data_101M
# 
_entry.id   101M 
# 
_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   101M         pdb_0000101m 10.2210/pdb101m/pdb 
WWPDB D_1000170003 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        101M 
_pdbx_database_status.recvd_initial_deposition_date   1997-12-13 
_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.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smith, R.D.'        1 
'Olson, J.S.'        2 
'Phillips Jr., G.N.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Correlations between Bound N-Alkyl Isocyanide Orientations and Pathways for Ligand Binding in Recombinant Myoglobins' 
_citation.journal_abbrev            'Thesis, Rice' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      1999 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0806 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   -1 
_citation.pdbx_database_id_DOI      ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Smith, R.D.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
_cell.entry_id           101M 
_cell.length_a           91.670 
_cell.length_b           91.670 
_cell.length_c           45.970 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         101M 
_symmetry.space_group_name_H-M             'P 6' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                168 
# 
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 MYOGLOBIN                         17317.121 1   ? 'INS(M0), F46V, D122N' ? ? 
2 non-polymer syn 'SULFATE ION'                     96.063    1   ? ?                      ? ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1   ? ?                      ? ? 
4 non-polymer syn 'N-BUTYL ISOCYANIDE'              83.132    1   ? ?                      ? ? 
5 water       nat water                             18.015    138 ? ?                      ? ? 
# 
_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       
;MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRVKHLKTEAEMKASEDLKKHGVTVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRVKHLKTEAEMKASEDLKKHGVTVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_strand_id                 A 
_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   MET n 
1 2   VAL n 
1 3   LEU n 
1 4   SER n 
1 5   GLU n 
1 6   GLY n 
1 7   GLU n 
1 8   TRP n 
1 9   GLN n 
1 10  LEU n 
1 11  VAL n 
1 12  LEU n 
1 13  HIS n 
1 14  VAL n 
1 15  TRP n 
1 16  ALA n 
1 17  LYS n 
1 18  VAL n 
1 19  GLU n 
1 20  ALA n 
1 21  ASP n 
1 22  VAL n 
1 23  ALA n 
1 24  GLY n 
1 25  HIS n 
1 26  GLY n 
1 27  GLN n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  ILE n 
1 32  ARG n 
1 33  LEU n 
1 34  PHE n 
1 35  LYS n 
1 36  SER n 
1 37  HIS n 
1 38  PRO n 
1 39  GLU n 
1 40  THR n 
1 41  LEU n 
1 42  GLU n 
1 43  LYS n 
1 44  PHE n 
1 45  ASP n 
1 46  ARG n 
1 47  VAL n 
1 48  LYS n 
1 49  HIS n 
1 50  LEU n 
1 51  LYS n 
1 52  THR n 
1 53  GLU n 
1 54  ALA n 
1 55  GLU n 
1 56  MET n 
1 57  LYS n 
1 58  ALA n 
1 59  SER n 
1 60  GLU n 
1 61  ASP n 
1 62  LEU n 
1 63  LYS n 
1 64  LYS n 
1 65  HIS n 
1 66  GLY n 
1 67  VAL n 
1 68  THR n 
1 69  VAL n 
1 70  LEU n 
1 71  THR n 
1 72  ALA n 
1 73  LEU n 
1 74  GLY n 
1 75  ALA n 
1 76  ILE n 
1 77  LEU n 
1 78  LYS n 
1 79  LYS n 
1 80  LYS n 
1 81  GLY n 
1 82  HIS n 
1 83  HIS n 
1 84  GLU n 
1 85  ALA n 
1 86  GLU n 
1 87  LEU n 
1 88  LYS n 
1 89  PRO n 
1 90  LEU n 
1 91  ALA n 
1 92  GLN n 
1 93  SER n 
1 94  HIS n 
1 95  ALA n 
1 96  THR n 
1 97  LYS n 
1 98  HIS n 
1 99  LYS n 
1 100 ILE n 
1 101 PRO n 
1 102 ILE n 
1 103 LYS n 
1 104 TYR n 
1 105 LEU n 
1 106 GLU n 
1 107 PHE n 
1 108 ILE n 
1 109 SER n 
1 110 GLU n 
1 111 ALA n 
1 112 ILE n 
1 113 ILE n 
1 114 HIS n 
1 115 VAL n 
1 116 LEU n 
1 117 HIS n 
1 118 SER n 
1 119 ARG n 
1 120 HIS n 
1 121 PRO n 
1 122 GLY n 
1 123 ASN n 
1 124 PHE n 
1 125 GLY n 
1 126 ALA n 
1 127 ASP n 
1 128 ALA n 
1 129 GLN n 
1 130 GLY n 
1 131 ALA n 
1 132 MET n 
1 133 ASN n 
1 134 LYS n 
1 135 ALA n 
1 136 LEU n 
1 137 GLU n 
1 138 LEU n 
1 139 PHE n 
1 140 ARG n 
1 141 LYS n 
1 142 ASP n 
1 143 ILE n 
1 144 ALA n 
1 145 ALA n 
1 146 LYS n 
1 147 TYR n 
1 148 LYS n 
1 149 GLU n 
1 150 LEU n 
1 151 GLY n 
1 152 TYR n 
1 153 GLN n 
1 154 GLY 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               'sperm whale' 
_entity_src_gen.gene_src_genus                     Physeter 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    'SKELETAL MUSCLE' 
_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      'Physeter catodon' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9755 
_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                SKELETAL 
_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               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'PHAGE RESISTANT TB1' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'PEMBL 19+' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MYG_PHYCA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P02185 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              101M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 154 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02185 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  153 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       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 101M VAL A 47  ? UNP P02185 PHE 46  'engineered mutation' 46  1 
1 101M ASN A 123 ? UNP P02185 ASP 122 'engineered mutation' 122 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 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                         ?    'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                             ?    'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                        ?    'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                           ?    'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                            ?    'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
NBN non-polymer         . 'N-BUTYL ISOCYANIDE'              ?    'C5 H9 N'          83.132  
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
SO4 non-polymer         . 'SULFATE ION'                     ?    'O4 S -2'          96.063  
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          101M 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.09 
_exptl_crystal.density_percent_sol   60.2 
_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              9.0 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '3.0 M AMMONIUM SULFATE, 20 MM TRIS, 1MM EDTA, PH 9.0' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           292 
_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   1994-09 
_diffrn_detector.details                'PINHOLE COLLIMATOR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'GRAPHITE(002)' 
_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                        SIEMENS 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     101M 
_reflns.observed_criterion_sigma_I   0. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             6.00 
_reflns.d_resolution_high            2.07 
_reflns.number_obs                   13624 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.0700000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        14.0 
_reflns.pdbx_redundancy              7.45 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.07 
_reflns_shell.d_res_low              2.08 
_reflns_shell.percent_possible_all   100. 
_reflns_shell.Rmerge_I_obs           0.2970000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        7.1 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 101M 
_refine.ls_number_reflns_obs                     12340 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               10000000.00 
_refine.pdbx_data_cutoff_low_absF                0.00100 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             5.00 
_refine.ls_d_res_high                            2.07 
_refine.ls_percent_reflns_obs                    97.8 
_refine.ls_R_factor_obs                          0.1570000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1570000 
_refine.ls_R_factor_R_free                       0.2020000 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  1220 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               24.8 
_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                      'SPERM WHALE MYOGLOBIN 0M, D122N (DEOXY)' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_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                        101M 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             0.17 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.23 
_refine_analyze.Luzzati_sigma_a_free            0.15 
_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        1221 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               1413 
_refine_hist.d_res_high                       2.07 
_refine_hist.d_res_low                        5.00 
# 
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                0.010 ?    ? ? '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             1.4   ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      18.9  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      1.36  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             2.47  1.50 ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            2.86  2.00 ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             8.73  2.50 ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            12.90 2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   8 
_refine_ls_shell.d_res_high                       2.07 
_refine_ls_shell.d_res_low                        2.16 
_refine_ls_shell.number_reflns_R_work             1287 
_refine_ls_shell.R_factor_R_work                  0.2090000 
_refine_ls_shell.percent_reflns_obs               92.9 
_refine_ls_shell.R_factor_R_free                  0.2110000 
_refine_ls_shell.R_factor_R_free_error            0.017 
_refine_ls_shell.percent_reflns_R_free            11.1 
_refine_ls_shell.number_reflns_R_free             161 
_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 PARAMETER.HEME TOPOLOGY.HEME 'X-RAY DIFFRACTION' 
3 PARAMETER.NBNC TOPOLOGY.NBNC 'X-RAY DIFFRACTION' 
4 PARAM19.SOLV   TOPH19.SOLV   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  101M 
_struct.title                     'SPERM WHALE MYOGLOBIN F46V N-BUTYL ISOCYANIDE AT PH 9.0' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        101M 
_struct_keywords.pdbx_keywords   'OXYGEN TRANSPORT' 
_struct_keywords.text            'LIGAND BINDING, OXYGEN STORAGE, OXYGEN BINDING, HEME, OXYGEN TRANSPORT' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 SER A 4   ? GLU A 19  ? SER A 3   GLU A 18  1 ? 16 
HELX_P HELX_P2 2 ASP A 21  ? SER A 36  ? ASP A 20  SER A 35  1 ? 16 
HELX_P HELX_P3 3 HIS A 37  ? LYS A 43  ? HIS A 36  LYS A 42  1 ? 7  
HELX_P HELX_P4 4 THR A 52  ? ALA A 58  ? THR A 51  ALA A 57  1 ? 7  
HELX_P HELX_P5 5 SER A 59  ? LYS A 78  ? SER A 58  LYS A 77  1 ? 20 
HELX_P HELX_P6 6 LEU A 87  ? ALA A 95  ? LEU A 86  ALA A 94  1 ? 9  
HELX_P HELX_P7 7 PRO A 101 ? ARG A 119 ? PRO A 100 ARG A 118 1 ? 19 
HELX_P HELX_P8 8 GLY A 125 ? LEU A 150 ? GLY A 124 LEU A 149 1 ? 26 
# 
_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 
metalc1 metalc ? ? A HIS 94 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 93  A HEM 155 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc2 metalc ? ? C HEM .  FE  ? ? ? 1_555 D NBN . C  ? ? A HEM 155 A NBN 156 1_555 ? ? ? ? ? ? ? 2.110 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 
HEM Unknown  ? ?   ?   ? 1  'LIGAND BINDING SITE.'               
AC1 Software A SO4 157 ? 6  'BINDING SITE FOR RESIDUE SO4 A 157' 
AC2 Software A HEM 155 ? 13 'BINDING SITE FOR RESIDUE HEM A 155' 
AC3 Software A NBN 156 ? 5  'BINDING SITE FOR RESIDUE NBN A 156' 
# 
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  HEM 1  HEM C .   ? HEM A 155 . ? 1_555 ? 
2  AC1 6  SER A 4   ? SER A 3   . ? 1_556 ? 
3  AC1 6  GLU A 5   ? GLU A 4   . ? 1_556 ? 
4  AC1 6  THR A 52  ? THR A 51  . ? 1_555 ? 
5  AC1 6  GLU A 53  ? GLU A 52  . ? 1_555 ? 
6  AC1 6  HOH E .   ? HOH A 268 . ? 1_555 ? 
7  AC1 6  HOH E .   ? HOH A 282 . ? 1_555 ? 
8  AC2 13 LYS A 43  ? LYS A 42  . ? 1_555 ? 
9  AC2 13 PHE A 44  ? PHE A 43  . ? 1_555 ? 
10 AC2 13 ARG A 46  ? ARG A 45  . ? 1_555 ? 
11 AC2 13 LEU A 90  ? LEU A 89  . ? 1_555 ? 
12 AC2 13 SER A 93  ? SER A 92  . ? 1_555 ? 
13 AC2 13 HIS A 94  ? HIS A 93  . ? 1_555 ? 
14 AC2 13 HIS A 98  ? HIS A 97  . ? 1_555 ? 
15 AC2 13 ILE A 100 ? ILE A 99  . ? 1_555 ? 
16 AC2 13 TYR A 104 ? TYR A 103 . ? 1_555 ? 
17 AC2 13 NBN D .   ? NBN A 156 . ? 1_555 ? 
18 AC2 13 HOH E .   ? HOH A 286 . ? 1_555 ? 
19 AC2 13 HOH E .   ? HOH A 287 . ? 1_555 ? 
20 AC2 13 HOH E .   ? HOH A 304 . ? 1_555 ? 
21 AC3 5  PHE A 44  ? PHE A 43  . ? 1_555 ? 
22 AC3 5  HIS A 65  ? HIS A 64  . ? 1_555 ? 
23 AC3 5  THR A 68  ? THR A 67  . ? 1_555 ? 
24 AC3 5  VAL A 69  ? VAL A 68  . ? 1_555 ? 
25 AC3 5  HEM C .   ? HEM A 155 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          101M 
_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                    101M 
_atom_sites.fract_transf_matrix[1][1]   0.010909 
_atom_sites.fract_transf_matrix[1][2]   0.006298 
_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]   0.012596 
_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]   0.021753 
_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  
FE 
N  
O  
S  
# 
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   . MET A 1 1   ? 24.277 8.374   -9.854  1.00 38.41  ? 0   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 24.404 9.859   -9.939  1.00 37.90  ? 0   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 25.814 10.249  -10.359 1.00 36.65  ? 0   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 26.748 9.469   -10.197 1.00 37.13  ? 0   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 24.070 10.495  -8.596  1.00 39.58  ? 0   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 24.880 9.939   -7.442  1.00 41.49  ? 0   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 24.262 10.555  -5.873  1.00 44.70  ? 0   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 24.822 12.266  -5.967  1.00 41.59  ? 0   MET A CE  1 
ATOM   9    N  N   . VAL A 1 2   ? 25.964 11.453  -10.903 1.00 34.54  ? 1   VAL A N   1 
ATOM   10   C  CA  . VAL A 1 2   ? 27.263 11.924  -11.359 1.00 32.46  ? 1   VAL A CA  1 
ATOM   11   C  C   . VAL A 1 2   ? 27.392 13.428  -11.115 1.00 30.70  ? 1   VAL A C   1 
ATOM   12   O  O   . VAL A 1 2   ? 26.443 14.184  -11.327 1.00 31.42  ? 1   VAL A O   1 
ATOM   13   C  CB  . VAL A 1 2   ? 27.455 11.631  -12.878 1.00 32.95  ? 1   VAL A CB  1 
ATOM   14   C  CG1 . VAL A 1 2   ? 28.756 12.209  -13.382 1.00 32.87  ? 1   VAL A CG1 1 
ATOM   15   C  CG2 . VAL A 1 2   ? 27.432 10.131  -13.140 1.00 33.54  ? 1   VAL A CG2 1 
ATOM   16   N  N   . LEU A 1 3   ? 28.555 13.855  -10.636 1.00 27.76  ? 2   LEU A N   1 
ATOM   17   C  CA  . LEU A 1 3   ? 28.797 15.269  -10.390 1.00 25.21  ? 2   LEU A CA  1 
ATOM   18   C  C   . LEU A 1 3   ? 29.492 15.903  -11.585 1.00 24.21  ? 2   LEU A C   1 
ATOM   19   O  O   . LEU A 1 3   ? 30.250 15.240  -12.306 1.00 23.80  ? 2   LEU A O   1 
ATOM   20   C  CB  . LEU A 1 3   ? 29.688 15.470  -9.152  1.00 24.30  ? 2   LEU A CB  1 
ATOM   21   C  CG  . LEU A 1 3   ? 29.084 15.416  -7.751  1.00 22.96  ? 2   LEU A CG  1 
ATOM   22   C  CD1 . LEU A 1 3   ? 28.730 13.988  -7.390  1.00 22.03  ? 2   LEU A CD1 1 
ATOM   23   C  CD2 . LEU A 1 3   ? 30.085 16.008  -6.776  1.00 21.94  ? 2   LEU A CD2 1 
ATOM   24   N  N   . SER A 1 4   ? 29.236 17.185  -11.800 1.00 23.04  ? 3   SER A N   1 
ATOM   25   C  CA  . SER A 1 4   ? 29.898 17.894  -12.882 1.00 22.62  ? 3   SER A CA  1 
ATOM   26   C  C   . SER A 1 4   ? 31.282 18.336  -12.384 1.00 22.06  ? 3   SER A C   1 
ATOM   27   O  O   . SER A 1 4   ? 31.565 18.268  -11.188 1.00 21.06  ? 3   SER A O   1 
ATOM   28   C  CB  . SER A 1 4   ? 29.061 19.097  -13.312 1.00 22.96  ? 3   SER A CB  1 
ATOM   29   O  OG  . SER A 1 4   ? 28.916 20.026  -12.260 1.00 24.01  ? 3   SER A OG  1 
ATOM   30   N  N   . GLU A 1 5   ? 32.151 18.759  -13.296 1.00 17.46  ? 4   GLU A N   1 
ATOM   31   C  CA  . GLU A 1 5   ? 33.489 19.212  -12.922 1.00 24.04  ? 4   GLU A CA  1 
ATOM   32   C  C   . GLU A 1 5   ? 33.346 20.443  -12.019 1.00 21.74  ? 4   GLU A C   1 
ATOM   33   O  O   . GLU A 1 5   ? 34.115 20.620  -11.076 1.00 20.06  ? 4   GLU A O   1 
ATOM   34   C  CB  . GLU A 1 5   ? 34.316 19.551  -14.178 1.00 22.74  ? 4   GLU A CB  1 
ATOM   35   C  CG  . GLU A 1 5   ? 35.720 20.158  -13.921 1.00 18.42  ? 4   GLU A CG  1 
ATOM   36   C  CD  . GLU A 1 5   ? 36.690 19.210  -13.205 1.00 27.97  ? 4   GLU A CD  1 
ATOM   37   O  OE1 . GLU A 1 5   ? 36.449 17.987  -13.166 1.00 27.73  ? 4   GLU A OE1 1 
ATOM   38   O  OE2 . GLU A 1 5   ? 37.711 19.692  -12.684 1.00 28.70  ? 4   GLU A OE2 1 
ATOM   39   N  N   . GLY A 1 6   ? 32.351 21.280  -12.308 1.00 19.09  ? 5   GLY A N   1 
ATOM   40   C  CA  . GLY A 1 6   ? 32.118 22.472  -11.504 1.00 18.12  ? 5   GLY A CA  1 
ATOM   41   C  C   . GLY A 1 6   ? 31.837 22.114  -10.053 1.00 18.29  ? 5   GLY A C   1 
ATOM   42   O  O   . GLY A 1 6   ? 32.353 22.758  -9.137  1.00 17.54  ? 5   GLY A O   1 
ATOM   43   N  N   . GLU A 1 7   ? 31.033 21.069  -9.845  1.00 16.68  ? 6   GLU A N   1 
ATOM   44   C  CA  . GLU A 1 7   ? 30.702 20.617  -8.498  1.00 13.59  ? 6   GLU A CA  1 
ATOM   45   C  C   . GLU A 1 7   ? 31.945 20.007  -7.807  1.00 17.58  ? 6   GLU A C   1 
ATOM   46   O  O   . GLU A 1 7   ? 32.199 20.278  -6.638  1.00 14.97  ? 6   GLU A O   1 
ATOM   47   C  CB  . GLU A 1 7   ? 29.510 19.648  -8.533  1.00 13.04  ? 6   GLU A CB  1 
ATOM   48   C  CG  . GLU A 1 7   ? 28.179 20.319  -8.911  1.00 16.58  ? 6   GLU A CG  1 
ATOM   49   C  CD  . GLU A 1 7   ? 27.056 19.316  -9.262  1.00 18.86  ? 6   GLU A CD  1 
ATOM   50   O  OE1 . GLU A 1 7   ? 27.338 18.242  -9.832  1.00 23.67  ? 6   GLU A OE1 1 
ATOM   51   O  OE2 . GLU A 1 7   ? 25.881 19.612  -8.979  1.00 29.24  ? 6   GLU A OE2 1 
ATOM   52   N  N   . TRP A 1 8   ? 32.747 19.242  -8.545  1.00 15.06  ? 7   TRP A N   1 
ATOM   53   C  CA  . TRP A 1 8   ? 33.970 18.675  -7.985  1.00 15.72  ? 7   TRP A CA  1 
ATOM   54   C  C   . TRP A 1 8   ? 34.932 19.799  -7.595  1.00 16.03  ? 7   TRP A C   1 
ATOM   55   O  O   . TRP A 1 8   ? 35.645 19.687  -6.599  1.00 16.52  ? 7   TRP A O   1 
ATOM   56   C  CB  . TRP A 1 8   ? 34.672 17.733  -8.986  1.00 15.72  ? 7   TRP A CB  1 
ATOM   57   C  CG  . TRP A 1 8   ? 34.046 16.382  -9.056  1.00 15.35  ? 7   TRP A CG  1 
ATOM   58   C  CD1 . TRP A 1 8   ? 33.473 15.795  -10.149 1.00 15.74  ? 7   TRP A CD1 1 
ATOM   59   C  CD2 . TRP A 1 8   ? 33.874 15.466  -7.966  1.00 15.25  ? 7   TRP A CD2 1 
ATOM   60   N  NE1 . TRP A 1 8   ? 32.940 14.573  -9.804  1.00 15.28  ? 7   TRP A NE1 1 
ATOM   61   C  CE2 . TRP A 1 8   ? 33.168 14.345  -8.469  1.00 15.63  ? 7   TRP A CE2 1 
ATOM   62   C  CE3 . TRP A 1 8   ? 34.237 15.486  -6.608  1.00 14.98  ? 7   TRP A CE3 1 
ATOM   63   C  CZ2 . TRP A 1 8   ? 32.813 13.244  -7.652  1.00 15.14  ? 7   TRP A CZ2 1 
ATOM   64   C  CZ3 . TRP A 1 8   ? 33.884 14.394  -5.801  1.00 15.08  ? 7   TRP A CZ3 1 
ATOM   65   C  CH2 . TRP A 1 8   ? 33.178 13.290  -6.328  1.00 14.28  ? 7   TRP A CH2 1 
ATOM   66   N  N   . GLN A 1 9   ? 34.973 20.871  -8.388  1.00 15.81  ? 8   GLN A N   1 
ATOM   67   C  CA  . GLN A 1 9   ? 35.856 21.987  -8.080  1.00 16.01  ? 8   GLN A CA  1 
ATOM   68   C  C   . GLN A 1 9   ? 35.445 22.668  -6.769  1.00 15.78  ? 8   GLN A C   1 
ATOM   69   O  O   . GLN A 1 9   ? 36.305 23.057  -5.973  1.00 15.65  ? 8   GLN A O   1 
ATOM   70   C  CB  . GLN A 1 9   ? 35.893 22.989  -9.235  1.00 17.95  ? 8   GLN A CB  1 
ATOM   71   C  CG  . GLN A 1 9   ? 36.613 22.459  -10.451 1.00 25.32  ? 8   GLN A CG  1 
ATOM   72   C  CD  . GLN A 1 9   ? 38.055 22.125  -10.145 1.00 39.60  ? 8   GLN A CD  1 
ATOM   73   O  OE1 . GLN A 1 9   ? 38.883 23.023  -9.983  1.00 67.02  ? 8   GLN A OE1 1 
ATOM   74   N  NE2 . GLN A 1 9   ? 38.366 20.830  -10.043 1.00 43.80  ? 8   GLN A NE2 1 
ATOM   75   N  N   . LEU A 1 10  ? 34.141 22.788  -6.533  1.00 14.97  ? 9   LEU A N   1 
ATOM   76   C  CA  . LEU A 1 10  ? 33.661 23.390  -5.284  1.00 14.87  ? 9   LEU A CA  1 
ATOM   77   C  C   . LEU A 1 10  ? 34.055 22.525  -4.081  1.00 14.68  ? 9   LEU A C   1 
ATOM   78   O  O   . LEU A 1 10  ? 34.515 23.031  -3.061  1.00 14.85  ? 9   LEU A O   1 
ATOM   79   C  CB  . LEU A 1 10  ? 32.141 23.586  -5.317  1.00 15.27  ? 9   LEU A CB  1 
ATOM   80   C  CG  . LEU A 1 10  ? 31.668 24.723  -6.235  1.00 15.96  ? 9   LEU A CG  1 
ATOM   81   C  CD1 . LEU A 1 10  ? 30.164 24.757  -6.306  1.00 15.80  ? 9   LEU A CD1 1 
ATOM   82   C  CD2 . LEU A 1 10  ? 32.205 26.043  -5.730  1.00 16.40  ? 9   LEU A CD2 1 
ATOM   83   N  N   . VAL A 1 11  ? 33.913 21.215  -4.236  1.00 13.96  ? 10  VAL A N   1 
ATOM   84   C  CA  . VAL A 1 11  ? 34.247 20.256  -3.195  1.00 13.50  ? 10  VAL A CA  1 
ATOM   85   C  C   . VAL A 1 11  ? 35.742 20.293  -2.878  1.00 14.08  ? 10  VAL A C   1 
ATOM   86   O  O   . VAL A 1 11  ? 36.144 20.446  -1.721  1.00 14.08  ? 10  VAL A O   1 
ATOM   87   C  CB  . VAL A 1 11  ? 33.821 18.826  -3.640  1.00 13.81  ? 10  VAL A CB  1 
ATOM   88   C  CG1 . VAL A 1 11  ? 34.428 17.746  -2.739  1.00 13.51  ? 10  VAL A CG1 1 
ATOM   89   C  CG2 . VAL A 1 11  ? 32.289 18.724  -3.657  1.00 13.28  ? 10  VAL A CG2 1 
ATOM   90   N  N   . LEU A 1 12  ? 36.563 20.208  -3.915  1.00 14.31  ? 11  LEU A N   1 
ATOM   91   C  CA  . LEU A 1 12  ? 38.005 20.200  -3.741  1.00 14.80  ? 11  LEU A CA  1 
ATOM   92   C  C   . LEU A 1 12  ? 38.590 21.529  -3.282  1.00 15.08  ? 11  LEU A C   1 
ATOM   93   O  O   . LEU A 1 12  ? 39.613 21.537  -2.605  1.00 15.16  ? 11  LEU A O   1 
ATOM   94   C  CB  . LEU A 1 12  ? 38.690 19.677  -5.007  1.00 15.74  ? 11  LEU A CB  1 
ATOM   95   C  CG  . LEU A 1 12  ? 38.310 18.212  -5.299  1.00 16.67  ? 11  LEU A CG  1 
ATOM   96   C  CD1 . LEU A 1 12  ? 38.911 17.765  -6.605  1.00 18.20  ? 11  LEU A CD1 1 
ATOM   97   C  CD2 . LEU A 1 12  ? 38.778 17.300  -4.167  1.00 17.64  ? 11  LEU A CD2 1 
ATOM   98   N  N   . HIS A 1 13  ? 37.915 22.640  -3.577  1.00 15.37  ? 12  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 38.390 23.965  -3.145  1.00 15.95  ? 12  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 38.229 24.124  -1.625  1.00 15.98  ? 12  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 39.105 24.662  -0.963  1.00 16.51  ? 12  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 37.650 25.092  -3.887  1.00 19.33  ? 12  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 38.064 26.470  -3.467  1.00 28.57  ? 12  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 39.323 26.998  -3.668  1.00 38.92  ? 12  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 37.357 27.443  -2.836  1.00 35.58  ? 12  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 39.341 28.247  -3.167  1.00 37.34  ? 12  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 38.171 28.566  -2.650  1.00 33.72  ? 12  HIS A NE2 1 
ATOM   108  N  N   . VAL A 1 14  ? 37.107 23.672  -1.070  1.00 15.74  ? 13  VAL A N   1 
ATOM   109  C  CA  . VAL A 1 14  ? 36.934 23.758  0.379   1.00 15.64  ? 13  VAL A CA  1 
ATOM   110  C  C   . VAL A 1 14  ? 37.792 22.681  1.085   1.00 15.33  ? 13  VAL A C   1 
ATOM   111  O  O   . VAL A 1 14  ? 38.342 22.921  2.160   1.00 15.39  ? 13  VAL A O   1 
ATOM   112  C  CB  . VAL A 1 14  ? 35.424 23.682  0.816   1.00 16.72  ? 13  VAL A CB  1 
ATOM   113  C  CG1 . VAL A 1 14  ? 34.851 22.287  0.601   1.00 16.66  ? 13  VAL A CG1 1 
ATOM   114  C  CG2 . VAL A 1 14  ? 35.283 24.085  2.288   1.00 17.08  ? 13  VAL A CG2 1 
ATOM   115  N  N   . TRP A 1 15  ? 37.958 21.524  0.448   1.00 14.73  ? 14  TRP A N   1 
ATOM   116  C  CA  . TRP A 1 15  ? 38.770 20.457  1.017   1.00 14.75  ? 14  TRP A CA  1 
ATOM   117  C  C   . TRP A 1 15  ? 40.241 20.879  1.166   1.00 14.64  ? 14  TRP A C   1 
ATOM   118  O  O   . TRP A 1 15  ? 40.921 20.456  2.099   1.00 15.14  ? 14  TRP A O   1 
ATOM   119  C  CB  . TRP A 1 15  ? 38.673 19.191  0.164   1.00 15.26  ? 14  TRP A CB  1 
ATOM   120  C  CG  . TRP A 1 15  ? 39.146 17.993  0.901   1.00 16.17  ? 14  TRP A CG  1 
ATOM   121  C  CD1 . TRP A 1 15  ? 40.356 17.387  0.782   1.00 16.11  ? 14  TRP A CD1 1 
ATOM   122  C  CD2 . TRP A 1 15  ? 38.458 17.320  1.969   1.00 16.43  ? 14  TRP A CD2 1 
ATOM   123  N  NE1 . TRP A 1 15  ? 40.477 16.388  1.722   1.00 16.54  ? 14  TRP A NE1 1 
ATOM   124  C  CE2 . TRP A 1 15  ? 39.328 16.325  2.463   1.00 15.93  ? 14  TRP A CE2 1 
ATOM   125  C  CE3 . TRP A 1 15  ? 37.191 17.471  2.561   1.00 16.69  ? 14  TRP A CE3 1 
ATOM   126  C  CZ2 . TRP A 1 15  ? 38.983 15.480  3.522   1.00 16.79  ? 14  TRP A CZ2 1 
ATOM   127  C  CZ3 . TRP A 1 15  ? 36.842 16.622  3.626   1.00 17.61  ? 14  TRP A CZ3 1 
ATOM   128  C  CH2 . TRP A 1 15  ? 37.744 15.638  4.093   1.00 16.93  ? 14  TRP A CH2 1 
ATOM   129  N  N   . ALA A 1 16  ? 40.726 21.722  0.254   1.00 14.42  ? 15  ALA A N   1 
ATOM   130  C  CA  . ALA A 1 16  ? 42.095 22.214  0.312   1.00 14.00  ? 15  ALA A CA  1 
ATOM   131  C  C   . ALA A 1 16  ? 42.328 22.999  1.608   1.00 14.30  ? 15  ALA A C   1 
ATOM   132  O  O   . ALA A 1 16  ? 43.427 22.982  2.156   1.00 14.23  ? 15  ALA A O   1 
ATOM   133  C  CB  . ALA A 1 16  ? 42.389 23.080  -0.896  1.00 14.14  ? 15  ALA A CB  1 
ATOM   134  N  N   . LYS A 1 17  ? 41.270 23.635  2.124   1.00 15.22  ? 16  LYS A N   1 
ATOM   135  C  CA  . LYS A 1 17  ? 41.345 24.400  3.376   1.00 17.82  ? 16  LYS A CA  1 
ATOM   136  C  C   . LYS A 1 17  ? 41.371 23.426  4.548   1.00 14.95  ? 16  LYS A C   1 
ATOM   137  O  O   . LYS A 1 17  ? 42.124 23.616  5.491   1.00 18.06  ? 16  LYS A O   1 
ATOM   138  C  CB  . LYS A 1 17  ? 40.146 25.350  3.539   1.00 11.85  ? 16  LYS A CB  1 
ATOM   139  C  CG  . LYS A 1 17  ? 39.931 26.312  2.396   1.00 15.52  ? 16  LYS A CG  1 
ATOM   140  C  CD  . LYS A 1 17  ? 41.171 27.093  2.107   1.00 22.34  ? 16  LYS A CD  1 
ATOM   141  C  CE  . LYS A 1 17  ? 41.010 27.867  0.817   1.00 43.61  ? 16  LYS A CE  1 
ATOM   142  N  NZ  . LYS A 1 17  ? 42.298 28.453  0.378   1.00 41.54  ? 16  LYS A NZ  1 
ATOM   143  N  N   . VAL A 1 18  ? 40.524 22.398  4.491   1.00 12.40  ? 17  VAL A N   1 
ATOM   144  C  CA  . VAL A 1 18  ? 40.473 21.367  5.522   1.00 12.29  ? 17  VAL A CA  1 
ATOM   145  C  C   . VAL A 1 18  ? 41.872 20.771  5.701   1.00 12.32  ? 17  VAL A C   1 
ATOM   146  O  O   . VAL A 1 18  ? 42.329 20.560  6.829   1.00 12.74  ? 17  VAL A O   1 
ATOM   147  C  CB  . VAL A 1 18  ? 39.496 20.242  5.116   1.00 12.43  ? 17  VAL A CB  1 
ATOM   148  C  CG1 . VAL A 1 18  ? 39.596 19.045  6.073   1.00 12.58  ? 17  VAL A CG1 1 
ATOM   149  C  CG2 . VAL A 1 18  ? 38.088 20.787  5.082   1.00 13.47  ? 17  VAL A CG2 1 
ATOM   150  N  N   . GLU A 1 19  ? 42.553 20.513  4.584   1.00 13.88  ? 18  GLU A N   1 
ATOM   151  C  CA  . GLU A 1 19  ? 43.904 19.940  4.618   1.00 14.94  ? 18  GLU A CA  1 
ATOM   152  C  C   . GLU A 1 19  ? 44.991 20.813  5.262   1.00 16.26  ? 18  GLU A C   1 
ATOM   153  O  O   . GLU A 1 19  ? 46.070 20.322  5.560   1.00 15.32  ? 18  GLU A O   1 
ATOM   154  C  CB  . GLU A 1 19  ? 44.327 19.461  3.235   1.00 12.91  ? 18  GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 19  ? 43.572 18.228  2.808   1.00 13.99  ? 18  GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 19  ? 44.011 17.692  1.458   1.00 16.75  ? 18  GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 19  ? 44.559 18.458  0.644   1.00 21.92  ? 18  GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 19  ? 43.791 16.493  1.217   1.00 23.33  ? 18  GLU A OE2 1 
ATOM   159  N  N   . ALA A 1 20  ? 44.708 22.090  5.501   1.00 14.20  ? 19  ALA A N   1 
ATOM   160  C  CA  . ALA A 1 20  ? 45.686 22.946  6.169   1.00 14.94  ? 19  ALA A CA  1 
ATOM   161  C  C   . ALA A 1 20  ? 45.780 22.500  7.624   1.00 14.81  ? 19  ALA A C   1 
ATOM   162  O  O   . ALA A 1 20  ? 46.773 22.759  8.295   1.00 15.01  ? 19  ALA A O   1 
ATOM   163  C  CB  . ALA A 1 20  ? 45.259 24.418  6.110   1.00 14.54  ? 19  ALA A CB  1 
ATOM   164  N  N   . ASP A 1 21  ? 44.731 21.837  8.111   1.00 12.28  ? 20  ASP A N   1 
ATOM   165  C  CA  . ASP A 1 21  ? 44.693 21.368  9.492   1.00 12.72  ? 20  ASP A CA  1 
ATOM   166  C  C   . ASP A 1 21  ? 43.810 20.117  9.606   1.00 18.12  ? 20  ASP A C   1 
ATOM   167  O  O   . ASP A 1 21  ? 42.686 20.173  10.131  1.00 13.62  ? 20  ASP A O   1 
ATOM   168  C  CB  . ASP A 1 21  ? 44.157 22.490  10.403  1.00 10.25  ? 20  ASP A CB  1 
ATOM   169  C  CG  . ASP A 1 21  ? 44.073 22.074  11.865  1.00 19.39  ? 20  ASP A CG  1 
ATOM   170  O  OD1 . ASP A 1 21  ? 44.848 21.187  12.301  1.00 17.74  ? 20  ASP A OD1 1 
ATOM   171  O  OD2 . ASP A 1 21  ? 43.195 22.613  12.564  1.00 26.16  ? 20  ASP A OD2 1 
ATOM   172  N  N   . VAL A 1 22  ? 44.343 18.987  9.164   1.00 14.51  ? 21  VAL A N   1 
ATOM   173  C  CA  . VAL A 1 22  ? 43.597 17.741  9.183   1.00 16.06  ? 21  VAL A CA  1 
ATOM   174  C  C   . VAL A 1 22  ? 43.223 17.273  10.588  1.00 15.92  ? 21  VAL A C   1 
ATOM   175  O  O   . VAL A 1 22  ? 42.095 16.857  10.810  1.00 16.38  ? 21  VAL A O   1 
ATOM   176  C  CB  . VAL A 1 22  ? 44.360 16.610  8.409   1.00 17.48  ? 21  VAL A CB  1 
ATOM   177  C  CG1 . VAL A 1 22  ? 43.603 15.292  8.507   1.00 16.78  ? 21  VAL A CG1 1 
ATOM   178  C  CG2 . VAL A 1 22  ? 44.521 17.021  6.937   1.00 17.19  ? 21  VAL A CG2 1 
ATOM   179  N  N   . ALA A 1 23  ? 44.151 17.364  11.537  1.00 15.42  ? 22  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 23  ? 43.871 16.937  12.907  1.00 15.58  ? 22  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 23  ? 42.787 17.773  13.591  1.00 15.11  ? 22  ALA A C   1 
ATOM   182  O  O   . ALA A 1 23  ? 41.894 17.227  14.221  1.00 14.57  ? 22  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 23  ? 45.154 16.940  13.734  1.00 16.03  ? 22  ALA A CB  1 
ATOM   184  N  N   . GLY A 1 24  ? 42.865 19.094  13.443  1.00 14.85  ? 23  GLY A N   1 
ATOM   185  C  CA  . GLY A 1 24  ? 41.882 19.978  14.035  1.00 13.95  ? 23  GLY A CA  1 
ATOM   186  C  C   . GLY A 1 24  ? 40.485 19.730  13.490  1.00 13.74  ? 23  GLY A C   1 
ATOM   187  O  O   . GLY A 1 24  ? 39.507 19.711  14.255  1.00 13.81  ? 23  GLY A O   1 
ATOM   188  N  N   . HIS A 1 25  ? 40.369 19.561  12.175  1.00 13.07  ? 24  HIS A N   1 
ATOM   189  C  CA  . HIS A 1 25  ? 39.059 19.308  11.561  1.00 12.67  ? 24  HIS A CA  1 
ATOM   190  C  C   . HIS A 1 25  ? 38.525 17.941  11.970  1.00 12.65  ? 24  HIS A C   1 
ATOM   191  O  O   . HIS A 1 25  ? 37.326 17.804  12.187  1.00 13.43  ? 24  HIS A O   1 
ATOM   192  C  CB  . HIS A 1 25  ? 39.138 19.392  10.037  1.00 10.49  ? 24  HIS A CB  1 
ATOM   193  C  CG  . HIS A 1 25  ? 39.212 20.790  9.513   1.00 13.59  ? 24  HIS A CG  1 
ATOM   194  N  ND1 . HIS A 1 25  ? 40.371 21.531  9.447   1.00 10.53  ? 24  HIS A ND1 1 
ATOM   195  C  CD2 . HIS A 1 25  ? 38.245 21.571  8.963   1.00 10.81  ? 24  HIS A CD2 1 
ATOM   196  C  CE1 . HIS A 1 25  ? 40.078 22.706  8.860   1.00 11.16  ? 24  HIS A CE1 1 
ATOM   197  N  NE2 . HIS A 1 25  ? 38.798 22.777  8.549   1.00 12.09  ? 24  HIS A NE2 1 
ATOM   198  N  N   . GLY A 1 26  ? 39.410 16.943  12.063  1.00 12.41  ? 25  GLY A N   1 
ATOM   199  C  CA  . GLY A 1 26  ? 39.014 15.593  12.468  1.00 13.17  ? 25  GLY A CA  1 
ATOM   200  C  C   . GLY A 1 26  ? 38.428 15.545  13.875  1.00 13.87  ? 25  GLY A C   1 
ATOM   201  O  O   . GLY A 1 26  ? 37.460 14.826  14.124  1.00 13.35  ? 25  GLY A O   1 
ATOM   202  N  N   . GLN A 1 27  ? 39.034 16.291  14.804  1.00 14.34  ? 26  GLN A N   1 
ATOM   203  C  CA  . GLN A 1 27  ? 38.534 16.366  16.171  1.00 15.16  ? 26  GLN A CA  1 
ATOM   204  C  C   . GLN A 1 27  ? 37.140 17.000  16.198  1.00 15.26  ? 26  GLN A C   1 
ATOM   205  O  O   . GLN A 1 27  ? 36.221 16.467  16.829  1.00 15.39  ? 26  GLN A O   1 
ATOM   206  C  CB  . GLN A 1 27  ? 39.448 17.215  17.054  1.00 17.03  ? 26  GLN A CB  1 
ATOM   207  C  CG  . GLN A 1 27  ? 40.466 16.432  17.822  1.00 28.33  ? 26  GLN A CG  1 
ATOM   208  C  CD  . GLN A 1 27  ? 41.526 17.332  18.433  1.00 40.00  ? 26  GLN A CD  1 
ATOM   209  O  OE1 . GLN A 1 27  ? 42.133 18.162  17.746  1.00 36.88  ? 26  GLN A OE1 1 
ATOM   210  N  NE2 . GLN A 1 27  ? 41.709 17.218  19.740  1.00 36.42  ? 26  GLN A NE2 1 
ATOM   211  N  N   . ASP A 1 28  ? 37.003 18.168  15.568  1.00 10.78  ? 27  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 28  ? 35.721 18.874  15.540  1.00 12.70  ? 27  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 28  ? 34.599 18.016  14.999  1.00 15.39  ? 27  ASP A C   1 
ATOM   214  O  O   . ASP A 1 28  ? 33.494 18.020  15.527  1.00 12.27  ? 27  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 28  ? 35.820 20.133  14.669  1.00 11.23  ? 27  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 28  ? 36.637 21.235  15.311  1.00 27.34  ? 27  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 28  ? 37.197 21.014  16.412  1.00 27.80  ? 27  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 28  ? 36.720 22.323  14.702  1.00 23.75  ? 27  ASP A OD2 1 
ATOM   219  N  N   . ILE A 1 29  ? 34.880 17.341  13.890  1.00 12.88  ? 28  ILE A N   1 
ATOM   220  C  CA  . ILE A 1 29  ? 33.906 16.477  13.242  1.00 13.76  ? 28  ILE A CA  1 
ATOM   221  C  C   . ILE A 1 29  ? 33.472 15.291  14.124  1.00 14.47  ? 28  ILE A C   1 
ATOM   222  O  O   . ILE A 1 29  ? 32.263 15.032  14.276  1.00 14.63  ? 28  ILE A O   1 
ATOM   223  C  CB  . ILE A 1 29  ? 34.446 15.993  11.846  1.00 13.13  ? 28  ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 29  ? 34.381 17.154  10.842  1.00 13.35  ? 28  ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 29  ? 33.644 14.809  11.323  1.00 12.02  ? 28  ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 29  ? 35.210 16.957  9.578   1.00 12.89  ? 28  ILE A CD1 1 
ATOM   227  N  N   . LEU A 1 30  ? 34.440 14.596  14.731  1.00 15.19  ? 29  LEU A N   1 
ATOM   228  C  CA  . LEU A 1 30  ? 34.118 13.441  15.571  1.00 15.68  ? 29  LEU A CA  1 
ATOM   229  C  C   . LEU A 1 30  ? 33.400 13.853  16.847  1.00 16.10  ? 29  LEU A C   1 
ATOM   230  O  O   . LEU A 1 30  ? 32.471 13.181  17.283  1.00 16.45  ? 29  LEU A O   1 
ATOM   231  C  CB  . LEU A 1 30  ? 35.359 12.614  15.898  1.00 15.76  ? 29  LEU A CB  1 
ATOM   232  C  CG  . LEU A 1 30  ? 35.978 11.809  14.749  1.00 16.40  ? 29  LEU A CG  1 
ATOM   233  C  CD1 . LEU A 1 30  ? 37.043 10.854  15.303  1.00 16.35  ? 29  LEU A CD1 1 
ATOM   234  C  CD2 . LEU A 1 30  ? 34.917 11.008  14.016  1.00 17.12  ? 29  LEU A CD2 1 
ATOM   235  N  N   . ILE A 1 31  ? 33.818 14.971  17.432  1.00 16.13  ? 30  ILE A N   1 
ATOM   236  C  CA  . ILE A 1 31  ? 33.178 15.463  18.644  1.00 16.60  ? 30  ILE A CA  1 
ATOM   237  C  C   . ILE A 1 31  ? 31.725 15.839  18.311  1.00 17.11  ? 30  ILE A C   1 
ATOM   238  O  O   . ILE A 1 31  ? 30.798 15.495  19.058  1.00 17.25  ? 30  ILE A O   1 
ATOM   239  C  CB  . ILE A 1 31  ? 33.974 16.652  19.250  1.00 15.99  ? 30  ILE A CB  1 
ATOM   240  C  CG1 . ILE A 1 31  ? 35.260 16.118  19.907  1.00 16.25  ? 30  ILE A CG1 1 
ATOM   241  C  CG2 . ILE A 1 31  ? 33.113 17.437  20.245  1.00 16.34  ? 30  ILE A CG2 1 
ATOM   242  C  CD1 . ILE A 1 31  ? 36.262 17.204  20.328  1.00 15.83  ? 30  ILE A CD1 1 
ATOM   243  N  N   . ARG A 1 32  ? 31.529 16.494  17.168  1.00 16.96  ? 31  ARG A N   1 
ATOM   244  C  CA  . ARG A 1 32  ? 30.191 16.862  16.720  1.00 17.72  ? 31  ARG A CA  1 
ATOM   245  C  C   . ARG A 1 32  ? 29.353 15.590  16.560  1.00 18.25  ? 31  ARG A C   1 
ATOM   246  O  O   . ARG A 1 32  ? 28.242 15.514  17.080  1.00 18.06  ? 31  ARG A O   1 
ATOM   247  C  CB  . ARG A 1 32  ? 30.274 17.644  15.403  1.00 19.03  ? 31  ARG A CB  1 
ATOM   248  C  CG  . ARG A 1 32  ? 28.959 17.951  14.704  1.00 27.75  ? 31  ARG A CG  1 
ATOM   249  C  CD  . ARG A 1 32  ? 27.820 18.210  15.662  1.00 35.54  ? 31  ARG A CD  1 
ATOM   250  N  NE  . ARG A 1 32  ? 27.590 19.622  15.937  1.00 55.89  ? 31  ARG A NE  1 
ATOM   251  C  CZ  . ARG A 1 32  ? 26.431 20.247  15.732  1.00 59.53  ? 31  ARG A CZ  1 
ATOM   252  N  NH1 . ARG A 1 32  ? 25.407 19.623  15.163  1.00 55.77  ? 31  ARG A NH1 1 
ATOM   253  N  NH2 . ARG A 1 32  ? 26.316 21.528  16.038  1.00 80.31  ? 31  ARG A NH2 1 
ATOM   254  N  N   . LEU A 1 33  ? 29.923 14.573  15.913  1.00 18.72  ? 32  LEU A N   1 
ATOM   255  C  CA  . LEU A 1 33  ? 29.229 13.303  15.710  1.00 18.89  ? 32  LEU A CA  1 
ATOM   256  C  C   . LEU A 1 33  ? 28.820 12.652  17.035  1.00 19.55  ? 32  LEU A C   1 
ATOM   257  O  O   . LEU A 1 33  ? 27.656 12.283  17.216  1.00 19.27  ? 32  LEU A O   1 
ATOM   258  C  CB  . LEU A 1 33  ? 30.107 12.321  14.912  1.00 18.43  ? 32  LEU A CB  1 
ATOM   259  C  CG  . LEU A 1 33  ? 29.518 10.900  14.774  1.00 18.35  ? 32  LEU A CG  1 
ATOM   260  C  CD1 . LEU A 1 33  ? 28.310 10.917  13.853  1.00 16.58  ? 32  LEU A CD1 1 
ATOM   261  C  CD2 . LEU A 1 33  ? 30.569 9.897   14.281  1.00 17.13  ? 32  LEU A CD2 1 
ATOM   262  N  N   . PHE A 1 34  ? 29.785 12.525  17.950  1.00 20.12  ? 33  PHE A N   1 
ATOM   263  C  CA  . PHE A 1 34  ? 29.574 11.902  19.263  1.00 20.56  ? 33  PHE A CA  1 
ATOM   264  C  C   . PHE A 1 34  ? 28.594 12.652  20.164  1.00 21.82  ? 33  PHE A C   1 
ATOM   265  O  O   . PHE A 1 34  ? 27.863 12.029  20.941  1.00 23.10  ? 33  PHE A O   1 
ATOM   266  C  CB  . PHE A 1 34  ? 30.905 11.724  19.981  1.00 19.32  ? 33  PHE A CB  1 
ATOM   267  C  CG  . PHE A 1 34  ? 31.858 10.805  19.263  1.00 18.94  ? 33  PHE A CG  1 
ATOM   268  C  CD1 . PHE A 1 34  ? 31.375 9.740   18.495  1.00 17.83  ? 33  PHE A CD1 1 
ATOM   269  C  CD2 . PHE A 1 34  ? 33.239 10.991  19.365  1.00 17.60  ? 33  PHE A CD2 1 
ATOM   270  C  CE1 . PHE A 1 34  ? 32.254 8.878   17.843  1.00 17.15  ? 33  PHE A CE1 1 
ATOM   271  C  CE2 . PHE A 1 34  ? 34.119 10.133  18.714  1.00 17.04  ? 33  PHE A CE2 1 
ATOM   272  C  CZ  . PHE A 1 34  ? 33.617 9.072   17.951  1.00 17.09  ? 33  PHE A CZ  1 
ATOM   273  N  N   . LYS A 1 35  ? 28.568 13.977  20.061  1.00 23.38  ? 34  LYS A N   1 
ATOM   274  C  CA  . LYS A 1 35  ? 27.645 14.757  20.863  1.00 25.09  ? 34  LYS A CA  1 
ATOM   275  C  C   . LYS A 1 35  ? 26.242 14.704  20.284  1.00 25.17  ? 34  LYS A C   1 
ATOM   276  O  O   . LYS A 1 35  ? 25.273 14.626  21.026  1.00 38.31  ? 34  LYS A O   1 
ATOM   277  C  CB  . LYS A 1 35  ? 28.086 16.223  20.966  1.00 20.77  ? 34  LYS A CB  1 
ATOM   278  C  CG  . LYS A 1 35  ? 29.350 16.430  21.783  1.00 42.45  ? 34  LYS A CG  1 
ATOM   279  C  CD  . LYS A 1 35  ? 29.403 17.826  22.398  1.00 68.05  ? 34  LYS A CD  1 
ATOM   280  C  CE  . LYS A 1 35  ? 29.075 18.906  21.384  1.00 74.10  ? 34  LYS A CE  1 
ATOM   281  N  NZ  . LYS A 1 35  ? 29.655 20.230  21.749  1.00 58.94  ? 34  LYS A NZ  1 
ATOM   282  N  N   . SER A 1 36  ? 26.131 14.777  18.961  1.00 26.05  ? 35  SER A N   1 
ATOM   283  C  CA  . SER A 1 36  ? 24.834 14.759  18.309  1.00 26.21  ? 35  SER A CA  1 
ATOM   284  C  C   . SER A 1 36  ? 24.189 13.390  18.335  1.00 26.05  ? 35  SER A C   1 
ATOM   285  O  O   . SER A 1 36  ? 22.970 13.289  18.389  1.00 25.95  ? 35  SER A O   1 
ATOM   286  C  CB  . SER A 1 36  ? 24.960 15.191  16.854  1.00 26.90  ? 35  SER A CB  1 
ATOM   287  O  OG  . SER A 1 36  ? 25.495 16.497  16.745  1.00 30.21  ? 35  SER A OG  1 
ATOM   288  N  N   . HIS A 1 37  ? 25.013 12.347  18.240  1.00 25.46  ? 36  HIS A N   1 
ATOM   289  C  CA  . HIS A 1 37  ? 24.534 10.971  18.219  1.00 25.07  ? 36  HIS A CA  1 
ATOM   290  C  C   . HIS A 1 37  ? 25.441 10.076  19.042  1.00 24.90  ? 36  HIS A C   1 
ATOM   291  O  O   . HIS A 1 37  ? 26.194 9.289   18.490  1.00 25.25  ? 36  HIS A O   1 
ATOM   292  C  CB  . HIS A 1 37  ? 24.470 10.443  16.774  1.00 23.40  ? 36  HIS A CB  1 
ATOM   293  C  CG  . HIS A 1 37  ? 23.718 11.332  15.835  1.00 21.61  ? 36  HIS A CG  1 
ATOM   294  N  ND1 . HIS A 1 37  ? 22.358 11.266  15.627  1.00 22.67  ? 36  HIS A ND1 1 
ATOM   295  C  CD2 . HIS A 1 37  ? 24.160 12.339  15.040  1.00 23.65  ? 36  HIS A CD2 1 
ATOM   296  C  CE1 . HIS A 1 37  ? 22.026 12.208  14.740  1.00 17.49  ? 36  HIS A CE1 1 
ATOM   297  N  NE2 . HIS A 1 37  ? 23.084 12.890  14.349  1.00 22.98  ? 36  HIS A NE2 1 
ATOM   298  N  N   . PRO A 1 38  ? 25.290 10.107  20.377  1.00 25.00  ? 37  PRO A N   1 
ATOM   299  C  CA  . PRO A 1 38  ? 26.053 9.339   21.363  1.00 24.52  ? 37  PRO A CA  1 
ATOM   300  C  C   . PRO A 1 38  ? 26.122 7.836   21.124  1.00 24.44  ? 37  PRO A C   1 
ATOM   301  O  O   . PRO A 1 38  ? 27.090 7.183   21.514  1.00 24.78  ? 37  PRO A O   1 
ATOM   302  C  CB  . PRO A 1 38  ? 25.321 9.652   22.666  1.00 25.11  ? 37  PRO A CB  1 
ATOM   303  C  CG  . PRO A 1 38  ? 24.767 11.032  22.422  1.00 24.88  ? 37  PRO A CG  1 
ATOM   304  C  CD  . PRO A 1 38  ? 24.219 10.875  21.045  1.00 25.04  ? 37  PRO A CD  1 
ATOM   305  N  N   . GLU A 1 39  ? 25.106 7.280   20.478  1.00 20.50  ? 38  GLU A N   1 
ATOM   306  C  CA  . GLU A 1 39  ? 25.099 5.847   20.204  1.00 27.23  ? 38  GLU A CA  1 
ATOM   307  C  C   . GLU A 1 39  ? 26.292 5.452   19.344  1.00 18.36  ? 38  GLU A C   1 
ATOM   308  O  O   . GLU A 1 39  ? 26.814 4.359   19.481  1.00 31.79  ? 38  GLU A O   1 
ATOM   309  C  CB  . GLU A 1 39  ? 23.779 5.401   19.539  1.00 20.46  ? 38  GLU A CB  1 
ATOM   310  C  CG  . GLU A 1 39  ? 23.458 6.000   18.159  1.00 21.91  ? 38  GLU A CG  1 
ATOM   311  C  CD  . GLU A 1 39  ? 22.672 7.310   18.209  1.00 38.03  ? 38  GLU A CD  1 
ATOM   312  O  OE1 . GLU A 1 39  ? 22.775 8.087   19.180  1.00 33.84  ? 38  GLU A OE1 1 
ATOM   313  O  OE2 . GLU A 1 39  ? 21.940 7.573   17.243  1.00 40.21  ? 38  GLU A OE2 1 
ATOM   314  N  N   . THR A 1 40  ? 26.760 6.365   18.497  1.00 22.46  ? 39  THR A N   1 
ATOM   315  C  CA  . THR A 1 40  ? 27.898 6.075   17.627  1.00 22.43  ? 39  THR A CA  1 
ATOM   316  C  C   . THR A 1 40  ? 29.208 5.857   18.383  1.00 22.93  ? 39  THR A C   1 
ATOM   317  O  O   . THR A 1 40  ? 30.073 5.113   17.922  1.00 22.99  ? 39  THR A O   1 
ATOM   318  C  CB  . THR A 1 40  ? 28.123 7.196   16.564  1.00 22.12  ? 39  THR A CB  1 
ATOM   319  O  OG1 . THR A 1 40  ? 28.520 8.416   17.210  1.00 21.24  ? 39  THR A OG1 1 
ATOM   320  C  CG2 . THR A 1 40  ? 26.868 7.424   15.751  1.00 20.86  ? 39  THR A CG2 1 
ATOM   321  N  N   . LEU A 1 41  ? 29.349 6.498   19.543  1.00 23.68  ? 40  LEU A N   1 
ATOM   322  C  CA  . LEU A 1 41  ? 30.572 6.385   20.345  1.00 24.19  ? 40  LEU A CA  1 
ATOM   323  C  C   . LEU A 1 41  ? 30.847 4.950   20.795  1.00 24.28  ? 40  LEU A C   1 
ATOM   324  O  O   . LEU A 1 41  ? 32.011 4.538   20.938  1.00 23.83  ? 40  LEU A O   1 
ATOM   325  C  CB  . LEU A 1 41  ? 30.499 7.330   21.554  1.00 25.26  ? 40  LEU A CB  1 
ATOM   326  C  CG  . LEU A 1 41  ? 31.720 7.466   22.478  1.00 25.40  ? 40  LEU A CG  1 
ATOM   327  C  CD1 . LEU A 1 41  ? 32.932 7.943   21.688  1.00 26.19  ? 40  LEU A CD1 1 
ATOM   328  C  CD2 . LEU A 1 41  ? 31.414 8.440   23.599  1.00 25.83  ? 40  LEU A CD2 1 
ATOM   329  N  N   . GLU A 1 42  ? 29.770 4.184   20.962  1.00 26.00  ? 41  GLU A N   1 
ATOM   330  C  CA  . GLU A 1 42  ? 29.857 2.786   21.382  1.00 24.55  ? 41  GLU A CA  1 
ATOM   331  C  C   . GLU A 1 42  ? 30.658 1.906   20.427  1.00 33.76  ? 41  GLU A C   1 
ATOM   332  O  O   . GLU A 1 42  ? 31.209 0.890   20.838  1.00 35.66  ? 41  GLU A O   1 
ATOM   333  C  CB  . GLU A 1 42  ? 28.461 2.190   21.522  1.00 33.39  ? 41  GLU A CB  1 
ATOM   334  C  CG  . GLU A 1 42  ? 27.648 2.725   22.678  1.00 55.70  ? 41  GLU A CG  1 
ATOM   335  C  CD  . GLU A 1 42  ? 26.298 2.048   22.772  1.00 67.02  ? 41  GLU A CD  1 
ATOM   336  O  OE1 . GLU A 1 42  ? 25.420 2.340   21.930  1.00 71.20  ? 41  GLU A OE1 1 
ATOM   337  O  OE2 . GLU A 1 42  ? 26.125 1.206   23.678  1.00 75.40  ? 41  GLU A OE2 1 
ATOM   338  N  N   . LYS A 1 43  ? 30.696 2.286   19.151  1.00 33.33  ? 42  LYS A N   1 
ATOM   339  C  CA  . LYS A 1 43  ? 31.421 1.522   18.136  1.00 25.60  ? 42  LYS A CA  1 
ATOM   340  C  C   . LYS A 1 43  ? 32.934 1.611   18.273  1.00 19.95  ? 42  LYS A C   1 
ATOM   341  O  O   . LYS A 1 43  ? 33.661 0.750   17.787  1.00 35.38  ? 42  LYS A O   1 
ATOM   342  C  CB  . LYS A 1 43  ? 31.007 1.987   16.739  1.00 17.82  ? 42  LYS A CB  1 
ATOM   343  C  CG  . LYS A 1 43  ? 29.599 1.623   16.363  1.00 19.30  ? 42  LYS A CG  1 
ATOM   344  C  CD  . LYS A 1 43  ? 29.501 0.142   16.074  1.00 28.08  ? 42  LYS A CD  1 
ATOM   345  C  CE  . LYS A 1 43  ? 28.079 -0.270  15.763  1.00 28.38  ? 42  LYS A CE  1 
ATOM   346  N  NZ  . LYS A 1 43  ? 28.051 -1.731  15.563  1.00 36.87  ? 42  LYS A NZ  1 
ATOM   347  N  N   . PHE A 1 44  ? 33.403 2.649   18.952  1.00 32.57  ? 43  PHE A N   1 
ATOM   348  C  CA  . PHE A 1 44  ? 34.832 2.864   19.120  1.00 32.86  ? 43  PHE A CA  1 
ATOM   349  C  C   . PHE A 1 44  ? 35.357 2.428   20.479  1.00 32.97  ? 43  PHE A C   1 
ATOM   350  O  O   . PHE A 1 44  ? 35.455 3.224   21.407  1.00 33.11  ? 43  PHE A O   1 
ATOM   351  C  CB  . PHE A 1 44  ? 35.153 4.340   18.865  1.00 32.29  ? 43  PHE A CB  1 
ATOM   352  C  CG  . PHE A 1 44  ? 34.782 4.803   17.490  1.00 32.34  ? 43  PHE A CG  1 
ATOM   353  C  CD1 . PHE A 1 44  ? 35.677 4.666   16.431  1.00 31.95  ? 43  PHE A CD1 1 
ATOM   354  C  CD2 . PHE A 1 44  ? 33.530 5.349   17.243  1.00 31.84  ? 43  PHE A CD2 1 
ATOM   355  C  CE1 . PHE A 1 44  ? 35.323 5.066   15.151  1.00 32.26  ? 43  PHE A CE1 1 
ATOM   356  C  CE2 . PHE A 1 44  ? 33.172 5.751   15.970  1.00 32.01  ? 43  PHE A CE2 1 
ATOM   357  C  CZ  . PHE A 1 44  ? 34.071 5.609   14.920  1.00 32.21  ? 43  PHE A CZ  1 
ATOM   358  N  N   . ASP A 1 45  ? 35.775 1.175   20.555  1.00 34.16  ? 44  ASP A N   1 
ATOM   359  C  CA  . ASP A 1 45  ? 36.281 0.599   21.794  1.00 41.63  ? 44  ASP A CA  1 
ATOM   360  C  C   . ASP A 1 45  ? 37.401 1.387   22.443  1.00 43.44  ? 44  ASP A C   1 
ATOM   361  O  O   . ASP A 1 45  ? 37.460 1.496   23.668  1.00 43.85  ? 44  ASP A O   1 
ATOM   362  C  CB  . ASP A 1 45  ? 36.725 -0.847  21.562  1.00 49.83  ? 44  ASP A CB  1 
ATOM   363  C  CG  . ASP A 1 45  ? 35.608 -1.713  20.999  1.00 66.28  ? 44  ASP A CG  1 
ATOM   364  O  OD1 . ASP A 1 45  ? 34.412 -1.418  21.258  1.00 59.23  ? 44  ASP A OD1 1 
ATOM   365  O  OD2 . ASP A 1 45  ? 35.929 -2.681  20.278  1.00 75.41  ? 44  ASP A OD2 1 
ATOM   366  N  N   . ARG A 1 46  ? 38.255 1.984   21.623  1.00 41.73  ? 45  ARG A N   1 
ATOM   367  C  CA  . ARG A 1 46  ? 39.378 2.737   22.144  1.00 41.45  ? 45  ARG A CA  1 
ATOM   368  C  C   . ARG A 1 46  ? 39.011 4.085   22.736  1.00 40.97  ? 45  ARG A C   1 
ATOM   369  O  O   . ARG A 1 46  ? 39.814 4.665   23.468  1.00 41.65  ? 45  ARG A O   1 
ATOM   370  C  CB  . ARG A 1 46  ? 40.441 2.938   21.053  1.00 43.13  ? 45  ARG A CB  1 
ATOM   371  C  CG  . ARG A 1 46  ? 41.785 2.307   21.396  1.00 53.08  ? 45  ARG A CG  1 
ATOM   372  C  CD  . ARG A 1 46  ? 42.910 2.709   20.435  1.00 64.99  ? 45  ARG A CD  1 
ATOM   373  N  NE  . ARG A 1 46  ? 42.767 2.098   19.118  1.00 80.05  ? 45  ARG A NE  1 
ATOM   374  C  CZ  . ARG A 1 46  ? 42.767 2.777   17.974  1.00 97.64  ? 45  ARG A CZ  1 
ATOM   375  N  NH1 . ARG A 1 46  ? 42.885 4.102   17.980  1.00 100.00 ? 45  ARG A NH1 1 
ATOM   376  N  NH2 . ARG A 1 46  ? 42.632 2.133   16.821  1.00 91.43  ? 45  ARG A NH2 1 
ATOM   377  N  N   . VAL A 1 47  ? 37.771 4.523   22.533  1.00 39.61  ? 46  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 47  ? 37.375 5.854   22.974  1.00 38.33  ? 46  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 47  ? 35.954 5.971   23.580  1.00 38.11  ? 46  VAL A C   1 
ATOM   380  O  O   . VAL A 1 47  ? 35.542 7.041   24.037  1.00 37.45  ? 46  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 47  ? 37.577 6.804   21.731  1.00 37.83  ? 46  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 47  ? 36.278 7.176   21.064  1.00 36.87  ? 46  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 47  ? 38.429 7.974   22.075  1.00 37.97  ? 46  VAL A CG2 1 
ATOM   384  N  N   . LYS A 1 48  ? 35.254 4.844   23.672  1.00 29.21  ? 47  LYS A N   1 
ATOM   385  C  CA  . LYS A 1 48  ? 33.882 4.813   24.172  1.00 23.48  ? 47  LYS A CA  1 
ATOM   386  C  C   . LYS A 1 48  ? 33.669 5.225   25.628  1.00 24.52  ? 47  LYS A C   1 
ATOM   387  O  O   . LYS A 1 48  ? 32.547 5.503   26.027  1.00 33.62  ? 47  LYS A O   1 
ATOM   388  C  CB  . LYS A 1 48  ? 33.280 3.426   23.946  1.00 23.59  ? 47  LYS A CB  1 
ATOM   389  C  CG  . LYS A 1 48  ? 33.623 2.411   25.019  1.00 40.22  ? 47  LYS A CG  1 
ATOM   390  C  CD  . LYS A 1 48  ? 32.863 1.109   24.831  1.00 52.55  ? 47  LYS A CD  1 
ATOM   391  C  CE  . LYS A 1 48  ? 33.774 0.036   24.272  1.00 62.41  ? 47  LYS A CE  1 
ATOM   392  N  NZ  . LYS A 1 48  ? 33.077 -1.260  24.087  1.00 74.01  ? 47  LYS A NZ  1 
ATOM   393  N  N   . HIS A 1 49  ? 34.741 5.249   26.413  1.00 31.16  ? 48  HIS A N   1 
ATOM   394  C  CA  . HIS A 1 49  ? 34.674 5.606   27.836  1.00 31.22  ? 48  HIS A CA  1 
ATOM   395  C  C   . HIS A 1 49  ? 34.701 7.112   28.107  1.00 30.83  ? 48  HIS A C   1 
ATOM   396  O  O   . HIS A 1 49  ? 34.532 7.529   29.249  1.00 31.04  ? 48  HIS A O   1 
ATOM   397  C  CB  . HIS A 1 49  ? 35.838 4.955   28.589  1.00 33.26  ? 48  HIS A CB  1 
ATOM   398  C  CG  . HIS A 1 49  ? 37.177 5.474   28.169  1.00 43.81  ? 48  HIS A CG  1 
ATOM   399  N  ND1 . HIS A 1 49  ? 37.694 5.329   26.897  1.00 49.90  ? 48  HIS A ND1 1 
ATOM   400  C  CD2 . HIS A 1 49  ? 38.087 6.210   28.857  1.00 46.44  ? 48  HIS A CD2 1 
ATOM   401  C  CE1 . HIS A 1 49  ? 38.876 5.973   26.846  1.00 53.26  ? 48  HIS A CE1 1 
ATOM   402  N  NE2 . HIS A 1 49  ? 39.163 6.526   28.010  1.00 56.20  ? 48  HIS A NE2 1 
ATOM   403  N  N   . LEU A 1 50  ? 35.003 7.911   27.083  1.00 30.17  ? 49  LEU A N   1 
ATOM   404  C  CA  . LEU A 1 50  ? 35.045 9.375   27.217  1.00 29.27  ? 49  LEU A CA  1 
ATOM   405  C  C   . LEU A 1 50  ? 33.637 9.891   27.507  1.00 28.58  ? 49  LEU A C   1 
ATOM   406  O  O   . LEU A 1 50  ? 32.695 9.606   26.782  1.00 28.38  ? 49  LEU A O   1 
ATOM   407  C  CB  . LEU A 1 50  ? 35.611 10.026  25.952  1.00 29.06  ? 49  LEU A CB  1 
ATOM   408  C  CG  . LEU A 1 50  ? 36.958 9.519   25.428  1.00 28.57  ? 49  LEU A CG  1 
ATOM   409  C  CD1 . LEU A 1 50  ? 37.293 10.245  24.158  1.00 28.23  ? 49  LEU A CD1 1 
ATOM   410  C  CD2 . LEU A 1 50  ? 38.053 9.730   26.445  1.00 28.89  ? 49  LEU A CD2 1 
ATOM   411  N  N   . LYS A 1 51  ? 33.515 10.640  28.595  1.00 24.55  ? 50  LYS A N   1 
ATOM   412  C  CA  . LYS A 1 51  ? 32.237 11.165  29.068  1.00 29.94  ? 50  LYS A CA  1 
ATOM   413  C  C   . LYS A 1 51  ? 31.906 12.604  28.683  1.00 23.26  ? 50  LYS A C   1 
ATOM   414  O  O   . LYS A 1 51  ? 30.742 12.950  28.517  1.00 34.91  ? 50  LYS A O   1 
ATOM   415  C  CB  . LYS A 1 51  ? 32.182 11.034  30.592  1.00 45.14  ? 50  LYS A CB  1 
ATOM   416  C  CG  . LYS A 1 51  ? 32.451 9.622   31.126  1.00 30.35  ? 50  LYS A CG  1 
ATOM   417  C  CD  . LYS A 1 51  ? 32.844 9.674   32.606  1.00 57.96  ? 50  LYS A CD  1 
ATOM   418  C  CE  . LYS A 1 51  ? 32.941 8.289   33.243  1.00 49.95  ? 50  LYS A CE  1 
ATOM   419  N  NZ  . LYS A 1 51  ? 31.612 7.630   33.359  1.00 51.06  ? 50  LYS A NZ  1 
ATOM   420  N  N   . THR A 1 52  ? 32.924 13.448  28.564  1.00 24.12  ? 51  THR A N   1 
ATOM   421  C  CA  . THR A 1 52  ? 32.694 14.849  28.229  1.00 23.89  ? 51  THR A CA  1 
ATOM   422  C  C   . THR A 1 52  ? 33.500 15.330  27.025  1.00 23.81  ? 51  THR A C   1 
ATOM   423  O  O   . THR A 1 52  ? 34.497 14.712  26.638  1.00 23.34  ? 51  THR A O   1 
ATOM   424  C  CB  . THR A 1 52  ? 33.052 15.780  29.435  1.00 24.11  ? 51  THR A CB  1 
ATOM   425  O  OG1 . THR A 1 52  ? 34.460 15.699  29.704  1.00 24.05  ? 51  THR A OG1 1 
ATOM   426  C  CG2 . THR A 1 52  ? 32.269 15.384  30.695  1.00 24.04  ? 51  THR A CG2 1 
ATOM   427  N  N   . GLU A 1 53  ? 33.098 16.483  26.495  1.00 19.92  ? 52  GLU A N   1 
ATOM   428  C  CA  . GLU A 1 53  ? 33.783 17.091  25.373  1.00 23.72  ? 52  GLU A CA  1 
ATOM   429  C  C   . GLU A 1 53  ? 35.220 17.425  25.737  1.00 23.12  ? 52  GLU A C   1 
ATOM   430  O  O   . GLU A 1 53  ? 36.100 17.350  24.887  1.00 25.70  ? 52  GLU A O   1 
ATOM   431  C  CB  . GLU A 1 53  ? 33.071 18.360  24.919  1.00 28.42  ? 52  GLU A CB  1 
ATOM   432  C  CG  . GLU A 1 53  ? 33.779 19.038  23.744  1.00 41.68  ? 52  GLU A CG  1 
ATOM   433  C  CD  . GLU A 1 53  ? 32.971 20.161  23.115  1.00 38.60  ? 52  GLU A CD  1 
ATOM   434  O  OE1 . GLU A 1 53  ? 31.764 20.277  23.415  1.00 41.28  ? 52  GLU A OE1 1 
ATOM   435  O  OE2 . GLU A 1 53  ? 33.542 20.922  22.307  1.00 49.31  ? 52  GLU A OE2 1 
ATOM   436  N  N   . ALA A 1 54  ? 35.454 17.798  26.997  1.00 21.99  ? 53  ALA A N   1 
ATOM   437  C  CA  . ALA A 1 54  ? 36.800 18.129  27.454  1.00 21.32  ? 53  ALA A CA  1 
ATOM   438  C  C   . ALA A 1 54  ? 37.678 16.893  27.382  1.00 21.17  ? 53  ALA A C   1 
ATOM   439  O  O   . ALA A 1 54  ? 38.845 16.975  27.014  1.00 20.69  ? 53  ALA A O   1 
ATOM   440  C  CB  . ALA A 1 54  ? 36.765 18.670  28.881  1.00 22.00  ? 53  ALA A CB  1 
ATOM   441  N  N   . GLU A 1 55  ? 37.114 15.745  27.747  1.00 18.34  ? 54  GLU A N   1 
ATOM   442  C  CA  . GLU A 1 55  ? 37.860 14.489  27.694  1.00 20.60  ? 54  GLU A CA  1 
ATOM   443  C  C   . GLU A 1 55  ? 38.137 14.149  26.245  1.00 22.25  ? 54  GLU A C   1 
ATOM   444  O  O   . GLU A 1 55  ? 39.231 13.717  25.892  1.00 19.44  ? 54  GLU A O   1 
ATOM   445  C  CB  . GLU A 1 55  ? 37.079 13.365  28.371  1.00 18.48  ? 54  GLU A CB  1 
ATOM   446  C  CG  . GLU A 1 55  ? 37.087 13.500  29.882  1.00 27.00  ? 54  GLU A CG  1 
ATOM   447  C  CD  . GLU A 1 55  ? 36.458 12.334  30.616  1.00 30.63  ? 54  GLU A CD  1 
ATOM   448  O  OE1 . GLU A 1 55  ? 35.749 11.528  29.990  1.00 34.98  ? 54  GLU A OE1 1 
ATOM   449  O  OE2 . GLU A 1 55  ? 36.673 12.226  31.840  1.00 38.33  ? 54  GLU A OE2 1 
ATOM   450  N  N   . MET A 1 56  ? 37.151 14.420  25.398  1.00 22.52  ? 55  MET A N   1 
ATOM   451  C  CA  . MET A 1 56  ? 37.272 14.165  23.970  1.00 22.24  ? 55  MET A CA  1 
ATOM   452  C  C   . MET A 1 56  ? 38.367 15.021  23.334  1.00 22.17  ? 55  MET A C   1 
ATOM   453  O  O   . MET A 1 56  ? 39.210 14.508  22.593  1.00 21.68  ? 55  MET A O   1 
ATOM   454  C  CB  . MET A 1 56  ? 35.937 14.411  23.293  1.00 21.93  ? 55  MET A CB  1 
ATOM   455  C  CG  . MET A 1 56  ? 34.971 13.294  23.521  1.00 22.76  ? 55  MET A CG  1 
ATOM   456  S  SD  . MET A 1 56  ? 33.389 13.680  22.839  1.00 25.74  ? 55  MET A SD  1 
ATOM   457  C  CE  . MET A 1 56  ? 32.348 12.662  23.891  1.00 25.19  ? 55  MET A CE  1 
ATOM   458  N  N   . LYS A 1 57  ? 38.397 16.302  23.700  1.00 18.45  ? 56  LYS A N   1 
ATOM   459  C  CA  . LYS A 1 57  ? 39.378 17.240  23.171  1.00 22.71  ? 56  LYS A CA  1 
ATOM   460  C  C   . LYS A 1 57  ? 40.781 16.919  23.590  1.00 23.43  ? 56  LYS A C   1 
ATOM   461  O  O   . LYS A 1 57  ? 41.720 17.320  22.920  1.00 29.40  ? 56  LYS A O   1 
ATOM   462  C  CB  . LYS A 1 57  ? 39.070 18.667  23.607  1.00 13.80  ? 56  LYS A CB  1 
ATOM   463  C  CG  . LYS A 1 57  ? 37.920 19.299  22.854  1.00 30.70  ? 56  LYS A CG  1 
ATOM   464  C  CD  . LYS A 1 57  ? 37.687 20.715  23.319  1.00 42.22  ? 56  LYS A CD  1 
ATOM   465  C  CE  . LYS A 1 57  ? 36.574 21.345  22.523  1.00 54.44  ? 56  LYS A CE  1 
ATOM   466  N  NZ  . LYS A 1 57  ? 36.199 22.686  23.043  1.00 94.11  ? 56  LYS A NZ  1 
ATOM   467  N  N   . ALA A 1 58  ? 40.926 16.212  24.706  1.00 24.17  ? 57  ALA A N   1 
ATOM   468  C  CA  . ALA A 1 58  ? 42.245 15.870  25.207  1.00 24.10  ? 57  ALA A CA  1 
ATOM   469  C  C   . ALA A 1 58  ? 42.712 14.501  24.759  1.00 24.17  ? 57  ALA A C   1 
ATOM   470  O  O   . ALA A 1 58  ? 43.892 14.178  24.861  1.00 24.80  ? 57  ALA A O   1 
ATOM   471  C  CB  . ALA A 1 58  ? 42.263 15.956  26.717  1.00 24.26  ? 57  ALA A CB  1 
ATOM   472  N  N   . SER A 1 59  ? 41.791 13.705  24.233  1.00 24.05  ? 58  SER A N   1 
ATOM   473  C  CA  . SER A 1 59  ? 42.106 12.360  23.794  1.00 23.68  ? 58  SER A CA  1 
ATOM   474  C  C   . SER A 1 59  ? 43.023 12.299  22.565  1.00 24.43  ? 58  SER A C   1 
ATOM   475  O  O   . SER A 1 59  ? 42.718 12.859  21.509  1.00 24.53  ? 58  SER A O   1 
ATOM   476  C  CB  . SER A 1 59  ? 40.813 11.598  23.535  1.00 23.20  ? 58  SER A CB  1 
ATOM   477  O  OG  . SER A 1 59  ? 41.107 10.316  23.022  1.00 23.93  ? 58  SER A OG  1 
ATOM   478  N  N   . GLU A 1 60  ? 44.156 11.618  22.716  1.00 25.17  ? 59  GLU A N   1 
ATOM   479  C  CA  . GLU A 1 60  ? 45.110 11.468  21.630  1.00 24.69  ? 59  GLU A CA  1 
ATOM   480  C  C   . GLU A 1 60  ? 44.585 10.444  20.637  1.00 26.92  ? 59  GLU A C   1 
ATOM   481  O  O   . GLU A 1 60  ? 44.823 10.556  19.445  1.00 27.57  ? 59  GLU A O   1 
ATOM   482  C  CB  . GLU A 1 60  ? 46.472 11.027  22.172  1.00 33.92  ? 59  GLU A CB  1 
ATOM   483  C  CG  . GLU A 1 60  ? 47.664 11.638  21.445  1.00 62.87  ? 59  GLU A CG  1 
ATOM   484  C  CD  . GLU A 1 60  ? 47.721 13.156  21.577  1.00 74.28  ? 59  GLU A CD  1 
ATOM   485  O  OE1 . GLU A 1 60  ? 47.188 13.705  22.568  1.00 87.47  ? 59  GLU A OE1 1 
ATOM   486  O  OE2 . GLU A 1 60  ? 48.308 13.806  20.687  1.00 76.06  ? 59  GLU A OE2 1 
ATOM   487  N  N   . ASP A 1 61  ? 43.867 9.442   21.134  1.00 22.66  ? 60  ASP A N   1 
ATOM   488  C  CA  . ASP A 1 61  ? 43.300 8.420   20.267  1.00 22.16  ? 60  ASP A CA  1 
ATOM   489  C  C   . ASP A 1 61  ? 42.200 9.002   19.389  1.00 20.24  ? 60  ASP A C   1 
ATOM   490  O  O   . ASP A 1 61  ? 42.070 8.629   18.222  1.00 19.35  ? 60  ASP A O   1 
ATOM   491  C  CB  . ASP A 1 61  ? 42.712 7.267   21.079  1.00 26.97  ? 60  ASP A CB  1 
ATOM   492  C  CG  . ASP A 1 61  ? 43.761 6.267   21.538  1.00 42.59  ? 60  ASP A CG  1 
ATOM   493  O  OD1 . ASP A 1 61  ? 44.819 6.131   20.876  1.00 46.70  ? 60  ASP A OD1 1 
ATOM   494  O  OD2 . ASP A 1 61  ? 43.504 5.602   22.563  1.00 48.78  ? 60  ASP A OD2 1 
ATOM   495  N  N   . LEU A 1 62  ? 41.395 9.898   19.948  1.00 18.12  ? 61  LEU A N   1 
ATOM   496  C  CA  . LEU A 1 62  ? 40.315 10.489  19.167  1.00 18.57  ? 61  LEU A CA  1 
ATOM   497  C  C   . LEU A 1 62  ? 40.906 11.316  18.024  1.00 18.43  ? 61  LEU A C   1 
ATOM   498  O  O   . LEU A 1 62  ? 40.434 11.243  16.889  1.00 18.14  ? 61  LEU A O   1 
ATOM   499  C  CB  . LEU A 1 62  ? 39.399 11.328  20.057  1.00 18.74  ? 61  LEU A CB  1 
ATOM   500  C  CG  . LEU A 1 62  ? 38.104 11.870  19.443  1.00 19.52  ? 61  LEU A CG  1 
ATOM   501  C  CD1 . LEU A 1 62  ? 37.023 11.951  20.503  1.00 19.62  ? 61  LEU A CD1 1 
ATOM   502  C  CD2 . LEU A 1 62  ? 38.343 13.244  18.821  1.00 19.57  ? 61  LEU A CD2 1 
ATOM   503  N  N   . LYS A 1 63  ? 41.992 12.027  18.313  1.00 14.10  ? 62  LYS A N   1 
ATOM   504  C  CA  . LYS A 1 63  ? 42.651 12.861  17.310  1.00 25.17  ? 62  LYS A CA  1 
ATOM   505  C  C   . LYS A 1 63  ? 43.225 12.008  16.175  1.00 19.47  ? 62  LYS A C   1 
ATOM   506  O  O   . LYS A 1 63  ? 43.117 12.381  15.008  1.00 20.51  ? 62  LYS A O   1 
ATOM   507  C  CB  . LYS A 1 63  ? 43.738 13.726  17.957  1.00 36.01  ? 62  LYS A CB  1 
ATOM   508  C  CG  . LYS A 1 63  ? 44.388 14.716  17.002  1.00 30.67  ? 62  LYS A CG  1 
ATOM   509  C  CD  . LYS A 1 63  ? 45.100 15.820  17.763  1.00 57.97  ? 62  LYS A CD  1 
ATOM   510  C  CE  . LYS A 1 63  ? 46.325 15.302  18.477  1.00 60.47  ? 62  LYS A CE  1 
ATOM   511  N  NZ  . LYS A 1 63  ? 46.959 16.349  19.326  1.00 95.13  ? 62  LYS A NZ  1 
ATOM   512  N  N   . LYS A 1 64  ? 43.827 10.868  16.520  1.00 15.72  ? 63  LYS A N   1 
ATOM   513  C  CA  . LYS A 1 64  ? 44.365 9.952   15.510  1.00 17.84  ? 63  LYS A CA  1 
ATOM   514  C  C   . LYS A 1 64  ? 43.220 9.405   14.638  1.00 16.64  ? 63  LYS A C   1 
ATOM   515  O  O   . LYS A 1 64  ? 43.347 9.344   13.420  1.00 22.11  ? 63  LYS A O   1 
ATOM   516  C  CB  . LYS A 1 64  ? 45.139 8.796   16.161  1.00 18.47  ? 63  LYS A CB  1 
ATOM   517  C  CG  . LYS A 1 64  ? 46.337 9.278   16.971  1.00 43.82  ? 63  LYS A CG  1 
ATOM   518  C  CD  . LYS A 1 64  ? 47.565 8.412   16.751  1.00 79.73  ? 63  LYS A CD  1 
ATOM   519  C  CE  . LYS A 1 64  ? 47.522 7.129   17.559  1.00 64.33  ? 63  LYS A CE  1 
ATOM   520  N  NZ  . LYS A 1 64  ? 47.697 7.392   19.011  1.00 81.18  ? 63  LYS A NZ  1 
ATOM   521  N  N   . HIS A 1 65  ? 42.102 9.040   15.260  1.00 16.01  ? 64  HIS A N   1 
ATOM   522  C  CA  . HIS A 1 65  ? 40.944 8.537   14.530  1.00 16.67  ? 64  HIS A CA  1 
ATOM   523  C  C   . HIS A 1 65  ? 40.443 9.582   13.535  1.00 17.00  ? 64  HIS A C   1 
ATOM   524  O  O   . HIS A 1 65  ? 40.003 9.245   12.441  1.00 16.92  ? 64  HIS A O   1 
ATOM   525  C  CB  . HIS A 1 65  ? 39.799 8.244   15.501  1.00 18.21  ? 64  HIS A CB  1 
ATOM   526  C  CG  . HIS A 1 65  ? 40.000 7.019   16.337  1.00 30.05  ? 64  HIS A CG  1 
ATOM   527  N  ND1 . HIS A 1 65  ? 39.083 6.654   17.294  1.00 35.15  ? 64  HIS A ND1 1 
ATOM   528  C  CD2 . HIS A 1 65  ? 40.923 6.033   16.204  1.00 34.21  ? 64  HIS A CD2 1 
ATOM   529  C  CE1 . HIS A 1 65  ? 39.458 5.462   17.709  1.00 36.97  ? 64  HIS A CE1 1 
ATOM   530  N  NE2 . HIS A 1 65  ? 40.566 5.045   17.079  1.00 38.23  ? 64  HIS A NE2 1 
ATOM   531  N  N   . GLY A 1 66  ? 40.433 10.842  13.969  1.00 16.46  ? 65  GLY A N   1 
ATOM   532  C  CA  . GLY A 1 66  ? 39.978 11.919  13.114  1.00 15.97  ? 65  GLY A CA  1 
ATOM   533  C  C   . GLY A 1 66  ? 40.872 12.059  11.892  1.00 15.92  ? 65  GLY A C   1 
ATOM   534  O  O   . GLY A 1 66  ? 40.372 12.239  10.788  1.00 15.66  ? 65  GLY A O   1 
ATOM   535  N  N   . VAL A 1 67  ? 42.187 11.997  12.087  1.00 15.57  ? 66  VAL A N   1 
ATOM   536  C  CA  . VAL A 1 67  ? 43.121 12.112  10.973  1.00 15.88  ? 66  VAL A CA  1 
ATOM   537  C  C   . VAL A 1 67  ? 42.898 10.960  9.979   1.00 16.30  ? 66  VAL A C   1 
ATOM   538  O  O   . VAL A 1 67  ? 42.860 11.178  8.771   1.00 16.82  ? 66  VAL A O   1 
ATOM   539  C  CB  . VAL A 1 67  ? 44.599 12.114  11.473  1.00 16.69  ? 66  VAL A CB  1 
ATOM   540  C  CG1 . VAL A 1 67  ? 45.577 11.864  10.302  1.00 15.99  ? 66  VAL A CG1 1 
ATOM   541  C  CG2 . VAL A 1 67  ? 44.929 13.452  12.140  1.00 15.60  ? 66  VAL A CG2 1 
ATOM   542  N  N   . THR A 1 68  ? 42.703 9.748   10.497  1.00 16.38  ? 67  THR A N   1 
ATOM   543  C  CA  . THR A 1 68  ? 42.479 8.562   9.666   1.00 16.57  ? 67  THR A CA  1 
ATOM   544  C  C   . THR A 1 68  ? 41.226 8.663   8.791   1.00 16.36  ? 67  THR A C   1 
ATOM   545  O  O   . THR A 1 68  ? 41.277 8.380   7.593   1.00 16.00  ? 67  THR A O   1 
ATOM   546  C  CB  . THR A 1 68  ? 42.405 7.293   10.545  1.00 16.87  ? 67  THR A CB  1 
ATOM   547  O  OG1 . THR A 1 68  ? 43.641 7.151   11.255  1.00 18.58  ? 67  THR A OG1 1 
ATOM   548  C  CG2 . THR A 1 68  ? 42.163 6.048   9.699   1.00 16.58  ? 67  THR A CG2 1 
ATOM   549  N  N   . VAL A 1 69  ? 40.107 9.072   9.383   1.00 16.09  ? 68  VAL A N   1 
ATOM   550  C  CA  . VAL A 1 69  ? 38.866 9.207   8.628   1.00 16.32  ? 68  VAL A CA  1 
ATOM   551  C  C   . VAL A 1 69  ? 38.986 10.263  7.531   1.00 15.35  ? 68  VAL A C   1 
ATOM   552  O  O   . VAL A 1 69  ? 38.536 10.046  6.420   1.00 14.58  ? 68  VAL A O   1 
ATOM   553  C  CB  . VAL A 1 69  ? 37.665 9.643   9.519   1.00 17.46  ? 68  VAL A CB  1 
ATOM   554  C  CG1 . VAL A 1 69  ? 36.378 9.662   8.695   1.00 18.23  ? 68  VAL A CG1 1 
ATOM   555  C  CG2 . VAL A 1 69  ? 37.495 8.717   10.660  1.00 19.48  ? 68  VAL A CG2 1 
ATOM   556  N  N   . LEU A 1 70  ? 39.529 11.431  7.874   1.00 14.71  ? 69  LEU A N   1 
ATOM   557  C  CA  . LEU A 1 70  ? 39.654 12.522  6.907   1.00 14.96  ? 69  LEU A CA  1 
ATOM   558  C  C   . LEU A 1 70  ? 40.646 12.233  5.800   1.00 14.27  ? 69  LEU A C   1 
ATOM   559  O  O   . LEU A 1 70  ? 40.445 12.656  4.669   1.00 14.38  ? 69  LEU A O   1 
ATOM   560  C  CB  . LEU A 1 70  ? 39.998 13.850  7.581   1.00 14.82  ? 69  LEU A CB  1 
ATOM   561  C  CG  . LEU A 1 70  ? 38.924 14.450  8.497   1.00 17.52  ? 69  LEU A CG  1 
ATOM   562  C  CD1 . LEU A 1 70  ? 39.251 15.935  8.752   1.00 16.43  ? 69  LEU A CD1 1 
ATOM   563  C  CD2 . LEU A 1 70  ? 37.543 14.324  7.863   1.00 18.33  ? 69  LEU A CD2 1 
ATOM   564  N  N   . THR A 1 71  ? 41.720 11.529  6.128   1.00 13.87  ? 70  THR A N   1 
ATOM   565  C  CA  . THR A 1 71  ? 42.713 11.167  5.120   1.00 14.57  ? 70  THR A CA  1 
ATOM   566  C  C   . THR A 1 71  ? 42.090 10.168  4.107   1.00 14.49  ? 70  THR A C   1 
ATOM   567  O  O   . THR A 1 71  ? 42.221 10.350  2.900   1.00 14.32  ? 70  THR A O   1 
ATOM   568  C  CB  . THR A 1 71  ? 43.987 10.568  5.784   1.00 15.27  ? 70  THR A CB  1 
ATOM   569  O  OG1 . THR A 1 71  ? 44.553 11.546  6.660   1.00 15.83  ? 70  THR A OG1 1 
ATOM   570  C  CG2 . THR A 1 71  ? 45.032 10.185  4.733   1.00 15.63  ? 70  THR A CG2 1 
ATOM   571  N  N   . ALA A 1 72  ? 41.373 9.154   4.598   1.00 13.91  ? 71  ALA A N   1 
ATOM   572  C  CA  . ALA A 1 72  ? 40.723 8.185   3.707   1.00 13.99  ? 71  ALA A CA  1 
ATOM   573  C  C   . ALA A 1 72  ? 39.624 8.870   2.885   1.00 13.64  ? 71  ALA A C   1 
ATOM   574  O  O   . ALA A 1 72  ? 39.512 8.641   1.686   1.00 13.91  ? 71  ALA A O   1 
ATOM   575  C  CB  . ALA A 1 72  ? 40.120 7.012   4.509   1.00 12.95  ? 71  ALA A CB  1 
ATOM   576  N  N   . LEU A 1 73  ? 38.832 9.734   3.517   1.00 13.67  ? 72  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 73  ? 37.762 10.433  2.812   1.00 13.56  ? 72  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 73  ? 38.342 11.348  1.756   1.00 13.74  ? 72  LEU A C   1 
ATOM   579  O  O   . LEU A 1 73  ? 37.851 11.380  0.633   1.00 13.66  ? 72  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 73  ? 36.866 11.226  3.772   1.00 13.74  ? 72  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 73  ? 35.719 12.004  3.093   1.00 14.92  ? 72  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 73  ? 34.791 11.045  2.310   1.00 15.38  ? 72  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 73  ? 34.929 12.829  4.128   1.00 14.89  ? 72  LEU A CD2 1 
ATOM   584  N  N   . GLY A 1 74  ? 39.400 12.070  2.109   1.00 13.67  ? 73  GLY A N   1 
ATOM   585  C  CA  . GLY A 1 74  ? 40.041 12.954  1.151   1.00 14.46  ? 73  GLY A CA  1 
ATOM   586  C  C   . GLY A 1 74  ? 40.567 12.204  -0.077  1.00 14.58  ? 73  GLY A C   1 
ATOM   587  O  O   . GLY A 1 74  ? 40.436 12.672  -1.205  1.00 14.49  ? 73  GLY A O   1 
ATOM   588  N  N   . ALA A 1 75  ? 41.148 11.030  0.141   1.00 14.74  ? 74  ALA A N   1 
ATOM   589  C  CA  . ALA A 1 75  ? 41.682 10.233  -0.967  1.00 15.76  ? 74  ALA A CA  1 
ATOM   590  C  C   . ALA A 1 75  ? 40.538 9.840   -1.920  1.00 15.76  ? 74  ALA A C   1 
ATOM   591  O  O   . ALA A 1 75  ? 40.685 9.855   -3.145  1.00 16.76  ? 74  ALA A O   1 
ATOM   592  C  CB  . ALA A 1 75  ? 42.388 9.006   -0.424  1.00 14.49  ? 74  ALA A CB  1 
ATOM   593  N  N   . ILE A 1 76  ? 39.377 9.565   -1.346  1.00 15.77  ? 75  ILE A N   1 
ATOM   594  C  CA  . ILE A 1 76  ? 38.201 9.198   -2.121  1.00 15.47  ? 75  ILE A CA  1 
ATOM   595  C  C   . ILE A 1 76  ? 37.675 10.400  -2.919  1.00 15.48  ? 75  ILE A C   1 
ATOM   596  O  O   . ILE A 1 76  ? 37.423 10.285  -4.112  1.00 15.82  ? 75  ILE A O   1 
ATOM   597  C  CB  . ILE A 1 76  ? 37.102 8.619   -1.183  1.00 15.70  ? 75  ILE A CB  1 
ATOM   598  C  CG1 . ILE A 1 76  ? 37.531 7.225   -0.698  1.00 16.61  ? 75  ILE A CG1 1 
ATOM   599  C  CG2 . ILE A 1 76  ? 35.762 8.545   -1.889  1.00 15.10  ? 75  ILE A CG2 1 
ATOM   600  C  CD1 . ILE A 1 76  ? 36.747 6.718   0.506   1.00 18.63  ? 75  ILE A CD1 1 
ATOM   601  N  N   . LEU A 1 77  ? 37.545 11.556  -2.277  1.00 15.31  ? 76  LEU A N   1 
ATOM   602  C  CA  . LEU A 1 77  ? 37.043 12.747  -2.960  1.00 15.33  ? 76  LEU A CA  1 
ATOM   603  C  C   . LEU A 1 77  ? 37.938 13.174  -4.129  1.00 15.59  ? 76  LEU A C   1 
ATOM   604  O  O   . LEU A 1 77  ? 37.455 13.603  -5.184  1.00 15.95  ? 76  LEU A O   1 
ATOM   605  C  CB  . LEU A 1 77  ? 36.881 13.902  -1.967  1.00 15.64  ? 76  LEU A CB  1 
ATOM   606  C  CG  . LEU A 1 77  ? 35.798 13.730  -0.892  1.00 15.76  ? 76  LEU A CG  1 
ATOM   607  C  CD1 . LEU A 1 77  ? 35.865 14.909  0.091   1.00 16.66  ? 76  LEU A CD1 1 
ATOM   608  C  CD2 . LEU A 1 77  ? 34.400 13.596  -1.515  1.00 15.59  ? 76  LEU A CD2 1 
ATOM   609  N  N   . LYS A 1 78  ? 39.246 13.049  -3.939  1.00 10.96  ? 77  LYS A N   1 
ATOM   610  C  CA  . LYS A 1 78  ? 40.200 13.416  -4.971  1.00 13.75  ? 77  LYS A CA  1 
ATOM   611  C  C   . LYS A 1 78  ? 40.129 12.553  -6.234  1.00 18.30  ? 77  LYS A C   1 
ATOM   612  O  O   . LYS A 1 78  ? 40.689 12.927  -7.257  1.00 18.04  ? 77  LYS A O   1 
ATOM   613  C  CB  . LYS A 1 78  ? 41.607 13.447  -4.396  1.00 14.38  ? 77  LYS A CB  1 
ATOM   614  C  CG  . LYS A 1 78  ? 41.799 14.594  -3.398  1.00 17.01  ? 77  LYS A CG  1 
ATOM   615  C  CD  . LYS A 1 78  ? 43.112 14.448  -2.663  1.00 16.79  ? 77  LYS A CD  1 
ATOM   616  C  CE  . LYS A 1 78  ? 43.349 15.610  -1.763  1.00 20.59  ? 77  LYS A CE  1 
ATOM   617  N  NZ  . LYS A 1 78  ? 44.698 15.538  -1.169  1.00 20.09  ? 77  LYS A NZ  1 
ATOM   618  N  N   . LYS A 1 79  ? 39.450 11.406  -6.151  1.00 15.24  ? 78  LYS A N   1 
ATOM   619  C  CA  . LYS A 1 79  ? 39.256 10.513  -7.302  1.00 18.28  ? 78  LYS A CA  1 
ATOM   620  C  C   . LYS A 1 79  ? 38.107 11.011  -8.180  1.00 18.94  ? 78  LYS A C   1 
ATOM   621  O  O   . LYS A 1 79  ? 37.901 10.506  -9.282  1.00 19.00  ? 78  LYS A O   1 
ATOM   622  C  CB  . LYS A 1 79  ? 38.948 9.074   -6.855  1.00 12.31  ? 78  LYS A CB  1 
ATOM   623  C  CG  . LYS A 1 79  ? 40.058 8.402   -6.058  1.00 25.64  ? 78  LYS A CG  1 
ATOM   624  C  CD  . LYS A 1 79  ? 41.390 8.455   -6.784  1.00 27.27  ? 78  LYS A CD  1 
ATOM   625  C  CE  . LYS A 1 79  ? 41.373 7.630   -8.053  1.00 32.49  ? 78  LYS A CE  1 
ATOM   626  N  NZ  . LYS A 1 79  ? 41.223 6.175   -7.763  1.00 55.16  ? 78  LYS A NZ  1 
ATOM   627  N  N   . LYS A 1 80  ? 37.322 11.952  -7.656  1.00 15.11  ? 79  LYS A N   1 
ATOM   628  C  CA  . LYS A 1 80  ? 36.200 12.535  -8.398  1.00 14.03  ? 79  LYS A CA  1 
ATOM   629  C  C   . LYS A 1 80  ? 35.218 11.516  -8.985  1.00 17.50  ? 79  LYS A C   1 
ATOM   630  O  O   . LYS A 1 80  ? 34.814 11.616  -10.145 1.00 20.85  ? 79  LYS A O   1 
ATOM   631  C  CB  . LYS A 1 80  ? 36.732 13.474  -9.488  1.00 12.58  ? 79  LYS A CB  1 
ATOM   632  C  CG  . LYS A 1 80  ? 37.537 14.629  -8.915  1.00 15.77  ? 79  LYS A CG  1 
ATOM   633  C  CD  . LYS A 1 80  ? 38.464 15.266  -9.921  1.00 26.30  ? 79  LYS A CD  1 
ATOM   634  C  CE  . LYS A 1 80  ? 37.734 15.964  -11.026 1.00 37.31  ? 79  LYS A CE  1 
ATOM   635  N  NZ  . LYS A 1 80  ? 38.682 16.840  -11.792 1.00 31.02  ? 79  LYS A NZ  1 
ATOM   636  N  N   . GLY A 1 81  ? 34.828 10.543  -8.165  1.00 17.74  ? 80  GLY A N   1 
ATOM   637  C  CA  . GLY A 1 81  ? 33.877 9.538   -8.600  1.00 17.93  ? 80  GLY A CA  1 
ATOM   638  C  C   . GLY A 1 81  ? 34.472 8.216   -9.068  1.00 18.43  ? 80  GLY A C   1 
ATOM   639  O  O   . GLY A 1 81  ? 33.737 7.232   -9.162  1.00 19.23  ? 80  GLY A O   1 
ATOM   640  N  N   . HIS A 1 82  ? 35.772 8.178   -9.369  1.00 17.70  ? 81  HIS A N   1 
ATOM   641  C  CA  . HIS A 1 82  ? 36.424 6.948   -9.830  1.00 17.96  ? 81  HIS A CA  1 
ATOM   642  C  C   . HIS A 1 82  ? 37.072 6.331   -8.609  1.00 18.07  ? 81  HIS A C   1 
ATOM   643  O  O   . HIS A 1 82  ? 38.284 6.169   -8.555  1.00 18.07  ? 81  HIS A O   1 
ATOM   644  C  CB  . HIS A 1 82  ? 37.488 7.302   -10.869 1.00 17.33  ? 81  HIS A CB  1 
ATOM   645  C  CG  . HIS A 1 82  ? 36.923 7.926   -12.108 1.00 21.80  ? 81  HIS A CG  1 
ATOM   646  N  ND1 . HIS A 1 82  ? 36.884 9.285   -12.346 1.00 29.19  ? 81  HIS A ND1 1 
ATOM   647  C  CD2 . HIS A 1 82  ? 36.331 7.349   -13.183 1.00 20.31  ? 81  HIS A CD2 1 
ATOM   648  C  CE1 . HIS A 1 82  ? 36.285 9.484   -13.529 1.00 23.50  ? 81  HIS A CE1 1 
ATOM   649  N  NE2 . HIS A 1 82  ? 35.932 8.338   -14.077 1.00 31.00  ? 81  HIS A NE2 1 
ATOM   650  N  N   . HIS A 1 83  ? 36.249 5.908   -7.659  1.00 18.15  ? 82  HIS A N   1 
ATOM   651  C  CA  . HIS A 1 83  ? 36.763 5.425   -6.381  1.00 18.12  ? 82  HIS A CA  1 
ATOM   652  C  C   . HIS A 1 83  ? 36.469 3.977   -6.004  1.00 18.26  ? 82  HIS A C   1 
ATOM   653  O  O   . HIS A 1 83  ? 36.597 3.597   -4.836  1.00 17.89  ? 82  HIS A O   1 
ATOM   654  C  CB  . HIS A 1 83  ? 36.205 6.348   -5.294  1.00 16.77  ? 82  HIS A CB  1 
ATOM   655  C  CG  . HIS A 1 83  ? 34.711 6.441   -5.314  1.00 15.19  ? 82  HIS A CG  1 
ATOM   656  N  ND1 . HIS A 1 83  ? 34.007 7.614   -5.167  1.00 16.60  ? 82  HIS A ND1 1 
ATOM   657  C  CD2 . HIS A 1 83  ? 33.779 5.477   -5.529  1.00 16.77  ? 82  HIS A CD2 1 
ATOM   658  C  CE1 . HIS A 1 83  ? 32.699 7.331   -5.300  1.00 20.03  ? 82  HIS A CE1 1 
ATOM   659  N  NE2 . HIS A 1 83  ? 32.515 6.043   -5.521  1.00 21.22  ? 82  HIS A NE2 1 
ATOM   660  N  N   . GLU A 1 84  ? 36.022 3.194   -6.972  1.00 19.59  ? 83  GLU A N   1 
ATOM   661  C  CA  . GLU A 1 84  ? 35.699 1.797   -6.737  1.00 24.12  ? 83  GLU A CA  1 
ATOM   662  C  C   . GLU A 1 84  ? 36.800 1.024   -5.987  1.00 31.10  ? 83  GLU A C   1 
ATOM   663  O  O   . GLU A 1 84  ? 36.516 0.307   -5.030  1.00 26.88  ? 83  GLU A O   1 
ATOM   664  C  CB  . GLU A 1 84  ? 35.340 1.110   -8.066  1.00 36.52  ? 83  GLU A CB  1 
ATOM   665  C  CG  . GLU A 1 84  ? 36.267 1.451   -9.260  1.00 68.75  ? 83  GLU A CG  1 
ATOM   666  C  CD  . GLU A 1 84  ? 36.009 2.830   -9.890  1.00 69.80  ? 83  GLU A CD  1 
ATOM   667  O  OE1 . GLU A 1 84  ? 34.877 3.359   -9.777  1.00 67.91  ? 83  GLU A OE1 1 
ATOM   668  O  OE2 . GLU A 1 84  ? 36.949 3.385   -10.503 1.00 42.41  ? 83  GLU A OE2 1 
ATOM   669  N  N   . ALA A 1 85  ? 38.055 1.213   -6.380  1.00 25.65  ? 84  ALA A N   1 
ATOM   670  C  CA  . ALA A 1 85  ? 39.162 0.519   -5.732  1.00 25.65  ? 84  ALA A CA  1 
ATOM   671  C  C   . ALA A 1 85  ? 39.333 0.911   -4.272  1.00 25.52  ? 84  ALA A C   1 
ATOM   672  O  O   . ALA A 1 85  ? 39.651 0.067   -3.441  1.00 24.98  ? 84  ALA A O   1 
ATOM   673  C  CB  . ALA A 1 85  ? 40.457 0.761   -6.482  1.00 25.75  ? 84  ALA A CB  1 
ATOM   674  N  N   . GLU A 1 86  ? 39.158 2.197   -3.977  1.00 23.55  ? 85  GLU A N   1 
ATOM   675  C  CA  . GLU A 1 86  ? 39.296 2.714   -2.615  1.00 24.29  ? 85  GLU A CA  1 
ATOM   676  C  C   . GLU A 1 86  ? 38.138 2.293   -1.712  1.00 20.43  ? 85  GLU A C   1 
ATOM   677  O  O   . GLU A 1 86  ? 38.310 2.139   -0.505  1.00 22.47  ? 85  GLU A O   1 
ATOM   678  C  CB  . GLU A 1 86  ? 39.400 4.247   -2.620  1.00 27.01  ? 85  GLU A CB  1 
ATOM   679  C  CG  . GLU A 1 86  ? 40.721 4.830   -3.148  1.00 24.94  ? 85  GLU A CG  1 
ATOM   680  C  CD  . GLU A 1 86  ? 40.884 4.748   -4.668  1.00 36.11  ? 85  GLU A CD  1 
ATOM   681  O  OE1 . GLU A 1 86  ? 39.887 4.578   -5.409  1.00 37.64  ? 85  GLU A OE1 1 
ATOM   682  O  OE2 . GLU A 1 86  ? 42.034 4.872   -5.131  1.00 54.23  ? 85  GLU A OE2 1 
ATOM   683  N  N   . LEU A 1 87  ? 36.973 2.083   -2.310  1.00 21.53  ? 86  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 87  ? 35.787 1.702   -1.567  1.00 22.37  ? 86  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 87  ? 35.717 0.249   -1.105  1.00 22.19  ? 86  LEU A C   1 
ATOM   686  O  O   . LEU A 1 87  ? 35.101 -0.046  -0.087  1.00 22.24  ? 86  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 87  ? 34.534 2.016   -2.390  1.00 23.56  ? 86  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 87  ? 33.610 3.127   -1.892  1.00 25.46  ? 86  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 87  ? 34.361 4.444   -1.730  1.00 26.00  ? 86  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 87  ? 32.480 3.286   -2.891  1.00 26.41  ? 86  LEU A CD2 1 
ATOM   691  N  N   . LYS A 1 88  ? 36.321 -0.663  -1.854  1.00 21.96  ? 87  LYS A N   1 
ATOM   692  C  CA  . LYS A 1 88  ? 36.268 -2.081  -1.510  1.00 30.39  ? 87  LYS A CA  1 
ATOM   693  C  C   . LYS A 1 88  ? 36.767 -2.472  -0.118  1.00 23.62  ? 87  LYS A C   1 
ATOM   694  O  O   . LYS A 1 88  ? 36.003 -3.037  0.668   1.00 20.01  ? 87  LYS A O   1 
ATOM   695  C  CB  . LYS A 1 88  ? 36.927 -2.916  -2.610  1.00 31.09  ? 87  LYS A CB  1 
ATOM   696  C  CG  . LYS A 1 88  ? 36.128 -2.843  -3.882  1.00 42.74  ? 87  LYS A CG  1 
ATOM   697  C  CD  . LYS A 1 88  ? 36.898 -3.289  -5.102  1.00 56.03  ? 87  LYS A CD  1 
ATOM   698  C  CE  . LYS A 1 88  ? 36.889 -4.783  -5.250  1.00 45.89  ? 87  LYS A CE  1 
ATOM   699  N  NZ  . LYS A 1 88  ? 37.070 -5.172  -6.680  1.00 56.90  ? 87  LYS A NZ  1 
ATOM   700  N  N   . PRO A 1 89  ? 38.035 -2.155  0.219   1.00 19.60  ? 88  PRO A N   1 
ATOM   701  C  CA  . PRO A 1 89  ? 38.532 -2.521  1.549   1.00 19.38  ? 88  PRO A CA  1 
ATOM   702  C  C   . PRO A 1 89  ? 37.775 -1.793  2.658   1.00 19.80  ? 88  PRO A C   1 
ATOM   703  O  O   . PRO A 1 89  ? 37.606 -2.324  3.758   1.00 19.67  ? 88  PRO A O   1 
ATOM   704  C  CB  . PRO A 1 89  ? 39.992 -2.080  1.495   1.00 19.32  ? 88  PRO A CB  1 
ATOM   705  C  CG  . PRO A 1 89  ? 39.967 -0.918  0.532   1.00 18.97  ? 88  PRO A CG  1 
ATOM   706  C  CD  . PRO A 1 89  ? 39.085 -1.462  -0.553  1.00 19.16  ? 88  PRO A CD  1 
ATOM   707  N  N   . LEU A 1 90  ? 37.318 -0.580  2.345   1.00 19.25  ? 89  LEU A N   1 
ATOM   708  C  CA  . LEU A 1 90  ? 36.583 0.254   3.280   1.00 19.30  ? 89  LEU A CA  1 
ATOM   709  C  C   . LEU A 1 90  ? 35.218 -0.349  3.610   1.00 18.74  ? 89  LEU A C   1 
ATOM   710  O  O   . LEU A 1 90  ? 34.814 -0.405  4.769   1.00 17.93  ? 89  LEU A O   1 
ATOM   711  C  CB  . LEU A 1 90  ? 36.372 1.625   2.653   1.00 21.41  ? 89  LEU A CB  1 
ATOM   712  C  CG  . LEU A 1 90  ? 36.099 2.774   3.608   1.00 23.97  ? 89  LEU A CG  1 
ATOM   713  C  CD1 . LEU A 1 90  ? 37.351 2.949   4.488   1.00 25.15  ? 89  LEU A CD1 1 
ATOM   714  C  CD2 . LEU A 1 90  ? 35.817 4.050   2.803   1.00 25.28  ? 89  LEU A CD2 1 
ATOM   715  N  N   . ALA A 1 91  ? 34.508 -0.786  2.577   1.00 17.83  ? 90  ALA A N   1 
ATOM   716  C  CA  . ALA A 1 91  ? 33.192 -1.367  2.745   1.00 17.79  ? 90  ALA A CA  1 
ATOM   717  C  C   . ALA A 1 91  ? 33.278 -2.687  3.518   1.00 17.79  ? 90  ALA A C   1 
ATOM   718  O  O   . ALA A 1 91  ? 32.428 -2.990  4.355   1.00 17.57  ? 90  ALA A O   1 
ATOM   719  C  CB  . ALA A 1 91  ? 32.557 -1.585  1.375   1.00 18.05  ? 90  ALA A CB  1 
ATOM   720  N  N   . GLN A 1 92  ? 34.328 -3.459  3.250   1.00 17.80  ? 91  GLN A N   1 
ATOM   721  C  CA  . GLN A 1 92  ? 34.500 -4.730  3.927   1.00 17.64  ? 91  GLN A CA  1 
ATOM   722  C  C   . GLN A 1 92  ? 34.746 -4.568  5.411   1.00 17.96  ? 91  GLN A C   1 
ATOM   723  O  O   . GLN A 1 92  ? 34.133 -5.271  6.221   1.00 18.32  ? 91  GLN A O   1 
ATOM   724  C  CB  . GLN A 1 92  ? 35.631 -5.558  3.314   1.00 17.05  ? 91  GLN A CB  1 
ATOM   725  C  CG  . GLN A 1 92  ? 35.748 -6.914  3.996   1.00 17.69  ? 91  GLN A CG  1 
ATOM   726  C  CD  . GLN A 1 92  ? 36.726 -7.845  3.320   1.00 20.82  ? 91  GLN A CD  1 
ATOM   727  O  OE1 . GLN A 1 92  ? 37.821 -7.446  2.950   1.00 21.27  ? 91  GLN A OE1 1 
ATOM   728  N  NE2 . GLN A 1 92  ? 36.334 -9.106  3.171   1.00 14.83  ? 91  GLN A NE2 1 
ATOM   729  N  N   . SER A 1 93  ? 35.650 -3.671  5.792   1.00 17.63  ? 92  SER A N   1 
ATOM   730  C  CA  . SER A 1 93  ? 35.897 -3.509  7.213   1.00 17.93  ? 92  SER A CA  1 
ATOM   731  C  C   . SER A 1 93  ? 34.698 -2.906  7.964   1.00 18.26  ? 92  SER A C   1 
ATOM   732  O  O   . SER A 1 93  ? 34.383 -3.345  9.072   1.00 18.48  ? 92  SER A O   1 
ATOM   733  C  CB  . SER A 1 93  ? 37.194 -2.742  7.481   1.00 17.83  ? 92  SER A CB  1 
ATOM   734  O  OG  . SER A 1 93  ? 37.106 -1.411  7.053   1.00 19.43  ? 92  SER A OG  1 
ATOM   735  N  N   . HIS A 1 94  ? 33.977 -1.965  7.357   1.00 17.80  ? 93  HIS A N   1 
ATOM   736  C  CA  . HIS A 1 94  ? 32.830 -1.391  8.053   1.00 18.32  ? 93  HIS A CA  1 
ATOM   737  C  C   . HIS A 1 94  ? 31.605 -2.282  8.092   1.00 19.08  ? 93  HIS A C   1 
ATOM   738  O  O   . HIS A 1 94  ? 30.800 -2.170  9.008   1.00 19.46  ? 93  HIS A O   1 
ATOM   739  C  CB  . HIS A 1 94  ? 32.471 -0.025  7.495   1.00 18.59  ? 93  HIS A CB  1 
ATOM   740  C  CG  . HIS A 1 94  ? 33.484 1.016   7.821   1.00 17.57  ? 93  HIS A CG  1 
ATOM   741  N  ND1 . HIS A 1 94  ? 34.771 0.972   7.333   1.00 24.61  ? 93  HIS A ND1 1 
ATOM   742  C  CD2 . HIS A 1 94  ? 33.431 2.086   8.645   1.00 20.34  ? 93  HIS A CD2 1 
ATOM   743  C  CE1 . HIS A 1 94  ? 35.468 1.971   7.840   1.00 24.73  ? 93  HIS A CE1 1 
ATOM   744  N  NE2 . HIS A 1 94  ? 34.677 2.662   8.641   1.00 23.04  ? 93  HIS A NE2 1 
ATOM   745  N  N   . ALA A 1 95  ? 31.466 -3.159  7.103   1.00 19.39  ? 94  ALA A N   1 
ATOM   746  C  CA  . ALA A 1 95  ? 30.336 -4.073  7.035   1.00 20.34  ? 94  ALA A CA  1 
ATOM   747  C  C   . ALA A 1 95  ? 30.571 -5.311  7.893   1.00 21.10  ? 94  ALA A C   1 
ATOM   748  O  O   . ALA A 1 95  ? 29.773 -5.619  8.771   1.00 21.89  ? 94  ALA A O   1 
ATOM   749  C  CB  . ALA A 1 95  ? 30.087 -4.497  5.597   1.00 20.13  ? 94  ALA A CB  1 
ATOM   750  N  N   . THR A 1 96  ? 31.723 -5.944  7.702   1.00 21.61  ? 95  THR A N   1 
ATOM   751  C  CA  . THR A 1 96  ? 32.072 -7.190  8.386   1.00 22.02  ? 95  THR A CA  1 
ATOM   752  C  C   . THR A 1 96  ? 32.761 -7.073  9.742   1.00 22.53  ? 95  THR A C   1 
ATOM   753  O  O   . THR A 1 96  ? 32.418 -7.798  10.669  1.00 23.24  ? 95  THR A O   1 
ATOM   754  C  CB  . THR A 1 96  ? 32.954 -8.061  7.466   1.00 22.32  ? 95  THR A CB  1 
ATOM   755  O  OG1 . THR A 1 96  ? 32.448 -7.974  6.131   1.00 21.73  ? 95  THR A OG1 1 
ATOM   756  C  CG2 . THR A 1 96  ? 32.952 -9.541  7.916   1.00 21.45  ? 95  THR A CG2 1 
ATOM   757  N  N   . LYS A 1 97  ? 33.761 -6.211  9.859   1.00 21.64  ? 96  LYS A N   1 
ATOM   758  C  CA  . LYS A 1 97  ? 34.454 -6.079  11.130  1.00 26.88  ? 96  LYS A CA  1 
ATOM   759  C  C   . LYS A 1 97  ? 33.743 -5.153  12.129  1.00 31.86  ? 96  LYS A C   1 
ATOM   760  O  O   . LYS A 1 97  ? 33.320 -5.591  13.197  1.00 36.78  ? 96  LYS A O   1 
ATOM   761  C  CB  . LYS A 1 97  ? 35.888 -5.612  10.898  1.00 28.79  ? 96  LYS A CB  1 
ATOM   762  C  CG  . LYS A 1 97  ? 36.850 -6.013  12.015  1.00 35.57  ? 96  LYS A CG  1 
ATOM   763  C  CD  . LYS A 1 97  ? 38.165 -5.271  11.876  1.00 55.25  ? 96  LYS A CD  1 
ATOM   764  C  CE  . LYS A 1 97  ? 39.330 -6.051  12.456  1.00 80.34  ? 96  LYS A CE  1 
ATOM   765  N  NZ  . LYS A 1 97  ? 39.794 -7.114  11.517  1.00 90.60  ? 96  LYS A NZ  1 
ATOM   766  N  N   . HIS A 1 98  ? 33.578 -3.888  11.755  1.00 32.04  ? 97  HIS A N   1 
ATOM   767  C  CA  . HIS A 1 98  ? 32.960 -2.882  12.619  1.00 32.23  ? 97  HIS A CA  1 
ATOM   768  C  C   . HIS A 1 98  ? 31.424 -2.860  12.656  1.00 32.70  ? 97  HIS A C   1 
ATOM   769  O  O   . HIS A 1 98  ? 30.851 -2.412  13.653  1.00 33.29  ? 97  HIS A O   1 
ATOM   770  C  CB  . HIS A 1 98  ? 33.467 -1.491  12.230  1.00 31.70  ? 97  HIS A CB  1 
ATOM   771  C  CG  . HIS A 1 98  ? 34.923 -1.448  11.869  1.00 33.74  ? 97  HIS A CG  1 
ATOM   772  N  ND1 . HIS A 1 98  ? 35.924 -2.049  12.601  1.00 32.24  ? 97  HIS A ND1 1 
ATOM   773  C  CD2 . HIS A 1 98  ? 35.548 -0.834  10.830  1.00 33.36  ? 97  HIS A CD2 1 
ATOM   774  C  CE1 . HIS A 1 98  ? 37.104 -1.781  12.004  1.00 28.00  ? 97  HIS A CE1 1 
ATOM   775  N  NE2 . HIS A 1 98  ? 36.932 -1.044  10.923  1.00 33.21  ? 97  HIS A NE2 1 
ATOM   776  N  N   . LYS A 1 99  ? 30.768 -3.316  11.581  1.00 30.50  ? 98  LYS A N   1 
ATOM   777  C  CA  . LYS A 1 99  ? 29.296 -3.331  11.474  1.00 23.13  ? 98  LYS A CA  1 
ATOM   778  C  C   . LYS A 1 99  ? 28.686 -1.951  11.683  1.00 32.58  ? 98  LYS A C   1 
ATOM   779  O  O   . LYS A 1 99  ? 27.986 -1.708  12.659  1.00 26.86  ? 98  LYS A O   1 
ATOM   780  C  CB  . LYS A 1 99  ? 28.678 -4.327  12.447  1.00 27.87  ? 98  LYS A CB  1 
ATOM   781  C  CG  . LYS A 1 99  ? 28.118 -5.559  11.760  1.00 67.51  ? 98  LYS A CG  1 
ATOM   782  C  CD  . LYS A 1 99  ? 28.648 -6.835  12.384  1.00 60.67  ? 98  LYS A CD  1 
ATOM   783  C  CE  . LYS A 1 99  ? 30.163 -6.879  12.311  1.00 73.97  ? 98  LYS A CE  1 
ATOM   784  N  NZ  . LYS A 1 99  ? 30.711 -8.157  12.837  1.00 83.45  ? 98  LYS A NZ  1 
ATOM   785  N  N   . ILE A 1 100 ? 28.905 -1.074  10.712  1.00 21.99  ? 99  ILE A N   1 
ATOM   786  C  CA  . ILE A 1 100 ? 28.442 0.291   10.773  1.00 21.17  ? 99  ILE A CA  1 
ATOM   787  C  C   . ILE A 1 100 ? 27.270 0.460   9.842   1.00 21.88  ? 99  ILE A C   1 
ATOM   788  O  O   . ILE A 1 100 ? 27.426 0.358   8.624   1.00 22.43  ? 99  ILE A O   1 
ATOM   789  C  CB  . ILE A 1 100 ? 29.561 1.257   10.300  1.00 20.50  ? 99  ILE A CB  1 
ATOM   790  C  CG1 . ILE A 1 100 ? 30.873 0.961   11.034  1.00 20.26  ? 99  ILE A CG1 1 
ATOM   791  C  CG2 . ILE A 1 100 ? 29.107 2.712   10.435  1.00 19.71  ? 99  ILE A CG2 1 
ATOM   792  C  CD1 . ILE A 1 100 ? 30.785 0.967   12.536  1.00 20.31  ? 99  ILE A CD1 1 
ATOM   793  N  N   . PRO A 1 101 ? 26.078 0.743   10.391  1.00 22.07  ? 100 PRO A N   1 
ATOM   794  C  CA  . PRO A 1 101 ? 24.920 0.922   9.510   1.00 22.57  ? 100 PRO A CA  1 
ATOM   795  C  C   . PRO A 1 101 ? 25.006 2.221   8.682   1.00 23.19  ? 100 PRO A C   1 
ATOM   796  O  O   . PRO A 1 101 ? 25.618 3.208   9.103   1.00 22.81  ? 100 PRO A O   1 
ATOM   797  C  CB  . PRO A 1 101 ? 23.738 0.925   10.494  1.00 22.51  ? 100 PRO A CB  1 
ATOM   798  C  CG  . PRO A 1 101 ? 24.332 1.438   11.753  1.00 22.22  ? 100 PRO A CG  1 
ATOM   799  C  CD  . PRO A 1 101 ? 25.681 0.764   11.810  1.00 21.66  ? 100 PRO A CD  1 
ATOM   800  N  N   . ILE A 1 102 ? 24.423 2.196   7.488   1.00 23.79  ? 101 ILE A N   1 
ATOM   801  C  CA  . ILE A 1 102 ? 24.424 3.358   6.599   1.00 24.96  ? 101 ILE A CA  1 
ATOM   802  C  C   . ILE A 1 102 ? 24.008 4.622   7.337   1.00 25.16  ? 101 ILE A C   1 
ATOM   803  O  O   . ILE A 1 102 ? 24.564 5.687   7.102   1.00 25.83  ? 101 ILE A O   1 
ATOM   804  C  CB  . ILE A 1 102 ? 23.487 3.124   5.362   1.00 25.80  ? 101 ILE A CB  1 
ATOM   805  C  CG1 . ILE A 1 102 ? 24.053 2.005   4.471   1.00 26.54  ? 101 ILE A CG1 1 
ATOM   806  C  CG2 . ILE A 1 102 ? 23.274 4.405   4.571   1.00 26.60  ? 101 ILE A CG2 1 
ATOM   807  C  CD1 . ILE A 1 102 ? 25.472 2.260   3.962   1.00 27.17  ? 101 ILE A CD1 1 
ATOM   808  N  N   . LYS A 1 103 ? 23.025 4.490   8.222   1.00 21.86  ? 102 LYS A N   1 
ATOM   809  C  CA  . LYS A 1 103 ? 22.502 5.598   9.034   1.00 20.48  ? 102 LYS A CA  1 
ATOM   810  C  C   . LYS A 1 103 ? 23.627 6.382   9.736   1.00 17.82  ? 102 LYS A C   1 
ATOM   811  O  O   . LYS A 1 103 ? 23.554 7.603   9.864   1.00 18.65  ? 102 LYS A O   1 
ATOM   812  C  CB  . LYS A 1 103 ? 21.533 5.024   10.082  1.00 26.50  ? 102 LYS A CB  1 
ATOM   813  C  CG  . LYS A 1 103 ? 20.949 6.017   11.042  1.00 49.26  ? 102 LYS A CG  1 
ATOM   814  C  CD  . LYS A 1 103 ? 19.785 6.806   10.436  1.00 72.73  ? 102 LYS A CD  1 
ATOM   815  C  CE  . LYS A 1 103 ? 18.800 7.307   11.515  1.00 95.55  ? 102 LYS A CE  1 
ATOM   816  N  NZ  . LYS A 1 103 ? 17.820 8.291   11.055  1.00 82.64  ? 102 LYS A NZ  1 
ATOM   817  N  N   . TYR A 1 104 ? 24.650 5.676   10.212  1.00 16.72  ? 103 TYR A N   1 
ATOM   818  C  CA  . TYR A 1 104 ? 25.770 6.334   10.882  1.00 16.88  ? 103 TYR A CA  1 
ATOM   819  C  C   . TYR A 1 104 ? 26.633 7.116   9.892   1.00 16.39  ? 103 TYR A C   1 
ATOM   820  O  O   . TYR A 1 104 ? 27.285 8.086   10.272  1.00 16.20  ? 103 TYR A O   1 
ATOM   821  C  CB  . TYR A 1 104 ? 26.632 5.325   11.640  1.00 16.57  ? 103 TYR A CB  1 
ATOM   822  C  CG  . TYR A 1 104 ? 26.030 4.762   12.921  1.00 17.87  ? 103 TYR A CG  1 
ATOM   823  C  CD1 . TYR A 1 104 ? 24.699 4.981   13.261  1.00 18.98  ? 103 TYR A CD1 1 
ATOM   824  C  CD2 . TYR A 1 104 ? 26.801 3.979   13.772  1.00 18.35  ? 103 TYR A CD2 1 
ATOM   825  C  CE1 . TYR A 1 104 ? 24.154 4.420   14.429  1.00 20.22  ? 103 TYR A CE1 1 
ATOM   826  C  CE2 . TYR A 1 104 ? 26.278 3.418   14.922  1.00 19.76  ? 103 TYR A CE2 1 
ATOM   827  C  CZ  . TYR A 1 104 ? 24.964 3.636   15.245  1.00 20.94  ? 103 TYR A CZ  1 
ATOM   828  O  OH  . TYR A 1 104 ? 24.462 3.049   16.379  1.00 22.91  ? 103 TYR A OH  1 
ATOM   829  N  N   . LEU A 1 105 ? 26.675 6.663   8.637   1.00 16.33  ? 104 LEU A N   1 
ATOM   830  C  CA  . LEU A 1 105 ? 27.444 7.353   7.598   1.00 15.99  ? 104 LEU A CA  1 
ATOM   831  C  C   . LEU A 1 105 ? 26.701 8.648   7.254   1.00 15.96  ? 104 LEU A C   1 
ATOM   832  O  O   . LEU A 1 105 ? 27.323 9.662   6.922   1.00 15.10  ? 104 LEU A O   1 
ATOM   833  C  CB  . LEU A 1 105 ? 27.647 6.465   6.369   1.00 16.49  ? 104 LEU A CB  1 
ATOM   834  C  CG  . LEU A 1 105 ? 28.432 5.162   6.632   1.00 17.26  ? 104 LEU A CG  1 
ATOM   835  C  CD1 . LEU A 1 105 ? 28.544 4.350   5.344   1.00 18.13  ? 104 LEU A CD1 1 
ATOM   836  C  CD2 . LEU A 1 105 ? 29.811 5.451   7.185   1.00 16.64  ? 104 LEU A CD2 1 
ATOM   837  N  N   . GLU A 1 106 ? 25.373 8.623   7.359   1.00 11.84  ? 105 GLU A N   1 
ATOM   838  C  CA  . GLU A 1 106 ? 24.583 9.832   7.142   1.00 16.11  ? 105 GLU A CA  1 
ATOM   839  C  C   . GLU A 1 106 ? 24.880 10.814  8.294   1.00 15.21  ? 105 GLU A C   1 
ATOM   840  O  O   . GLU A 1 106 ? 25.044 12.013  8.066   1.00 15.53  ? 105 GLU A O   1 
ATOM   841  C  CB  . GLU A 1 106 ? 23.096 9.507   7.144   1.00 15.95  ? 105 GLU A CB  1 
ATOM   842  C  CG  . GLU A 1 106 ? 22.609 8.830   5.879   1.00 30.07  ? 105 GLU A CG  1 
ATOM   843  C  CD  . GLU A 1 106 ? 21.179 8.312   5.980   1.00 39.99  ? 105 GLU A CD  1 
ATOM   844  O  OE1 . GLU A 1 106 ? 20.511 8.546   6.946   1.00 37.58  ? 105 GLU A OE1 1 
ATOM   845  O  OE2 . GLU A 1 106 ? 20.751 7.619   5.044   1.00 41.07  ? 105 GLU A OE2 1 
ATOM   846  N  N   . PHE A 1 107 ? 24.962 10.292  9.523   1.00 15.05  ? 106 PHE A N   1 
ATOM   847  C  CA  . PHE A 1 107 ? 25.255 11.114  10.696  1.00 15.17  ? 106 PHE A CA  1 
ATOM   848  C  C   . PHE A 1 107 ? 26.614 11.810  10.592  1.00 14.86  ? 106 PHE A C   1 
ATOM   849  O  O   . PHE A 1 107 ? 26.725 12.979  10.954  1.00 14.34  ? 106 PHE A O   1 
ATOM   850  C  CB  . PHE A 1 107 ? 25.234 10.287  11.985  1.00 16.09  ? 106 PHE A CB  1 
ATOM   851  C  CG  . PHE A 1 107 ? 23.864 9.765   12.376  1.00 17.81  ? 106 PHE A CG  1 
ATOM   852  C  CD1 . PHE A 1 107 ? 22.710 10.224  11.754  1.00 18.00  ? 106 PHE A CD1 1 
ATOM   853  C  CD2 . PHE A 1 107 ? 23.739 8.826   13.396  1.00 17.99  ? 106 PHE A CD2 1 
ATOM   854  C  CE1 . PHE A 1 107 ? 21.459 9.757   12.147  1.00 18.79  ? 106 PHE A CE1 1 
ATOM   855  C  CE2 . PHE A 1 107 ? 22.487 8.360   13.790  1.00 18.31  ? 106 PHE A CE2 1 
ATOM   856  C  CZ  . PHE A 1 107 ? 21.357 8.827   13.166  1.00 18.23  ? 106 PHE A CZ  1 
ATOM   857  N  N   . ILE A 1 108 ? 27.648 11.092  10.149  1.00 14.34  ? 107 ILE A N   1 
ATOM   858  C  CA  . ILE A 1 108 ? 28.968 11.707  10.027  1.00 14.48  ? 107 ILE A CA  1 
ATOM   859  C  C   . ILE A 1 108 ? 28.984 12.711  8.863   1.00 15.05  ? 107 ILE A C   1 
ATOM   860  O  O   . ILE A 1 108 ? 29.715 13.709  8.907   1.00 15.26  ? 107 ILE A O   1 
ATOM   861  C  CB  . ILE A 1 108 ? 30.134 10.663  9.904   1.00 14.62  ? 107 ILE A CB  1 
ATOM   862  C  CG1 . ILE A 1 108 ? 31.483 11.353  10.220  1.00 14.37  ? 107 ILE A CG1 1 
ATOM   863  C  CG2 . ILE A 1 108 ? 30.164 10.034  8.505   1.00 13.15  ? 107 ILE A CG2 1 
ATOM   864  C  CD1 . ILE A 1 108 ? 32.676 10.403  10.336  1.00 14.25  ? 107 ILE A CD1 1 
ATOM   865  N  N   . SER A 1 109 ? 28.159 12.460  7.842   1.00 15.26  ? 108 SER A N   1 
ATOM   866  C  CA  . SER A 1 109 ? 28.047 13.363  6.693   1.00 15.68  ? 108 SER A CA  1 
ATOM   867  C  C   . SER A 1 109 ? 27.545 14.710  7.184   1.00 15.90  ? 108 SER A C   1 
ATOM   868  O  O   . SER A 1 109 ? 28.077 15.757  6.805   1.00 16.25  ? 108 SER A O   1 
ATOM   869  C  CB  . SER A 1 109 ? 27.082 12.802  5.652   1.00 15.50  ? 108 SER A CB  1 
ATOM   870  O  OG  . SER A 1 109 ? 27.672 11.680  5.004   1.00 17.49  ? 108 SER A OG  1 
ATOM   871  N  N   . GLU A 1 110 ? 26.527 14.660  8.044   1.00 17.48  ? 109 GLU A N   1 
ATOM   872  C  CA  . GLU A 1 110 ? 25.931 15.835  8.659   1.00 19.02  ? 109 GLU A CA  1 
ATOM   873  C  C   . GLU A 1 110 ? 26.971 16.580  9.497   1.00 9.86   ? 109 GLU A C   1 
ATOM   874  O  O   . GLU A 1 110 ? 27.023 17.810  9.482   1.00 10.23  ? 109 GLU A O   1 
ATOM   875  C  CB  . GLU A 1 110 ? 24.769 15.399  9.554   1.00 17.30  ? 109 GLU A CB  1 
ATOM   876  C  CG  . GLU A 1 110 ? 24.105 16.524  10.329  1.00 35.11  ? 109 GLU A CG  1 
ATOM   877  C  CD  . GLU A 1 110 ? 23.070 16.017  11.339  1.00 74.83  ? 109 GLU A CD  1 
ATOM   878  O  OE1 . GLU A 1 110 ? 23.176 14.858  11.820  1.00 60.11  ? 109 GLU A OE1 1 
ATOM   879  O  OE2 . GLU A 1 110 ? 22.145 16.795  11.664  1.00 88.99  ? 109 GLU A OE2 1 
ATOM   880  N  N   . ALA A 1 111 ? 27.790 15.836  10.231  1.00 11.06  ? 110 ALA A N   1 
ATOM   881  C  CA  . ALA A 1 111 ? 28.823 16.443  11.075  1.00 12.23  ? 110 ALA A CA  1 
ATOM   882  C  C   . ALA A 1 111 ? 29.872 17.166  10.216  1.00 12.35  ? 110 ALA A C   1 
ATOM   883  O  O   . ALA A 1 111 ? 30.348 18.255  10.580  1.00 13.15  ? 110 ALA A O   1 
ATOM   884  C  CB  . ALA A 1 111 ? 29.494 15.379  11.961  1.00 11.22  ? 110 ALA A CB  1 
ATOM   885  N  N   . ILE A 1 112 ? 30.210 16.571  9.071   1.00 11.96  ? 111 ILE A N   1 
ATOM   886  C  CA  . ILE A 1 112 ? 31.192 17.159  8.161   1.00 12.38  ? 111 ILE A CA  1 
ATOM   887  C  C   . ILE A 1 112 ? 30.672 18.484  7.591   1.00 12.69  ? 111 ILE A C   1 
ATOM   888  O  O   . ILE A 1 112 ? 31.343 19.516  7.658   1.00 12.48  ? 111 ILE A O   1 
ATOM   889  C  CB  . ILE A 1 112 ? 31.555 16.179  7.013   1.00 12.70  ? 111 ILE A CB  1 
ATOM   890  C  CG1 . ILE A 1 112 ? 32.413 15.038  7.574   1.00 12.53  ? 111 ILE A CG1 1 
ATOM   891  C  CG2 . ILE A 1 112 ? 32.315 16.930  5.885   1.00 11.83  ? 111 ILE A CG2 1 
ATOM   892  C  CD1 . ILE A 1 112 ? 32.451 13.805  6.706   1.00 13.30  ? 111 ILE A CD1 1 
ATOM   893  N  N   . ILE A 1 113 ? 29.443 18.457  7.105   1.00 13.31  ? 112 ILE A N   1 
ATOM   894  C  CA  . ILE A 1 113 ? 28.832 19.645  6.544   1.00 14.91  ? 112 ILE A CA  1 
ATOM   895  C  C   . ILE A 1 113 ? 28.716 20.761  7.590   1.00 15.30  ? 112 ILE A C   1 
ATOM   896  O  O   . ILE A 1 113 ? 28.997 21.930  7.286   1.00 15.30  ? 112 ILE A O   1 
ATOM   897  C  CB  . ILE A 1 113 ? 27.467 19.295  5.938   1.00 15.57  ? 112 ILE A CB  1 
ATOM   898  C  CG1 . ILE A 1 113 ? 27.686 18.453  4.680   1.00 15.70  ? 112 ILE A CG1 1 
ATOM   899  C  CG2 . ILE A 1 113 ? 26.644 20.576  5.645   1.00 16.14  ? 112 ILE A CG2 1 
ATOM   900  C  CD1 . ILE A 1 113 ? 26.396 17.872  4.128   1.00 18.03  ? 112 ILE A CD1 1 
ATOM   901  N  N   . HIS A 1 114 ? 28.366 20.386  8.825   1.00 14.97  ? 113 HIS A N   1 
ATOM   902  C  CA  . HIS A 1 114 ? 28.230 21.342  9.908   1.00 15.13  ? 113 HIS A CA  1 
ATOM   903  C  C   . HIS A 1 114 ? 29.552 22.034  10.221  1.00 15.44  ? 113 HIS A C   1 
ATOM   904  O  O   . HIS A 1 114 ? 29.598 23.249  10.435  1.00 15.64  ? 113 HIS A O   1 
ATOM   905  C  CB  . HIS A 1 114 ? 27.730 20.650  11.178  1.00 17.79  ? 113 HIS A CB  1 
ATOM   906  C  CG  . HIS A 1 114 ? 27.597 21.579  12.347  1.00 23.44  ? 113 HIS A CG  1 
ATOM   907  N  ND1 . HIS A 1 114 ? 26.452 22.286  12.641  1.00 29.78  ? 113 HIS A ND1 1 
ATOM   908  C  CD2 . HIS A 1 114 ? 28.524 21.990  13.250  1.00 24.06  ? 113 HIS A CD2 1 
ATOM   909  C  CE1 . HIS A 1 114 ? 26.719 23.099  13.675  1.00 24.39  ? 113 HIS A CE1 1 
ATOM   910  N  NE2 . HIS A 1 114 ? 27.966 22.954  14.080  1.00 29.30  ? 113 HIS A NE2 1 
ATOM   911  N  N   . VAL A 1 115 ? 30.618 21.250  10.294  1.00 14.94  ? 114 VAL A N   1 
ATOM   912  C  CA  . VAL A 1 115 ? 31.931 21.791  10.611  1.00 14.73  ? 114 VAL A CA  1 
ATOM   913  C  C   . VAL A 1 115 ? 32.499 22.683  9.505   1.00 14.66  ? 114 VAL A C   1 
ATOM   914  O  O   . VAL A 1 115 ? 33.068 23.740  9.813   1.00 14.94  ? 114 VAL A O   1 
ATOM   915  C  CB  . VAL A 1 115 ? 32.920 20.662  10.987  1.00 14.48  ? 114 VAL A CB  1 
ATOM   916  C  CG1 . VAL A 1 115 ? 34.340 21.219  11.164  1.00 13.11  ? 114 VAL A CG1 1 
ATOM   917  C  CG2 . VAL A 1 115 ? 32.440 19.999  12.268  1.00 13.96  ? 114 VAL A CG2 1 
ATOM   918  N  N   . LEU A 1 116 ? 32.338 22.280  8.237   1.00 13.94  ? 115 LEU A N   1 
ATOM   919  C  CA  . LEU A 1 116 ? 32.835 23.092  7.122   1.00 13.91  ? 115 LEU A CA  1 
ATOM   920  C  C   . LEU A 1 116 ? 32.080 24.408  7.094   1.00 14.23  ? 115 LEU A C   1 
ATOM   921  O  O   . LEU A 1 116 ? 32.648 25.463  6.832   1.00 13.51  ? 115 LEU A O   1 
ATOM   922  C  CB  . LEU A 1 116 ? 32.666 22.375  5.781   1.00 14.09  ? 115 LEU A CB  1 
ATOM   923  C  CG  . LEU A 1 116 ? 33.424 21.045  5.668   1.00 15.85  ? 115 LEU A CG  1 
ATOM   924  C  CD1 . LEU A 1 116 ? 33.409 20.552  4.236   1.00 16.60  ? 115 LEU A CD1 1 
ATOM   925  C  CD2 . LEU A 1 116 ? 34.834 21.202  6.155   1.00 15.79  ? 115 LEU A CD2 1 
ATOM   926  N  N   . HIS A 1 117 ? 30.786 24.333  7.380   1.00 14.42  ? 116 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 117 ? 29.968 25.515  7.403   1.00 15.44  ? 116 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 117 ? 30.475 26.489  8.469   1.00 16.15  ? 116 HIS A C   1 
ATOM   929  O  O   . HIS A 1 117 ? 30.602 27.680  8.191   1.00 16.39  ? 116 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 117 ? 28.511 25.146  7.646   1.00 15.97  ? 116 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 117 ? 27.603 26.331  7.736   1.00 23.94  ? 116 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 117 ? 27.213 27.089  6.653   1.00 27.64  ? 116 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 117 ? 27.027 26.913  8.821   1.00 20.22  ? 116 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 117 ? 26.432 28.083  7.102   1.00 23.91  ? 116 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 117 ? 26.290 28.016  8.411   1.00 30.41  ? 116 HIS A NE2 1 
ATOM   936  N  N   . SER A 1 118 ? 30.831 25.980  9.651   1.00 16.25  ? 117 SER A N   1 
ATOM   937  C  CA  . SER A 1 118 ? 31.319 26.838  10.732  1.00 17.46  ? 117 SER A CA  1 
ATOM   938  C  C   . SER A 1 118 ? 32.694 27.451  10.476  1.00 16.93  ? 117 SER A C   1 
ATOM   939  O  O   . SER A 1 118 ? 32.892 28.658  10.634  1.00 16.79  ? 117 SER A O   1 
ATOM   940  C  CB  . SER A 1 118 ? 31.411 26.060  12.046  1.00 17.33  ? 117 SER A CB  1 
ATOM   941  O  OG  . SER A 1 118 ? 30.143 25.595  12.424  1.00 23.22  ? 117 SER A OG  1 
ATOM   942  N  N   . ARG A 1 119 ? 33.642 26.604  10.099  1.00 16.00  ? 118 ARG A N   1 
ATOM   943  C  CA  . ARG A 1 119 ? 35.002 27.048  9.883   1.00 16.09  ? 118 ARG A CA  1 
ATOM   944  C  C   . ARG A 1 119 ? 35.311 27.709  8.563   1.00 16.42  ? 118 ARG A C   1 
ATOM   945  O  O   . ARG A 1 119 ? 36.267 28.465  8.477   1.00 16.85  ? 118 ARG A O   1 
ATOM   946  C  CB  . ARG A 1 119 ? 35.956 25.877  10.095  1.00 16.31  ? 118 ARG A CB  1 
ATOM   947  C  CG  . ARG A 1 119 ? 35.923 25.326  11.507  1.00 17.66  ? 118 ARG A CG  1 
ATOM   948  C  CD  . ARG A 1 119 ? 36.833 24.121  11.658  1.00 18.91  ? 118 ARG A CD  1 
ATOM   949  N  NE  . ARG A 1 119 ? 38.232 24.485  11.507  1.00 23.08  ? 118 ARG A NE  1 
ATOM   950  C  CZ  . ARG A 1 119 ? 39.221 23.958  12.218  1.00 28.58  ? 118 ARG A CZ  1 
ATOM   951  N  NH1 . ARG A 1 119 ? 38.969 23.042  13.139  1.00 19.83  ? 118 ARG A NH1 1 
ATOM   952  N  NH2 . ARG A 1 119 ? 40.465 24.345  11.995  1.00 22.14  ? 118 ARG A NH2 1 
ATOM   953  N  N   . HIS A 1 120 ? 34.513 27.438  7.535   1.00 16.21  ? 119 HIS A N   1 
ATOM   954  C  CA  . HIS A 1 120 ? 34.776 27.995  6.215   1.00 16.52  ? 119 HIS A CA  1 
ATOM   955  C  C   . HIS A 1 120 ? 33.570 28.657  5.558   1.00 16.96  ? 119 HIS A C   1 
ATOM   956  O  O   . HIS A 1 120 ? 33.264 28.372  4.401   1.00 16.55  ? 119 HIS A O   1 
ATOM   957  C  CB  . HIS A 1 120 ? 35.322 26.881  5.307   1.00 15.35  ? 119 HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 120 ? 36.503 26.173  5.887   1.00 16.81  ? 119 HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 120 ? 37.754 26.740  6.014   1.00 17.07  ? 119 HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 120 ? 36.596 24.945  6.456   1.00 12.45  ? 119 HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 120 ? 38.553 25.864  6.649   1.00 15.79  ? 119 HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 120 ? 37.906 24.754  6.940   1.00 14.56  ? 119 HIS A NE2 1 
ATOM   963  N  N   . PRO A 1 121 ? 32.924 29.613  6.253   1.00 17.60  ? 120 PRO A N   1 
ATOM   964  C  CA  . PRO A 1 121 ? 31.752 30.293  5.690   1.00 18.44  ? 120 PRO A CA  1 
ATOM   965  C  C   . PRO A 1 121 ? 31.994 30.906  4.305   1.00 18.89  ? 120 PRO A C   1 
ATOM   966  O  O   . PRO A 1 121 ? 31.163 30.775  3.420   1.00 19.93  ? 120 PRO A O   1 
ATOM   967  C  CB  . PRO A 1 121 ? 31.416 31.353  6.755   1.00 18.40  ? 120 PRO A CB  1 
ATOM   968  C  CG  . PRO A 1 121 ? 32.734 31.641  7.386   1.00 18.17  ? 120 PRO A CG  1 
ATOM   969  C  CD  . PRO A 1 121 ? 33.343 30.256  7.512   1.00 17.55  ? 120 PRO A CD  1 
ATOM   970  N  N   . GLY A 1 122 ? 33.168 31.490  4.101   1.00 19.23  ? 121 GLY A N   1 
ATOM   971  C  CA  . GLY A 1 122 ? 33.482 32.098  2.826   1.00 19.49  ? 121 GLY A CA  1 
ATOM   972  C  C   . GLY A 1 122 ? 33.638 31.118  1.674   1.00 19.88  ? 121 GLY A C   1 
ATOM   973  O  O   . GLY A 1 122 ? 33.383 31.492  0.531   1.00 21.13  ? 121 GLY A O   1 
ATOM   974  N  N   . ASN A 1 123 ? 34.066 29.885  1.947   1.00 18.33  ? 122 ASN A N   1 
ATOM   975  C  CA  . ASN A 1 123 ? 34.224 28.896  0.881   1.00 17.56  ? 122 ASN A CA  1 
ATOM   976  C  C   . ASN A 1 123 ? 33.145 27.830  0.958   1.00 17.40  ? 122 ASN A C   1 
ATOM   977  O  O   . ASN A 1 123 ? 33.271 26.768  0.330   1.00 18.22  ? 122 ASN A O   1 
ATOM   978  C  CB  . ASN A 1 123 ? 35.603 28.215  0.956   1.00 16.47  ? 122 ASN A CB  1 
ATOM   979  C  CG  . ASN A 1 123 ? 36.744 29.175  0.651   1.00 23.94  ? 122 ASN A CG  1 
ATOM   980  O  OD1 . ASN A 1 123 ? 37.668 29.352  1.452   1.00 21.42  ? 122 ASN A OD1 1 
ATOM   981  N  ND2 . ASN A 1 123 ? 36.674 29.812  -0.504  1.00 17.36  ? 122 ASN A ND2 1 
ATOM   982  N  N   . PHE A 1 124 ? 32.082 28.095  1.714   1.00 16.20  ? 123 PHE A N   1 
ATOM   983  C  CA  . PHE A 1 124 ? 31.031 27.091  1.861   1.00 15.22  ? 123 PHE A CA  1 
ATOM   984  C  C   . PHE A 1 124 ? 29.638 27.707  1.810   1.00 15.07  ? 123 PHE A C   1 
ATOM   985  O  O   . PHE A 1 124 ? 28.854 27.581  2.755   1.00 14.90  ? 123 PHE A O   1 
ATOM   986  C  CB  . PHE A 1 124 ? 31.233 26.291  3.167   1.00 14.16  ? 123 PHE A CB  1 
ATOM   987  C  CG  . PHE A 1 124 ? 30.680 24.889  3.137   1.00 13.87  ? 123 PHE A CG  1 
ATOM   988  C  CD1 . PHE A 1 124 ? 31.217 23.933  2.294   1.00 13.81  ? 123 PHE A CD1 1 
ATOM   989  C  CD2 . PHE A 1 124 ? 29.654 24.508  4.002   1.00 13.82  ? 123 PHE A CD2 1 
ATOM   990  C  CE1 . PHE A 1 124 ? 30.736 22.601  2.319   1.00 14.46  ? 123 PHE A CE1 1 
ATOM   991  C  CE2 . PHE A 1 124 ? 29.175 23.194  4.037   1.00 13.98  ? 123 PHE A CE2 1 
ATOM   992  C  CZ  . PHE A 1 124 ? 29.714 22.240  3.198   1.00 14.00  ? 123 PHE A CZ  1 
ATOM   993  N  N   . GLY A 1 125 ? 29.374 28.424  0.723   1.00 14.89  ? 124 GLY A N   1 
ATOM   994  C  CA  . GLY A 1 125 ? 28.066 29.008  0.499   1.00 14.52  ? 124 GLY A CA  1 
ATOM   995  C  C   . GLY A 1 125 ? 27.131 27.883  0.064   1.00 14.67  ? 124 GLY A C   1 
ATOM   996  O  O   . GLY A 1 125 ? 27.517 26.713  0.061   1.00 13.74  ? 124 GLY A O   1 
ATOM   997  N  N   . ALA A 1 126 ? 25.924 28.240  -0.357  1.00 14.54  ? 125 ALA A N   1 
ATOM   998  C  CA  . ALA A 1 126 ? 24.917 27.259  -0.746  1.00 14.94  ? 125 ALA A CA  1 
ATOM   999  C  C   . ALA A 1 126 ? 25.330 26.324  -1.882  1.00 15.13  ? 125 ALA A C   1 
ATOM   1000 O  O   . ALA A 1 126 ? 25.058 25.124  -1.837  1.00 15.68  ? 125 ALA A O   1 
ATOM   1001 C  CB  . ALA A 1 126 ? 23.600 27.970  -1.090  1.00 14.69  ? 125 ALA A CB  1 
ATOM   1002 N  N   . ASP A 1 127 ? 25.955 26.880  -2.913  1.00 13.43  ? 126 ASP A N   1 
ATOM   1003 C  CA  . ASP A 1 127 ? 26.388 26.088  -4.051  1.00 10.99  ? 126 ASP A CA  1 
ATOM   1004 C  C   . ASP A 1 127 ? 27.429 25.070  -3.619  1.00 14.91  ? 126 ASP A C   1 
ATOM   1005 O  O   . ASP A 1 127 ? 27.315 23.908  -3.964  1.00 15.09  ? 126 ASP A O   1 
ATOM   1006 C  CB  . ASP A 1 127 ? 26.948 26.989  -5.153  1.00 21.24  ? 126 ASP A CB  1 
ATOM   1007 C  CG  . ASP A 1 127 ? 25.867 27.804  -5.856  1.00 26.37  ? 126 ASP A CG  1 
ATOM   1008 O  OD1 . ASP A 1 127 ? 24.685 27.408  -5.820  1.00 25.47  ? 126 ASP A OD1 1 
ATOM   1009 O  OD2 . ASP A 1 127 ? 26.209 28.840  -6.458  1.00 35.73  ? 126 ASP A OD2 1 
ATOM   1010 N  N   . ALA A 1 128 ? 28.446 25.508  -2.875  1.00 13.00  ? 127 ALA A N   1 
ATOM   1011 C  CA  . ALA A 1 128 ? 29.495 24.603  -2.377  1.00 13.19  ? 127 ALA A CA  1 
ATOM   1012 C  C   . ALA A 1 128 ? 28.926 23.532  -1.425  1.00 13.50  ? 127 ALA A C   1 
ATOM   1013 O  O   . ALA A 1 128 ? 29.358 22.381  -1.455  1.00 14.17  ? 127 ALA A O   1 
ATOM   1014 C  CB  . ALA A 1 128 ? 30.631 25.403  -1.677  1.00 12.59  ? 127 ALA A CB  1 
ATOM   1015 N  N   . GLN A 1 129 ? 27.973 23.902  -0.575  1.00 12.96  ? 128 GLN A N   1 
ATOM   1016 C  CA  . GLN A 1 129 ? 27.375 22.922  0.329   1.00 13.45  ? 128 GLN A CA  1 
ATOM   1017 C  C   . GLN A 1 129 ? 26.566 21.885  -0.482  1.00 13.71  ? 128 GLN A C   1 
ATOM   1018 O  O   . GLN A 1 129 ? 26.579 20.692  -0.161  1.00 14.19  ? 128 GLN A O   1 
ATOM   1019 C  CB  . GLN A 1 129 ? 26.479 23.596  1.390   1.00 13.18  ? 128 GLN A CB  1 
ATOM   1020 C  CG  . GLN A 1 129 ? 25.765 22.583  2.295   1.00 15.46  ? 128 GLN A CG  1 
ATOM   1021 C  CD  . GLN A 1 129 ? 25.069 23.195  3.504   1.00 17.66  ? 128 GLN A CD  1 
ATOM   1022 O  OE1 . GLN A 1 129 ? 25.372 24.311  3.925   1.00 19.04  ? 128 GLN A OE1 1 
ATOM   1023 N  NE2 . GLN A 1 129 ? 24.140 22.445  4.081   1.00 16.30  ? 128 GLN A NE2 1 
ATOM   1024 N  N   . GLY A 1 130 ? 25.861 22.348  -1.516  1.00 13.17  ? 129 GLY A N   1 
ATOM   1025 C  CA  . GLY A 1 130 ? 25.088 21.443  -2.354  1.00 13.25  ? 129 GLY A CA  1 
ATOM   1026 C  C   . GLY A 1 130 ? 26.014 20.439  -3.043  1.00 13.29  ? 129 GLY A C   1 
ATOM   1027 O  O   . GLY A 1 130 ? 25.688 19.247  -3.146  1.00 13.24  ? 129 GLY A O   1 
ATOM   1028 N  N   . ALA A 1 131 ? 27.172 20.913  -3.501  1.00 12.37  ? 130 ALA A N   1 
ATOM   1029 C  CA  . ALA A 1 131 ? 28.145 20.044  -4.156  1.00 13.20  ? 130 ALA A CA  1 
ATOM   1030 C  C   . ALA A 1 131 ? 28.715 19.001  -3.176  1.00 13.32  ? 130 ALA A C   1 
ATOM   1031 O  O   . ALA A 1 131 ? 28.837 17.822  -3.517  1.00 13.58  ? 130 ALA A O   1 
ATOM   1032 C  CB  . ALA A 1 131 ? 29.268 20.869  -4.757  1.00 12.82  ? 130 ALA A CB  1 
ATOM   1033 N  N   . MET A 1 132 ? 29.046 19.439  -1.963  1.00 13.52  ? 131 MET A N   1 
ATOM   1034 C  CA  . MET A 1 132 ? 29.592 18.553  -0.926  1.00 14.15  ? 131 MET A CA  1 
ATOM   1035 C  C   . MET A 1 132 ? 28.563 17.476  -0.540  1.00 13.73  ? 131 MET A C   1 
ATOM   1036 O  O   . MET A 1 132 ? 28.891 16.292  -0.427  1.00 12.90  ? 131 MET A O   1 
ATOM   1037 C  CB  . MET A 1 132 ? 30.018 19.379  0.312   1.00 14.76  ? 131 MET A CB  1 
ATOM   1038 C  CG  . MET A 1 132 ? 30.675 18.564  1.445   1.00 15.74  ? 131 MET A CG  1 
ATOM   1039 S  SD  . MET A 1 132 ? 32.201 17.676  0.927   1.00 18.67  ? 131 MET A SD  1 
ATOM   1040 C  CE  . MET A 1 132 ? 33.349 18.957  1.034   1.00 16.91  ? 131 MET A CE  1 
ATOM   1041 N  N   . ASN A 1 133 ? 27.317 17.899  -0.341  1.00 13.80  ? 132 ASN A N   1 
ATOM   1042 C  CA  . ASN A 1 133 ? 26.253 16.967  -0.011  1.00 14.77  ? 132 ASN A CA  1 
ATOM   1043 C  C   . ASN A 1 133 ? 26.109 15.913  -1.129  1.00 15.12  ? 132 ASN A C   1 
ATOM   1044 O  O   . ASN A 1 133 ? 25.927 14.725  -0.860  1.00 15.96  ? 132 ASN A O   1 
ATOM   1045 C  CB  . ASN A 1 133 ? 24.925 17.699  0.156   1.00 13.92  ? 132 ASN A CB  1 
ATOM   1046 C  CG  . ASN A 1 133 ? 23.770 16.739  0.357   1.00 16.64  ? 132 ASN A CG  1 
ATOM   1047 O  OD1 . ASN A 1 133 ? 23.803 15.923  1.265   1.00 17.59  ? 132 ASN A OD1 1 
ATOM   1048 N  ND2 . ASN A 1 133 ? 22.777 16.796  -0.521  1.00 18.26  ? 132 ASN A ND2 1 
ATOM   1049 N  N   . LYS A 1 134 ? 26.201 16.364  -2.377  1.00 17.32  ? 133 LYS A N   1 
ATOM   1050 C  CA  . LYS A 1 134 ? 26.084 15.489  -3.538  1.00 14.82  ? 133 LYS A CA  1 
ATOM   1051 C  C   . LYS A 1 134 ? 27.246 14.480  -3.574  1.00 17.90  ? 133 LYS A C   1 
ATOM   1052 O  O   . LYS A 1 134 ? 27.050 13.289  -3.860  1.00 13.48  ? 133 LYS A O   1 
ATOM   1053 C  CB  . LYS A 1 134 ? 26.057 16.345  -4.803  1.00 19.71  ? 133 LYS A CB  1 
ATOM   1054 C  CG  . LYS A 1 134 ? 25.420 15.682  -5.984  1.00 28.22  ? 133 LYS A CG  1 
ATOM   1055 C  CD  . LYS A 1 134 ? 25.308 16.625  -7.163  1.00 27.62  ? 133 LYS A CD  1 
ATOM   1056 C  CE  . LYS A 1 134 ? 24.914 15.859  -8.413  1.00 52.97  ? 133 LYS A CE  1 
ATOM   1057 N  NZ  . LYS A 1 134 ? 24.905 16.725  -9.614  1.00 74.53  ? 133 LYS A NZ  1 
ATOM   1058 N  N   . ALA A 1 135 ? 28.442 14.950  -3.229  1.00 12.87  ? 134 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 135 ? 29.630 14.091  -3.218  1.00 13.47  ? 134 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 135 ? 29.534 13.030  -2.115  1.00 13.87  ? 134 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 135 ? 29.860 11.859  -2.339  1.00 14.49  ? 134 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 135 ? 30.910 14.939  -3.056  1.00 12.22  ? 134 ALA A CB  1 
ATOM   1063 N  N   . LEU A 1 136 ? 29.034 13.434  -0.946  1.00 13.82  ? 135 LEU A N   1 
ATOM   1064 C  CA  . LEU A 1 136 ? 28.879 12.522  0.189   1.00 13.98  ? 135 LEU A CA  1 
ATOM   1065 C  C   . LEU A 1 136 ? 27.727 11.537  -0.044  1.00 14.11  ? 135 LEU A C   1 
ATOM   1066 O  O   . LEU A 1 136 ? 27.775 10.407  0.425   1.00 14.20  ? 135 LEU A O   1 
ATOM   1067 C  CB  . LEU A 1 136 ? 28.695 13.310  1.496   1.00 13.75  ? 135 LEU A CB  1 
ATOM   1068 C  CG  . LEU A 1 136 ? 29.929 14.062  2.025   1.00 14.13  ? 135 LEU A CG  1 
ATOM   1069 C  CD1 . LEU A 1 136 ? 29.580 14.870  3.284   1.00 13.81  ? 135 LEU A CD1 1 
ATOM   1070 C  CD2 . LEU A 1 136 ? 31.034 13.075  2.339   1.00 13.90  ? 135 LEU A CD2 1 
ATOM   1071 N  N   . GLU A 1 137 ? 26.679 11.973  -0.744  1.00 13.49  ? 136 GLU A N   1 
ATOM   1072 C  CA  . GLU A 1 137 ? 25.573 11.074  -1.066  1.00 16.04  ? 136 GLU A CA  1 
ATOM   1073 C  C   . GLU A 1 137 ? 26.067 9.999   -2.047  1.00 14.96  ? 136 GLU A C   1 
ATOM   1074 O  O   . GLU A 1 137 ? 25.653 8.831   -1.963  1.00 16.34  ? 136 GLU A O   1 
ATOM   1075 C  CB  . GLU A 1 137 ? 24.414 11.828  -1.707  1.00 12.46  ? 136 GLU A CB  1 
ATOM   1076 C  CG  . GLU A 1 137 ? 23.703 12.789  -0.789  1.00 44.80  ? 136 GLU A CG  1 
ATOM   1077 C  CD  . GLU A 1 137 ? 22.473 13.394  -1.432  1.00 52.55  ? 136 GLU A CD  1 
ATOM   1078 O  OE1 . GLU A 1 137 ? 22.235 13.142  -2.637  1.00 48.81  ? 136 GLU A OE1 1 
ATOM   1079 O  OE2 . GLU A 1 137 ? 21.740 14.118  -0.728  1.00 56.19  ? 136 GLU A OE2 1 
ATOM   1080 N  N   . LEU A 1 138 ? 26.900 10.421  -3.008  1.00 15.12  ? 137 LEU A N   1 
ATOM   1081 C  CA  . LEU A 1 138 ? 27.482 9.515   -4.002  1.00 15.96  ? 137 LEU A CA  1 
ATOM   1082 C  C   . LEU A 1 138 ? 28.283 8.449   -3.238  1.00 15.89  ? 137 LEU A C   1 
ATOM   1083 O  O   . LEU A 1 138 ? 28.123 7.250   -3.486  1.00 15.91  ? 137 LEU A O   1 
ATOM   1084 C  CB  . LEU A 1 138 ? 28.393 10.273  -4.992  1.00 16.54  ? 137 LEU A CB  1 
ATOM   1085 C  CG  . LEU A 1 138 ? 29.149 9.382   -5.990  1.00 17.78  ? 137 LEU A CG  1 
ATOM   1086 C  CD1 . LEU A 1 138 ? 28.184 8.728   -6.969  1.00 19.20  ? 137 LEU A CD1 1 
ATOM   1087 C  CD2 . LEU A 1 138 ? 30.192 10.163  -6.740  1.00 18.22  ? 137 LEU A CD2 1 
ATOM   1088 N  N   . PHE A 1 139 ? 29.104 8.901   -2.290  1.00 15.56  ? 138 PHE A N   1 
ATOM   1089 C  CA  . PHE A 1 139 ? 29.901 8.016   -1.440  1.00 16.09  ? 138 PHE A CA  1 
ATOM   1090 C  C   . PHE A 1 139 ? 29.003 7.006   -0.703  1.00 15.97  ? 138 PHE A C   1 
ATOM   1091 O  O   . PHE A 1 139 ? 29.276 5.805   -0.743  1.00 16.01  ? 138 PHE A O   1 
ATOM   1092 C  CB  . PHE A 1 139 ? 30.706 8.854   -0.438  1.00 17.10  ? 138 PHE A CB  1 
ATOM   1093 C  CG  . PHE A 1 139 ? 31.336 8.055   0.682   1.00 18.65  ? 138 PHE A CG  1 
ATOM   1094 C  CD1 . PHE A 1 139 ? 32.408 7.211   0.438   1.00 19.08  ? 138 PHE A CD1 1 
ATOM   1095 C  CD2 . PHE A 1 139 ? 30.851 8.152   1.981   1.00 18.98  ? 138 PHE A CD2 1 
ATOM   1096 C  CE1 . PHE A 1 139 ? 32.983 6.479   1.465   1.00 19.60  ? 138 PHE A CE1 1 
ATOM   1097 C  CE2 . PHE A 1 139 ? 31.426 7.417   3.011   1.00 19.50  ? 138 PHE A CE2 1 
ATOM   1098 C  CZ  . PHE A 1 139 ? 32.496 6.579   2.748   1.00 19.07  ? 138 PHE A CZ  1 
ATOM   1099 N  N   . ARG A 1 140 ? 27.936 7.487   -0.055  1.00 15.51  ? 139 ARG A N   1 
ATOM   1100 C  CA  . ARG A 1 140 ? 27.002 6.615   0.673   1.00 16.38  ? 139 ARG A CA  1 
ATOM   1101 C  C   . ARG A 1 140 ? 26.266 5.598   -0.209  1.00 16.38  ? 139 ARG A C   1 
ATOM   1102 O  O   . ARG A 1 140 ? 25.990 4.478   0.225   1.00 17.17  ? 139 ARG A O   1 
ATOM   1103 C  CB  . ARG A 1 140 ? 25.967 7.431   1.468   1.00 14.71  ? 139 ARG A CB  1 
ATOM   1104 C  CG  . ARG A 1 140 ? 26.585 8.244   2.606   1.00 21.56  ? 139 ARG A CG  1 
ATOM   1105 C  CD  . ARG A 1 140 ? 25.567 8.664   3.645   1.00 14.30  ? 139 ARG A CD  1 
ATOM   1106 N  NE  . ARG A 1 140 ? 24.454 9.404   3.064   1.00 18.17  ? 139 ARG A NE  1 
ATOM   1107 C  CZ  . ARG A 1 140 ? 24.460 10.703  2.777   1.00 21.08  ? 139 ARG A CZ  1 
ATOM   1108 N  NH1 . ARG A 1 140 ? 25.530 11.459  3.004   1.00 20.58  ? 139 ARG A NH1 1 
ATOM   1109 N  NH2 . ARG A 1 140 ? 23.378 11.247  2.255   1.00 16.97  ? 139 ARG A NH2 1 
ATOM   1110 N  N   . LYS A 1 141 ? 25.890 6.026   -1.411  1.00 16.09  ? 140 LYS A N   1 
ATOM   1111 C  CA  . LYS A 1 141 ? 25.192 5.173   -2.374  1.00 20.00  ? 140 LYS A CA  1 
ATOM   1112 C  C   . LYS A 1 141 ? 26.098 4.014   -2.808  1.00 21.76  ? 140 LYS A C   1 
ATOM   1113 O  O   . LYS A 1 141 ? 25.676 2.863   -2.836  1.00 14.42  ? 140 LYS A O   1 
ATOM   1114 C  CB  . LYS A 1 141 ? 24.790 5.986   -3.611  1.00 27.06  ? 140 LYS A CB  1 
ATOM   1115 C  CG  . LYS A 1 141 ? 23.972 5.206   -4.634  1.00 45.99  ? 140 LYS A CG  1 
ATOM   1116 C  CD  . LYS A 1 141 ? 23.402 6.100   -5.741  1.00 79.30  ? 140 LYS A CD  1 
ATOM   1117 C  CE  . LYS A 1 141 ? 24.365 6.287   -6.920  1.00 85.35  ? 140 LYS A CE  1 
ATOM   1118 N  NZ  . LYS A 1 141 ? 25.631 6.990   -6.564  1.00 82.64  ? 140 LYS A NZ  1 
ATOM   1119 N  N   . ASP A 1 142 ? 27.341 4.329   -3.160  1.00 13.76  ? 141 ASP A N   1 
ATOM   1120 C  CA  . ASP A 1 142 ? 28.285 3.302   -3.582  1.00 14.64  ? 141 ASP A CA  1 
ATOM   1121 C  C   . ASP A 1 142 ? 28.650 2.361   -2.438  1.00 18.09  ? 141 ASP A C   1 
ATOM   1122 O  O   . ASP A 1 142 ? 28.698 1.146   -2.626  1.00 18.83  ? 141 ASP A O   1 
ATOM   1123 C  CB  . ASP A 1 142 ? 29.519 3.943   -4.215  1.00 17.81  ? 141 ASP A CB  1 
ATOM   1124 C  CG  . ASP A 1 142 ? 29.211 4.607   -5.550  1.00 21.65  ? 141 ASP A CG  1 
ATOM   1125 O  OD1 . ASP A 1 142 ? 28.120 4.365   -6.097  1.00 22.33  ? 141 ASP A OD1 1 
ATOM   1126 O  OD2 . ASP A 1 142 ? 30.043 5.385   -6.048  1.00 22.08  ? 141 ASP A OD2 1 
ATOM   1127 N  N   . ILE A 1 143 ? 28.849 2.907   -1.243  1.00 19.69  ? 142 ILE A N   1 
ATOM   1128 C  CA  . ILE A 1 143 ? 29.172 2.078   -0.082  1.00 20.48  ? 142 ILE A CA  1 
ATOM   1129 C  C   . ILE A 1 143 ? 28.030 1.100   0.235   1.00 20.33  ? 142 ILE A C   1 
ATOM   1130 O  O   . ILE A 1 143 ? 28.283 -0.080  0.528   1.00 20.05  ? 142 ILE A O   1 
ATOM   1131 C  CB  . ILE A 1 143 ? 29.456 2.930   1.190   1.00 21.51  ? 142 ILE A CB  1 
ATOM   1132 C  CG1 . ILE A 1 143 ? 30.911 3.387   1.209   1.00 23.16  ? 142 ILE A CG1 1 
ATOM   1133 C  CG2 . ILE A 1 143 ? 29.196 2.110   2.455   1.00 22.03  ? 142 ILE A CG2 1 
ATOM   1134 C  CD1 . ILE A 1 143 ? 31.869 2.331   1.774   1.00 24.63  ? 142 ILE A CD1 1 
ATOM   1135 N  N   . ALA A 1 144 ? 26.786 1.591   0.204   1.00 19.87  ? 143 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 144 ? 25.639 0.732   0.505   1.00 20.12  ? 143 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 144 ? 25.446 -0.353  -0.549  1.00 20.01  ? 143 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 144 ? 25.058 -1.458  -0.215  1.00 20.33  ? 143 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 144 ? 24.379 1.531   0.717   1.00 19.82  ? 143 ALA A CB  1 
ATOM   1140 N  N   . ALA A 1 145 ? 25.776 -0.058  -1.804  1.00 19.98  ? 144 ALA A N   1 
ATOM   1141 C  CA  . ALA A 1 145 ? 25.681 -1.066  -2.853  1.00 20.13  ? 144 ALA A CA  1 
ATOM   1142 C  C   . ALA A 1 145 ? 26.718 -2.168  -2.538  1.00 20.63  ? 144 ALA A C   1 
ATOM   1143 O  O   . ALA A 1 145 ? 26.431 -3.366  -2.671  1.00 20.63  ? 144 ALA A O   1 
ATOM   1144 C  CB  . ALA A 1 145 ? 25.962 -0.444  -4.200  1.00 19.92  ? 144 ALA A CB  1 
ATOM   1145 N  N   . LYS A 1 146 ? 27.908 -1.759  -2.090  1.00 14.94  ? 145 LYS A N   1 
ATOM   1146 C  CA  . LYS A 1 146 ? 28.961 -2.703  -1.733  1.00 18.47  ? 145 LYS A CA  1 
ATOM   1147 C  C   . LYS A 1 146 ? 28.572 -3.526  -0.501  1.00 19.66  ? 145 LYS A C   1 
ATOM   1148 O  O   . LYS A 1 146 ? 28.871 -4.722  -0.426  1.00 17.53  ? 145 LYS A O   1 
ATOM   1149 C  CB  . LYS A 1 146 ? 30.280 -1.969  -1.501  1.00 17.80  ? 145 LYS A CB  1 
ATOM   1150 C  CG  . LYS A 1 146 ? 31.031 -1.636  -2.759  1.00 36.20  ? 145 LYS A CG  1 
ATOM   1151 C  CD  . LYS A 1 146 ? 30.080 -1.244  -3.902  1.00 73.26  ? 145 LYS A CD  1 
ATOM   1152 C  CE  . LYS A 1 146 ? 30.622 -0.117  -4.755  1.00 63.31  ? 145 LYS A CE  1 
ATOM   1153 N  NZ  . LYS A 1 146 ? 29.511 0.471   -5.560  1.00 26.86  ? 145 LYS A NZ  1 
ATOM   1154 N  N   . TYR A 1 147 ? 27.903 -2.885  0.455   1.00 19.77  ? 146 TYR A N   1 
ATOM   1155 C  CA  . TYR A 1 147 ? 27.428 -3.564  1.666   1.00 19.91  ? 146 TYR A CA  1 
ATOM   1156 C  C   . TYR A 1 147 ? 26.536 -4.755  1.286   1.00 19.89  ? 146 TYR A C   1 
ATOM   1157 O  O   . TYR A 1 147 ? 26.667 -5.858  1.817   1.00 19.66  ? 146 TYR A O   1 
ATOM   1158 C  CB  . TYR A 1 147 ? 26.589 -2.598  2.503   1.00 20.59  ? 146 TYR A CB  1 
ATOM   1159 C  CG  . TYR A 1 147 ? 27.328 -1.832  3.587   1.00 21.16  ? 146 TYR A CG  1 
ATOM   1160 C  CD1 . TYR A 1 147 ? 28.716 -1.668  3.565   1.00 20.53  ? 146 TYR A CD1 1 
ATOM   1161 C  CD2 . TYR A 1 147 ? 26.618 -1.268  4.649   1.00 22.22  ? 146 TYR A CD2 1 
ATOM   1162 C  CE1 . TYR A 1 147 ? 29.372 -0.960  4.584   1.00 20.93  ? 146 TYR A CE1 1 
ATOM   1163 C  CE2 . TYR A 1 147 ? 27.263 -0.561  5.660   1.00 22.12  ? 146 TYR A CE2 1 
ATOM   1164 C  CZ  . TYR A 1 147 ? 28.625 -0.411  5.625   1.00 21.42  ? 146 TYR A CZ  1 
ATOM   1165 O  OH  . TYR A 1 147 ? 29.207 0.309   6.636   1.00 20.90  ? 146 TYR A OH  1 
ATOM   1166 N  N   . LYS A 1 148 ? 25.611 -4.506  0.371   1.00 19.69  ? 147 LYS A N   1 
ATOM   1167 C  CA  . LYS A 1 148 ? 24.702 -5.535  -0.111  1.00 21.47  ? 147 LYS A CA  1 
ATOM   1168 C  C   . LYS A 1 148 ? 25.451 -6.695  -0.780  1.00 18.52  ? 147 LYS A C   1 
ATOM   1169 O  O   . LYS A 1 148 ? 25.205 -7.858  -0.464  1.00 21.47  ? 147 LYS A O   1 
ATOM   1170 C  CB  . LYS A 1 148 ? 23.851 -4.999  -1.248  1.00 20.52  ? 147 LYS A CB  1 
ATOM   1171 C  CG  . LYS A 1 148 ? 22.578 -5.867  -1.484  1.00 32.74  ? 147 LYS A CG  1 
ATOM   1172 C  CD  . LYS A 1 148 ? 21.612 -5.212  -2.434  1.00 64.47  ? 147 LYS A CD  1 
ATOM   1173 C  CE  . LYS A 1 148 ? 20.772 -6.289  -3.099  1.00 83.74  ? 147 LYS A CE  1 
ATOM   1174 N  NZ  . LYS A 1 148 ? 20.297 -7.337  -2.134  1.00 87.66  ? 147 LYS A NZ  1 
ATOM   1175 N  N   . GLU A 1 149 ? 26.410 -6.374  -1.654  1.00 19.36  ? 148 GLU A N   1 
ATOM   1176 C  CA  . GLU A 1 149 ? 27.194 -7.412  -2.326  1.00 21.36  ? 148 GLU A CA  1 
ATOM   1177 C  C   . GLU A 1 149 ? 27.942 -8.261  -1.300  1.00 26.24  ? 148 GLU A C   1 
ATOM   1178 O  O   . GLU A 1 149 ? 28.101 -9.471  -1.484  1.00 21.22  ? 148 GLU A O   1 
ATOM   1179 C  CB  . GLU A 1 149 ? 28.203 -6.801  -3.310  1.00 16.10  ? 148 GLU A CB  1 
ATOM   1180 C  CG  . GLU A 1 149 ? 27.557 -6.172  -4.525  1.00 36.64  ? 148 GLU A CG  1 
ATOM   1181 C  CD  . GLU A 1 149 ? 28.537 -5.386  -5.393  1.00 49.34  ? 148 GLU A CD  1 
ATOM   1182 O  OE1 . GLU A 1 149 ? 29.722 -5.777  -5.460  1.00 47.38  ? 148 GLU A OE1 1 
ATOM   1183 O  OE2 . GLU A 1 149 ? 28.121 -4.372  -5.998  1.00 59.66  ? 148 GLU A OE2 1 
ATOM   1184 N  N   . LEU A 1 150 ? 28.362 -7.623  -0.207  1.00 25.00  ? 149 LEU A N   1 
ATOM   1185 C  CA  . LEU A 1 150 ? 29.106 -8.294  0.852   1.00 25.80  ? 149 LEU A CA  1 
ATOM   1186 C  C   . LEU A 1 150 ? 28.219 -9.028  1.854   1.00 26.62  ? 149 LEU A C   1 
ATOM   1187 O  O   . LEU A 1 150 ? 28.722 -9.698  2.749   1.00 26.63  ? 149 LEU A O   1 
ATOM   1188 C  CB  . LEU A 1 150 ? 30.013 -7.299  1.577   1.00 25.40  ? 149 LEU A CB  1 
ATOM   1189 C  CG  . LEU A 1 150 ? 31.141 -6.664  0.762   1.00 25.18  ? 149 LEU A CG  1 
ATOM   1190 C  CD1 . LEU A 1 150 ? 31.713 -5.460  1.501   1.00 24.78  ? 149 LEU A CD1 1 
ATOM   1191 C  CD2 . LEU A 1 150 ? 32.225 -7.672  0.488   1.00 24.81  ? 149 LEU A CD2 1 
ATOM   1192 N  N   . GLY A 1 151 ? 26.907 -8.890  1.717   1.00 27.83  ? 150 GLY A N   1 
ATOM   1193 C  CA  . GLY A 1 151 ? 26.003 -9.589  2.616   1.00 30.10  ? 150 GLY A CA  1 
ATOM   1194 C  C   . GLY A 1 151 ? 25.544 -8.856  3.861   1.00 31.94  ? 150 GLY A C   1 
ATOM   1195 O  O   . GLY A 1 151 ? 24.929 -9.453  4.737   1.00 31.56  ? 150 GLY A O   1 
ATOM   1196 N  N   . TYR A 1 152 ? 25.821 -7.560  3.935   1.00 34.23  ? 151 TYR A N   1 
ATOM   1197 C  CA  . TYR A 1 152 ? 25.428 -6.776  5.085   1.00 36.68  ? 151 TYR A CA  1 
ATOM   1198 C  C   . TYR A 1 152 ? 24.287 -5.834  4.754   1.00 38.75  ? 151 TYR A C   1 
ATOM   1199 O  O   . TYR A 1 152 ? 23.153 -6.046  5.173   1.00 39.40  ? 151 TYR A O   1 
ATOM   1200 C  CB  . TYR A 1 152 ? 26.624 -5.986  5.613   1.00 37.13  ? 151 TYR A CB  1 
ATOM   1201 C  CG  . TYR A 1 152 ? 26.319 -5.078  6.788   1.00 37.85  ? 151 TYR A CG  1 
ATOM   1202 C  CD1 . TYR A 1 152 ? 25.674 -5.557  7.914   1.00 38.50  ? 151 TYR A CD1 1 
ATOM   1203 C  CD2 . TYR A 1 152 ? 26.670 -3.732  6.762   1.00 38.39  ? 151 TYR A CD2 1 
ATOM   1204 C  CE1 . TYR A 1 152 ? 25.377 -4.720  8.988   1.00 38.95  ? 151 TYR A CE1 1 
ATOM   1205 C  CE2 . TYR A 1 152 ? 26.380 -2.884  7.830   1.00 38.63  ? 151 TYR A CE2 1 
ATOM   1206 C  CZ  . TYR A 1 152 ? 25.727 -3.385  8.936   1.00 39.03  ? 151 TYR A CZ  1 
ATOM   1207 O  OH  . TYR A 1 152 ? 25.362 -2.543  9.964   1.00 39.21  ? 151 TYR A OH  1 
ATOM   1208 N  N   . GLN A 1 153 ? 24.585 -4.802  3.977   1.00 41.07  ? 152 GLN A N   1 
ATOM   1209 C  CA  . GLN A 1 153 ? 23.594 -3.777  3.632   1.00 43.96  ? 152 GLN A CA  1 
ATOM   1210 C  C   . GLN A 1 153 ? 22.790 -3.325  4.860   1.00 45.06  ? 152 GLN A C   1 
ATOM   1211 O  O   . GLN A 1 153 ? 21.587 -3.090  4.787   1.00 45.47  ? 152 GLN A O   1 
ATOM   1212 C  CB  . GLN A 1 153 ? 22.653 -4.233  2.507   1.00 45.87  ? 152 GLN A CB  1 
ATOM   1213 C  CG  . GLN A 1 153 ? 21.736 -3.105  1.997   1.00 54.47  ? 152 GLN A CG  1 
ATOM   1214 C  CD  . GLN A 1 153 ? 22.377 -1.722  2.103   1.00 56.21  ? 152 GLN A CD  1 
ATOM   1215 O  OE1 . GLN A 1 153 ? 23.513 -1.506  1.692   1.00 52.86  ? 152 GLN A OE1 1 
ATOM   1216 N  NE2 . GLN A 1 153 ? 21.644 -0.789  2.691   1.00 71.86  ? 152 GLN A NE2 1 
ATOM   1217 N  N   . GLY A 1 154 ? 23.474 -3.227  5.994   1.00 45.98  ? 153 GLY A N   1 
ATOM   1218 C  CA  . GLY A 1 154 ? 22.818 -2.798  7.211   1.00 47.07  ? 153 GLY A CA  1 
ATOM   1219 C  C   . GLY A 1 154 ? 22.695 -1.282  7.219   1.00 47.54  ? 153 GLY A C   1 
ATOM   1220 O  O   . GLY A 1 154 ? 21.870 -0.745  7.992   1.00 48.11  ? 153 GLY A O   1 
ATOM   1221 O  OXT . GLY A 1 154 ? 23.431 -0.634  6.445   1.00 48.02  ? 153 GLY A OXT 1 
HETATM 1222 S  S   . SO4 B 2 .   ? 30.746 18.706  28.896  1.00 47.98  ? 157 SO4 A S   1 
HETATM 1223 O  O1  . SO4 B 2 .   ? 30.697 20.077  28.620  1.00 48.06  ? 157 SO4 A O1  1 
HETATM 1224 O  O2  . SO4 B 2 .   ? 31.104 18.021  27.725  1.00 47.52  ? 157 SO4 A O2  1 
HETATM 1225 O  O3  . SO4 B 2 .   ? 29.468 18.179  29.331  1.00 47.79  ? 157 SO4 A O3  1 
HETATM 1226 O  O4  . SO4 B 2 .   ? 31.722 18.578  29.881  1.00 47.85  ? 157 SO4 A O4  1 
HETATM 1227 C  CHA . HEM C 3 .   ? 38.056 2.293   11.078  1.00 21.35  ? 155 HEM A CHA 1 
HETATM 1228 C  CHB . HEM C 3 .   ? 37.306 5.212   7.384   1.00 18.29  ? 155 HEM A CHB 1 
HETATM 1229 C  CHC . HEM C 3 .   ? 32.964 6.205   9.051   1.00 16.45  ? 155 HEM A CHC 1 
HETATM 1230 C  CHD . HEM C 3 .   ? 33.598 3.200   12.667  1.00 19.12  ? 155 HEM A CHD 1 
HETATM 1231 C  C1A . HEM C 3 .   ? 38.286 2.995   9.925   1.00 21.23  ? 155 HEM A C1A 1 
HETATM 1232 C  C2A . HEM C 3 .   ? 39.557 3.037   9.214   1.00 21.38  ? 155 HEM A C2A 1 
HETATM 1233 C  C3A . HEM C 3 .   ? 39.302 3.871   8.151   1.00 20.28  ? 155 HEM A C3A 1 
HETATM 1234 C  C4A . HEM C 3 .   ? 37.919 4.323   8.239   1.00 19.51  ? 155 HEM A C4A 1 
HETATM 1235 C  CMA . HEM C 3 .   ? 40.314 4.221   7.055   1.00 18.93  ? 155 HEM A CMA 1 
HETATM 1236 C  CAA . HEM C 3 .   ? 40.877 2.216   9.299   1.00 23.71  ? 155 HEM A CAA 1 
HETATM 1237 C  CBA . HEM C 3 .   ? 41.015 0.742   8.951   1.00 26.45  ? 155 HEM A CBA 1 
HETATM 1238 C  CGA . HEM C 3 .   ? 39.678 0.033   8.861   1.00 28.72  ? 155 HEM A CGA 1 
HETATM 1239 O  O1A . HEM C 3 .   ? 39.251 -0.566  9.881   1.00 30.24  ? 155 HEM A O1A 1 
HETATM 1240 O  O2A . HEM C 3 .   ? 39.048 0.091   7.778   1.00 29.74  ? 155 HEM A O2A 1 
HETATM 1241 C  C1B . HEM C 3 .   ? 36.020 5.716   7.478   1.00 17.24  ? 155 HEM A C1B 1 
HETATM 1242 C  C2B . HEM C 3 .   ? 35.456 6.694   6.556   1.00 16.49  ? 155 HEM A C2B 1 
HETATM 1243 C  C3B . HEM C 3 .   ? 34.224 6.980   7.014   1.00 16.26  ? 155 HEM A C3B 1 
HETATM 1244 C  C4B . HEM C 3 .   ? 34.055 6.156   8.231   1.00 16.22  ? 155 HEM A C4B 1 
HETATM 1245 C  CMB . HEM C 3 .   ? 36.090 7.246   5.263   1.00 16.42  ? 155 HEM A CMB 1 
HETATM 1246 C  CAB . HEM C 3 .   ? 33.335 8.005   6.658   1.00 16.24  ? 155 HEM A CAB 1 
HETATM 1247 C  CBB . HEM C 3 .   ? 33.491 9.122   5.794   1.00 17.32  ? 155 HEM A CBB 1 
HETATM 1248 C  C1C . HEM C 3 .   ? 32.740 5.507   10.200  1.00 15.99  ? 155 HEM A C1C 1 
HETATM 1249 C  C2C . HEM C 3 .   ? 31.615 5.707   11.080  1.00 16.52  ? 155 HEM A C2C 1 
HETATM 1250 C  C3C . HEM C 3 .   ? 31.785 4.829   12.131  1.00 17.63  ? 155 HEM A C3C 1 
HETATM 1251 C  C4C . HEM C 3 .   ? 33.028 4.126   11.834  1.00 17.34  ? 155 HEM A C4C 1 
HETATM 1252 C  CMC . HEM C 3 .   ? 30.484 6.704   10.837  1.00 15.53  ? 155 HEM A CMC 1 
HETATM 1253 C  CAC . HEM C 3 .   ? 31.081 4.630   13.357  1.00 17.63  ? 155 HEM A CAC 1 
HETATM 1254 C  CBC . HEM C 3 .   ? 29.969 5.338   13.897  1.00 18.52  ? 155 HEM A CBC 1 
HETATM 1255 C  C1D . HEM C 3 .   ? 34.852 2.615   12.500  1.00 21.31  ? 155 HEM A C1D 1 
HETATM 1256 C  C2D . HEM C 3 .   ? 35.466 1.757   13.490  1.00 22.47  ? 155 HEM A C2D 1 
HETATM 1257 C  C3D . HEM C 3 .   ? 36.729 1.540   13.083  1.00 23.41  ? 155 HEM A C3D 1 
HETATM 1258 C  C4D . HEM C 3 .   ? 36.872 2.243   11.803  1.00 22.48  ? 155 HEM A C4D 1 
HETATM 1259 C  CMD . HEM C 3 .   ? 34.783 1.147   14.698  1.00 22.53  ? 155 HEM A CMD 1 
HETATM 1260 C  CAD . HEM C 3 .   ? 37.941 1.000   13.841  1.00 26.65  ? 155 HEM A CAD 1 
HETATM 1261 C  CBD . HEM C 3 .   ? 38.463 1.843   15.019  1.00 30.96  ? 155 HEM A CBD 1 
HETATM 1262 C  CGD . HEM C 3 .   ? 39.586 1.145   15.786  1.00 33.23  ? 155 HEM A CGD 1 
HETATM 1263 O  O1D . HEM C 3 .   ? 39.326 0.697   16.930  1.00 35.48  ? 155 HEM A O1D 1 
HETATM 1264 O  O2D . HEM C 3 .   ? 40.714 1.027   15.245  1.00 34.38  ? 155 HEM A O2D 1 
HETATM 1265 N  NA  . HEM C 3 .   ? 37.312 3.780   9.325   1.00 19.73  ? 155 HEM A NA  1 
HETATM 1266 N  NB  . HEM C 3 .   ? 35.132 5.385   8.500   1.00 17.06  ? 155 HEM A NB  1 
HETATM 1267 N  NC  . HEM C 3 .   ? 33.591 4.565   10.657  1.00 17.07  ? 155 HEM A NC  1 
HETATM 1268 N  ND  . HEM C 3 .   ? 35.728 2.887   11.451  1.00 21.03  ? 155 HEM A ND  1 
HETATM 1269 FE FE  . HEM C 3 .   ? 35.502 4.204   9.980   1.00 18.78  ? 155 HEM A FE  1 
HETATM 1270 C  C   . NBN D 4 .   ? 36.437 5.629   11.224  0.68 19.01  ? 156 NBN A C   1 
HETATM 1271 N  N   . NBN D 4 .   ? 36.674 6.332   11.970  0.68 19.66  ? 156 NBN A N   1 
HETATM 1272 C  C1  . NBN D 4 .   ? 37.691 6.621   13.103  0.68 19.98  ? 156 NBN A C1  1 
HETATM 1273 C  C2  . NBN D 4 .   ? 38.602 5.446   13.328  0.68 20.27  ? 156 NBN A C2  1 
HETATM 1274 C  C3  . NBN D 4 .   ? 39.713 5.441   12.363  0.68 20.94  ? 156 NBN A C3  1 
HETATM 1275 C  C4  . NBN D 4 .   ? 40.675 4.358   12.790  0.68 20.98  ? 156 NBN A C4  1 
HETATM 1276 O  O   . HOH E 5 .   ? 35.636 -2.996  15.255  0.36 12.26  ? 201 HOH A O   1 
HETATM 1277 O  O   . HOH E 5 .   ? 32.694 19.805  17.167  0.84 19.38  ? 202 HOH A O   1 
HETATM 1278 O  O   . HOH E 5 .   ? 26.221 14.314  13.400  0.89 28.18  ? 203 HOH A O   1 
HETATM 1279 O  O   . HOH E 5 .   ? 22.566 7.494   2.350   0.87 36.92  ? 204 HOH A O   1 
HETATM 1280 O  O   . HOH E 5 .   ? 30.932 6.438   -8.815  1.00 41.84  ? 205 HOH A O   1 
HETATM 1281 O  O   . HOH E 5 .   ? 24.541 30.283  6.889   0.63 25.58  ? 206 HOH A O   1 
HETATM 1282 O  O   . HOH E 5 .   ? 25.187 14.290  2.886   0.81 26.13  ? 207 HOH A O   1 
HETATM 1283 O  O   . HOH E 5 .   ? 22.103 13.723  1.959   0.96 26.43  ? 208 HOH A O   1 
HETATM 1284 O  O   . HOH E 5 .   ? 30.014 8.951   35.439  1.00 35.90  ? 209 HOH A O   1 
HETATM 1285 O  O   . HOH E 5 .   ? 30.631 11.672  35.807  0.93 21.70  ? 210 HOH A O   1 
HETATM 1286 O  O   . HOH E 5 .   ? 31.937 13.143  -12.160 1.00 17.10  ? 211 HOH A O   1 
HETATM 1287 O  O   . HOH E 5 .   ? 34.706 13.187  33.417  1.00 24.72  ? 212 HOH A O   1 
HETATM 1288 O  O   . HOH E 5 .   ? 35.965 30.906  4.862   0.88 25.13  ? 213 HOH A O   1 
HETATM 1289 O  O   . HOH E 5 .   ? 37.788 28.957  4.292   1.00 23.24  ? 214 HOH A O   1 
HETATM 1290 O  O   . HOH E 5 .   ? 47.139 19.251  7.852   1.00 21.52  ? 215 HOH A O   1 
HETATM 1291 O  O   . HOH E 5 .   ? 35.554 33.553  5.043   1.00 35.51  ? 216 HOH A O   1 
HETATM 1292 O  O   . HOH E 5 .   ? 45.287 12.661  -0.522  0.63 28.06  ? 217 HOH A O   1 
HETATM 1293 O  O   . HOH E 5 .   ? 22.243 26.519  -4.167  0.53 36.19  ? 218 HOH A O   1 
HETATM 1294 O  O   . HOH E 5 .   ? 34.356 25.644  -2.155  0.99 18.86  ? 219 HOH A O   1 
HETATM 1295 O  O   . HOH E 5 .   ? 43.314 5.775   14.083  0.83 33.75  ? 220 HOH A O   1 
HETATM 1296 O  O   . HOH E 5 .   ? 35.554 15.655  -13.704 0.69 27.98  ? 221 HOH A O   1 
HETATM 1297 O  O   . HOH E 5 .   ? 35.044 10.234  -5.370  1.00 16.54  ? 222 HOH A O   1 
HETATM 1298 O  O   . HOH E 5 .   ? 43.738 11.098  -7.107  0.70 39.04  ? 223 HOH A O   1 
HETATM 1299 O  O   . HOH E 5 .   ? 41.663 19.566  -2.545  0.71 29.09  ? 224 HOH A O   1 
HETATM 1300 O  O   . HOH E 5 .   ? 29.014 28.495  -2.787  1.00 22.71  ? 225 HOH A O   1 
HETATM 1301 O  O   . HOH E 5 .   ? 47.114 17.474  10.936  0.85 16.95  ? 226 HOH A O   1 
HETATM 1302 O  O   . HOH E 5 .   ? 49.157 23.679  7.865   0.45 6.24   ? 227 HOH A O   1 
HETATM 1303 O  O   . HOH E 5 .   ? 39.456 -6.272  0.390   0.45 18.39  ? 228 HOH A O   1 
HETATM 1304 O  O   . HOH E 5 .   ? 47.195 20.062  12.092  0.79 27.14  ? 229 HOH A O   1 
HETATM 1305 O  O   . HOH E 5 .   ? 41.694 14.434  14.419  0.64 19.99  ? 230 HOH A O   1 
HETATM 1306 O  O   . HOH E 5 .   ? 25.279 16.763  13.167  0.91 45.56  ? 231 HOH A O   1 
HETATM 1307 O  O   . HOH E 5 .   ? 27.502 6.144   24.003  0.34 12.97  ? 232 HOH A O   1 
HETATM 1308 O  O   . HOH E 5 .   ? 32.714 -1.677  16.431  0.37 7.65   ? 233 HOH A O   1 
HETATM 1309 O  O   . HOH E 5 .   ? 43.562 6.760   6.302   0.56 19.34  ? 234 HOH A O   1 
HETATM 1310 O  O   . HOH E 5 .   ? 26.622 30.313  -3.254  0.87 35.39  ? 235 HOH A O   1 
HETATM 1311 O  O   . HOH E 5 .   ? 43.770 12.412  1.711   0.89 19.03  ? 236 HOH A O   1 
HETATM 1312 O  O   . HOH E 5 .   ? 39.271 -4.219  4.681   0.55 22.84  ? 237 HOH A O   1 
HETATM 1313 O  O   . HOH E 5 .   ? 34.830 29.856  12.497  0.81 23.30  ? 238 HOH A O   1 
HETATM 1314 O  O   . HOH E 5 .   ? 42.908 14.832  3.150   1.00 41.54  ? 239 HOH A O   1 
HETATM 1315 O  O   . HOH E 5 .   ? 43.209 9.837   -4.230  0.92 19.85  ? 240 HOH A O   1 
HETATM 1316 O  O   . HOH E 5 .   ? 40.614 6.101   0.818   0.34 2.00   ? 241 HOH A O   1 
HETATM 1317 O  O   . HOH E 5 .   ? 40.042 10.664  -11.016 0.76 38.98  ? 242 HOH A O   1 
HETATM 1318 O  O   . HOH E 5 .   ? 40.074 3.074   1.213   0.83 38.72  ? 243 HOH A O   1 
HETATM 1319 O  O   . HOH E 5 .   ? 27.467 25.351  11.096  1.00 41.86  ? 244 HOH A O   1 
HETATM 1320 O  O   . HOH E 5 .   ? 31.263 30.732  11.225  1.00 34.25  ? 245 HOH A O   1 
HETATM 1321 O  O   . HOH E 5 .   ? 20.885 2.219   8.815   0.51 14.38  ? 246 HOH A O   1 
HETATM 1322 O  O   . HOH E 5 .   ? 19.343 15.372  1.025   0.88 50.46  ? 247 HOH A O   1 
HETATM 1323 O  O   . HOH E 5 .   ? 33.427 28.236  -3.034  1.00 44.12  ? 248 HOH A O   1 
HETATM 1324 O  O   . HOH E 5 .   ? 27.534 -10.802 -3.746  0.42 14.53  ? 249 HOH A O   1 
HETATM 1325 O  O   . HOH E 5 .   ? 24.801 -4.357  -4.615  0.37 9.21   ? 250 HOH A O   1 
HETATM 1326 O  O   . HOH E 5 .   ? 26.214 23.149  -6.451  1.00 27.31  ? 251 HOH A O   1 
HETATM 1327 O  O   . HOH E 5 .   ? 31.921 21.850  -1.051  0.56 24.04  ? 252 HOH A O   1 
HETATM 1328 O  O   . HOH E 5 .   ? 44.385 26.738  -0.823  1.00 39.65  ? 253 HOH A O   1 
HETATM 1329 O  O   . HOH E 5 .   ? 40.900 12.361  27.622  0.35 6.66   ? 254 HOH A O   1 
HETATM 1330 O  O   . HOH E 5 .   ? 44.897 21.387  15.094  0.51 19.22  ? 255 HOH A O   1 
HETATM 1331 O  O   . HOH E 5 .   ? 39.769 26.352  9.925   1.00 24.54  ? 256 HOH A O   1 
HETATM 1332 O  O   . HOH E 5 .   ? 28.113 30.114  4.349   0.73 32.35  ? 257 HOH A O   1 
HETATM 1333 O  O   . HOH E 5 .   ? 41.236 14.703  20.600  0.98 21.47  ? 258 HOH A O   1 
HETATM 1334 O  O   . HOH E 5 .   ? 27.920 12.176  23.647  0.45 25.64  ? 259 HOH A O   1 
HETATM 1335 O  O   . HOH E 5 .   ? 40.653 19.211  27.130  0.96 35.73  ? 260 HOH A O   1 
HETATM 1336 O  O   . HOH E 5 .   ? 38.995 12.758  33.007  0.56 26.01  ? 261 HOH A O   1 
HETATM 1337 O  O   . HOH E 5 .   ? 31.185 29.366  -1.418  0.92 29.20  ? 262 HOH A O   1 
HETATM 1338 O  O   . HOH E 5 .   ? 23.330 1.530   -3.772  0.93 38.08  ? 263 HOH A O   1 
HETATM 1339 O  O   . HOH E 5 .   ? 39.105 21.814  26.599  1.00 52.76  ? 264 HOH A O   1 
HETATM 1340 O  O   . HOH E 5 .   ? 28.047 -8.320  9.038   0.26 2.83   ? 265 HOH A O   1 
HETATM 1341 O  O   . HOH E 5 .   ? 20.727 9.658   17.232  1.00 40.20  ? 266 HOH A O   1 
HETATM 1342 O  O   . HOH E 5 .   ? 39.824 21.447  16.984  0.48 20.91  ? 267 HOH A O   1 
HETATM 1343 O  O   . HOH E 5 .   ? 31.109 21.510  30.969  0.78 27.35  ? 268 HOH A O   1 
HETATM 1344 O  O   . HOH E 5 .   ? 25.247 20.689  -6.664  0.53 13.05  ? 269 HOH A O   1 
HETATM 1345 O  O   . HOH E 5 .   ? 41.890 15.172  -7.575  0.63 23.24  ? 270 HOH A O   1 
HETATM 1346 O  O   . HOH E 5 .   ? 32.201 10.450  -3.509  0.82 32.30  ? 271 HOH A O   1 
HETATM 1347 O  O   . HOH E 5 .   ? 48.852 20.024  14.408  0.96 44.55  ? 272 HOH A O   1 
HETATM 1348 O  O   . HOH E 5 .   ? 45.087 10.967  -2.827  0.80 23.86  ? 273 HOH A O   1 
HETATM 1349 O  O   . HOH E 5 .   ? 43.790 6.366   -3.654  0.72 43.34  ? 274 HOH A O   1 
HETATM 1350 O  O   . HOH E 5 .   ? 36.756 24.689  15.999  0.85 45.09  ? 275 HOH A O   1 
HETATM 1351 O  O   . HOH E 5 .   ? 21.803 13.659  9.652   0.96 43.48  ? 276 HOH A O   1 
HETATM 1352 O  O   . HOH E 5 .   ? 20.646 5.769   15.588  0.37 15.34  ? 277 HOH A O   1 
HETATM 1353 O  O   . HOH E 5 .   ? 44.830 25.158  2.252   0.98 49.70  ? 278 HOH A O   1 
HETATM 1354 O  O   . HOH E 5 .   ? 32.937 25.419  -9.655  0.44 16.19  ? 279 HOH A O   1 
HETATM 1355 O  O   . HOH E 5 .   ? 28.152 27.732  -8.564  0.94 51.07  ? 280 HOH A O   1 
HETATM 1356 O  O   . HOH E 5 .   ? 35.196 30.717  -2.699  1.00 51.54  ? 281 HOH A O   1 
HETATM 1357 O  O   . HOH E 5 .   ? 33.436 19.536  28.293  0.81 30.59  ? 282 HOH A O   1 
HETATM 1358 O  O   . HOH E 5 .   ? 25.107 22.125  -10.155 0.55 34.20  ? 283 HOH A O   1 
HETATM 1359 O  O   . HOH E 5 .   ? 39.237 3.162   -8.262  1.00 34.85  ? 284 HOH A O   1 
HETATM 1360 O  O   . HOH E 5 .   ? 31.346 32.729  13.318  0.42 18.95  ? 285 HOH A O   1 
HETATM 1361 O  O   . HOH E 5 .   ? 36.519 -0.178  17.896  0.90 38.54  ? 286 HOH A O   1 
HETATM 1362 O  O   . HOH E 5 .   ? 38.564 2.732   18.719  0.55 17.78  ? 287 HOH A O   1 
HETATM 1363 O  O   . HOH E 5 .   ? 30.132 10.659  26.140  0.36 18.38  ? 288 HOH A O   1 
HETATM 1364 O  O   . HOH E 5 .   ? 36.854 4.464   -13.579 0.81 38.38  ? 289 HOH A O   1 
HETATM 1365 O  O   . HOH E 5 .   ? 27.373 5.340   -8.830  0.54 26.40  ? 290 HOH A O   1 
HETATM 1366 O  O   . HOH E 5 .   ? 32.075 1.884   -6.445  0.75 37.30  ? 291 HOH A O   1 
HETATM 1367 O  O   . HOH E 5 .   ? 40.784 -2.354  -4.023  0.29 12.31  ? 292 HOH A O   1 
HETATM 1368 O  O   . HOH E 5 .   ? 38.692 31.184  -2.441  0.66 32.11  ? 293 HOH A O   1 
HETATM 1369 O  O   . HOH E 5 .   ? 47.194 24.955  10.604  0.84 44.93  ? 294 HOH A O   1 
HETATM 1370 O  O   . HOH E 5 .   ? 34.034 31.418  14.962  0.52 36.13  ? 295 HOH A O   1 
HETATM 1371 O  O   . HOH E 5 .   ? 31.071 7.595   27.503  0.63 32.87  ? 296 HOH A O   1 
HETATM 1372 O  O   . HOH E 5 .   ? 33.788 23.237  30.704  0.64 39.14  ? 297 HOH A O   1 
HETATM 1373 O  O   . HOH E 5 .   ? 25.278 17.607  -12.018 0.56 32.27  ? 298 HOH A O   1 
HETATM 1374 O  O   . HOH E 5 .   ? 21.415 7.748   -8.816  0.48 29.69  ? 299 HOH A O   1 
HETATM 1375 O  O   . HOH E 5 .   ? 42.482 29.132  -3.537  0.48 27.61  ? 300 HOH A O   1 
HETATM 1376 O  O   . HOH E 5 .   ? 23.188 23.847  -3.514  0.46 25.13  ? 301 HOH A O   1 
HETATM 1377 O  O   . HOH E 5 .   ? 22.959 7.257   -2.133  0.76 43.13  ? 302 HOH A O   1 
HETATM 1378 O  O   . HOH E 5 .   ? 23.834 15.545  5.192   0.68 34.54  ? 303 HOH A O   1 
HETATM 1379 O  O   . HOH E 5 .   ? 39.887 -0.633  5.129   0.60 35.31  ? 304 HOH A O   1 
HETATM 1380 O  O   . HOH E 5 .   ? 29.072 -9.111  6.284   0.69 37.84  ? 305 HOH A O   1 
HETATM 1381 O  O   . HOH E 5 .   ? 21.916 1.326   6.785   0.72 42.32  ? 306 HOH A O   1 
HETATM 1382 O  O   . HOH E 5 .   ? 18.377 6.767   6.900   0.66 39.04  ? 307 HOH A O   1 
HETATM 1383 O  O   . HOH E 5 .   ? 46.391 8.895   7.898   0.50 25.35  ? 308 HOH A O   1 
HETATM 1384 O  O   . HOH E 5 .   ? 48.010 9.126   10.162  0.60 34.14  ? 309 HOH A O   1 
HETATM 1385 O  O   . HOH E 5 .   ? 30.229 20.017  18.925  0.66 31.75  ? 310 HOH A O   1 
HETATM 1386 O  O   . HOH E 5 .   ? 34.675 20.639  19.217  0.54 24.69  ? 311 HOH A O   1 
HETATM 1387 O  O   . HOH E 5 .   ? 28.518 11.760  28.729  0.28 27.00  ? 312 HOH A O   1 
HETATM 1388 O  O   . HOH E 5 .   ? 32.254 6.469   30.644  0.40 30.36  ? 313 HOH A O   1 
HETATM 1389 O  O   . HOH E 5 .   ? 40.742 5.881   -10.852 0.37 30.46  ? 314 HOH A O   1 
HETATM 1390 O  O   . HOH E 5 .   ? 27.168 23.526  -8.314  0.33 28.77  ? 315 HOH A O   1 
HETATM 1391 O  O   . HOH E 5 .   ? 28.521 -2.349  -7.024  0.32 28.33  ? 316 HOH A O   1 
HETATM 1392 O  O   . HOH E 5 .   ? 25.803 2.353   -6.384  0.31 28.65  ? 317 HOH A O   1 
HETATM 1393 O  O   . HOH E 5 .   ? 44.136 16.467  -6.383  0.34 29.36  ? 318 HOH A O   1 
HETATM 1394 O  O   . HOH E 5 .   ? 42.780 18.817  -5.108  0.27 27.67  ? 319 HOH A O   1 
HETATM 1395 O  O   . HOH E 5 .   ? 31.586 -2.955  -4.495  0.37 29.62  ? 320 HOH A O   1 
HETATM 1396 O  O   . HOH E 5 .   ? 22.068 -0.590  -3.191  0.34 28.19  ? 321 HOH A O   1 
HETATM 1397 O  O   . HOH E 5 .   ? 31.577 -4.125  -2.549  0.35 30.63  ? 322 HOH A O   1 
HETATM 1398 O  O   . HOH E 5 .   ? 40.063 -4.705  -1.916  0.31 30.62  ? 323 HOH A O   1 
HETATM 1399 O  O   . HOH E 5 .   ? 40.744 30.579  -1.276  0.42 31.10  ? 324 HOH A O   1 
HETATM 1400 O  O   . HOH E 5 .   ? 22.633 -4.018  0.119   0.49 32.42  ? 325 HOH A O   1 
HETATM 1401 O  O   . HOH E 5 .   ? 39.728 -6.468  2.562   0.39 28.33  ? 326 HOH A O   1 
HETATM 1402 O  O   . HOH E 5 .   ? 23.766 17.652  5.748   0.36 30.42  ? 327 HOH A O   1 
HETATM 1403 O  O   . HOH E 5 .   ? 23.087 12.937  6.384   0.29 26.48  ? 328 HOH A O   1 
HETATM 1404 O  O   . HOH E 5 .   ? 22.747 -7.645  7.662   0.25 25.89  ? 329 HOH A O   1 
HETATM 1405 O  O   . HOH E 5 .   ? 19.691 9.411   8.942   0.25 28.30  ? 330 HOH A O   1 
HETATM 1406 O  O   . HOH E 5 .   ? 29.536 29.990  9.576   0.30 29.08  ? 331 HOH A O   1 
HETATM 1407 O  O   . HOH E 5 .   ? 45.870 26.406  8.824   0.07 28.54  ? 332 HOH A O   1 
HETATM 1408 O  O   . HOH E 5 .   ? 45.836 8.820   12.130  0.38 28.79  ? 333 HOH A O   1 
HETATM 1409 O  O   . HOH E 5 .   ? 19.316 5.243   12.172  0.36 28.54  ? 334 HOH A O   1 
HETATM 1410 O  O   . HOH E 5 .   ? 48.889 17.640  14.045  0.39 30.76  ? 335 HOH A O   1 
HETATM 1411 O  O   . HOH E 5 .   ? 34.630 23.523  14.046  0.26 26.99  ? 336 HOH A O   1 
HETATM 1412 O  O   . HOH E 5 .   ? 25.803 18.817  18.514  0.38 33.79  ? 337 HOH A O   1 
HETATM 1413 O  O   . HOH E 5 .   ? 31.249 21.185  20.442  0.36 29.67  ? 338 HOH A 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   MET 1   0   0   MET MET A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   SER 4   3   3   SER SER A . n 
A 1 5   GLU 5   4   4   GLU GLU A . n 
A 1 6   GLY 6   5   5   GLY GLY A . n 
A 1 7   GLU 7   6   6   GLU GLU A . n 
A 1 8   TRP 8   7   7   TRP TRP A . n 
A 1 9   GLN 9   8   8   GLN GLN A . n 
A 1 10  LEU 10  9   9   LEU LEU A . n 
A 1 11  VAL 11  10  10  VAL VAL A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  HIS 13  12  12  HIS HIS A . n 
A 1 14  VAL 14  13  13  VAL VAL A . n 
A 1 15  TRP 15  14  14  TRP TRP A . n 
A 1 16  ALA 16  15  15  ALA ALA A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  VAL 18  17  17  VAL VAL A . n 
A 1 19  GLU 19  18  18  GLU GLU A . n 
A 1 20  ALA 20  19  19  ALA ALA A . n 
A 1 21  ASP 21  20  20  ASP ASP A . n 
A 1 22  VAL 22  21  21  VAL VAL A . n 
A 1 23  ALA 23  22  22  ALA ALA A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  HIS 25  24  24  HIS HIS A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  GLN 27  26  26  GLN GLN A . n 
A 1 28  ASP 28  27  27  ASP ASP A . n 
A 1 29  ILE 29  28  28  ILE ILE A . n 
A 1 30  LEU 30  29  29  LEU LEU A . n 
A 1 31  ILE 31  30  30  ILE ILE A . n 
A 1 32  ARG 32  31  31  ARG ARG A . n 
A 1 33  LEU 33  32  32  LEU LEU A . n 
A 1 34  PHE 34  33  33  PHE PHE A . n 
A 1 35  LYS 35  34  34  LYS LYS A . n 
A 1 36  SER 36  35  35  SER SER A . n 
A 1 37  HIS 37  36  36  HIS HIS A . n 
A 1 38  PRO 38  37  37  PRO PRO A . n 
A 1 39  GLU 39  38  38  GLU GLU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  LEU 41  40  40  LEU LEU A . n 
A 1 42  GLU 42  41  41  GLU GLU A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  PHE 44  43  43  PHE PHE A . n 
A 1 45  ASP 45  44  44  ASP ASP A . n 
A 1 46  ARG 46  45  45  ARG ARG A . n 
A 1 47  VAL 47  46  46  VAL VAL A . n 
A 1 48  LYS 48  47  47  LYS LYS A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  LEU 50  49  49  LEU LEU A . n 
A 1 51  LYS 51  50  50  LYS LYS A . n 
A 1 52  THR 52  51  51  THR THR A . n 
A 1 53  GLU 53  52  52  GLU GLU A . n 
A 1 54  ALA 54  53  53  ALA ALA A . n 
A 1 55  GLU 55  54  54  GLU GLU A . n 
A 1 56  MET 56  55  55  MET MET A . n 
A 1 57  LYS 57  56  56  LYS LYS A . n 
A 1 58  ALA 58  57  57  ALA ALA A . n 
A 1 59  SER 59  58  58  SER SER A . n 
A 1 60  GLU 60  59  59  GLU GLU A . n 
A 1 61  ASP 61  60  60  ASP ASP A . n 
A 1 62  LEU 62  61  61  LEU LEU A . n 
A 1 63  LYS 63  62  62  LYS LYS A . n 
A 1 64  LYS 64  63  63  LYS LYS A . n 
A 1 65  HIS 65  64  64  HIS HIS A . n 
A 1 66  GLY 66  65  65  GLY GLY A . n 
A 1 67  VAL 67  66  66  VAL VAL A . n 
A 1 68  THR 68  67  67  THR THR A . n 
A 1 69  VAL 69  68  68  VAL VAL A . n 
A 1 70  LEU 70  69  69  LEU LEU A . n 
A 1 71  THR 71  70  70  THR THR A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  LEU 73  72  72  LEU LEU A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  ALA 75  74  74  ALA ALA A . n 
A 1 76  ILE 76  75  75  ILE ILE A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  LYS 78  77  77  LYS LYS A . n 
A 1 79  LYS 79  78  78  LYS LYS A . n 
A 1 80  LYS 80  79  79  LYS LYS A . n 
A 1 81  GLY 81  80  80  GLY GLY A . n 
A 1 82  HIS 82  81  81  HIS HIS A . n 
A 1 83  HIS 83  82  82  HIS HIS A . n 
A 1 84  GLU 84  83  83  GLU GLU A . n 
A 1 85  ALA 85  84  84  ALA ALA A . n 
A 1 86  GLU 86  85  85  GLU GLU A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  LYS 88  87  87  LYS LYS A . n 
A 1 89  PRO 89  88  88  PRO PRO A . n 
A 1 90  LEU 90  89  89  LEU LEU A . n 
A 1 91  ALA 91  90  90  ALA ALA A . n 
A 1 92  GLN 92  91  91  GLN GLN A . n 
A 1 93  SER 93  92  92  SER SER A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  ALA 95  94  94  ALA ALA A . n 
A 1 96  THR 96  95  95  THR THR A . n 
A 1 97  LYS 97  96  96  LYS LYS A . n 
A 1 98  HIS 98  97  97  HIS HIS A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 PRO 101 100 100 PRO PRO A . n 
A 1 102 ILE 102 101 101 ILE ILE A . n 
A 1 103 LYS 103 102 102 LYS LYS A . n 
A 1 104 TYR 104 103 103 TYR TYR A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 GLU 106 105 105 GLU GLU A . n 
A 1 107 PHE 107 106 106 PHE PHE A . n 
A 1 108 ILE 108 107 107 ILE ILE A . n 
A 1 109 SER 109 108 108 SER SER A . n 
A 1 110 GLU 110 109 109 GLU GLU A . n 
A 1 111 ALA 111 110 110 ALA ALA A . n 
A 1 112 ILE 112 111 111 ILE ILE A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 HIS 114 113 113 HIS HIS A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 HIS 117 116 116 HIS HIS A . n 
A 1 118 SER 118 117 117 SER SER A . n 
A 1 119 ARG 119 118 118 ARG ARG A . n 
A 1 120 HIS 120 119 119 HIS HIS A . n 
A 1 121 PRO 121 120 120 PRO PRO A . n 
A 1 122 GLY 122 121 121 GLY GLY A . n 
A 1 123 ASN 123 122 122 ASN ASN A . n 
A 1 124 PHE 124 123 123 PHE PHE A . n 
A 1 125 GLY 125 124 124 GLY GLY A . n 
A 1 126 ALA 126 125 125 ALA ALA A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 ALA 128 127 127 ALA ALA A . n 
A 1 129 GLN 129 128 128 GLN GLN A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 MET 132 131 131 MET MET A . n 
A 1 133 ASN 133 132 132 ASN ASN A . n 
A 1 134 LYS 134 133 133 LYS LYS A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 LEU 136 135 135 LEU LEU A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 LEU 138 137 137 LEU LEU A . n 
A 1 139 PHE 139 138 138 PHE PHE A . n 
A 1 140 ARG 140 139 139 ARG ARG A . n 
A 1 141 LYS 141 140 140 LYS LYS A . n 
A 1 142 ASP 142 141 141 ASP ASP A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 ALA 144 143 143 ALA ALA A . n 
A 1 145 ALA 145 144 144 ALA ALA A . n 
A 1 146 LYS 146 145 145 LYS LYS A . n 
A 1 147 TYR 147 146 146 TYR TYR A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 GLU 149 148 148 GLU GLU A . n 
A 1 150 LEU 150 149 149 LEU LEU A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 TYR 152 151 151 TYR TYR A . n 
A 1 153 GLN 153 152 152 GLN GLN A . n 
A 1 154 GLY 154 153 153 GLY GLY A . 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 
B 2 SO4 1   157 157 SO4 SO4 A . 
C 3 HEM 1   155 155 HEM HEM A . 
D 4 NBN 1   156 156 NBN NBN A . 
E 5 HOH 1   201 201 HOH HOH A . 
E 5 HOH 2   202 202 HOH HOH A . 
E 5 HOH 3   203 203 HOH HOH A . 
E 5 HOH 4   204 204 HOH HOH A . 
E 5 HOH 5   205 205 HOH HOH A . 
E 5 HOH 6   206 206 HOH HOH A . 
E 5 HOH 7   207 207 HOH HOH A . 
E 5 HOH 8   208 208 HOH HOH A . 
E 5 HOH 9   209 209 HOH HOH A . 
E 5 HOH 10  210 210 HOH HOH A . 
E 5 HOH 11  211 211 HOH HOH A . 
E 5 HOH 12  212 212 HOH HOH A . 
E 5 HOH 13  213 213 HOH HOH A . 
E 5 HOH 14  214 214 HOH HOH A . 
E 5 HOH 15  215 215 HOH HOH A . 
E 5 HOH 16  216 216 HOH HOH A . 
E 5 HOH 17  217 217 HOH HOH A . 
E 5 HOH 18  218 218 HOH HOH A . 
E 5 HOH 19  219 219 HOH HOH A . 
E 5 HOH 20  220 220 HOH HOH A . 
E 5 HOH 21  221 221 HOH HOH A . 
E 5 HOH 22  222 222 HOH HOH A . 
E 5 HOH 23  223 223 HOH HOH A . 
E 5 HOH 24  224 224 HOH HOH A . 
E 5 HOH 25  225 225 HOH HOH A . 
E 5 HOH 26  226 226 HOH HOH A . 
E 5 HOH 27  227 227 HOH HOH A . 
E 5 HOH 28  228 228 HOH HOH A . 
E 5 HOH 29  229 229 HOH HOH A . 
E 5 HOH 30  230 230 HOH HOH A . 
E 5 HOH 31  231 231 HOH HOH A . 
E 5 HOH 32  232 232 HOH HOH A . 
E 5 HOH 33  233 233 HOH HOH A . 
E 5 HOH 34  234 234 HOH HOH A . 
E 5 HOH 35  235 235 HOH HOH A . 
E 5 HOH 36  236 236 HOH HOH A . 
E 5 HOH 37  237 237 HOH HOH A . 
E 5 HOH 38  238 238 HOH HOH A . 
E 5 HOH 39  239 239 HOH HOH A . 
E 5 HOH 40  240 240 HOH HOH A . 
E 5 HOH 41  241 241 HOH HOH A . 
E 5 HOH 42  242 242 HOH HOH A . 
E 5 HOH 43  243 243 HOH HOH A . 
E 5 HOH 44  244 244 HOH HOH A . 
E 5 HOH 45  245 245 HOH HOH A . 
E 5 HOH 46  246 246 HOH HOH A . 
E 5 HOH 47  247 247 HOH HOH A . 
E 5 HOH 48  248 248 HOH HOH A . 
E 5 HOH 49  249 249 HOH HOH A . 
E 5 HOH 50  250 250 HOH HOH A . 
E 5 HOH 51  251 251 HOH HOH A . 
E 5 HOH 52  252 252 HOH HOH A . 
E 5 HOH 53  253 253 HOH HOH A . 
E 5 HOH 54  254 254 HOH HOH A . 
E 5 HOH 55  255 255 HOH HOH A . 
E 5 HOH 56  256 256 HOH HOH A . 
E 5 HOH 57  257 257 HOH HOH A . 
E 5 HOH 58  258 258 HOH HOH A . 
E 5 HOH 59  259 259 HOH HOH A . 
E 5 HOH 60  260 260 HOH HOH A . 
E 5 HOH 61  261 261 HOH HOH A . 
E 5 HOH 62  262 262 HOH HOH A . 
E 5 HOH 63  263 263 HOH HOH A . 
E 5 HOH 64  264 264 HOH HOH A . 
E 5 HOH 65  265 265 HOH HOH A . 
E 5 HOH 66  266 266 HOH HOH A . 
E 5 HOH 67  267 267 HOH HOH A . 
E 5 HOH 68  268 268 HOH HOH A . 
E 5 HOH 69  269 269 HOH HOH A . 
E 5 HOH 70  270 270 HOH HOH A . 
E 5 HOH 71  271 271 HOH HOH A . 
E 5 HOH 72  272 272 HOH HOH A . 
E 5 HOH 73  273 273 HOH HOH A . 
E 5 HOH 74  274 274 HOH HOH A . 
E 5 HOH 75  275 275 HOH HOH A . 
E 5 HOH 76  276 276 HOH HOH A . 
E 5 HOH 77  277 277 HOH HOH A . 
E 5 HOH 78  278 278 HOH HOH A . 
E 5 HOH 79  279 279 HOH HOH A . 
E 5 HOH 80  280 280 HOH HOH A . 
E 5 HOH 81  281 281 HOH HOH A . 
E 5 HOH 82  282 282 HOH HOH A . 
E 5 HOH 83  283 283 HOH HOH A . 
E 5 HOH 84  284 284 HOH HOH A . 
E 5 HOH 85  285 285 HOH HOH A . 
E 5 HOH 86  286 286 HOH HOH A . 
E 5 HOH 87  287 287 HOH HOH A . 
E 5 HOH 88  288 288 HOH HOH A . 
E 5 HOH 89  289 289 HOH HOH A . 
E 5 HOH 90  290 290 HOH HOH A . 
E 5 HOH 91  291 291 HOH HOH A . 
E 5 HOH 92  292 292 HOH HOH A . 
E 5 HOH 93  293 293 HOH HOH A . 
E 5 HOH 94  294 294 HOH HOH A . 
E 5 HOH 95  295 295 HOH HOH A . 
E 5 HOH 96  296 296 HOH HOH A . 
E 5 HOH 97  297 297 HOH HOH A . 
E 5 HOH 98  298 298 HOH HOH A . 
E 5 HOH 99  299 299 HOH HOH A . 
E 5 HOH 100 300 300 HOH HOH A . 
E 5 HOH 101 301 301 HOH HOH A . 
E 5 HOH 102 302 302 HOH HOH A . 
E 5 HOH 103 303 303 HOH HOH A . 
E 5 HOH 104 304 304 HOH HOH A . 
E 5 HOH 105 305 305 HOH HOH A . 
E 5 HOH 106 306 306 HOH HOH A . 
E 5 HOH 107 307 307 HOH HOH A . 
E 5 HOH 108 308 308 HOH HOH A . 
E 5 HOH 109 309 309 HOH HOH A . 
E 5 HOH 110 310 310 HOH HOH A . 
E 5 HOH 111 311 311 HOH HOH A . 
E 5 HOH 112 312 312 HOH HOH A . 
E 5 HOH 113 313 313 HOH HOH A . 
E 5 HOH 114 314 314 HOH HOH A . 
E 5 HOH 115 315 315 HOH HOH A . 
E 5 HOH 116 316 316 HOH HOH A . 
E 5 HOH 117 317 317 HOH HOH A . 
E 5 HOH 118 318 318 HOH HOH A . 
E 5 HOH 119 319 319 HOH HOH A . 
E 5 HOH 120 320 320 HOH HOH A . 
E 5 HOH 121 321 321 HOH HOH A . 
E 5 HOH 122 322 322 HOH HOH A . 
E 5 HOH 123 323 323 HOH HOH A . 
E 5 HOH 124 324 324 HOH HOH A . 
E 5 HOH 125 325 325 HOH HOH A . 
E 5 HOH 126 326 326 HOH HOH A . 
E 5 HOH 127 327 327 HOH HOH A . 
E 5 HOH 128 328 328 HOH HOH A . 
E 5 HOH 129 329 329 HOH HOH A . 
E 5 HOH 130 330 330 HOH HOH A . 
E 5 HOH 131 331 331 HOH HOH A . 
E 5 HOH 132 332 332 HOH HOH A . 
E 5 HOH 133 333 333 HOH HOH A . 
E 5 HOH 134 334 334 HOH HOH A . 
E 5 HOH 135 335 335 HOH HOH A . 
E 5 HOH 136 336 336 HOH HOH A . 
E 5 HOH 137 337 337 HOH HOH A . 
E 5 HOH 138 338 338 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     332 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NA ? C HEM . ? A HEM 155 ? 1_555 89.5  ? 
2  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NB ? C HEM . ? A HEM 155 ? 1_555 83.7  ? 
3  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NB ? C HEM . ? A HEM 155 ? 1_555 93.0  ? 
4  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 88.6  ? 
5  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 177.6 ? 
6  NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 88.1  ? 
7  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 91.6  ? 
8  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 89.9  ? 
9  NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 174.5 ? 
10 NC  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 88.8  ? 
11 NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 C  ? D NBN . ? A NBN 156 ? 1_555 175.7 ? 
12 NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 C  ? D NBN . ? A NBN 156 ? 1_555 86.2  ? 
13 NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 C  ? D NBN . ? A NBN 156 ? 1_555 97.1  ? 
14 NC  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 C  ? D NBN . ? A NBN 156 ? 1_555 95.7  ? 
15 ND  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 C  ? D NBN . ? A NBN 156 ? 1_555 87.8  ? 
# 
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 1998-04-08 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2018-03-07 
5 'Structure model' 1 4 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' 'Data collection'           
4 4 'Structure model' Other                       
5 5 'Structure model' 'Database references'       
6 5 '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' diffrn_source        
2 4 'Structure model' pdbx_database_status 
3 5 'Structure model' database_2           
4 5 'Structure model' struct_conn          
5 5 'Structure model' struct_ref_seq_dif   
6 5 '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' '_diffrn_source.source'               
2  4 'Structure model' '_pdbx_database_status.process_site'  
3  5 'Structure model' '_database_2.pdbx_DOI'                
4  5 'Structure model' '_database_2.pdbx_database_accession' 
5  5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  5 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  5 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  5 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
12 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
13 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
14 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
15 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
16 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'     
17 5 'Structure model' '_struct_ref_seq_dif.details'         
18 5 'Structure model' '_struct_site.pdbx_auth_asym_id'      
19 5 'Structure model' '_struct_site.pdbx_auth_comp_id'      
20 5 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
X-PLOR 'model building' 3.851 ? 1 
X-PLOR refinement       3.851 ? 2 
XDS    'data reduction' .     ? 3 
XSCALE 'data scaling'   .     ? 4 
X-PLOR phasing          3.851 ? 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 ASP A 20  ? ? -151.70 75.97  
2 1 LYS A 98  ? ? 56.03   70.18  
3 1 TYR A 151 ? ? -108.10 -71.27 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                     SO4 
3 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
4 'N-BUTYL ISOCYANIDE'              NBN 
5 water                             HOH 
# 
