data_1N19
# 
_entry.id   1N19 
# 
_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   1N19         pdb_00001n19 10.2210/pdb1n19/pdb 
RCSB  RCSB017392   ?            ?                   
WWPDB D_1000017392 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1N18 
_pdbx_database_related.details        'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A, C111S' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1N19 
_pdbx_database_status.recvd_initial_deposition_date   2002-10-16 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Cardoso, R.M.F.' 1 
'Thayer, M.M.'    2 
'DiDonato, M.'    3 
'Lo, T.P.'        4 
'Bruns, C.K.'     5 
'Getzoff, E.D.'   6 
'Tainer, J.A.'    7 
# 
_citation.id                        primary 
_citation.title                     
;Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase.
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            324 
_citation.page_first                247 
_citation.page_last                 256 
_citation.year                      2002 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12441104 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(02)01090-2' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cardoso, R.M.F.' 1 ? 
primary 'Thayer, M.M.'    2 ? 
primary 'DiDonato, M.'    3 ? 
primary 'Lo, T.P.'        4 ? 
primary 'Bruns, C.K.'     5 ? 
primary 'Getzoff, E.D.'   6 ? 
primary 'Tainer, J.A.'    7 ? 
# 
_cell.entry_id           1N19 
_cell.length_a           114.700 
_cell.length_b           47.900 
_cell.length_c           56.200 
_cell.angle_alpha        90.00 
_cell.angle_beta         96.80 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1N19 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide Dismutase [Cu-Zn]' 15938.681 2   1.15.1.1 'A4V, C6A, C111S' ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    2   ?        ?                 ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    2   ?        ?                 ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    1   ?        ?                 ? ? 
5 water       nat water                          18.015    262 ?        ?                 ? ? 
# 
_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       
;MATKVVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKVVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   VAL n 
1 6   VAL n 
1 7   ALA n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 SER n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     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               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           0 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1N19 A 1 ? 154 ? P00441 0 ? 153 ? 0 153 
2 1 1N19 B 1 ? 154 ? P00441 0 ? 153 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1N19 VAL A 5   ? UNP P00441 ALA 4   'engineered mutation' 4   1 
1 1N19 ALA A 7   ? UNP P00441 CYS 6   'engineered mutation' 6   2 
1 1N19 SER A 112 ? UNP P00441 CYS 111 'engineered mutation' 111 3 
2 1N19 VAL B 5   ? UNP P00441 ALA 4   'engineered mutation' 4   4 
2 1N19 ALA B 7   ? UNP P00441 CYS 6   'engineered mutation' 6   5 
2 1N19 SER B 112 ? UNP P00441 CYS 111 'engineered mutation' 111 6 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ? 'C4 H7 N O4'     133.103 
CU1 non-polymer         . 'COPPER (I) ION' ? 'Cu 1'           63.546  
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE       ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'    ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'       ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1N19 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.40 
_exptl_crystal.density_percent_sol   48.83 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    'ammonium sulfate, NaCl, Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           90 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1999-08-11 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL7-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL7-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.08 
# 
_reflns.entry_id                     1N19 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             27.9 
_reflns.d_resolution_high            1.8 
_reflns.number_obs                   23675 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         84.0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.058 
_reflns.pdbx_netI_over_sigmaI        17.7 
_reflns.B_iso_Wilson_estimate        19.3 
_reflns.pdbx_redundancy              3.3 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.83 
_reflns_shell.percent_possible_all   45.2 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.393 
_reflns_shell.meanI_over_sigI_obs    1.57 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1N19 
_refine.ls_number_reflns_obs                     22597 
_refine.ls_number_reflns_all                     22597 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             27.90 
_refine.ls_d_res_high                            1.86 
_refine.ls_percent_reflns_obs                    87.9 
_refine.ls_R_factor_obs                          0.207 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.207 
_refine.ls_R_factor_R_free                       0.26 
_refine.ls_R_factor_R_free_error                 0.006 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 7.1 
_refine.ls_number_reflns_R_free                  1598 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               43.3 
_refine.aniso_B[1][1]                            5.58 
_refine.aniso_B[2][2]                            6.40 
_refine.aniso_B[3][3]                            -11.98 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            12.73 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.371032 
_refine.solvent_model_param_bsol                 65.923 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_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_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_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                        1N19 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             0.34 
_refine_analyze.Luzzati_d_res_low_obs           5 
_refine_analyze.Luzzati_coordinate_error_free   0.32 
_refine_analyze.Luzzati_sigma_a_free            0.36 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2222 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_refine_hist.number_atoms_solvent             262 
_refine_hist.number_atoms_total               2493 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        27.90 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.005 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      24.9  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.69  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.38  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.19  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             1.97  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            2.81  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.86 
_refine_ls_shell.d_res_low                        1.98 
_refine_ls_shell.number_reflns_R_work             2502 
_refine_ls_shell.R_factor_R_work                  0.34 
_refine_ls_shell.percent_reflns_obs               63.8 
_refine_ls_shell.R_factor_R_free                  0.361 
_refine_ls_shell.R_factor_R_free_error            0.025 
_refine_ls_shell.percent_reflns_R_free            7.7 
_refine_ls_shell.number_reflns_R_free             209 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_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 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 
2 ION.PARAM         ?           'X-RAY DIFFRACTION' 
3 WATER_REP.PARAM   ?           'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1N19 
_struct.title                     'Structure of the HSOD A4V mutant' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1N19 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'Greek Key beta-barrel, oxidoreductase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 SER A 108 ? SER A 112 ? SER A 107 SER A 111 5 ? 5 
HELX_P HELX_P3 3 GLU A 134 ? GLY A 139 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P4 4 CYS B 58  ? GLY B 62  ? CYS B 57  GLY B 61  5 ? 5 
HELX_P HELX_P5 5 ASN B 132 ? LYS B 137 ? ASN B 131 LYS B 136 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 58  SG  ? ? ? 1_555 A CYS 147 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
disulf2  disulf ? ? B CYS 58  SG  ? ? ? 1_555 B CYS 147 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc1  metalc ? ? A HIS 47  ND1 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 46  A CU1 154 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc2  metalc ? ? A HIS 49  NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 48  A CU1 154 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc3  metalc ? ? A HIS 64  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  155 1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc4  metalc ? ? A HIS 72  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  155 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc5  metalc ? ? A HIS 81  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  155 1_555 ? ? ? ? ? ? ? 1.868 ? ? 
metalc6  metalc ? ? A ASP 84  OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  155 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc7  metalc ? ? A HIS 121 NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 120 A CU1 154 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc8  metalc ? ? B HIS 47  ND1 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 46  B CU1 154 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
metalc9  metalc ? ? B HIS 49  NE2 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 48  B CU1 154 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc10 metalc ? ? B HIS 64  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 63  B ZN  155 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc11 metalc ? ? B HIS 72  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 71  B ZN  155 1_555 ? ? ? ? ? ? ? 1.893 ? ? 
metalc12 metalc ? ? B HIS 81  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 80  B ZN  155 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc13 metalc ? ? B ASP 84  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
metalc14 metalc ? ? B ASP 84  OD2 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 2.600 ? ? 
metalc15 metalc ? ? B HIS 121 NE2 ? ? ? 1_555 E CU1 .   CU ? ? B HIS 120 B CU1 154 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
A 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
A 3 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
A 4 LYS A 4   ? LEU A 9   ? LYS A 3   LEU A 8   
A 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
B 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
B 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
B 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
B 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
C 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
C 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
C 3 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
C 4 LYS B 4   ? LYS B 10  ? LYS B 3   LYS B 9   
C 5 GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
D 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
D 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
D 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
D 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ASP A 102 ? O ASP A 101 N VAL A 30  ? N VAL A 29  
A 2 3 O TRP A 33  ? O TRP A 32  N ASN A 20  ? N ASN A 19  
A 3 4 O PHE A 21  ? O PHE A 20  N VAL A 5   ? N VAL A 4   
A 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
B 1 2 O ALA A 90  ? O ALA A 89  N GLY A 42  ? N GLY A 41  
B 2 3 N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
B 3 4 N LEU A 118 ? N LEU A 117 O GLY A 148 ? O GLY A 147 
C 1 2 O ILE B 100 ? O ILE B 99  N VAL B 32  ? N VAL B 31  
C 2 3 O TRP B 33  ? O TRP B 32  N ASN B 20  ? N ASN B 19  
C 3 4 O PHE B 21  ? O PHE B 20  N VAL B 5   ? N VAL B 4   
C 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
D 1 2 O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
D 2 3 N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
D 3 4 N LEU B 118 ? N LEU B 117 O GLY B 148 ? O GLY B 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A CU1 154 ? 4 'BINDING SITE FOR RESIDUE CU1 A 154' 
AC2 Software A ZN  155 ? 4 'BINDING SITE FOR RESIDUE ZN A 155'  
AC3 Software B CU1 154 ? 4 'BINDING SITE FOR RESIDUE CU1 B 154' 
AC4 Software B ZN  155 ? 4 'BINDING SITE FOR RESIDUE ZN B 155'  
AC5 Software B SO4 300 ? 6 'BINDING SITE FOR RESIDUE SO4 B 300' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 47  ? HIS A 46  . ? 1_555 ? 
2  AC1 4 HIS A 49  ? HIS A 48  . ? 1_555 ? 
3  AC1 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
4  AC1 4 HIS A 121 ? HIS A 120 . ? 1_555 ? 
5  AC2 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
6  AC2 4 HIS A 72  ? HIS A 71  . ? 1_555 ? 
7  AC2 4 HIS A 81  ? HIS A 80  . ? 1_555 ? 
8  AC2 4 ASP A 84  ? ASP A 83  . ? 1_555 ? 
9  AC3 4 HIS B 47  ? HIS B 46  . ? 1_555 ? 
10 AC3 4 HIS B 49  ? HIS B 48  . ? 1_555 ? 
11 AC3 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
12 AC3 4 HIS B 121 ? HIS B 120 . ? 1_555 ? 
13 AC4 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
14 AC4 4 HIS B 72  ? HIS B 71  . ? 1_555 ? 
15 AC4 4 HIS B 81  ? HIS B 80  . ? 1_555 ? 
16 AC4 4 ASP B 84  ? ASP B 83  . ? 1_555 ? 
17 AC5 6 HOH H .   ? HOH A 269 . ? 4_545 ? 
18 AC5 6 GLY B 109 ? GLY B 108 . ? 1_555 ? 
19 AC5 6 ASP B 110 ? ASP B 109 . ? 1_555 ? 
20 AC5 6 GLY B 131 ? GLY B 130 . ? 4_546 ? 
21 AC5 6 HOH I .   ? HOH B 321 . ? 1_555 ? 
22 AC5 6 HOH I .   ? HOH B 362 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1N19 
_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                    1N19 
_atom_sites.fract_transf_matrix[1][1]   0.008718 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001040 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020877 
_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]   0.017920 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 2   ? 28.734 -5.089  7.213   1.00 55.36 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 2   ? 27.596 -5.741  6.498   1.00 54.99 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 2   ? 27.655 -5.469  4.999   1.00 52.89 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 2   ? 28.442 -6.083  4.285   1.00 53.59 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 2   ? 26.264 -5.242  7.069   1.00 57.60 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 3   ? 26.824 -4.544  4.529   1.00 50.06 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 3   ? 26.782 -4.206  3.113   1.00 46.38 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 3   ? 27.498 -2.891  2.813   1.00 44.78 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 3   ? 27.740 -2.565  1.654   1.00 43.52 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 3   ? 25.321 -4.097  2.605   1.00 47.76 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 3   ? 24.693 -2.941  3.178   1.00 47.15 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 3   ? 24.525 -5.340  3.005   1.00 49.55 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 4   ? 27.831 -2.128  3.848   1.00 43.38 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 4   ? 28.524 -0.859  3.633   1.00 42.93 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 4   ? 29.720 -0.670  4.563   1.00 41.20 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 4   ? 29.608 -0.835  5.776   1.00 40.83 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 4   ? 27.577 0.329   3.837   1.00 45.15 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 4   ? 26.220 0.220   3.168   1.00 49.96 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 4   ? 25.432 1.514   3.365   1.00 52.95 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 4   ? 23.996 1.407   2.862   1.00 56.45 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 4   ? 23.162 0.500   3.703   1.00 57.19 ? 3   LYS A NZ  1 
ATOM   22   N  N   . VAL A 1 5   ? 30.868 -0.330  3.989   1.00 38.29 ? 4   VAL A N   1 
ATOM   23   C  CA  . VAL A 1 5   ? 32.054 -0.072  4.787   1.00 35.94 ? 4   VAL A CA  1 
ATOM   24   C  C   . VAL A 1 5   ? 32.680 1.216   4.270   1.00 35.80 ? 4   VAL A C   1 
ATOM   25   O  O   . VAL A 1 5   ? 32.314 1.710   3.202   1.00 34.81 ? 4   VAL A O   1 
ATOM   26   C  CB  . VAL A 1 5   ? 33.071 -1.244  4.727   1.00 35.27 ? 4   VAL A CB  1 
ATOM   27   C  CG1 . VAL A 1 5   ? 32.443 -2.502  5.322   1.00 31.41 ? 4   VAL A CG1 1 
ATOM   28   C  CG2 . VAL A 1 5   ? 33.508 -1.494  3.298   1.00 37.61 ? 4   VAL A CG2 1 
ATOM   29   N  N   . VAL A 1 6   ? 33.607 1.775   5.034   1.00 33.46 ? 5   VAL A N   1 
ATOM   30   C  CA  . VAL A 1 6   ? 34.244 3.014   4.631   1.00 34.23 ? 5   VAL A CA  1 
ATOM   31   C  C   . VAL A 1 6   ? 35.684 3.050   5.098   1.00 33.43 ? 5   VAL A C   1 
ATOM   32   O  O   . VAL A 1 6   ? 36.060 2.349   6.042   1.00 32.85 ? 5   VAL A O   1 
ATOM   33   C  CB  . VAL A 1 6   ? 33.495 4.236   5.226   1.00 34.96 ? 5   VAL A CB  1 
ATOM   34   C  CG1 . VAL A 1 6   ? 33.537 4.181   6.751   1.00 30.81 ? 5   VAL A CG1 1 
ATOM   35   C  CG2 . VAL A 1 6   ? 34.114 5.535   4.718   1.00 34.16 ? 5   VAL A CG2 1 
ATOM   36   N  N   . ALA A 1 7   ? 36.487 3.865   4.424   1.00 33.16 ? 6   ALA A N   1 
ATOM   37   C  CA  . ALA A 1 7   ? 37.885 4.026   4.784   1.00 32.55 ? 6   ALA A CA  1 
ATOM   38   C  C   . ALA A 1 7   ? 38.279 5.496   4.707   1.00 33.42 ? 6   ALA A C   1 
ATOM   39   O  O   . ALA A 1 7   ? 38.072 6.157   3.690   1.00 32.68 ? 6   ALA A O   1 
ATOM   40   C  CB  . ALA A 1 7   ? 38.772 3.196   3.858   1.00 31.27 ? 6   ALA A CB  1 
ATOM   41   N  N   . VAL A 1 8   ? 38.834 6.007   5.798   1.00 33.80 ? 7   VAL A N   1 
ATOM   42   C  CA  . VAL A 1 8   ? 39.288 7.384   5.847   1.00 35.66 ? 7   VAL A CA  1 
ATOM   43   C  C   . VAL A 1 8   ? 40.798 7.401   5.611   1.00 36.69 ? 7   VAL A C   1 
ATOM   44   O  O   . VAL A 1 8   ? 41.568 6.950   6.455   1.00 36.23 ? 7   VAL A O   1 
ATOM   45   C  CB  . VAL A 1 8   ? 38.976 8.005   7.203   1.00 36.55 ? 7   VAL A CB  1 
ATOM   46   C  CG1 . VAL A 1 8   ? 39.529 9.426   7.271   1.00 36.95 ? 7   VAL A CG1 1 
ATOM   47   C  CG2 . VAL A 1 8   ? 37.478 8.001   7.414   1.00 38.68 ? 7   VAL A CG2 1 
ATOM   48   N  N   . LEU A 1 9   ? 41.217 7.924   4.464   1.00 36.28 ? 8   LEU A N   1 
ATOM   49   C  CA  . LEU A 1 9   ? 42.634 7.966   4.114   1.00 38.42 ? 8   LEU A CA  1 
ATOM   50   C  C   . LEU A 1 9   ? 43.370 9.168   4.703   1.00 38.84 ? 8   LEU A C   1 
ATOM   51   O  O   . LEU A 1 9   ? 43.001 10.317  4.459   1.00 38.75 ? 8   LEU A O   1 
ATOM   52   C  CB  . LEU A 1 9   ? 42.798 7.956   2.589   1.00 37.95 ? 8   LEU A CB  1 
ATOM   53   C  CG  . LEU A 1 9   ? 42.090 6.828   1.820   1.00 39.59 ? 8   LEU A CG  1 
ATOM   54   C  CD1 . LEU A 1 9   ? 42.225 7.052   0.316   1.00 38.40 ? 8   LEU A CD1 1 
ATOM   55   C  CD2 . LEU A 1 9   ? 42.682 5.485   2.209   1.00 39.66 ? 8   LEU A CD2 1 
ATOM   56   N  N   . LYS A 1 10  ? 44.409 8.882   5.484   1.00 40.04 ? 9   LYS A N   1 
ATOM   57   C  CA  . LYS A 1 10  ? 45.237 9.905   6.118   1.00 41.99 ? 9   LYS A CA  1 
ATOM   58   C  C   . LYS A 1 10  ? 46.698 9.498   5.996   1.00 43.16 ? 9   LYS A C   1 
ATOM   59   O  O   . LYS A 1 10  ? 47.027 8.308   6.010   1.00 40.82 ? 9   LYS A O   1 
ATOM   60   C  CB  . LYS A 1 10  ? 44.887 10.053  7.603   1.00 43.23 ? 9   LYS A CB  1 
ATOM   61   C  CG  . LYS A 1 10  ? 43.496 10.599  7.876   1.00 47.21 ? 9   LYS A CG  1 
ATOM   62   C  CD  . LYS A 1 10  ? 43.217 10.699  9.373   1.00 48.14 ? 9   LYS A CD  1 
ATOM   63   C  CE  . LYS A 1 10  ? 41.822 11.246  9.632   0.00 50.09 ? 9   LYS A CE  1 
ATOM   64   N  NZ  . LYS A 1 10  ? 41.502 11.317  11.083  1.00 53.08 ? 9   LYS A NZ  1 
ATOM   65   N  N   . GLY A 1 11  ? 47.570 10.492  5.880   1.00 44.06 ? 10  GLY A N   1 
ATOM   66   C  CA  . GLY A 1 11  ? 48.989 10.224  5.761   1.00 46.99 ? 10  GLY A CA  1 
ATOM   67   C  C   . GLY A 1 11  ? 49.780 11.355  6.377   1.00 49.10 ? 10  GLY A C   1 
ATOM   68   O  O   . GLY A 1 11  ? 49.196 12.290  6.930   1.00 48.73 ? 10  GLY A O   1 
ATOM   69   N  N   . ASP A 1 12  ? 51.104 11.274  6.285   1.00 50.47 ? 11  ASP A N   1 
ATOM   70   C  CA  . ASP A 1 12  ? 51.979 12.302  6.840   1.00 53.06 ? 11  ASP A CA  1 
ATOM   71   C  C   . ASP A 1 12  ? 51.998 13.553  5.961   1.00 53.42 ? 11  ASP A C   1 
ATOM   72   O  O   . ASP A 1 12  ? 52.525 14.590  6.363   1.00 53.58 ? 11  ASP A O   1 
ATOM   73   C  CB  . ASP A 1 12  ? 53.406 11.762  6.976   1.00 56.04 ? 11  ASP A CB  1 
ATOM   74   C  CG  . ASP A 1 12  ? 53.535 10.704  8.060   1.00 58.66 ? 11  ASP A CG  1 
ATOM   75   O  OD1 . ASP A 1 12  ? 54.407 9.817   7.923   1.00 62.21 ? 11  ASP A OD1 1 
ATOM   76   O  OD2 . ASP A 1 12  ? 52.782 10.758  9.057   1.00 60.28 ? 11  ASP A OD2 1 
ATOM   77   N  N   . GLY A 1 13  ? 51.423 13.448  4.766   1.00 52.33 ? 12  GLY A N   1 
ATOM   78   C  CA  . GLY A 1 13  ? 51.396 14.575  3.853   1.00 52.41 ? 12  GLY A CA  1 
ATOM   79   C  C   . GLY A 1 13  ? 50.007 15.143  3.642   1.00 52.73 ? 12  GLY A C   1 
ATOM   80   O  O   . GLY A 1 13  ? 49.112 14.896  4.447   1.00 54.98 ? 12  GLY A O   1 
ATOM   81   N  N   . PRO A 1 14  ? 49.792 15.909  2.563   1.00 52.35 ? 13  PRO A N   1 
ATOM   82   C  CA  . PRO A 1 14  ? 48.502 16.525  2.237   1.00 51.59 ? 13  PRO A CA  1 
ATOM   83   C  C   . PRO A 1 14  ? 47.440 15.583  1.668   1.00 50.84 ? 13  PRO A C   1 
ATOM   84   O  O   . PRO A 1 14  ? 46.274 15.957  1.556   1.00 51.39 ? 13  PRO A O   1 
ATOM   85   C  CB  . PRO A 1 14  ? 48.893 17.598  1.233   1.00 51.84 ? 13  PRO A CB  1 
ATOM   86   C  CG  . PRO A 1 14  ? 49.997 16.931  0.487   1.00 50.38 ? 13  PRO A CG  1 
ATOM   87   C  CD  . PRO A 1 14  ? 50.825 16.345  1.608   1.00 50.98 ? 13  PRO A CD  1 
ATOM   88   N  N   . VAL A 1 15  ? 47.841 14.369  1.304   1.00 49.79 ? 14  VAL A N   1 
ATOM   89   C  CA  . VAL A 1 15  ? 46.908 13.402  0.737   1.00 47.39 ? 14  VAL A CA  1 
ATOM   90   C  C   . VAL A 1 15  ? 45.909 12.899  1.777   1.00 48.04 ? 14  VAL A C   1 
ATOM   91   O  O   . VAL A 1 15  ? 46.292 12.352  2.812   1.00 48.54 ? 14  VAL A O   1 
ATOM   92   C  CB  . VAL A 1 15  ? 47.663 12.204  0.131   1.00 47.04 ? 14  VAL A CB  1 
ATOM   93   C  CG1 . VAL A 1 15  ? 46.677 11.238  -0.516  1.00 45.57 ? 14  VAL A CG1 1 
ATOM   94   C  CG2 . VAL A 1 15  ? 48.666 12.699  -0.895  1.00 47.21 ? 14  VAL A CG2 1 
ATOM   95   N  N   . GLN A 1 16  ? 44.625 13.100  1.497   1.00 48.33 ? 15  GLN A N   1 
ATOM   96   C  CA  . GLN A 1 16  ? 43.554 12.675  2.396   1.00 47.67 ? 15  GLN A CA  1 
ATOM   97   C  C   . GLN A 1 16  ? 42.263 12.466  1.623   1.00 45.74 ? 15  GLN A C   1 
ATOM   98   O  O   . GLN A 1 16  ? 42.065 13.056  0.559   1.00 44.42 ? 15  GLN A O   1 
ATOM   99   C  CB  . GLN A 1 16  ? 43.332 13.721  3.492   1.00 50.62 ? 15  GLN A CB  1 
ATOM   100  C  CG  . GLN A 1 16  ? 43.177 15.144  2.974   1.00 55.68 ? 15  GLN A CG  1 
ATOM   101  C  CD  . GLN A 1 16  ? 42.947 16.154  4.085   1.00 58.22 ? 15  GLN A CD  1 
ATOM   102  O  OE1 . GLN A 1 16  ? 43.099 17.358  3.884   1.00 60.26 ? 15  GLN A OE1 1 
ATOM   103  N  NE2 . GLN A 1 16  ? 42.570 15.667  5.263   1.00 59.59 ? 15  GLN A NE2 1 
ATOM   104  N  N   . GLY A 1 17  ? 41.384 11.621  2.154   1.00 44.21 ? 16  GLY A N   1 
ATOM   105  C  CA  . GLY A 1 17  ? 40.124 11.369  1.478   1.00 41.31 ? 16  GLY A CA  1 
ATOM   106  C  C   . GLY A 1 17  ? 39.248 10.346  2.173   1.00 39.88 ? 16  GLY A C   1 
ATOM   107  O  O   . GLY A 1 17  ? 39.605 9.806   3.215   1.00 40.24 ? 16  GLY A O   1 
ATOM   108  N  N   . ILE A 1 18  ? 38.089 10.088  1.585   1.00 39.25 ? 17  ILE A N   1 
ATOM   109  C  CA  . ILE A 1 18  ? 37.139 9.125   2.121   1.00 36.75 ? 17  ILE A CA  1 
ATOM   110  C  C   . ILE A 1 18  ? 36.664 8.248   0.972   1.00 36.40 ? 17  ILE A C   1 
ATOM   111  O  O   . ILE A 1 18  ? 36.307 8.751   -0.084  1.00 35.78 ? 17  ILE A O   1 
ATOM   112  C  CB  . ILE A 1 18  ? 35.922 9.838   2.736   1.00 39.16 ? 17  ILE A CB  1 
ATOM   113  C  CG1 . ILE A 1 18  ? 36.341 10.587  4.004   1.00 38.29 ? 17  ILE A CG1 1 
ATOM   114  C  CG2 . ILE A 1 18  ? 34.813 8.834   3.022   1.00 34.86 ? 17  ILE A CG2 1 
ATOM   115  C  CD1 . ILE A 1 18  ? 35.189 11.289  4.694   1.00 40.03 ? 17  ILE A CD1 1 
ATOM   116  N  N   . ILE A 1 19  ? 36.666 6.939   1.182   1.00 35.15 ? 18  ILE A N   1 
ATOM   117  C  CA  . ILE A 1 19  ? 36.242 6.000   0.156   1.00 35.08 ? 18  ILE A CA  1 
ATOM   118  C  C   . ILE A 1 19  ? 35.184 5.061   0.709   1.00 36.63 ? 18  ILE A C   1 
ATOM   119  O  O   . ILE A 1 19  ? 35.398 4.407   1.728   1.00 35.72 ? 18  ILE A O   1 
ATOM   120  C  CB  . ILE A 1 19  ? 37.419 5.147   -0.356  1.00 35.78 ? 18  ILE A CB  1 
ATOM   121  C  CG1 . ILE A 1 19  ? 38.465 6.036   -1.028  1.00 37.20 ? 18  ILE A CG1 1 
ATOM   122  C  CG2 . ILE A 1 19  ? 36.903 4.078   -1.310  1.00 34.20 ? 18  ILE A CG2 1 
ATOM   123  C  CD1 . ILE A 1 19  ? 37.935 6.858   -2.199  1.00 40.26 ? 18  ILE A CD1 1 
ATOM   124  N  N   . ASN A 1 20  ? 34.049 4.983   0.018   1.00 36.86 ? 19  ASN A N   1 
ATOM   125  C  CA  . ASN A 1 20  ? 32.958 4.127   0.448   1.00 36.87 ? 19  ASN A CA  1 
ATOM   126  C  C   . ASN A 1 20  ? 32.927 2.850   -0.371  1.00 36.56 ? 19  ASN A C   1 
ATOM   127  O  O   . ASN A 1 20  ? 33.338 2.830   -1.530  1.00 38.99 ? 19  ASN A O   1 
ATOM   128  C  CB  . ASN A 1 20  ? 31.626 4.863   0.302   1.00 36.14 ? 19  ASN A CB  1 
ATOM   129  C  CG  . ASN A 1 20  ? 31.622 6.211   1.007   1.00 40.97 ? 19  ASN A CG  1 
ATOM   130  O  OD1 . ASN A 1 20  ? 31.577 6.288   2.237   1.00 38.37 ? 19  ASN A OD1 1 
ATOM   131  N  ND2 . ASN A 1 20  ? 31.683 7.284   0.223   1.00 42.43 ? 19  ASN A ND2 1 
ATOM   132  N  N   . PHE A 1 21  ? 32.452 1.782   0.250   1.00 36.47 ? 20  PHE A N   1 
ATOM   133  C  CA  . PHE A 1 21  ? 32.334 0.493   -0.407  1.00 38.73 ? 20  PHE A CA  1 
ATOM   134  C  C   . PHE A 1 21  ? 30.936 0.000   -0.086  1.00 40.49 ? 20  PHE A C   1 
ATOM   135  O  O   . PHE A 1 21  ? 30.490 0.111   1.058   1.00 40.67 ? 20  PHE A O   1 
ATOM   136  C  CB  . PHE A 1 21  ? 33.323 -0.521  0.169   1.00 38.41 ? 20  PHE A CB  1 
ATOM   137  C  CG  . PHE A 1 21  ? 34.772 -0.177  -0.036  1.00 38.50 ? 20  PHE A CG  1 
ATOM   138  C  CD1 . PHE A 1 21  ? 35.527 -0.856  -0.989  1.00 39.53 ? 20  PHE A CD1 1 
ATOM   139  C  CD2 . PHE A 1 21  ? 35.407 0.757   0.779   1.00 38.70 ? 20  PHE A CD2 1 
ATOM   140  C  CE1 . PHE A 1 21  ? 36.896 -0.619  -1.125  1.00 35.98 ? 20  PHE A CE1 1 
ATOM   141  C  CE2 . PHE A 1 21  ? 36.782 1.001   0.650   1.00 37.83 ? 20  PHE A CE2 1 
ATOM   142  C  CZ  . PHE A 1 21  ? 37.523 0.308   -0.303  1.00 36.93 ? 20  PHE A CZ  1 
ATOM   143  N  N   . GLU A 1 22  ? 30.241 -0.536  -1.082  1.00 42.22 ? 21  GLU A N   1 
ATOM   144  C  CA  . GLU A 1 22  ? 28.911 -1.076  -0.844  1.00 43.86 ? 21  GLU A CA  1 
ATOM   145  C  C   . GLU A 1 22  ? 28.678 -2.351  -1.640  1.00 43.86 ? 21  GLU A C   1 
ATOM   146  O  O   . GLU A 1 22  ? 28.921 -2.399  -2.843  1.00 42.63 ? 21  GLU A O   1 
ATOM   147  C  CB  . GLU A 1 22  ? 27.830 -0.052  -1.182  1.00 45.63 ? 21  GLU A CB  1 
ATOM   148  C  CG  . GLU A 1 22  ? 26.434 -0.569  -0.895  1.00 50.67 ? 21  GLU A CG  1 
ATOM   149  C  CD  . GLU A 1 22  ? 25.369 0.494   -1.041  1.00 53.07 ? 21  GLU A CD  1 
ATOM   150  O  OE1 . GLU A 1 22  ? 25.222 1.046   -2.154  1.00 55.17 ? 21  GLU A OE1 1 
ATOM   151  O  OE2 . GLU A 1 22  ? 24.678 0.774   -0.040  1.00 55.60 ? 21  GLU A OE2 1 
ATOM   152  N  N   . GLN A 1 23  ? 28.225 -3.392  -0.950  1.00 44.50 ? 22  GLN A N   1 
ATOM   153  C  CA  . GLN A 1 23  ? 27.949 -4.665  -1.595  1.00 45.74 ? 22  GLN A CA  1 
ATOM   154  C  C   . GLN A 1 23  ? 26.528 -5.106  -1.251  1.00 47.13 ? 22  GLN A C   1 
ATOM   155  O  O   . GLN A 1 23  ? 26.284 -5.725  -0.215  1.00 45.97 ? 22  GLN A O   1 
ATOM   156  C  CB  . GLN A 1 23  ? 28.956 -5.722  -1.147  1.00 44.10 ? 22  GLN A CB  1 
ATOM   157  C  CG  . GLN A 1 23  ? 28.739 -7.064  -1.804  1.00 45.42 ? 22  GLN A CG  1 
ATOM   158  C  CD  . GLN A 1 23  ? 29.713 -8.115  -1.324  1.00 46.00 ? 22  GLN A CD  1 
ATOM   159  O  OE1 . GLN A 1 23  ? 29.881 -8.320  -0.124  1.00 46.80 ? 22  GLN A OE1 1 
ATOM   160  N  NE2 . GLN A 1 23  ? 30.354 -8.800  -2.264  1.00 47.14 ? 22  GLN A NE2 1 
ATOM   161  N  N   . LYS A 1 24  ? 25.599 -4.776  -2.144  1.00 49.90 ? 23  LYS A N   1 
ATOM   162  C  CA  . LYS A 1 24  ? 24.187 -5.090  -1.967  1.00 52.57 ? 23  LYS A CA  1 
ATOM   163  C  C   . LYS A 1 24  ? 23.882 -6.562  -1.756  1.00 52.83 ? 23  LYS A C   1 
ATOM   164  O  O   . LYS A 1 24  ? 23.186 -6.926  -0.812  1.00 52.80 ? 23  LYS A O   1 
ATOM   165  C  CB  . LYS A 1 24  ? 23.385 -4.598  -3.173  1.00 55.45 ? 23  LYS A CB  1 
ATOM   166  C  CG  . LYS A 1 24  ? 23.412 -3.098  -3.387  1.00 59.40 ? 23  LYS A CG  1 
ATOM   167  C  CD  . LYS A 1 24  ? 22.710 -2.369  -2.259  1.00 61.45 ? 23  LYS A CD  1 
ATOM   168  C  CE  . LYS A 1 24  ? 22.485 -0.912  -2.621  1.00 62.76 ? 23  LYS A CE  1 
ATOM   169  N  NZ  . LYS A 1 24  ? 21.652 -0.789  -3.854  1.00 63.43 ? 23  LYS A NZ  1 
ATOM   170  N  N   . GLU A 1 25  ? 24.390 -7.410  -2.642  1.00 53.67 ? 24  GLU A N   1 
ATOM   171  C  CA  . GLU A 1 25  ? 24.119 -8.832  -2.535  1.00 54.48 ? 24  GLU A CA  1 
ATOM   172  C  C   . GLU A 1 25  ? 25.277 -9.666  -2.023  1.00 54.05 ? 24  GLU A C   1 
ATOM   173  O  O   . GLU A 1 25  ? 26.425 -9.475  -2.411  1.00 51.41 ? 24  GLU A O   1 
ATOM   174  C  CB  . GLU A 1 25  ? 23.626 -9.370  -3.880  1.00 56.24 ? 24  GLU A CB  1 
ATOM   175  C  CG  . GLU A 1 25  ? 22.274 -8.796  -4.297  1.00 59.79 ? 24  GLU A CG  1 
ATOM   176  C  CD  . GLU A 1 25  ? 21.177 -9.046  -3.262  1.00 61.65 ? 24  GLU A CD  1 
ATOM   177  O  OE1 . GLU A 1 25  ? 20.065 -8.501  -3.432  1.00 62.99 ? 24  GLU A OE1 1 
ATOM   178  O  OE2 . GLU A 1 25  ? 21.419 -9.786  -2.280  1.00 63.86 ? 24  GLU A OE2 1 
ATOM   179  N  N   . SER A 1 26  ? 24.930 -10.597 -1.142  1.00 55.53 ? 25  SER A N   1 
ATOM   180  C  CA  . SER A 1 26  ? 25.864 -11.504 -0.494  1.00 57.52 ? 25  SER A CA  1 
ATOM   181  C  C   . SER A 1 26  ? 27.224 -11.662 -1.162  1.00 58.36 ? 25  SER A C   1 
ATOM   182  O  O   . SER A 1 26  ? 28.257 -11.344 -0.565  1.00 59.79 ? 25  SER A O   1 
ATOM   183  C  CB  . SER A 1 26  ? 25.207 -12.878 -0.333  1.00 59.42 ? 25  SER A CB  1 
ATOM   184  O  OG  . SER A 1 26  ? 25.991 -13.723 0.493   1.00 61.00 ? 25  SER A OG  1 
ATOM   185  N  N   . ASN A 1 27  ? 27.230 -12.150 -2.397  1.00 58.76 ? 26  ASN A N   1 
ATOM   186  C  CA  . ASN A 1 27  ? 28.482 -12.363 -3.118  1.00 58.76 ? 26  ASN A CA  1 
ATOM   187  C  C   . ASN A 1 27  ? 28.621 -11.508 -4.365  1.00 56.93 ? 26  ASN A C   1 
ATOM   188  O  O   . ASN A 1 27  ? 29.527 -11.715 -5.164  1.00 56.71 ? 26  ASN A O   1 
ATOM   189  C  CB  . ASN A 1 27  ? 28.607 -13.835 -3.505  1.00 60.54 ? 26  ASN A CB  1 
ATOM   190  C  CG  . ASN A 1 27  ? 29.710 -14.535 -2.756  1.00 62.36 ? 26  ASN A CG  1 
ATOM   191  O  OD1 . ASN A 1 27  ? 30.892 -14.333 -3.039  1.00 63.98 ? 26  ASN A OD1 1 
ATOM   192  N  ND2 . ASN A 1 27  ? 29.334 -15.357 -1.783  1.00 63.58 ? 26  ASN A ND2 1 
ATOM   193  N  N   . GLY A 1 28  ? 27.719 -10.548 -4.524  1.00 56.03 ? 27  GLY A N   1 
ATOM   194  C  CA  . GLY A 1 28  ? 27.748 -9.689  -5.688  1.00 53.93 ? 27  GLY A CA  1 
ATOM   195  C  C   . GLY A 1 28  ? 28.920 -8.735  -5.733  1.00 53.84 ? 27  GLY A C   1 
ATOM   196  O  O   . GLY A 1 28  ? 29.827 -8.814  -4.904  1.00 54.16 ? 27  GLY A O   1 
ATOM   197  N  N   . PRO A 1 29  ? 28.922 -7.811  -6.706  1.00 52.30 ? 28  PRO A N   1 
ATOM   198  C  CA  . PRO A 1 29  ? 29.972 -6.812  -6.900  1.00 51.42 ? 28  PRO A CA  1 
ATOM   199  C  C   . PRO A 1 29  ? 29.974 -5.758  -5.805  1.00 49.69 ? 28  PRO A C   1 
ATOM   200  O  O   . PRO A 1 29  ? 28.975 -5.565  -5.113  1.00 49.02 ? 28  PRO A O   1 
ATOM   201  C  CB  . PRO A 1 29  ? 29.627 -6.219  -8.261  1.00 51.62 ? 28  PRO A CB  1 
ATOM   202  C  CG  . PRO A 1 29  ? 28.137 -6.260  -8.246  1.00 51.83 ? 28  PRO A CG  1 
ATOM   203  C  CD  . PRO A 1 29  ? 27.867 -7.650  -7.724  1.00 52.72 ? 28  PRO A CD  1 
ATOM   204  N  N   . VAL A 1 30  ? 31.105 -5.079  -5.658  1.00 47.06 ? 29  VAL A N   1 
ATOM   205  C  CA  . VAL A 1 30  ? 31.231 -4.037  -4.654  1.00 45.06 ? 29  VAL A CA  1 
ATOM   206  C  C   . VAL A 1 30  ? 31.394 -2.698  -5.343  1.00 44.19 ? 29  VAL A C   1 
ATOM   207  O  O   . VAL A 1 30  ? 32.268 -2.530  -6.187  1.00 43.70 ? 29  VAL A O   1 
ATOM   208  C  CB  . VAL A 1 30  ? 32.459 -4.260  -3.749  1.00 44.19 ? 29  VAL A CB  1 
ATOM   209  C  CG1 . VAL A 1 30  ? 32.573 -3.118  -2.738  1.00 44.31 ? 29  VAL A CG1 1 
ATOM   210  C  CG2 . VAL A 1 30  ? 32.340 -5.591  -3.033  1.00 44.67 ? 29  VAL A CG2 1 
ATOM   211  N  N   . LYS A 1 31  ? 30.544 -1.748  -4.980  1.00 43.39 ? 30  LYS A N   1 
ATOM   212  C  CA  . LYS A 1 31  ? 30.622 -0.422  -5.555  1.00 42.62 ? 30  LYS A CA  1 
ATOM   213  C  C   . LYS A 1 31  ? 31.592 0.362   -4.676  1.00 41.77 ? 30  LYS A C   1 
ATOM   214  O  O   . LYS A 1 31  ? 31.425 0.435   -3.462  1.00 42.45 ? 30  LYS A O   1 
ATOM   215  C  CB  . LYS A 1 31  ? 29.232 0.221   -5.560  1.00 45.61 ? 30  LYS A CB  1 
ATOM   216  C  CG  . LYS A 1 31  ? 29.090 1.386   -6.518  1.00 49.43 ? 30  LYS A CG  1 
ATOM   217  C  CD  . LYS A 1 31  ? 27.653 1.893   -6.552  1.00 50.23 ? 30  LYS A CD  1 
ATOM   218  C  CE  . LYS A 1 31  ? 27.450 2.896   -7.677  0.00 50.52 ? 30  LYS A CE  1 
ATOM   219  N  NZ  . LYS A 1 31  ? 28.362 4.065   -7.552  0.00 50.94 ? 30  LYS A NZ  1 
ATOM   220  N  N   . VAL A 1 32  ? 32.616 0.930   -5.294  1.00 39.51 ? 31  VAL A N   1 
ATOM   221  C  CA  . VAL A 1 32  ? 33.622 1.695   -4.573  1.00 39.19 ? 31  VAL A CA  1 
ATOM   222  C  C   . VAL A 1 32  ? 33.630 3.128   -5.082  1.00 38.39 ? 31  VAL A C   1 
ATOM   223  O  O   . VAL A 1 32  ? 33.825 3.363   -6.265  1.00 38.80 ? 31  VAL A O   1 
ATOM   224  C  CB  . VAL A 1 32  ? 35.024 1.095   -4.789  1.00 37.35 ? 31  VAL A CB  1 
ATOM   225  C  CG1 . VAL A 1 32  ? 36.045 1.829   -3.932  1.00 38.86 ? 31  VAL A CG1 1 
ATOM   226  C  CG2 . VAL A 1 32  ? 35.008 -0.389  -4.465  1.00 37.19 ? 31  VAL A CG2 1 
ATOM   227  N  N   . TRP A 1 33  ? 33.428 4.087   -4.192  1.00 38.90 ? 32  TRP A N   1 
ATOM   228  C  CA  . TRP A 1 33  ? 33.404 5.479   -4.615  1.00 41.01 ? 32  TRP A CA  1 
ATOM   229  C  C   . TRP A 1 33  ? 33.746 6.419   -3.474  1.00 40.83 ? 32  TRP A C   1 
ATOM   230  O  O   . TRP A 1 33  ? 33.576 6.088   -2.301  1.00 40.87 ? 32  TRP A O   1 
ATOM   231  C  CB  . TRP A 1 33  ? 32.017 5.834   -5.161  1.00 41.97 ? 32  TRP A CB  1 
ATOM   232  C  CG  . TRP A 1 33  ? 31.005 6.091   -4.083  1.00 43.64 ? 32  TRP A CG  1 
ATOM   233  C  CD1 . TRP A 1 33  ? 30.662 7.302   -3.553  1.00 44.06 ? 32  TRP A CD1 1 
ATOM   234  C  CD2 . TRP A 1 33  ? 30.235 5.112   -3.372  1.00 44.22 ? 32  TRP A CD2 1 
ATOM   235  N  NE1 . TRP A 1 33  ? 29.728 7.139   -2.559  1.00 45.07 ? 32  TRP A NE1 1 
ATOM   236  C  CE2 . TRP A 1 33  ? 29.448 5.804   -2.427  1.00 44.64 ? 32  TRP A CE2 1 
ATOM   237  C  CE3 . TRP A 1 33  ? 30.135 3.717   -3.443  1.00 46.58 ? 32  TRP A CE3 1 
ATOM   238  C  CZ2 . TRP A 1 33  ? 28.571 5.148   -1.554  1.00 47.38 ? 32  TRP A CZ2 1 
ATOM   239  C  CZ3 . TRP A 1 33  ? 29.261 3.063   -2.574  1.00 47.88 ? 32  TRP A CZ3 1 
ATOM   240  C  CH2 . TRP A 1 33  ? 28.491 3.781   -1.644  1.00 47.63 ? 32  TRP A CH2 1 
ATOM   241  N  N   . GLY A 1 34  ? 34.219 7.602   -3.836  1.00 40.99 ? 33  GLY A N   1 
ATOM   242  C  CA  . GLY A 1 34  ? 34.581 8.595   -2.852  1.00 40.64 ? 33  GLY A CA  1 
ATOM   243  C  C   . GLY A 1 34  ? 35.443 9.616   -3.548  1.00 42.73 ? 33  GLY A C   1 
ATOM   244  O  O   . GLY A 1 34  ? 35.385 9.741   -4.772  1.00 42.74 ? 33  GLY A O   1 
ATOM   245  N  N   . SER A 1 35  ? 36.252 10.333  -2.778  1.00 44.01 ? 34  SER A N   1 
ATOM   246  C  CA  . SER A 1 35  ? 37.131 11.346  -3.333  1.00 46.86 ? 34  SER A CA  1 
ATOM   247  C  C   . SER A 1 35  ? 38.437 11.439  -2.556  1.00 47.89 ? 34  SER A C   1 
ATOM   248  O  O   . SER A 1 35  ? 38.470 11.214  -1.346  1.00 48.29 ? 34  SER A O   1 
ATOM   249  C  CB  . SER A 1 35  ? 36.436 12.707  -3.315  1.00 47.44 ? 34  SER A CB  1 
ATOM   250  O  OG  . SER A 1 35  ? 37.344 13.725  -3.682  1.00 50.95 ? 34  SER A OG  1 
ATOM   251  N  N   . ILE A 1 36  ? 39.510 11.775  -3.263  1.00 48.06 ? 35  ILE A N   1 
ATOM   252  C  CA  . ILE A 1 36  ? 40.827 11.921  -2.655  1.00 47.51 ? 35  ILE A CA  1 
ATOM   253  C  C   . ILE A 1 36  ? 41.438 13.219  -3.178  1.00 48.91 ? 35  ILE A C   1 
ATOM   254  O  O   . ILE A 1 36  ? 41.329 13.528  -4.363  1.00 48.77 ? 35  ILE A O   1 
ATOM   255  C  CB  . ILE A 1 36  ? 41.746 10.742  -3.033  1.00 46.73 ? 35  ILE A CB  1 
ATOM   256  C  CG1 . ILE A 1 36  ? 41.080 9.416   -2.652  1.00 43.76 ? 35  ILE A CG1 1 
ATOM   257  C  CG2 . ILE A 1 36  ? 43.079 10.884  -2.326  1.00 46.53 ? 35  ILE A CG2 1 
ATOM   258  C  CD1 . ILE A 1 36  ? 41.798 8.193   -3.173  1.00 43.68 ? 35  ILE A CD1 1 
ATOM   259  N  N   . LYS A 1 37  ? 42.077 13.980  -2.298  1.00 49.37 ? 36  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 37  ? 42.683 15.241  -2.703  1.00 50.29 ? 36  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 37  ? 44.151 15.300  -2.305  1.00 50.74 ? 36  LYS A C   1 
ATOM   262  O  O   . LYS A 1 37  ? 44.637 14.443  -1.568  1.00 49.84 ? 36  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 37  ? 41.939 16.405  -2.047  1.00 51.69 ? 36  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 37  ? 42.147 16.490  -0.547  1.00 51.58 ? 36  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 37  ? 41.333 17.617  0.063   1.00 55.56 ? 36  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 37  ? 41.870 17.980  1.434   1.00 55.97 ? 36  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 37  ? 40.993 18.934  2.173   1.00 58.34 ? 36  LYS A NZ  1 
ATOM   268  N  N   . GLY A 1 38  ? 44.850 16.321  -2.796  1.00 50.19 ? 37  GLY A N   1 
ATOM   269  C  CA  . GLY A 1 38  ? 46.252 16.498  -2.462  1.00 49.75 ? 37  GLY A CA  1 
ATOM   270  C  C   . GLY A 1 38  ? 47.225 15.648  -3.251  1.00 49.54 ? 37  GLY A C   1 
ATOM   271  O  O   . GLY A 1 38  ? 48.416 15.620  -2.946  1.00 48.64 ? 37  GLY A O   1 
ATOM   272  N  N   . LEU A 1 39  ? 46.724 14.953  -4.265  1.00 50.10 ? 38  LEU A N   1 
ATOM   273  C  CA  . LEU A 1 39  ? 47.563 14.092  -5.090  1.00 51.58 ? 38  LEU A CA  1 
ATOM   274  C  C   . LEU A 1 39  ? 48.092 14.864  -6.290  1.00 52.99 ? 38  LEU A C   1 
ATOM   275  O  O   . LEU A 1 39  ? 47.548 15.910  -6.648  1.00 53.01 ? 38  LEU A O   1 
ATOM   276  C  CB  . LEU A 1 39  ? 46.758 12.894  -5.596  1.00 51.03 ? 38  LEU A CB  1 
ATOM   277  C  CG  . LEU A 1 39  ? 46.148 11.927  -4.580  1.00 50.92 ? 38  LEU A CG  1 
ATOM   278  C  CD1 . LEU A 1 39  ? 45.041 11.130  -5.246  1.00 50.64 ? 38  LEU A CD1 1 
ATOM   279  C  CD2 . LEU A 1 39  ? 47.227 11.010  -4.023  1.00 48.79 ? 38  LEU A CD2 1 
ATOM   280  N  N   . THR A 1 40  ? 49.157 14.357  -6.904  1.00 53.08 ? 39  THR A N   1 
ATOM   281  C  CA  . THR A 1 40  ? 49.704 15.007  -8.086  1.00 52.14 ? 39  THR A CA  1 
ATOM   282  C  C   . THR A 1 40  ? 48.805 14.547  -9.219  1.00 51.80 ? 39  THR A C   1 
ATOM   283  O  O   . THR A 1 40  ? 48.117 13.537  -9.092  1.00 50.28 ? 39  THR A O   1 
ATOM   284  C  CB  . THR A 1 40  ? 51.158 14.571  -8.378  1.00 53.70 ? 39  THR A CB  1 
ATOM   285  O  OG1 . THR A 1 40  ? 51.193 13.176  -8.699  1.00 53.07 ? 39  THR A OG1 1 
ATOM   286  C  CG2 . THR A 1 40  ? 52.047 14.848  -7.172  1.00 51.93 ? 39  THR A CG2 1 
ATOM   287  N  N   . GLU A 1 41  ? 48.803 15.284  -10.321 1.00 51.90 ? 40  GLU A N   1 
ATOM   288  C  CA  . GLU A 1 41  ? 47.959 14.940  -11.456 1.00 51.11 ? 40  GLU A CA  1 
ATOM   289  C  C   . GLU A 1 41  ? 48.417 13.629  -12.085 1.00 50.54 ? 40  GLU A C   1 
ATOM   290  O  O   . GLU A 1 41  ? 49.607 13.422  -12.300 1.00 50.18 ? 40  GLU A O   1 
ATOM   291  C  CB  . GLU A 1 41  ? 48.002 16.077  -12.486 1.00 53.12 ? 40  GLU A CB  1 
ATOM   292  C  CG  . GLU A 1 41  ? 47.155 15.851  -13.723 1.00 53.94 ? 40  GLU A CG  1 
ATOM   293  C  CD  . GLU A 1 41  ? 47.167 17.048  -14.672 1.00 56.32 ? 40  GLU A CD  1 
ATOM   294  O  OE1 . GLU A 1 41  ? 46.631 16.916  -15.795 1.00 54.82 ? 40  GLU A OE1 1 
ATOM   295  O  OE2 . GLU A 1 41  ? 47.701 18.116  -14.294 1.00 54.72 ? 40  GLU A OE2 1 
ATOM   296  N  N   . GLY A 1 42  ? 47.476 12.736  -12.366 1.00 50.33 ? 41  GLY A N   1 
ATOM   297  C  CA  . GLY A 1 42  ? 47.842 11.467  -12.973 1.00 50.55 ? 41  GLY A CA  1 
ATOM   298  C  C   . GLY A 1 42  ? 47.355 10.221  -12.251 1.00 50.00 ? 41  GLY A C   1 
ATOM   299  O  O   . GLY A 1 42  ? 46.538 10.295  -11.329 1.00 48.35 ? 41  GLY A O   1 
ATOM   300  N  N   . LEU A 1 43  ? 47.858 9.067   -12.683 1.00 49.65 ? 42  LEU A N   1 
ATOM   301  C  CA  . LEU A 1 43  ? 47.472 7.794   -12.089 1.00 49.24 ? 42  LEU A CA  1 
ATOM   302  C  C   . LEU A 1 43  ? 48.124 7.614   -10.719 1.00 48.51 ? 42  LEU A C   1 
ATOM   303  O  O   . LEU A 1 43  ? 49.142 8.242   -10.416 1.00 48.98 ? 42  LEU A O   1 
ATOM   304  C  CB  . LEU A 1 43  ? 47.856 6.632   -13.016 1.00 49.20 ? 42  LEU A CB  1 
ATOM   305  C  CG  . LEU A 1 43  ? 47.193 6.577   -14.401 1.00 48.94 ? 42  LEU A CG  1 
ATOM   306  C  CD1 . LEU A 1 43  ? 47.668 5.337   -15.142 1.00 49.65 ? 42  LEU A CD1 1 
ATOM   307  C  CD2 . LEU A 1 43  ? 45.678 6.551   -14.261 1.00 48.42 ? 42  LEU A CD2 1 
ATOM   308  N  N   . HIS A 1 44  ? 47.520 6.760   -9.897  1.00 46.69 ? 43  HIS A N   1 
ATOM   309  C  CA  . HIS A 1 44  ? 48.011 6.485   -8.549  1.00 44.37 ? 43  HIS A CA  1 
ATOM   310  C  C   . HIS A 1 44  ? 47.576 5.095   -8.111  1.00 42.84 ? 43  HIS A C   1 
ATOM   311  O  O   . HIS A 1 44  ? 46.385 4.771   -8.160  1.00 44.70 ? 43  HIS A O   1 
ATOM   312  C  CB  . HIS A 1 44  ? 47.460 7.524   -7.573  1.00 42.27 ? 43  HIS A CB  1 
ATOM   313  C  CG  . HIS A 1 44  ? 48.143 8.853   -7.655  1.00 44.99 ? 43  HIS A CG  1 
ATOM   314  N  ND1 . HIS A 1 44  ? 49.348 9.109   -7.037  1.00 45.43 ? 43  HIS A ND1 1 
ATOM   315  C  CD2 . HIS A 1 44  ? 47.792 10.000  -8.284  1.00 43.90 ? 43  HIS A CD2 1 
ATOM   316  C  CE1 . HIS A 1 44  ? 49.709 10.357  -7.280  1.00 45.34 ? 43  HIS A CE1 1 
ATOM   317  N  NE2 . HIS A 1 44  ? 48.782 10.919  -8.034  1.00 45.97 ? 43  HIS A NE2 1 
ATOM   318  N  N   . GLY A 1 45  ? 48.539 4.272   -7.698  1.00 41.00 ? 44  GLY A N   1 
ATOM   319  C  CA  . GLY A 1 45  ? 48.221 2.922   -7.249  1.00 38.05 ? 44  GLY A CA  1 
ATOM   320  C  C   . GLY A 1 45  ? 47.121 2.949   -6.203  1.00 34.67 ? 44  GLY A C   1 
ATOM   321  O  O   . GLY A 1 45  ? 47.126 3.809   -5.332  1.00 36.87 ? 44  GLY A O   1 
ATOM   322  N  N   . PHE A 1 46  ? 46.194 1.999   -6.280  1.00 35.94 ? 45  PHE A N   1 
ATOM   323  C  CA  . PHE A 1 46  ? 45.057 1.935   -5.363  1.00 33.96 ? 45  PHE A CA  1 
ATOM   324  C  C   . PHE A 1 46  ? 44.754 0.473   -5.033  1.00 34.73 ? 45  PHE A C   1 
ATOM   325  O  O   . PHE A 1 46  ? 44.168 -0.246  -5.850  1.00 34.19 ? 45  PHE A O   1 
ATOM   326  C  CB  . PHE A 1 46  ? 43.859 2.586   -6.056  1.00 35.18 ? 45  PHE A CB  1 
ATOM   327  C  CG  . PHE A 1 46  ? 42.704 2.912   -5.149  1.00 35.20 ? 45  PHE A CG  1 
ATOM   328  C  CD1 . PHE A 1 46  ? 42.880 3.713   -4.025  1.00 33.13 ? 45  PHE A CD1 1 
ATOM   329  C  CD2 . PHE A 1 46  ? 41.412 2.499   -5.480  1.00 32.15 ? 45  PHE A CD2 1 
ATOM   330  C  CE1 . PHE A 1 46  ? 41.781 4.105   -3.247  1.00 32.96 ? 45  PHE A CE1 1 
ATOM   331  C  CE2 . PHE A 1 46  ? 40.309 2.887   -4.708  1.00 31.80 ? 45  PHE A CE2 1 
ATOM   332  C  CZ  . PHE A 1 46  ? 40.497 3.692   -3.595  1.00 33.15 ? 45  PHE A CZ  1 
ATOM   333  N  N   . HIS A 1 47  ? 45.151 0.025   -3.842  1.00 33.62 ? 46  HIS A N   1 
ATOM   334  C  CA  . HIS A 1 47  ? 44.914 -1.361  -3.458  1.00 32.72 ? 46  HIS A CA  1 
ATOM   335  C  C   . HIS A 1 47  ? 44.483 -1.562  -2.015  1.00 32.53 ? 46  HIS A C   1 
ATOM   336  O  O   . HIS A 1 47  ? 44.620 -0.682  -1.164  1.00 30.02 ? 46  HIS A O   1 
ATOM   337  C  CB  . HIS A 1 47  ? 46.172 -2.227  -3.661  1.00 33.74 ? 46  HIS A CB  1 
ATOM   338  C  CG  . HIS A 1 47  ? 47.135 -1.696  -4.674  1.00 34.92 ? 46  HIS A CG  1 
ATOM   339  N  ND1 . HIS A 1 47  ? 48.192 -0.881  -4.337  1.00 36.75 ? 46  HIS A ND1 1 
ATOM   340  C  CD2 . HIS A 1 47  ? 47.197 -1.856  -6.017  1.00 34.08 ? 46  HIS A CD2 1 
ATOM   341  C  CE1 . HIS A 1 47  ? 48.863 -0.559  -5.427  1.00 35.98 ? 46  HIS A CE1 1 
ATOM   342  N  NE2 . HIS A 1 47  ? 48.280 -1.138  -6.461  1.00 36.64 ? 46  HIS A NE2 1 
ATOM   343  N  N   . VAL A 1 48  ? 43.952 -2.750  -1.759  1.00 29.63 ? 47  VAL A N   1 
ATOM   344  C  CA  . VAL A 1 48  ? 43.567 -3.133  -0.420  1.00 31.47 ? 47  VAL A CA  1 
ATOM   345  C  C   . VAL A 1 48  ? 44.769 -3.961  0.030   1.00 31.78 ? 47  VAL A C   1 
ATOM   346  O  O   . VAL A 1 48  ? 45.193 -4.890  -0.668  1.00 31.49 ? 47  VAL A O   1 
ATOM   347  C  CB  . VAL A 1 48  ? 42.293 -4.010  -0.408  1.00 29.43 ? 47  VAL A CB  1 
ATOM   348  C  CG1 . VAL A 1 48  ? 42.068 -4.585  0.983   1.00 28.64 ? 47  VAL A CG1 1 
ATOM   349  C  CG2 . VAL A 1 48  ? 41.086 -3.186  -0.863  1.00 27.89 ? 47  VAL A CG2 1 
ATOM   350  N  N   . HIS A 1 49  ? 45.338 -3.591  1.170   1.00 31.36 ? 48  HIS A N   1 
ATOM   351  C  CA  . HIS A 1 49  ? 46.478 -4.300  1.714   1.00 30.94 ? 48  HIS A CA  1 
ATOM   352  C  C   . HIS A 1 49  ? 45.992 -5.257  2.787   1.00 30.16 ? 48  HIS A C   1 
ATOM   353  O  O   . HIS A 1 49  ? 44.906 -5.081  3.336   1.00 30.20 ? 48  HIS A O   1 
ATOM   354  C  CB  . HIS A 1 49  ? 47.503 -3.313  2.268   1.00 28.09 ? 48  HIS A CB  1 
ATOM   355  C  CG  . HIS A 1 49  ? 48.325 -2.654  1.206   1.00 30.94 ? 48  HIS A CG  1 
ATOM   356  N  ND1 . HIS A 1 49  ? 49.701 -2.718  1.185   1.00 30.85 ? 48  HIS A ND1 1 
ATOM   357  C  CD2 . HIS A 1 49  ? 47.962 -1.962  0.102   1.00 31.11 ? 48  HIS A CD2 1 
ATOM   358  C  CE1 . HIS A 1 49  ? 50.150 -2.095  0.110   1.00 32.65 ? 48  HIS A CE1 1 
ATOM   359  N  NE2 . HIS A 1 49  ? 49.116 -1.628  -0.565  1.00 32.23 ? 48  HIS A NE2 1 
ATOM   360  N  N   . GLU A 1 50  ? 46.808 -6.261  3.086   1.00 31.56 ? 49  GLU A N   1 
ATOM   361  C  CA  . GLU A 1 50  ? 46.446 -7.301  4.043   1.00 31.13 ? 49  GLU A CA  1 
ATOM   362  C  C   . GLU A 1 50  ? 46.012 -6.947  5.452   1.00 29.25 ? 49  GLU A C   1 
ATOM   363  O  O   . GLU A 1 50  ? 44.936 -7.354  5.879   1.00 28.14 ? 49  GLU A O   1 
ATOM   364  C  CB  . GLU A 1 50  ? 47.565 -8.334  4.145   1.00 31.29 ? 49  GLU A CB  1 
ATOM   365  C  CG  . GLU A 1 50  ? 47.152 -9.583  4.922   1.00 33.08 ? 49  GLU A CG  1 
ATOM   366  C  CD  . GLU A 1 50  ? 48.191 -10.673 4.833   1.00 32.69 ? 49  GLU A CD  1 
ATOM   367  O  OE1 . GLU A 1 50  ? 47.916 -11.807 5.280   1.00 37.39 ? 49  GLU A OE1 1 
ATOM   368  O  OE2 . GLU A 1 50  ? 49.289 -10.384 4.323   1.00 34.62 ? 49  GLU A OE2 1 
ATOM   369  N  N   . PHE A 1 51  ? 46.839 -6.204  6.176   1.00 29.96 ? 50  PHE A N   1 
ATOM   370  C  CA  . PHE A 1 51  ? 46.528 -5.877  7.562   1.00 28.55 ? 50  PHE A CA  1 
ATOM   371  C  C   . PHE A 1 51  ? 45.950 -4.501  7.820   1.00 28.34 ? 50  PHE A C   1 
ATOM   372  O  O   . PHE A 1 51  ? 46.323 -3.531  7.174   1.00 29.21 ? 50  PHE A O   1 
ATOM   373  C  CB  . PHE A 1 51  ? 47.785 -6.055  8.402   1.00 29.21 ? 50  PHE A CB  1 
ATOM   374  C  CG  . PHE A 1 51  ? 48.418 -7.406  8.257   1.00 32.18 ? 50  PHE A CG  1 
ATOM   375  C  CD1 . PHE A 1 51  ? 47.754 -8.550  8.698   1.00 33.06 ? 50  PHE A CD1 1 
ATOM   376  C  CD2 . PHE A 1 51  ? 49.668 -7.542  7.661   1.00 33.89 ? 50  PHE A CD2 1 
ATOM   377  C  CE1 . PHE A 1 51  ? 48.328 -9.814  8.543   1.00 33.65 ? 50  PHE A CE1 1 
ATOM   378  C  CE2 . PHE A 1 51  ? 50.257 -8.808  7.500   1.00 32.74 ? 50  PHE A CE2 1 
ATOM   379  C  CZ  . PHE A 1 51  ? 49.585 -9.940  7.941   1.00 32.25 ? 50  PHE A CZ  1 
ATOM   380  N  N   . GLY A 1 52  ? 45.029 -4.437  8.777   1.00 30.18 ? 51  GLY A N   1 
ATOM   381  C  CA  . GLY A 1 52  ? 44.424 -3.173  9.158   1.00 31.57 ? 51  GLY A CA  1 
ATOM   382  C  C   . GLY A 1 52  ? 45.223 -2.729  10.366  1.00 31.73 ? 51  GLY A C   1 
ATOM   383  O  O   . GLY A 1 52  ? 44.679 -2.300  11.385  1.00 32.34 ? 51  GLY A O   1 
ATOM   384  N  N   . ASP A 1 53  ? 46.539 -2.863  10.240  1.00 33.18 ? 52  ASP A N   1 
ATOM   385  C  CA  . ASP A 1 53  ? 47.474 -2.531  11.305  1.00 31.81 ? 52  ASP A CA  1 
ATOM   386  C  C   . ASP A 1 53  ? 48.124 -1.176  11.049  1.00 32.11 ? 52  ASP A C   1 
ATOM   387  O  O   . ASP A 1 53  ? 48.991 -1.046  10.187  1.00 30.35 ? 52  ASP A O   1 
ATOM   388  C  CB  . ASP A 1 53  ? 48.533 -3.631  11.390  1.00 31.59 ? 52  ASP A CB  1 
ATOM   389  C  CG  . ASP A 1 53  ? 49.442 -3.474  12.582  1.00 33.36 ? 52  ASP A CG  1 
ATOM   390  O  OD1 . ASP A 1 53  ? 49.943 -4.503  13.070  1.00 33.62 ? 52  ASP A OD1 1 
ATOM   391  O  OD2 . ASP A 1 53  ? 49.657 -2.327  13.027  1.00 33.78 ? 52  ASP A OD2 1 
ATOM   392  N  N   . ASN A 1 54  ? 47.705 -0.179  11.825  1.00 32.10 ? 53  ASN A N   1 
ATOM   393  C  CA  . ASN A 1 54  ? 48.198 1.187   11.690  1.00 31.18 ? 53  ASN A CA  1 
ATOM   394  C  C   . ASN A 1 54  ? 49.201 1.532   12.795  1.00 32.49 ? 53  ASN A C   1 
ATOM   395  O  O   . ASN A 1 54  ? 49.361 2.695   13.146  1.00 31.85 ? 53  ASN A O   1 
ATOM   396  C  CB  . ASN A 1 54  ? 46.999 2.139   11.763  1.00 33.71 ? 53  ASN A CB  1 
ATOM   397  C  CG  . ASN A 1 54  ? 47.369 3.583   11.481  1.00 38.57 ? 53  ASN A CG  1 
ATOM   398  O  OD1 . ASN A 1 54  ? 46.751 4.511   12.017  1.00 40.12 ? 53  ASN A OD1 1 
ATOM   399  N  ND2 . ASN A 1 54  ? 48.366 3.785   10.627  1.00 38.68 ? 53  ASN A ND2 1 
ATOM   400  N  N   . THR A 1 55  ? 49.875 0.532   13.354  1.00 33.32 ? 54  THR A N   1 
ATOM   401  C  CA  . THR A 1 55  ? 50.821 0.806   14.433  1.00 31.70 ? 54  THR A CA  1 
ATOM   402  C  C   . THR A 1 55  ? 52.093 1.511   13.937  1.00 33.59 ? 54  THR A C   1 
ATOM   403  O  O   . THR A 1 55  ? 52.816 2.127   14.719  1.00 34.22 ? 54  THR A O   1 
ATOM   404  C  CB  . THR A 1 55  ? 51.204 -0.486  15.181  1.00 31.40 ? 54  THR A CB  1 
ATOM   405  O  OG1 . THR A 1 55  ? 51.751 -1.426  14.255  1.00 28.96 ? 54  THR A OG1 1 
ATOM   406  C  CG2 . THR A 1 55  ? 49.970 -1.107  15.866  1.00 32.34 ? 54  THR A CG2 1 
ATOM   407  N  N   . ALA A 1 56  ? 52.367 1.417   12.639  1.00 33.51 ? 55  ALA A N   1 
ATOM   408  C  CA  . ALA A 1 56  ? 53.533 2.075   12.051  1.00 35.03 ? 55  ALA A CA  1 
ATOM   409  C  C   . ALA A 1 56  ? 53.062 2.800   10.800  1.00 35.84 ? 55  ALA A C   1 
ATOM   410  O  O   . ALA A 1 56  ? 53.617 2.621   9.713   1.00 37.41 ? 55  ALA A O   1 
ATOM   411  C  CB  . ALA A 1 56  ? 54.613 1.050   11.691  1.00 31.73 ? 55  ALA A CB  1 
ATOM   412  N  N   . GLY A 1 57  ? 52.022 3.611   10.952  1.00 36.82 ? 56  GLY A N   1 
ATOM   413  C  CA  . GLY A 1 57  ? 51.500 4.338   9.810   1.00 37.55 ? 56  GLY A CA  1 
ATOM   414  C  C   . GLY A 1 57  ? 51.020 3.372   8.742   1.00 38.44 ? 56  GLY A C   1 
ATOM   415  O  O   . GLY A 1 57  ? 50.479 2.306   9.054   1.00 39.87 ? 56  GLY A O   1 
ATOM   416  N  N   . CYS A 1 58  ? 51.233 3.719   7.480   1.00 35.46 ? 57  CYS A N   1 
ATOM   417  C  CA  . CYS A 1 58  ? 50.791 2.856   6.390   1.00 35.78 ? 57  CYS A CA  1 
ATOM   418  C  C   . CYS A 1 58  ? 51.706 1.666   6.089   1.00 33.30 ? 57  CYS A C   1 
ATOM   419  O  O   . CYS A 1 58  ? 51.312 0.738   5.381   1.00 32.45 ? 57  CYS A O   1 
ATOM   420  C  CB  . CYS A 1 58  ? 50.591 3.691   5.123   1.00 37.34 ? 57  CYS A CB  1 
ATOM   421  S  SG  . CYS A 1 58  ? 49.412 5.062   5.360   1.00 41.56 ? 57  CYS A SG  1 
ATOM   422  N  N   . THR A 1 59  ? 52.916 1.674   6.636   1.00 31.89 ? 58  THR A N   1 
ATOM   423  C  CA  . THR A 1 59  ? 53.840 0.583   6.374   1.00 31.13 ? 58  THR A CA  1 
ATOM   424  C  C   . THR A 1 59  ? 53.430 -0.719  7.061   1.00 29.23 ? 58  THR A C   1 
ATOM   425  O  O   . THR A 1 59  ? 53.726 -1.804  6.560   1.00 30.01 ? 58  THR A O   1 
ATOM   426  C  CB  . THR A 1 59  ? 55.276 0.950   6.792   1.00 32.77 ? 58  THR A CB  1 
ATOM   427  O  OG1 . THR A 1 59  ? 55.364 1.023   8.218   1.00 36.40 ? 58  THR A OG1 1 
ATOM   428  C  CG2 . THR A 1 59  ? 55.670 2.300   6.195   1.00 35.22 ? 58  THR A CG2 1 
ATOM   429  N  N   . SER A 1 60  ? 52.734 -0.624  8.190   1.00 29.27 ? 59  SER A N   1 
ATOM   430  C  CA  . SER A 1 60  ? 52.312 -1.829  8.898   1.00 29.98 ? 59  SER A CA  1 
ATOM   431  C  C   . SER A 1 60  ? 51.117 -2.513  8.242   1.00 30.87 ? 59  SER A C   1 
ATOM   432  O  O   . SER A 1 60  ? 50.687 -3.585  8.680   1.00 32.20 ? 59  SER A O   1 
ATOM   433  C  CB  . SER A 1 60  ? 52.024 -1.528  10.381  1.00 29.52 ? 59  SER A CB  1 
ATOM   434  O  OG  . SER A 1 60  ? 51.420 -0.255  10.573  1.00 30.22 ? 59  SER A OG  1 
ATOM   435  N  N   . ALA A 1 61  ? 50.594 -1.913  7.176   1.00 30.23 ? 60  ALA A N   1 
ATOM   436  C  CA  . ALA A 1 61  ? 49.465 -2.500  6.463   1.00 28.88 ? 60  ALA A CA  1 
ATOM   437  C  C   . ALA A 1 61  ? 49.912 -3.768  5.739   1.00 28.11 ? 60  ALA A C   1 
ATOM   438  O  O   . ALA A 1 61  ? 49.086 -4.560  5.291   1.00 26.00 ? 60  ALA A O   1 
ATOM   439  C  CB  . ALA A 1 61  ? 48.891 -1.510  5.461   1.00 27.88 ? 60  ALA A CB  1 
ATOM   440  N  N   . GLY A 1 62  ? 51.222 -3.953  5.615   1.00 29.30 ? 61  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 62  ? 51.718 -5.141  4.946   1.00 30.29 ? 61  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 62  ? 51.596 -5.083  3.435   1.00 29.24 ? 61  GLY A C   1 
ATOM   443  O  O   . GLY A 1 62  ? 51.512 -4.002  2.855   1.00 30.10 ? 61  GLY A O   1 
ATOM   444  N  N   . PRO A 1 63  ? 51.590 -6.243  2.762   1.00 30.37 ? 62  PRO A N   1 
ATOM   445  C  CA  . PRO A 1 63  ? 51.486 -6.298  1.302   1.00 27.86 ? 62  PRO A CA  1 
ATOM   446  C  C   . PRO A 1 63  ? 50.057 -6.222  0.788   1.00 29.26 ? 62  PRO A C   1 
ATOM   447  O  O   . PRO A 1 63  ? 49.124 -6.003  1.551   1.00 30.46 ? 62  PRO A O   1 
ATOM   448  C  CB  . PRO A 1 63  ? 52.149 -7.626  0.971   1.00 29.44 ? 62  PRO A CB  1 
ATOM   449  C  CG  . PRO A 1 63  ? 51.729 -8.484  2.102   1.00 29.76 ? 62  PRO A CG  1 
ATOM   450  C  CD  . PRO A 1 63  ? 51.857 -7.580  3.324   1.00 29.31 ? 62  PRO A CD  1 
ATOM   451  N  N   . HIS A 1 64  ? 49.886 -6.398  -0.516  1.00 32.23 ? 63  HIS A N   1 
ATOM   452  C  CA  . HIS A 1 64  ? 48.553 -6.362  -1.094  1.00 33.42 ? 63  HIS A CA  1 
ATOM   453  C  C   . HIS A 1 64  ? 47.800 -7.587  -0.600  1.00 33.72 ? 63  HIS A C   1 
ATOM   454  O  O   . HIS A 1 64  ? 48.384 -8.664  -0.475  1.00 33.63 ? 63  HIS A O   1 
ATOM   455  C  CB  . HIS A 1 64  ? 48.638 -6.392  -2.623  1.00 37.56 ? 63  HIS A CB  1 
ATOM   456  C  CG  . HIS A 1 64  ? 49.354 -5.217  -3.214  1.00 40.89 ? 63  HIS A CG  1 
ATOM   457  N  ND1 . HIS A 1 64  ? 49.530 -5.058  -4.571  1.00 42.01 ? 63  HIS A ND1 1 
ATOM   458  C  CD2 . HIS A 1 64  ? 49.927 -4.135  -2.632  1.00 42.36 ? 63  HIS A CD2 1 
ATOM   459  C  CE1 . HIS A 1 64  ? 50.178 -3.931  -4.800  1.00 43.70 ? 63  HIS A CE1 1 
ATOM   460  N  NE2 . HIS A 1 64  ? 50.431 -3.351  -3.640  1.00 42.44 ? 63  HIS A NE2 1 
ATOM   461  N  N   . PHE A 1 65  ? 46.515 -7.425  -0.302  1.00 32.93 ? 64  PHE A N   1 
ATOM   462  C  CA  . PHE A 1 65  ? 45.678 -8.540  0.152   1.00 33.37 ? 64  PHE A CA  1 
ATOM   463  C  C   . PHE A 1 65  ? 45.779 -9.608  -0.943  1.00 34.29 ? 64  PHE A C   1 
ATOM   464  O  O   . PHE A 1 65  ? 45.421 -9.346  -2.088  1.00 34.57 ? 64  PHE A O   1 
ATOM   465  C  CB  . PHE A 1 65  ? 44.236 -8.048  0.296   1.00 32.96 ? 64  PHE A CB  1 
ATOM   466  C  CG  . PHE A 1 65  ? 43.289 -9.060  0.859   1.00 33.89 ? 64  PHE A CG  1 
ATOM   467  C  CD1 . PHE A 1 65  ? 41.958 -9.069  0.450   1.00 35.06 ? 64  PHE A CD1 1 
ATOM   468  C  CD2 . PHE A 1 65  ? 43.705 -9.984  1.808   1.00 33.71 ? 64  PHE A CD2 1 
ATOM   469  C  CE1 . PHE A 1 65  ? 41.055 -9.983  0.974   1.00 35.08 ? 64  PHE A CE1 1 
ATOM   470  C  CE2 . PHE A 1 65  ? 42.812 -10.904 2.343   1.00 35.42 ? 64  PHE A CE2 1 
ATOM   471  C  CZ  . PHE A 1 65  ? 41.481 -10.904 1.924   1.00 35.72 ? 64  PHE A CZ  1 
ATOM   472  N  N   . ASN A 1 66  ? 46.258 -10.804 -0.599  1.00 36.12 ? 65  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 66  ? 46.437 -11.862 -1.595  1.00 38.96 ? 65  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 66  ? 46.172 -13.280 -1.067  1.00 39.84 ? 65  ASN A C   1 
ATOM   475  O  O   . ASN A 1 66  ? 47.078 -14.108 -1.001  1.00 41.15 ? 65  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 66  ? 47.866 -11.758 -2.148  1.00 39.69 ? 65  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 66  ? 48.132 -12.707 -3.294  1.00 40.03 ? 65  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 66  ? 47.319 -12.855 -4.201  1.00 40.76 ? 65  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 66  ? 49.295 -13.337 -3.270  1.00 42.91 ? 65  ASN A ND2 1 
ATOM   480  N  N   . PRO A 1 67  ? 44.912 -13.585 -0.718  1.00 41.50 ? 66  PRO A N   1 
ATOM   481  C  CA  . PRO A 1 67  ? 44.513 -14.898 -0.192  1.00 42.37 ? 66  PRO A CA  1 
ATOM   482  C  C   . PRO A 1 67  ? 44.728 -16.074 -1.146  1.00 44.04 ? 66  PRO A C   1 
ATOM   483  O  O   . PRO A 1 67  ? 45.021 -17.185 -0.706  1.00 44.94 ? 66  PRO A O   1 
ATOM   484  C  CB  . PRO A 1 67  ? 43.032 -14.716 0.126   1.00 42.15 ? 66  PRO A CB  1 
ATOM   485  C  CG  . PRO A 1 67  ? 42.862 -13.245 0.231   1.00 45.09 ? 66  PRO A CG  1 
ATOM   486  C  CD  . PRO A 1 67  ? 43.741 -12.704 -0.838  1.00 39.51 ? 66  PRO A CD  1 
ATOM   487  N  N   . LEU A 1 68  ? 44.566 -15.834 -2.444  1.00 44.03 ? 67  LEU A N   1 
ATOM   488  C  CA  . LEU A 1 68  ? 44.736 -16.895 -3.432  1.00 46.04 ? 67  LEU A CA  1 
ATOM   489  C  C   . LEU A 1 68  ? 46.173 -17.025 -3.935  1.00 47.72 ? 67  LEU A C   1 
ATOM   490  O  O   . LEU A 1 68  ? 46.454 -17.783 -4.867  1.00 49.00 ? 67  LEU A O   1 
ATOM   491  C  CB  . LEU A 1 68  ? 43.786 -16.681 -4.616  1.00 46.25 ? 67  LEU A CB  1 
ATOM   492  C  CG  . LEU A 1 68  ? 42.295 -16.825 -4.306  1.00 46.43 ? 67  LEU A CG  1 
ATOM   493  C  CD1 . LEU A 1 68  ? 41.848 -15.673 -3.432  1.00 47.21 ? 67  LEU A CD1 1 
ATOM   494  C  CD2 . LEU A 1 68  ? 41.498 -16.837 -5.597  1.00 46.33 ? 67  LEU A CD2 1 
ATOM   495  N  N   . SER A 1 69  ? 47.081 -16.282 -3.315  1.00 48.50 ? 68  SER A N   1 
ATOM   496  C  CA  . SER A 1 69  ? 48.492 -16.326 -3.679  1.00 48.87 ? 68  SER A CA  1 
ATOM   497  C  C   . SER A 1 69  ? 48.777 -16.226 -5.175  1.00 48.41 ? 68  SER A C   1 
ATOM   498  O  O   . SER A 1 69  ? 49.528 -17.036 -5.721  1.00 47.84 ? 68  SER A O   1 
ATOM   499  C  CB  . SER A 1 69  ? 49.118 -17.608 -3.129  1.00 51.13 ? 68  SER A CB  1 
ATOM   500  O  OG  . SER A 1 69  ? 48.891 -17.718 -1.734  1.00 53.61 ? 68  SER A OG  1 
ATOM   501  N  N   . ARG A 1 70  ? 48.182 -15.236 -5.836  1.00 46.95 ? 69  ARG A N   1 
ATOM   502  C  CA  . ARG A 1 70  ? 48.413 -15.026 -7.262  1.00 47.07 ? 69  ARG A CA  1 
ATOM   503  C  C   . ARG A 1 70  ? 49.405 -13.874 -7.389  1.00 45.69 ? 69  ARG A C   1 
ATOM   504  O  O   . ARG A 1 70  ? 49.853 -13.324 -6.388  1.00 45.06 ? 69  ARG A O   1 
ATOM   505  C  CB  . ARG A 1 70  ? 47.111 -14.650 -7.989  1.00 48.35 ? 69  ARG A CB  1 
ATOM   506  C  CG  . ARG A 1 70  ? 45.951 -15.619 -7.801  1.00 50.88 ? 69  ARG A CG  1 
ATOM   507  C  CD  . ARG A 1 70  ? 46.243 -16.997 -8.364  1.00 55.88 ? 69  ARG A CD  1 
ATOM   508  N  NE  . ARG A 1 70  ? 45.321 -17.990 -7.817  1.00 59.47 ? 69  ARG A NE  1 
ATOM   509  C  CZ  . ARG A 1 70  ? 45.469 -19.307 -7.939  1.00 60.97 ? 69  ARG A CZ  1 
ATOM   510  N  NH1 . ARG A 1 70  ? 44.575 -20.125 -7.397  1.00 61.26 ? 69  ARG A NH1 1 
ATOM   511  N  NH2 . ARG A 1 70  ? 46.509 -19.808 -8.598  1.00 61.05 ? 69  ARG A NH2 1 
ATOM   512  N  N   . LYS A 1 71  ? 49.743 -13.511 -8.620  1.00 43.79 ? 70  LYS A N   1 
ATOM   513  C  CA  . LYS A 1 71  ? 50.665 -12.413 -8.861  1.00 43.75 ? 70  LYS A CA  1 
ATOM   514  C  C   . LYS A 1 71  ? 49.910 -11.088 -8.970  1.00 43.03 ? 70  LYS A C   1 
ATOM   515  O  O   . LYS A 1 71  ? 48.683 -11.070 -9.080  1.00 42.05 ? 70  LYS A O   1 
ATOM   516  C  CB  . LYS A 1 71  ? 51.457 -12.654 -10.148 1.00 45.34 ? 70  LYS A CB  1 
ATOM   517  C  CG  . LYS A 1 71  ? 52.422 -13.823 -10.077 1.00 47.40 ? 70  LYS A CG  1 
ATOM   518  C  CD  . LYS A 1 71  ? 53.217 -13.970 -11.374 1.00 51.79 ? 70  LYS A CD  1 
ATOM   519  C  CE  . LYS A 1 71  ? 54.238 -15.101 -11.269 1.00 55.04 ? 70  LYS A CE  1 
ATOM   520  N  NZ  . LYS A 1 71  ? 54.985 -15.326 -12.543 1.00 59.18 ? 70  LYS A NZ  1 
ATOM   521  N  N   . HIS A 1 72  ? 50.650 -9.984  -8.942  1.00 41.95 ? 71  HIS A N   1 
ATOM   522  C  CA  . HIS A 1 72  ? 50.045 -8.663  -9.040  1.00 41.79 ? 71  HIS A CA  1 
ATOM   523  C  C   . HIS A 1 72  ? 49.587 -8.347  -10.461 1.00 43.86 ? 71  HIS A C   1 
ATOM   524  O  O   . HIS A 1 72  ? 50.239 -8.719  -11.434 1.00 45.56 ? 71  HIS A O   1 
ATOM   525  C  CB  . HIS A 1 72  ? 51.034 -7.584  -8.612  1.00 37.95 ? 71  HIS A CB  1 
ATOM   526  C  CG  . HIS A 1 72  ? 50.479 -6.199  -8.713  1.00 35.70 ? 71  HIS A CG  1 
ATOM   527  N  ND1 . HIS A 1 72  ? 49.546 -5.706  -7.827  1.00 35.66 ? 71  HIS A ND1 1 
ATOM   528  C  CD2 . HIS A 1 72  ? 50.681 -5.223  -9.627  1.00 35.48 ? 71  HIS A CD2 1 
ATOM   529  C  CE1 . HIS A 1 72  ? 49.196 -4.486  -8.193  1.00 35.14 ? 71  HIS A CE1 1 
ATOM   530  N  NE2 . HIS A 1 72  ? 49.870 -4.169  -9.282  1.00 36.81 ? 71  HIS A NE2 1 
ATOM   531  N  N   . GLY A 1 73  ? 48.475 -7.635  -10.576 1.00 44.67 ? 72  GLY A N   1 
ATOM   532  C  CA  . GLY A 1 73  ? 47.983 -7.275  -11.890 1.00 44.99 ? 72  GLY A CA  1 
ATOM   533  C  C   . GLY A 1 73  ? 47.027 -6.105  -11.841 1.00 46.11 ? 72  GLY A C   1 
ATOM   534  O  O   . GLY A 1 73  ? 47.050 -5.302  -10.901 1.00 45.74 ? 72  GLY A O   1 
ATOM   535  N  N   . GLY A 1 74  ? 46.191 -6.009  -12.870 1.00 45.00 ? 73  GLY A N   1 
ATOM   536  C  CA  . GLY A 1 74  ? 45.212 -4.946  -12.940 1.00 44.27 ? 73  GLY A CA  1 
ATOM   537  C  C   . GLY A 1 74  ? 43.885 -5.518  -12.496 1.00 43.24 ? 73  GLY A C   1 
ATOM   538  O  O   . GLY A 1 74  ? 43.715 -6.738  -12.490 1.00 45.84 ? 73  GLY A O   1 
ATOM   539  N  N   . PRO A 1 75  ? 42.915 -4.674  -12.129 1.00 43.66 ? 74  PRO A N   1 
ATOM   540  C  CA  . PRO A 1 75  ? 41.609 -5.171  -11.683 1.00 43.53 ? 74  PRO A CA  1 
ATOM   541  C  C   . PRO A 1 75  ? 40.854 -6.068  -12.675 1.00 45.59 ? 74  PRO A C   1 
ATOM   542  O  O   . PRO A 1 75  ? 40.126 -6.976  -12.266 1.00 45.07 ? 74  PRO A O   1 
ATOM   543  C  CB  . PRO A 1 75  ? 40.851 -3.886  -11.344 1.00 42.98 ? 74  PRO A CB  1 
ATOM   544  C  CG  . PRO A 1 75  ? 41.456 -2.874  -12.268 1.00 44.22 ? 74  PRO A CG  1 
ATOM   545  C  CD  . PRO A 1 75  ? 42.929 -3.203  -12.203 1.00 41.59 ? 74  PRO A CD  1 
ATOM   546  N  N   . LYS A 1 76  ? 41.041 -5.833  -13.972 1.00 48.78 ? 75  LYS A N   1 
ATOM   547  C  CA  . LYS A 1 76  ? 40.357 -6.629  -14.991 1.00 50.41 ? 75  LYS A CA  1 
ATOM   548  C  C   . LYS A 1 76  ? 41.042 -7.958  -15.313 1.00 51.40 ? 75  LYS A C   1 
ATOM   549  O  O   . LYS A 1 76  ? 40.503 -8.778  -16.059 1.00 52.59 ? 75  LYS A O   1 
ATOM   550  C  CB  . LYS A 1 76  ? 40.199 -5.817  -16.283 1.00 52.30 ? 75  LYS A CB  1 
ATOM   551  C  CG  . LYS A 1 76  ? 39.139 -4.720  -16.225 1.00 55.05 ? 75  LYS A CG  1 
ATOM   552  C  CD  . LYS A 1 76  ? 39.502 -3.628  -15.232 1.00 58.04 ? 75  LYS A CD  1 
ATOM   553  C  CE  . LYS A 1 76  ? 38.422 -2.562  -15.157 1.00 58.96 ? 75  LYS A CE  1 
ATOM   554  N  NZ  . LYS A 1 76  ? 38.223 -1.867  -16.457 0.00 58.70 ? 75  LYS A NZ  1 
ATOM   555  N  N   . ASP A 1 77  ? 42.223 -8.176  -14.746 1.00 51.37 ? 76  ASP A N   1 
ATOM   556  C  CA  . ASP A 1 77  ? 42.974 -9.401  -14.994 1.00 50.58 ? 76  ASP A CA  1 
ATOM   557  C  C   . ASP A 1 77  ? 42.491 -10.587 -14.176 1.00 51.84 ? 76  ASP A C   1 
ATOM   558  O  O   . ASP A 1 77  ? 42.043 -10.436 -13.036 1.00 50.47 ? 76  ASP A O   1 
ATOM   559  C  CB  . ASP A 1 77  ? 44.456 -9.167  -14.706 1.00 51.62 ? 76  ASP A CB  1 
ATOM   560  C  CG  . ASP A 1 77  ? 45.055 -8.102  -15.590 1.00 51.35 ? 76  ASP A CG  1 
ATOM   561  O  OD1 . ASP A 1 77  ? 46.148 -7.591  -15.257 1.00 51.55 ? 76  ASP A OD1 1 
ATOM   562  O  OD2 . ASP A 1 77  ? 44.436 -7.784  -16.625 1.00 52.47 ? 76  ASP A OD2 1 
ATOM   563  N  N   . GLU A 1 78  ? 42.581 -11.774 -14.769 1.00 52.44 ? 77  GLU A N   1 
ATOM   564  C  CA  . GLU A 1 78  ? 42.178 -12.995 -14.083 1.00 53.47 ? 77  GLU A CA  1 
ATOM   565  C  C   . GLU A 1 78  ? 43.246 -13.257 -13.025 1.00 52.15 ? 77  GLU A C   1 
ATOM   566  O  O   . GLU A 1 78  ? 42.945 -13.684 -11.908 1.00 52.82 ? 77  GLU A O   1 
ATOM   567  C  CB  . GLU A 1 78  ? 42.100 -14.159 -15.080 1.00 54.47 ? 77  GLU A CB  1 
ATOM   568  C  CG  . GLU A 1 78  ? 41.631 -15.488 -14.488 1.00 55.83 ? 77  GLU A CG  1 
ATOM   569  C  CD  . GLU A 1 78  ? 42.730 -16.244 -13.759 1.00 56.67 ? 77  GLU A CD  1 
ATOM   570  O  OE1 . GLU A 1 78  ? 42.446 -17.340 -13.230 0.00 56.07 ? 77  GLU A OE1 1 
ATOM   571  O  OE2 . GLU A 1 78  ? 43.877 -15.751 -13.717 0.00 56.07 ? 77  GLU A OE2 1 
ATOM   572  N  N   . GLU A 1 79  ? 44.497 -12.988 -13.392 1.00 51.79 ? 78  GLU A N   1 
ATOM   573  C  CA  . GLU A 1 79  ? 45.626 -13.166 -12.485 1.00 50.21 ? 78  GLU A CA  1 
ATOM   574  C  C   . GLU A 1 79  ? 45.918 -11.841 -11.788 1.00 48.40 ? 78  GLU A C   1 
ATOM   575  O  O   . GLU A 1 79  ? 46.486 -10.920 -12.382 1.00 47.67 ? 78  GLU A O   1 
ATOM   576  C  CB  . GLU A 1 79  ? 46.868 -13.624 -13.252 1.00 51.25 ? 78  GLU A CB  1 
ATOM   577  C  CG  . GLU A 1 79  ? 48.099 -13.898 -12.378 1.00 53.03 ? 78  GLU A CG  1 
ATOM   578  C  CD  . GLU A 1 79  ? 47.969 -15.151 -11.523 1.00 55.46 ? 78  GLU A CD  1 
ATOM   579  O  OE1 . GLU A 1 79  ? 48.913 -15.448 -10.755 1.00 53.68 ? 78  GLU A OE1 1 
ATOM   580  O  OE2 . GLU A 1 79  ? 46.929 -15.843 -11.619 1.00 58.10 ? 78  GLU A OE2 1 
ATOM   581  N  N   . ARG A 1 80  ? 45.512 -11.744 -10.530 1.00 45.58 ? 79  ARG A N   1 
ATOM   582  C  CA  . ARG A 1 80  ? 45.742 -10.532 -9.749  1.00 44.69 ? 79  ARG A CA  1 
ATOM   583  C  C   . ARG A 1 80  ? 45.468 -10.790 -8.280  1.00 41.40 ? 79  ARG A C   1 
ATOM   584  O  O   . ARG A 1 80  ? 44.923 -11.829 -7.918  1.00 41.54 ? 79  ARG A O   1 
ATOM   585  C  CB  . ARG A 1 80  ? 44.848 -9.396  -10.246 1.00 43.68 ? 79  ARG A CB  1 
ATOM   586  C  CG  . ARG A 1 80  ? 43.352 -9.682  -10.177 1.00 48.07 ? 79  ARG A CG  1 
ATOM   587  C  CD  . ARG A 1 80  ? 42.680 -8.908  -9.041  1.00 52.30 ? 79  ARG A CD  1 
ATOM   588  N  NE  . ARG A 1 80  ? 41.375 -8.392  -9.440  1.00 53.21 ? 79  ARG A NE  1 
ATOM   589  C  CZ  . ARG A 1 80  ? 40.574 -7.661  -8.670  1.00 53.83 ? 79  ARG A CZ  1 
ATOM   590  N  NH1 . ARG A 1 80  ? 39.411 -7.248  -9.149  1.00 52.98 ? 79  ARG A NH1 1 
ATOM   591  N  NH2 . ARG A 1 80  ? 40.922 -7.343  -7.429  1.00 51.78 ? 79  ARG A NH2 1 
ATOM   592  N  N   . HIS A 1 81  ? 45.870 -9.842  -7.439  1.00 40.28 ? 80  HIS A N   1 
ATOM   593  C  CA  . HIS A 1 81  ? 45.657 -9.936  -6.000  1.00 37.82 ? 80  HIS A CA  1 
ATOM   594  C  C   . HIS A 1 81  ? 44.221 -9.526  -5.732  1.00 36.52 ? 80  HIS A C   1 
ATOM   595  O  O   . HIS A 1 81  ? 43.686 -8.672  -6.427  1.00 37.89 ? 80  HIS A O   1 
ATOM   596  C  CB  . HIS A 1 81  ? 46.588 -8.970  -5.275  1.00 35.44 ? 80  HIS A CB  1 
ATOM   597  C  CG  . HIS A 1 81  ? 48.038 -9.262  -5.482  1.00 34.01 ? 80  HIS A CG  1 
ATOM   598  N  ND1 . HIS A 1 81  ? 48.983 -8.270  -5.616  1.00 31.18 ? 80  HIS A ND1 1 
ATOM   599  C  CD2 . HIS A 1 81  ? 48.709 -10.436 -5.543  1.00 34.12 ? 80  HIS A CD2 1 
ATOM   600  C  CE1 . HIS A 1 81  ? 50.177 -8.821  -5.747  1.00 31.83 ? 80  HIS A CE1 1 
ATOM   601  N  NE2 . HIS A 1 81  ? 50.037 -10.133 -5.706  1.00 31.81 ? 80  HIS A NE2 1 
ATOM   602  N  N   . VAL A 1 82  ? 43.587 -10.119 -4.732  1.00 37.51 ? 81  VAL A N   1 
ATOM   603  C  CA  . VAL A 1 82  ? 42.212 -9.739  -4.436  1.00 37.09 ? 81  VAL A CA  1 
ATOM   604  C  C   . VAL A 1 82  ? 42.166 -8.229  -4.225  1.00 36.83 ? 81  VAL A C   1 
ATOM   605  O  O   . VAL A 1 82  ? 41.229 -7.558  -4.648  1.00 37.88 ? 81  VAL A O   1 
ATOM   606  C  CB  . VAL A 1 82  ? 41.678 -10.454 -3.172  1.00 36.75 ? 81  VAL A CB  1 
ATOM   607  C  CG1 . VAL A 1 82  ? 40.323 -9.871  -2.769  1.00 35.97 ? 81  VAL A CG1 1 
ATOM   608  C  CG2 . VAL A 1 82  ? 41.542 -11.952 -3.440  1.00 35.43 ? 81  VAL A CG2 1 
ATOM   609  N  N   . GLY A 1 83  ? 43.203 -7.690  -3.599  1.00 37.18 ? 82  GLY A N   1 
ATOM   610  C  CA  . GLY A 1 83  ? 43.229 -6.265  -3.334  1.00 36.37 ? 82  GLY A CA  1 
ATOM   611  C  C   . GLY A 1 83  ? 43.648 -5.346  -4.462  1.00 37.22 ? 82  GLY A C   1 
ATOM   612  O  O   . GLY A 1 83  ? 43.697 -4.133  -4.274  1.00 37.36 ? 82  GLY A O   1 
ATOM   613  N  N   . ASP A 1 84  ? 43.943 -5.889  -5.637  1.00 36.84 ? 83  ASP A N   1 
ATOM   614  C  CA  . ASP A 1 84  ? 44.373 -5.040  -6.744  1.00 38.90 ? 83  ASP A CA  1 
ATOM   615  C  C   . ASP A 1 84  ? 43.222 -4.288  -7.393  1.00 39.40 ? 83  ASP A C   1 
ATOM   616  O  O   . ASP A 1 84  ? 42.457 -4.859  -8.168  1.00 38.98 ? 83  ASP A O   1 
ATOM   617  C  CB  . ASP A 1 84  ? 45.111 -5.868  -7.798  1.00 39.00 ? 83  ASP A CB  1 
ATOM   618  C  CG  . ASP A 1 84  ? 46.399 -6.473  -7.268  1.00 40.65 ? 83  ASP A CG  1 
ATOM   619  O  OD1 . ASP A 1 84  ? 46.884 -6.004  -6.213  1.00 37.10 ? 83  ASP A OD1 1 
ATOM   620  O  OD2 . ASP A 1 84  ? 46.931 -7.403  -7.912  1.00 38.80 ? 83  ASP A OD2 1 
ATOM   621  N  N   . LEU A 1 85  ? 43.107 -3.002  -7.076  1.00 38.74 ? 84  LEU A N   1 
ATOM   622  C  CA  . LEU A 1 85  ? 42.043 -2.180  -7.627  1.00 40.42 ? 84  LEU A CA  1 
ATOM   623  C  C   . LEU A 1 85  ? 42.559 -1.184  -8.663  1.00 40.46 ? 84  LEU A C   1 
ATOM   624  O  O   . LEU A 1 85  ? 41.918 -0.168  -8.930  1.00 39.67 ? 84  LEU A O   1 
ATOM   625  C  CB  . LEU A 1 85  ? 41.302 -1.444  -6.499  1.00 40.83 ? 84  LEU A CB  1 
ATOM   626  C  CG  . LEU A 1 85  ? 40.505 -2.346  -5.549  1.00 40.13 ? 84  LEU A CG  1 
ATOM   627  C  CD1 . LEU A 1 85  ? 39.814 -1.502  -4.479  1.00 40.87 ? 84  LEU A CD1 1 
ATOM   628  C  CD2 . LEU A 1 85  ? 39.473 -3.145  -6.343  1.00 39.21 ? 84  LEU A CD2 1 
ATOM   629  N  N   . GLY A 1 86  ? 43.722 -1.485  -9.238  1.00 39.60 ? 85  GLY A N   1 
ATOM   630  C  CA  . GLY A 1 86  ? 44.296 -0.631  -10.265 1.00 39.36 ? 85  GLY A CA  1 
ATOM   631  C  C   . GLY A 1 86  ? 44.790 0.746   -9.861  1.00 38.96 ? 85  GLY A C   1 
ATOM   632  O  O   . GLY A 1 86  ? 45.561 0.889   -8.909  1.00 37.60 ? 85  GLY A O   1 
ATOM   633  N  N   . ASN A 1 87  ? 44.347 1.760   -10.602 1.00 37.59 ? 86  ASN A N   1 
ATOM   634  C  CA  . ASN A 1 87  ? 44.750 3.145   -10.366 1.00 38.34 ? 86  ASN A CA  1 
ATOM   635  C  C   . ASN A 1 87  ? 43.568 4.093   -10.252 1.00 38.91 ? 86  ASN A C   1 
ATOM   636  O  O   . ASN A 1 87  ? 42.499 3.843   -10.799 1.00 40.00 ? 86  ASN A O   1 
ATOM   637  C  CB  . ASN A 1 87  ? 45.608 3.662   -11.525 1.00 39.71 ? 86  ASN A CB  1 
ATOM   638  C  CG  . ASN A 1 87  ? 46.915 2.919   -11.680 1.00 43.47 ? 86  ASN A CG  1 
ATOM   639  O  OD1 . ASN A 1 87  ? 47.821 3.047   -10.853 1.00 46.73 ? 86  ASN A OD1 1 
ATOM   640  N  ND2 . ASN A 1 87  ? 47.028 2.140   -12.750 1.00 44.90 ? 86  ASN A ND2 1 
ATOM   641  N  N   . VAL A 1 88  ? 43.771 5.188   -9.538  1.00 40.65 ? 87  VAL A N   1 
ATOM   642  C  CA  . VAL A 1 88  ? 42.745 6.213   -9.436  1.00 43.12 ? 87  VAL A CA  1 
ATOM   643  C  C   . VAL A 1 88  ? 43.382 7.381   -10.174 1.00 45.19 ? 87  VAL A C   1 
ATOM   644  O  O   . VAL A 1 88  ? 44.608 7.497   -10.207 1.00 46.10 ? 87  VAL A O   1 
ATOM   645  C  CB  . VAL A 1 88  ? 42.434 6.611   -7.980  1.00 41.67 ? 87  VAL A CB  1 
ATOM   646  C  CG1 . VAL A 1 88  ? 41.612 5.520   -7.323  1.00 40.76 ? 87  VAL A CG1 1 
ATOM   647  C  CG2 . VAL A 1 88  ? 43.721 6.860   -7.210  1.00 44.40 ? 87  VAL A CG2 1 
ATOM   648  N  N   . THR A 1 89  ? 42.568 8.236   -10.777 1.00 46.34 ? 88  THR A N   1 
ATOM   649  C  CA  . THR A 1 89  ? 43.115 9.360   -11.527 1.00 48.12 ? 88  THR A CA  1 
ATOM   650  C  C   . THR A 1 89  ? 42.810 10.719  -10.925 1.00 46.45 ? 88  THR A C   1 
ATOM   651  O  O   . THR A 1 89  ? 41.650 11.097  -10.789 1.00 47.29 ? 88  THR A O   1 
ATOM   652  C  CB  . THR A 1 89  ? 42.593 9.352   -12.974 1.00 48.94 ? 88  THR A CB  1 
ATOM   653  O  OG1 . THR A 1 89  ? 42.843 8.070   -13.562 1.00 50.45 ? 88  THR A OG1 1 
ATOM   654  C  CG2 . THR A 1 89  ? 43.286 10.433  -13.797 1.00 50.25 ? 88  THR A CG2 1 
ATOM   655  N  N   . ALA A 1 90  ? 43.860 11.450  -10.566 1.00 45.38 ? 89  ALA A N   1 
ATOM   656  C  CA  . ALA A 1 90  ? 43.704 12.784  -10.008 1.00 45.81 ? 89  ALA A CA  1 
ATOM   657  C  C   . ALA A 1 90  ? 43.650 13.765  -11.174 1.00 48.46 ? 89  ALA A C   1 
ATOM   658  O  O   . ALA A 1 90  ? 44.387 13.615  -12.152 1.00 47.36 ? 89  ALA A O   1 
ATOM   659  C  CB  . ALA A 1 90  ? 44.873 13.121  -9.104  1.00 43.39 ? 89  ALA A CB  1 
ATOM   660  N  N   . ASP A 1 91  ? 42.776 14.760  -11.071 1.00 51.68 ? 90  ASP A N   1 
ATOM   661  C  CA  . ASP A 1 91  ? 42.627 15.763  -12.122 1.00 54.24 ? 90  ASP A CA  1 
ATOM   662  C  C   . ASP A 1 91  ? 43.731 16.804  -12.002 1.00 55.37 ? 90  ASP A C   1 
ATOM   663  O  O   . ASP A 1 91  ? 44.609 16.694  -11.139 1.00 55.07 ? 90  ASP A O   1 
ATOM   664  C  CB  . ASP A 1 91  ? 41.257 16.440  -12.014 1.00 55.05 ? 90  ASP A CB  1 
ATOM   665  C  CG  . ASP A 1 91  ? 41.108 17.278  -10.749 1.00 55.07 ? 90  ASP A CG  1 
ATOM   666  O  OD1 . ASP A 1 91  ? 39.961 17.633  -10.415 1.00 57.19 ? 90  ASP A OD1 1 
ATOM   667  O  OD2 . ASP A 1 91  ? 42.124 17.593  -10.095 1.00 56.55 ? 90  ASP A OD2 1 
ATOM   668  N  N   . LYS A 1 92  ? 43.677 17.814  -12.867 1.00 56.56 ? 91  LYS A N   1 
ATOM   669  C  CA  . LYS A 1 92  ? 44.669 18.883  -12.868 1.00 56.68 ? 91  LYS A CA  1 
ATOM   670  C  C   . LYS A 1 92  ? 44.819 19.519  -11.481 1.00 56.17 ? 91  LYS A C   1 
ATOM   671  O  O   . LYS A 1 92  ? 45.879 20.036  -11.137 1.00 55.64 ? 91  LYS A O   1 
ATOM   672  C  CB  . LYS A 1 92  ? 44.274 19.955  -13.891 1.00 56.53 ? 91  LYS A CB  1 
ATOM   673  C  CG  . LYS A 1 92  ? 42.914 20.592  -13.633 1.00 57.24 ? 91  LYS A CG  1 
ATOM   674  C  CD  . LYS A 1 92  ? 42.553 21.615  -14.706 1.00 57.70 ? 91  LYS A CD  1 
ATOM   675  C  CE  . LYS A 1 92  ? 41.198 22.247  -14.431 0.00 57.05 ? 91  LYS A CE  1 
ATOM   676  N  NZ  . LYS A 1 92  ? 41.179 22.964  -13.127 0.00 56.87 ? 91  LYS A NZ  1 
ATOM   677  N  N   . ASP A 1 93  ? 43.759 19.473  -10.684 1.00 56.79 ? 92  ASP A N   1 
ATOM   678  C  CA  . ASP A 1 93  ? 43.801 20.060  -9.354  1.00 57.86 ? 92  ASP A CA  1 
ATOM   679  C  C   . ASP A 1 93  ? 44.155 19.045  -8.272  1.00 57.88 ? 92  ASP A C   1 
ATOM   680  O  O   . ASP A 1 93  ? 44.029 19.327  -7.077  1.00 57.14 ? 92  ASP A O   1 
ATOM   681  C  CB  . ASP A 1 93  ? 42.468 20.736  -9.046  1.00 60.18 ? 92  ASP A CB  1 
ATOM   682  C  CG  . ASP A 1 93  ? 42.159 21.863  -10.018 1.00 62.64 ? 92  ASP A CG  1 
ATOM   683  O  OD1 . ASP A 1 93  ? 43.032 22.742  -10.194 1.00 63.45 ? 92  ASP A OD1 1 
ATOM   684  O  OD2 . ASP A 1 93  ? 41.056 21.867  -10.606 1.00 61.84 ? 92  ASP A OD2 1 
ATOM   685  N  N   . GLY A 1 94  ? 44.608 17.870  -8.704  1.00 55.84 ? 93  GLY A N   1 
ATOM   686  C  CA  . GLY A 1 94  ? 45.010 16.835  -7.768  1.00 54.57 ? 93  GLY A CA  1 
ATOM   687  C  C   . GLY A 1 94  ? 43.903 16.186  -6.967  1.00 52.93 ? 93  GLY A C   1 
ATOM   688  O  O   . GLY A 1 94  ? 44.122 15.737  -5.843  1.00 52.29 ? 93  GLY A O   1 
ATOM   689  N  N   . VAL A 1 95  ? 42.711 16.138  -7.545  1.00 51.65 ? 94  VAL A N   1 
ATOM   690  C  CA  . VAL A 1 95  ? 41.573 15.523  -6.891  1.00 49.38 ? 94  VAL A CA  1 
ATOM   691  C  C   . VAL A 1 95  ? 41.156 14.315  -7.713  1.00 50.52 ? 94  VAL A C   1 
ATOM   692  O  O   . VAL A 1 95  ? 40.925 14.420  -8.917  1.00 49.70 ? 94  VAL A O   1 
ATOM   693  C  CB  . VAL A 1 95  ? 40.402 16.513  -6.774  1.00 50.10 ? 94  VAL A CB  1 
ATOM   694  C  CG1 . VAL A 1 95  ? 39.132 15.780  -6.348  1.00 47.19 ? 94  VAL A CG1 1 
ATOM   695  C  CG2 . VAL A 1 95  ? 40.759 17.603  -5.765  1.00 45.93 ? 94  VAL A CG2 1 
ATOM   696  N  N   . ALA A 1 96  ? 41.079 13.162  -7.060  1.00 48.31 ? 95  ALA A N   1 
ATOM   697  C  CA  . ALA A 1 96  ? 40.707 11.944  -7.749  1.00 49.78 ? 95  ALA A CA  1 
ATOM   698  C  C   . ALA A 1 96  ? 39.334 11.449  -7.330  1.00 51.36 ? 95  ALA A C   1 
ATOM   699  O  O   . ALA A 1 96  ? 39.150 10.941  -6.222  1.00 52.94 ? 95  ALA A O   1 
ATOM   700  C  CB  . ALA A 1 96  ? 41.753 10.861  -7.503  1.00 48.16 ? 95  ALA A CB  1 
ATOM   701  N  N   . ASP A 1 97  ? 38.367 11.612  -8.224  1.00 51.15 ? 96  ASP A N   1 
ATOM   702  C  CA  . ASP A 1 97  ? 37.019 11.152  -7.962  1.00 51.73 ? 96  ASP A CA  1 
ATOM   703  C  C   . ASP A 1 97  ? 37.016 9.674   -8.301  1.00 51.62 ? 96  ASP A C   1 
ATOM   704  O  O   . ASP A 1 97  ? 37.150 9.286   -9.461  1.00 51.87 ? 96  ASP A O   1 
ATOM   705  C  CB  . ASP A 1 97  ? 36.021 11.910  -8.836  1.00 53.13 ? 96  ASP A CB  1 
ATOM   706  C  CG  . ASP A 1 97  ? 35.902 13.370  -8.442  1.00 55.74 ? 96  ASP A CG  1 
ATOM   707  O  OD1 . ASP A 1 97  ? 35.327 14.158  -9.221  1.00 57.46 ? 96  ASP A OD1 1 
ATOM   708  O  OD2 . ASP A 1 97  ? 36.382 13.731  -7.345  1.00 58.33 ? 96  ASP A OD2 1 
ATOM   709  N  N   . VAL A 1 98  ? 36.891 8.845   -7.275  1.00 51.27 ? 97  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 98  ? 36.888 7.413   -7.475  1.00 50.54 ? 97  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 98  ? 35.480 6.912   -7.718  1.00 51.20 ? 97  VAL A C   1 
ATOM   712  O  O   . VAL A 1 98  ? 34.533 7.349   -7.071  1.00 52.29 ? 97  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 98  ? 37.469 6.683   -6.250  1.00 51.22 ? 97  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 98  ? 37.455 5.181   -6.482  1.00 50.30 ? 97  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 98  ? 38.887 7.170   -5.982  1.00 50.91 ? 97  VAL A CG2 1 
ATOM   716  N  N   . SER A 1 99  ? 35.347 5.996   -8.665  1.00 51.63 ? 98  SER A N   1 
ATOM   717  C  CA  . SER A 1 99  ? 34.052 5.414   -8.980  1.00 52.66 ? 98  SER A CA  1 
ATOM   718  C  C   . SER A 1 99  ? 34.277 4.165   -9.810  1.00 52.67 ? 98  SER A C   1 
ATOM   719  O  O   . SER A 1 99  ? 34.524 4.237   -11.011 1.00 52.80 ? 98  SER A O   1 
ATOM   720  C  CB  . SER A 1 99  ? 33.184 6.406   -9.750  1.00 52.61 ? 98  SER A CB  1 
ATOM   721  O  OG  . SER A 1 99  ? 31.874 5.885   -9.907  1.00 56.56 ? 98  SER A OG  1 
ATOM   722  N  N   . ILE A 1 100 ? 34.201 3.013   -9.159  1.00 52.02 ? 99  ILE A N   1 
ATOM   723  C  CA  . ILE A 1 100 ? 34.414 1.754   -9.843  1.00 50.78 ? 99  ILE A CA  1 
ATOM   724  C  C   . ILE A 1 100 ? 33.678 0.643   -9.141  1.00 50.83 ? 99  ILE A C   1 
ATOM   725  O  O   . ILE A 1 100 ? 33.275 0.775   -7.985  1.00 50.61 ? 99  ILE A O   1 
ATOM   726  C  CB  . ILE A 1 100 ? 35.909 1.379   -9.874  1.00 51.75 ? 99  ILE A CB  1 
ATOM   727  C  CG1 . ILE A 1 100 ? 36.478 1.414   -8.453  1.00 50.50 ? 99  ILE A CG1 1 
ATOM   728  C  CG2 . ILE A 1 100 ? 36.663 2.312   -10.800 1.00 52.02 ? 99  ILE A CG2 1 
ATOM   729  C  CD1 . ILE A 1 100 ? 37.978 1.210   -8.376  1.00 50.44 ? 99  ILE A CD1 1 
ATOM   730  N  N   . GLU A 1 101 ? 33.507 -0.454  -9.861  1.00 49.67 ? 100 GLU A N   1 
ATOM   731  C  CA  . GLU A 1 101 ? 32.841 -1.630  -9.339  1.00 49.89 ? 100 GLU A CA  1 
ATOM   732  C  C   . GLU A 1 101 ? 33.872 -2.739  -9.450  1.00 48.34 ? 100 GLU A C   1 
ATOM   733  O  O   . GLU A 1 101 ? 34.736 -2.695  -10.323 1.00 48.03 ? 100 GLU A O   1 
ATOM   734  C  CB  . GLU A 1 101 ? 31.611 -1.964  -10.186 1.00 51.40 ? 100 GLU A CB  1 
ATOM   735  C  CG  . GLU A 1 101 ? 30.825 -3.161  -9.689  1.00 55.14 ? 100 GLU A CG  1 
ATOM   736  C  CD  . GLU A 1 101 ? 29.591 -3.443  -10.532 1.00 57.10 ? 100 GLU A CD  1 
ATOM   737  O  OE1 . GLU A 1 101 ? 29.743 -3.718  -11.742 1.00 57.96 ? 100 GLU A OE1 1 
ATOM   738  O  OE2 . GLU A 1 101 ? 28.468 -3.390  -9.983  1.00 58.18 ? 100 GLU A OE2 1 
ATOM   739  N  N   . ASP A 1 102 ? 33.795 -3.720  -8.560  1.00 47.31 ? 101 ASP A N   1 
ATOM   740  C  CA  . ASP A 1 102 ? 34.734 -4.830  -8.577  1.00 47.63 ? 101 ASP A CA  1 
ATOM   741  C  C   . ASP A 1 102 ? 34.023 -6.022  -7.972  1.00 48.27 ? 101 ASP A C   1 
ATOM   742  O  O   . ASP A 1 102 ? 33.276 -5.875  -7.007  1.00 49.53 ? 101 ASP A O   1 
ATOM   743  C  CB  . ASP A 1 102 ? 35.982 -4.467  -7.766  1.00 46.49 ? 101 ASP A CB  1 
ATOM   744  C  CG  . ASP A 1 102 ? 37.135 -5.421  -8.007  1.00 47.38 ? 101 ASP A CG  1 
ATOM   745  O  OD1 . ASP A 1 102 ? 37.164 -6.508  -7.384  1.00 44.67 ? 101 ASP A OD1 1 
ATOM   746  O  OD2 . ASP A 1 102 ? 38.010 -5.076  -8.833  1.00 46.53 ? 101 ASP A OD2 1 
ATOM   747  N  N   . SER A 1 103 ? 34.241 -7.201  -8.543  1.00 48.98 ? 102 SER A N   1 
ATOM   748  C  CA  . SER A 1 103 ? 33.587 -8.398  -8.040  1.00 50.18 ? 102 SER A CA  1 
ATOM   749  C  C   . SER A 1 103 ? 34.550 -9.411  -7.441  1.00 49.31 ? 102 SER A C   1 
ATOM   750  O  O   . SER A 1 103 ? 34.151 -10.526 -7.103  1.00 51.38 ? 102 SER A O   1 
ATOM   751  C  CB  . SER A 1 103 ? 32.751 -9.049  -9.148  1.00 50.80 ? 102 SER A CB  1 
ATOM   752  O  OG  . SER A 1 103 ? 33.505 -9.201  -10.336 1.00 55.21 ? 102 SER A OG  1 
ATOM   753  N  N   . VAL A 1 104 ? 35.815 -9.031  -7.306  1.00 48.19 ? 103 VAL A N   1 
ATOM   754  C  CA  . VAL A 1 104 ? 36.794 -9.927  -6.704  1.00 46.69 ? 103 VAL A CA  1 
ATOM   755  C  C   . VAL A 1 104 ? 36.812 -9.653  -5.205  1.00 46.40 ? 103 VAL A C   1 
ATOM   756  O  O   . VAL A 1 104 ? 36.688 -10.576 -4.399  1.00 45.59 ? 103 VAL A O   1 
ATOM   757  C  CB  . VAL A 1 104 ? 38.203 -9.708  -7.284  1.00 48.12 ? 103 VAL A CB  1 
ATOM   758  C  CG1 . VAL A 1 104 ? 39.192 -10.648 -6.617  1.00 46.38 ? 103 VAL A CG1 1 
ATOM   759  C  CG2 . VAL A 1 104 ? 38.184 -9.942  -8.782  1.00 48.80 ? 103 VAL A CG2 1 
ATOM   760  N  N   . ILE A 1 105 ? 36.963 -8.387  -4.825  1.00 45.43 ? 104 ILE A N   1 
ATOM   761  C  CA  . ILE A 1 105 ? 36.960 -8.046  -3.405  1.00 44.95 ? 104 ILE A CA  1 
ATOM   762  C  C   . ILE A 1 105 ? 35.564 -8.357  -2.884  1.00 45.78 ? 104 ILE A C   1 
ATOM   763  O  O   . ILE A 1 105 ? 34.630 -8.530  -3.668  1.00 46.59 ? 104 ILE A O   1 
ATOM   764  C  CB  . ILE A 1 105 ? 37.265 -6.549  -3.152  1.00 42.52 ? 104 ILE A CB  1 
ATOM   765  C  CG1 . ILE A 1 105 ? 36.236 -5.674  -3.870  1.00 41.43 ? 104 ILE A CG1 1 
ATOM   766  C  CG2 . ILE A 1 105 ? 38.677 -6.218  -3.609  1.00 41.95 ? 104 ILE A CG2 1 
ATOM   767  C  CD1 . ILE A 1 105 ? 36.359 -4.193  -3.551  1.00 41.24 ? 104 ILE A CD1 1 
ATOM   768  N  N   . SER A 1 106 ? 35.417 -8.434  -1.568  1.00 45.57 ? 105 SER A N   1 
ATOM   769  C  CA  . SER A 1 106 ? 34.120 -8.739  -0.980  1.00 44.30 ? 105 SER A CA  1 
ATOM   770  C  C   . SER A 1 106 ? 34.051 -8.209  0.449   1.00 44.28 ? 105 SER A C   1 
ATOM   771  O  O   . SER A 1 106 ? 35.086 -7.973  1.077   1.00 41.73 ? 105 SER A O   1 
ATOM   772  C  CB  . SER A 1 106 ? 33.908 -10.256 -0.988  1.00 44.78 ? 105 SER A CB  1 
ATOM   773  O  OG  . SER A 1 106 ? 32.655 -10.619 -0.434  1.00 47.94 ? 105 SER A OG  1 
ATOM   774  N  N   . LEU A 1 107 ? 32.833 -8.015  0.954   1.00 43.64 ? 106 LEU A N   1 
ATOM   775  C  CA  . LEU A 1 107 ? 32.655 -7.535  2.318   1.00 44.18 ? 106 LEU A CA  1 
ATOM   776  C  C   . LEU A 1 107 ? 32.337 -8.702  3.251   1.00 45.42 ? 106 LEU A C   1 
ATOM   777  O  O   . LEU A 1 107 ? 31.978 -8.507  4.414   1.00 45.45 ? 106 LEU A O   1 
ATOM   778  C  CB  . LEU A 1 107 ? 31.539 -6.489  2.388   1.00 42.14 ? 106 LEU A CB  1 
ATOM   779  C  CG  . LEU A 1 107 ? 31.640 -5.255  1.482   1.00 41.25 ? 106 LEU A CG  1 
ATOM   780  C  CD1 . LEU A 1 107 ? 30.832 -4.123  2.109   1.00 41.27 ? 106 LEU A CD1 1 
ATOM   781  C  CD2 . LEU A 1 107 ? 33.079 -4.821  1.311   1.00 41.95 ? 106 LEU A CD2 1 
ATOM   782  N  N   . SER A 1 108 ? 32.480 -9.918  2.732   1.00 45.93 ? 107 SER A N   1 
ATOM   783  C  CA  . SER A 1 108 ? 32.221 -11.120 3.515   1.00 46.32 ? 107 SER A CA  1 
ATOM   784  C  C   . SER A 1 108 ? 33.003 -12.299 2.944   1.00 46.50 ? 107 SER A C   1 
ATOM   785  O  O   . SER A 1 108 ? 33.466 -12.248 1.808   1.00 44.87 ? 107 SER A O   1 
ATOM   786  C  CB  . SER A 1 108 ? 30.729 -11.441 3.505   1.00 48.34 ? 107 SER A CB  1 
ATOM   787  O  OG  . SER A 1 108 ? 30.293 -11.717 2.188   1.00 52.12 ? 107 SER A OG  1 
ATOM   788  N  N   . GLY A 1 109 ? 33.153 -13.350 3.745   1.00 47.17 ? 108 GLY A N   1 
ATOM   789  C  CA  . GLY A 1 109 ? 33.874 -14.528 3.301   1.00 48.08 ? 108 GLY A CA  1 
ATOM   790  C  C   . GLY A 1 109 ? 35.387 -14.400 3.396   1.00 49.22 ? 108 GLY A C   1 
ATOM   791  O  O   . GLY A 1 109 ? 35.910 -13.519 4.079   1.00 48.77 ? 108 GLY A O   1 
ATOM   792  N  N   . ASP A 1 110 ? 36.089 -15.300 2.711   1.00 49.87 ? 109 ASP A N   1 
ATOM   793  C  CA  . ASP A 1 110 ? 37.550 -15.305 2.704   1.00 50.85 ? 109 ASP A CA  1 
ATOM   794  C  C   . ASP A 1 110 ? 38.156 -14.154 1.897   1.00 49.76 ? 109 ASP A C   1 
ATOM   795  O  O   . ASP A 1 110 ? 39.353 -13.881 2.018   1.00 51.49 ? 109 ASP A O   1 
ATOM   796  C  CB  . ASP A 1 110 ? 38.092 -16.631 2.152   1.00 52.08 ? 109 ASP A CB  1 
ATOM   797  C  CG  . ASP A 1 110 ? 37.776 -17.807 3.054   0.00 52.56 ? 109 ASP A CG  1 
ATOM   798  O  OD1 . ASP A 1 110 ? 37.312 -17.580 4.195   0.00 52.92 ? 109 ASP A OD1 1 
ATOM   799  O  OD2 . ASP A 1 110 ? 37.985 -18.962 2.631   0.00 52.92 ? 109 ASP A OD2 1 
ATOM   800  N  N   . HIS A 1 111 ? 37.344 -13.500 1.065   1.00 47.72 ? 110 HIS A N   1 
ATOM   801  C  CA  . HIS A 1 111 ? 37.800 -12.370 0.249   1.00 45.10 ? 110 HIS A CA  1 
ATOM   802  C  C   . HIS A 1 111 ? 37.409 -11.049 0.903   1.00 42.63 ? 110 HIS A C   1 
ATOM   803  O  O   . HIS A 1 111 ? 37.616 -9.983  0.318   1.00 42.39 ? 110 HIS A O   1 
ATOM   804  C  CB  . HIS A 1 111 ? 37.159 -12.434 -1.142  1.00 48.53 ? 110 HIS A CB  1 
ATOM   805  C  CG  . HIS A 1 111 ? 37.750 -13.479 -2.037  1.00 51.35 ? 110 HIS A CG  1 
ATOM   806  N  ND1 . HIS A 1 111 ? 38.343 -14.624 -1.550  1.00 52.83 ? 110 HIS A ND1 1 
ATOM   807  C  CD2 . HIS A 1 111 ? 37.809 -13.567 -3.386  1.00 51.20 ? 110 HIS A CD2 1 
ATOM   808  C  CE1 . HIS A 1 111 ? 38.742 -15.373 -2.563  1.00 52.91 ? 110 HIS A CE1 1 
ATOM   809  N  NE2 . HIS A 1 111 ? 38.429 -14.756 -3.687  1.00 54.02 ? 110 HIS A NE2 1 
ATOM   810  N  N   . SER A 1 112 ? 36.849 -11.121 2.108   1.00 39.35 ? 111 SER A N   1 
ATOM   811  C  CA  . SER A 1 112 ? 36.406 -9.920  2.819   1.00 36.92 ? 111 SER A CA  1 
ATOM   812  C  C   . SER A 1 112 ? 37.535 -8.927  3.087   1.00 36.19 ? 111 SER A C   1 
ATOM   813  O  O   . SER A 1 112 ? 38.626 -9.310  3.509   1.00 35.45 ? 111 SER A O   1 
ATOM   814  C  CB  . SER A 1 112 ? 35.755 -10.308 4.141   1.00 36.41 ? 111 SER A CB  1 
ATOM   815  O  OG  . SER A 1 112 ? 35.186 -9.169  4.758   1.00 40.53 ? 111 SER A OG  1 
ATOM   816  N  N   . ILE A 1 113 ? 37.267 -7.648  2.850   1.00 35.48 ? 112 ILE A N   1 
ATOM   817  C  CA  . ILE A 1 113 ? 38.277 -6.623  3.074   1.00 34.38 ? 112 ILE A CA  1 
ATOM   818  C  C   . ILE A 1 113 ? 38.000 -5.814  4.347   1.00 33.85 ? 112 ILE A C   1 
ATOM   819  O  O   . ILE A 1 113 ? 38.690 -4.836  4.632   1.00 34.78 ? 112 ILE A O   1 
ATOM   820  C  CB  . ILE A 1 113 ? 38.388 -5.669  1.858   1.00 34.53 ? 112 ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 113 ? 37.077 -4.903  1.662   1.00 35.19 ? 112 ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 113 ? 38.726 -6.480  0.597   1.00 33.31 ? 112 ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 113 ? 37.117 -3.903  0.507   1.00 35.94 ? 112 ILE A CD1 1 
ATOM   824  N  N   . ILE A 1 114 ? 36.997 -6.219  5.115   1.00 31.31 ? 113 ILE A N   1 
ATOM   825  C  CA  . ILE A 1 114 ? 36.689 -5.510  6.351   1.00 31.88 ? 113 ILE A CA  1 
ATOM   826  C  C   . ILE A 1 114 ? 37.831 -5.709  7.351   1.00 32.62 ? 113 ILE A C   1 
ATOM   827  O  O   . ILE A 1 114 ? 38.296 -6.825  7.564   1.00 31.42 ? 113 ILE A O   1 
ATOM   828  C  CB  . ILE A 1 114 ? 35.356 -6.005  6.952   1.00 33.38 ? 113 ILE A CB  1 
ATOM   829  C  CG1 . ILE A 1 114 ? 34.206 -5.619  6.011   1.00 34.03 ? 113 ILE A CG1 1 
ATOM   830  C  CG2 . ILE A 1 114 ? 35.135 -5.403  8.340   1.00 33.49 ? 113 ILE A CG2 1 
ATOM   831  C  CD1 . ILE A 1 114 ? 32.846 -6.071  6.470   1.00 35.80 ? 113 ILE A CD1 1 
ATOM   832  N  N   . GLY A 1 115 ? 38.291 -4.617  7.954   1.00 30.94 ? 114 GLY A N   1 
ATOM   833  C  CA  . GLY A 1 115 ? 39.375 -4.713  8.911   1.00 27.86 ? 114 GLY A CA  1 
ATOM   834  C  C   . GLY A 1 115 ? 40.739 -4.735  8.238   1.00 28.77 ? 114 GLY A C   1 
ATOM   835  O  O   . GLY A 1 115 ? 41.750 -4.964  8.897   1.00 28.98 ? 114 GLY A O   1 
ATOM   836  N  N   . ARG A 1 116 ? 40.778 -4.514  6.925   1.00 27.58 ? 115 ARG A N   1 
ATOM   837  C  CA  . ARG A 1 116 ? 42.038 -4.489  6.201   1.00 27.93 ? 115 ARG A CA  1 
ATOM   838  C  C   . ARG A 1 116 ? 42.327 -3.022  5.850   1.00 27.94 ? 115 ARG A C   1 
ATOM   839  O  O   . ARG A 1 116 ? 41.606 -2.141  6.319   1.00 30.51 ? 115 ARG A O   1 
ATOM   840  C  CB  . ARG A 1 116 ? 41.963 -5.427  4.975   1.00 26.78 ? 115 ARG A CB  1 
ATOM   841  C  CG  . ARG A 1 116 ? 41.724 -6.904  5.416   1.00 27.72 ? 115 ARG A CG  1 
ATOM   842  C  CD  . ARG A 1 116 ? 41.935 -7.949  4.318   1.00 27.75 ? 115 ARG A CD  1 
ATOM   843  N  NE  . ARG A 1 116 ? 41.550 -9.297  4.761   1.00 28.98 ? 115 ARG A NE  1 
ATOM   844  C  CZ  . ARG A 1 116 ? 42.312 -10.125 5.478   1.00 30.92 ? 115 ARG A CZ  1 
ATOM   845  N  NH1 . ARG A 1 116 ? 41.842 -11.321 5.825   1.00 31.94 ? 115 ARG A NH1 1 
ATOM   846  N  NH2 . ARG A 1 116 ? 43.543 -9.780  5.840   1.00 27.67 ? 115 ARG A NH2 1 
ATOM   847  N  N   . THR A 1 117 ? 43.363 -2.735  5.068   1.00 28.62 ? 116 THR A N   1 
ATOM   848  C  CA  . THR A 1 117 ? 43.686 -1.330  4.773   1.00 26.22 ? 116 THR A CA  1 
ATOM   849  C  C   . THR A 1 117 ? 43.605 -0.939  3.307   1.00 26.60 ? 116 THR A C   1 
ATOM   850  O  O   . THR A 1 117 ? 43.988 -1.702  2.421   1.00 27.45 ? 116 THR A O   1 
ATOM   851  C  CB  . THR A 1 117 ? 45.117 -0.955  5.285   1.00 27.86 ? 116 THR A CB  1 
ATOM   852  O  OG1 . THR A 1 117 ? 45.201 -1.170  6.703   1.00 28.16 ? 116 THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 117 ? 45.429 0.519   4.995   1.00 29.30 ? 116 THR A CG2 1 
ATOM   854  N  N   . LEU A 1 118 ? 43.091 0.258   3.052   1.00 27.39 ? 117 LEU A N   1 
ATOM   855  C  CA  . LEU A 1 118 ? 43.008 0.766   1.688   1.00 30.02 ? 117 LEU A CA  1 
ATOM   856  C  C   . LEU A 1 118 ? 44.189 1.722   1.573   1.00 30.43 ? 117 LEU A C   1 
ATOM   857  O  O   . LEU A 1 118 ? 44.415 2.540   2.469   1.00 31.38 ? 117 LEU A O   1 
ATOM   858  C  CB  . LEU A 1 118 ? 41.689 1.513   1.457   1.00 32.57 ? 117 LEU A CB  1 
ATOM   859  C  CG  . LEU A 1 118 ? 41.503 2.097   0.051   1.00 33.79 ? 117 LEU A CG  1 
ATOM   860  C  CD1 . LEU A 1 118 ? 41.505 0.972   -0.979  1.00 33.70 ? 117 LEU A CD1 1 
ATOM   861  C  CD2 . LEU A 1 118 ? 40.192 2.879   -0.018  1.00 32.08 ? 117 LEU A CD2 1 
ATOM   862  N  N   . VAL A 1 119 ? 44.962 1.613   0.499   1.00 29.67 ? 118 VAL A N   1 
ATOM   863  C  CA  . VAL A 1 119 ? 46.134 2.481   0.332   1.00 32.22 ? 118 VAL A CA  1 
ATOM   864  C  C   . VAL A 1 119 ? 46.169 3.198   -1.016  1.00 31.95 ? 118 VAL A C   1 
ATOM   865  O  O   . VAL A 1 119 ? 45.796 2.625   -2.039  1.00 34.80 ? 118 VAL A O   1 
ATOM   866  C  CB  . VAL A 1 119 ? 47.453 1.659   0.483   1.00 32.06 ? 118 VAL A CB  1 
ATOM   867  C  CG1 . VAL A 1 119 ? 48.675 2.559   0.309   1.00 30.91 ? 118 VAL A CG1 1 
ATOM   868  C  CG2 . VAL A 1 119 ? 47.493 0.983   1.841   1.00 32.79 ? 118 VAL A CG2 1 
ATOM   869  N  N   . VAL A 1 120 ? 46.614 4.451   -0.992  1.00 31.82 ? 119 VAL A N   1 
ATOM   870  C  CA  . VAL A 1 120 ? 46.753 5.264   -2.198  1.00 32.15 ? 119 VAL A CA  1 
ATOM   871  C  C   . VAL A 1 120 ? 48.259 5.521   -2.340  1.00 32.23 ? 119 VAL A C   1 
ATOM   872  O  O   . VAL A 1 120 ? 48.933 5.947   -1.377  1.00 32.03 ? 119 VAL A O   1 
ATOM   873  C  CB  . VAL A 1 120 ? 45.937 6.594   -2.094  1.00 30.55 ? 119 VAL A CB  1 
ATOM   874  C  CG1 . VAL A 1 120 ? 46.432 7.445   -0.937  1.00 33.46 ? 119 VAL A CG1 1 
ATOM   875  C  CG2 . VAL A 1 120 ? 46.021 7.359   -3.401  1.00 34.22 ? 119 VAL A CG2 1 
ATOM   876  N  N   . HIS A 1 121 ? 48.793 5.239   -3.522  1.00 33.15 ? 120 HIS A N   1 
ATOM   877  C  CA  . HIS A 1 121 ? 50.227 5.361   -3.743  1.00 33.04 ? 120 HIS A CA  1 
ATOM   878  C  C   . HIS A 1 121 ? 50.738 6.611   -4.465  1.00 36.93 ? 120 HIS A C   1 
ATOM   879  O  O   . HIS A 1 121 ? 50.000 7.294   -5.171  1.00 34.25 ? 120 HIS A O   1 
ATOM   880  C  CB  . HIS A 1 121 ? 50.679 4.145   -4.528  1.00 31.85 ? 120 HIS A CB  1 
ATOM   881  C  CG  . HIS A 1 121 ? 50.652 2.872   -3.743  1.00 30.89 ? 120 HIS A CG  1 
ATOM   882  N  ND1 . HIS A 1 121 ? 51.747 2.414   -3.042  1.00 33.04 ? 120 HIS A ND1 1 
ATOM   883  C  CD2 . HIS A 1 121 ? 49.654 1.988   -3.500  1.00 30.56 ? 120 HIS A CD2 1 
ATOM   884  C  CE1 . HIS A 1 121 ? 51.426 1.306   -2.399  1.00 31.83 ? 120 HIS A CE1 1 
ATOM   885  N  NE2 . HIS A 1 121 ? 50.161 1.025   -2.657  1.00 28.43 ? 120 HIS A NE2 1 
ATOM   886  N  N   . GLU A 1 122 ? 52.048 6.822   -4.339  1.00 39.11 ? 121 GLU A N   1 
ATOM   887  C  CA  . GLU A 1 122 ? 52.773 7.947   -4.940  1.00 42.05 ? 121 GLU A CA  1 
ATOM   888  C  C   . GLU A 1 122 ? 52.792 7.876   -6.456  1.00 43.16 ? 121 GLU A C   1 
ATOM   889  O  O   . GLU A 1 122 ? 52.504 8.859   -7.134  1.00 45.13 ? 121 GLU A O   1 
ATOM   890  C  CB  . GLU A 1 122 ? 54.218 7.991   -4.388  1.00 45.28 ? 121 GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 122 ? 55.112 9.119   -4.917  1.00 49.74 ? 121 GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 122 ? 56.511 9.081   -4.311  1.00 52.24 ? 121 GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 122 ? 56.645 9.311   -3.089  1.00 55.33 ? 121 GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 122 ? 57.479 8.810   -5.052  1.00 55.88 ? 121 GLU A OE2 1 
ATOM   895  N  N   . LYS A 1 123 ? 53.084 6.690   -6.975  1.00 41.43 ? 122 LYS A N   1 
ATOM   896  C  CA  . LYS A 1 123 ? 53.156 6.483   -8.410  1.00 41.76 ? 122 LYS A CA  1 
ATOM   897  C  C   . LYS A 1 123 ? 52.027 5.601   -8.963  1.00 42.57 ? 122 LYS A C   1 
ATOM   898  O  O   . LYS A 1 123 ? 51.191 5.088   -8.215  1.00 42.47 ? 122 LYS A O   1 
ATOM   899  C  CB  . LYS A 1 123 ? 54.518 5.874   -8.761  1.00 41.67 ? 122 LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 123 ? 55.689 6.530   -8.014  1.00 41.74 ? 122 LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 123 ? 57.056 6.040   -8.501  1.00 44.12 ? 122 LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 123 ? 57.211 4.541   -8.342  1.00 44.18 ? 122 LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 123 ? 58.548 4.069   -8.789  1.00 45.97 ? 122 LYS A NZ  1 
ATOM   904  N  N   . ALA A 1 124 ? 52.004 5.436   -10.282 1.00 40.97 ? 123 ALA A N   1 
ATOM   905  C  CA  . ALA A 1 124 ? 50.990 4.620   -10.935 1.00 39.76 ? 123 ALA A CA  1 
ATOM   906  C  C   . ALA A 1 124 ? 51.320 3.132   -10.823 1.00 40.68 ? 123 ALA A C   1 
ATOM   907  O  O   . ALA A 1 124 ? 52.485 2.745   -10.774 1.00 41.61 ? 123 ALA A O   1 
ATOM   908  C  CB  . ALA A 1 124 ? 50.875 5.017   -12.413 1.00 39.12 ? 123 ALA A CB  1 
ATOM   909  N  N   . ASP A 1 125 ? 50.283 2.304   -10.779 1.00 40.29 ? 124 ASP A N   1 
ATOM   910  C  CA  . ASP A 1 125 ? 50.446 0.857   -10.705 1.00 41.67 ? 124 ASP A CA  1 
ATOM   911  C  C   . ASP A 1 125 ? 50.551 0.364   -12.152 1.00 41.63 ? 124 ASP A C   1 
ATOM   912  O  O   . ASP A 1 125 ? 49.610 0.522   -12.929 1.00 42.13 ? 124 ASP A O   1 
ATOM   913  C  CB  . ASP A 1 125 ? 49.227 0.241   -10.008 1.00 39.86 ? 124 ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 125 ? 49.261 -1.275  -9.983  1.00 40.60 ? 124 ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 125 ? 48.439 -1.865  -9.248  1.00 39.03 ? 124 ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 125 ? 50.096 -1.877  -10.689 1.00 42.58 ? 124 ASP A OD2 1 
ATOM   917  N  N   . ASP A 1 126 ? 51.689 -0.223  -12.511 1.00 40.92 ? 125 ASP A N   1 
ATOM   918  C  CA  . ASP A 1 126 ? 51.895 -0.702  -13.877 1.00 40.78 ? 125 ASP A CA  1 
ATOM   919  C  C   . ASP A 1 126 ? 51.127 -1.978  -14.217 1.00 41.27 ? 125 ASP A C   1 
ATOM   920  O  O   . ASP A 1 126 ? 51.400 -2.635  -15.218 1.00 43.01 ? 125 ASP A O   1 
ATOM   921  C  CB  . ASP A 1 126 ? 53.395 -0.883  -14.153 1.00 40.75 ? 125 ASP A CB  1 
ATOM   922  C  CG  . ASP A 1 126 ? 54.004 -2.042  -13.391 1.00 39.56 ? 125 ASP A CG  1 
ATOM   923  O  OD1 . ASP A 1 126 ? 55.236 -2.028  -13.192 1.00 42.06 ? 125 ASP A OD1 1 
ATOM   924  O  OD2 . ASP A 1 126 ? 53.265 -2.968  -13.009 1.00 38.63 ? 125 ASP A OD2 1 
ATOM   925  N  N   . LEU A 1 127 ? 50.168 -2.319  -13.369 1.00 41.04 ? 126 LEU A N   1 
ATOM   926  C  CA  . LEU A 1 127 ? 49.314 -3.481  -13.568 1.00 41.88 ? 126 LEU A CA  1 
ATOM   927  C  C   . LEU A 1 127 ? 50.047 -4.783  -13.847 1.00 42.25 ? 126 LEU A C   1 
ATOM   928  O  O   . LEU A 1 127 ? 49.447 -5.739  -14.334 1.00 43.02 ? 126 LEU A O   1 
ATOM   929  C  CB  . LEU A 1 127 ? 48.332 -3.196  -14.705 1.00 41.15 ? 126 LEU A CB  1 
ATOM   930  C  CG  . LEU A 1 127 ? 47.707 -1.801  -14.633 1.00 42.30 ? 126 LEU A CG  1 
ATOM   931  C  CD1 . LEU A 1 127 ? 46.638 -1.669  -15.694 1.00 41.74 ? 126 LEU A CD1 1 
ATOM   932  C  CD2 . LEU A 1 127 ? 47.120 -1.562  -13.253 1.00 39.62 ? 126 LEU A CD2 1 
ATOM   933  N  N   . GLY A 1 128 ? 51.339 -4.825  -13.545 1.00 42.76 ? 127 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 128 ? 52.104 -6.038  -13.769 1.00 42.52 ? 127 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 128 ? 52.649 -6.165  -15.180 1.00 43.91 ? 127 GLY A C   1 
ATOM   936  O  O   . GLY A 1 128 ? 52.975 -7.265  -15.631 1.00 42.78 ? 127 GLY A O   1 
ATOM   937  N  N   . LYS A 1 129 ? 52.751 -5.040  -15.880 1.00 44.01 ? 128 LYS A N   1 
ATOM   938  C  CA  . LYS A 1 129 ? 53.255 -5.044  -17.249 1.00 45.22 ? 128 LYS A CA  1 
ATOM   939  C  C   . LYS A 1 129 ? 54.618 -4.369  -17.326 1.00 45.74 ? 128 LYS A C   1 
ATOM   940  O  O   . LYS A 1 129 ? 55.122 -4.096  -18.412 1.00 46.08 ? 128 LYS A O   1 
ATOM   941  C  CB  . LYS A 1 129 ? 52.276 -4.320  -18.183 1.00 47.77 ? 128 LYS A CB  1 
ATOM   942  C  CG  . LYS A 1 129 ? 50.849 -4.843  -18.137 1.00 48.17 ? 128 LYS A CG  1 
ATOM   943  C  CD  . LYS A 1 129 ? 50.791 -6.329  -18.445 1.00 51.83 ? 128 LYS A CD  1 
ATOM   944  C  CE  . LYS A 1 129 ? 49.383 -6.884  -18.266 1.00 53.31 ? 128 LYS A CE  1 
ATOM   945  N  NZ  . LYS A 1 129 ? 48.395 -6.208  -19.150 0.00 53.24 ? 128 LYS A NZ  1 
ATOM   946  N  N   . GLY A 1 130 ? 55.213 -4.094  -16.170 1.00 44.87 ? 129 GLY A N   1 
ATOM   947  C  CA  . GLY A 1 130 ? 56.513 -3.454  -16.154 1.00 43.64 ? 129 GLY A CA  1 
ATOM   948  C  C   . GLY A 1 130 ? 57.610 -4.440  -16.513 1.00 43.54 ? 129 GLY A C   1 
ATOM   949  O  O   . GLY A 1 130 ? 57.442 -5.648  -16.347 1.00 44.67 ? 129 GLY A O   1 
ATOM   950  N  N   . GLY A 1 131 ? 58.733 -3.920  -16.998 1.00 42.50 ? 130 GLY A N   1 
ATOM   951  C  CA  . GLY A 1 131 ? 59.851 -4.763  -17.378 1.00 42.41 ? 130 GLY A CA  1 
ATOM   952  C  C   . GLY A 1 131 ? 60.821 -5.036  -16.244 1.00 42.57 ? 130 GLY A C   1 
ATOM   953  O  O   . GLY A 1 131 ? 62.021 -4.772  -16.358 1.00 42.96 ? 130 GLY A O   1 
ATOM   954  N  N   . ASN A 1 132 ? 60.297 -5.559  -15.141 1.00 40.28 ? 131 ASN A N   1 
ATOM   955  C  CA  . ASN A 1 132 ? 61.117 -5.888  -13.984 1.00 38.61 ? 131 ASN A CA  1 
ATOM   956  C  C   . ASN A 1 132 ? 60.351 -6.852  -13.087 1.00 39.51 ? 131 ASN A C   1 
ATOM   957  O  O   . ASN A 1 132 ? 59.165 -7.104  -13.304 1.00 38.31 ? 131 ASN A O   1 
ATOM   958  C  CB  . ASN A 1 132 ? 61.480 -4.625  -13.207 1.00 37.26 ? 131 ASN A CB  1 
ATOM   959  C  CG  . ASN A 1 132 ? 60.269 -3.765  -12.892 1.00 37.58 ? 131 ASN A CG  1 
ATOM   960  O  OD1 . ASN A 1 132 ? 59.364 -4.183  -12.173 1.00 37.09 ? 131 ASN A OD1 1 
ATOM   961  N  ND2 . ASN A 1 132 ? 60.249 -2.556  -13.438 1.00 37.89 ? 131 ASN A ND2 1 
ATOM   962  N  N   . GLU A 1 133 ? 61.039 -7.392  -12.084 1.00 39.06 ? 132 GLU A N   1 
ATOM   963  C  CA  . GLU A 1 133 ? 60.431 -8.337  -11.157 1.00 39.43 ? 132 GLU A CA  1 
ATOM   964  C  C   . GLU A 1 133 ? 59.406 -7.695  -10.226 1.00 39.43 ? 132 GLU A C   1 
ATOM   965  O  O   . GLU A 1 133 ? 58.350 -8.274  -9.960  1.00 40.42 ? 132 GLU A O   1 
ATOM   966  C  CB  . GLU A 1 133 ? 61.523 -9.012  -10.328 1.00 40.79 ? 132 GLU A CB  1 
ATOM   967  C  CG  . GLU A 1 133 ? 62.478 -9.882  -11.140 1.00 43.03 ? 132 GLU A CG  1 
ATOM   968  C  CD  . GLU A 1 133 ? 61.788 -11.086 -11.760 1.00 47.73 ? 132 GLU A CD  1 
ATOM   969  O  OE1 . GLU A 1 133 ? 61.087 -11.808 -11.023 1.00 48.88 ? 132 GLU A OE1 1 
ATOM   970  O  OE2 . GLU A 1 133 ? 61.948 -11.318 -12.981 1.00 51.37 ? 132 GLU A OE2 1 
ATOM   971  N  N   . GLU A 1 134 ? 59.716 -6.495  -9.743  1.00 38.33 ? 133 GLU A N   1 
ATOM   972  C  CA  . GLU A 1 134 ? 58.839 -5.792  -8.820  1.00 38.62 ? 133 GLU A CA  1 
ATOM   973  C  C   . GLU A 1 134 ? 57.431 -5.594  -9.366  1.00 39.99 ? 133 GLU A C   1 
ATOM   974  O  O   . GLU A 1 134 ? 56.460 -5.590  -8.610  1.00 40.55 ? 133 GLU A O   1 
ATOM   975  C  CB  . GLU A 1 134 ? 59.443 -4.435  -8.452  1.00 39.36 ? 133 GLU A CB  1 
ATOM   976  C  CG  . GLU A 1 134 ? 58.663 -3.708  -7.368  1.00 39.54 ? 133 GLU A CG  1 
ATOM   977  C  CD  . GLU A 1 134 ? 58.620 -4.502  -6.079  1.00 41.13 ? 133 GLU A CD  1 
ATOM   978  O  OE1 . GLU A 1 134 ? 57.743 -4.227  -5.236  1.00 40.36 ? 133 GLU A OE1 1 
ATOM   979  O  OE2 . GLU A 1 134 ? 59.470 -5.403  -5.907  1.00 38.61 ? 133 GLU A OE2 1 
ATOM   980  N  N   . SER A 1 135 ? 57.329 -5.447  -10.683 1.00 41.81 ? 134 SER A N   1 
ATOM   981  C  CA  . SER A 1 135 ? 56.052 -5.227  -11.343 1.00 41.20 ? 134 SER A CA  1 
ATOM   982  C  C   . SER A 1 135 ? 54.994 -6.272  -11.014 1.00 41.71 ? 134 SER A C   1 
ATOM   983  O  O   . SER A 1 135 ? 53.828 -5.939  -10.831 1.00 42.08 ? 134 SER A O   1 
ATOM   984  C  CB  . SER A 1 135 ? 56.254 -5.160  -12.857 1.00 41.40 ? 134 SER A CB  1 
ATOM   985  O  OG  . SER A 1 135 ? 55.014 -4.973  -13.516 1.00 41.73 ? 134 SER A OG  1 
ATOM   986  N  N   . THR A 1 136 ? 55.391 -7.535  -10.946 1.00 42.67 ? 135 THR A N   1 
ATOM   987  C  CA  . THR A 1 136 ? 54.443 -8.597  -10.633 1.00 42.98 ? 135 THR A CA  1 
ATOM   988  C  C   . THR A 1 136 ? 54.315 -8.805  -9.128  1.00 41.40 ? 135 THR A C   1 
ATOM   989  O  O   . THR A 1 136 ? 53.692 -9.765  -8.685  1.00 41.62 ? 135 THR A O   1 
ATOM   990  C  CB  . THR A 1 136 ? 54.850 -9.936  -11.296 1.00 45.17 ? 135 THR A CB  1 
ATOM   991  O  OG1 . THR A 1 136 ? 56.244 -10.176 -11.078 1.00 46.02 ? 135 THR A OG1 1 
ATOM   992  C  CG2 . THR A 1 136 ? 54.577 -9.897  -12.795 1.00 48.66 ? 135 THR A CG2 1 
ATOM   993  N  N   . LYS A 1 137 ? 54.908 -7.900  -8.351  1.00 41.83 ? 136 LYS A N   1 
ATOM   994  C  CA  . LYS A 1 137 ? 54.851 -7.965  -6.891  1.00 42.09 ? 136 LYS A CA  1 
ATOM   995  C  C   . LYS A 1 137 ? 53.982 -6.830  -6.372  1.00 42.33 ? 136 LYS A C   1 
ATOM   996  O  O   . LYS A 1 137 ? 52.982 -7.062  -5.695  1.00 43.17 ? 136 LYS A O   1 
ATOM   997  C  CB  . LYS A 1 137 ? 56.247 -7.824  -6.263  1.00 44.80 ? 136 LYS A CB  1 
ATOM   998  C  CG  . LYS A 1 137 ? 57.279 -8.884  -6.659  1.00 46.96 ? 136 LYS A CG  1 
ATOM   999  C  CD  . LYS A 1 137 ? 56.823 -10.300 -6.317  1.00 51.26 ? 136 LYS A CD  1 
ATOM   1000 C  CE  . LYS A 1 137 ? 56.620 -10.497 -4.819  1.00 53.40 ? 136 LYS A CE  1 
ATOM   1001 N  NZ  . LYS A 1 137 ? 56.204 -11.888 -4.487  0.00 52.79 ? 136 LYS A NZ  1 
ATOM   1002 N  N   . THR A 1 138 ? 54.370 -5.599  -6.693  1.00 40.54 ? 137 THR A N   1 
ATOM   1003 C  CA  . THR A 1 138 ? 53.635 -4.429  -6.241  1.00 38.86 ? 137 THR A CA  1 
ATOM   1004 C  C   . THR A 1 138 ? 53.255 -3.451  -7.344  1.00 39.36 ? 137 THR A C   1 
ATOM   1005 O  O   . THR A 1 138 ? 52.786 -2.349  -7.051  1.00 38.78 ? 137 THR A O   1 
ATOM   1006 C  CB  . THR A 1 138 ? 54.437 -3.629  -5.218  1.00 38.20 ? 137 THR A CB  1 
ATOM   1007 O  OG1 . THR A 1 138 ? 55.567 -3.039  -5.864  1.00 38.85 ? 137 THR A OG1 1 
ATOM   1008 C  CG2 . THR A 1 138 ? 54.915 -4.519  -4.099  1.00 36.83 ? 137 THR A CG2 1 
ATOM   1009 N  N   . GLY A 1 139 ? 53.463 -3.837  -8.600  1.00 37.89 ? 138 GLY A N   1 
ATOM   1010 C  CA  . GLY A 1 139 ? 53.135 -2.944  -9.699  1.00 38.42 ? 138 GLY A CA  1 
ATOM   1011 C  C   . GLY A 1 139 ? 53.941 -1.657  -9.688  1.00 37.77 ? 138 GLY A C   1 
ATOM   1012 O  O   . GLY A 1 139 ? 53.605 -0.704  -10.390 1.00 39.46 ? 138 GLY A O   1 
ATOM   1013 N  N   . ASN A 1 140 ? 55.005 -1.627  -8.888  1.00 37.36 ? 139 ASN A N   1 
ATOM   1014 C  CA  . ASN A 1 140 ? 55.877 -0.459  -8.778  1.00 36.35 ? 139 ASN A CA  1 
ATOM   1015 C  C   . ASN A 1 140 ? 55.173 0.844   -8.386  1.00 37.67 ? 139 ASN A C   1 
ATOM   1016 O  O   . ASN A 1 140 ? 55.686 1.933   -8.648  1.00 37.66 ? 139 ASN A O   1 
ATOM   1017 C  CB  . ASN A 1 140 ? 56.627 -0.250  -10.100 1.00 36.78 ? 139 ASN A CB  1 
ATOM   1018 C  CG  . ASN A 1 140 ? 57.821 -1.160  -10.238 1.00 35.53 ? 139 ASN A CG  1 
ATOM   1019 O  OD1 . ASN A 1 140 ? 58.802 -1.024  -9.506  1.00 37.59 ? 139 ASN A OD1 1 
ATOM   1020 N  ND2 . ASN A 1 140 ? 57.748 -2.101  -11.171 1.00 34.96 ? 139 ASN A ND2 1 
ATOM   1021 N  N   . ALA A 1 141 ? 54.018 0.737   -7.740  1.00 38.40 ? 140 ALA A N   1 
ATOM   1022 C  CA  . ALA A 1 141 ? 53.247 1.917   -7.331  1.00 40.95 ? 140 ALA A CA  1 
ATOM   1023 C  C   . ALA A 1 141 ? 53.990 2.864   -6.390  1.00 41.37 ? 140 ALA A C   1 
ATOM   1024 O  O   . ALA A 1 141 ? 53.626 4.035   -6.261  1.00 42.92 ? 140 ALA A O   1 
ATOM   1025 C  CB  . ALA A 1 141 ? 51.937 1.479   -6.698  1.00 39.06 ? 140 ALA A CB  1 
ATOM   1026 N  N   . GLY A 1 142 ? 55.013 2.358   -5.711  1.00 41.56 ? 141 GLY A N   1 
ATOM   1027 C  CA  . GLY A 1 142 ? 55.786 3.215   -4.831  1.00 41.48 ? 141 GLY A CA  1 
ATOM   1028 C  C   . GLY A 1 142 ? 55.302 3.426   -3.405  1.00 42.38 ? 141 GLY A C   1 
ATOM   1029 O  O   . GLY A 1 142 ? 54.592 2.592   -2.834  1.00 39.86 ? 141 GLY A O   1 
ATOM   1030 N  N   . SER A 1 143 ? 55.689 4.565   -2.836  1.00 40.00 ? 142 SER A N   1 
ATOM   1031 C  CA  . SER A 1 143 ? 55.344 4.895   -1.464  1.00 40.95 ? 142 SER A CA  1 
ATOM   1032 C  C   . SER A 1 143 ? 53.855 5.066   -1.207  1.00 40.05 ? 142 SER A C   1 
ATOM   1033 O  O   . SER A 1 143 ? 53.071 5.425   -2.088  1.00 39.03 ? 142 SER A O   1 
ATOM   1034 C  CB  . SER A 1 143 ? 56.087 6.159   -1.017  1.00 42.46 ? 142 SER A CB  1 
ATOM   1035 O  OG  . SER A 1 143 ? 55.461 7.327   -1.512  1.00 45.75 ? 142 SER A OG  1 
ATOM   1036 N  N   . ARG A 1 144 ? 53.484 4.811   0.035   1.00 39.33 ? 143 ARG A N   1 
ATOM   1037 C  CA  . ARG A 1 144 ? 52.110 4.902   0.475   1.00 38.62 ? 143 ARG A CA  1 
ATOM   1038 C  C   . ARG A 1 144 ? 51.875 6.311   0.995   1.00 39.14 ? 143 ARG A C   1 
ATOM   1039 O  O   . ARG A 1 144 ? 52.402 6.689   2.035   1.00 41.68 ? 143 ARG A O   1 
ATOM   1040 C  CB  . ARG A 1 144 ? 51.893 3.850   1.561   1.00 38.36 ? 143 ARG A CB  1 
ATOM   1041 C  CG  . ARG A 1 144 ? 52.521 2.514   1.165   1.00 34.51 ? 143 ARG A CG  1 
ATOM   1042 C  CD  . ARG A 1 144 ? 52.355 1.405   2.195   1.00 35.85 ? 143 ARG A CD  1 
ATOM   1043 N  NE  . ARG A 1 144 ? 52.945 0.165   1.694   1.00 34.95 ? 143 ARG A NE  1 
ATOM   1044 C  CZ  . ARG A 1 144 ? 52.736 -1.042  2.212   1.00 33.70 ? 143 ARG A CZ  1 
ATOM   1045 N  NH1 . ARG A 1 144 ? 53.324 -2.101  1.671   1.00 34.92 ? 143 ARG A NH1 1 
ATOM   1046 N  NH2 . ARG A 1 144 ? 51.940 -1.198  3.263   1.00 32.71 ? 143 ARG A NH2 1 
ATOM   1047 N  N   . LEU A 1 145 ? 51.083 7.088   0.262   1.00 40.59 ? 144 LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 145 ? 50.806 8.469   0.645   1.00 41.26 ? 144 LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 145 ? 49.742 8.577   1.731   1.00 41.63 ? 144 LEU A C   1 
ATOM   1050 O  O   . LEU A 1 145 ? 49.842 9.414   2.625   1.00 41.52 ? 144 LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 145 ? 50.378 9.282   -0.579  1.00 39.94 ? 144 LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 145 ? 51.355 9.302   -1.758  1.00 42.15 ? 144 LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 145 ? 50.829 10.249  -2.828  1.00 41.73 ? 144 LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 145 ? 52.731 9.743   -1.290  1.00 41.79 ? 144 LEU A CD2 1 
ATOM   1055 N  N   . ALA A 1 146 ? 48.717 7.738   1.646   1.00 40.33 ? 145 ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 146 ? 47.658 7.760   2.638   1.00 37.88 ? 145 ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 146 ? 46.992 6.400   2.716   1.00 37.35 ? 145 ALA A C   1 
ATOM   1058 O  O   . ALA A 1 146 ? 46.989 5.637   1.750   1.00 35.14 ? 145 ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 146 ? 46.637 8.831   2.295   1.00 36.76 ? 145 ALA A CB  1 
ATOM   1060 N  N   . CYS A 1 147 ? 46.441 6.094   3.883   1.00 36.54 ? 146 CYS A N   1 
ATOM   1061 C  CA  . CYS A 1 147 ? 45.780 4.820   4.086   1.00 35.12 ? 146 CYS A CA  1 
ATOM   1062 C  C   . CYS A 1 147 ? 44.740 4.949   5.180   1.00 33.51 ? 146 CYS A C   1 
ATOM   1063 O  O   . CYS A 1 147 ? 44.651 5.975   5.845   1.00 29.79 ? 146 CYS A O   1 
ATOM   1064 C  CB  . CYS A 1 147 ? 46.805 3.758   4.478   1.00 34.32 ? 146 CYS A CB  1 
ATOM   1065 S  SG  . CYS A 1 147 ? 47.701 4.139   6.015   1.00 38.20 ? 146 CYS A SG  1 
ATOM   1066 N  N   . GLY A 1 148 ? 43.954 3.895   5.357   1.00 32.80 ? 147 GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 148 ? 42.929 3.896   6.378   1.00 32.60 ? 147 GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 148 ? 42.366 2.495   6.501   1.00 32.43 ? 147 GLY A C   1 
ATOM   1069 O  O   . GLY A 1 148 ? 42.212 1.794   5.501   1.00 31.31 ? 147 GLY A O   1 
ATOM   1070 N  N   . VAL A 1 149 ? 42.071 2.082   7.724   1.00 30.96 ? 148 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 149 ? 41.507 0.759   7.958   1.00 31.44 ? 148 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 149 ? 40.062 0.766   7.475   1.00 32.13 ? 148 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 149 ? 39.327 1.723   7.723   1.00 32.29 ? 148 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 149 ? 41.539 0.400   9.453   1.00 30.72 ? 148 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 149 ? 40.919 -0.972  9.655   1.00 25.82 ? 148 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 149 ? 42.985 0.426   9.960   1.00 28.58 ? 148 VAL A CG2 1 
ATOM   1077 N  N   . ILE A 1 150 ? 39.663 -0.304  6.792   1.00 30.91 ? 149 ILE A N   1 
ATOM   1078 C  CA  . ILE A 1 150 ? 38.322 -0.433  6.242   1.00 30.63 ? 149 ILE A CA  1 
ATOM   1079 C  C   . ILE A 1 150 ? 37.334 -0.879  7.305   1.00 32.94 ? 149 ILE A C   1 
ATOM   1080 O  O   . ILE A 1 150 ? 37.380 -2.019  7.782   1.00 33.99 ? 149 ILE A O   1 
ATOM   1081 C  CB  . ILE A 1 150 ? 38.331 -1.423  5.062   1.00 31.13 ? 149 ILE A CB  1 
ATOM   1082 C  CG1 . ILE A 1 150 ? 39.263 -0.898  3.968   1.00 30.43 ? 149 ILE A CG1 1 
ATOM   1083 C  CG2 . ILE A 1 150 ? 36.923 -1.632  4.536   1.00 32.88 ? 149 ILE A CG2 1 
ATOM   1084 C  CD1 . ILE A 1 150 ? 39.420 -1.839  2.756   1.00 33.63 ? 149 ILE A CD1 1 
ATOM   1085 N  N   . GLY A 1 151 ? 36.433 0.027   7.670   1.00 30.88 ? 150 GLY A N   1 
ATOM   1086 C  CA  . GLY A 1 151 ? 35.472 -0.275  8.710   1.00 32.40 ? 150 GLY A CA  1 
ATOM   1087 C  C   . GLY A 1 151 ? 34.005 -0.244  8.335   1.00 33.49 ? 150 GLY A C   1 
ATOM   1088 O  O   . GLY A 1 151 ? 33.606 0.354   7.333   1.00 34.02 ? 150 GLY A O   1 
ATOM   1089 N  N   . ILE A 1 152 ? 33.199 -0.881  9.176   1.00 34.30 ? 151 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 152 ? 31.764 -0.966  8.962   1.00 35.44 ? 151 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 152 ? 31.086 0.402   9.063   1.00 37.22 ? 151 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 152 ? 31.295 1.153   10.020  1.00 34.58 ? 151 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 152 ? 31.125 -1.960  9.965   1.00 34.37 ? 151 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 152 ? 31.738 -3.347  9.755   1.00 33.94 ? 151 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 152 ? 29.609 -2.023  9.762   1.00 33.29 ? 151 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 152 ? 31.242 -4.398  10.719  1.00 35.98 ? 151 ILE A CD1 1 
ATOM   1097 N  N   . ALA A 1 153 ? 30.279 0.722   8.056   1.00 36.47 ? 152 ALA A N   1 
ATOM   1098 C  CA  . ALA A 1 153 ? 29.576 1.992   8.025   1.00 38.02 ? 152 ALA A CA  1 
ATOM   1099 C  C   . ALA A 1 153 ? 28.077 1.781   8.150   1.00 40.14 ? 152 ALA A C   1 
ATOM   1100 O  O   . ALA A 1 153 ? 27.565 0.692   7.893   1.00 38.70 ? 152 ALA A O   1 
ATOM   1101 C  CB  . ALA A 1 153 ? 29.900 2.739   6.732   1.00 39.58 ? 152 ALA A CB  1 
ATOM   1102 N  N   . GLN A 1 154 ? 27.384 2.834   8.563   1.00 42.58 ? 153 GLN A N   1 
ATOM   1103 C  CA  . GLN A 1 154 ? 25.938 2.797   8.742   1.00 46.28 ? 153 GLN A CA  1 
ATOM   1104 C  C   . GLN A 1 154 ? 25.178 2.682   7.425   1.00 47.21 ? 153 GLN A C   1 
ATOM   1105 O  O   . GLN A 1 154 ? 25.796 2.952   6.374   1.00 43.34 ? 153 GLN A O   1 
ATOM   1106 C  CB  . GLN A 1 154 ? 25.481 4.043   9.502   1.00 47.90 ? 153 GLN A CB  1 
ATOM   1107 C  CG  . GLN A 1 154 ? 23.980 4.240   9.523   1.00 51.22 ? 153 GLN A CG  1 
ATOM   1108 C  CD  . GLN A 1 154 ? 23.530 5.084   10.689  1.00 51.83 ? 153 GLN A CD  1 
ATOM   1109 O  OE1 . GLN A 1 154 ? 24.025 6.191   10.899  1.00 54.91 ? 153 GLN A OE1 1 
ATOM   1110 N  NE2 . GLN A 1 154 ? 22.582 4.565   11.459  1.00 53.87 ? 153 GLN A NE2 1 
ATOM   1111 O  OXT . GLN A 1 154 ? 23.980 2.326   7.449   1.00 43.34 ? 153 GLN A OXT 1 
ATOM   1112 N  N   . ALA B 1 2   ? 40.619 -14.211 11.182  1.00 41.36 ? 1   ALA B N   1 
ATOM   1113 C  CA  . ALA B 1 2   ? 41.878 -13.828 11.879  1.00 43.19 ? 1   ALA B CA  1 
ATOM   1114 C  C   . ALA B 1 2   ? 41.834 -14.205 13.356  1.00 43.00 ? 1   ALA B C   1 
ATOM   1115 O  O   . ALA B 1 2   ? 40.765 -14.454 13.920  1.00 43.02 ? 1   ALA B O   1 
ATOM   1116 C  CB  . ALA B 1 2   ? 42.108 -12.330 11.742  1.00 44.22 ? 1   ALA B CB  1 
ATOM   1117 N  N   . THR B 1 3   ? 43.004 -14.246 13.982  1.00 42.08 ? 2   THR B N   1 
ATOM   1118 C  CA  . THR B 1 3   ? 43.088 -14.578 15.392  1.00 40.97 ? 2   THR B CA  1 
ATOM   1119 C  C   . THR B 1 3   ? 43.684 -13.411 16.161  1.00 40.50 ? 2   THR B C   1 
ATOM   1120 O  O   . THR B 1 3   ? 43.734 -13.428 17.390  1.00 38.45 ? 2   THR B O   1 
ATOM   1121 C  CB  . THR B 1 3   ? 43.954 -15.838 15.629  1.00 44.84 ? 2   THR B CB  1 
ATOM   1122 O  OG1 . THR B 1 3   ? 45.269 -15.632 15.093  1.00 45.13 ? 2   THR B OG1 1 
ATOM   1123 C  CG2 . THR B 1 3   ? 43.315 -17.051 14.967  1.00 45.13 ? 2   THR B CG2 1 
ATOM   1124 N  N   . LYS B 1 4   ? 44.122 -12.384 15.439  1.00 38.56 ? 3   LYS B N   1 
ATOM   1125 C  CA  . LYS B 1 4   ? 44.709 -11.228 16.098  1.00 38.61 ? 3   LYS B CA  1 
ATOM   1126 C  C   . LYS B 1 4   ? 44.384 -9.913  15.390  1.00 36.89 ? 3   LYS B C   1 
ATOM   1127 O  O   . LYS B 1 4   ? 44.606 -9.774  14.188  1.00 36.58 ? 3   LYS B O   1 
ATOM   1128 C  CB  . LYS B 1 4   ? 46.232 -11.408 16.186  1.00 42.68 ? 3   LYS B CB  1 
ATOM   1129 C  CG  . LYS B 1 4   ? 46.924 -10.379 17.054  1.00 46.30 ? 3   LYS B CG  1 
ATOM   1130 C  CD  . LYS B 1 4   ? 48.442 -10.479 16.971  1.00 52.21 ? 3   LYS B CD  1 
ATOM   1131 C  CE  . LYS B 1 4   ? 48.964 -11.775 17.565  1.00 55.39 ? 3   LYS B CE  1 
ATOM   1132 N  NZ  . LYS B 1 4   ? 50.454 -11.740 17.703  1.00 59.18 ? 3   LYS B NZ  1 
ATOM   1133 N  N   . VAL B 1 5   ? 43.850 -8.954  16.139  1.00 35.01 ? 4   VAL B N   1 
ATOM   1134 C  CA  . VAL B 1 5   ? 43.517 -7.645  15.586  1.00 33.29 ? 4   VAL B CA  1 
ATOM   1135 C  C   . VAL B 1 5   ? 44.078 -6.554  16.494  1.00 33.32 ? 4   VAL B C   1 
ATOM   1136 O  O   . VAL B 1 5   ? 44.475 -6.822  17.631  1.00 30.59 ? 4   VAL B O   1 
ATOM   1137 C  CB  . VAL B 1 5   ? 41.983 -7.452  15.437  1.00 33.52 ? 4   VAL B CB  1 
ATOM   1138 C  CG1 . VAL B 1 5   ? 41.414 -8.489  14.463  1.00 31.84 ? 4   VAL B CG1 1 
ATOM   1139 C  CG2 . VAL B 1 5   ? 41.309 -7.554  16.801  1.00 35.13 ? 4   VAL B CG2 1 
ATOM   1140 N  N   . VAL B 1 6   ? 44.096 -5.322  15.990  1.00 31.73 ? 5   VAL B N   1 
ATOM   1141 C  CA  . VAL B 1 6   ? 44.629 -4.197  16.737  1.00 30.33 ? 5   VAL B CA  1 
ATOM   1142 C  C   . VAL B 1 6   ? 43.900 -2.897  16.411  1.00 30.96 ? 5   VAL B C   1 
ATOM   1143 O  O   . VAL B 1 6   ? 43.348 -2.725  15.316  1.00 31.38 ? 5   VAL B O   1 
ATOM   1144 C  CB  . VAL B 1 6   ? 46.146 -4.015  16.431  1.00 31.71 ? 5   VAL B CB  1 
ATOM   1145 C  CG1 . VAL B 1 6   ? 46.352 -3.778  14.926  1.00 31.37 ? 5   VAL B CG1 1 
ATOM   1146 C  CG2 . VAL B 1 6   ? 46.716 -2.855  17.231  1.00 32.07 ? 5   VAL B CG2 1 
ATOM   1147 N  N   . ALA B 1 7   ? 43.892 -1.992  17.379  1.00 29.75 ? 6   ALA B N   1 
ATOM   1148 C  CA  . ALA B 1 7   ? 43.272 -0.690  17.210  1.00 30.25 ? 6   ALA B CA  1 
ATOM   1149 C  C   . ALA B 1 7   ? 44.248 0.369   17.709  1.00 31.32 ? 6   ALA B C   1 
ATOM   1150 O  O   . ALA B 1 7   ? 44.787 0.264   18.813  1.00 32.74 ? 6   ALA B O   1 
ATOM   1151 C  CB  . ALA B 1 7   ? 41.962 -0.619  17.998  1.00 31.34 ? 6   ALA B CB  1 
ATOM   1152 N  N   . VAL B 1 8   ? 44.491 1.377   16.888  1.00 31.37 ? 7   VAL B N   1 
ATOM   1153 C  CA  . VAL B 1 8   ? 45.389 2.455   17.267  1.00 33.28 ? 7   VAL B CA  1 
ATOM   1154 C  C   . VAL B 1 8   ? 44.501 3.649   17.591  1.00 34.33 ? 7   VAL B C   1 
ATOM   1155 O  O   . VAL B 1 8   ? 43.864 4.221   16.712  1.00 36.20 ? 7   VAL B O   1 
ATOM   1156 C  CB  . VAL B 1 8   ? 46.372 2.785   16.128  1.00 32.05 ? 7   VAL B CB  1 
ATOM   1157 C  CG1 . VAL B 1 8   ? 47.156 4.037   16.462  1.00 31.88 ? 7   VAL B CG1 1 
ATOM   1158 C  CG2 . VAL B 1 8   ? 47.328 1.606   15.929  1.00 31.46 ? 7   VAL B CG2 1 
ATOM   1159 N  N   . LEU B 1 9   ? 44.451 4.002   18.870  1.00 34.00 ? 8   LEU B N   1 
ATOM   1160 C  CA  . LEU B 1 9   ? 43.603 5.093   19.342  1.00 36.11 ? 8   LEU B CA  1 
ATOM   1161 C  C   . LEU B 1 9   ? 44.245 6.460   19.171  1.00 36.88 ? 8   LEU B C   1 
ATOM   1162 O  O   . LEU B 1 9   ? 45.387 6.669   19.563  1.00 37.48 ? 8   LEU B O   1 
ATOM   1163 C  CB  . LEU B 1 9   ? 43.255 4.875   20.818  1.00 34.59 ? 8   LEU B CB  1 
ATOM   1164 C  CG  . LEU B 1 9   ? 42.681 3.495   21.168  1.00 35.87 ? 8   LEU B CG  1 
ATOM   1165 C  CD1 . LEU B 1 9   ? 42.635 3.315   22.669  1.00 36.82 ? 8   LEU B CD1 1 
ATOM   1166 C  CD2 . LEU B 1 9   ? 41.283 3.350   20.578  1.00 37.12 ? 8   LEU B CD2 1 
ATOM   1167 N  N   . LYS B 1 10  ? 43.493 7.380   18.580  1.00 37.77 ? 9   LYS B N   1 
ATOM   1168 C  CA  . LYS B 1 10  ? 43.954 8.743   18.355  1.00 41.27 ? 9   LYS B CA  1 
ATOM   1169 C  C   . LYS B 1 10  ? 42.758 9.682   18.415  1.00 42.99 ? 9   LYS B C   1 
ATOM   1170 O  O   . LYS B 1 10  ? 41.637 9.299   18.066  1.00 40.91 ? 9   LYS B O   1 
ATOM   1171 C  CB  . LYS B 1 10  ? 44.633 8.857   16.990  1.00 43.34 ? 9   LYS B CB  1 
ATOM   1172 C  CG  . LYS B 1 10  ? 45.875 7.995   16.856  1.00 45.61 ? 9   LYS B CG  1 
ATOM   1173 C  CD  . LYS B 1 10  ? 46.396 8.005   15.431  1.00 49.35 ? 9   LYS B CD  1 
ATOM   1174 C  CE  . LYS B 1 10  ? 47.668 7.191   15.303  1.00 49.74 ? 9   LYS B CE  1 
ATOM   1175 N  NZ  . LYS B 1 10  ? 48.137 7.169   13.898  1.00 51.34 ? 9   LYS B NZ  1 
ATOM   1176 N  N   . GLY B 1 11  ? 42.998 10.908  18.865  1.00 44.05 ? 10  GLY B N   1 
ATOM   1177 C  CA  . GLY B 1 11  ? 41.927 11.879  18.955  1.00 47.63 ? 10  GLY B CA  1 
ATOM   1178 C  C   . GLY B 1 11  ? 42.415 13.300  18.751  1.00 51.07 ? 10  GLY B C   1 
ATOM   1179 O  O   . GLY B 1 11  ? 43.563 13.525  18.360  1.00 51.06 ? 10  GLY B O   1 
ATOM   1180 N  N   . ASP B 1 12  ? 41.533 14.259  19.010  1.00 53.59 ? 11  ASP B N   1 
ATOM   1181 C  CA  . ASP B 1 12  ? 41.859 15.673  18.873  1.00 56.55 ? 11  ASP B CA  1 
ATOM   1182 C  C   . ASP B 1 12  ? 42.866 16.099  19.933  1.00 56.78 ? 11  ASP B C   1 
ATOM   1183 O  O   . ASP B 1 12  ? 43.642 17.031  19.727  1.00 58.56 ? 11  ASP B O   1 
ATOM   1184 C  CB  . ASP B 1 12  ? 40.594 16.521  19.018  1.00 58.50 ? 11  ASP B CB  1 
ATOM   1185 C  CG  . ASP B 1 12  ? 39.777 16.574  17.747  1.00 61.09 ? 11  ASP B CG  1 
ATOM   1186 O  OD1 . ASP B 1 12  ? 38.598 16.982  17.815  1.00 62.22 ? 11  ASP B OD1 1 
ATOM   1187 O  OD2 . ASP B 1 12  ? 40.317 16.220  16.677  1.00 63.29 ? 11  ASP B OD2 1 
ATOM   1188 N  N   . GLY B 1 13  ? 42.854 15.408  21.065  1.00 56.44 ? 12  GLY B N   1 
ATOM   1189 C  CA  . GLY B 1 13  ? 43.758 15.759  22.143  1.00 55.28 ? 12  GLY B CA  1 
ATOM   1190 C  C   . GLY B 1 13  ? 45.012 14.919  22.274  1.00 54.62 ? 12  GLY B C   1 
ATOM   1191 O  O   . GLY B 1 13  ? 45.475 14.326  21.297  1.00 56.19 ? 12  GLY B O   1 
ATOM   1192 N  N   . PRO B 1 14  ? 45.583 14.852  23.489  1.00 53.23 ? 13  PRO B N   1 
ATOM   1193 C  CA  . PRO B 1 14  ? 46.795 14.112  23.854  1.00 52.12 ? 13  PRO B CA  1 
ATOM   1194 C  C   . PRO B 1 14  ? 46.588 12.621  24.094  1.00 50.30 ? 13  PRO B C   1 
ATOM   1195 O  O   . PRO B 1 14  ? 47.553 11.881  24.307  1.00 49.95 ? 13  PRO B O   1 
ATOM   1196 C  CB  . PRO B 1 14  ? 47.238 14.816  25.127  1.00 52.37 ? 13  PRO B CB  1 
ATOM   1197 C  CG  . PRO B 1 14  ? 45.935 15.070  25.791  1.00 52.37 ? 13  PRO B CG  1 
ATOM   1198 C  CD  . PRO B 1 14  ? 45.087 15.615  24.650  1.00 52.65 ? 13  PRO B CD  1 
ATOM   1199 N  N   . VAL B 1 15  ? 45.334 12.183  24.085  1.00 48.25 ? 14  VAL B N   1 
ATOM   1200 C  CA  . VAL B 1 15  ? 45.043 10.776  24.322  1.00 45.61 ? 14  VAL B CA  1 
ATOM   1201 C  C   . VAL B 1 15  ? 45.421 9.901   23.132  1.00 43.51 ? 14  VAL B C   1 
ATOM   1202 O  O   . VAL B 1 15  ? 44.997 10.148  22.008  1.00 43.63 ? 14  VAL B O   1 
ATOM   1203 C  CB  . VAL B 1 15  ? 43.549 10.562  24.636  1.00 45.86 ? 14  VAL B CB  1 
ATOM   1204 C  CG1 . VAL B 1 15  ? 43.321 9.130   25.099  1.00 44.04 ? 14  VAL B CG1 1 
ATOM   1205 C  CG2 . VAL B 1 15  ? 43.097 11.551  25.700  1.00 43.59 ? 14  VAL B CG2 1 
ATOM   1206 N  N   . GLN B 1 16  ? 46.228 8.880   23.388  1.00 42.47 ? 15  GLN B N   1 
ATOM   1207 C  CA  . GLN B 1 16  ? 46.640 7.958   22.342  1.00 44.34 ? 15  GLN B CA  1 
ATOM   1208 C  C   . GLN B 1 16  ? 47.077 6.624   22.933  1.00 42.00 ? 15  GLN B C   1 
ATOM   1209 O  O   . GLN B 1 16  ? 47.468 6.549   24.097  1.00 42.65 ? 15  GLN B O   1 
ATOM   1210 C  CB  . GLN B 1 16  ? 47.781 8.555   21.516  1.00 47.39 ? 15  GLN B CB  1 
ATOM   1211 C  CG  . GLN B 1 16  ? 49.025 8.904   22.313  1.00 52.01 ? 15  GLN B CG  1 
ATOM   1212 C  CD  . GLN B 1 16  ? 50.176 9.306   21.418  1.00 54.30 ? 15  GLN B CD  1 
ATOM   1213 O  OE1 . GLN B 1 16  ? 50.106 10.323  20.722  1.00 54.39 ? 15  GLN B OE1 1 
ATOM   1214 N  NE2 . GLN B 1 16  ? 51.244 8.502   21.422  1.00 54.27 ? 15  GLN B NE2 1 
ATOM   1215 N  N   . GLY B 1 17  ? 47.003 5.570   22.125  1.00 40.99 ? 16  GLY B N   1 
ATOM   1216 C  CA  . GLY B 1 17  ? 47.398 4.253   22.593  1.00 37.29 ? 16  GLY B CA  1 
ATOM   1217 C  C   . GLY B 1 17  ? 47.196 3.168   21.554  1.00 36.64 ? 16  GLY B C   1 
ATOM   1218 O  O   . GLY B 1 17  ? 46.591 3.399   20.510  1.00 36.38 ? 16  GLY B O   1 
ATOM   1219 N  N   . ILE B 1 18  ? 47.721 1.981   21.840  1.00 35.06 ? 17  ILE B N   1 
ATOM   1220 C  CA  . ILE B 1 18  ? 47.588 0.834   20.954  1.00 32.99 ? 17  ILE B CA  1 
ATOM   1221 C  C   . ILE B 1 18  ? 46.963 -0.282  21.777  1.00 32.20 ? 17  ILE B C   1 
ATOM   1222 O  O   . ILE B 1 18  ? 47.422 -0.565  22.880  1.00 31.90 ? 17  ILE B O   1 
ATOM   1223 C  CB  . ILE B 1 18  ? 48.961 0.368   20.440  1.00 33.37 ? 17  ILE B CB  1 
ATOM   1224 C  CG1 . ILE B 1 18  ? 49.609 1.480   19.606  1.00 33.70 ? 17  ILE B CG1 1 
ATOM   1225 C  CG2 . ILE B 1 18  ? 48.813 -0.901  19.634  1.00 33.71 ? 17  ILE B CG2 1 
ATOM   1226 C  CD1 . ILE B 1 18  ? 50.972 1.113   19.037  1.00 34.13 ? 17  ILE B CD1 1 
ATOM   1227 N  N   . ILE B 1 19  ? 45.909 -0.905  21.259  1.00 29.87 ? 18  ILE B N   1 
ATOM   1228 C  CA  . ILE B 1 19  ? 45.246 -1.990  21.978  1.00 30.62 ? 18  ILE B CA  1 
ATOM   1229 C  C   . ILE B 1 19  ? 45.202 -3.240  21.116  1.00 30.74 ? 18  ILE B C   1 
ATOM   1230 O  O   . ILE B 1 19  ? 44.749 -3.202  19.969  1.00 30.54 ? 18  ILE B O   1 
ATOM   1231 C  CB  . ILE B 1 19  ? 43.806 -1.611  22.369  1.00 29.39 ? 18  ILE B CB  1 
ATOM   1232 C  CG1 . ILE B 1 19  ? 43.811 -0.347  23.238  1.00 30.63 ? 18  ILE B CG1 1 
ATOM   1233 C  CG2 . ILE B 1 19  ? 43.162 -2.752  23.139  1.00 30.71 ? 18  ILE B CG2 1 
ATOM   1234 C  CD1 . ILE B 1 19  ? 44.515 -0.533  24.578  1.00 32.72 ? 18  ILE B CD1 1 
ATOM   1235 N  N   . ASN B 1 20  ? 45.667 -4.351  21.676  1.00 31.61 ? 19  ASN B N   1 
ATOM   1236 C  CA  . ASN B 1 20  ? 45.694 -5.612  20.953  1.00 32.64 ? 19  ASN B CA  1 
ATOM   1237 C  C   . ASN B 1 20  ? 44.592 -6.558  21.412  1.00 32.89 ? 19  ASN B C   1 
ATOM   1238 O  O   . ASN B 1 20  ? 44.215 -6.567  22.585  1.00 34.44 ? 19  ASN B O   1 
ATOM   1239 C  CB  . ASN B 1 20  ? 47.053 -6.288  21.145  1.00 33.43 ? 19  ASN B CB  1 
ATOM   1240 C  CG  . ASN B 1 20  ? 48.207 -5.360  20.847  1.00 35.39 ? 19  ASN B CG  1 
ATOM   1241 O  OD1 . ASN B 1 20  ? 48.516 -5.093  19.691  1.00 35.51 ? 19  ASN B OD1 1 
ATOM   1242 N  ND2 . ASN B 1 20  ? 48.843 -4.846  21.896  1.00 34.92 ? 19  ASN B ND2 1 
ATOM   1243 N  N   . PHE B 1 21  ? 44.094 -7.357  20.471  1.00 33.06 ? 20  PHE B N   1 
ATOM   1244 C  CA  . PHE B 1 21  ? 43.055 -8.347  20.730  1.00 32.80 ? 20  PHE B CA  1 
ATOM   1245 C  C   . PHE B 1 21  ? 43.539 -9.670  20.130  1.00 34.00 ? 20  PHE B C   1 
ATOM   1246 O  O   . PHE B 1 21  ? 44.063 -9.700  19.016  1.00 30.78 ? 20  PHE B O   1 
ATOM   1247 C  CB  . PHE B 1 21  ? 41.744 -7.979  20.024  1.00 32.48 ? 20  PHE B CB  1 
ATOM   1248 C  CG  . PHE B 1 21  ? 41.138 -6.665  20.457  1.00 31.86 ? 20  PHE B CG  1 
ATOM   1249 C  CD1 . PHE B 1 21  ? 39.982 -6.642  21.231  1.00 32.08 ? 20  PHE B CD1 1 
ATOM   1250 C  CD2 . PHE B 1 21  ? 41.671 -5.459  20.019  1.00 32.25 ? 20  PHE B CD2 1 
ATOM   1251 C  CE1 . PHE B 1 21  ? 39.361 -5.440  21.557  1.00 32.13 ? 20  PHE B CE1 1 
ATOM   1252 C  CE2 . PHE B 1 21  ? 41.062 -4.249  20.336  1.00 30.50 ? 20  PHE B CE2 1 
ATOM   1253 C  CZ  . PHE B 1 21  ? 39.904 -4.239  21.104  1.00 32.17 ? 20  PHE B CZ  1 
ATOM   1254 N  N   . GLU B 1 22  ? 43.365 -10.765 20.859  1.00 34.13 ? 21  GLU B N   1 
ATOM   1255 C  CA  . GLU B 1 22  ? 43.755 -12.062 20.335  1.00 35.57 ? 21  GLU B CA  1 
ATOM   1256 C  C   . GLU B 1 22  ? 42.746 -13.108 20.793  1.00 36.77 ? 21  GLU B C   1 
ATOM   1257 O  O   . GLU B 1 22  ? 42.358 -13.140 21.957  1.00 35.05 ? 21  GLU B O   1 
ATOM   1258 C  CB  . GLU B 1 22  ? 45.164 -12.456 20.789  1.00 37.13 ? 21  GLU B CB  1 
ATOM   1259 C  CG  . GLU B 1 22  ? 45.656 -13.742 20.117  1.00 42.63 ? 21  GLU B CG  1 
ATOM   1260 C  CD  . GLU B 1 22  ? 47.116 -14.064 20.403  1.00 45.17 ? 21  GLU B CD  1 
ATOM   1261 O  OE1 . GLU B 1 22  ? 47.722 -14.801 19.598  1.00 45.40 ? 21  GLU B OE1 1 
ATOM   1262 O  OE2 . GLU B 1 22  ? 47.655 -13.593 21.428  1.00 48.16 ? 21  GLU B OE2 1 
ATOM   1263 N  N   . GLN B 1 23  ? 42.325 -13.951 19.856  1.00 36.82 ? 22  GLN B N   1 
ATOM   1264 C  CA  . GLN B 1 23  ? 41.355 -15.007 20.120  1.00 40.00 ? 22  GLN B CA  1 
ATOM   1265 C  C   . GLN B 1 23  ? 41.804 -16.278 19.390  1.00 42.14 ? 22  GLN B C   1 
ATOM   1266 O  O   . GLN B 1 23  ? 41.604 -16.418 18.186  1.00 40.28 ? 22  GLN B O   1 
ATOM   1267 C  CB  . GLN B 1 23  ? 39.966 -14.580 19.627  1.00 38.52 ? 22  GLN B CB  1 
ATOM   1268 C  CG  . GLN B 1 23  ? 38.914 -15.664 19.749  1.00 34.55 ? 22  GLN B CG  1 
ATOM   1269 C  CD  . GLN B 1 23  ? 37.562 -15.245 19.214  1.00 36.66 ? 22  GLN B CD  1 
ATOM   1270 O  OE1 . GLN B 1 23  ? 37.460 -14.636 18.147  1.00 36.40 ? 22  GLN B OE1 1 
ATOM   1271 N  NE2 . GLN B 1 23  ? 36.507 -15.593 19.943  1.00 35.23 ? 22  GLN B NE2 1 
ATOM   1272 N  N   . LYS B 1 24  ? 42.409 -17.197 20.133  1.00 44.97 ? 23  LYS B N   1 
ATOM   1273 C  CA  . LYS B 1 24  ? 42.910 -18.439 19.555  1.00 49.21 ? 23  LYS B CA  1 
ATOM   1274 C  C   . LYS B 1 24  ? 41.843 -19.396 19.032  1.00 50.04 ? 23  LYS B C   1 
ATOM   1275 O  O   . LYS B 1 24  ? 42.067 -20.075 18.033  1.00 51.85 ? 23  LYS B O   1 
ATOM   1276 C  CB  . LYS B 1 24  ? 43.801 -19.170 20.568  1.00 49.88 ? 23  LYS B CB  1 
ATOM   1277 C  CG  . LYS B 1 24  ? 45.044 -18.393 20.982  1.00 50.67 ? 23  LYS B CG  1 
ATOM   1278 C  CD  . LYS B 1 24  ? 45.881 -19.178 21.980  0.00 51.06 ? 23  LYS B CD  1 
ATOM   1279 C  CE  . LYS B 1 24  ? 47.118 -18.399 22.398  0.00 51.39 ? 23  LYS B CE  1 
ATOM   1280 N  NZ  . LYS B 1 24  ? 47.940 -19.153 23.384  0.00 51.68 ? 23  LYS B NZ  1 
ATOM   1281 N  N   . GLU B 1 25  ? 40.692 -19.458 19.694  1.00 50.73 ? 24  GLU B N   1 
ATOM   1282 C  CA  . GLU B 1 25  ? 39.626 -20.359 19.261  1.00 49.84 ? 24  GLU B CA  1 
ATOM   1283 C  C   . GLU B 1 25  ? 38.395 -19.600 18.761  1.00 49.26 ? 24  GLU B C   1 
ATOM   1284 O  O   . GLU B 1 25  ? 38.067 -18.523 19.260  1.00 48.46 ? 24  GLU B O   1 
ATOM   1285 C  CB  . GLU B 1 25  ? 39.228 -21.288 20.412  1.00 53.27 ? 24  GLU B CB  1 
ATOM   1286 C  CG  . GLU B 1 25  ? 40.401 -21.929 21.161  0.00 57.36 ? 24  GLU B CG  1 
ATOM   1287 C  CD  . GLU B 1 25  ? 41.150 -22.982 20.354  1.00 60.61 ? 24  GLU B CD  1 
ATOM   1288 O  OE1 . GLU B 1 25  ? 42.161 -23.508 20.872  1.00 61.66 ? 24  GLU B OE1 1 
ATOM   1289 O  OE2 . GLU B 1 25  ? 40.734 -23.290 19.213  1.00 63.08 ? 24  GLU B OE2 1 
ATOM   1290 N  N   . SER B 1 26  ? 37.716 -20.177 17.774  1.00 48.78 ? 25  SER B N   1 
ATOM   1291 C  CA  . SER B 1 26  ? 36.527 -19.572 17.177  1.00 47.24 ? 25  SER B CA  1 
ATOM   1292 C  C   . SER B 1 26  ? 35.487 -19.165 18.219  1.00 46.45 ? 25  SER B C   1 
ATOM   1293 O  O   . SER B 1 26  ? 34.838 -18.129 18.087  1.00 45.64 ? 25  SER B O   1 
ATOM   1294 C  CB  . SER B 1 26  ? 35.900 -20.542 16.176  1.00 48.06 ? 25  SER B CB  1 
ATOM   1295 O  OG  . SER B 1 26  ? 34.712 -20.005 15.632  1.00 51.79 ? 25  SER B OG  1 
ATOM   1296 N  N   . ASN B 1 27  ? 35.323 -19.987 19.248  1.00 45.20 ? 26  ASN B N   1 
ATOM   1297 C  CA  . ASN B 1 27  ? 34.376 -19.681 20.307  1.00 43.17 ? 26  ASN B CA  1 
ATOM   1298 C  C   . ASN B 1 27  ? 35.110 -19.603 21.639  1.00 41.71 ? 26  ASN B C   1 
ATOM   1299 O  O   . ASN B 1 27  ? 34.571 -19.963 22.684  1.00 40.74 ? 26  ASN B O   1 
ATOM   1300 C  CB  . ASN B 1 27  ? 33.280 -20.745 20.373  1.00 43.97 ? 26  ASN B CB  1 
ATOM   1301 C  CG  . ASN B 1 27  ? 33.835 -22.138 20.571  1.00 46.14 ? 26  ASN B CG  1 
ATOM   1302 O  OD1 . ASN B 1 27  ? 34.922 -22.312 21.129  1.00 44.14 ? 26  ASN B OD1 1 
ATOM   1303 N  ND2 . ASN B 1 27  ? 33.083 -23.142 20.131  1.00 45.90 ? 26  ASN B ND2 1 
ATOM   1304 N  N   . GLY B 1 28  ? 36.352 -19.138 21.588  1.00 39.69 ? 27  GLY B N   1 
ATOM   1305 C  CA  . GLY B 1 28  ? 37.142 -19.006 22.796  1.00 38.65 ? 27  GLY B CA  1 
ATOM   1306 C  C   . GLY B 1 28  ? 37.146 -17.565 23.265  1.00 39.21 ? 27  GLY B C   1 
ATOM   1307 O  O   . GLY B 1 28  ? 36.620 -16.690 22.572  1.00 40.38 ? 27  GLY B O   1 
ATOM   1308 N  N   . PRO B 1 29  ? 37.728 -17.278 24.435  1.00 38.65 ? 28  PRO B N   1 
ATOM   1309 C  CA  . PRO B 1 29  ? 37.771 -15.910 24.956  1.00 38.25 ? 28  PRO B CA  1 
ATOM   1310 C  C   . PRO B 1 29  ? 38.664 -14.975 24.149  1.00 39.14 ? 28  PRO B C   1 
ATOM   1311 O  O   . PRO B 1 29  ? 39.455 -15.415 23.316  1.00 42.93 ? 28  PRO B O   1 
ATOM   1312 C  CB  . PRO B 1 29  ? 38.284 -16.103 26.375  1.00 37.79 ? 28  PRO B CB  1 
ATOM   1313 C  CG  . PRO B 1 29  ? 39.172 -17.299 26.251  1.00 39.38 ? 28  PRO B CG  1 
ATOM   1314 C  CD  . PRO B 1 29  ? 38.355 -18.219 25.381  1.00 39.06 ? 28  PRO B CD  1 
ATOM   1315 N  N   . VAL B 1 30  ? 38.537 -13.681 24.405  1.00 38.73 ? 29  VAL B N   1 
ATOM   1316 C  CA  . VAL B 1 30  ? 39.346 -12.688 23.715  1.00 37.48 ? 29  VAL B CA  1 
ATOM   1317 C  C   . VAL B 1 30  ? 40.228 -11.940 24.702  1.00 35.72 ? 29  VAL B C   1 
ATOM   1318 O  O   . VAL B 1 30  ? 39.736 -11.340 25.647  1.00 35.82 ? 29  VAL B O   1 
ATOM   1319 C  CB  . VAL B 1 30  ? 38.459 -11.671 22.974  1.00 37.90 ? 29  VAL B CB  1 
ATOM   1320 C  CG1 . VAL B 1 30  ? 39.306 -10.517 22.460  1.00 38.63 ? 29  VAL B CG1 1 
ATOM   1321 C  CG2 . VAL B 1 30  ? 37.756 -12.353 21.817  1.00 38.27 ? 29  VAL B CG2 1 
ATOM   1322 N  N   . LYS B 1 31  ? 41.537 -11.994 24.489  1.00 36.45 ? 30  LYS B N   1 
ATOM   1323 C  CA  . LYS B 1 31  ? 42.467 -11.289 25.360  1.00 37.34 ? 30  LYS B CA  1 
ATOM   1324 C  C   . LYS B 1 31  ? 42.699 -9.889  24.810  1.00 37.86 ? 30  LYS B C   1 
ATOM   1325 O  O   . LYS B 1 31  ? 42.923 -9.726  23.612  1.00 38.34 ? 30  LYS B O   1 
ATOM   1326 C  CB  . LYS B 1 31  ? 43.796 -12.040 25.460  1.00 40.59 ? 30  LYS B CB  1 
ATOM   1327 C  CG  . LYS B 1 31  ? 43.750 -13.389 26.179  0.00 43.41 ? 30  LYS B CG  1 
ATOM   1328 C  CD  . LYS B 1 31  ? 45.141 -14.010 26.192  0.00 47.07 ? 30  LYS B CD  1 
ATOM   1329 C  CE  . LYS B 1 31  ? 45.133 -15.294 26.995  0.00 49.36 ? 30  LYS B CE  1 
ATOM   1330 N  NZ  . LYS B 1 31  ? 46.403 -16.073 27.058  1.00 57.66 ? 30  LYS B NZ  1 
ATOM   1331 N  N   . VAL B 1 32  ? 42.602 -8.893  25.686  1.00 36.93 ? 31  VAL B N   1 
ATOM   1332 C  CA  . VAL B 1 32  ? 42.772 -7.501  25.297  1.00 38.13 ? 31  VAL B CA  1 
ATOM   1333 C  C   . VAL B 1 32  ? 43.868 -6.870  26.149  1.00 39.89 ? 31  VAL B C   1 
ATOM   1334 O  O   . VAL B 1 32  ? 43.782 -6.876  27.381  1.00 41.04 ? 31  VAL B O   1 
ATOM   1335 C  CB  . VAL B 1 32  ? 41.462 -6.710  25.531  1.00 37.01 ? 31  VAL B CB  1 
ATOM   1336 C  CG1 . VAL B 1 32  ? 41.589 -5.287  24.998  1.00 36.54 ? 31  VAL B CG1 1 
ATOM   1337 C  CG2 . VAL B 1 32  ? 40.309 -7.425  24.882  1.00 36.89 ? 31  VAL B CG2 1 
ATOM   1338 N  N   . TRP B 1 33  ? 44.897 -6.326  25.502  1.00 39.91 ? 32  TRP B N   1 
ATOM   1339 C  CA  . TRP B 1 33  ? 45.987 -5.689  26.231  1.00 39.19 ? 32  TRP B CA  1 
ATOM   1340 C  C   . TRP B 1 33  ? 46.637 -4.540  25.459  1.00 39.67 ? 32  TRP B C   1 
ATOM   1341 O  O   . TRP B 1 33  ? 46.612 -4.497  24.227  1.00 36.85 ? 32  TRP B O   1 
ATOM   1342 C  CB  . TRP B 1 33  ? 47.038 -6.735  26.620  1.00 40.42 ? 32  TRP B CB  1 
ATOM   1343 C  CG  . TRP B 1 33  ? 47.925 -7.197  25.506  1.00 39.42 ? 32  TRP B CG  1 
ATOM   1344 C  CD1 . TRP B 1 33  ? 49.195 -6.772  25.243  1.00 39.74 ? 32  TRP B CD1 1 
ATOM   1345 C  CD2 . TRP B 1 33  ? 47.627 -8.198  24.526  1.00 40.59 ? 32  TRP B CD2 1 
ATOM   1346 N  NE1 . TRP B 1 33  ? 49.708 -7.448  24.164  1.00 40.80 ? 32  TRP B NE1 1 
ATOM   1347 C  CE2 . TRP B 1 33  ? 48.765 -8.330  23.704  1.00 40.79 ? 32  TRP B CE2 1 
ATOM   1348 C  CE3 . TRP B 1 33  ? 46.508 -8.994  24.260  1.00 40.58 ? 32  TRP B CE3 1 
ATOM   1349 C  CZ2 . TRP B 1 33  ? 48.817 -9.231  22.636  1.00 42.77 ? 32  TRP B CZ2 1 
ATOM   1350 C  CZ3 . TRP B 1 33  ? 46.560 -9.887  23.197  1.00 39.37 ? 32  TRP B CZ3 1 
ATOM   1351 C  CH2 . TRP B 1 33  ? 47.704 -9.998  22.400  1.00 40.74 ? 32  TRP B CH2 1 
ATOM   1352 N  N   . GLY B 1 34  ? 47.208 -3.601  26.204  1.00 39.63 ? 33  GLY B N   1 
ATOM   1353 C  CA  . GLY B 1 34  ? 47.845 -2.456  25.590  1.00 38.92 ? 33  GLY B CA  1 
ATOM   1354 C  C   . GLY B 1 34  ? 47.925 -1.306  26.565  1.00 40.96 ? 33  GLY B C   1 
ATOM   1355 O  O   . GLY B 1 34  ? 47.671 -1.475  27.757  1.00 42.45 ? 33  GLY B O   1 
ATOM   1356 N  N   . SER B 1 35  ? 48.257 -0.125  26.067  1.00 42.23 ? 34  SER B N   1 
ATOM   1357 C  CA  . SER B 1 35  ? 48.383 1.025   26.941  1.00 43.63 ? 34  SER B CA  1 
ATOM   1358 C  C   . SER B 1 35  ? 47.806 2.268   26.291  1.00 42.90 ? 34  SER B C   1 
ATOM   1359 O  O   . SER B 1 35  ? 47.724 2.358   25.070  1.00 43.47 ? 34  SER B O   1 
ATOM   1360 C  CB  . SER B 1 35  ? 49.867 1.242   27.271  1.00 44.81 ? 34  SER B CB  1 
ATOM   1361 O  OG  . SER B 1 35  ? 50.039 2.167   28.330  1.00 48.35 ? 34  SER B OG  1 
ATOM   1362 N  N   . ILE B 1 36  ? 47.408 3.228   27.114  1.00 43.17 ? 35  ILE B N   1 
ATOM   1363 C  CA  . ILE B 1 36  ? 46.856 4.480   26.621  1.00 44.39 ? 35  ILE B CA  1 
ATOM   1364 C  C   . ILE B 1 36  ? 47.460 5.589   27.468  1.00 45.27 ? 35  ILE B C   1 
ATOM   1365 O  O   . ILE B 1 36  ? 47.558 5.458   28.682  1.00 47.17 ? 35  ILE B O   1 
ATOM   1366 C  CB  . ILE B 1 36  ? 45.312 4.527   26.766  1.00 43.58 ? 35  ILE B CB  1 
ATOM   1367 C  CG1 . ILE B 1 36  ? 44.681 3.260   26.182  1.00 43.32 ? 35  ILE B CG1 1 
ATOM   1368 C  CG2 . ILE B 1 36  ? 44.767 5.753   26.044  1.00 44.49 ? 35  ILE B CG2 1 
ATOM   1369 C  CD1 . ILE B 1 36  ? 43.164 3.227   26.286  1.00 43.17 ? 35  ILE B CD1 1 
ATOM   1370 N  N   . LYS B 1 37  ? 47.864 6.678   26.829  1.00 47.18 ? 36  LYS B N   1 
ATOM   1371 C  CA  . LYS B 1 37  ? 48.458 7.791   27.552  1.00 49.62 ? 36  LYS B CA  1 
ATOM   1372 C  C   . LYS B 1 37  ? 47.694 9.072   27.289  1.00 50.52 ? 36  LYS B C   1 
ATOM   1373 O  O   . LYS B 1 37  ? 46.777 9.094   26.470  1.00 50.58 ? 36  LYS B O   1 
ATOM   1374 C  CB  . LYS B 1 37  ? 49.920 7.961   27.127  1.00 51.28 ? 36  LYS B CB  1 
ATOM   1375 C  CG  . LYS B 1 37  ? 50.108 8.438   25.703  1.00 51.54 ? 36  LYS B CG  1 
ATOM   1376 C  CD  . LYS B 1 37  ? 51.588 8.416   25.389  1.00 52.63 ? 36  LYS B CD  1 
ATOM   1377 C  CE  . LYS B 1 37  ? 51.817 9.033   24.031  0.00 52.81 ? 36  LYS B CE  1 
ATOM   1378 N  NZ  . LYS B 1 37  ? 53.178 8.893   23.448  0.00 53.16 ? 36  LYS B NZ  1 
ATOM   1379 N  N   . GLY B 1 38  ? 48.083 10.137  27.987  1.00 51.84 ? 37  GLY B N   1 
ATOM   1380 C  CA  . GLY B 1 38  ? 47.442 11.426  27.809  1.00 50.64 ? 37  GLY B CA  1 
ATOM   1381 C  C   . GLY B 1 38  ? 46.116 11.548  28.532  1.00 51.82 ? 37  GLY B C   1 
ATOM   1382 O  O   . GLY B 1 38  ? 45.401 12.542  28.376  1.00 50.56 ? 37  GLY B O   1 
ATOM   1383 N  N   . LEU B 1 39  ? 45.785 10.539  29.329  1.00 51.27 ? 38  LEU B N   1 
ATOM   1384 C  CA  . LEU B 1 39  ? 44.530 10.524  30.076  1.00 53.22 ? 38  LEU B CA  1 
ATOM   1385 C  C   . LEU B 1 39  ? 44.667 11.164  31.451  1.00 55.75 ? 38  LEU B C   1 
ATOM   1386 O  O   . LEU B 1 39  ? 45.755 11.184  32.032  1.00 55.12 ? 38  LEU B O   1 
ATOM   1387 C  CB  . LEU B 1 39  ? 44.058 9.087   30.270  1.00 51.51 ? 38  LEU B CB  1 
ATOM   1388 C  CG  . LEU B 1 39  ? 43.663 8.258   29.050  1.00 49.97 ? 38  LEU B CG  1 
ATOM   1389 C  CD1 . LEU B 1 39  ? 43.676 6.786   29.434  1.00 45.90 ? 38  LEU B CD1 1 
ATOM   1390 C  CD2 . LEU B 1 39  ? 42.290 8.699   28.551  1.00 47.64 ? 38  LEU B CD2 1 
ATOM   1391 N  N   . THR B 1 40  ? 43.559 11.684  31.972  1.00 56.88 ? 39  THR B N   1 
ATOM   1392 C  CA  . THR B 1 40  ? 43.573 12.278  33.302  1.00 56.92 ? 39  THR B CA  1 
ATOM   1393 C  C   . THR B 1 40  ? 43.538 11.099  34.257  1.00 56.36 ? 39  THR B C   1 
ATOM   1394 O  O   . THR B 1 40  ? 42.941 10.068  33.953  1.00 56.25 ? 39  THR B O   1 
ATOM   1395 C  CB  . THR B 1 40  ? 42.334 13.154  33.566  1.00 57.06 ? 39  THR B CB  1 
ATOM   1396 O  OG1 . THR B 1 40  ? 41.151 12.356  33.443  1.00 57.65 ? 39  THR B OG1 1 
ATOM   1397 C  CG2 . THR B 1 40  ? 42.272 14.307  32.575  1.00 56.85 ? 39  THR B CG2 1 
ATOM   1398 N  N   . GLU B 1 41  ? 44.196 11.244  35.400  1.00 57.62 ? 40  GLU B N   1 
ATOM   1399 C  CA  . GLU B 1 41  ? 44.236 10.184  36.402  1.00 57.34 ? 40  GLU B CA  1 
ATOM   1400 C  C   . GLU B 1 41  ? 42.797 9.744   36.664  1.00 56.79 ? 40  GLU B C   1 
ATOM   1401 O  O   . GLU B 1 41  ? 41.883 10.571  36.648  1.00 57.60 ? 40  GLU B O   1 
ATOM   1402 C  CB  . GLU B 1 41  ? 44.864 10.727  37.687  1.00 57.98 ? 40  GLU B CB  1 
ATOM   1403 C  CG  . GLU B 1 41  ? 45.556 9.702   38.560  0.00 59.55 ? 40  GLU B CG  1 
ATOM   1404 C  CD  . GLU B 1 41  ? 46.144 10.329  39.809  1.00 60.80 ? 40  GLU B CD  1 
ATOM   1405 O  OE1 . GLU B 1 41  ? 46.666 11.463  39.718  1.00 60.76 ? 40  GLU B OE1 1 
ATOM   1406 O  OE2 . GLU B 1 41  ? 46.096 9.686   40.880  1.00 62.36 ? 40  GLU B OE2 1 
ATOM   1407 N  N   . GLY B 1 42  ? 42.586 8.451   36.889  1.00 55.47 ? 41  GLY B N   1 
ATOM   1408 C  CA  . GLY B 1 42  ? 41.238 7.980   37.151  1.00 55.36 ? 41  GLY B CA  1 
ATOM   1409 C  C   . GLY B 1 42  ? 40.641 7.069   36.089  1.00 55.07 ? 41  GLY B C   1 
ATOM   1410 O  O   . GLY B 1 42  ? 41.298 6.730   35.103  1.00 55.75 ? 41  GLY B O   1 
ATOM   1411 N  N   . LEU B 1 43  ? 39.382 6.683   36.296  1.00 53.06 ? 42  LEU B N   1 
ATOM   1412 C  CA  . LEU B 1 43  ? 38.663 5.790   35.387  1.00 51.47 ? 42  LEU B CA  1 
ATOM   1413 C  C   . LEU B 1 43  ? 38.168 6.430   34.093  1.00 49.69 ? 42  LEU B C   1 
ATOM   1414 O  O   . LEU B 1 43  ? 37.860 7.621   34.048  1.00 50.10 ? 42  LEU B O   1 
ATOM   1415 C  CB  . LEU B 1 43  ? 37.468 5.167   36.112  1.00 52.69 ? 42  LEU B CB  1 
ATOM   1416 C  CG  . LEU B 1 43  ? 37.749 4.142   37.212  1.00 52.66 ? 42  LEU B CG  1 
ATOM   1417 C  CD1 . LEU B 1 43  ? 36.447 3.733   37.867  1.00 53.68 ? 42  LEU B CD1 1 
ATOM   1418 C  CD2 . LEU B 1 43  ? 38.430 2.930   36.621  1.00 53.93 ? 42  LEU B CD2 1 
ATOM   1419 N  N   . HIS B 1 44  ? 38.075 5.614   33.045  1.00 48.08 ? 43  HIS B N   1 
ATOM   1420 C  CA  . HIS B 1 44  ? 37.606 6.067   31.735  1.00 43.97 ? 43  HIS B CA  1 
ATOM   1421 C  C   . HIS B 1 44  ? 36.825 4.960   31.024  1.00 41.69 ? 43  HIS B C   1 
ATOM   1422 O  O   . HIS B 1 44  ? 37.291 3.823   30.945  1.00 38.39 ? 43  HIS B O   1 
ATOM   1423 C  CB  . HIS B 1 44  ? 38.795 6.466   30.863  1.00 46.38 ? 43  HIS B CB  1 
ATOM   1424 C  CG  . HIS B 1 44  ? 39.536 7.667   31.357  1.00 46.66 ? 43  HIS B CG  1 
ATOM   1425 N  ND1 . HIS B 1 44  ? 39.089 8.954   31.153  1.00 48.93 ? 43  HIS B ND1 1 
ATOM   1426 C  CD2 . HIS B 1 44  ? 40.708 7.778   32.025  1.00 47.75 ? 43  HIS B CD2 1 
ATOM   1427 C  CE1 . HIS B 1 44  ? 39.956 9.807   31.667  1.00 47.60 ? 43  HIS B CE1 1 
ATOM   1428 N  NE2 . HIS B 1 44  ? 40.949 9.119   32.202  1.00 49.26 ? 43  HIS B NE2 1 
ATOM   1429 N  N   . GLY B 1 45  ? 35.640 5.292   30.515  1.00 38.81 ? 44  GLY B N   1 
ATOM   1430 C  CA  . GLY B 1 45  ? 34.840 4.305   29.798  1.00 36.92 ? 44  GLY B CA  1 
ATOM   1431 C  C   . GLY B 1 45  ? 35.650 3.674   28.675  1.00 34.29 ? 44  GLY B C   1 
ATOM   1432 O  O   . GLY B 1 45  ? 36.526 4.323   28.102  1.00 34.60 ? 44  GLY B O   1 
ATOM   1433 N  N   . PHE B 1 46  ? 35.352 2.421   28.345  1.00 34.09 ? 45  PHE B N   1 
ATOM   1434 C  CA  . PHE B 1 46  ? 36.103 1.693   27.316  1.00 35.39 ? 45  PHE B CA  1 
ATOM   1435 C  C   . PHE B 1 46  ? 35.180 0.704   26.586  1.00 33.27 ? 45  PHE B C   1 
ATOM   1436 O  O   . PHE B 1 46  ? 34.803 -0.315  27.153  1.00 34.22 ? 45  PHE B O   1 
ATOM   1437 C  CB  . PHE B 1 46  ? 37.244 0.940   28.015  1.00 35.57 ? 45  PHE B CB  1 
ATOM   1438 C  CG  . PHE B 1 46  ? 38.296 0.389   27.093  1.00 34.28 ? 45  PHE B CG  1 
ATOM   1439 C  CD1 . PHE B 1 46  ? 39.000 1.221   26.226  1.00 33.61 ? 45  PHE B CD1 1 
ATOM   1440 C  CD2 . PHE B 1 46  ? 38.634 -0.962  27.149  1.00 33.52 ? 45  PHE B CD2 1 
ATOM   1441 C  CE1 . PHE B 1 46  ? 40.025 0.713   25.435  1.00 32.71 ? 45  PHE B CE1 1 
ATOM   1442 C  CE2 . PHE B 1 46  ? 39.655 -1.479  26.363  1.00 31.09 ? 45  PHE B CE2 1 
ATOM   1443 C  CZ  . PHE B 1 46  ? 40.353 -0.644  25.504  1.00 30.13 ? 45  PHE B CZ  1 
ATOM   1444 N  N   . HIS B 1 47  ? 34.808 1.006   25.342  1.00 30.29 ? 46  HIS B N   1 
ATOM   1445 C  CA  . HIS B 1 47  ? 33.929 0.108   24.599  1.00 29.15 ? 46  HIS B CA  1 
ATOM   1446 C  C   . HIS B 1 47  ? 34.134 0.061   23.099  1.00 29.14 ? 46  HIS B C   1 
ATOM   1447 O  O   . HIS B 1 47  ? 34.748 0.947   22.498  1.00 26.92 ? 46  HIS B O   1 
ATOM   1448 C  CB  . HIS B 1 47  ? 32.443 0.442   24.812  1.00 29.63 ? 46  HIS B CB  1 
ATOM   1449 C  CG  . HIS B 1 47  ? 32.180 1.411   25.918  1.00 32.58 ? 46  HIS B CG  1 
ATOM   1450 N  ND1 . HIS B 1 47  ? 32.236 2.775   25.741  1.00 33.86 ? 46  HIS B ND1 1 
ATOM   1451 C  CD2 . HIS B 1 47  ? 31.868 1.211   27.219  1.00 33.66 ? 46  HIS B CD2 1 
ATOM   1452 C  CE1 . HIS B 1 47  ? 31.966 3.375   26.887  1.00 36.30 ? 46  HIS B CE1 1 
ATOM   1453 N  NE2 . HIS B 1 47  ? 31.740 2.448   27.799  1.00 34.95 ? 46  HIS B NE2 1 
ATOM   1454 N  N   . VAL B 1 48  ? 33.583 -0.991  22.506  1.00 26.51 ? 47  VAL B N   1 
ATOM   1455 C  CA  . VAL B 1 48  ? 33.610 -1.159  21.067  1.00 27.78 ? 47  VAL B CA  1 
ATOM   1456 C  C   . VAL B 1 48  ? 32.294 -0.540  20.589  1.00 28.79 ? 47  VAL B C   1 
ATOM   1457 O  O   . VAL B 1 48  ? 31.209 -0.903  21.068  1.00 29.27 ? 47  VAL B O   1 
ATOM   1458 C  CB  . VAL B 1 48  ? 33.630 -2.645  20.669  1.00 27.51 ? 47  VAL B CB  1 
ATOM   1459 C  CG1 . VAL B 1 48  ? 33.610 -2.774  19.146  1.00 27.74 ? 47  VAL B CG1 1 
ATOM   1460 C  CG2 . VAL B 1 48  ? 34.868 -3.313  21.240  1.00 27.85 ? 47  VAL B CG2 1 
ATOM   1461 N  N   . HIS B 1 49  ? 32.394 0.416   19.675  1.00 30.34 ? 48  HIS B N   1 
ATOM   1462 C  CA  . HIS B 1 49  ? 31.219 1.066   19.131  1.00 31.36 ? 48  HIS B CA  1 
ATOM   1463 C  C   . HIS B 1 49  ? 30.860 0.419   17.805  1.00 33.09 ? 48  HIS B C   1 
ATOM   1464 O  O   . HIS B 1 49  ? 31.714 -0.173  17.137  1.00 33.00 ? 48  HIS B O   1 
ATOM   1465 C  CB  . HIS B 1 49  ? 31.462 2.564   18.975  1.00 30.49 ? 48  HIS B CB  1 
ATOM   1466 C  CG  . HIS B 1 49  ? 31.362 3.316   20.267  1.00 30.15 ? 48  HIS B CG  1 
ATOM   1467 N  ND1 . HIS B 1 49  ? 30.559 4.423   20.422  1.00 30.29 ? 48  HIS B ND1 1 
ATOM   1468 C  CD2 . HIS B 1 49  ? 31.965 3.119   21.466  1.00 29.97 ? 48  HIS B CD2 1 
ATOM   1469 C  CE1 . HIS B 1 49  ? 30.668 4.878   21.658  1.00 31.71 ? 48  HIS B CE1 1 
ATOM   1470 N  NE2 . HIS B 1 49  ? 31.516 4.104   22.313  1.00 29.08 ? 48  HIS B NE2 1 
ATOM   1471 N  N   . GLU B 1 50  ? 29.593 0.540   17.429  1.00 33.50 ? 49  GLU B N   1 
ATOM   1472 C  CA  . GLU B 1 50  ? 29.088 -0.093  16.226  1.00 33.14 ? 49  GLU B CA  1 
ATOM   1473 C  C   . GLU B 1 50  ? 29.834 0.130   14.927  1.00 34.82 ? 49  GLU B C   1 
ATOM   1474 O  O   . GLU B 1 50  ? 30.211 -0.833  14.258  1.00 32.36 ? 49  GLU B O   1 
ATOM   1475 C  CB  . GLU B 1 50  ? 27.621 0.280   16.011  1.00 36.19 ? 49  GLU B CB  1 
ATOM   1476 C  CG  . GLU B 1 50  ? 26.974 -0.504  14.874  1.00 38.97 ? 49  GLU B CG  1 
ATOM   1477 C  CD  . GLU B 1 50  ? 25.473 -0.308  14.786  1.00 43.06 ? 49  GLU B CD  1 
ATOM   1478 O  OE1 . GLU B 1 50  ? 24.826 -1.034  13.998  1.00 43.46 ? 49  GLU B OE1 1 
ATOM   1479 O  OE2 . GLU B 1 50  ? 24.939 0.568   15.501  1.00 44.31 ? 49  GLU B OE2 1 
ATOM   1480 N  N   . PHE B 1 51  ? 30.057 1.391   14.573  1.00 34.23 ? 50  PHE B N   1 
ATOM   1481 C  CA  . PHE B 1 51  ? 30.687 1.702   13.302  1.00 36.39 ? 50  PHE B CA  1 
ATOM   1482 C  C   . PHE B 1 51  ? 32.166 2.013   13.259  1.00 36.08 ? 50  PHE B C   1 
ATOM   1483 O  O   . PHE B 1 51  ? 32.678 2.775   14.075  1.00 36.08 ? 50  PHE B O   1 
ATOM   1484 C  CB  . PHE B 1 51  ? 29.940 2.856   12.650  1.00 37.38 ? 50  PHE B CB  1 
ATOM   1485 C  CG  . PHE B 1 51  ? 28.470 2.638   12.567  1.00 39.46 ? 50  PHE B CG  1 
ATOM   1486 C  CD1 . PHE B 1 51  ? 27.952 1.589   11.819  1.00 40.24 ? 50  PHE B CD1 1 
ATOM   1487 C  CD2 . PHE B 1 51  ? 27.598 3.469   13.256  1.00 39.66 ? 50  PHE B CD2 1 
ATOM   1488 C  CE1 . PHE B 1 51  ? 26.579 1.371   11.761  1.00 42.17 ? 50  PHE B CE1 1 
ATOM   1489 C  CE2 . PHE B 1 51  ? 26.226 3.260   13.204  1.00 41.12 ? 50  PHE B CE2 1 
ATOM   1490 C  CZ  . PHE B 1 51  ? 25.717 2.208   12.455  1.00 41.06 ? 50  PHE B CZ  1 
ATOM   1491 N  N   . GLY B 1 52  ? 32.839 1.417   12.278  1.00 36.27 ? 51  GLY B N   1 
ATOM   1492 C  CA  . GLY B 1 52  ? 34.253 1.663   12.080  1.00 35.89 ? 51  GLY B CA  1 
ATOM   1493 C  C   . GLY B 1 52  ? 34.332 2.805   11.087  1.00 36.37 ? 51  GLY B C   1 
ATOM   1494 O  O   . GLY B 1 52  ? 35.007 2.715   10.064  1.00 36.97 ? 51  GLY B O   1 
ATOM   1495 N  N   . ASP B 1 53  ? 33.626 3.885   11.404  1.00 38.47 ? 52  ASP B N   1 
ATOM   1496 C  CA  . ASP B 1 53  ? 33.551 5.064   10.551  1.00 39.37 ? 52  ASP B CA  1 
ATOM   1497 C  C   . ASP B 1 53  ? 34.207 6.257   11.230  1.00 40.04 ? 52  ASP B C   1 
ATOM   1498 O  O   . ASP B 1 53  ? 33.701 6.777   12.224  1.00 39.54 ? 52  ASP B O   1 
ATOM   1499 C  CB  . ASP B 1 53  ? 32.077 5.354   10.246  1.00 39.73 ? 52  ASP B CB  1 
ATOM   1500 C  CG  . ASP B 1 53  ? 31.881 6.550   9.340   1.00 39.48 ? 52  ASP B CG  1 
ATOM   1501 O  OD1 . ASP B 1 53  ? 30.812 6.625   8.704   1.00 41.72 ? 52  ASP B OD1 1 
ATOM   1502 O  OD2 . ASP B 1 53  ? 32.774 7.415   9.269   1.00 41.75 ? 52  ASP B OD2 1 
ATOM   1503 N  N   . ASN B 1 54  ? 35.337 6.692   10.689  1.00 41.24 ? 53  ASN B N   1 
ATOM   1504 C  CA  . ASN B 1 54  ? 36.057 7.814   11.272  1.00 43.28 ? 53  ASN B CA  1 
ATOM   1505 C  C   . ASN B 1 54  ? 35.934 9.082   10.434  1.00 43.53 ? 53  ASN B C   1 
ATOM   1506 O  O   . ASN B 1 54  ? 36.779 9.971   10.522  1.00 45.09 ? 53  ASN B O   1 
ATOM   1507 C  CB  . ASN B 1 54  ? 37.534 7.453   11.435  1.00 44.41 ? 53  ASN B CB  1 
ATOM   1508 C  CG  . ASN B 1 54  ? 38.262 8.398   12.364  1.00 46.72 ? 53  ASN B CG  1 
ATOM   1509 O  OD1 . ASN B 1 54  ? 39.480 8.546   12.290  1.00 50.78 ? 53  ASN B OD1 1 
ATOM   1510 N  ND2 . ASN B 1 54  ? 37.519 9.031   13.259  1.00 49.18 ? 53  ASN B ND2 1 
ATOM   1511 N  N   . THR B 1 55  ? 34.881 9.170   9.630   1.00 43.86 ? 54  THR B N   1 
ATOM   1512 C  CA  . THR B 1 55  ? 34.678 10.339  8.778   1.00 45.60 ? 54  THR B CA  1 
ATOM   1513 C  C   . THR B 1 55  ? 34.541 11.631  9.583   1.00 47.89 ? 54  THR B C   1 
ATOM   1514 O  O   . THR B 1 55  ? 34.868 12.713  9.092   1.00 48.98 ? 54  THR B O   1 
ATOM   1515 C  CB  . THR B 1 55  ? 33.436 10.167  7.887   1.00 44.41 ? 54  THR B CB  1 
ATOM   1516 O  OG1 . THR B 1 55  ? 32.320 9.774   8.694   1.00 45.55 ? 54  THR B OG1 1 
ATOM   1517 C  CG2 . THR B 1 55  ? 33.693 9.112   6.812   1.00 44.11 ? 54  THR B CG2 1 
ATOM   1518 N  N   . ALA B 1 56  ? 34.062 11.519  10.819  1.00 48.87 ? 55  ALA B N   1 
ATOM   1519 C  CA  . ALA B 1 56  ? 33.906 12.684  11.683  1.00 50.47 ? 55  ALA B CA  1 
ATOM   1520 C  C   . ALA B 1 56  ? 34.448 12.386  13.078  1.00 51.25 ? 55  ALA B C   1 
ATOM   1521 O  O   . ALA B 1 56  ? 33.682 12.250  14.030  1.00 54.54 ? 55  ALA B O   1 
ATOM   1522 C  CB  . ALA B 1 56  ? 32.442 13.081  11.767  1.00 48.57 ? 55  ALA B CB  1 
ATOM   1523 N  N   . GLY B 1 57  ? 35.766 12.283  13.203  1.00 49.88 ? 56  GLY B N   1 
ATOM   1524 C  CA  . GLY B 1 57  ? 36.345 11.992  14.502  1.00 49.29 ? 56  GLY B CA  1 
ATOM   1525 C  C   . GLY B 1 57  ? 35.731 10.736  15.098  1.00 48.37 ? 56  GLY B C   1 
ATOM   1526 O  O   . GLY B 1 57  ? 35.343 9.831   14.363  1.00 49.72 ? 56  GLY B O   1 
ATOM   1527 N  N   . CYS B 1 58  ? 35.624 10.680  16.422  1.00 46.48 ? 57  CYS B N   1 
ATOM   1528 C  CA  . CYS B 1 58  ? 35.062 9.509   17.089  1.00 44.12 ? 57  CYS B CA  1 
ATOM   1529 C  C   . CYS B 1 58  ? 33.541 9.517   17.154  1.00 44.04 ? 57  CYS B C   1 
ATOM   1530 O  O   . CYS B 1 58  ? 32.923 8.491   17.419  1.00 43.98 ? 57  CYS B O   1 
ATOM   1531 C  CB  . CYS B 1 58  ? 35.626 9.384   18.508  1.00 43.87 ? 57  CYS B CB  1 
ATOM   1532 S  SG  . CYS B 1 58  ? 37.439 9.250   18.550  1.00 47.92 ? 57  CYS B SG  1 
ATOM   1533 N  N   . THR B 1 59  ? 32.925 10.665  16.906  1.00 42.33 ? 58  THR B N   1 
ATOM   1534 C  CA  . THR B 1 59  ? 31.477 10.726  16.980  1.00 42.98 ? 58  THR B CA  1 
ATOM   1535 C  C   . THR B 1 59  ? 30.795 9.868   15.914  1.00 41.84 ? 58  THR B C   1 
ATOM   1536 O  O   . THR B 1 59  ? 29.718 9.326   16.153  1.00 41.74 ? 58  THR B O   1 
ATOM   1537 C  CB  . THR B 1 59  ? 30.978 12.191  16.908  1.00 44.92 ? 58  THR B CB  1 
ATOM   1538 O  OG1 . THR B 1 59  ? 29.564 12.208  16.683  1.00 48.43 ? 58  THR B OG1 1 
ATOM   1539 C  CG2 . THR B 1 59  ? 31.678 12.942  15.810  1.00 49.07 ? 58  THR B CG2 1 
ATOM   1540 N  N   . SER B 1 60  ? 31.431 9.707   14.756  1.00 40.24 ? 59  SER B N   1 
ATOM   1541 C  CA  . SER B 1 60  ? 30.840 8.896   13.691  1.00 40.35 ? 59  SER B CA  1 
ATOM   1542 C  C   . SER B 1 60  ? 30.921 7.383   13.943  1.00 38.73 ? 59  SER B C   1 
ATOM   1543 O  O   . SER B 1 60  ? 30.447 6.589   13.138  1.00 39.09 ? 59  SER B O   1 
ATOM   1544 C  CB  . SER B 1 60  ? 31.472 9.239   12.332  1.00 40.97 ? 59  SER B CB  1 
ATOM   1545 O  OG  . SER B 1 60  ? 32.887 9.203   12.380  1.00 44.96 ? 59  SER B OG  1 
ATOM   1546 N  N   . ALA B 1 61  ? 31.507 6.983   15.066  1.00 39.06 ? 60  ALA B N   1 
ATOM   1547 C  CA  . ALA B 1 61  ? 31.604 5.561   15.401  1.00 37.48 ? 60  ALA B CA  1 
ATOM   1548 C  C   . ALA B 1 61  ? 30.240 5.034   15.868  1.00 36.39 ? 60  ALA B C   1 
ATOM   1549 O  O   . ALA B 1 61  ? 30.055 3.832   16.052  1.00 33.94 ? 60  ALA B O   1 
ATOM   1550 C  CB  . ALA B 1 61  ? 32.650 5.354   16.503  1.00 39.59 ? 60  ALA B CB  1 
ATOM   1551 N  N   . GLY B 1 62  ? 29.291 5.945   16.073  1.00 35.19 ? 61  GLY B N   1 
ATOM   1552 C  CA  . GLY B 1 62  ? 27.963 5.548   16.508  1.00 33.02 ? 61  GLY B CA  1 
ATOM   1553 C  C   . GLY B 1 62  ? 27.854 5.077   17.949  1.00 32.92 ? 61  GLY B C   1 
ATOM   1554 O  O   . GLY B 1 62  ? 28.737 5.325   18.761  1.00 32.88 ? 61  GLY B O   1 
ATOM   1555 N  N   . PRO B 1 63  ? 26.762 4.389   18.298  1.00 33.43 ? 62  PRO B N   1 
ATOM   1556 C  CA  . PRO B 1 63  ? 26.545 3.888   19.657  1.00 33.31 ? 62  PRO B CA  1 
ATOM   1557 C  C   . PRO B 1 63  ? 27.374 2.659   19.975  1.00 33.94 ? 62  PRO B C   1 
ATOM   1558 O  O   . PRO B 1 63  ? 28.129 2.175   19.136  1.00 33.99 ? 62  PRO B O   1 
ATOM   1559 C  CB  . PRO B 1 63  ? 25.053 3.586   19.667  1.00 34.49 ? 62  PRO B CB  1 
ATOM   1560 C  CG  . PRO B 1 63  ? 24.816 3.114   18.273  1.00 34.54 ? 62  PRO B CG  1 
ATOM   1561 C  CD  . PRO B 1 63  ? 25.589 4.113   17.448  1.00 34.73 ? 62  PRO B CD  1 
ATOM   1562 N  N   . HIS B 1 64  ? 27.248 2.166   21.200  1.00 34.52 ? 63  HIS B N   1 
ATOM   1563 C  CA  . HIS B 1 64  ? 27.978 0.969   21.585  1.00 32.96 ? 63  HIS B CA  1 
ATOM   1564 C  C   . HIS B 1 64  ? 27.547 -0.192  20.678  1.00 33.45 ? 63  HIS B C   1 
ATOM   1565 O  O   . HIS B 1 64  ? 26.378 -0.303  20.304  1.00 31.78 ? 63  HIS B O   1 
ATOM   1566 C  CB  . HIS B 1 64  ? 27.685 0.618   23.046  1.00 30.94 ? 63  HIS B CB  1 
ATOM   1567 C  CG  . HIS B 1 64  ? 28.187 1.631   24.030  1.00 29.62 ? 63  HIS B CG  1 
ATOM   1568 N  ND1 . HIS B 1 64  ? 28.024 1.485   25.391  1.00 30.69 ? 63  HIS B ND1 1 
ATOM   1569 C  CD2 . HIS B 1 64  ? 28.835 2.806   23.853  1.00 32.03 ? 63  HIS B CD2 1 
ATOM   1570 C  CE1 . HIS B 1 64  ? 28.549 2.527   26.011  1.00 31.01 ? 63  HIS B CE1 1 
ATOM   1571 N  NE2 . HIS B 1 64  ? 29.047 3.345   25.102  1.00 31.92 ? 63  HIS B NE2 1 
ATOM   1572 N  N   . PHE B 1 65  ? 28.501 -1.040  20.307  1.00 35.16 ? 64  PHE B N   1 
ATOM   1573 C  CA  . PHE B 1 65  ? 28.207 -2.200  19.469  1.00 34.45 ? 64  PHE B CA  1 
ATOM   1574 C  C   . PHE B 1 65  ? 27.183 -3.033  20.240  1.00 34.79 ? 64  PHE B C   1 
ATOM   1575 O  O   . PHE B 1 65  ? 27.486 -3.556  21.319  1.00 34.34 ? 64  PHE B O   1 
ATOM   1576 C  CB  . PHE B 1 65  ? 29.477 -3.021  19.248  1.00 33.42 ? 64  PHE B CB  1 
ATOM   1577 C  CG  . PHE B 1 65  ? 29.266 -4.238  18.391  1.00 34.44 ? 64  PHE B CG  1 
ATOM   1578 C  CD1 . PHE B 1 65  ? 29.935 -5.422  18.670  1.00 34.32 ? 64  PHE B CD1 1 
ATOM   1579 C  CD2 . PHE B 1 65  ? 28.413 -4.194  17.295  1.00 31.60 ? 64  PHE B CD2 1 
ATOM   1580 C  CE1 . PHE B 1 65  ? 29.755 -6.549  17.866  1.00 33.28 ? 64  PHE B CE1 1 
ATOM   1581 C  CE2 . PHE B 1 65  ? 28.229 -5.315  16.487  1.00 33.85 ? 64  PHE B CE2 1 
ATOM   1582 C  CZ  . PHE B 1 65  ? 28.899 -6.491  16.772  1.00 32.67 ? 64  PHE B CZ  1 
ATOM   1583 N  N   . ASN B 1 66  ? 25.989 -3.184  19.678  1.00 34.73 ? 65  ASN B N   1 
ATOM   1584 C  CA  . ASN B 1 66  ? 24.917 -3.900  20.359  1.00 36.00 ? 65  ASN B CA  1 
ATOM   1585 C  C   . ASN B 1 66  ? 24.005 -4.686  19.406  1.00 37.33 ? 65  ASN B C   1 
ATOM   1586 O  O   . ASN B 1 66  ? 22.833 -4.361  19.249  1.00 35.44 ? 65  ASN B O   1 
ATOM   1587 C  CB  . ASN B 1 66  ? 24.107 -2.869  21.156  1.00 37.12 ? 65  ASN B CB  1 
ATOM   1588 C  CG  . ASN B 1 66  ? 22.937 -3.474  21.907  1.00 40.55 ? 65  ASN B CG  1 
ATOM   1589 O  OD1 . ASN B 1 66  ? 22.927 -4.666  22.226  1.00 37.94 ? 65  ASN B OD1 1 
ATOM   1590 N  ND2 . ASN B 1 66  ? 21.947 -2.636  22.216  1.00 38.48 ? 65  ASN B ND2 1 
ATOM   1591 N  N   . PRO B 1 67  ? 24.540 -5.744  18.775  1.00 37.45 ? 66  PRO B N   1 
ATOM   1592 C  CA  . PRO B 1 67  ? 23.795 -6.585  17.835  1.00 38.34 ? 66  PRO B CA  1 
ATOM   1593 C  C   . PRO B 1 67  ? 22.645 -7.371  18.453  1.00 39.53 ? 66  PRO B C   1 
ATOM   1594 O  O   . PRO B 1 67  ? 21.703 -7.744  17.754  1.00 41.12 ? 66  PRO B O   1 
ATOM   1595 C  CB  . PRO B 1 67  ? 24.882 -7.490  17.249  1.00 38.11 ? 66  PRO B CB  1 
ATOM   1596 C  CG  . PRO B 1 67  ? 25.839 -7.642  18.392  1.00 36.38 ? 66  PRO B CG  1 
ATOM   1597 C  CD  . PRO B 1 67  ? 25.925 -6.228  18.928  1.00 37.92 ? 66  PRO B CD  1 
ATOM   1598 N  N   . LEU B 1 68  ? 22.713 -7.614  19.757  1.00 39.04 ? 67  LEU B N   1 
ATOM   1599 C  CA  . LEU B 1 68  ? 21.665 -8.367  20.441  1.00 41.79 ? 67  LEU B CA  1 
ATOM   1600 C  C   . LEU B 1 68  ? 20.581 -7.467  21.034  1.00 43.84 ? 67  LEU B C   1 
ATOM   1601 O  O   . LEU B 1 68  ? 19.647 -7.947  21.676  1.00 44.38 ? 67  LEU B O   1 
ATOM   1602 C  CB  . LEU B 1 68  ? 22.281 -9.230  21.547  1.00 41.30 ? 67  LEU B CB  1 
ATOM   1603 C  CG  . LEU B 1 68  ? 23.425 -10.149 21.097  1.00 42.08 ? 67  LEU B CG  1 
ATOM   1604 C  CD1 . LEU B 1 68  ? 23.794 -11.098 22.229  1.00 41.21 ? 67  LEU B CD1 1 
ATOM   1605 C  CD2 . LEU B 1 68  ? 23.007 -10.936 19.862  1.00 42.28 ? 67  LEU B CD2 1 
ATOM   1606 N  N   . SER B 1 69  ? 20.714 -6.163  20.820  1.00 44.29 ? 68  SER B N   1 
ATOM   1607 C  CA  . SER B 1 69  ? 19.746 -5.194  21.333  1.00 45.80 ? 68  SER B CA  1 
ATOM   1608 C  C   . SER B 1 69  ? 19.482 -5.350  22.829  1.00 44.82 ? 68  SER B C   1 
ATOM   1609 O  O   . SER B 1 69  ? 18.343 -5.555  23.247  1.00 43.17 ? 68  SER B O   1 
ATOM   1610 C  CB  . SER B 1 69  ? 18.426 -5.318  20.571  1.00 45.90 ? 68  SER B CB  1 
ATOM   1611 O  OG  . SER B 1 69  ? 18.618 -5.057  19.194  1.00 49.75 ? 68  SER B OG  1 
ATOM   1612 N  N   . ARG B 1 70  ? 20.545 -5.254  23.622  1.00 44.75 ? 69  ARG B N   1 
ATOM   1613 C  CA  . ARG B 1 70  ? 20.456 -5.363  25.075  1.00 44.10 ? 69  ARG B CA  1 
ATOM   1614 C  C   . ARG B 1 70  ? 20.679 -3.965  25.666  1.00 44.66 ? 69  ARG B C   1 
ATOM   1615 O  O   . ARG B 1 70  ? 20.890 -2.997  24.927  1.00 42.96 ? 69  ARG B O   1 
ATOM   1616 C  CB  . ARG B 1 70  ? 21.540 -6.312  25.607  1.00 44.63 ? 69  ARG B CB  1 
ATOM   1617 C  CG  . ARG B 1 70  ? 21.558 -7.698  24.973  1.00 47.75 ? 69  ARG B CG  1 
ATOM   1618 C  CD  . ARG B 1 70  ? 20.366 -8.536  25.408  1.00 48.93 ? 69  ARG B CD  1 
ATOM   1619 N  NE  . ARG B 1 70  ? 20.196 -9.735  24.589  1.00 48.96 ? 69  ARG B NE  1 
ATOM   1620 C  CZ  . ARG B 1 70  ? 20.981 -10.808 24.636  1.00 51.25 ? 69  ARG B CZ  1 
ATOM   1621 N  NH1 . ARG B 1 70  ? 20.732 -11.840 23.842  1.00 50.09 ? 69  ARG B NH1 1 
ATOM   1622 N  NH2 . ARG B 1 70  ? 22.008 -10.860 25.478  1.00 52.17 ? 69  ARG B NH2 1 
ATOM   1623 N  N   . LYS B 1 71  ? 20.632 -3.863  26.991  1.00 43.39 ? 70  LYS B N   1 
ATOM   1624 C  CA  . LYS B 1 71  ? 20.858 -2.589  27.654  1.00 44.33 ? 70  LYS B CA  1 
ATOM   1625 C  C   . LYS B 1 71  ? 22.327 -2.534  28.032  1.00 44.71 ? 70  LYS B C   1 
ATOM   1626 O  O   . LYS B 1 71  ? 22.981 -3.575  28.118  1.00 45.33 ? 70  LYS B O   1 
ATOM   1627 C  CB  . LYS B 1 71  ? 19.988 -2.476  28.909  1.00 45.74 ? 70  LYS B CB  1 
ATOM   1628 C  CG  . LYS B 1 71  ? 18.490 -2.471  28.627  1.00 46.39 ? 70  LYS B CG  1 
ATOM   1629 C  CD  . LYS B 1 71  ? 18.102 -1.342  27.680  1.00 49.61 ? 70  LYS B CD  1 
ATOM   1630 C  CE  . LYS B 1 71  ? 16.613 -1.360  27.379  0.00 49.39 ? 70  LYS B CE  1 
ATOM   1631 N  NZ  . LYS B 1 71  ? 16.218 -0.268  26.447  0.00 50.16 ? 70  LYS B NZ  1 
ATOM   1632 N  N   . HIS B 1 72  ? 22.845 -1.328  28.254  1.00 41.50 ? 71  HIS B N   1 
ATOM   1633 C  CA  . HIS B 1 72  ? 24.248 -1.157  28.620  1.00 41.06 ? 71  HIS B CA  1 
ATOM   1634 C  C   . HIS B 1 72  ? 24.528 -1.819  29.956  1.00 41.86 ? 71  HIS B C   1 
ATOM   1635 O  O   . HIS B 1 72  ? 23.638 -1.920  30.798  1.00 42.32 ? 71  HIS B O   1 
ATOM   1636 C  CB  . HIS B 1 72  ? 24.605 0.331   28.713  1.00 39.46 ? 71  HIS B CB  1 
ATOM   1637 C  CG  . HIS B 1 72  ? 26.043 0.584   29.045  1.00 37.86 ? 71  HIS B CG  1 
ATOM   1638 N  ND1 . HIS B 1 72  ? 27.077 0.260   28.189  1.00 32.78 ? 71  HIS B ND1 1 
ATOM   1639 C  CD2 . HIS B 1 72  ? 26.621 1.116   30.148  1.00 34.62 ? 71  HIS B CD2 1 
ATOM   1640 C  CE1 . HIS B 1 72  ? 28.228 0.583   28.751  1.00 34.64 ? 71  HIS B CE1 1 
ATOM   1641 N  NE2 . HIS B 1 72  ? 27.978 1.103   29.941  1.00 36.60 ? 71  HIS B NE2 1 
ATOM   1642 N  N   . GLY B 1 73  ? 25.767 -2.264  30.149  1.00 41.82 ? 72  GLY B N   1 
ATOM   1643 C  CA  . GLY B 1 73  ? 26.142 -2.903  31.396  1.00 42.50 ? 72  GLY B CA  1 
ATOM   1644 C  C   . GLY B 1 73  ? 27.644 -3.055  31.533  1.00 42.11 ? 72  GLY B C   1 
ATOM   1645 O  O   . GLY B 1 73  ? 28.385 -2.661  30.641  1.00 43.53 ? 72  GLY B O   1 
ATOM   1646 N  N   . GLY B 1 74  ? 28.093 -3.612  32.653  1.00 43.18 ? 73  GLY B N   1 
ATOM   1647 C  CA  . GLY B 1 74  ? 29.516 -3.824  32.866  1.00 43.77 ? 73  GLY B CA  1 
ATOM   1648 C  C   . GLY B 1 74  ? 29.900 -5.101  32.144  1.00 43.28 ? 73  GLY B C   1 
ATOM   1649 O  O   . GLY B 1 74  ? 29.023 -5.908  31.838  1.00 44.17 ? 73  GLY B O   1 
ATOM   1650 N  N   . PRO B 1 75  ? 31.186 -5.325  31.851  1.00 44.35 ? 74  PRO B N   1 
ATOM   1651 C  CA  . PRO B 1 75  ? 31.563 -6.558  31.149  1.00 45.95 ? 74  PRO B CA  1 
ATOM   1652 C  C   . PRO B 1 75  ? 31.142 -7.858  31.838  1.00 49.26 ? 74  PRO B C   1 
ATOM   1653 O  O   . PRO B 1 75  ? 30.985 -8.891  31.184  1.00 49.84 ? 74  PRO B O   1 
ATOM   1654 C  CB  . PRO B 1 75  ? 33.081 -6.433  31.019  1.00 45.24 ? 74  PRO B CB  1 
ATOM   1655 C  CG  . PRO B 1 75  ? 33.461 -5.566  32.167  1.00 44.88 ? 74  PRO B CG  1 
ATOM   1656 C  CD  . PRO B 1 75  ? 32.375 -4.523  32.180  1.00 43.12 ? 74  PRO B CD  1 
ATOM   1657 N  N   . LYS B 1 76  ? 30.935 -7.805  33.150  1.00 51.68 ? 75  LYS B N   1 
ATOM   1658 C  CA  . LYS B 1 76  ? 30.551 -9.001  33.896  1.00 54.19 ? 75  LYS B CA  1 
ATOM   1659 C  C   . LYS B 1 76  ? 29.051 -9.148  34.144  1.00 55.49 ? 75  LYS B C   1 
ATOM   1660 O  O   . LYS B 1 76  ? 28.618 -10.087 34.805  1.00 56.42 ? 75  LYS B O   1 
ATOM   1661 C  CB  . LYS B 1 76  ? 31.319 -9.037  35.220  1.00 54.47 ? 75  LYS B CB  1 
ATOM   1662 C  CG  . LYS B 1 76  ? 32.824 -9.033  34.997  1.00 56.21 ? 75  LYS B CG  1 
ATOM   1663 C  CD  . LYS B 1 76  ? 33.643 -9.055  36.273  1.00 57.56 ? 75  LYS B CD  1 
ATOM   1664 C  CE  . LYS B 1 76  ? 35.132 -8.964  35.933  1.00 57.68 ? 75  LYS B CE  1 
ATOM   1665 N  NZ  . LYS B 1 76  ? 36.022 -9.066  37.128  1.00 58.51 ? 75  LYS B NZ  1 
ATOM   1666 N  N   . ASP B 1 77  ? 28.258 -8.236  33.594  1.00 55.79 ? 76  ASP B N   1 
ATOM   1667 C  CA  . ASP B 1 77  ? 26.809 -8.278  33.769  1.00 56.57 ? 76  ASP B CA  1 
ATOM   1668 C  C   . ASP B 1 77  ? 26.151 -9.104  32.672  1.00 56.47 ? 76  ASP B C   1 
ATOM   1669 O  O   . ASP B 1 77  ? 26.499 -8.965  31.498  1.00 58.07 ? 76  ASP B O   1 
ATOM   1670 C  CB  . ASP B 1 77  ? 26.253 -6.855  33.753  1.00 58.31 ? 76  ASP B CB  1 
ATOM   1671 C  CG  . ASP B 1 77  ? 26.833 -6.000  34.856  1.00 59.16 ? 76  ASP B CG  1 
ATOM   1672 O  OD1 . ASP B 1 77  ? 26.717 -4.759  34.775  1.00 60.42 ? 76  ASP B OD1 1 
ATOM   1673 O  OD2 . ASP B 1 77  ? 27.401 -6.572  35.810  1.00 60.67 ? 76  ASP B OD2 1 
ATOM   1674 N  N   . GLU B 1 78  ? 25.207 -9.964  33.044  1.00 54.92 ? 77  GLU B N   1 
ATOM   1675 C  CA  . GLU B 1 78  ? 24.538 -10.793 32.049  1.00 54.66 ? 77  GLU B CA  1 
ATOM   1676 C  C   . GLU B 1 78  ? 23.934 -9.901  30.965  1.00 51.98 ? 77  GLU B C   1 
ATOM   1677 O  O   . GLU B 1 78  ? 24.070 -10.182 29.773  1.00 52.59 ? 77  GLU B O   1 
ATOM   1678 C  CB  . GLU B 1 78  ? 23.454 -11.665 32.701  1.00 56.83 ? 77  GLU B CB  1 
ATOM   1679 C  CG  . GLU B 1 78  ? 22.717 -12.572 31.714  1.00 59.38 ? 77  GLU B CG  1 
ATOM   1680 C  CD  . GLU B 1 78  ? 22.232 -13.875 32.341  1.00 61.19 ? 77  GLU B CD  1 
ATOM   1681 O  OE1 . GLU B 1 78  ? 23.085 -14.678 32.778  1.00 63.27 ? 77  GLU B OE1 1 
ATOM   1682 O  OE2 . GLU B 1 78  ? 21.003 -14.102 32.391  1.00 60.08 ? 77  GLU B OE2 1 
ATOM   1683 N  N   . GLU B 1 79  ? 23.278 -8.821  31.381  1.00 48.31 ? 78  GLU B N   1 
ATOM   1684 C  CA  . GLU B 1 79  ? 22.686 -7.879  30.438  1.00 45.21 ? 78  GLU B CA  1 
ATOM   1685 C  C   . GLU B 1 79  ? 23.771 -6.846  30.092  1.00 43.60 ? 78  GLU B C   1 
ATOM   1686 O  O   . GLU B 1 79  ? 24.341 -6.212  30.985  1.00 41.28 ? 78  GLU B O   1 
ATOM   1687 C  CB  . GLU B 1 79  ? 21.472 -7.194  31.077  1.00 46.40 ? 78  GLU B CB  1 
ATOM   1688 C  CG  . GLU B 1 79  ? 20.720 -6.232  30.167  1.00 48.62 ? 78  GLU B CG  1 
ATOM   1689 C  CD  . GLU B 1 79  ? 19.880 -6.937  29.111  1.00 51.63 ? 78  GLU B CD  1 
ATOM   1690 O  OE1 . GLU B 1 79  ? 19.302 -6.235  28.252  1.00 48.57 ? 78  GLU B OE1 1 
ATOM   1691 O  OE2 . GLU B 1 79  ? 19.791 -8.188  29.139  1.00 52.96 ? 78  GLU B OE2 1 
ATOM   1692 N  N   . ARG B 1 80  ? 24.069 -6.694  28.802  1.00 41.10 ? 79  ARG B N   1 
ATOM   1693 C  CA  . ARG B 1 80  ? 25.092 -5.745  28.356  1.00 37.86 ? 79  ARG B CA  1 
ATOM   1694 C  C   . ARG B 1 80  ? 25.217 -5.723  26.846  1.00 36.25 ? 79  ARG B C   1 
ATOM   1695 O  O   . ARG B 1 80  ? 24.759 -6.630  26.158  1.00 35.84 ? 79  ARG B O   1 
ATOM   1696 C  CB  . ARG B 1 80  ? 26.457 -6.121  28.938  1.00 38.55 ? 79  ARG B CB  1 
ATOM   1697 C  CG  . ARG B 1 80  ? 26.935 -7.520  28.530  1.00 41.20 ? 79  ARG B CG  1 
ATOM   1698 C  CD  . ARG B 1 80  ? 28.159 -7.463  27.616  1.00 46.86 ? 79  ARG B CD  1 
ATOM   1699 N  NE  . ARG B 1 80  ? 29.375 -7.874  28.308  1.00 45.91 ? 79  ARG B NE  1 
ATOM   1700 C  CZ  . ARG B 1 80  ? 30.578 -7.957  27.747  1.00 45.52 ? 79  ARG B CZ  1 
ATOM   1701 N  NH1 . ARG B 1 80  ? 31.612 -8.350  28.478  1.00 44.36 ? 79  ARG B NH1 1 
ATOM   1702 N  NH2 . ARG B 1 80  ? 30.757 -7.647  26.468  1.00 46.13 ? 79  ARG B NH2 1 
ATOM   1703 N  N   . HIS B 1 81  ? 25.844 -4.677  26.328  1.00 32.96 ? 80  HIS B N   1 
ATOM   1704 C  CA  . HIS B 1 81  ? 26.068 -4.576  24.895  1.00 32.43 ? 80  HIS B CA  1 
ATOM   1705 C  C   . HIS B 1 81  ? 27.279 -5.465  24.624  1.00 30.27 ? 80  HIS B C   1 
ATOM   1706 O  O   . HIS B 1 81  ? 28.120 -5.650  25.505  1.00 28.87 ? 80  HIS B O   1 
ATOM   1707 C  CB  . HIS B 1 81  ? 26.420 -3.134  24.512  1.00 33.53 ? 80  HIS B CB  1 
ATOM   1708 C  CG  . HIS B 1 81  ? 25.337 -2.144  24.802  1.00 35.07 ? 80  HIS B CG  1 
ATOM   1709 N  ND1 . HIS B 1 81  ? 25.589 -0.909  25.365  1.00 33.93 ? 80  HIS B ND1 1 
ATOM   1710 C  CD2 . HIS B 1 81  ? 24.003 -2.187  24.568  1.00 34.47 ? 80  HIS B CD2 1 
ATOM   1711 C  CE1 . HIS B 1 81  ? 24.456 -0.235  25.462  1.00 34.36 ? 80  HIS B CE1 1 
ATOM   1712 N  NE2 . HIS B 1 81  ? 23.480 -0.988  24.984  1.00 33.62 ? 80  HIS B NE2 1 
ATOM   1713 N  N   . VAL B 1 82  ? 27.378 -6.016  23.422  1.00 30.70 ? 81  VAL B N   1 
ATOM   1714 C  CA  . VAL B 1 82  ? 28.532 -6.844  23.091  1.00 31.27 ? 81  VAL B CA  1 
ATOM   1715 C  C   . VAL B 1 82  ? 29.817 -6.033  23.293  1.00 31.94 ? 81  VAL B C   1 
ATOM   1716 O  O   . VAL B 1 82  ? 30.824 -6.561  23.748  1.00 34.96 ? 81  VAL B O   1 
ATOM   1717 C  CB  . VAL B 1 82  ? 28.490 -7.321  21.614  1.00 31.93 ? 81  VAL B CB  1 
ATOM   1718 C  CG1 . VAL B 1 82  ? 29.820 -7.963  21.240  1.00 30.94 ? 81  VAL B CG1 1 
ATOM   1719 C  CG2 . VAL B 1 82  ? 27.368 -8.330  21.414  1.00 32.89 ? 81  VAL B CG2 1 
ATOM   1720 N  N   . GLY B 1 83  ? 29.769 -4.742  22.967  1.00 32.90 ? 82  GLY B N   1 
ATOM   1721 C  CA  . GLY B 1 83  ? 30.957 -3.907  23.094  1.00 32.76 ? 82  GLY B CA  1 
ATOM   1722 C  C   . GLY B 1 83  ? 31.300 -3.288  24.444  1.00 33.80 ? 82  GLY B C   1 
ATOM   1723 O  O   . GLY B 1 83  ? 32.232 -2.488  24.535  1.00 34.32 ? 82  GLY B O   1 
ATOM   1724 N  N   . ASP B 1 84  ? 30.584 -3.645  25.501  1.00 32.51 ? 83  ASP B N   1 
ATOM   1725 C  CA  . ASP B 1 84  ? 30.868 -3.060  26.806  1.00 33.84 ? 83  ASP B CA  1 
ATOM   1726 C  C   . ASP B 1 84  ? 32.046 -3.672  27.543  1.00 34.32 ? 83  ASP B C   1 
ATOM   1727 O  O   . ASP B 1 84  ? 31.932 -4.748  28.130  1.00 35.16 ? 83  ASP B O   1 
ATOM   1728 C  CB  . ASP B 1 84  ? 29.623 -3.121  27.686  1.00 33.13 ? 83  ASP B CB  1 
ATOM   1729 C  CG  . ASP B 1 84  ? 28.517 -2.255  27.154  1.00 31.05 ? 83  ASP B CG  1 
ATOM   1730 O  OD1 . ASP B 1 84  ? 28.854 -1.271  26.464  1.00 31.43 ? 83  ASP B OD1 1 
ATOM   1731 O  OD2 . ASP B 1 84  ? 27.330 -2.539  27.431  1.00 33.49 ? 83  ASP B OD2 1 
ATOM   1732 N  N   . LEU B 1 85  ? 33.173 -2.966  27.528  1.00 33.97 ? 84  LEU B N   1 
ATOM   1733 C  CA  . LEU B 1 85  ? 34.378 -3.445  28.195  1.00 36.43 ? 84  LEU B CA  1 
ATOM   1734 C  C   . LEU B 1 85  ? 34.736 -2.698  29.479  1.00 35.95 ? 84  LEU B C   1 
ATOM   1735 O  O   . LEU B 1 85  ? 35.889 -2.697  29.900  1.00 35.80 ? 84  LEU B O   1 
ATOM   1736 C  CB  . LEU B 1 85  ? 35.563 -3.427  27.215  1.00 33.54 ? 84  LEU B CB  1 
ATOM   1737 C  CG  . LEU B 1 85  ? 35.372 -4.347  26.000  1.00 33.59 ? 84  LEU B CG  1 
ATOM   1738 C  CD1 . LEU B 1 85  ? 36.554 -4.214  25.043  1.00 32.19 ? 84  LEU B CD1 1 
ATOM   1739 C  CD2 . LEU B 1 85  ? 35.218 -5.792  26.470  1.00 33.11 ? 84  LEU B CD2 1 
ATOM   1740 N  N   . GLY B 1 86  ? 33.739 -2.064  30.089  1.00 37.90 ? 85  GLY B N   1 
ATOM   1741 C  CA  . GLY B 1 86  ? 33.941 -1.359  31.346  1.00 37.85 ? 85  GLY B CA  1 
ATOM   1742 C  C   . GLY B 1 86  ? 34.817 -0.124  31.362  1.00 39.12 ? 85  GLY B C   1 
ATOM   1743 O  O   . GLY B 1 86  ? 34.672 0.775   30.526  1.00 38.39 ? 85  GLY B O   1 
ATOM   1744 N  N   . ASN B 1 87  ? 35.722 -0.080  32.336  1.00 38.79 ? 86  ASN B N   1 
ATOM   1745 C  CA  . ASN B 1 87  ? 36.632 1.044   32.500  1.00 41.84 ? 86  ASN B CA  1 
ATOM   1746 C  C   . ASN B 1 87  ? 38.105 0.643   32.532  1.00 42.54 ? 86  ASN B C   1 
ATOM   1747 O  O   . ASN B 1 87  ? 38.450 -0.478  32.907  1.00 42.11 ? 86  ASN B O   1 
ATOM   1748 C  CB  . ASN B 1 87  ? 36.333 1.781   33.807  1.00 43.54 ? 86  ASN B CB  1 
ATOM   1749 C  CG  . ASN B 1 87  ? 34.980 2.444   33.814  1.00 44.02 ? 86  ASN B CG  1 
ATOM   1750 O  OD1 . ASN B 1 87  ? 34.710 3.336   33.013  1.00 45.75 ? 86  ASN B OD1 1 
ATOM   1751 N  ND2 . ASN B 1 87  ? 34.120 2.017   34.729  1.00 44.12 ? 86  ASN B ND2 1 
ATOM   1752 N  N   . VAL B 1 88  ? 38.961 1.580   32.132  1.00 42.11 ? 87  VAL B N   1 
ATOM   1753 C  CA  . VAL B 1 88  ? 40.410 1.404   32.175  1.00 43.90 ? 87  VAL B CA  1 
ATOM   1754 C  C   . VAL B 1 88  ? 40.854 2.479   33.173  1.00 46.44 ? 87  VAL B C   1 
ATOM   1755 O  O   . VAL B 1 88  ? 40.165 3.492   33.334  1.00 46.84 ? 87  VAL B O   1 
ATOM   1756 C  CB  . VAL B 1 88  ? 41.082 1.650   30.792  1.00 42.77 ? 87  VAL B CB  1 
ATOM   1757 C  CG1 . VAL B 1 88  ? 40.632 0.590   29.808  1.00 41.70 ? 87  VAL B CG1 1 
ATOM   1758 C  CG2 . VAL B 1 88  ? 40.738 3.039   30.263  1.00 41.56 ? 87  VAL B CG2 1 
ATOM   1759 N  N   . THR B 1 89  ? 41.987 2.275   33.838  1.00 48.37 ? 88  THR B N   1 
ATOM   1760 C  CA  . THR B 1 89  ? 42.452 3.235   34.835  1.00 49.17 ? 88  THR B CA  1 
ATOM   1761 C  C   . THR B 1 89  ? 43.815 3.845   34.561  1.00 49.52 ? 88  THR B C   1 
ATOM   1762 O  O   . THR B 1 89  ? 44.790 3.132   34.345  1.00 49.49 ? 88  THR B O   1 
ATOM   1763 C  CB  . THR B 1 89  ? 42.491 2.583   36.227  1.00 50.46 ? 88  THR B CB  1 
ATOM   1764 O  OG1 . THR B 1 89  ? 41.182 2.108   36.562  1.00 49.78 ? 88  THR B OG1 1 
ATOM   1765 C  CG2 . THR B 1 89  ? 42.950 3.586   37.278  1.00 49.57 ? 88  THR B CG2 1 
ATOM   1766 N  N   . ALA B 1 90  ? 43.873 5.174   34.582  1.00 51.63 ? 89  ALA B N   1 
ATOM   1767 C  CA  . ALA B 1 90  ? 45.119 5.894   34.357  1.00 54.00 ? 89  ALA B CA  1 
ATOM   1768 C  C   . ALA B 1 90  ? 45.791 6.178   35.691  1.00 55.49 ? 89  ALA B C   1 
ATOM   1769 O  O   . ALA B 1 90  ? 45.126 6.300   36.723  1.00 56.19 ? 89  ALA B O   1 
ATOM   1770 C  CB  . ALA B 1 90  ? 44.852 7.211   33.620  1.00 54.47 ? 89  ALA B CB  1 
ATOM   1771 N  N   . ASP B 1 91  ? 47.115 6.265   35.672  1.00 56.56 ? 90  ASP B N   1 
ATOM   1772 C  CA  . ASP B 1 91  ? 47.853 6.571   36.887  1.00 57.36 ? 90  ASP B CA  1 
ATOM   1773 C  C   . ASP B 1 91  ? 48.201 8.059   36.849  1.00 59.30 ? 90  ASP B C   1 
ATOM   1774 O  O   . ASP B 1 91  ? 47.961 8.738   35.841  1.00 60.27 ? 90  ASP B O   1 
ATOM   1775 C  CB  . ASP B 1 91  ? 49.125 5.721   36.989  1.00 55.76 ? 90  ASP B CB  1 
ATOM   1776 C  CG  . ASP B 1 91  ? 49.949 5.733   35.715  1.00 55.61 ? 90  ASP B CG  1 
ATOM   1777 O  OD1 . ASP B 1 91  ? 50.081 6.813   35.090  1.00 55.77 ? 90  ASP B OD1 1 
ATOM   1778 O  OD2 . ASP B 1 91  ? 50.491 4.665   35.352  1.00 54.32 ? 90  ASP B OD2 1 
ATOM   1779 N  N   . LYS B 1 92  ? 48.768 8.568   37.938  1.00 59.64 ? 91  LYS B N   1 
ATOM   1780 C  CA  . LYS B 1 92  ? 49.121 9.984   38.013  1.00 59.78 ? 91  LYS B CA  1 
ATOM   1781 C  C   . LYS B 1 92  ? 49.712 10.613  36.747  1.00 60.05 ? 91  LYS B C   1 
ATOM   1782 O  O   . LYS B 1 92  ? 49.473 11.787  36.464  1.00 60.32 ? 91  LYS B O   1 
ATOM   1783 C  CB  . LYS B 1 92  ? 50.069 10.227  39.187  1.00 59.77 ? 91  LYS B CB  1 
ATOM   1784 C  CG  . LYS B 1 92  ? 49.444 9.991   40.534  0.00 59.22 ? 91  LYS B CG  1 
ATOM   1785 C  CD  . LYS B 1 92  ? 50.427 10.184  41.659  0.00 59.33 ? 91  LYS B CD  1 
ATOM   1786 C  CE  . LYS B 1 92  ? 49.670 10.233  42.967  1.00 59.51 ? 91  LYS B CE  1 
ATOM   1787 N  NZ  . LYS B 1 92  ? 48.658 11.334  42.968  1.00 61.15 ? 91  LYS B NZ  1 
ATOM   1788 N  N   . ASP B 1 93  ? 50.485 9.846   35.990  1.00 60.86 ? 92  ASP B N   1 
ATOM   1789 C  CA  . ASP B 1 93  ? 51.089 10.363  34.769  1.00 61.05 ? 92  ASP B CA  1 
ATOM   1790 C  C   . ASP B 1 93  ? 50.204 10.306  33.517  1.00 60.23 ? 92  ASP B C   1 
ATOM   1791 O  O   . ASP B 1 93  ? 50.645 10.671  32.434  1.00 60.96 ? 92  ASP B O   1 
ATOM   1792 C  CB  . ASP B 1 93  ? 52.425 9.647   34.535  1.00 62.82 ? 92  ASP B CB  1 
ATOM   1793 C  CG  . ASP B 1 93  ? 53.362 9.808   35.706  1.00 64.89 ? 92  ASP B CG  1 
ATOM   1794 O  OD1 . ASP B 1 93  ? 53.025 9.293   36.793  1.00 65.79 ? 92  ASP B OD1 1 
ATOM   1795 O  OD2 . ASP B 1 93  ? 54.420 10.456  35.544  1.00 64.46 ? 92  ASP B OD2 1 
ATOM   1796 N  N   . GLY B 1 94  ? 48.966 9.846   33.666  1.00 58.80 ? 93  GLY B N   1 
ATOM   1797 C  CA  . GLY B 1 94  ? 48.061 9.770   32.530  1.00 58.34 ? 93  GLY B CA  1 
ATOM   1798 C  C   . GLY B 1 94  ? 48.136 8.488   31.709  1.00 57.51 ? 93  GLY B C   1 
ATOM   1799 O  O   . GLY B 1 94  ? 47.708 8.445   30.551  1.00 57.22 ? 93  GLY B O   1 
ATOM   1800 N  N   . VAL B 1 95  ? 48.674 7.433   32.309  1.00 55.75 ? 94  VAL B N   1 
ATOM   1801 C  CA  . VAL B 1 95  ? 48.804 6.164   31.618  1.00 54.95 ? 94  VAL B CA  1 
ATOM   1802 C  C   . VAL B 1 95  ? 47.914 5.090   32.206  1.00 54.69 ? 94  VAL B C   1 
ATOM   1803 O  O   . VAL B 1 95  ? 47.844 4.921   33.420  1.00 54.49 ? 94  VAL B O   1 
ATOM   1804 C  CB  . VAL B 1 95  ? 50.259 5.660   31.650  1.00 55.79 ? 94  VAL B CB  1 
ATOM   1805 C  CG1 . VAL B 1 95  ? 50.311 4.180   31.250  1.00 55.03 ? 94  VAL B CG1 1 
ATOM   1806 C  CG2 . VAL B 1 95  ? 51.113 6.498   30.713  1.00 56.42 ? 94  VAL B CG2 1 
ATOM   1807 N  N   . ALA B 1 96  ? 47.241 4.358   31.327  1.00 54.13 ? 95  ALA B N   1 
ATOM   1808 C  CA  . ALA B 1 96  ? 46.353 3.281   31.737  1.00 53.76 ? 95  ALA B CA  1 
ATOM   1809 C  C   . ALA B 1 96  ? 46.808 1.999   31.066  1.00 53.92 ? 95  ALA B C   1 
ATOM   1810 O  O   . ALA B 1 96  ? 46.884 1.930   29.838  1.00 53.49 ? 95  ALA B O   1 
ATOM   1811 C  CB  . ALA B 1 96  ? 44.921 3.600   31.333  1.00 52.98 ? 95  ALA B CB  1 
ATOM   1812 N  N   . ASP B 1 97  ? 47.132 0.994   31.869  1.00 53.60 ? 96  ASP B N   1 
ATOM   1813 C  CA  . ASP B 1 97  ? 47.562 -0.281  31.324  1.00 54.47 ? 96  ASP B CA  1 
ATOM   1814 C  C   . ASP B 1 97  ? 46.379 -1.219  31.244  1.00 53.60 ? 96  ASP B C   1 
ATOM   1815 O  O   . ASP B 1 97  ? 45.766 -1.561  32.256  1.00 53.30 ? 96  ASP B O   1 
ATOM   1816 C  CB  . ASP B 1 97  ? 48.667 -0.896  32.176  1.00 57.66 ? 96  ASP B CB  1 
ATOM   1817 C  CG  . ASP B 1 97  ? 50.043 -0.440  31.744  1.00 60.41 ? 96  ASP B CG  1 
ATOM   1818 O  OD1 . ASP B 1 97  ? 50.403 0.726   32.024  1.00 61.06 ? 96  ASP B OD1 1 
ATOM   1819 O  OD2 . ASP B 1 97  ? 50.756 -1.247  31.105  1.00 60.29 ? 96  ASP B OD2 1 
ATOM   1820 N  N   . VAL B 1 98  ? 46.070 -1.634  30.023  1.00 51.35 ? 97  VAL B N   1 
ATOM   1821 C  CA  . VAL B 1 98  ? 44.940 -2.508  29.772  1.00 49.41 ? 97  VAL B CA  1 
ATOM   1822 C  C   . VAL B 1 98  ? 45.319 -3.975  29.726  1.00 49.06 ? 97  VAL B C   1 
ATOM   1823 O  O   . VAL B 1 98  ? 46.292 -4.354  29.089  1.00 50.43 ? 97  VAL B O   1 
ATOM   1824 C  CB  . VAL B 1 98  ? 44.270 -2.139  28.444  1.00 47.85 ? 97  VAL B CB  1 
ATOM   1825 C  CG1 . VAL B 1 98  ? 43.060 -3.011  28.218  1.00 46.18 ? 97  VAL B CG1 1 
ATOM   1826 C  CG2 . VAL B 1 98  ? 43.895 -0.665  28.450  1.00 47.02 ? 97  VAL B CG2 1 
ATOM   1827 N  N   . SER B 1 99  ? 44.529 -4.793  30.410  1.00 49.85 ? 98  SER B N   1 
ATOM   1828 C  CA  . SER B 1 99  ? 44.735 -6.232  30.443  1.00 50.65 ? 98  SER B CA  1 
ATOM   1829 C  C   . SER B 1 99  ? 43.377 -6.840  30.752  1.00 50.86 ? 98  SER B C   1 
ATOM   1830 O  O   . SER B 1 99  ? 43.036 -7.066  31.909  1.00 51.93 ? 98  SER B O   1 
ATOM   1831 C  CB  . SER B 1 99  ? 45.744 -6.612  31.524  1.00 51.84 ? 98  SER B CB  1 
ATOM   1832 O  OG  . SER B 1 99  ? 46.158 -7.957  31.369  1.00 54.66 ? 98  SER B OG  1 
ATOM   1833 N  N   . ILE B 1 100 ? 42.606 -7.091  29.701  1.00 51.33 ? 99  ILE B N   1 
ATOM   1834 C  CA  . ILE B 1 100 ? 41.259 -7.645  29.811  1.00 50.46 ? 99  ILE B CA  1 
ATOM   1835 C  C   . ILE B 1 100 ? 41.108 -8.992  29.103  1.00 49.35 ? 99  ILE B C   1 
ATOM   1836 O  O   . ILE B 1 100 ? 41.865 -9.322  28.194  1.00 50.51 ? 99  ILE B O   1 
ATOM   1837 C  CB  . ILE B 1 100 ? 40.223 -6.666  29.171  1.00 50.35 ? 99  ILE B CB  1 
ATOM   1838 C  CG1 . ILE B 1 100 ? 40.155 -5.373  29.975  1.00 50.26 ? 99  ILE B CG1 1 
ATOM   1839 C  CG2 . ILE B 1 100 ? 38.853 -7.312  29.074  1.00 49.72 ? 99  ILE B CG2 1 
ATOM   1840 C  CD1 . ILE B 1 100 ? 39.266 -4.319  29.350  1.00 48.28 ? 99  ILE B CD1 1 
ATOM   1841 N  N   . GLU B 1 101 ? 40.125 -9.768  29.543  1.00 47.67 ? 100 GLU B N   1 
ATOM   1842 C  CA  . GLU B 1 101 ? 39.793 -11.036 28.917  1.00 46.04 ? 100 GLU B CA  1 
ATOM   1843 C  C   . GLU B 1 101 ? 38.272 -10.989 28.859  1.00 44.29 ? 100 GLU B C   1 
ATOM   1844 O  O   . GLU B 1 101 ? 37.614 -10.855 29.891  1.00 42.69 ? 100 GLU B O   1 
ATOM   1845 C  CB  . GLU B 1 101 ? 40.246 -12.228 29.757  1.00 48.49 ? 100 GLU B CB  1 
ATOM   1846 C  CG  . GLU B 1 101 ? 40.456 -13.475 28.908  1.00 54.37 ? 100 GLU B CG  1 
ATOM   1847 C  CD  . GLU B 1 101 ? 40.632 -14.748 29.719  1.00 57.28 ? 100 GLU B CD  1 
ATOM   1848 O  OE1 . GLU B 1 101 ? 39.615 -15.289 30.212  1.00 58.62 ? 100 GLU B OE1 1 
ATOM   1849 O  OE2 . GLU B 1 101 ? 41.787 -15.205 29.859  1.00 58.62 ? 100 GLU B OE2 1 
ATOM   1850 N  N   . ASP B 1 102 ? 37.705 -11.086 27.664  1.00 41.59 ? 101 ASP B N   1 
ATOM   1851 C  CA  . ASP B 1 102 ? 36.255 -11.009 27.537  1.00 40.23 ? 101 ASP B CA  1 
ATOM   1852 C  C   . ASP B 1 102 ? 35.702 -12.175 26.733  1.00 39.40 ? 101 ASP B C   1 
ATOM   1853 O  O   . ASP B 1 102 ? 36.324 -12.625 25.774  1.00 37.95 ? 101 ASP B O   1 
ATOM   1854 C  CB  . ASP B 1 102 ? 35.882 -9.673  26.880  1.00 37.09 ? 101 ASP B CB  1 
ATOM   1855 C  CG  . ASP B 1 102 ? 34.424 -9.309  27.070  1.00 38.09 ? 101 ASP B CG  1 
ATOM   1856 O  OD1 . ASP B 1 102 ? 33.603 -9.620  26.177  1.00 33.85 ? 101 ASP B OD1 1 
ATOM   1857 O  OD2 . ASP B 1 102 ? 34.101 -8.711  28.123  1.00 34.75 ? 101 ASP B OD2 1 
ATOM   1858 N  N   . SER B 1 103 ? 34.533 -12.673 27.131  1.00 38.83 ? 102 SER B N   1 
ATOM   1859 C  CA  . SER B 1 103 ? 33.920 -13.788 26.427  1.00 36.69 ? 102 SER B CA  1 
ATOM   1860 C  C   . SER B 1 103 ? 32.747 -13.381 25.555  1.00 37.07 ? 102 SER B C   1 
ATOM   1861 O  O   . SER B 1 103 ? 32.171 -14.220 24.865  1.00 36.86 ? 102 SER B O   1 
ATOM   1862 C  CB  . SER B 1 103 ? 33.481 -14.877 27.413  1.00 41.32 ? 102 SER B CB  1 
ATOM   1863 O  OG  . SER B 1 103 ? 32.989 -14.334 28.620  1.00 47.29 ? 102 SER B OG  1 
ATOM   1864 N  N   . VAL B 1 104 ? 32.398 -12.096 25.556  1.00 36.00 ? 103 VAL B N   1 
ATOM   1865 C  CA  . VAL B 1 104 ? 31.281 -11.654 24.732  1.00 34.94 ? 103 VAL B CA  1 
ATOM   1866 C  C   . VAL B 1 104 ? 31.740 -11.139 23.376  1.00 33.39 ? 103 VAL B C   1 
ATOM   1867 O  O   . VAL B 1 104 ? 31.153 -11.487 22.346  1.00 34.92 ? 103 VAL B O   1 
ATOM   1868 C  CB  . VAL B 1 104 ? 30.446 -10.572 25.434  1.00 36.42 ? 103 VAL B CB  1 
ATOM   1869 C  CG1 . VAL B 1 104 ? 29.203 -10.268 24.604  1.00 35.87 ? 103 VAL B CG1 1 
ATOM   1870 C  CG2 . VAL B 1 104 ? 30.050 -11.047 26.815  1.00 37.97 ? 103 VAL B CG2 1 
ATOM   1871 N  N   . ILE B 1 105 ? 32.777 -10.307 23.353  1.00 31.85 ? 104 ILE B N   1 
ATOM   1872 C  CA  . ILE B 1 105 ? 33.269 -9.826  22.065  1.00 31.55 ? 104 ILE B CA  1 
ATOM   1873 C  C   . ILE B 1 105 ? 33.915 -11.037 21.390  1.00 32.27 ? 104 ILE B C   1 
ATOM   1874 O  O   . ILE B 1 105 ? 34.227 -12.021 22.064  1.00 32.57 ? 104 ILE B O   1 
ATOM   1875 C  CB  . ILE B 1 105 ? 34.335 -8.712  22.207  1.00 30.28 ? 104 ILE B CB  1 
ATOM   1876 C  CG1 . ILE B 1 105 ? 35.480 -9.185  23.099  1.00 30.87 ? 104 ILE B CG1 1 
ATOM   1877 C  CG2 . ILE B 1 105 ? 33.707 -7.449  22.774  1.00 31.39 ? 104 ILE B CG2 1 
ATOM   1878 C  CD1 . ILE B 1 105 ? 36.685 -8.270  23.051  1.00 31.55 ? 104 ILE B CD1 1 
ATOM   1879 N  N   . SER B 1 106 ? 34.095 -10.969 20.074  1.00 33.40 ? 105 SER B N   1 
ATOM   1880 C  CA  . SER B 1 106 ? 34.708 -12.058 19.309  1.00 33.32 ? 105 SER B CA  1 
ATOM   1881 C  C   . SER B 1 106 ? 35.310 -11.518 18.017  1.00 34.15 ? 105 SER B C   1 
ATOM   1882 O  O   . SER B 1 106 ? 35.069 -10.365 17.651  1.00 34.15 ? 105 SER B O   1 
ATOM   1883 C  CB  . SER B 1 106 ? 33.659 -13.116 18.965  1.00 33.53 ? 105 SER B CB  1 
ATOM   1884 O  OG  . SER B 1 106 ? 34.221 -14.152 18.173  1.00 32.67 ? 105 SER B OG  1 
ATOM   1885 N  N   . LEU B 1 107 ? 36.082 -12.352 17.320  1.00 33.84 ? 106 LEU B N   1 
ATOM   1886 C  CA  . LEU B 1 107 ? 36.684 -11.925 16.069  1.00 34.72 ? 106 LEU B CA  1 
ATOM   1887 C  C   . LEU B 1 107 ? 36.014 -12.591 14.878  1.00 35.63 ? 106 LEU B C   1 
ATOM   1888 O  O   . LEU B 1 107 ? 36.549 -12.569 13.779  1.00 36.60 ? 106 LEU B O   1 
ATOM   1889 C  CB  . LEU B 1 107 ? 38.183 -12.229 16.039  1.00 35.51 ? 106 LEU B CB  1 
ATOM   1890 C  CG  . LEU B 1 107 ? 39.074 -11.635 17.130  1.00 35.59 ? 106 LEU B CG  1 
ATOM   1891 C  CD1 . LEU B 1 107 ? 40.520 -11.759 16.684  1.00 35.69 ? 106 LEU B CD1 1 
ATOM   1892 C  CD2 . LEU B 1 107 ? 38.731 -10.179 17.389  1.00 38.73 ? 106 LEU B CD2 1 
ATOM   1893 N  N   . SER B 1 108 ? 34.850 -13.190 15.106  1.00 34.78 ? 107 SER B N   1 
ATOM   1894 C  CA  . SER B 1 108 ? 34.095 -13.831 14.039  1.00 36.94 ? 107 SER B CA  1 
ATOM   1895 C  C   . SER B 1 108 ? 32.615 -13.886 14.417  1.00 35.54 ? 107 SER B C   1 
ATOM   1896 O  O   . SER B 1 108 ? 32.262 -13.727 15.583  1.00 34.45 ? 107 SER B O   1 
ATOM   1897 C  CB  . SER B 1 108 ? 34.617 -15.248 13.785  1.00 37.98 ? 107 SER B CB  1 
ATOM   1898 O  OG  . SER B 1 108 ? 34.490 -16.044 14.945  1.00 44.13 ? 107 SER B OG  1 
ATOM   1899 N  N   . GLY B 1 109 ? 31.751 -14.084 13.425  1.00 34.45 ? 108 GLY B N   1 
ATOM   1900 C  CA  . GLY B 1 109 ? 30.328 -14.167 13.697  1.00 35.49 ? 108 GLY B CA  1 
ATOM   1901 C  C   . GLY B 1 109 ? 29.623 -12.858 14.017  1.00 36.66 ? 108 GLY B C   1 
ATOM   1902 O  O   . GLY B 1 109 ? 30.111 -11.773 13.700  1.00 33.67 ? 108 GLY B O   1 
ATOM   1903 N  N   . ASP B 1 110 ? 28.454 -12.977 14.640  1.00 37.02 ? 109 ASP B N   1 
ATOM   1904 C  CA  . ASP B 1 110 ? 27.628 -11.832 15.028  1.00 38.77 ? 109 ASP B CA  1 
ATOM   1905 C  C   . ASP B 1 110 ? 28.327 -10.901 16.009  1.00 36.32 ? 109 ASP B C   1 
ATOM   1906 O  O   . ASP B 1 110 ? 28.170 -9.681  15.947  1.00 37.69 ? 109 ASP B O   1 
ATOM   1907 C  CB  . ASP B 1 110 ? 26.332 -12.317 15.682  1.00 43.31 ? 109 ASP B CB  1 
ATOM   1908 C  CG  . ASP B 1 110 ? 25.392 -12.986 14.706  1.00 48.85 ? 109 ASP B CG  1 
ATOM   1909 O  OD1 . ASP B 1 110 ? 24.512 -13.743 15.170  1.00 53.46 ? 109 ASP B OD1 1 
ATOM   1910 O  OD2 . ASP B 1 110 ? 25.516 -12.750 13.484  1.00 50.72 ? 109 ASP B OD2 1 
ATOM   1911 N  N   . HIS B 1 111 ? 29.088 -11.479 16.930  1.00 35.58 ? 110 HIS B N   1 
ATOM   1912 C  CA  . HIS B 1 111 ? 29.781 -10.677 17.929  1.00 34.23 ? 110 HIS B CA  1 
ATOM   1913 C  C   . HIS B 1 111 ? 31.129 -10.166 17.439  1.00 33.08 ? 110 HIS B C   1 
ATOM   1914 O  O   . HIS B 1 111 ? 31.916 -9.645  18.229  1.00 31.41 ? 110 HIS B O   1 
ATOM   1915 C  CB  . HIS B 1 111 ? 29.996 -11.479 19.218  1.00 35.52 ? 110 HIS B CB  1 
ATOM   1916 C  CG  . HIS B 1 111 ? 28.735 -12.010 19.829  1.00 38.40 ? 110 HIS B CG  1 
ATOM   1917 N  ND1 . HIS B 1 111 ? 28.679 -12.474 21.126  1.00 38.58 ? 110 HIS B ND1 1 
ATOM   1918 C  CD2 . HIS B 1 111 ? 27.497 -12.192 19.310  1.00 38.57 ? 110 HIS B CD2 1 
ATOM   1919 C  CE1 . HIS B 1 111 ? 27.460 -12.921 21.379  1.00 39.76 ? 110 HIS B CE1 1 
ATOM   1920 N  NE2 . HIS B 1 111 ? 26.724 -12.761 20.294  1.00 39.27 ? 110 HIS B NE2 1 
ATOM   1921 N  N   . SER B 1 112 ? 31.400 -10.311 16.144  1.00 32.85 ? 111 SER B N   1 
ATOM   1922 C  CA  . SER B 1 112 ? 32.678 -9.863  15.598  1.00 33.34 ? 111 SER B CA  1 
ATOM   1923 C  C   . SER B 1 112 ? 32.876 -8.360  15.712  1.00 32.68 ? 111 SER B C   1 
ATOM   1924 O  O   . SER B 1 112 ? 32.025 -7.585  15.297  1.00 33.42 ? 111 SER B O   1 
ATOM   1925 C  CB  . SER B 1 112 ? 32.821 -10.247 14.128  1.00 31.24 ? 111 SER B CB  1 
ATOM   1926 O  OG  . SER B 1 112 ? 34.072 -9.780  13.635  1.00 31.07 ? 111 SER B OG  1 
ATOM   1927 N  N   . ILE B 1 113 ? 34.016 -7.957  16.260  1.00 32.61 ? 112 ILE B N   1 
ATOM   1928 C  CA  . ILE B 1 113 ? 34.333 -6.538  16.410  1.00 31.58 ? 112 ILE B CA  1 
ATOM   1929 C  C   . ILE B 1 113 ? 35.278 -6.075  15.302  1.00 29.28 ? 112 ILE B C   1 
ATOM   1930 O  O   . ILE B 1 113 ? 35.756 -4.936  15.317  1.00 27.54 ? 112 ILE B O   1 
ATOM   1931 C  CB  . ILE B 1 113 ? 35.010 -6.261  17.768  1.00 29.50 ? 112 ILE B CB  1 
ATOM   1932 C  CG1 . ILE B 1 113 ? 36.348 -7.006  17.843  1.00 31.81 ? 112 ILE B CG1 1 
ATOM   1933 C  CG2 . ILE B 1 113 ? 34.097 -6.697  18.900  1.00 30.11 ? 112 ILE B CG2 1 
ATOM   1934 C  CD1 . ILE B 1 113 ? 37.124 -6.778  19.133  1.00 31.88 ? 112 ILE B CD1 1 
ATOM   1935 N  N   . ILE B 1 114 ? 35.559 -6.947  14.340  1.00 26.27 ? 113 ILE B N   1 
ATOM   1936 C  CA  . ILE B 1 114 ? 36.465 -6.555  13.267  1.00 28.32 ? 113 ILE B CA  1 
ATOM   1937 C  C   . ILE B 1 114 ? 35.805 -5.466  12.440  1.00 26.04 ? 113 ILE B C   1 
ATOM   1938 O  O   . ILE B 1 114 ? 34.640 -5.582  12.079  1.00 29.26 ? 113 ILE B O   1 
ATOM   1939 C  CB  . ILE B 1 114 ? 36.846 -7.757  12.361  1.00 26.05 ? 113 ILE B CB  1 
ATOM   1940 C  CG1 . ILE B 1 114 ? 37.580 -8.816  13.191  1.00 29.21 ? 113 ILE B CG1 1 
ATOM   1941 C  CG2 . ILE B 1 114 ? 37.743 -7.284  11.215  1.00 28.75 ? 113 ILE B CG2 1 
ATOM   1942 C  CD1 . ILE B 1 114 ? 38.070 -10.007 12.392  1.00 30.60 ? 113 ILE B CD1 1 
ATOM   1943 N  N   . GLY B 1 115 ? 36.540 -4.394  12.169  1.00 25.73 ? 114 GLY B N   1 
ATOM   1944 C  CA  . GLY B 1 115 ? 35.985 -3.315  11.373  1.00 28.34 ? 114 GLY B CA  1 
ATOM   1945 C  C   . GLY B 1 115 ? 35.106 -2.357  12.155  1.00 31.04 ? 114 GLY B C   1 
ATOM   1946 O  O   . GLY B 1 115 ? 34.412 -1.532  11.570  1.00 31.83 ? 114 GLY B O   1 
ATOM   1947 N  N   . ARG B 1 116 ? 35.109 -2.476  13.476  1.00 30.05 ? 115 ARG B N   1 
ATOM   1948 C  CA  . ARG B 1 116 ? 34.315 -1.582  14.298  1.00 32.20 ? 115 ARG B CA  1 
ATOM   1949 C  C   . ARG B 1 116 ? 35.300 -0.660  15.018  1.00 32.99 ? 115 ARG B C   1 
ATOM   1950 O  O   . ARG B 1 116 ? 36.501 -0.718  14.745  1.00 32.65 ? 115 ARG B O   1 
ATOM   1951 C  CB  . ARG B 1 116 ? 33.428 -2.397  15.252  1.00 35.31 ? 115 ARG B CB  1 
ATOM   1952 C  CG  . ARG B 1 116 ? 32.411 -3.248  14.463  1.00 35.71 ? 115 ARG B CG  1 
ATOM   1953 C  CD  . ARG B 1 116 ? 31.430 -3.999  15.341  1.00 38.56 ? 115 ARG B CD  1 
ATOM   1954 N  NE  . ARG B 1 116 ? 30.641 -4.960  14.571  1.00 39.13 ? 115 ARG B NE  1 
ATOM   1955 C  CZ  . ARG B 1 116 ? 29.660 -4.639  13.732  1.00 40.50 ? 115 ARG B CZ  1 
ATOM   1956 N  NH1 . ARG B 1 116 ? 29.008 -5.590  13.077  1.00 40.55 ? 115 ARG B NH1 1 
ATOM   1957 N  NH2 . ARG B 1 116 ? 29.320 -3.375  13.554  1.00 39.91 ? 115 ARG B NH2 1 
ATOM   1958 N  N   . THR B 1 117 ? 34.814 0.185   15.921  1.00 32.35 ? 116 THR B N   1 
ATOM   1959 C  CA  . THR B 1 117 ? 35.694 1.133   16.600  1.00 31.01 ? 116 THR B CA  1 
ATOM   1960 C  C   . THR B 1 117 ? 35.843 0.952   18.107  1.00 31.69 ? 116 THR B C   1 
ATOM   1961 O  O   . THR B 1 117 ? 34.864 0.709   18.820  1.00 31.85 ? 116 THR B O   1 
ATOM   1962 C  CB  . THR B 1 117 ? 35.218 2.579   16.350  1.00 30.51 ? 116 THR B CB  1 
ATOM   1963 O  OG1 . THR B 1 117 ? 35.207 2.848   14.940  1.00 31.74 ? 116 THR B OG1 1 
ATOM   1964 C  CG2 . THR B 1 117 ? 36.141 3.573   17.045  1.00 29.84 ? 116 THR B CG2 1 
ATOM   1965 N  N   . LEU B 1 118 ? 37.082 1.066   18.582  1.00 29.57 ? 117 LEU B N   1 
ATOM   1966 C  CA  . LEU B 1 118 ? 37.374 0.980   20.007  1.00 29.11 ? 117 LEU B CA  1 
ATOM   1967 C  C   . LEU B 1 118 ? 37.445 2.438   20.439  1.00 29.87 ? 117 LEU B C   1 
ATOM   1968 O  O   . LEU B 1 118 ? 38.117 3.242   19.794  1.00 30.77 ? 117 LEU B O   1 
ATOM   1969 C  CB  . LEU B 1 118 ? 38.719 0.294   20.251  1.00 28.93 ? 117 LEU B CB  1 
ATOM   1970 C  CG  . LEU B 1 118 ? 39.075 0.170   21.733  1.00 28.47 ? 117 LEU B CG  1 
ATOM   1971 C  CD1 . LEU B 1 118 ? 38.007 -0.670  22.430  1.00 29.20 ? 117 LEU B CD1 1 
ATOM   1972 C  CD2 . LEU B 1 118 ? 40.453 -0.441  21.894  1.00 24.26 ? 117 LEU B CD2 1 
ATOM   1973 N  N   . VAL B 1 119 ? 36.743 2.775   21.514  1.00 31.48 ? 118 VAL B N   1 
ATOM   1974 C  CA  . VAL B 1 119 ? 36.693 4.148   22.010  1.00 32.28 ? 118 VAL B CA  1 
ATOM   1975 C  C   . VAL B 1 119 ? 37.031 4.260   23.502  1.00 33.21 ? 118 VAL B C   1 
ATOM   1976 O  O   . VAL B 1 119 ? 36.640 3.406   24.299  1.00 33.30 ? 118 VAL B O   1 
ATOM   1977 C  CB  . VAL B 1 119 ? 35.272 4.758   21.805  1.00 31.22 ? 118 VAL B CB  1 
ATOM   1978 C  CG1 . VAL B 1 119 ? 35.250 6.204   22.283  1.00 31.17 ? 118 VAL B CG1 1 
ATOM   1979 C  CG2 . VAL B 1 119 ? 34.860 4.683   20.332  1.00 30.15 ? 118 VAL B CG2 1 
ATOM   1980 N  N   . VAL B 1 120 ? 37.763 5.313   23.866  1.00 33.46 ? 119 VAL B N   1 
ATOM   1981 C  CA  . VAL B 1 120 ? 38.096 5.564   25.263  1.00 34.94 ? 119 VAL B CA  1 
ATOM   1982 C  C   . VAL B 1 120 ? 37.505 6.941   25.591  1.00 35.77 ? 119 VAL B C   1 
ATOM   1983 O  O   . VAL B 1 120 ? 37.740 7.919   24.876  1.00 34.64 ? 119 VAL B O   1 
ATOM   1984 C  CB  . VAL B 1 120 ? 39.623 5.515   25.520  1.00 34.94 ? 119 VAL B CB  1 
ATOM   1985 C  CG1 . VAL B 1 120 ? 40.339 6.590   24.724  1.00 36.80 ? 119 VAL B CG1 1 
ATOM   1986 C  CG2 . VAL B 1 120 ? 39.889 5.654   27.014  1.00 37.08 ? 119 VAL B CG2 1 
ATOM   1987 N  N   . HIS B 1 121 ? 36.712 6.990   26.660  1.00 35.75 ? 120 HIS B N   1 
ATOM   1988 C  CA  . HIS B 1 121 ? 36.006 8.200   27.086  1.00 39.15 ? 120 HIS B CA  1 
ATOM   1989 C  C   . HIS B 1 121 ? 36.683 9.061   28.139  1.00 42.38 ? 120 HIS B C   1 
ATOM   1990 O  O   . HIS B 1 121 ? 37.557 8.606   28.869  1.00 43.57 ? 120 HIS B O   1 
ATOM   1991 C  CB  . HIS B 1 121 ? 34.616 7.820   27.603  1.00 36.15 ? 120 HIS B CB  1 
ATOM   1992 C  CG  . HIS B 1 121 ? 33.721 7.246   26.554  1.00 36.27 ? 120 HIS B CG  1 
ATOM   1993 N  ND1 . HIS B 1 121 ? 32.838 8.013   25.827  1.00 37.13 ? 120 HIS B ND1 1 
ATOM   1994 C  CD2 . HIS B 1 121 ? 33.603 5.984   26.078  1.00 34.62 ? 120 HIS B CD2 1 
ATOM   1995 C  CE1 . HIS B 1 121 ? 32.214 7.249   24.949  1.00 38.20 ? 120 HIS B CE1 1 
ATOM   1996 N  NE2 . HIS B 1 121 ? 32.660 6.014   25.081  1.00 34.96 ? 120 HIS B NE2 1 
ATOM   1997 N  N   . GLU B 1 122 ? 36.224 10.308  28.218  1.00 45.79 ? 121 GLU B N   1 
ATOM   1998 C  CA  . GLU B 1 122 ? 36.732 11.300  29.161  1.00 47.95 ? 121 GLU B CA  1 
ATOM   1999 C  C   . GLU B 1 122 ? 36.439 10.950  30.615  1.00 48.29 ? 121 GLU B C   1 
ATOM   2000 O  O   . GLU B 1 122 ? 37.299 11.112  31.477  1.00 50.41 ? 121 GLU B O   1 
ATOM   2001 C  CB  . GLU B 1 122 ? 36.123 12.667  28.846  1.00 50.36 ? 121 GLU B CB  1 
ATOM   2002 C  CG  . GLU B 1 122 ? 36.697 13.811  29.665  1.00 53.80 ? 121 GLU B CG  1 
ATOM   2003 C  CD  . GLU B 1 122 ? 36.045 15.140  29.343  1.00 56.31 ? 121 GLU B CD  1 
ATOM   2004 O  OE1 . GLU B 1 122 ? 36.558 16.182  29.812  1.00 57.98 ? 121 GLU B OE1 1 
ATOM   2005 O  OE2 . GLU B 1 122 ? 35.018 15.142  28.628  1.00 56.36 ? 121 GLU B OE2 1 
ATOM   2006 N  N   . LYS B 1 123 ? 35.228 10.471  30.888  1.00 47.64 ? 122 LYS B N   1 
ATOM   2007 C  CA  . LYS B 1 123 ? 34.844 10.117  32.250  1.00 48.62 ? 122 LYS B CA  1 
ATOM   2008 C  C   . LYS B 1 123 ? 34.594 8.624   32.441  1.00 47.42 ? 122 LYS B C   1 
ATOM   2009 O  O   . LYS B 1 123 ? 34.597 7.853   31.479  1.00 46.65 ? 122 LYS B O   1 
ATOM   2010 C  CB  . LYS B 1 123 ? 33.604 10.916  32.667  1.00 50.52 ? 122 LYS B CB  1 
ATOM   2011 C  CG  . LYS B 1 123 ? 33.856 12.421  32.761  1.00 53.21 ? 122 LYS B CG  1 
ATOM   2012 C  CD  . LYS B 1 123 ? 32.579 13.198  33.067  1.00 55.41 ? 122 LYS B CD  1 
ATOM   2013 C  CE  . LYS B 1 123 ? 32.055 12.925  34.474  1.00 56.35 ? 122 LYS B CE  1 
ATOM   2014 N  NZ  . LYS B 1 123 ? 32.945 13.479  35.537  1.00 58.50 ? 122 LYS B NZ  1 
ATOM   2015 N  N   . ALA B 1 124 ? 34.376 8.228   33.692  1.00 46.07 ? 123 ALA B N   1 
ATOM   2016 C  CA  . ALA B 1 124 ? 34.137 6.829   34.039  1.00 43.12 ? 123 ALA B CA  1 
ATOM   2017 C  C   . ALA B 1 124 ? 32.765 6.293   33.625  1.00 42.88 ? 123 ALA B C   1 
ATOM   2018 O  O   . ALA B 1 124 ? 31.780 7.028   33.553  1.00 41.49 ? 123 ALA B O   1 
ATOM   2019 C  CB  . ALA B 1 124 ? 34.334 6.631   35.536  1.00 44.69 ? 123 ALA B CB  1 
ATOM   2020 N  N   . ASP B 1 125 ? 32.725 4.991   33.355  1.00 41.00 ? 124 ASP B N   1 
ATOM   2021 C  CA  . ASP B 1 125 ? 31.516 4.283   32.951  1.00 42.04 ? 124 ASP B CA  1 
ATOM   2022 C  C   . ASP B 1 125 ? 30.821 3.745   34.212  1.00 42.85 ? 124 ASP B C   1 
ATOM   2023 O  O   . ASP B 1 125 ? 31.422 2.995   34.976  1.00 41.67 ? 124 ASP B O   1 
ATOM   2024 C  CB  . ASP B 1 125 ? 31.915 3.132   32.011  1.00 40.72 ? 124 ASP B CB  1 
ATOM   2025 C  CG  . ASP B 1 125 ? 30.725 2.340   31.493  1.00 42.07 ? 124 ASP B CG  1 
ATOM   2026 O  OD1 . ASP B 1 125 ? 30.893 1.623   30.479  1.00 41.06 ? 124 ASP B OD1 1 
ATOM   2027 O  OD2 . ASP B 1 125 ? 29.635 2.415   32.092  1.00 37.39 ? 124 ASP B OD2 1 
ATOM   2028 N  N   . ASP B 1 126 ? 29.558 4.118   34.427  1.00 44.36 ? 125 ASP B N   1 
ATOM   2029 C  CA  . ASP B 1 126 ? 28.835 3.667   35.621  1.00 45.47 ? 125 ASP B CA  1 
ATOM   2030 C  C   . ASP B 1 126 ? 28.243 2.267   35.514  1.00 46.56 ? 125 ASP B C   1 
ATOM   2031 O  O   . ASP B 1 126 ? 27.378 1.881   36.305  1.00 46.71 ? 125 ASP B O   1 
ATOM   2032 C  CB  . ASP B 1 126 ? 27.745 4.680   36.013  1.00 44.49 ? 125 ASP B CB  1 
ATOM   2033 C  CG  . ASP B 1 126 ? 26.585 4.732   35.030  1.00 45.56 ? 125 ASP B CG  1 
ATOM   2034 O  OD1 . ASP B 1 126 ? 25.875 5.764   35.031  1.00 43.59 ? 125 ASP B OD1 1 
ATOM   2035 O  OD2 . ASP B 1 126 ? 26.360 3.756   34.278  1.00 43.47 ? 125 ASP B OD2 1 
ATOM   2036 N  N   . LEU B 1 127 ? 28.721 1.514   34.529  1.00 47.04 ? 126 LEU B N   1 
ATOM   2037 C  CA  . LEU B 1 127 ? 28.295 0.138   34.306  1.00 47.75 ? 126 LEU B CA  1 
ATOM   2038 C  C   . LEU B 1 127 ? 26.797 -0.098  34.112  1.00 46.92 ? 126 LEU B C   1 
ATOM   2039 O  O   . LEU B 1 127 ? 26.338 -1.238  34.157  1.00 47.91 ? 126 LEU B O   1 
ATOM   2040 C  CB  . LEU B 1 127 ? 28.804 -0.748  35.448  1.00 48.80 ? 126 LEU B CB  1 
ATOM   2041 C  CG  . LEU B 1 127 ? 30.320 -0.917  35.577  1.00 50.03 ? 126 LEU B CG  1 
ATOM   2042 C  CD1 . LEU B 1 127 ? 30.947 0.351   36.124  1.00 51.33 ? 126 LEU B CD1 1 
ATOM   2043 C  CD2 . LEU B 1 127 ? 30.622 -2.085  36.498  1.00 50.63 ? 126 LEU B CD2 1 
ATOM   2044 N  N   . GLY B 1 128 ? 26.035 0.966   33.896  1.00 45.81 ? 127 GLY B N   1 
ATOM   2045 C  CA  . GLY B 1 128 ? 24.607 0.806   33.685  1.00 45.21 ? 127 GLY B CA  1 
ATOM   2046 C  C   . GLY B 1 128 ? 23.767 0.643   34.941  1.00 45.12 ? 127 GLY B C   1 
ATOM   2047 O  O   . GLY B 1 128 ? 22.635 0.160   34.873  1.00 43.37 ? 127 GLY B O   1 
ATOM   2048 N  N   . LYS B 1 129 ? 24.314 1.047   36.084  1.00 45.66 ? 128 LYS B N   1 
ATOM   2049 C  CA  . LYS B 1 129 ? 23.603 0.954   37.357  1.00 46.77 ? 128 LYS B CA  1 
ATOM   2050 C  C   . LYS B 1 129 ? 23.081 2.315   37.819  1.00 46.41 ? 128 LYS B C   1 
ATOM   2051 O  O   . LYS B 1 129 ? 22.572 2.442   38.935  1.00 45.92 ? 128 LYS B O   1 
ATOM   2052 C  CB  . LYS B 1 129 ? 24.519 0.389   38.451  1.00 47.72 ? 128 LYS B CB  1 
ATOM   2053 C  CG  . LYS B 1 129 ? 24.791 -1.109  38.375  1.00 49.98 ? 128 LYS B CG  1 
ATOM   2054 C  CD  . LYS B 1 129 ? 25.686 -1.470  37.208  1.00 54.53 ? 128 LYS B CD  1 
ATOM   2055 C  CE  . LYS B 1 129 ? 26.094 -2.943  37.243  1.00 54.58 ? 128 LYS B CE  1 
ATOM   2056 N  NZ  . LYS B 1 129 ? 24.933 -3.867  37.084  1.00 56.00 ? 128 LYS B NZ  1 
ATOM   2057 N  N   . GLY B 1 130 ? 23.212 3.327   36.968  1.00 45.16 ? 129 GLY B N   1 
ATOM   2058 C  CA  . GLY B 1 130 ? 22.760 4.660   37.329  1.00 44.19 ? 129 GLY B CA  1 
ATOM   2059 C  C   . GLY B 1 130 ? 21.252 4.814   37.371  1.00 42.25 ? 129 GLY B C   1 
ATOM   2060 O  O   . GLY B 1 130 ? 20.528 4.125   36.652  1.00 40.80 ? 129 GLY B O   1 
ATOM   2061 N  N   . GLY B 1 131 ? 20.779 5.727   38.214  1.00 42.43 ? 130 GLY B N   1 
ATOM   2062 C  CA  . GLY B 1 131 ? 19.351 5.958   38.332  1.00 39.75 ? 130 GLY B CA  1 
ATOM   2063 C  C   . GLY B 1 131 ? 18.850 6.892   37.251  1.00 39.87 ? 130 GLY B C   1 
ATOM   2064 O  O   . GLY B 1 131 ? 18.238 7.922   37.532  1.00 39.61 ? 130 GLY B O   1 
ATOM   2065 N  N   . ASN B 1 132 ? 19.118 6.535   36.003  1.00 38.21 ? 131 ASN B N   1 
ATOM   2066 C  CA  . ASN B 1 132 ? 18.693 7.341   34.870  1.00 39.22 ? 131 ASN B CA  1 
ATOM   2067 C  C   . ASN B 1 132 ? 18.775 6.491   33.619  1.00 38.76 ? 131 ASN B C   1 
ATOM   2068 O  O   . ASN B 1 132 ? 19.538 5.526   33.567  1.00 38.92 ? 131 ASN B O   1 
ATOM   2069 C  CB  . ASN B 1 132 ? 19.573 8.596   34.744  1.00 40.92 ? 131 ASN B CB  1 
ATOM   2070 C  CG  . ASN B 1 132 ? 21.055 8.276   34.680  1.00 40.83 ? 131 ASN B CG  1 
ATOM   2071 O  OD1 . ASN B 1 132 ? 21.564 7.832   33.653  1.00 39.61 ? 131 ASN B OD1 1 
ATOM   2072 N  ND2 . ASN B 1 132 ? 21.754 8.499   35.786  1.00 40.08 ? 131 ASN B ND2 1 
ATOM   2073 N  N   . GLU B 1 133 ? 17.981 6.835   32.615  1.00 38.67 ? 132 GLU B N   1 
ATOM   2074 C  CA  . GLU B 1 133 ? 17.978 6.062   31.386  1.00 40.83 ? 132 GLU B CA  1 
ATOM   2075 C  C   . GLU B 1 133 ? 19.306 6.121   30.647  1.00 42.71 ? 132 GLU B C   1 
ATOM   2076 O  O   . GLU B 1 133 ? 19.742 5.129   30.071  1.00 43.10 ? 132 GLU B O   1 
ATOM   2077 C  CB  . GLU B 1 133 ? 16.851 6.524   30.465  1.00 40.89 ? 132 GLU B CB  1 
ATOM   2078 C  CG  . GLU B 1 133 ? 16.697 5.644   29.229  1.00 44.84 ? 132 GLU B CG  1 
ATOM   2079 C  CD  . GLU B 1 133 ? 15.463 5.975   28.430  1.00 46.10 ? 132 GLU B CD  1 
ATOM   2080 O  OE1 . GLU B 1 133 ? 15.325 7.139   28.002  1.00 47.77 ? 132 GLU B OE1 1 
ATOM   2081 O  OE2 . GLU B 1 133 ? 14.626 5.070   28.233  1.00 49.57 ? 132 GLU B OE2 1 
ATOM   2082 N  N   . GLU B 1 134 ? 19.956 7.280   30.673  1.00 43.26 ? 133 GLU B N   1 
ATOM   2083 C  CA  . GLU B 1 134 ? 21.234 7.437   29.990  1.00 43.25 ? 133 GLU B CA  1 
ATOM   2084 C  C   . GLU B 1 134 ? 22.251 6.387   30.441  1.00 42.17 ? 133 GLU B C   1 
ATOM   2085 O  O   . GLU B 1 134 ? 23.052 5.906   29.646  1.00 39.59 ? 133 GLU B O   1 
ATOM   2086 C  CB  . GLU B 1 134 ? 21.803 8.834   30.236  1.00 44.80 ? 133 GLU B CB  1 
ATOM   2087 C  CG  . GLU B 1 134 ? 23.069 9.114   29.445  1.00 47.48 ? 133 GLU B CG  1 
ATOM   2088 C  CD  . GLU B 1 134 ? 22.830 9.096   27.953  1.00 49.74 ? 133 GLU B CD  1 
ATOM   2089 O  OE1 . GLU B 1 134 ? 23.816 8.996   27.196  1.00 53.41 ? 133 GLU B OE1 1 
ATOM   2090 O  OE2 . GLU B 1 134 ? 21.656 9.186   27.529  1.00 51.89 ? 133 GLU B OE2 1 
ATOM   2091 N  N   . SER B 1 135 ? 22.216 6.037   31.720  1.00 41.42 ? 134 SER B N   1 
ATOM   2092 C  CA  . SER B 1 135 ? 23.140 5.048   32.258  1.00 40.79 ? 134 SER B CA  1 
ATOM   2093 C  C   . SER B 1 135 ? 22.975 3.708   31.554  1.00 40.39 ? 134 SER B C   1 
ATOM   2094 O  O   . SER B 1 135 ? 23.933 2.948   31.406  1.00 41.16 ? 134 SER B O   1 
ATOM   2095 C  CB  . SER B 1 135 ? 22.900 4.871   33.760  1.00 40.99 ? 134 SER B CB  1 
ATOM   2096 O  OG  . SER B 1 135 ? 23.696 3.828   34.301  1.00 39.59 ? 134 SER B OG  1 
ATOM   2097 N  N   . THR B 1 136 ? 21.758 3.429   31.107  1.00 39.52 ? 135 THR B N   1 
ATOM   2098 C  CA  . THR B 1 136 ? 21.466 2.163   30.449  1.00 38.67 ? 135 THR B CA  1 
ATOM   2099 C  C   . THR B 1 136 ? 21.780 2.193   28.965  1.00 39.16 ? 135 THR B C   1 
ATOM   2100 O  O   . THR B 1 136 ? 21.571 1.206   28.250  1.00 37.27 ? 135 THR B O   1 
ATOM   2101 C  CB  . THR B 1 136 ? 19.992 1.783   30.626  1.00 37.75 ? 135 THR B CB  1 
ATOM   2102 O  OG1 . THR B 1 136 ? 19.182 2.600   29.777  1.00 36.61 ? 135 THR B OG1 1 
ATOM   2103 C  CG2 . THR B 1 136 ? 19.572 1.991   32.068  1.00 37.90 ? 135 THR B CG2 1 
ATOM   2104 N  N   . LYS B 1 137 ? 22.283 3.331   28.503  1.00 39.41 ? 136 LYS B N   1 
ATOM   2105 C  CA  . LYS B 1 137 ? 22.625 3.474   27.099  1.00 39.47 ? 136 LYS B CA  1 
ATOM   2106 C  C   . LYS B 1 137 ? 24.117 3.683   26.906  1.00 38.50 ? 136 LYS B C   1 
ATOM   2107 O  O   . LYS B 1 137 ? 24.744 3.001   26.091  1.00 38.39 ? 136 LYS B O   1 
ATOM   2108 C  CB  . LYS B 1 137 ? 21.866 4.647   26.476  1.00 42.13 ? 136 LYS B CB  1 
ATOM   2109 C  CG  . LYS B 1 137 ? 20.353 4.568   26.636  1.00 46.64 ? 136 LYS B CG  1 
ATOM   2110 C  CD  . LYS B 1 137 ? 19.643 5.636   25.815  1.00 51.00 ? 136 LYS B CD  1 
ATOM   2111 C  CE  . LYS B 1 137 ? 20.123 7.031   26.186  1.00 55.97 ? 136 LYS B CE  1 
ATOM   2112 N  NZ  . LYS B 1 137 ? 19.464 8.101   25.376  1.00 58.89 ? 136 LYS B NZ  1 
ATOM   2113 N  N   . THR B 1 138 ? 24.689 4.603   27.674  1.00 36.20 ? 137 THR B N   1 
ATOM   2114 C  CA  . THR B 1 138 ? 26.103 4.921   27.536  1.00 35.47 ? 137 THR B CA  1 
ATOM   2115 C  C   . THR B 1 138 ? 26.923 4.771   28.798  1.00 35.06 ? 137 THR B C   1 
ATOM   2116 O  O   . THR B 1 138 ? 28.151 4.764   28.743  1.00 35.64 ? 137 THR B O   1 
ATOM   2117 C  CB  . THR B 1 138 ? 26.288 6.369   27.058  1.00 37.59 ? 137 THR B CB  1 
ATOM   2118 O  OG1 . THR B 1 138 ? 25.848 7.270   28.084  1.00 36.73 ? 137 THR B OG1 1 
ATOM   2119 C  CG2 . THR B 1 138 ? 25.474 6.622   25.796  1.00 36.49 ? 137 THR B CG2 1 
ATOM   2120 N  N   . GLY B 1 139 ? 26.256 4.660   29.939  1.00 35.52 ? 138 GLY B N   1 
ATOM   2121 C  CA  . GLY B 1 139 ? 26.989 4.550   31.187  1.00 34.53 ? 138 GLY B CA  1 
ATOM   2122 C  C   . GLY B 1 139 ? 27.488 5.917   31.647  1.00 34.37 ? 138 GLY B C   1 
ATOM   2123 O  O   . GLY B 1 139 ? 28.290 6.009   32.557  1.00 35.23 ? 138 GLY B O   1 
ATOM   2124 N  N   . ASN B 1 140 ? 27.017 6.981   31.003  1.00 36.62 ? 139 ASN B N   1 
ATOM   2125 C  CA  . ASN B 1 140 ? 27.409 8.349   31.362  1.00 36.61 ? 139 ASN B CA  1 
ATOM   2126 C  C   . ASN B 1 140 ? 28.921 8.574   31.379  1.00 36.23 ? 139 ASN B C   1 
ATOM   2127 O  O   . ASN B 1 140 ? 29.420 9.344   32.194  1.00 35.94 ? 139 ASN B O   1 
ATOM   2128 C  CB  . ASN B 1 140 ? 26.844 8.713   32.737  1.00 36.79 ? 139 ASN B CB  1 
ATOM   2129 C  CG  . ASN B 1 140 ? 25.335 8.829   32.742  1.00 38.13 ? 139 ASN B CG  1 
ATOM   2130 O  OD1 . ASN B 1 140 ? 24.767 9.699   32.088  1.00 39.92 ? 139 ASN B OD1 1 
ATOM   2131 N  ND2 . ASN B 1 140 ? 24.675 7.950   33.485  1.00 37.79 ? 139 ASN B ND2 1 
ATOM   2132 N  N   . ALA B 1 141 ? 29.639 7.918   30.471  1.00 35.40 ? 140 ALA B N   1 
ATOM   2133 C  CA  . ALA B 1 141 ? 31.096 8.030   30.400  1.00 36.08 ? 140 ALA B CA  1 
ATOM   2134 C  C   . ALA B 1 141 ? 31.570 9.312   29.711  1.00 37.69 ? 140 ALA B C   1 
ATOM   2135 O  O   . ALA B 1 141 ? 32.767 9.603   29.675  1.00 38.90 ? 140 ALA B O   1 
ATOM   2136 C  CB  . ALA B 1 141 ? 31.677 6.802   29.688  1.00 33.06 ? 140 ALA B CB  1 
ATOM   2137 N  N   . GLY B 1 142 ? 30.636 10.070  29.149  1.00 39.75 ? 141 GLY B N   1 
ATOM   2138 C  CA  . GLY B 1 142 ? 31.005 11.318  28.505  1.00 40.75 ? 141 GLY B CA  1 
ATOM   2139 C  C   . GLY B 1 142 ? 31.573 11.257  27.097  1.00 42.34 ? 141 GLY B C   1 
ATOM   2140 O  O   . GLY B 1 142 ? 31.360 10.295  26.348  1.00 42.27 ? 141 GLY B O   1 
ATOM   2141 N  N   . SER B 1 143 ? 32.320 12.296  26.737  1.00 41.26 ? 142 SER B N   1 
ATOM   2142 C  CA  . SER B 1 143 ? 32.880 12.390  25.401  1.00 41.73 ? 142 SER B CA  1 
ATOM   2143 C  C   . SER B 1 143 ? 33.980 11.391  25.083  1.00 40.23 ? 142 SER B C   1 
ATOM   2144 O  O   . SER B 1 143 ? 34.642 10.839  25.966  1.00 39.19 ? 142 SER B O   1 
ATOM   2145 C  CB  . SER B 1 143 ? 33.386 13.813  25.132  1.00 42.39 ? 142 SER B CB  1 
ATOM   2146 O  OG  . SER B 1 143 ? 34.572 14.065  25.856  1.00 45.55 ? 142 SER B OG  1 
ATOM   2147 N  N   . ARG B 1 144 ? 34.170 11.189  23.789  1.00 40.59 ? 143 ARG B N   1 
ATOM   2148 C  CA  . ARG B 1 144 ? 35.156 10.261  23.272  1.00 41.28 ? 143 ARG B CA  1 
ATOM   2149 C  C   . ARG B 1 144 ? 36.467 10.998  23.014  1.00 41.19 ? 143 ARG B C   1 
ATOM   2150 O  O   . ARG B 1 144 ? 36.542 11.864  22.143  1.00 43.22 ? 143 ARG B O   1 
ATOM   2151 C  CB  . ARG B 1 144 ? 34.593 9.644   21.995  1.00 40.11 ? 143 ARG B CB  1 
ATOM   2152 C  CG  . ARG B 1 144 ? 33.117 9.326   22.151  1.00 41.27 ? 143 ARG B CG  1 
ATOM   2153 C  CD  . ARG B 1 144 ? 32.478 8.714   20.918  1.00 38.33 ? 143 ARG B CD  1 
ATOM   2154 N  NE  . ARG B 1 144 ? 31.040 8.562   21.127  1.00 37.74 ? 143 ARG B NE  1 
ATOM   2155 C  CZ  . ARG B 1 144 ? 30.218 7.924   20.302  1.00 40.44 ? 143 ARG B CZ  1 
ATOM   2156 N  NH1 . ARG B 1 144 ? 28.922 7.844   20.585  1.00 39.34 ? 143 ARG B NH1 1 
ATOM   2157 N  NH2 . ARG B 1 144 ? 30.689 7.361   19.197  1.00 37.61 ? 143 ARG B NH2 1 
ATOM   2158 N  N   . LEU B 1 145 ? 37.496 10.645  23.776  1.00 41.36 ? 144 LEU B N   1 
ATOM   2159 C  CA  . LEU B 1 145 ? 38.801 11.290  23.664  1.00 41.37 ? 144 LEU B CA  1 
ATOM   2160 C  C   . LEU B 1 145 ? 39.644 10.729  22.533  1.00 41.04 ? 144 LEU B C   1 
ATOM   2161 O  O   . LEU B 1 145 ? 40.293 11.479  21.803  1.00 40.03 ? 144 LEU B O   1 
ATOM   2162 C  CB  . LEU B 1 145 ? 39.569 11.152  24.984  1.00 43.01 ? 144 LEU B CB  1 
ATOM   2163 C  CG  . LEU B 1 145 ? 38.889 11.701  26.243  1.00 44.14 ? 144 LEU B CG  1 
ATOM   2164 C  CD1 . LEU B 1 145 ? 39.781 11.456  27.445  1.00 44.92 ? 144 LEU B CD1 1 
ATOM   2165 C  CD2 . LEU B 1 145 ? 38.614 13.188  26.084  1.00 46.45 ? 144 LEU B CD2 1 
ATOM   2166 N  N   . ALA B 1 146 ? 39.642 9.408   22.401  1.00 38.39 ? 145 ALA B N   1 
ATOM   2167 C  CA  . ALA B 1 146 ? 40.408 8.752   21.356  1.00 38.75 ? 145 ALA B CA  1 
ATOM   2168 C  C   . ALA B 1 146 ? 39.670 7.510   20.863  1.00 37.99 ? 145 ALA B C   1 
ATOM   2169 O  O   . ALA B 1 146 ? 38.874 6.924   21.591  1.00 36.00 ? 145 ALA B O   1 
ATOM   2170 C  CB  . ALA B 1 146 ? 41.788 8.367   21.886  1.00 37.24 ? 145 ALA B CB  1 
ATOM   2171 N  N   . CYS B 1 147 ? 39.943 7.112   19.627  1.00 38.37 ? 146 CYS B N   1 
ATOM   2172 C  CA  . CYS B 1 147 ? 39.312 5.933   19.045  1.00 37.60 ? 146 CYS B CA  1 
ATOM   2173 C  C   . CYS B 1 147 ? 40.134 5.427   17.870  1.00 37.42 ? 146 CYS B C   1 
ATOM   2174 O  O   . CYS B 1 147 ? 41.011 6.130   17.354  1.00 35.72 ? 146 CYS B O   1 
ATOM   2175 C  CB  . CYS B 1 147 ? 37.891 6.257   18.576  1.00 38.33 ? 146 CYS B CB  1 
ATOM   2176 S  SG  . CYS B 1 147 ? 37.813 7.621   17.378  1.00 40.89 ? 146 CYS B SG  1 
ATOM   2177 N  N   . GLY B 1 148 ? 39.847 4.199   17.458  1.00 34.79 ? 147 GLY B N   1 
ATOM   2178 C  CA  . GLY B 1 148 ? 40.548 3.606   16.341  1.00 32.41 ? 147 GLY B CA  1 
ATOM   2179 C  C   . GLY B 1 148 ? 39.770 2.430   15.792  1.00 32.42 ? 147 GLY B C   1 
ATOM   2180 O  O   . GLY B 1 148 ? 39.100 1.707   16.541  1.00 30.77 ? 147 GLY B O   1 
ATOM   2181 N  N   . VAL B 1 149 ? 39.844 2.242   14.479  1.00 30.99 ? 148 VAL B N   1 
ATOM   2182 C  CA  . VAL B 1 149 ? 39.155 1.138   13.845  1.00 30.11 ? 148 VAL B CA  1 
ATOM   2183 C  C   . VAL B 1 149 ? 39.932 -0.141  14.131  1.00 29.02 ? 148 VAL B C   1 
ATOM   2184 O  O   . VAL B 1 149 ? 41.162 -0.183  14.037  1.00 28.36 ? 148 VAL B O   1 
ATOM   2185 C  CB  . VAL B 1 149 ? 39.032 1.361   12.317  1.00 30.63 ? 148 VAL B CB  1 
ATOM   2186 C  CG1 . VAL B 1 149 ? 38.255 0.214   11.680  1.00 28.58 ? 148 VAL B CG1 1 
ATOM   2187 C  CG2 . VAL B 1 149 ? 38.320 2.693   12.046  1.00 29.60 ? 148 VAL B CG2 1 
ATOM   2188 N  N   . ILE B 1 150 ? 39.193 -1.180  14.487  1.00 30.01 ? 149 ILE B N   1 
ATOM   2189 C  CA  . ILE B 1 150 ? 39.759 -2.484  14.815  1.00 30.88 ? 149 ILE B CA  1 
ATOM   2190 C  C   . ILE B 1 150 ? 40.122 -3.276  13.561  1.00 31.26 ? 149 ILE B C   1 
ATOM   2191 O  O   . ILE B 1 150 ? 39.246 -3.804  12.884  1.00 32.78 ? 149 ILE B O   1 
ATOM   2192 C  CB  . ILE B 1 150 ? 38.741 -3.264  15.659  1.00 29.57 ? 149 ILE B CB  1 
ATOM   2193 C  CG1 . ILE B 1 150 ? 38.426 -2.456  16.918  1.00 26.39 ? 149 ILE B CG1 1 
ATOM   2194 C  CG2 . ILE B 1 150 ? 39.269 -4.662  15.975  1.00 29.87 ? 149 ILE B CG2 1 
ATOM   2195 C  CD1 . ILE B 1 150 ? 37.249 -2.994  17.724  1.00 32.30 ? 149 ILE B CD1 1 
ATOM   2196 N  N   . GLY B 1 151 ? 41.415 -3.373  13.259  1.00 31.46 ? 150 GLY B N   1 
ATOM   2197 C  CA  . GLY B 1 151 ? 41.830 -4.080  12.058  1.00 30.77 ? 150 GLY B CA  1 
ATOM   2198 C  C   . GLY B 1 151 ? 42.641 -5.349  12.256  1.00 33.42 ? 150 GLY B C   1 
ATOM   2199 O  O   . GLY B 1 151 ? 43.234 -5.570  13.311  1.00 32.83 ? 150 GLY B O   1 
ATOM   2200 N  N   . ILE B 1 152 ? 42.666 -6.178  11.218  1.00 31.70 ? 151 ILE B N   1 
ATOM   2201 C  CA  . ILE B 1 152 ? 43.385 -7.442  11.232  1.00 32.82 ? 151 ILE B CA  1 
ATOM   2202 C  C   . ILE B 1 152 ? 44.879 -7.175  11.331  1.00 33.85 ? 151 ILE B C   1 
ATOM   2203 O  O   . ILE B 1 152 ? 45.433 -6.396  10.556  1.00 32.60 ? 151 ILE B O   1 
ATOM   2204 C  CB  . ILE B 1 152 ? 43.048 -8.259  9.958   1.00 33.15 ? 151 ILE B CB  1 
ATOM   2205 C  CG1 . ILE B 1 152 ? 41.527 -8.484  9.901   1.00 32.43 ? 151 ILE B CG1 1 
ATOM   2206 C  CG2 . ILE B 1 152 ? 43.793 -9.600  9.966   1.00 32.44 ? 151 ILE B CG2 1 
ATOM   2207 C  CD1 . ILE B 1 152 ? 41.025 -9.199  8.647   1.00 30.19 ? 151 ILE B CD1 1 
ATOM   2208 N  N   . ALA B 1 153 ? 45.525 -7.825  12.298  1.00 35.65 ? 152 ALA B N   1 
ATOM   2209 C  CA  . ALA B 1 153 ? 46.947 -7.623  12.535  1.00 35.41 ? 152 ALA B CA  1 
ATOM   2210 C  C   . ALA B 1 153 ? 47.813 -8.828  12.226  1.00 37.45 ? 152 ALA B C   1 
ATOM   2211 O  O   . ALA B 1 153 ? 49.037 -8.730  12.272  1.00 35.89 ? 152 ALA B O   1 
ATOM   2212 C  CB  . ALA B 1 153 ? 47.169 -7.192  13.985  1.00 34.76 ? 152 ALA B CB  1 
ATOM   2213 N  N   . GLN B 1 154 ? 47.201 -9.968  11.930  1.00 40.79 ? 153 GLN B N   1 
ATOM   2214 C  CA  . GLN B 1 154 ? 47.992 -11.153 11.612  1.00 45.80 ? 153 GLN B CA  1 
ATOM   2215 C  C   . GLN B 1 154 ? 47.280 -12.140 10.686  1.00 47.57 ? 153 GLN B C   1 
ATOM   2216 O  O   . GLN B 1 154 ? 47.381 -13.376 10.856  1.00 43.34 ? 153 GLN B O   1 
ATOM   2217 C  CB  . GLN B 1 154 ? 48.398 -11.869 12.900  1.00 48.43 ? 153 GLN B CB  1 
ATOM   2218 C  CG  . GLN B 1 154 ? 49.385 -13.009 12.687  1.00 53.41 ? 153 GLN B CG  1 
ATOM   2219 C  CD  . GLN B 1 154 ? 49.688 -13.766 13.970  1.00 56.10 ? 153 GLN B CD  1 
ATOM   2220 O  OE1 . GLN B 1 154 ? 50.532 -14.657 13.990  1.00 57.69 ? 153 GLN B OE1 1 
ATOM   2221 N  NE2 . GLN B 1 154 ? 48.995 -13.412 15.047  1.00 58.33 ? 153 GLN B NE2 1 
ATOM   2222 O  OXT . GLN B 1 154 ? 46.597 -11.657 9.760   1.00 43.34 ? 153 GLN B OXT 1 
HETATM 2223 CU CU  . CU1 C 2 .   ? 49.016 -0.623  -2.387  1.00 38.19 ? 154 CU1 A CU  1 
HETATM 2224 ZN ZN  . ZN  D 3 .   ? 48.833 -6.464  -6.069  1.00 35.95 ? 155 ZN  A ZN  1 
HETATM 2225 CU CU  . CU1 E 2 .   ? 32.204 4.142   24.279  1.00 41.51 ? 154 CU1 B CU  1 
HETATM 2226 ZN ZN  . ZN  F 3 .   ? 27.210 -0.177  26.352  1.00 34.27 ? 155 ZN  B ZN  1 
HETATM 2227 S  S   . SO4 G 4 .   ? 27.415 -16.571 15.424  1.00 51.95 ? 300 SO4 B S   1 
HETATM 2228 O  O1  . SO4 G 4 .   ? 28.697 -16.291 16.097  1.00 49.53 ? 300 SO4 B O1  1 
HETATM 2229 O  O2  . SO4 G 4 .   ? 26.319 -16.524 16.412  1.00 51.78 ? 300 SO4 B O2  1 
HETATM 2230 O  O3  . SO4 G 4 .   ? 27.477 -17.910 14.806  1.00 53.30 ? 300 SO4 B O3  1 
HETATM 2231 O  O4  . SO4 G 4 .   ? 27.154 -15.568 14.375  1.00 50.43 ? 300 SO4 B O4  1 
HETATM 2232 O  O   . HOH H 5 .   ? 42.165 4.054   9.855   1.00 31.22 ? 156 HOH A O   1 
HETATM 2233 O  O   . HOH H 5 .   ? 45.269 -11.989 6.482   1.00 40.88 ? 157 HOH A O   1 
HETATM 2234 O  O   . HOH H 5 .   ? 53.230 -1.936  -1.931  1.00 40.18 ? 158 HOH A O   1 
HETATM 2235 O  O   . HOH H 5 .   ? 43.600 -13.171 8.122   1.00 54.45 ? 159 HOH A O   1 
HETATM 2236 O  O   . HOH H 5 .   ? 64.457 -5.381  -15.593 1.00 38.03 ? 160 HOH A O   1 
HETATM 2237 O  O   . HOH H 5 .   ? 56.196 -0.524  -5.317  1.00 36.69 ? 161 HOH A O   1 
HETATM 2238 O  O   . HOH H 5 .   ? 62.260 6.913   -7.193  1.00 52.34 ? 162 HOH A O   1 
HETATM 2239 O  O   . HOH H 5 .   ? 52.241 -5.675  9.645   1.00 30.89 ? 163 HOH A O   1 
HETATM 2240 O  O   . HOH H 5 .   ? 50.449 12.661  -5.008  1.00 50.08 ? 164 HOH A O   1 
HETATM 2241 O  O   . HOH H 5 .   ? 37.271 -9.289  7.800   1.00 50.08 ? 165 HOH A O   1 
HETATM 2242 O  O   . HOH H 5 .   ? 39.106 -10.968 -12.185 1.00 48.44 ? 166 HOH A O   1 
HETATM 2243 O  O   . HOH H 5 .   ? 50.617 -6.574  11.680  1.00 35.23 ? 167 HOH A O   1 
HETATM 2244 O  O   . HOH H 5 .   ? 40.005 0.641   -10.868 1.00 41.55 ? 168 HOH A O   1 
HETATM 2245 O  O   . HOH H 5 .   ? 59.632 -7.102  -3.599  1.00 44.28 ? 169 HOH A O   1 
HETATM 2246 O  O   . HOH H 5 .   ? 44.739 -13.277 -3.718  1.00 38.41 ? 170 HOH A O   1 
HETATM 2247 O  O   . HOH H 5 .   ? 61.229 -7.153  -7.247  1.00 30.53 ? 171 HOH A O   1 
HETATM 2248 O  O   . HOH H 5 .   ? 45.375 -0.505  13.259  1.00 31.98 ? 172 HOH A O   1 
HETATM 2249 O  O   . HOH H 5 .   ? 28.372 5.161   9.684   1.00 57.92 ? 173 HOH A O   1 
HETATM 2250 O  O   . HOH H 5 .   ? 53.235 -4.246  -0.947  1.00 40.55 ? 174 HOH A O   1 
HETATM 2251 O  O   . HOH H 5 .   ? 26.393 -6.580  -4.896  1.00 44.46 ? 175 HOH A O   1 
HETATM 2252 O  O   . HOH H 5 .   ? 48.602 0.747   8.014   1.00 36.72 ? 176 HOH A O   1 
HETATM 2253 O  O   . HOH H 5 .   ? 55.847 4.049   1.973   1.00 45.64 ? 177 HOH A O   1 
HETATM 2254 O  O   . HOH H 5 .   ? 43.028 -3.782  -15.309 1.00 42.83 ? 178 HOH A O   1 
HETATM 2255 O  O   . HOH H 5 .   ? 45.010 1.895   -14.979 1.00 43.80 ? 179 HOH A O   1 
HETATM 2256 O  O   . HOH H 5 .   ? 39.157 -11.970 4.690   1.00 44.58 ? 180 HOH A O   1 
HETATM 2257 O  O   . HOH H 5 .   ? 38.544 -11.766 8.424   1.00 52.08 ? 181 HOH A O   1 
HETATM 2258 O  O   . HOH H 5 .   ? 52.345 -6.815  -2.408  1.00 40.09 ? 182 HOH A O   1 
HETATM 2259 O  O   . HOH H 5 .   ? 60.276 5.528   -6.936  1.00 58.85 ? 183 HOH A O   1 
HETATM 2260 O  O   . HOH H 5 .   ? 46.123 6.369   8.766   1.00 39.82 ? 184 HOH A O   1 
HETATM 2261 O  O   . HOH H 5 .   ? 46.108 -3.123  -9.600  1.00 46.87 ? 185 HOH A O   1 
HETATM 2262 O  O   . HOH H 5 .   ? 50.781 14.586  -2.956  1.00 54.53 ? 186 HOH A O   1 
HETATM 2263 O  O   . HOH H 5 .   ? 42.758 -17.651 -8.708  1.00 50.77 ? 187 HOH A O   1 
HETATM 2264 O  O   . HOH H 5 .   ? 50.074 12.431  2.289   1.00 53.63 ? 188 HOH A O   1 
HETATM 2265 O  O   . HOH H 5 .   ? 54.653 -4.870  1.974   1.00 45.57 ? 189 HOH A O   1 
HETATM 2266 O  O   . HOH H 5 .   ? 26.819 -1.851  6.976   1.00 48.95 ? 190 HOH A O   1 
HETATM 2267 O  O   . HOH H 5 .   ? 54.304 0.188   -3.164  1.00 35.74 ? 191 HOH A O   1 
HETATM 2268 O  O   . HOH H 5 .   ? 42.573 -17.888 2.724   1.00 54.70 ? 192 HOH A O   1 
HETATM 2269 O  O   . HOH H 5 .   ? 38.170 -1.229  -12.035 1.00 50.97 ? 193 HOH A O   1 
HETATM 2270 O  O   . HOH H 5 .   ? 60.700 -9.691  -6.282  1.00 41.08 ? 194 HOH A O   1 
HETATM 2271 O  O   . HOH H 5 .   ? 44.987 -17.916 2.029   1.00 55.72 ? 195 HOH A O   1 
HETATM 2272 O  O   . HOH H 5 .   ? 55.040 0.198   -0.354  1.00 53.75 ? 196 HOH A O   1 
HETATM 2273 O  O   . HOH H 5 .   ? 35.483 -0.451  -12.652 1.00 52.43 ? 197 HOH A O   1 
HETATM 2274 O  O   . HOH H 5 .   ? 58.220 -3.201  -2.985  1.00 41.95 ? 198 HOH A O   1 
HETATM 2275 O  O   . HOH H 5 .   ? 44.869 3.830   9.278   1.00 49.79 ? 199 HOH A O   1 
HETATM 2276 O  O   . HOH H 5 .   ? 31.427 8.785   4.042   1.00 45.00 ? 200 HOH A O   1 
HETATM 2277 O  O   . HOH H 5 .   ? 22.427 -11.467 -0.093  1.00 56.40 ? 201 HOH A O   1 
HETATM 2278 O  O   . HOH H 5 .   ? 32.263 -10.048 -4.338  1.00 57.02 ? 202 HOH A O   1 
HETATM 2279 O  O   . HOH H 5 .   ? 50.135 -10.100 -13.749 1.00 46.30 ? 203 HOH A O   1 
HETATM 2280 O  O   . HOH H 5 .   ? 39.012 11.667  -11.567 1.00 55.80 ? 204 HOH A O   1 
HETATM 2281 O  O   . HOH H 5 .   ? 50.788 17.741  -10.043 1.00 51.98 ? 205 HOH A O   1 
HETATM 2282 O  O   . HOH H 5 .   ? 47.389 -11.356 1.746   1.00 44.05 ? 206 HOH A O   1 
HETATM 2283 O  O   . HOH H 5 .   ? 23.095 -1.718  1.324   1.00 51.94 ? 207 HOH A O   1 
HETATM 2284 O  O   . HOH H 5 .   ? 46.648 -4.539  -17.979 1.00 52.37 ? 208 HOH A O   1 
HETATM 2285 O  O   . HOH H 5 .   ? 37.312 -3.502  -11.018 1.00 45.92 ? 209 HOH A O   1 
HETATM 2286 O  O   . HOH H 5 .   ? 38.348 -14.719 -6.714  1.00 53.04 ? 210 HOH A O   1 
HETATM 2287 O  O   . HOH H 5 .   ? 39.165 4.623   7.985   1.00 40.27 ? 211 HOH A O   1 
HETATM 2288 O  O   . HOH H 5 .   ? 48.756 7.311   10.271  1.00 58.68 ? 212 HOH A O   1 
HETATM 2289 O  O   . HOH H 5 .   ? 42.393 0.893   -12.839 1.00 45.99 ? 213 HOH A O   1 
HETATM 2290 O  O   . HOH H 5 .   ? 59.404 8.164   -2.519  1.00 63.66 ? 214 HOH A O   1 
HETATM 2291 O  O   . HOH H 5 .   ? 51.249 4.484   15.701  1.00 58.94 ? 215 HOH A O   1 
HETATM 2292 O  O   . HOH H 5 .   ? 25.426 -8.110  1.085   1.00 55.08 ? 216 HOH A O   1 
HETATM 2293 O  O   . HOH H 5 .   ? 56.487 1.643   1.457   1.00 54.11 ? 217 HOH A O   1 
HETATM 2294 O  O   . HOH H 5 .   ? 57.162 -6.787  -2.243  1.00 57.49 ? 218 HOH A O   1 
HETATM 2295 O  O   . HOH H 5 .   ? 51.778 -11.866 -1.550  1.00 52.09 ? 219 HOH A O   1 
HETATM 2296 O  O   . HOH H 5 .   ? 49.885 1.274   -15.579 1.00 47.24 ? 220 HOH A O   1 
HETATM 2297 O  O   . HOH H 5 .   ? 23.129 -8.672  1.976   1.00 49.79 ? 221 HOH A O   1 
HETATM 2298 O  O   . HOH H 5 .   ? 59.564 -10.364 -3.000  1.00 59.67 ? 222 HOH A O   1 
HETATM 2299 O  O   . HOH H 5 .   ? 52.742 -11.490 -6.129  1.00 51.36 ? 223 HOH A O   1 
HETATM 2300 O  O   . HOH H 5 .   ? 38.438 5.509   -9.896  1.00 51.94 ? 224 HOH A O   1 
HETATM 2301 O  O   . HOH H 5 .   ? 50.049 -11.867 1.573   1.00 52.73 ? 225 HOH A O   1 
HETATM 2302 O  O   . HOH H 5 .   ? 39.685 7.981   -10.358 1.00 57.55 ? 226 HOH A O   1 
HETATM 2303 O  O   . HOH H 5 .   ? 60.072 1.012   -17.806 1.00 59.08 ? 227 HOH A O   1 
HETATM 2304 O  O   . HOH H 5 .   ? 50.545 -13.558 5.801   1.00 62.00 ? 228 HOH A O   1 
HETATM 2305 O  O   . HOH H 5 .   ? 54.188 -9.651  -3.179  1.00 64.26 ? 229 HOH A O   1 
HETATM 2306 O  O   . HOH H 5 .   ? 55.930 -0.623  3.900   1.00 52.33 ? 230 HOH A O   1 
HETATM 2307 O  O   . HOH H 5 .   ? 59.111 4.998   -11.824 1.00 53.14 ? 231 HOH A O   1 
HETATM 2308 O  O   . HOH H 5 .   ? 49.720 15.029  8.233   1.00 61.04 ? 232 HOH A O   1 
HETATM 2309 O  O   . HOH H 5 .   ? 51.793 9.097   -11.399 1.00 54.59 ? 233 HOH A O   1 
HETATM 2310 O  O   . HOH H 5 .   ? 31.707 8.628   -7.783  1.00 58.75 ? 234 HOH A O   1 
HETATM 2311 O  O   . HOH H 5 .   ? 57.177 6.310   -4.677  1.00 48.65 ? 235 HOH A O   1 
HETATM 2312 O  O   . HOH H 5 .   ? 61.225 -9.250  -15.658 1.00 65.45 ? 236 HOH A O   1 
HETATM 2313 O  O   . HOH H 5 .   ? 40.704 -13.332 -9.425  1.00 54.94 ? 237 HOH A O   1 
HETATM 2314 O  O   . HOH H 5 .   ? 51.793 11.657  -11.449 1.00 46.44 ? 238 HOH A O   1 
HETATM 2315 O  O   . HOH H 5 .   ? 39.889 3.348   -10.629 1.00 51.79 ? 239 HOH A O   1 
HETATM 2316 O  O   . HOH H 5 .   ? 46.663 -19.144 -1.532  1.00 55.70 ? 240 HOH A O   1 
HETATM 2317 O  O   . HOH H 5 .   ? 52.521 11.579  -5.991  1.00 52.73 ? 241 HOH A O   1 
HETATM 2318 O  O   . HOH H 5 .   ? 41.842 -14.397 4.038   1.00 50.04 ? 242 HOH A O   1 
HETATM 2319 O  O   . HOH H 5 .   ? 50.230 -14.838 0.037   1.00 53.95 ? 243 HOH A O   1 
HETATM 2320 O  O   . HOH H 5 .   ? 43.930 -5.638  -17.735 1.00 48.80 ? 244 HOH A O   1 
HETATM 2321 O  O   . HOH H 5 .   ? 27.268 8.454   -1.597  1.00 57.76 ? 245 HOH A O   1 
HETATM 2322 O  O   . HOH H 5 .   ? 50.437 -1.087  -17.405 1.00 53.52 ? 246 HOH A O   1 
HETATM 2323 O  O   . HOH H 5 .   ? 26.042 -0.754  -4.228  1.00 54.23 ? 247 HOH A O   1 
HETATM 2324 O  O   . HOH H 5 .   ? 43.288 13.440  11.638  1.00 60.24 ? 248 HOH A O   1 
HETATM 2325 O  O   . HOH H 5 .   ? 32.143 -12.736 9.684   1.00 58.96 ? 249 HOH A O   1 
HETATM 2326 O  O   . HOH H 5 .   ? 36.153 -3.829  -13.444 1.00 56.60 ? 250 HOH A O   1 
HETATM 2327 O  O   . HOH H 5 .   ? 56.652 -2.277  -1.009  1.00 62.11 ? 251 HOH A O   1 
HETATM 2328 O  O   . HOH H 5 .   ? 41.306 -14.345 7.643   1.00 66.45 ? 252 HOH A O   1 
HETATM 2329 O  O   . HOH H 5 .   ? 42.171 19.634  -3.146  1.00 58.39 ? 253 HOH A O   1 
HETATM 2330 O  O   . HOH H 5 .   ? 26.609 -3.353  -4.819  1.00 48.76 ? 254 HOH A O   1 
HETATM 2331 O  O   . HOH H 5 .   ? 54.795 3.686   -11.932 1.00 42.42 ? 255 HOH A O   1 
HETATM 2332 O  O   . HOH H 5 .   ? 33.508 -9.850  7.123   1.00 48.68 ? 256 HOH A O   1 
HETATM 2333 O  O   . HOH H 5 .   ? 19.951 1.201   -4.280  1.00 61.81 ? 257 HOH A O   1 
HETATM 2334 O  O   . HOH H 5 .   ? 47.940 -16.284 2.886   1.00 60.63 ? 258 HOH A O   1 
HETATM 2335 O  O   . HOH H 5 .   ? 44.820 -20.790 -10.355 1.00 62.64 ? 259 HOH A O   1 
HETATM 2336 O  O   . HOH H 5 .   ? 44.650 19.209  -3.126  1.00 57.48 ? 260 HOH A O   1 
HETATM 2337 O  O   . HOH H 5 .   ? 33.571 -1.886  -13.557 1.00 49.63 ? 261 HOH A O   1 
HETATM 2338 O  O   . HOH H 5 .   ? 59.331 -0.948  -15.783 1.00 61.13 ? 262 HOH A O   1 
HETATM 2339 O  O   . HOH H 5 .   ? 55.909 -12.825 -8.784  1.00 56.51 ? 263 HOH A O   1 
HETATM 2340 O  O   . HOH H 5 .   ? 47.295 19.947  -3.676  1.00 53.86 ? 264 HOH A O   1 
HETATM 2341 O  O   . HOH H 5 .   ? 22.050 1.779   12.279  1.00 56.36 ? 265 HOH A O   1 
HETATM 2342 O  O   . HOH H 5 .   ? 47.146 -16.868 5.945   1.00 60.94 ? 266 HOH A O   1 
HETATM 2343 O  O   . HOH H 5 .   ? 52.154 -18.978 -4.811  1.00 57.98 ? 267 HOH A O   1 
HETATM 2344 O  O   . HOH H 5 .   ? 38.772 14.219  -10.444 1.00 57.68 ? 268 HOH A O   1 
HETATM 2345 O  O   . HOH H 5 .   ? 31.221 4.321   -12.661 1.00 60.60 ? 269 HOH A O   1 
HETATM 2346 O  O   . HOH H 5 .   ? 56.094 -7.855  -16.068 1.00 51.30 ? 270 HOH A O   1 
HETATM 2347 O  O   . HOH H 5 .   ? 57.274 -9.096  -13.626 1.00 58.74 ? 271 HOH A O   1 
HETATM 2348 O  O   . HOH H 5 .   ? 45.458 -15.588 4.462   1.00 61.35 ? 272 HOH A O   1 
HETATM 2349 O  O   . HOH H 5 .   ? 34.057 -13.041 -8.417  1.00 65.48 ? 273 HOH A O   1 
HETATM 2350 O  O   . HOH H 5 .   ? 42.203 -20.499 -6.681  1.00 62.34 ? 274 HOH A O   1 
HETATM 2351 O  O   . HOH H 5 .   ? 30.454 -9.265  6.759   1.00 61.40 ? 275 HOH A O   1 
HETATM 2352 O  O   . HOH H 5 .   ? 41.163 12.097  6.019   1.00 49.41 ? 276 HOH A O   1 
HETATM 2353 O  O   . HOH H 5 .   ? 57.235 3.270   -12.606 1.00 48.76 ? 277 HOH A O   1 
HETATM 2354 O  O   . HOH H 5 .   ? 34.083 -17.551 1.084   1.00 57.42 ? 278 HOH A O   1 
HETATM 2355 O  O   . HOH H 5 .   ? 42.637 -0.923  -15.030 1.00 62.99 ? 279 HOH A O   1 
HETATM 2356 O  O   . HOH H 5 .   ? 49.576 8.791   -15.330 1.00 59.05 ? 280 HOH A O   1 
HETATM 2357 O  O   . HOH H 5 .   ? 37.416 9.331   -13.716 1.00 66.94 ? 281 HOH A O   1 
HETATM 2358 O  O   . HOH H 5 .   ? 39.420 6.320   -14.253 1.00 51.15 ? 282 HOH A O   1 
HETATM 2359 O  O   . HOH H 5 .   ? 31.495 -15.056 10.026  1.00 55.28 ? 283 HOH A O   1 
HETATM 2360 O  O   . HOH H 5 .   ? 33.755 -14.597 9.224   1.00 58.77 ? 284 HOH A O   1 
HETATM 2361 O  O   . HOH H 5 .   ? 32.433 -12.878 6.933   1.00 54.28 ? 285 HOH A O   1 
HETATM 2362 O  O   . HOH I 5 .   ? 24.588 -6.792  21.914  1.00 41.37 ? 301 HOH B O   1 
HETATM 2363 O  O   . HOH I 5 .   ? 43.271 0.126   33.342  1.00 40.91 ? 302 HOH B O   1 
HETATM 2364 O  O   . HOH I 5 .   ? 41.612 3.681   12.798  1.00 38.29 ? 303 HOH B O   1 
HETATM 2365 O  O   . HOH I 5 .   ? 35.711 -8.468  30.230  1.00 37.01 ? 304 HOH B O   1 
HETATM 2366 O  O   . HOH I 5 .   ? 26.412 -2.702  11.986  1.00 53.25 ? 305 HOH B O   1 
HETATM 2367 O  O   . HOH I 5 .   ? 23.374 -9.367  27.222  1.00 40.43 ? 306 HOH B O   1 
HETATM 2368 O  O   . HOH I 5 .   ? 36.684 4.945   8.962   1.00 34.89 ? 307 HOH B O   1 
HETATM 2369 O  O   . HOH I 5 .   ? 24.413 -14.203 19.600  1.00 48.98 ? 308 HOH B O   1 
HETATM 2370 O  O   . HOH I 5 .   ? 20.632 1.560   35.779  1.00 42.99 ? 309 HOH B O   1 
HETATM 2371 O  O   . HOH I 5 .   ? 24.941 -2.320  17.428  1.00 41.73 ? 310 HOH B O   1 
HETATM 2372 O  O   . HOH I 5 .   ? 30.862 -1.210  29.735  1.00 36.78 ? 311 HOH B O   1 
HETATM 2373 O  O   . HOH I 5 .   ? 43.385 1.360   14.312  1.00 28.76 ? 312 HOH B O   1 
HETATM 2374 O  O   . HOH I 5 .   ? 31.085 -5.408  34.996  1.00 37.51 ? 313 HOH B O   1 
HETATM 2375 O  O   . HOH I 5 .   ? 34.856 6.896   14.423  1.00 39.98 ? 314 HOH B O   1 
HETATM 2376 O  O   . HOH I 5 .   ? 32.635 14.532  28.427  1.00 51.17 ? 315 HOH B O   1 
HETATM 2377 O  O   . HOH I 5 .   ? 40.841 2.445   39.151  1.00 46.22 ? 316 HOH B O   1 
HETATM 2378 O  O   . HOH I 5 .   ? 26.351 11.314  30.755  1.00 38.48 ? 317 HOH B O   1 
HETATM 2379 O  O   . HOH I 5 .   ? 25.026 3.329   22.992  1.00 37.22 ? 318 HOH B O   1 
HETATM 2380 O  O   . HOH I 5 .   ? 42.659 13.401  23.262  1.00 54.72 ? 319 HOH B O   1 
HETATM 2381 O  O   . HOH I 5 .   ? 21.618 0.242   21.048  1.00 50.00 ? 320 HOH B O   1 
HETATM 2382 O  O   . HOH I 5 .   ? 29.984 -14.291 17.144  1.00 39.46 ? 321 HOH B O   1 
HETATM 2383 O  O   . HOH I 5 .   ? 25.247 -8.130  24.234  1.00 43.01 ? 322 HOH B O   1 
HETATM 2384 O  O   . HOH I 5 .   ? 25.614 -10.587 26.333  1.00 42.54 ? 323 HOH B O   1 
HETATM 2385 O  O   . HOH I 5 .   ? 30.644 9.689   35.288  1.00 60.23 ? 324 HOH B O   1 
HETATM 2386 O  O   . HOH I 5 .   ? 26.816 5.286   22.750  1.00 42.22 ? 325 HOH B O   1 
HETATM 2387 O  O   . HOH I 5 .   ? 28.021 7.131   11.377  1.00 54.54 ? 326 HOH B O   1 
HETATM 2388 O  O   . HOH I 5 .   ? 21.113 0.355   25.383  1.00 35.52 ? 327 HOH B O   1 
HETATM 2389 O  O   . HOH I 5 .   ? 21.834 -17.409 31.851  1.00 39.96 ? 328 HOH B O   1 
HETATM 2390 O  O   . HOH I 5 .   ? 49.957 5.509   13.404  1.00 56.41 ? 329 HOH B O   1 
HETATM 2391 O  O   . HOH I 5 .   ? 36.791 -6.910  32.048  1.00 39.08 ? 330 HOH B O   1 
HETATM 2392 O  O   . HOH I 5 .   ? 40.468 -17.839 22.326  1.00 41.19 ? 331 HOH B O   1 
HETATM 2393 O  O   . HOH I 5 .   ? 34.371 -10.921 11.182  1.00 39.61 ? 332 HOH B O   1 
HETATM 2394 O  O   . HOH I 5 .   ? 17.114 -8.110  23.370  1.00 50.23 ? 333 HOH B O   1 
HETATM 2395 O  O   . HOH I 5 .   ? 27.041 -11.340 28.991  1.00 47.75 ? 334 HOH B O   1 
HETATM 2396 O  O   . HOH I 5 .   ? 37.918 13.096  7.761   1.00 56.64 ? 335 HOH B O   1 
HETATM 2397 O  O   . HOH I 5 .   ? 40.895 8.046   15.054  1.00 41.80 ? 336 HOH B O   1 
HETATM 2398 O  O   . HOH I 5 .   ? 46.590 7.229   40.964  1.00 37.55 ? 337 HOH B O   1 
HETATM 2399 O  O   . HOH I 5 .   ? 24.697 -4.077  15.255  1.00 51.07 ? 338 HOH B O   1 
HETATM 2400 O  O   . HOH I 5 .   ? 29.643 -8.249  13.380  1.00 42.90 ? 339 HOH B O   1 
HETATM 2401 O  O   . HOH I 5 .   ? 29.701 5.677   26.711  1.00 40.08 ? 340 HOH B O   1 
HETATM 2402 O  O   . HOH I 5 .   ? 25.329 -6.081  13.734  1.00 40.77 ? 341 HOH B O   1 
HETATM 2403 O  O   . HOH I 5 .   ? 36.596 5.343   13.877  1.00 43.46 ? 342 HOH B O   1 
HETATM 2404 O  O   . HOH I 5 .   ? 39.394 6.206   13.675  1.00 47.59 ? 343 HOH B O   1 
HETATM 2405 O  O   . HOH I 5 .   ? 30.871 -8.469  10.633  1.00 39.38 ? 344 HOH B O   1 
HETATM 2406 O  O   . HOH I 5 .   ? 27.338 9.731   28.331  1.00 46.54 ? 345 HOH B O   1 
HETATM 2407 O  O   . HOH I 5 .   ? 50.616 -3.851  18.513  1.00 48.70 ? 346 HOH B O   1 
HETATM 2408 O  O   . HOH I 5 .   ? 28.687 -10.895 31.005  1.00 44.83 ? 347 HOH B O   1 
HETATM 2409 O  O   . HOH I 5 .   ? 33.197 -4.132  35.663  1.00 61.17 ? 348 HOH B O   1 
HETATM 2410 O  O   . HOH I 5 .   ? 29.404 8.417   26.385  1.00 42.48 ? 349 HOH B O   1 
HETATM 2411 O  O   . HOH I 5 .   ? 33.366 -11.849 29.754  1.00 40.42 ? 350 HOH B O   1 
HETATM 2412 O  O   . HOH I 5 .   ? 41.055 -1.211  35.945  1.00 63.37 ? 351 HOH B O   1 
HETATM 2413 O  O   . HOH I 5 .   ? 18.359 -7.814  17.474  1.00 63.11 ? 352 HOH B O   1 
HETATM 2414 O  O   . HOH I 5 .   ? 50.687 -10.232 26.262  1.00 56.56 ? 353 HOH B O   1 
HETATM 2415 O  O   . HOH I 5 .   ? 42.636 -16.297 23.071  1.00 40.85 ? 354 HOH B O   1 
HETATM 2416 O  O   . HOH I 5 .   ? 40.335 15.039  23.397  1.00 61.85 ? 355 HOH B O   1 
HETATM 2417 O  O   . HOH I 5 .   ? 33.672 12.693  19.235  1.00 61.64 ? 356 HOH B O   1 
HETATM 2418 O  O   . HOH I 5 .   ? 42.549 -3.761  34.373  1.00 53.38 ? 357 HOH B O   1 
HETATM 2419 O  O   . HOH I 5 .   ? 39.910 10.744  15.017  1.00 55.47 ? 358 HOH B O   1 
HETATM 2420 O  O   . HOH I 5 .   ? 31.095 -23.892 17.380  1.00 57.21 ? 359 HOH B O   1 
HETATM 2421 O  O   . HOH I 5 .   ? 37.751 -13.528 11.837  1.00 48.12 ? 360 HOH B O   1 
HETATM 2422 O  O   . HOH I 5 .   ? 50.744 -8.579  14.735  1.00 55.31 ? 361 HOH B O   1 
HETATM 2423 O  O   . HOH I 5 .   ? 25.885 -16.299 19.090  1.00 45.60 ? 362 HOH B O   1 
HETATM 2424 O  O   . HOH I 5 .   ? 21.611 -0.637  32.033  1.00 47.37 ? 363 HOH B O   1 
HETATM 2425 O  O   . HOH I 5 .   ? 51.185 -2.787  21.894  1.00 57.30 ? 364 HOH B O   1 
HETATM 2426 O  O   . HOH I 5 .   ? 35.857 -12.804 36.953  1.00 52.89 ? 365 HOH B O   1 
HETATM 2427 O  O   . HOH I 5 .   ? 26.459 -5.262  11.188  1.00 58.44 ? 366 HOH B O   1 
HETATM 2428 O  O   . HOH I 5 .   ? 43.509 -6.941  34.654  1.00 51.91 ? 367 HOH B O   1 
HETATM 2429 O  O   . HOH I 5 .   ? 47.489 -14.184 28.795  1.00 55.86 ? 368 HOH B O   1 
HETATM 2430 O  O   . HOH I 5 .   ? 26.590 -8.350  13.931  1.00 45.34 ? 369 HOH B O   1 
HETATM 2431 O  O   . HOH I 5 .   ? 39.435 15.875  30.797  1.00 61.19 ? 370 HOH B O   1 
HETATM 2432 O  O   . HOH I 5 .   ? 24.134 -3.166  34.739  1.00 43.82 ? 371 HOH B O   1 
HETATM 2433 O  O   . HOH I 5 .   ? 28.932 1.026   38.904  1.00 51.02 ? 372 HOH B O   1 
HETATM 2434 O  O   . HOH I 5 .   ? 34.961 -9.281  9.412   1.00 41.69 ? 373 HOH B O   1 
HETATM 2435 O  O   . HOH I 5 .   ? 44.812 -9.923  28.497  1.00 46.08 ? 374 HOH B O   1 
HETATM 2436 O  O   . HOH I 5 .   ? 37.213 -4.184  31.544  1.00 54.37 ? 375 HOH B O   1 
HETATM 2437 O  O   . HOH I 5 .   ? 26.926 -8.907  11.272  1.00 57.93 ? 376 HOH B O   1 
HETATM 2438 O  O   . HOH I 5 .   ? 35.160 0.122   36.697  1.00 55.51 ? 377 HOH B O   1 
HETATM 2439 O  O   . HOH I 5 .   ? 38.114 -11.567 37.414  1.00 59.93 ? 378 HOH B O   1 
HETATM 2440 O  O   . HOH I 5 .   ? 27.873 10.473  20.107  1.00 60.29 ? 379 HOH B O   1 
HETATM 2441 O  O   . HOH I 5 .   ? 38.682 11.674  10.387  1.00 66.50 ? 380 HOH B O   1 
HETATM 2442 O  O   . HOH I 5 .   ? 32.214 3.404   37.795  1.00 47.06 ? 381 HOH B O   1 
HETATM 2443 O  O   . HOH I 5 .   ? 39.216 -9.341  32.544  1.00 43.46 ? 382 HOH B O   1 
HETATM 2444 O  O   . HOH I 5 .   ? 34.643 -14.820 22.700  1.00 39.88 ? 383 HOH B O   1 
HETATM 2445 O  O   . HOH I 5 .   ? 48.736 9.197   17.843  1.00 54.22 ? 384 HOH B O   1 
HETATM 2446 O  O   . HOH I 5 .   ? 21.240 -0.291  40.293  1.00 54.20 ? 385 HOH B O   1 
HETATM 2447 O  O   . HOH I 5 .   ? 48.558 10.963  14.829  1.00 57.36 ? 386 HOH B O   1 
HETATM 2448 O  O   . HOH I 5 .   ? 25.487 7.185   19.511  1.00 62.05 ? 387 HOH B O   1 
HETATM 2449 O  O   . HOH I 5 .   ? 21.126 2.209   23.434  1.00 55.54 ? 388 HOH B O   1 
HETATM 2450 O  O   . HOH I 5 .   ? 50.480 9.252   15.295  1.00 64.00 ? 389 HOH B O   1 
HETATM 2451 O  O   . HOH I 5 .   ? 40.079 -7.872  34.481  1.00 52.70 ? 390 HOH B O   1 
HETATM 2452 O  O   . HOH I 5 .   ? 54.719 -5.349  24.032  1.00 59.14 ? 391 HOH B O   1 
HETATM 2453 O  O   . HOH I 5 .   ? 39.354 11.677  35.354  1.00 53.23 ? 392 HOH B O   1 
HETATM 2454 O  O   . HOH I 5 .   ? 18.399 -0.708  24.659  1.00 53.05 ? 393 HOH B O   1 
HETATM 2455 O  O   . HOH I 5 .   ? 50.286 9.837   29.997  1.00 57.08 ? 394 HOH B O   1 
HETATM 2456 O  O   . HOH I 5 .   ? 50.658 -8.664  18.569  1.00 58.53 ? 395 HOH B O   1 
HETATM 2457 O  O   . HOH I 5 .   ? 32.403 -21.216 16.475  1.00 52.78 ? 396 HOH B O   1 
HETATM 2458 O  O   . HOH I 5 .   ? 48.104 -12.929 30.902  1.00 54.06 ? 397 HOH B O   1 
HETATM 2459 O  O   . HOH I 5 .   ? 39.766 13.884  21.103  1.00 56.96 ? 398 HOH B O   1 
HETATM 2460 O  O   . HOH I 5 .   ? 38.924 13.918  12.688  1.00 59.65 ? 399 HOH B O   1 
HETATM 2461 O  O   . HOH I 5 .   ? 39.664 -22.164 16.658  1.00 68.61 ? 400 HOH B O   1 
HETATM 2462 O  O   . HOH I 5 .   ? 24.985 -19.558 15.908  1.00 61.13 ? 401 HOH B O   1 
HETATM 2463 O  O   . HOH I 5 .   ? 24.841 10.972  21.018  1.00 48.02 ? 402 HOH B O   1 
HETATM 2464 O  O   . HOH I 5 .   ? 36.956 10.124  35.621  1.00 60.68 ? 403 HOH B O   1 
HETATM 2465 O  O   . HOH I 5 .   ? 22.771 2.424   14.779  1.00 54.96 ? 404 HOH B O   1 
HETATM 2466 O  O   . HOH I 5 .   ? 54.070 6.996   36.497  1.00 63.66 ? 405 HOH B O   1 
HETATM 2467 O  O   . HOH I 5 .   ? 16.309 -6.312  15.477  1.00 50.49 ? 406 HOH B O   1 
HETATM 2468 O  O   . HOH I 5 .   ? 33.984 15.457  15.192  1.00 59.23 ? 407 HOH B O   1 
HETATM 2469 O  O   . HOH I 5 .   ? 49.169 -14.299 32.859  1.00 61.30 ? 408 HOH B O   1 
HETATM 2470 O  O   . HOH I 5 .   ? 20.310 10.662  25.791  1.00 60.92 ? 409 HOH B O   1 
HETATM 2471 O  O   . HOH I 5 .   ? 51.769 -12.206 23.913  1.00 53.03 ? 410 HOH B O   1 
HETATM 2472 O  O   . HOH I 5 .   ? 31.739 16.102  17.259  1.00 56.81 ? 411 HOH B O   1 
HETATM 2473 O  O   . HOH I 5 .   ? 49.342 -10.818 31.799  1.00 60.02 ? 412 HOH B O   1 
HETATM 2474 O  O   . HOH I 5 .   ? 39.497 12.902  31.506  1.00 55.50 ? 413 HOH B O   1 
HETATM 2475 O  O   . HOH I 5 .   ? 53.258 12.756  35.886  1.00 66.33 ? 414 HOH B O   1 
HETATM 2476 O  O   . HOH I 5 .   ? 35.931 -12.822 10.236  1.00 55.39 ? 415 HOH B O   1 
HETATM 2477 O  O   . HOH I 5 .   ? 38.367 16.853  13.917  1.00 61.47 ? 416 HOH B O   1 
HETATM 2478 O  O   . HOH I 5 .   ? 28.682 -4.436  36.294  1.00 56.43 ? 417 HOH B O   1 
HETATM 2479 O  O   . HOH I 5 .   ? 23.826 -6.036  39.450  1.00 60.94 ? 418 HOH B O   1 
HETATM 2480 O  O   . HOH I 5 .   ? 33.581 -26.029 21.142  1.00 54.17 ? 419 HOH B O   1 
HETATM 2481 O  O   . HOH I 5 .   ? 32.007 -18.016 13.845  1.00 60.22 ? 420 HOH B O   1 
HETATM 2482 O  O   . HOH I 5 .   ? 47.752 -12.314 35.256  1.00 58.37 ? 421 HOH B O   1 
HETATM 2483 O  O   . HOH I 5 .   ? 18.777 3.662   22.355  1.00 57.64 ? 422 HOH B O   1 
HETATM 2484 O  O   . HOH I 5 .   ? 38.048 16.914  27.192  1.00 61.94 ? 423 HOH B O   1 
HETATM 2485 O  O   . HOH I 5 .   ? 43.582 5.873   14.724  1.00 55.18 ? 424 HOH B O   1 
HETATM 2486 O  O   . HOH I 5 .   ? 42.819 -16.222 27.795  1.00 56.66 ? 425 HOH B O   1 
HETATM 2487 O  O   . HOH I 5 .   ? 40.582 18.217  22.114  1.00 64.30 ? 426 HOH B O   1 
HETATM 2488 O  O   . HOH I 5 .   ? 37.197 12.957  18.527  1.00 62.81 ? 427 HOH B O   1 
HETATM 2489 O  O   . HOH I 5 .   ? 39.274 -17.405 16.040  1.00 57.85 ? 428 HOH B O   1 
HETATM 2490 O  O   . HOH I 5 .   ? 42.980 7.978   12.480  1.00 59.83 ? 429 HOH B O   1 
HETATM 2491 O  O   . HOH I 5 .   ? 41.590 -12.801 36.483  1.00 51.35 ? 430 HOH B O   1 
HETATM 2492 O  O   . HOH I 5 .   ? 22.455 -12.344 12.780  1.00 57.77 ? 431 HOH B O   1 
HETATM 2493 O  O   . HOH I 5 .   ? 49.468 6.774   39.615  1.00 58.71 ? 432 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   VAL 5   4   4   VAL VAL A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   VAL 5   4   4   VAL VAL B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   ALA 7   6   6   ALA ALA B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 SER 112 111 111 SER SER B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU1 1   154 154 CU1 CU1 A . 
D 3 ZN  1   155 155 ZN  ZN2 A . 
E 2 CU1 1   154 154 CU1 CU1 B . 
F 3 ZN  1   155 155 ZN  ZN2 B . 
G 4 SO4 1   300 1   SO4 SO4 B . 
H 5 HOH 1   156 3   HOH HOH A . 
H 5 HOH 2   157 4   HOH HOH A . 
H 5 HOH 3   158 5   HOH HOH A . 
H 5 HOH 4   159 6   HOH HOH A . 
H 5 HOH 5   160 8   HOH HOH A . 
H 5 HOH 6   161 9   HOH HOH A . 
H 5 HOH 7   162 10  HOH HOH A . 
H 5 HOH 8   163 11  HOH HOH A . 
H 5 HOH 9   164 13  HOH HOH A . 
H 5 HOH 10  165 16  HOH HOH A . 
H 5 HOH 11  166 19  HOH HOH A . 
H 5 HOH 12  167 21  HOH HOH A . 
H 5 HOH 13  168 22  HOH HOH A . 
H 5 HOH 14  169 23  HOH HOH A . 
H 5 HOH 15  170 24  HOH HOH A . 
H 5 HOH 16  171 25  HOH HOH A . 
H 5 HOH 17  172 27  HOH HOH A . 
H 5 HOH 18  173 31  HOH HOH A . 
H 5 HOH 19  174 33  HOH HOH A . 
H 5 HOH 20  175 37  HOH HOH A . 
H 5 HOH 21  176 38  HOH HOH A . 
H 5 HOH 22  177 39  HOH HOH A . 
H 5 HOH 23  178 40  HOH HOH A . 
H 5 HOH 24  179 47  HOH HOH A . 
H 5 HOH 25  180 48  HOH HOH A . 
H 5 HOH 26  181 49  HOH HOH A . 
H 5 HOH 27  182 50  HOH HOH A . 
H 5 HOH 28  183 52  HOH HOH A . 
H 5 HOH 29  184 53  HOH HOH A . 
H 5 HOH 30  185 56  HOH HOH A . 
H 5 HOH 31  186 57  HOH HOH A . 
H 5 HOH 32  187 61  HOH HOH A . 
H 5 HOH 33  188 62  HOH HOH A . 
H 5 HOH 34  189 63  HOH HOH A . 
H 5 HOH 35  190 65  HOH HOH A . 
H 5 HOH 36  191 67  HOH HOH A . 
H 5 HOH 37  192 72  HOH HOH A . 
H 5 HOH 38  193 74  HOH HOH A . 
H 5 HOH 39  194 76  HOH HOH A . 
H 5 HOH 40  195 78  HOH HOH A . 
H 5 HOH 41  196 82  HOH HOH A . 
H 5 HOH 42  197 83  HOH HOH A . 
H 5 HOH 43  198 84  HOH HOH A . 
H 5 HOH 44  199 86  HOH HOH A . 
H 5 HOH 45  200 87  HOH HOH A . 
H 5 HOH 46  201 90  HOH HOH A . 
H 5 HOH 47  202 91  HOH HOH A . 
H 5 HOH 48  203 92  HOH HOH A . 
H 5 HOH 49  204 93  HOH HOH A . 
H 5 HOH 50  205 94  HOH HOH A . 
H 5 HOH 51  206 96  HOH HOH A . 
H 5 HOH 52  207 97  HOH HOH A . 
H 5 HOH 53  208 99  HOH HOH A . 
H 5 HOH 54  209 101 HOH HOH A . 
H 5 HOH 55  210 102 HOH HOH A . 
H 5 HOH 56  211 103 HOH HOH A . 
H 5 HOH 57  212 104 HOH HOH A . 
H 5 HOH 58  213 105 HOH HOH A . 
H 5 HOH 59  214 106 HOH HOH A . 
H 5 HOH 60  215 111 HOH HOH A . 
H 5 HOH 61  216 112 HOH HOH A . 
H 5 HOH 62  217 113 HOH HOH A . 
H 5 HOH 63  218 116 HOH HOH A . 
H 5 HOH 64  219 118 HOH HOH A . 
H 5 HOH 65  220 119 HOH HOH A . 
H 5 HOH 66  221 120 HOH HOH A . 
H 5 HOH 67  222 121 HOH HOH A . 
H 5 HOH 68  223 122 HOH HOH A . 
H 5 HOH 69  224 123 HOH HOH A . 
H 5 HOH 70  225 124 HOH HOH A . 
H 5 HOH 71  226 126 HOH HOH A . 
H 5 HOH 72  227 128 HOH HOH A . 
H 5 HOH 73  228 130 HOH HOH A . 
H 5 HOH 74  229 131 HOH HOH A . 
H 5 HOH 75  230 132 HOH HOH A . 
H 5 HOH 76  231 137 HOH HOH A . 
H 5 HOH 77  232 138 HOH HOH A . 
H 5 HOH 78  233 141 HOH HOH A . 
H 5 HOH 79  234 142 HOH HOH A . 
H 5 HOH 80  235 145 HOH HOH A . 
H 5 HOH 81  236 148 HOH HOH A . 
H 5 HOH 82  237 149 HOH HOH A . 
H 5 HOH 83  238 152 HOH HOH A . 
H 5 HOH 84  239 154 HOH HOH A . 
H 5 HOH 85  240 156 HOH HOH A . 
H 5 HOH 86  241 158 HOH HOH A . 
H 5 HOH 87  242 159 HOH HOH A . 
H 5 HOH 88  243 161 HOH HOH A . 
H 5 HOH 89  244 166 HOH HOH A . 
H 5 HOH 90  245 167 HOH HOH A . 
H 5 HOH 91  246 169 HOH HOH A . 
H 5 HOH 92  247 170 HOH HOH A . 
H 5 HOH 93  248 171 HOH HOH A . 
H 5 HOH 94  249 176 HOH HOH A . 
H 5 HOH 95  250 177 HOH HOH A . 
H 5 HOH 96  251 178 HOH HOH A . 
H 5 HOH 97  252 179 HOH HOH A . 
H 5 HOH 98  253 180 HOH HOH A . 
H 5 HOH 99  254 183 HOH HOH A . 
H 5 HOH 100 255 184 HOH HOH A . 
H 5 HOH 101 256 186 HOH HOH A . 
H 5 HOH 102 257 193 HOH HOH A . 
H 5 HOH 103 258 196 HOH HOH A . 
H 5 HOH 104 259 199 HOH HOH A . 
H 5 HOH 105 260 201 HOH HOH A . 
H 5 HOH 106 261 203 HOH HOH A . 
H 5 HOH 107 262 205 HOH HOH A . 
H 5 HOH 108 263 208 HOH HOH A . 
H 5 HOH 109 264 212 HOH HOH A . 
H 5 HOH 110 265 214 HOH HOH A . 
H 5 HOH 111 266 220 HOH HOH A . 
H 5 HOH 112 267 223 HOH HOH A . 
H 5 HOH 113 268 224 HOH HOH A . 
H 5 HOH 114 269 227 HOH HOH A . 
H 5 HOH 115 270 228 HOH HOH A . 
H 5 HOH 116 271 230 HOH HOH A . 
H 5 HOH 117 272 233 HOH HOH A . 
H 5 HOH 118 273 235 HOH HOH A . 
H 5 HOH 119 274 237 HOH HOH A . 
H 5 HOH 120 275 239 HOH HOH A . 
H 5 HOH 121 276 240 HOH HOH A . 
H 5 HOH 122 277 243 HOH HOH A . 
H 5 HOH 123 278 246 HOH HOH A . 
H 5 HOH 124 279 249 HOH HOH A . 
H 5 HOH 125 280 251 HOH HOH A . 
H 5 HOH 126 281 254 HOH HOH A . 
H 5 HOH 127 282 256 HOH HOH A . 
H 5 HOH 128 283 257 HOH HOH A . 
H 5 HOH 129 284 258 HOH HOH A . 
H 5 HOH 130 285 259 HOH HOH A . 
I 5 HOH 1   301 1   HOH HOH B . 
I 5 HOH 2   302 2   HOH HOH B . 
I 5 HOH 3   303 7   HOH HOH B . 
I 5 HOH 4   304 12  HOH HOH B . 
I 5 HOH 5   305 14  HOH HOH B . 
I 5 HOH 6   306 15  HOH HOH B . 
I 5 HOH 7   307 17  HOH HOH B . 
I 5 HOH 8   308 18  HOH HOH B . 
I 5 HOH 9   309 20  HOH HOH B . 
I 5 HOH 10  310 26  HOH HOH B . 
I 5 HOH 11  311 28  HOH HOH B . 
I 5 HOH 12  312 29  HOH HOH B . 
I 5 HOH 13  313 30  HOH HOH B . 
I 5 HOH 14  314 32  HOH HOH B . 
I 5 HOH 15  315 34  HOH HOH B . 
I 5 HOH 16  316 35  HOH HOH B . 
I 5 HOH 17  317 36  HOH HOH B . 
I 5 HOH 18  318 41  HOH HOH B . 
I 5 HOH 19  319 42  HOH HOH B . 
I 5 HOH 20  320 43  HOH HOH B . 
I 5 HOH 21  321 44  HOH HOH B . 
I 5 HOH 22  322 45  HOH HOH B . 
I 5 HOH 23  323 46  HOH HOH B . 
I 5 HOH 24  324 51  HOH HOH B . 
I 5 HOH 25  325 54  HOH HOH B . 
I 5 HOH 26  326 55  HOH HOH B . 
I 5 HOH 27  327 58  HOH HOH B . 
I 5 HOH 28  328 59  HOH HOH B . 
I 5 HOH 29  329 60  HOH HOH B . 
I 5 HOH 30  330 64  HOH HOH B . 
I 5 HOH 31  331 66  HOH HOH B . 
I 5 HOH 32  332 68  HOH HOH B . 
I 5 HOH 33  333 69  HOH HOH B . 
I 5 HOH 34  334 70  HOH HOH B . 
I 5 HOH 35  335 71  HOH HOH B . 
I 5 HOH 36  336 73  HOH HOH B . 
I 5 HOH 37  337 75  HOH HOH B . 
I 5 HOH 38  338 77  HOH HOH B . 
I 5 HOH 39  339 79  HOH HOH B . 
I 5 HOH 40  340 80  HOH HOH B . 
I 5 HOH 41  341 81  HOH HOH B . 
I 5 HOH 42  342 85  HOH HOH B . 
I 5 HOH 43  343 88  HOH HOH B . 
I 5 HOH 44  344 89  HOH HOH B . 
I 5 HOH 45  345 95  HOH HOH B . 
I 5 HOH 46  346 98  HOH HOH B . 
I 5 HOH 47  347 100 HOH HOH B . 
I 5 HOH 48  348 107 HOH HOH B . 
I 5 HOH 49  349 108 HOH HOH B . 
I 5 HOH 50  350 109 HOH HOH B . 
I 5 HOH 51  351 110 HOH HOH B . 
I 5 HOH 52  352 114 HOH HOH B . 
I 5 HOH 53  353 115 HOH HOH B . 
I 5 HOH 54  354 117 HOH HOH B . 
I 5 HOH 55  355 125 HOH HOH B . 
I 5 HOH 56  356 127 HOH HOH B . 
I 5 HOH 57  357 129 HOH HOH B . 
I 5 HOH 58  358 133 HOH HOH B . 
I 5 HOH 59  359 134 HOH HOH B . 
I 5 HOH 60  360 135 HOH HOH B . 
I 5 HOH 61  361 136 HOH HOH B . 
I 5 HOH 62  362 139 HOH HOH B . 
I 5 HOH 63  363 140 HOH HOH B . 
I 5 HOH 64  364 143 HOH HOH B . 
I 5 HOH 65  365 144 HOH HOH B . 
I 5 HOH 66  366 146 HOH HOH B . 
I 5 HOH 67  367 147 HOH HOH B . 
I 5 HOH 68  368 150 HOH HOH B . 
I 5 HOH 69  369 151 HOH HOH B . 
I 5 HOH 70  370 153 HOH HOH B . 
I 5 HOH 71  371 155 HOH HOH B . 
I 5 HOH 72  372 157 HOH HOH B . 
I 5 HOH 73  373 160 HOH HOH B . 
I 5 HOH 74  374 162 HOH HOH B . 
I 5 HOH 75  375 163 HOH HOH B . 
I 5 HOH 76  376 164 HOH HOH B . 
I 5 HOH 77  377 165 HOH HOH B . 
I 5 HOH 78  378 168 HOH HOH B . 
I 5 HOH 79  379 172 HOH HOH B . 
I 5 HOH 80  380 173 HOH HOH B . 
I 5 HOH 81  381 174 HOH HOH B . 
I 5 HOH 82  382 175 HOH HOH B . 
I 5 HOH 83  383 181 HOH HOH B . 
I 5 HOH 84  384 182 HOH HOH B . 
I 5 HOH 85  385 185 HOH HOH B . 
I 5 HOH 86  386 187 HOH HOH B . 
I 5 HOH 87  387 188 HOH HOH B . 
I 5 HOH 88  388 189 HOH HOH B . 
I 5 HOH 89  389 190 HOH HOH B . 
I 5 HOH 90  390 191 HOH HOH B . 
I 5 HOH 91  391 192 HOH HOH B . 
I 5 HOH 92  392 194 HOH HOH B . 
I 5 HOH 93  393 195 HOH HOH B . 
I 5 HOH 94  394 197 HOH HOH B . 
I 5 HOH 95  395 198 HOH HOH B . 
I 5 HOH 96  396 200 HOH HOH B . 
I 5 HOH 97  397 202 HOH HOH B . 
I 5 HOH 98  398 204 HOH HOH B . 
I 5 HOH 99  399 206 HOH HOH B . 
I 5 HOH 100 400 207 HOH HOH B . 
I 5 HOH 101 401 209 HOH HOH B . 
I 5 HOH 102 402 210 HOH HOH B . 
I 5 HOH 103 403 211 HOH HOH B . 
I 5 HOH 104 404 213 HOH HOH B . 
I 5 HOH 105 405 215 HOH HOH B . 
I 5 HOH 106 406 216 HOH HOH B . 
I 5 HOH 107 407 217 HOH HOH B . 
I 5 HOH 108 408 218 HOH HOH B . 
I 5 HOH 109 409 219 HOH HOH B . 
I 5 HOH 110 410 221 HOH HOH B . 
I 5 HOH 111 411 222 HOH HOH B . 
I 5 HOH 112 412 225 HOH HOH B . 
I 5 HOH 113 413 226 HOH HOH B . 
I 5 HOH 114 414 229 HOH HOH B . 
I 5 HOH 115 415 231 HOH HOH B . 
I 5 HOH 116 416 232 HOH HOH B . 
I 5 HOH 117 417 234 HOH HOH B . 
I 5 HOH 118 418 236 HOH HOH B . 
I 5 HOH 119 419 238 HOH HOH B . 
I 5 HOH 120 420 241 HOH HOH B . 
I 5 HOH 121 421 242 HOH HOH B . 
I 5 HOH 122 422 244 HOH HOH B . 
I 5 HOH 123 423 245 HOH HOH B . 
I 5 HOH 124 424 247 HOH HOH B . 
I 5 HOH 125 425 248 HOH HOH B . 
I 5 HOH 126 426 250 HOH HOH B . 
I 5 HOH 127 427 252 HOH HOH B . 
I 5 HOH 128 428 253 HOH HOH B . 
I 5 HOH 129 429 255 HOH HOH B . 
I 5 HOH 130 430 260 HOH HOH B . 
I 5 HOH 131 431 261 HOH HOH B . 
I 5 HOH 132 432 262 HOH HOH B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1540  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  14000 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 49  ? A HIS 48  ? 1_555 139.5 ? 
2  ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 101.2 ? 
3  NE2 ? A HIS 49 ? A HIS 48 ? 1_555 CU ? C CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 118.8 ? 
4  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 72  ? A HIS 71  ? 1_555 104.0 ? 
5  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 115.7 ? 
6  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 122.6 ? 
7  ND1 ? A HIS 64 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 102.3 ? 
8  ND1 ? A HIS 72 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 101.1 ? 
9  ND1 ? A HIS 81 ? A HIS 80 ? 1_555 ZN ? D ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 84  ? A ASP 83  ? 1_555 108.5 ? 
10 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? E CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 49  ? B HIS 48  ? 1_555 133.0 ? 
11 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? E CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 109.2 ? 
12 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 CU ? E CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 116.8 ? 
13 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 72  ? B HIS 71  ? 1_555 106.9 ? 
14 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 81  ? B HIS 80  ? 1_555 112.0 ? 
15 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 81  ? B HIS 80  ? 1_555 119.9 ? 
16 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 98.2  ? 
17 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 97.5  ? 
18 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 84  ? B ASP 83  ? 1_555 119.4 ? 
19 ND1 ? B HIS 64 ? B HIS 63 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 153.8 ? 
20 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 79.1  ? 
21 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 84.9  ? 
22 OD1 ? B ASP 84 ? B ASP 83 ? 1_555 ZN ? F ZN  . ? B ZN  155 ? 1_555 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 55.6  ? 
# 
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 2002-11-27 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-10-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2             
2 4 'Structure model' pdbx_struct_conn_angle 
3 4 'Structure model' struct_conn            
4 4 'Structure model' struct_ref_seq_dif     
5 4 'Structure model' struct_site            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_database_2.pdbx_DOI'                        
2  4 'Structure model' '_database_2.pdbx_database_accession'         
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
13 4 'Structure model' '_pdbx_struct_conn_angle.value'               
14 4 'Structure model' '_struct_conn.pdbx_dist_value'                
15 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
16 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
17 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
18 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
19 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
20 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
21 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
22 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
23 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
24 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
25 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
26 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
27 4 'Structure model' '_struct_ref_seq_dif.details'                 
28 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
29 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
30 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
AMoRE     phasing          . ? 3 
CNS       refinement       . ? 4 
# 
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 SER A 25  ? ? -18.49  -61.55 
2 1 SER A 98  ? ? -164.85 100.40 
3 1 LEU A 126 ? ? 51.10   17.03  
4 1 LYS B 91  ? ? -39.95  -34.44 
5 1 SER B 98  ? ? -155.18 87.89  
6 1 LEU B 126 ? ? 56.25   13.02  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 0 A LYS 9   ? CE  ? A LYS 10  CE  
2  1 Y 0 A LYS 30  ? CE  ? A LYS 31  CE  
3  1 Y 0 A LYS 30  ? NZ  ? A LYS 31  NZ  
4  1 Y 0 A LYS 75  ? NZ  ? A LYS 76  NZ  
5  1 Y 0 A GLU 77  ? OE1 ? A GLU 78  OE1 
6  1 Y 0 A GLU 77  ? OE2 ? A GLU 78  OE2 
7  1 Y 0 A LYS 91  ? CE  ? A LYS 92  CE  
8  1 Y 0 A LYS 91  ? NZ  ? A LYS 92  NZ  
9  1 Y 0 A ASP 109 ? CG  ? A ASP 110 CG  
10 1 Y 0 A ASP 109 ? OD1 ? A ASP 110 OD1 
11 1 Y 0 A ASP 109 ? OD2 ? A ASP 110 OD2 
12 1 Y 0 A LYS 128 ? NZ  ? A LYS 129 NZ  
13 1 Y 0 A LYS 136 ? NZ  ? A LYS 137 NZ  
14 1 Y 0 B LYS 23  ? CD  ? B LYS 24  CD  
15 1 Y 0 B LYS 23  ? CE  ? B LYS 24  CE  
16 1 Y 0 B LYS 23  ? NZ  ? B LYS 24  NZ  
17 1 Y 0 B GLU 24  ? CG  ? B GLU 25  CG  
18 1 Y 0 B LYS 30  ? CG  ? B LYS 31  CG  
19 1 Y 0 B LYS 30  ? CD  ? B LYS 31  CD  
20 1 Y 0 B LYS 30  ? CE  ? B LYS 31  CE  
21 1 Y 0 B LYS 36  ? CE  ? B LYS 37  CE  
22 1 Y 0 B LYS 36  ? NZ  ? B LYS 37  NZ  
23 1 Y 0 B GLU 40  ? CG  ? B GLU 41  CG  
24 1 Y 0 B LYS 70  ? CE  ? B LYS 71  CE  
25 1 Y 0 B LYS 70  ? NZ  ? B LYS 71  NZ  
26 1 Y 0 B LYS 91  ? CG  ? B LYS 92  CG  
27 1 Y 0 B LYS 91  ? CD  ? B LYS 92  CD  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 0 ? A MET 1 
2 1 Y 1 B MET 0 ? B MET 1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (I) ION' CU1 
3 'ZINC ION'       ZN  
4 'SULFATE ION'    SO4 
5 water            HOH 
# 
