . HOH G 4 .   ? 54.933 20.845 -5.493  1.00 29.30 ? 437 HOH A O   1 
HETATM 2278 O  O   . HOH G 4 .   ? 47.443 21.358 3.331   1.00 47.47 ? 438 HOH A O   1 
HETATM 2279 O  O   . HOH G 4 .   ? 62.720 33.148 -11.259 1.00 45.30 ? 439 HOH A O   1 
HETATM 2280 O  O   . HOH G 4 .   ? 68.860 34.767 -6.501  1.00 44.92 ? 440 HOH A O   1 
HETATM 2281 O  O   . HOH G 4 .   ? 50.724 42.734 6.820   1.00 36.28 ? 443 HOH A O   1 
HETATM 2282 O  O   . HOH G 4 .   ? 49.340 26.030 -2.292  1.00 53.57 ? 453 HOH A O   1 
HETATM 2283 O  O   . HOH G 4 .   ? 59.904 17.809 -10.058 1.00 54.53 ? 454 HOH A O   1 
HETATM 2284 O  O   . HOH G 4 .   ? 60.958 22.438 13.882  1.00 59.26 ? 455 HOH A O   1 
HETATM 2285 O  O   . HOH G 4 .   ? 63.100 25.600 15.635  1.00 59.27 ? 456 HOH A O   1 
HETATM 2286 O  O   . HOH G 4 .   ? 63.285 29.145 14.204  1.00 37.69 ? 457 HOH A O   1 
HETATM 2287 O  O   . HOH G 4 .   ? 72.327 27.854 4.813   1.00 37.01 ? 458 HOH A O   1 
HETATM 2288 O  O   . HOH G 4 .   ? 77.448 29.405 3.829   1.00 70.08 ? 459 HOH A O   1 
HETATM 2289 O  O   . HOH G 4 .   ? 78.259 30.219 6.748   1.00 63.39 ? 460 HOH A O   1 
HETATM 2290 O  O   . HOH G 4 .   ? 76.648 30.063 0.101   1.00 57.54 ? 461 HOH A O   1 
HETATM 2291 O  O   . HOH G 4 .   ? 73.593 42.515 11.702  1.00 27.72 ? 464 HOH A O   1 
HETATM 2292 O  O   . HOH G 4 .   ? 43.457 30.608 1.838   1.00 58.23 ? 473 HOH A O   1 
HETATM 2293 O  O   . HOH G 4 .   ? 68.416 27.182 10.133  1.00 49.60 ? 474 HOH A O   1 
HETATM 2294 O  O   . HOH G 4 .   ? 76.069 32.100 14.777  1.00 57.51 ? 475 HOH A O   1 
HETATM 2295 O  O   . HOH G 4 .   ? 68.796 34.645 12.923  1.00 66.38 ? 476 HOH A O   1 
HETATM 2296 O  O   . HOH G 4 .   ? 64.402 19.985 6.292   1.00 36.62 ? 477 HOH A O   1 
HETATM 2297 O  O   . HOH G 4 .   ? 66.739 26.153 7.126   1.00 56.70 ? 478 HOH A O   1 
HETATM 2298 O  O   . HOH G 4 .   ? 67.318 23.129 -3.040  1.00 37.38 ? 479 HOH A O   1 
HETATM 2299 O  O   . HOH G 4 .   ? 69.229 26.271 3.901   1.00 48.94 ? 480 HOH A O   1 
HETATM 2300 O  O   . HOH G 4 .   ? 64.027 17.258 5.854   1.00 49.83 ? 481 HOH A O   1 
HETATM 2301 O  O   . HOH G 4 .   ? 74.297 38.738 8.095   1.00 58.68 ? 482 HOH A O   1 
HETATM 2302 O  O   . HOH G 4 .   ? 74.894 36.687 2.789   1.00 34.40 ? 483 HOH A O   1 
HETATM 2303 O  O   . HOH G 4 .   ? 83.767 40.038 9.885   1.00 51.26 ? 484 HOH A O   1 
HETATM 2304 O  O   . HOH G 4 .   ? 73.813 38.311 12.390  1.00 43.61 ? 485 HOH A O   1 
HETATM 2305 O  O   . HOH G 4 .   ? 46.953 5.648  2.338   1.00 66.39 ? 491 HOH A O   1 
HETATM 2306 O  O   . HOH G 4 .   ? 43.351 5.217  -3.508  1.00 56.23 ? 492 HOH A O   1 
HETATM 2307 O  O   . HOH G 4 .   ? 45.725 14.587 -0.200  1.00 45.49 ? 493 HOH A O   1 
HETATM 2308 O  O   . HOH G 4 .   ? 49.617 6.354  -2.363  1.00 56.29 ? 494 HOH A O   1 
HETATM 2309 O  O   . HOH G 4 .   ? 50.095 4.305  0.365   1.00 39.98 ? 495 HOH A O   1 
HETATM 2310 O  O   . HOH G 4 .   ? 44.491 20.462 14.551  1.00 48.82 ? 496 HOH A O   1 
HETATM 2311 O  O   . HOH G 4 .   ? 50.635 19.717 13.925  1.00 50.78 ? 497 HOH A O   1 
HETATM 2312 O  O   . HOH G 4 .   ? 70.592 35.522 -10.260 1.00 44.65 ? 498 HOH A O   1 
HETATM 2313 O  O   . HOH G 4 .   ? 71.267 39.963 -9.559  1.00 58.39 ? 499 HOH A O   1 
HETATM 2314 O  O   . HOH G 4 .   ? 67.751 42.382 -7.808  1.00 53.40 ? 500 HOH A O   1 
HETATM 2315 O  O   . HOH G 4 .   ? 71.199 33.157 -9.539  1.00 79.48 ? 501 HOH A O   1 
HETATM 2316 O  O   . HOH G 4 .   ? 70.902 37.910 -11.232 1.00 52.22 ? 502 HOH A O   1 
HETATM 2317 O  O   . HOH G 4 .   ? 72.423 29.971 14.073  1.00 52.05 ? 504 HOH A O   1 
HETATM 2318 O  O   . HOH G 4 .   ? 46.544 40.156 20.333  1.00 71.05 ? 508 HOH A O   1 
HETATM 2319 O  O   . HOH G 4 .   ? 68.044 49.392 -2.452  1.00 61.87 ? 512 HOH A O   1 
HETATM 2320 O  O   . HOH G 4 .   ? 49.299 45.344 7.706   1.00 63.74 ? 523 HOH A O   1 
HETATM 2321 O  O   . HOH G 4 .   ? 60.897 39.964 -8.390  1.00 62.44 ? 525 HOH A O   1 
HETATM 2322 O  O   . HOH G 4 .   ? 54.061 26.828 -7.892  1.00 49.48 ? 527 HOH A O   1 
HETATM 2323 O  O   . HOH G 4 .   ? 58.487 35.303 -10.957 1.00 64.06 ? 528 HOH A O   1 
HETATM 2324 O  O   . HOH G 4 .   ? 52.738 30.489 -12.071 1.00 62.25 ? 529 HOH A O   1 
HETATM 2325 O  O   . HOH H 4 .   ? 55.640 62.473 5.597   1.00 48.38 ? 356 HOH B O   1 
HETATM 2326 O  O   . HOH H 4 .   ? 52.699 59.911 9.491   1.00 27.27 ? 357 HOH B O   1 
HETATM 2327 O  O   . HOH H 4 .   ? 55.270 67.420 4.639   1.00 34.75 ? 358 HOH B O   1 
HETATM 2328 O  O   . HOH H 4 .   ? 54.549 64.728 3.263   1.00 25.24 ? 359 HOH B O   1 
HETATM 2329 O  O   . HOH H 4 .   ? 61.196 69.988 -9.561  1.00 39.42 ? 360 HOH B O   1 
HETATM 2330 O  O   . HOH H 4 .   ? 57.846 62.501 -16.848 1.00 48.59 ? 361 HOH B O   1 
HETATM 2331 O  O   . HOH H 4 .   ? 52.845 60.083 -14.561 1.00 27.50 ? 362 HOH B O   1 
HETATM 2332 O  O   . HOH H 4 .   ? 65.178 59.801 -7.961  1.00 21.41 ? 363 HOH B O   1 
HETATM 2333 O  O   . HOH H 4 .   ? 64.432 60.693 -10.594 1.00 27.47 ? 364 HOH B O   1 
HETATM 2334 O  O   . HOH H 4 .   ? 62.361 52.812 8.356   1.00 19.70 ? 368 HOH B O   1 
HETATM 2335 O  O   . HOH H 4 .   ? 59.082 50.429 15.647  1.00 56.91 ? 369 HOH B O   1 
HETATM 2336 O  O   . HOH H 4 .   ? 56.769 45.618 6.098   1.00 21.41 ? 370 HOH B O   1 
HETATM 2337 O  O   . HOH H 4 .   ? 59.808 52.311 -16.744 1.00 40.35 ? 371 HOH B O   1 
HETATM 2338 O  O   . HOH H 4 .   ? 53.983 39.617 -12.378 1.00 28.79 ? 375 HOH B O   1 
HETATM 2339 O  O   . HOH H 4 .   ? 54.552 64.301 -6.924  1.00 18.23 ? 376 HOH B O   1 
HETATM 2340 O  O   . HOH H 4 .   ? 49.013 71.406 -5.697  1.00 38.28 ? 377 HOH B O   1 
HETATM 2341 O  O   . HOH H 4 .   ? 52.089 73.886 -0.360  1.00 41.65 ? 378 HOH B O   1 
HETATM 2342 O  O   . HOH H 4 .   ? 45.298 72.626 -8.727  1.00 32.05 ? 379 HOH B O   1 
HETATM 2343 O  O   . HOH H 4 .   ? 42.386 69.706 -1.842  1.00 33.16 ? 380 HOH B O   1 
HETATM 2344 O  O   . HOH H 4 .   ? 56.159 47.501 16.422  1.00 63.65 ? 381 HOH B O   1 
HETATM 2345 O  O   . HOH H 4 .   ? 41.566 60.708 7.477   1.00 20.92 ? 383 HOH B O   1 
HETATM 2346 O  O   . HOH H 4 .   ? 34.392 56.785 0.241   1.00 33.08 ? 384 HOH B O   1 
HETATM 2347 O  O   . HOH H 4 .   ? 42.660 52.117 7.017   1.00 19.55 ? 385 HOH B O   1 
HETATM 2348 O  O   . HOH H 4 .   ? 43.452 56.231 7.328   1.00 19.75 ? 386 HOH B O   1 
HETATM 2349 O  O   . HOH H 4 .   ? 48.488 47.237 3.574   1.00 31.88 ? 387 HOH B O   1 
HETATM 2350 O  O   . HOH H 4 .   ? 64.464 65.864 -2.001  1.00 38.85 ? 396 HOH B O   1 
HETATM 2351 O  O   . HOH H 4 .   ? 60.487 60.695 5.714   1.00 44.58 ? 397 HOH B O   1 
HETATM 2352 O  O   . HOH H 4 .   ? 63.115 64.343 0.443   1.00 45.54 ? 398 HOH B O   1 
HETATM 2353 O  O   . HOH H 4 .   ? 61.178 51.521 10.686  1.00 31.99 ? 402 HOH B O   1 
HETATM 2354 O  O   . HOH H 4 .   ? 63.004 50.245 7.175   1.00 35.21 ? 405 HOH B O   1 
HETATM 2355 O  O   . HOH H 4 .   ? 66.593 51.484 -1.045  1.00 33.06 ? 408 HOH B O   1 
HETATM 2356 O  O   . HOH H 4 .   ? 61.934 63.970 3.856   1.00 57.23 ? 411 HOH B O   1 
HETATM 2357 O  O   . HOH H 4 .   ? 64.022 61.930 -0.976  1.00 51.82 ? 412 HOH B O   1 
HETATM 2358 O  O   . HOH H 4 .   ? 60.859 62.850 0.499   1.00 26.97 ? 413 HOH B O   1 
HETATM 2359 O  O   . HOH H 4 .   ? 64.605 49.326 -6.875  1.00 36.13 ? 414 HOH B O   1 
HETATM 2360 O  O   . HOH H 4 .   ? 60.802 51.306 13.580  1.00 39.99 ? 415 HOH B O   1 
HETATM 2361 O  O   . HOH H 4 .   ? 54.840 55.755 15.281  1.00 42.29 ? 417 HOH B O   1 
HETATM 2362 O  O   . HOH H 4 .   ? 58.730 46.878 15.472  1.00 44.65 ? 426 HOH B O   1 
HETATM 2363 O  O   . HOH H 4 .   ? 49.977 45.415 -0.183  1.00 17.09 ? 432 HOH B O   1 
HETATM 2364 O  O   . HOH H 4 .   ? 59.772 58.459 7.876   1.00 33.91 ? 433 HOH B O   1 
HETATM 2365 O  O   . HOH H 4 .   ? 62.209 47.648 11.068  1.00 39.97 ? 435 HOH B O   1 
HETATM 2366 O  O   . HOH H 4 .   ? 62.197 71.522 -7.244  1.00 52.06 ? 436 HOH B O   1 
HETATM 2367 O  O   . HOH H 4 .   ? 40.196 48.793 -7.162  1.00 55.86 ? 441 HOH B O   1 
HETATM 2368 O  O   . HOH H 4 .   ? 51.243 45.942 3.001   1.00 27.81 ? 442 HOH B O   1 
HETATM 2369 O  O   . HOH H 4 .   ? 49.725 49.245 5.518   1.00 33.63 ? 444 HOH B O   1 
HETATM 2370 O  O   . HOH H 4 .   ? 49.500 51.059 8.171   1.00 40.22 ? 445 HOH B O   1 
HETATM 2371 O  O   . HOH H 4 .   ? 41.249 62.166 4.156   1.00 43.87 ? 446 HOH B O   1 
HETATM 2372 O  O   . HOH H 4 .   ? 42.432 65.009 4.836   1.00 48.55 ? 447 HOH B O   1 
HETATM 2373 O  O   . HOH H 4 .   ? 31.500 56.418 -0.585  1.00 59.30 ? 448 HOH B O   1 
HETATM 2374 O  O   . HOH H 4 .   ? 42.801 71.774 2.696   1.00 65.25 ? 449 HOH B O   1 
HETATM 2375 O  O   . HOH H 4 .   ? 43.315 67.689 0.721   1.00 38.77 ? 450 HOH B O   1 
HETATM 2376 O  O   . HOH H 4 .   ? 45.296 70.333 0.235   1.00 39.63 ? 451 HOH B O   1 
HETATM 2377 O  O   . HOH H 4 .   ? 42.772 63.997 7.473   1.00 47.00 ? 452 HOH B O   1 
HETATM 2378 O  O   . HOH H 4 .   ? 35.385 59.272 5.761   1.00 59.72 ? 462 HOH B O   1 
HETATM 2379 O  O   . HOH H 4 .   ? 37.364 61.262 7.093   1.00 62.87 ? 463 HOH B O   1 
HETATM 2380 O  O   . HOH H 4 .   ? 40.965 71.075 0.448   1.00 64.67 ? 465 HOH B O   1 
HETATM 2381 O  O   . HOH H 4 .   ? 30.996 68.691 -1.782  1.00 50.20 ? 466 HOH B O   1 
HETATM 2382 O  O   . HOH H 4 .   ? 32.513 65.956 1.286   1.00 66.27 ? 467 HOH B O   1 
HETATM 2383 O  O   . HOH H 4 .   ? 35.142 65.545 2.163   1.00 45.97 ? 468 HOH B O   1 
HETATM 2384 O  O   . HOH H 4 .   ? 39.998 60.307 5.501   1.00 44.39 ? 469 HOH B O   1 
HETATM 2385 O  O   . HOH H 4 .   ? 47.020 61.238 -14.874 1.00 47.22 ? 470 HOH B O   1 
HETATM 2386 O  O   . HOH H 4 .   ? 46.177 61.374 -11.749 1.00 53.31 ? 471 HOH B O   1 
HETATM 2387 O  O   . HOH H 4 .   ? 36.893 60.869 -15.171 1.00 33.53 ? 472 HOH B O   1 
HETATM 2388 O  O   . HOH H 4 .   ? 37.133 64.642 -8.506  1.00 57.14 ? 486 HOH B O   1 
HETATM 2389 O  O   . HOH H 4 .   ? 44.301 59.526 -11.011 1.00 29.32 ? 487 HOH B O   1 
HETATM 2390 O  O   . HOH H 4 .   ? 39.572 61.751 -10.458 1.00 65.47 ? 488 HOH B O   1 
HETATM 2391 O  O   . HOH H 4 .   ? 40.372 53.583 -11.941 1.00 35.33 ? 489 HOH B O   1 
HETATM 2392 O  O   . HOH H 4 .   ? 35.123 58.386 -15.574 1.00 73.66 ? 490 HOH B O   1 
HETATM 2393 O  O   . HOH H 4 .   ? 62.706 43.962 -6.269  1.00 58.67 ? 503 HOH B O   1 
HETATM 2394 O  O   . HOH H 4 .   ? 61.865 70.365 -12.907 1.00 44.68 ? 505 HOH B O   1 
HETATM 2395 O  O   . HOH H 4 .   ? 48.007 56.260 8.806   1.00 29.18 ? 506 HOH B O   1 
HETATM 2396 O  O   . HOH H 4 .   ? 51.471 51.227 14.437  1.00 61.31 ? 507 HOH B O   1 
HETATM 2397 O  O   . HOH H 4 .   ? 58.488 62.150 2.240   1.00 40.67 ? 509 HOH B O   1 
HETATM 2398 O  O   . HOH H 4 .   ? 60.010 60.122 12.441  1.00 60.68 ? 510 HOH B O   1 
HETATM 2399 O  O   . HOH H 4 .   ? 54.927 59.228 14.563  1.00 53.82 ? 511 HOH B O   1 
HETATM 2400 O  O   . HOH H 4 .   ? 57.543 66.575 -19.324 1.00 58.41 ? 513 HOH B O   1 
HETATM 2401 O  O   . HOH H 4 .   ? 56.898 69.104 -22.845 1.00 41.38 ? 514 HOH B O   1 
HETATM 2402 O  O   . HOH H 4 .   ? 48.558 55.634 -24.098 1.00 69.09 ? 515 HOH B O   1 
HETATM 2403 O  O   . HOH H 4 .   ? 55.791 61.331 -20.572 1.00 63.52 ? 516 HOH B O   1 
HETATM 2404 O  O   . HOH H 4 .   ? 58.759 71.100 -9.909  1.00 44.44 ? 517 HOH B O   1 
HETATM 2405 O  O   . HOH H 4 .   ? 63.833 59.903 6.079   1.00 48.98 ? 518 HOH B O   1 
HETATM 2406 O  O   . HOH H 4 .   ? 69.427 55.179 0.599   1.00 69.20 ? 519 HOH B O   1 
HETATM 2407 O  O   . HOH H 4 .   ? 67.286 55.084 -2.574  1.00 44.90 ? 520 HOH B O   1 
HETATM 2408 O  O   . HOH H 4 .   ? 67.476 51.984 -4.171  1.00 58.17 ? 521 HOH B O   1 
HETATM 2409 O  O   . HOH H 4 .   ? 51.375 47.688 8.119   1.00 60.44 ? 522 HOH B O   1 
HETATM 2410 O  O   . HOH H 4 .   ? 59.168 41.852 -11.953 1.00 59.45 ? 524 HOH B O   1 
HETATM 2411 O  O   . HOH H 4 .   ? 65.337 43.012 -12.900 1.00 61.13 ? 526 HOH B O   1 
HETATM 2412 O  O   . HOH H 4 .   ? 50.564 30.127 -10.480 1.00 64.66 ? 530 HOH B O   1 
HETATM 2413 O  O   . HOH H 4 .   ? 48.131 37.554 -7.969  1.00 53.45 ? 531 HOH B O   1 
HETATM 2414 O  O   . HOH H 4 .   ? 43.136 43.688 -7.514  1.00 59.70 ? 532 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU  1  154 154 CU  CU  A . 
D 3 ZN  1  155 155 ZN  ZN  A . 
E 2 CU  1  154 154 CU  CU  B . 
F 3 ZN  1  155 155 ZN  ZN  B . 
G 4 HOH 1  365 365 HOH HOH A . 
G 4 HOH 2  366 366 HOH HOH A . 
G 4 HOH 3  367 367 HOH HOH A . 
G 4 HOH 4  372 372 HOH HOH A . 
G 4 HOH 5  373 373 HOH HOH A . 
G 4 HOH 6  374 374 HOH HOH A . 
G 4 HOH 7  382 382 HOH HOH A . 
G 4 HOH 8  388 388 HOH HOH A . 
G 4 HOH 9  389 389 HOH HOH A . 
G 4 HOH 10 390 390 HOH HOH A . 
G 4 HOH 11 391 391 HOH HOH A . 
G 4 HOH 12 392 392 HOH HOH A . 
G 4 HOH 13 393 393 HOH HOH A . 
G 4 HOH 14 394 394 HOH HOH A . 
G 4 HOH 15 395 395 HOH HOH A . 
G 4 HOH 16 399 399 HOH HOH A . 
G 4 HOH 17 400 400 HOH HOH A . 
G 4 HOH 18 401 401 HOH HOH A . 
G 4 HOH 19 403 403 HOH HOH A . 
G 4 HOH 20 404 404 HOH HOH A . 
G 4 HOH 21 406 406 HOH HOH A . 
G 4 HOH 22 407 407 HOH HOH A . 
G 4 HOH 23 409 409 HOH HOH A . 
G 4 HOH 24 410 410 HOH HOH A . 
G 4 HOH 25 418 418 HOH HOH A . 
G 4 HOH 26 419 419 HOH HOH A . 
G 4 HOH 27 420 420 HOH HOH A . 
G 4 HOH 28 421 421 HOH HOH A . 
G 4 HOH 29 422 422 HOH HOH A . 
G 4 HOH 30 423 423 HOH HOH A . 
G 4 HOH 31 424 424 HOH HOH A . 
G 4 HOH 32 425 425 HOH HOH A . 
G 4 HOH 33 427 427 HOH HOH A . 
G 4 HOH 34 428 428 HOH HOH A . 
G 4 HOH 35 429 429 HOH HOH A . 
G 4 HOH 36 430 430 HOH HOH A . 
G 4 HOH 37 431 431 HOH HOH A . 
G 4 HOH 38 434 434 HOH HOH A . 
G 4 HOH 39 437 437 HOH HOH A . 
G 4 HOH 40 438 438 HOH HOH A . 
G 4 HOH 41 439 439 HOH HOH A . 
G 4 HOH 42 440 440 HOH HOH A . 
G 4 HOH 43 443 443 HOH HOH A . 
G 4 HOH 44 453 453 HOH HOH A . 
G 4 HOH 45 454 454 HOH HOH A . 
G 4 HOH 46 455 455 HOH HOH A . 
G 4 HOH 47 456 456 HOH HOH A . 
G 4 HOH 48 457 457 HOH HOH A . 
G 4 HOH 49 458 458 HOH HOH A . 
G 4 HOH 50 459 459 HOH HOH A . 
G 4 HOH 51 460 460 HOH HOH A . 
G 4 HOH 52 461 461 HOH HOH A . 
G 4 HOH 53 464 464 HOH HOH A . 
G 4 HOH 54 473 473 HOH HOH A . 
G 4 HOH 55 474 474 HOH HOH A . 
G 4 HOH 56 475 475 HOH HOH A . 
G 4 HOH 57 476 476 HOH HOH A . 
G 4 HOH 58 477 477 HOH HOH A . 
G 4 HOH 59 478 478 HOH HOH A . 
G 4 HOH 60 479 479 HOH HOH A . 
G 4 HOH 61 480 480 HOH HOH A . 
G 4 HOH 62 481 481 HOH HOH A . 
G 4 HOH 63 482 482 HOH HOH A . 
G 4 HOH 64 483 483 HOH HOH A . 
G 4 HOH 65 484 484 HOH HOH A . 
G 4 HOH 66 485 485 HOH HOH A . 
G 4 HOH 67 491 491 HOH HOH A . 
G 4 HOH 68 492 492 HOH HOH A . 
G 4 HOH 69 493 493 HOH HOH A . 
G 4 HOH 70 494 494 HOH HOH A . 
G 4 HOH 71 495 495 HOH HOH A . 
G 4 HOH 72 496 496 HOH HOH A . 
G 4 HOH 73 497 497 HOH HOH A . 
G 4 HOH 74 498 498 HOH HOH A . 
G 4 HOH 75 499 499 HOH HOH A . 
G 4 HOH 76 500 500 HOH HOH A . 
G 4 HOH 77 501 501 HOH HOH A . 
G 4 HOH 78 502 502 HOH HOH A . 
G 4 HOH 79 504 504 HOH HOH A . 
G 4 HOH 80 508 508 HOH HOH A . 
G 4 HOH 81 512 512 HOH HOH A . 
G 4 HOH 82 523 523 HOH HOH A . 
G 4 HOH 83 525 525 HOH HOH A . 
G 4 HOH 84 527 527 HOH HOH A . 
G 4 HOH 85 528 528 HOH HOH A . 
G 4 HOH 86 529 529 HOH HOH A . 
H 4 HOH 1  356 356 HOH HOH B . 
H 4 HOH 2  357 357 HOH HOH B . 
H 4 HOH 3  358 358 HOH HOH B . 
H 4 HOH 4  359 359 HOH HOH B . 
H 4 HOH 5  360 360 HOH HOH B . 
H 4 HOH 6  361 361 HOH HOH B . 
H 4 HOH 7  362 362 HOH HOH B . 
H 4 HOH 8  363 363 HOH HOH B . 
H 4 HOH 9  364 364 HOH HOH B . 
H 4 HOH 10 368 368 HOH HOH B . 
H 4 HOH 11 369 369 HOH HOH B . 
H 4 HOH 12 370 370 HOH HOH B . 
H 4 HOH 13 371 371 HOH HOH B . 
H 4 HOH 14 375 375 HOH HOH B . 
H 4 HOH 15 376 376 HOH HOH B . 
H 4 HOH 16 377 377 HOH HOH B . 
H 4 HOH 17 378 378 HOH HOH B . 
H 4 HOH 18 379 379 HOH HOH B . 
H 4 HOH 19 380 380 HOH HOH B . 
H 4 HOH 20 381 381 HOH HOH B . 
H 4 HOH 21 383 383 HOH HOH B . 
H 4 HOH 22 384 384 HOH HOH B . 
H 4 HOH 23 385 385 HOH HOH B . 
H 4 HOH 24 386 386 HOH HOH B . 
H 4 HOH 25 387 387 HOH HOH B . 
H 4 HOH 26 396 396 HOH HOH B . 
H 4 HOH 27 397 397 HOH HOH B . 
H 4 HOH 28 398 398 HOH HOH B . 
H 4 HOH 29 402 402 HOH HOH B . 
H 4 HOH 30 405 405 HOH HOH B . 
H 4 HOH 31 408 408 HOH HOH B . 
H 4 HOH 32 411 411 HOH HOH B . 
H 4 HOH 33 412 412 HOH HOH B . 
H 4 HOH 34 413 413 HOH HOH B . 
H 4 HOH 35 414 414 HOH HOH B . 
H 4 HOH 36 415 415 HOH HOH B . 
H 4 HOH 37 417 417 HOH HOH B . 
H 4 HOH 38 426 426 HOH HOH B . 
H 4 HOH 39 432 432 HOH HOH B . 
H 4 HOH 40 433 433 HOH HOH B . 
H 4 HOH 41 435 435 HOH HOH B . 
H 4 HOH 42 436 436 HOH HOH B . 
H 4 HOH 43 441 441 HOH HOH B . 
H 4 HOH 44 442 442 HOH HOH B . 
H 4 HOH 45 444 444 HOH HOH B . 
H 4 HOH 46 445 445 HOH HOH B . 
H 4 HOH 47 446 446 HOH HOH B . 
H 4 HOH 48 447 447 HOH HOH B . 
H 4 HOH 49 448 448 HOH HOH B . 
H 4 HOH 50 449 449 HOH HOH B . 
H 4 HOH 51 450 450 HOH HOH B . 
H 4 HOH 52 451 451 HOH HOH B . 
H 4 HOH 53 452 452 HOH HOH B . 
H 4 HOH 54 462 462 HOH HOH B . 
H 4 HOH 55 463 463 HOH HOH B . 
H 4 HOH 56 465 465 HOH HOH B . 
H 4 HOH 57 466 466 HOH HOH B . 
H 4 HOH 58 467 467 HOH HOH B . 
H 4 HOH 59 468 468 HOH HOH B . 
H 4 HOH 60 469 469 HOH HOH B . 
H 4 HOH 61 470 470 HOH HOH B . 
H 4 HOH 62 471 471 HOH HOH B . 
H 4 HOH 63 472 472 HOH HOH B . 
H 4 HOH 64 486 486 HOH HOH B . 
H 4 HOH 65 487 487 HOH HOH B . 
H 4 HOH 66 488 488 HOH HOH B . 
H 4 HOH 67 489 489 HOH HOH B . 
H 4 HOH 68 490 490 HOH HOH B . 
H 4 HOH 69 503 503 HOH HOH B . 
H 4 HOH 70 505 505 HOH HOH B . 
H 4 HOH 71 506 506 HOH HOH B . 
H 4 HOH 72 507 507 HOH HOH B . 
H 4 HOH 73 509 509 HOH HOH B . 
H 4 HOH 74 510 510 HOH HOH B . 
H 4 HOH 75 511 511 HOH HOH B . 
H 4 HOH 76 513 513 HOH HOH B . 
H 4 HOH 77 514 514 HOH HOH B . 
H 4 HOH 78 515 515 HOH HOH B . 
H 4 HOH 79 516 516 HOH HOH B . 
H 4 HOH 80 517 517 HOH HOH B . 
H 4 HOH 81 518 518 HOH HOH B . 
H 4 HOH 82 519 519 HOH HOH B . 
H 4 HOH 83 520 520 HOH HOH B . 
H 4 HOH 84 521 521 HOH HOH B . 
H 4 HOH 85 522 522 HOH HOH B . 
H 4 HOH 86 524 524 HOH HOH B . 
H 4 HOH 87 526 526 HOH HOH B . 
H 4 HOH 88 530 530 HOH HOH B . 
H 4 HOH 89 531 531 HOH HOH B . 
H 4 HOH 90 532 532 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)' 1440  ? 
1 MORE         -25   ? 
1 'SSA (A^2)'  13950 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 138.9 ? 
2  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 78.2  ? 
3  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 95.4  ? 
4  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 110.7 ? 
5  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 103.1 ? 
6  NE2 ? A HIS 63 ? A HIS 63 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 133.3 ? 
7  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 106.8 ? 
8  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 107.3 ? 
9  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 120.4 ? 
10 ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 106.2 ? 
11 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 101.4 ? 
12 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 113.8 ? 
13 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 144.5 ? 
14 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 95.1  ? 
15 NE2 ? B HIS 48 ? B HIS 48 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 116.5 ? 
16 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 110.4 ? 
17 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 102.0 ? 
18 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 121.6 ? 
19 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 106.5 ? 
20 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 101.7 ? 
21 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 114.0 ? 
22 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 158.6 ? 
23 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 77.4  ? 
24 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 89.5  ? 
25 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 52.2  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 1998-02-25 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-11-03 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2             
2 4 'Structure model' pdbx_struct_conn_angle 
3 4 'Structure model' struct_conn            
4 4 'Structure model' struct_ref_seq_dif     
5 4 'Structure model' struct_site            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_database_2.pdbx_DOI'                       
2  4 'Structure model' '_database_2.pdbx_database_accession'        
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'  
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id' 
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.value'              
8  4 'Structure model' '_struct_conn.pdbx_dist_value'               
9  4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'            
10 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'            
11 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'             
12 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'           
13 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'           
14 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'           
15 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'            
16 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'            
17 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'            
18 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'             
19 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'           
20 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'           
21 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'           
22 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'            
23 4 'Structure model' '_struct_ref_seq_dif.details'                
24 4 'Structure model' '_struct_site.pdbx_auth_asym_id'             
25 4 'Structure model' '_struct_site.pdbx_auth_comp_id'             
26 4 'Structure model' '_struct_site.pdbx_auth_seq_id'              
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' .   ? 1 
SCALEPACK 'data scaling'   .   ? 2 
X-PLOR    'model building' 3.1 ? 3 
X-PLOR    refinement       3.1 ? 4 
X-PLOR    phasing          3.1 ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 65  ? ? -142.42 58.91  
2 1 LYS A 136 ? ? -106.17 -65.00 
3 1 GLU B 24  ? ? -25.13  69.34  
4 1 SER B 25  ? ? 171.53  172.33 
5 1 ASN B 26  ? ? -99.96  59.56  
6 1 ASP B 109 ? ? 80.10   -67.08 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 'ZINC ION'        ZN  
4 water             HOH 
# 
