data_1PTZ
# 
_entry.id   1PTZ 
# 
_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   1PTZ         pdb_00001ptz 10.2210/pdb1ptz/pdb 
RCSB  RCSB019561   ?            ?                   
WWPDB D_1000019561 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1PU0 
_pdbx_database_related.details        'Structure of Human Cu,Zn Superoxide Dismutase' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1PTZ 
_pdbx_database_status.recvd_initial_deposition_date   2003-06-23 
_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 
'DiDonato, M.'    1  
'Craig, L.'       2  
'Huff, M.E.'      3  
'Thayer, M.M.'    4  
'Cardoso, R.M.F.' 5  
'Kassmann, C.J.'  6  
'Lo, T.P.'        7  
'Bruns, C.K.'     8  
'Powers, E.T.'    9  
'Kelly, J.W.'     10 
'Getzoff, E.D.'   11 
'Tainer, J.A.'    12 
# 
_citation.id                        primary 
_citation.title                     
'ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            332 
_citation.page_first                601 
_citation.page_last                 615 
_citation.year                      2003 
_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   12963370 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(03)00889-1' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'DiDonato, M.'    1  ? 
primary 'Craig, L.'       2  ? 
primary 'Huff, M.E.'      3  ? 
primary 'Thayer, M.M.'    4  ? 
primary 'Cardoso, R.M.F.' 5  ? 
primary 'Kassmann, C.J.'  6  ? 
primary 'Lo, T.P.'        7  ? 
primary 'Bruns, C.K.'     8  ? 
primary 'Powers, E.T.'    9  ? 
primary 'Kelly, J.W.'     10 ? 
primary 'Getzoff, E.D.'   11 ? 
primary 'Tainer, J.A.'    12 ? 
# 
_cell.entry_id           1PTZ 
_cell.length_a           111.199 
_cell.length_b           47.525 
_cell.length_c           56.041 
_cell.angle_alpha        90.00 
_cell.angle_beta         97.99 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1PTZ 
_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]' 15798.477 2   1.15.1.1 'C6A, C111S, H43R' ? ? 
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    221 ?        ?                  ? ? 
# 
_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       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLRGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLRGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  ARG n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 SER n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_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.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1PTZ A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 1PTZ B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1PTZ ALA A 6   ? UNP P00441 CYS 6   'engineered mutation' 6   1 
1 1PTZ ARG A 43  ? UNP P00441 HIS 43  'engineered mutation' 43  2 
1 1PTZ SER A 111 ? UNP P00441 CYS 111 'engineered mutation' 111 3 
2 1PTZ ALA B 6   ? UNP P00441 CYS 6   'engineered mutation' 6   4 
2 1PTZ ARG B 43  ? UNP P00441 HIS 43  'engineered mutation' 43  5 
2 1PTZ SER B 111 ? 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 
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          1PTZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.98 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            294 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    'ammonium sulphate, sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           96 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   1999-03-23 
_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                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9780 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'NSLS BEAMLINE X12B' 
_diffrn_source.pdbx_synchrotron_site       NSLS 
_diffrn_source.pdbx_synchrotron_beamline   X12B 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9780 
# 
_reflns.entry_id                     1PTZ 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             29.05 
_reflns.d_resolution_high            1.80 
_reflns.number_obs                   25294 
_reflns.number_all                   25294 
_reflns.percent_possible_obs         97.4 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.057 
_reflns.pdbx_netI_over_sigmaI        15.4 
_reflns.B_iso_Wilson_estimate        17.6 
_reflns.pdbx_redundancy              3.15 
_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              1.86 
_reflns_shell.percent_possible_all   97.9 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.185 
_reflns_shell.meanI_over_sigI_obs    4.72 
_reflns_shell.pdbx_redundancy        3.13 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2524 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1PTZ 
_refine.ls_number_reflns_obs                     25294 
_refine.ls_number_reflns_all                     25294 
_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                             29.05 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    96.1 
_refine.ls_R_factor_obs                          0.186 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.186 
_refine.ls_R_factor_R_free                       0.215 
_refine.ls_R_factor_R_free_error                 0.004 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  2506 
_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                               24.7 
_refine.aniso_B[1][1]                            1.00 
_refine.aniso_B[2][2]                            5.67 
_refine.aniso_B[3][3]                            -6.67 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            4.55 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.378359 
_refine.solvent_model_param_bsol                 45.1901 
_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       'Engh & Huber' 
_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                        1PTZ 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_refine_analyze.Luzzati_sigma_a_obs             0.11 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.23 
_refine_analyze.Luzzati_sigma_a_free            0.15 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_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        2220 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_refine_hist.number_atoms_solvent             221 
_refine_hist.number_atoms_total               2450 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        29.05 
# 
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           0.024 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        1.3   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d 25.2  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d 0.67  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        1.21  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       1.82  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        2.21  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       3.25  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.d_res_high                       1.80 
_refine_ls_shell.d_res_low                        1.86 
_refine_ls_shell.number_reflns_R_work             1403 
_refine_ls_shell.R_factor_R_work                  0.23 
_refine_ls_shell.percent_reflns_obs               56.9 
_refine_ls_shell.R_factor_R_free                  0.283 
_refine_ls_shell.R_factor_R_free_error            0.025 
_refine_ls_shell.percent_reflns_R_free            8.4 
_refine_ls_shell.number_reflns_R_free             128 
_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                     ? 
# 
_struct.entry_id                  1PTZ 
_struct.title                     
'Crystal structure of the human CU, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (FALS) Mutant H43R' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1PTZ 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'SOD, FALS MUTANT, AMYOTROPHIC LATERAL SCLEROSIS, 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 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               'The biological assembly is a homodimer. The asymmetric unit contains one homodimer.' 
_struct_biol.pdbx_parent_biol_id   ? 
# 
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 CYS A 57  ? GLY A 61  ? CYS A 57  GLY A 61  5 ? 5 
HELX_P HELX_P2 2 GLU A 133 ? GLY A 138 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3 3 ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4 4 GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 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 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc1  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 46  A CU1 200 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
metalc2  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 48  A CU1 200 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc3  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  201 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc4  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  201 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc5  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  201 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc6  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  201 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc7  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 C CU1 .   CU ? ? A HIS 120 A CU1 200 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc8  metalc ? ? B HIS 46  ND1 ? ? ? 1_555 F CU1 .   CU ? ? B HIS 46  B CU1 200 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc9  metalc ? ? B HIS 48  NE2 ? ? ? 1_555 F CU1 .   CU ? ? B HIS 48  B CU1 200 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc10 metalc ? ? B HIS 63  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 63  B ZN  201 1_555 ? ? ? ? ? ? ? 1.979 ? ? 
metalc11 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 71  B ZN  201 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc12 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? B HIS 80  B ZN  201 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc13 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 G ZN  .   ZN ? ? B ASP 83  B ZN  201 1_555 ? ? ? ? ? ? ? 1.943 ? ? 
metalc14 metalc ? ? B ASP 83  OD2 ? ? ? 1_555 G ZN  .   ZN ? ? B ASP 83  B ZN  201 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc15 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 F CU1 .   CU ? ? B HIS 120 B CU1 200 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
# 
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 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
A 4 LYS A 3   ? LEU A 8   ? LYS A 3   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLU B 21  ? GLN B 15  GLU B 21  
C 4 LYS B 3   ? LEU B 8   ? LYS B 3   LEU B 8   
C 5 GLY B 150 ? GLN B 153 ? GLY B 150 GLN B 153 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ILE A 99  ? O ILE A 99  N VAL A 31  ? N VAL A 31  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ILE B 99  ? O ILE B 99  N VAL B 31  ? N VAL B 31  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O GLY B 16  ? O GLY B 16  N LEU B 8   ? N LEU B 8   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
D 3 4 N LEU B 117 ? N LEU B 117 O GLY B 147 ? 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 200 ? 4 'BINDING SITE FOR RESIDUE CU1 A 200' 
AC2 Software A ZN  201 ? 4 'BINDING SITE FOR RESIDUE ZN A 201'  
AC3 Software B CU1 200 ? 4 'BINDING SITE FOR RESIDUE CU1 B 200' 
AC4 Software B ZN  201 ? 4 'BINDING SITE FOR RESIDUE ZN B 201'  
AC5 Software A SO4 600 ? 3 'BINDING SITE FOR RESIDUE SO4 A 600' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 46  ? HIS A 46  . ? 1_555 ? 
2  AC1 4 HIS A 48  ? HIS A 48  . ? 1_555 ? 
3  AC1 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
4  AC1 4 HIS A 120 ? HIS A 120 . ? 1_555 ? 
5  AC2 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
6  AC2 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
7  AC2 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
8  AC2 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
9  AC3 4 HIS B 46  ? HIS B 46  . ? 1_555 ? 
10 AC3 4 HIS B 48  ? HIS B 48  . ? 1_555 ? 
11 AC3 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
12 AC3 4 HIS B 120 ? HIS B 120 . ? 1_555 ? 
13 AC4 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
14 AC4 4 HIS B 71  ? HIS B 71  . ? 1_555 ? 
15 AC4 4 HIS B 80  ? HIS B 80  . ? 1_555 ? 
16 AC4 4 ASP B 83  ? ASP B 83  . ? 1_555 ? 
17 AC5 3 ASP A 76  ? ASP A 76  . ? 1_555 ? 
18 AC5 3 GLU A 77  ? GLU A 77  . ? 1_555 ? 
19 AC5 3 LYS B 75  ? LYS B 75  . ? 1_554 ? 
# 
_database_PDB_matrix.entry_id          1PTZ 
_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                    1PTZ 
_atom_sites.fract_transf_matrix[1][1]   0.008993 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001262 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021042 
_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]   0.018019 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 27.686 -6.987  5.722   1.00 38.29 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 26.906 -5.716  5.746   1.00 37.04 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 26.421 -5.365  4.344   1.00 35.37 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 26.800 -6.011  3.370   1.00 36.65 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 27.771 -4.587  6.294   1.00 37.67 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 25.575 -4.344  4.253   1.00 32.91 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 25.046 -3.900  2.970   1.00 31.03 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 25.659 -2.557  2.588   1.00 27.71 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 25.656 -2.174  1.422   1.00 25.19 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 23.513 -3.749  3.017   1.00 33.14 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 23.039 -3.290  1.745   1.00 37.69 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 23.105 -2.755  4.089   1.00 33.76 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 26.179 -1.846  3.582   1.00 25.66 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 26.804 -0.544  3.358   1.00 23.62 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 28.063 -0.433  4.204   1.00 21.71 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 28.112 -0.931  5.326   1.00 19.63 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 25.850 0.587   3.739   1.00 26.16 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 24.587 0.682   2.897   1.00 28.63 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 23.660 1.754   3.468   1.00 33.26 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 22.372 1.896   2.664   1.00 35.55 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 22.614 2.452   1.306   1.00 38.35 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 29.080 0.221   3.657   1.00 19.88 ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 30.339 0.403   4.363   1.00 19.69 ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 30.927 1.742   3.954   1.00 18.16 ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 30.472 2.365   2.988   1.00 18.14 ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 31.307 -0.729  4.023   1.00 20.11 ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 31.936 2.184   4.691   1.00 18.44 ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 32.570 3.459   4.400   1.00 18.26 ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 34.016 3.465   4.867   1.00 19.04 ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 34.382 2.780   5.827   1.00 18.98 ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 31.827 4.622   5.096   1.00 18.54 ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 31.894 4.457   6.607   1.00 16.91 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 32.437 5.956   4.678   1.00 19.42 ? 5   VAL A CG2 1 
ATOM   34   N  N   . ALA A 1 6   ? 34.837 4.240   4.172   1.00 18.19 ? 6   ALA A N   1 
ATOM   35   C  CA  . ALA A 1 6   ? 36.241 4.369   4.527   1.00 17.86 ? 6   ALA A CA  1 
ATOM   36   C  C   . ALA A 1 6   ? 36.599 5.849   4.476   1.00 18.69 ? 6   ALA A C   1 
ATOM   37   O  O   . ALA A 1 6   ? 36.427 6.493   3.443   1.00 19.93 ? 6   ALA A O   1 
ATOM   38   C  CB  . ALA A 1 6   ? 37.108 3.588   3.545   1.00 18.62 ? 6   ALA A CB  1 
ATOM   39   N  N   . VAL A 1 7   ? 37.058 6.390   5.599   1.00 18.61 ? 7   VAL A N   1 
ATOM   40   C  CA  . VAL A 1 7   ? 37.469 7.785   5.648   1.00 18.00 ? 7   VAL A CA  1 
ATOM   41   C  C   . VAL A 1 7   ? 38.976 7.776   5.439   1.00 17.78 ? 7   VAL A C   1 
ATOM   42   O  O   . VAL A 1 7   ? 39.731 7.319   6.299   1.00 19.71 ? 7   VAL A O   1 
ATOM   43   C  CB  . VAL A 1 7   ? 37.135 8.434   7.003   1.00 18.91 ? 7   VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 7   ? 37.630 9.873   7.021   1.00 19.18 ? 7   VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 7   ? 35.624 8.401   7.232   1.00 21.22 ? 7   VAL A CG2 1 
ATOM   46   N  N   . LEU A 1 8   ? 39.406 8.267   4.284   1.00 17.47 ? 8   LEU A N   1 
ATOM   47   C  CA  . LEU A 1 8   ? 40.818 8.297   3.933   1.00 19.04 ? 8   LEU A CA  1 
ATOM   48   C  C   . LEU A 1 8   ? 41.575 9.490   4.501   1.00 20.14 ? 8   LEU A C   1 
ATOM   49   O  O   . LEU A 1 8   ? 41.185 10.644  4.305   1.00 19.02 ? 8   LEU A O   1 
ATOM   50   C  CB  . LEU A 1 8   ? 40.981 8.286   2.408   1.00 20.58 ? 8   LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 8   ? 40.313 7.149   1.628   1.00 20.09 ? 8   LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 8   ? 40.516 7.354   0.138   1.00 21.88 ? 8   LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 8   ? 40.900 5.823   2.064   1.00 22.75 ? 8   LEU A CD2 1 
ATOM   54   N  N   . LYS A 1 9   ? 42.665 9.191   5.205   1.00 19.53 ? 9   LYS A N   1 
ATOM   55   C  CA  . LYS A 1 9   ? 43.530 10.210  5.796   1.00 21.67 ? 9   LYS A CA  1 
ATOM   56   C  C   . LYS A 1 9   ? 44.973 9.710   5.750   1.00 20.53 ? 9   LYS A C   1 
ATOM   57   O  O   . LYS A 1 9   ? 45.221 8.505   5.811   1.00 19.90 ? 9   LYS A O   1 
ATOM   58   C  CB  . LYS A 1 9   ? 43.139 10.483  7.254   1.00 23.82 ? 9   LYS A CB  1 
ATOM   59   C  CG  . LYS A 1 9   ? 41.687 10.888  7.442   1.00 29.05 ? 9   LYS A CG  1 
ATOM   60   C  CD  . LYS A 1 9   ? 41.457 11.583  8.780   1.00 34.00 ? 9   LYS A CD  1 
ATOM   61   C  CE  . LYS A 1 9   ? 40.020 12.081  8.897   1.00 35.59 ? 9   LYS A CE  1 
ATOM   62   N  NZ  . LYS A 1 9   ? 39.819 12.931  10.101  1.00 40.69 ? 9   LYS A NZ  1 
ATOM   63   N  N   . GLY A 1 10  ? 45.918 10.636  5.638   1.00 21.39 ? 10  GLY A N   1 
ATOM   64   C  CA  . GLY A 1 10  ? 47.324 10.261  5.600   1.00 23.06 ? 10  GLY A CA  1 
ATOM   65   C  C   . GLY A 1 10  ? 48.156 11.308  6.316   1.00 24.39 ? 10  GLY A C   1 
ATOM   66   O  O   . GLY A 1 10  ? 47.624 12.074  7.117   1.00 24.13 ? 10  GLY A O   1 
ATOM   67   N  N   . ASP A 1 11  ? 49.454 11.351  6.043   1.00 25.41 ? 11  ASP A N   1 
ATOM   68   C  CA  . ASP A 1 11  ? 50.305 12.344  6.689   1.00 29.57 ? 11  ASP A CA  1 
ATOM   69   C  C   . ASP A 1 11  ? 50.316 13.649  5.901   1.00 29.81 ? 11  ASP A C   1 
ATOM   70   O  O   . ASP A 1 11  ? 50.765 14.679  6.405   1.00 31.23 ? 11  ASP A O   1 
ATOM   71   C  CB  . ASP A 1 11  ? 51.736 11.824  6.832   1.00 31.82 ? 11  ASP A CB  1 
ATOM   72   C  CG  . ASP A 1 11  ? 51.852 10.701  7.843   1.00 33.98 ? 11  ASP A CG  1 
ATOM   73   O  OD1 . ASP A 1 11  ? 51.191 10.784  8.902   1.00 35.16 ? 11  ASP A OD1 1 
ATOM   74   O  OD2 . ASP A 1 11  ? 52.614 9.746   7.585   1.00 36.87 ? 11  ASP A OD2 1 
ATOM   75   N  N   . GLY A 1 12  ? 49.813 13.599  4.669   1.00 28.95 ? 12  GLY A N   1 
ATOM   76   C  CA  . GLY A 1 12  ? 49.785 14.781  3.825   1.00 27.36 ? 12  GLY A CA  1 
ATOM   77   C  C   . GLY A 1 12  ? 48.410 15.396  3.638   1.00 26.72 ? 12  GLY A C   1 
ATOM   78   O  O   . GLY A 1 12  ? 47.537 15.240  4.487   1.00 27.35 ? 12  GLY A O   1 
ATOM   79   N  N   . PRO A 1 13  ? 48.184 16.104  2.523   1.00 27.91 ? 13  PRO A N   1 
ATOM   80   C  CA  . PRO A 1 13  ? 46.895 16.744  2.247   1.00 27.29 ? 13  PRO A CA  1 
ATOM   81   C  C   . PRO A 1 13  ? 45.818 15.845  1.639   1.00 27.19 ? 13  PRO A C   1 
ATOM   82   O  O   . PRO A 1 13  ? 44.661 16.250  1.531   1.00 25.39 ? 13  PRO A O   1 
ATOM   83   C  CB  . PRO A 1 13  ? 47.282 17.874  1.309   1.00 28.81 ? 13  PRO A CB  1 
ATOM   84   C  CG  . PRO A 1 13  ? 48.355 17.234  0.487   1.00 29.26 ? 13  PRO A CG  1 
ATOM   85   C  CD  . PRO A 1 13  ? 49.193 16.517  1.530   1.00 28.18 ? 13  PRO A CD  1 
ATOM   86   N  N   . VAL A 1 14  ? 46.187 14.633  1.241   1.00 24.41 ? 14  VAL A N   1 
ATOM   87   C  CA  . VAL A 1 14  ? 45.214 13.730  0.634   1.00 23.28 ? 14  VAL A CA  1 
ATOM   88   C  C   . VAL A 1 14  ? 44.174 13.221  1.629   1.00 24.07 ? 14  VAL A C   1 
ATOM   89   O  O   . VAL A 1 14  ? 44.512 12.633  2.660   1.00 23.45 ? 14  VAL A O   1 
ATOM   90   C  CB  . VAL A 1 14  ? 45.900 12.510  -0.018  1.00 22.74 ? 14  VAL A CB  1 
ATOM   91   C  CG1 . VAL A 1 14  ? 44.850 11.592  -0.620  1.00 20.69 ? 14  VAL A CG1 1 
ATOM   92   C  CG2 . VAL A 1 14  ? 46.875 12.971  -1.095  1.00 24.21 ? 14  VAL A CG2 1 
ATOM   93   N  N   . GLN A 1 15  ? 42.903 13.440  1.306   1.00 23.03 ? 15  GLN A N   1 
ATOM   94   C  CA  . GLN A 1 15  ? 41.817 12.993  2.162   1.00 23.68 ? 15  GLN A CA  1 
ATOM   95   C  C   . GLN A 1 15  ? 40.525 12.844  1.379   1.00 23.35 ? 15  GLN A C   1 
ATOM   96   O  O   . GLN A 1 15  ? 40.367 13.422  0.305   1.00 22.81 ? 15  GLN A O   1 
ATOM   97   C  CB  . GLN A 1 15  ? 41.608 13.968  3.323   1.00 27.18 ? 15  GLN A CB  1 
ATOM   98   C  CG  . GLN A 1 15  ? 41.316 15.398  2.909   1.00 31.60 ? 15  GLN A CG  1 
ATOM   99   C  CD  . GLN A 1 15  ? 41.072 16.302  4.107   1.00 35.68 ? 15  GLN A CD  1 
ATOM   100  O  OE1 . GLN A 1 15  ? 40.073 16.160  4.811   1.00 39.91 ? 15  GLN A OE1 1 
ATOM   101  N  NE2 . GLN A 1 15  ? 41.990 17.231  4.348   1.00 38.02 ? 15  GLN A NE2 1 
ATOM   102  N  N   . GLY A 1 16  ? 39.604 12.058  1.924   1.00 22.79 ? 16  GLY A N   1 
ATOM   103  C  CA  . GLY A 1 16  ? 38.335 11.847  1.260   1.00 23.44 ? 16  GLY A CA  1 
ATOM   104  C  C   . GLY A 1 16  ? 37.535 10.752  1.932   1.00 23.19 ? 16  GLY A C   1 
ATOM   105  O  O   . GLY A 1 16  ? 37.964 10.188  2.939   1.00 22.10 ? 16  GLY A O   1 
ATOM   106  N  N   . ILE A 1 17  ? 36.365 10.462  1.374   1.00 22.35 ? 17  ILE A N   1 
ATOM   107  C  CA  . ILE A 1 17  ? 35.484 9.428   1.906   1.00 20.70 ? 17  ILE A CA  1 
ATOM   108  C  C   . ILE A 1 17  ? 34.998 8.564   0.754   1.00 21.09 ? 17  ILE A C   1 
ATOM   109  O  O   . ILE A 1 17  ? 34.589 9.077   -0.288  1.00 20.92 ? 17  ILE A O   1 
ATOM   110  C  CB  . ILE A 1 17  ? 34.242 10.041  2.635   1.00 23.25 ? 17  ILE A CB  1 
ATOM   111  C  CG1 . ILE A 1 17  ? 34.574 10.372  4.094   1.00 26.03 ? 17  ILE A CG1 1 
ATOM   112  C  CG2 . ILE A 1 17  ? 33.103 9.043   2.661   1.00 23.09 ? 17  ILE A CG2 1 
ATOM   113  C  CD1 . ILE A 1 17  ? 35.727 11.288  4.283   1.00 29.19 ? 17  ILE A CD1 1 
ATOM   114  N  N   . ILE A 1 18  ? 35.061 7.250   0.938   1.00 19.12 ? 18  ILE A N   1 
ATOM   115  C  CA  . ILE A 1 18  ? 34.601 6.321   -0.083  1.00 18.00 ? 18  ILE A CA  1 
ATOM   116  C  C   . ILE A 1 18  ? 33.508 5.445   0.515   1.00 19.11 ? 18  ILE A C   1 
ATOM   117  O  O   . ILE A 1 18  ? 33.687 4.847   1.573   1.00 18.08 ? 18  ILE A O   1 
ATOM   118  C  CB  . ILE A 1 18  ? 35.752 5.440   -0.599  1.00 17.60 ? 18  ILE A CB  1 
ATOM   119  C  CG1 . ILE A 1 18  ? 36.769 6.314   -1.337  1.00 18.74 ? 18  ILE A CG1 1 
ATOM   120  C  CG2 . ILE A 1 18  ? 35.221 4.358   -1.528  1.00 17.25 ? 18  ILE A CG2 1 
ATOM   121  C  CD1 . ILE A 1 18  ? 36.238 6.934   -2.617  1.00 19.79 ? 18  ILE A CD1 1 
ATOM   122  N  N   . ASN A 1 19  ? 32.376 5.389   -0.177  1.00 19.61 ? 19  ASN A N   1 
ATOM   123  C  CA  . ASN A 1 19  ? 31.227 4.612   0.263   1.00 19.59 ? 19  ASN A CA  1 
ATOM   124  C  C   . ASN A 1 19  ? 31.143 3.289   -0.484  1.00 18.85 ? 19  ASN A C   1 
ATOM   125  O  O   . ASN A 1 19  ? 31.519 3.206   -1.650  1.00 19.33 ? 19  ASN A O   1 
ATOM   126  C  CB  . ASN A 1 19  ? 29.950 5.411   0.011   1.00 21.18 ? 19  ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 19  ? 30.017 6.810   0.586   1.00 24.65 ? 19  ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 19  ? 29.942 6.999   1.803   1.00 25.63 ? 19  ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 19  ? 30.177 7.803   -0.288  1.00 22.63 ? 19  ASN A ND2 1 
ATOM   130  N  N   . PHE A 1 20  ? 30.640 2.262   0.195   1.00 18.72 ? 20  PHE A N   1 
ATOM   131  C  CA  . PHE A 1 20  ? 30.473 0.937   -0.399  1.00 18.66 ? 20  PHE A CA  1 
ATOM   132  C  C   . PHE A 1 20  ? 29.016 0.531   -0.217  1.00 18.45 ? 20  PHE A C   1 
ATOM   133  O  O   . PHE A 1 20  ? 28.421 0.786   0.831   1.00 18.01 ? 20  PHE A O   1 
ATOM   134  C  CB  . PHE A 1 20  ? 31.358 -0.093  0.307   1.00 18.66 ? 20  PHE A CB  1 
ATOM   135  C  CG  . PHE A 1 20  ? 32.830 0.168   0.173   1.00 16.96 ? 20  PHE A CG  1 
ATOM   136  C  CD1 . PHE A 1 20  ? 33.568 -0.440  -0.839  1.00 18.25 ? 20  PHE A CD1 1 
ATOM   137  C  CD2 . PHE A 1 20  ? 33.485 0.996   1.075   1.00 18.68 ? 20  PHE A CD2 1 
ATOM   138  C  CE1 . PHE A 1 20  ? 34.942 -0.233  -0.949  1.00 16.38 ? 20  PHE A CE1 1 
ATOM   139  C  CE2 . PHE A 1 20  ? 34.864 1.213   0.975   1.00 17.10 ? 20  PHE A CE2 1 
ATOM   140  C  CZ  . PHE A 1 20  ? 35.591 0.596   -0.038  1.00 17.23 ? 20  PHE A CZ  1 
ATOM   141  N  N   . GLU A 1 21  ? 28.447 -0.103  -1.234  1.00 20.02 ? 21  GLU A N   1 
ATOM   142  C  CA  . GLU A 1 21  ? 27.061 -0.544  -1.166  1.00 21.14 ? 21  GLU A CA  1 
ATOM   143  C  C   . GLU A 1 21  ? 26.914 -1.887  -1.866  1.00 20.92 ? 21  GLU A C   1 
ATOM   144  O  O   . GLU A 1 21  ? 27.331 -2.054  -3.011  1.00 18.10 ? 21  GLU A O   1 
ATOM   145  C  CB  . GLU A 1 21  ? 26.152 0.501   -1.819  1.00 25.86 ? 21  GLU A CB  1 
ATOM   146  C  CG  . GLU A 1 21  ? 24.672 0.157   -1.831  1.00 32.43 ? 21  GLU A CG  1 
ATOM   147  C  CD  . GLU A 1 21  ? 23.819 1.328   -2.294  1.00 37.27 ? 21  GLU A CD  1 
ATOM   148  O  OE1 . GLU A 1 21  ? 23.323 2.083   -1.432  1.00 41.17 ? 21  GLU A OE1 1 
ATOM   149  O  OE2 . GLU A 1 21  ? 23.660 1.507   -3.520  1.00 40.08 ? 21  GLU A OE2 1 
ATOM   150  N  N   . GLN A 1 22  ? 26.344 -2.851  -1.155  1.00 21.45 ? 22  GLN A N   1 
ATOM   151  C  CA  . GLN A 1 22  ? 26.129 -4.185  -1.703  1.00 22.44 ? 22  GLN A CA  1 
ATOM   152  C  C   . GLN A 1 22  ? 24.725 -4.600  -1.293  1.00 23.72 ? 22  GLN A C   1 
ATOM   153  O  O   . GLN A 1 22  ? 24.507 -5.114  -0.193  1.00 23.26 ? 22  GLN A O   1 
ATOM   154  C  CB  . GLN A 1 22  ? 27.174 -5.158  -1.152  1.00 22.71 ? 22  GLN A CB  1 
ATOM   155  C  CG  . GLN A 1 22  ? 27.133 -6.556  -1.766  1.00 24.20 ? 22  GLN A CG  1 
ATOM   156  C  CD  . GLN A 1 22  ? 28.226 -7.455  -1.214  1.00 22.85 ? 22  GLN A CD  1 
ATOM   157  O  OE1 . GLN A 1 22  ? 28.446 -7.505  -0.006  1.00 24.10 ? 22  GLN A OE1 1 
ATOM   158  N  NE2 . GLN A 1 22  ? 28.913 -8.173  -2.098  1.00 24.78 ? 22  GLN A NE2 1 
ATOM   159  N  N   . LYS A 1 23  ? 23.776 -4.361  -2.190  1.00 25.73 ? 23  LYS A N   1 
ATOM   160  C  CA  . LYS A 1 23  ? 22.376 -4.663  -1.925  1.00 29.82 ? 23  LYS A CA  1 
ATOM   161  C  C   . LYS A 1 23  ? 22.073 -6.152  -1.826  1.00 29.41 ? 23  LYS A C   1 
ATOM   162  O  O   . LYS A 1 23  ? 21.054 -6.542  -1.250  1.00 29.74 ? 23  LYS A O   1 
ATOM   163  C  CB  . LYS A 1 23  ? 21.490 -4.058  -3.013  1.00 33.39 ? 23  LYS A CB  1 
ATOM   164  C  CG  . LYS A 1 23  ? 21.757 -2.593  -3.333  1.00 38.07 ? 23  LYS A CG  1 
ATOM   165  C  CD  . LYS A 1 23  ? 23.086 -2.447  -4.050  1.00 41.10 ? 23  LYS A CD  1 
ATOM   166  C  CE  . LYS A 1 23  ? 23.323 -1.037  -4.556  1.00 43.10 ? 23  LYS A CE  1 
ATOM   167  N  NZ  . LYS A 1 23  ? 24.706 -0.876  -5.095  1.00 43.54 ? 23  LYS A NZ  1 
ATOM   168  N  N   . GLU A 1 24  ? 22.942 -6.988  -2.388  1.00 29.39 ? 24  GLU A N   1 
ATOM   169  C  CA  . GLU A 1 24  ? 22.706 -8.427  -2.350  1.00 31.34 ? 24  GLU A CA  1 
ATOM   170  C  C   . GLU A 1 24  ? 23.914 -9.219  -1.846  1.00 29.72 ? 24  GLU A C   1 
ATOM   171  O  O   . GLU A 1 24  ? 25.057 -8.863  -2.116  1.00 30.46 ? 24  GLU A O   1 
ATOM   172  C  CB  . GLU A 1 24  ? 22.289 -8.915  -3.741  1.00 34.34 ? 24  GLU A CB  1 
ATOM   173  C  CG  . GLU A 1 24  ? 20.934 -9.618  -3.747  1.00 41.15 ? 24  GLU A CG  1 
ATOM   174  C  CD  . GLU A 1 24  ? 19.782 -8.718  -3.316  1.00 44.55 ? 24  GLU A CD  1 
ATOM   175  O  OE1 . GLU A 1 24  ? 18.926 -9.182  -2.528  1.00 46.66 ? 24  GLU A OE1 1 
ATOM   176  O  OE2 . GLU A 1 24  ? 19.725 -7.556  -3.774  1.00 46.96 ? 24  GLU A OE2 1 
ATOM   177  N  N   . SER A 1 25  ? 23.650 -10.293 -1.107  1.00 29.90 ? 25  SER A N   1 
ATOM   178  C  CA  . SER A 1 25  ? 24.709 -11.134 -0.555  1.00 29.05 ? 25  SER A CA  1 
ATOM   179  C  C   . SER A 1 25  ? 25.673 -11.599 -1.646  1.00 29.65 ? 25  SER A C   1 
ATOM   180  O  O   . SER A 1 25  ? 25.276 -12.261 -2.609  1.00 28.41 ? 25  SER A O   1 
ATOM   181  C  CB  . SER A 1 25  ? 24.103 -12.348 0.158   1.00 30.48 ? 25  SER A CB  1 
ATOM   182  O  OG  . SER A 1 25  ? 25.096 -13.077 0.866   1.00 31.25 ? 25  SER A OG  1 
ATOM   183  N  N   . ASN A 1 26  ? 26.944 -11.248 -1.476  1.00 29.11 ? 26  ASN A N   1 
ATOM   184  C  CA  . ASN A 1 26  ? 28.000 -11.583 -2.427  1.00 30.38 ? 26  ASN A CA  1 
ATOM   185  C  C   . ASN A 1 26  ? 27.686 -11.138 -3.855  1.00 28.92 ? 26  ASN A C   1 
ATOM   186  O  O   . ASN A 1 26  ? 28.139 -11.749 -4.825  1.00 28.78 ? 26  ASN A O   1 
ATOM   187  C  CB  . ASN A 1 26  ? 28.306 -13.085 -2.388  1.00 33.73 ? 26  ASN A CB  1 
ATOM   188  C  CG  . ASN A 1 26  ? 29.173 -13.470 -1.195  1.00 35.99 ? 26  ASN A CG  1 
ATOM   189  O  OD1 . ASN A 1 26  ? 29.497 -14.642 -0.996  1.00 38.23 ? 26  ASN A OD1 1 
ATOM   190  N  ND2 . ASN A 1 26  ? 29.558 -12.477 -0.397  1.00 34.55 ? 26  ASN A ND2 1 
ATOM   191  N  N   . GLY A 1 27  ? 26.917 -10.060 -3.972  1.00 27.09 ? 27  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 27  ? 26.573 -9.524  -5.276  1.00 23.74 ? 27  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 27  ? 27.531 -8.397  -5.614  1.00 24.29 ? 27  GLY A C   1 
ATOM   194  O  O   . GLY A 1 27  ? 28.493 -8.169  -4.873  1.00 21.23 ? 27  GLY A O   1 
ATOM   195  N  N   . PRO A 1 28  ? 27.307 -7.668  -6.717  1.00 24.34 ? 28  PRO A N   1 
ATOM   196  C  CA  . PRO A 1 28  ? 28.226 -6.578  -7.055  1.00 24.01 ? 28  PRO A CA  1 
ATOM   197  C  C   . PRO A 1 28  ? 28.269 -5.477  -6.001  1.00 23.92 ? 28  PRO A C   1 
ATOM   198  O  O   . PRO A 1 28  ? 27.273 -5.207  -5.327  1.00 22.11 ? 28  PRO A O   1 
ATOM   199  C  CB  . PRO A 1 28  ? 27.705 -6.087  -8.405  1.00 25.23 ? 28  PRO A CB  1 
ATOM   200  C  CG  . PRO A 1 28  ? 26.250 -6.424  -8.359  1.00 28.97 ? 28  PRO A CG  1 
ATOM   201  C  CD  . PRO A 1 28  ? 26.249 -7.797  -7.734  1.00 25.11 ? 28  PRO A CD  1 
ATOM   202  N  N   . VAL A 1 29  ? 29.432 -4.849  -5.861  1.00 21.03 ? 29  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 29  ? 29.609 -3.780  -4.888  1.00 20.29 ? 29  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 29  ? 29.844 -2.440  -5.574  1.00 20.59 ? 29  VAL A C   1 
ATOM   205  O  O   . VAL A 1 29  ? 30.725 -2.316  -6.421  1.00 20.62 ? 29  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 29  ? 30.819 -4.058  -3.958  1.00 18.52 ? 29  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 29  ? 30.958 -2.934  -2.935  1.00 20.60 ? 29  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 29  ? 30.644 -5.400  -3.253  1.00 20.80 ? 29  VAL A CG2 1 
ATOM   209  N  N   . LYS A 1 30  ? 29.045 -1.442  -5.215  1.00 20.75 ? 30  LYS A N   1 
ATOM   210  C  CA  . LYS A 1 30  ? 29.210 -0.109  -5.776  1.00 22.13 ? 30  LYS A CA  1 
ATOM   211  C  C   . LYS A 1 30  ? 30.156 0.629   -4.838  1.00 20.55 ? 30  LYS A C   1 
ATOM   212  O  O   . LYS A 1 30  ? 29.984 0.597   -3.622  1.00 19.41 ? 30  LYS A O   1 
ATOM   213  C  CB  . LYS A 1 30  ? 27.867 0.622   -5.856  1.00 25.21 ? 30  LYS A CB  1 
ATOM   214  C  CG  . LYS A 1 30  ? 26.879 -0.023  -6.815  1.00 32.99 ? 30  LYS A CG  1 
ATOM   215  C  CD  . LYS A 1 30  ? 26.484 0.920   -7.951  1.00 39.05 ? 30  LYS A CD  1 
ATOM   216  C  CE  . LYS A 1 30  ? 27.687 1.348   -8.793  1.00 42.30 ? 30  LYS A CE  1 
ATOM   217  N  NZ  . LYS A 1 30  ? 27.273 2.117   -10.006 1.00 42.59 ? 30  LYS A NZ  1 
ATOM   218  N  N   . VAL A 1 31  ? 31.161 1.274   -5.418  1.00 18.93 ? 31  VAL A N   1 
ATOM   219  C  CA  . VAL A 1 31  ? 32.167 2.018   -4.668  1.00 19.10 ? 31  VAL A CA  1 
ATOM   220  C  C   . VAL A 1 31  ? 32.169 3.446   -5.211  1.00 20.11 ? 31  VAL A C   1 
ATOM   221  O  O   . VAL A 1 31  ? 32.488 3.662   -6.378  1.00 19.35 ? 31  VAL A O   1 
ATOM   222  C  CB  . VAL A 1 31  ? 33.563 1.399   -4.887  1.00 19.10 ? 31  VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 31  ? 34.590 2.071   -3.990  1.00 18.74 ? 31  VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 31  ? 33.503 -0.102  -4.628  1.00 19.17 ? 31  VAL A CG2 1 
ATOM   225  N  N   . TRP A 1 32  ? 31.820 4.417   -4.372  1.00 18.82 ? 32  TRP A N   1 
ATOM   226  C  CA  . TRP A 1 32  ? 31.771 5.804   -4.828  1.00 20.83 ? 32  TRP A CA  1 
ATOM   227  C  C   . TRP A 1 32  ? 32.120 6.793   -3.723  1.00 19.84 ? 32  TRP A C   1 
ATOM   228  O  O   . TRP A 1 32  ? 31.918 6.525   -2.541  1.00 19.56 ? 32  TRP A O   1 
ATOM   229  C  CB  . TRP A 1 32  ? 30.372 6.124   -5.368  1.00 21.43 ? 32  TRP A CB  1 
ATOM   230  C  CG  . TRP A 1 32  ? 29.387 6.479   -4.291  1.00 26.69 ? 32  TRP A CG  1 
ATOM   231  C  CD1 . TRP A 1 32  ? 29.088 7.734   -3.832  1.00 25.72 ? 32  TRP A CD1 1 
ATOM   232  C  CD2 . TRP A 1 32  ? 28.615 5.569   -3.500  1.00 27.36 ? 32  TRP A CD2 1 
ATOM   233  N  NE1 . TRP A 1 32  ? 28.178 7.658   -2.805  1.00 31.31 ? 32  TRP A NE1 1 
ATOM   234  C  CE2 . TRP A 1 32  ? 27.871 6.342   -2.581  1.00 29.56 ? 32  TRP A CE2 1 
ATOM   235  C  CE3 . TRP A 1 32  ? 28.480 4.176   -3.477  1.00 29.01 ? 32  TRP A CE3 1 
ATOM   236  C  CZ2 . TRP A 1 32  ? 27.003 5.767   -1.646  1.00 33.17 ? 32  TRP A CZ2 1 
ATOM   237  C  CZ3 . TRP A 1 32  ? 27.617 3.602   -2.546  1.00 32.30 ? 32  TRP A CZ3 1 
ATOM   238  C  CH2 . TRP A 1 32  ? 26.889 4.399   -1.643  1.00 32.54 ? 32  TRP A CH2 1 
ATOM   239  N  N   . GLY A 1 33  ? 32.634 7.946   -4.129  1.00 19.41 ? 33  GLY A N   1 
ATOM   240  C  CA  . GLY A 1 33  ? 33.004 8.974   -3.180  1.00 18.57 ? 33  GLY A CA  1 
ATOM   241  C  C   . GLY A 1 33  ? 33.931 9.952   -3.868  1.00 18.99 ? 33  GLY A C   1 
ATOM   242  O  O   . GLY A 1 33  ? 33.931 10.056  -5.095  1.00 18.39 ? 33  GLY A O   1 
ATOM   243  N  N   . SER A 1 34  ? 34.722 10.674  -3.087  1.00 18.62 ? 34  SER A N   1 
ATOM   244  C  CA  . SER A 1 34  ? 35.660 11.626  -3.659  1.00 20.24 ? 34  SER A CA  1 
ATOM   245  C  C   . SER A 1 34  ? 36.893 11.711  -2.782  1.00 20.84 ? 34  SER A C   1 
ATOM   246  O  O   . SER A 1 34  ? 36.817 11.526  -1.569  1.00 22.27 ? 34  SER A O   1 
ATOM   247  C  CB  . SER A 1 34  ? 35.014 13.006  -3.780  1.00 21.62 ? 34  SER A CB  1 
ATOM   248  O  OG  . SER A 1 34  ? 34.536 13.445  -2.523  1.00 26.72 ? 34  SER A OG  1 
ATOM   249  N  N   . ILE A 1 35  ? 38.029 11.978  -3.413  1.00 21.17 ? 35  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 35  ? 39.306 12.100  -2.719  1.00 20.49 ? 35  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 35  ? 39.924 13.397  -3.230  1.00 22.33 ? 35  ILE A C   1 
ATOM   252  O  O   . ILE A 1 35  ? 39.944 13.635  -4.434  1.00 23.30 ? 35  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 35  ? 40.249 10.933  -3.082  1.00 20.45 ? 35  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 35  ? 39.556 9.597   -2.812  1.00 18.44 ? 35  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 35  ? 41.531 11.022  -2.269  1.00 17.55 ? 35  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 35  ? 40.376 8.402   -3.245  1.00 20.66 ? 35  ILE A CD1 1 
ATOM   257  N  N   . LYS A 1 36  ? 40.413 14.237  -2.325  1.00 23.65 ? 36  LYS A N   1 
ATOM   258  C  CA  . LYS A 1 36  ? 41.023 15.498  -2.731  1.00 24.52 ? 36  LYS A CA  1 
ATOM   259  C  C   . LYS A 1 36  ? 42.475 15.582  -2.269  1.00 25.81 ? 36  LYS A C   1 
ATOM   260  O  O   . LYS A 1 36  ? 42.936 14.755  -1.481  1.00 23.70 ? 36  LYS A O   1 
ATOM   261  C  CB  . LYS A 1 36  ? 40.230 16.676  -2.159  1.00 27.47 ? 36  LYS A CB  1 
ATOM   262  C  CG  . LYS A 1 36  ? 40.218 16.747  -0.643  1.00 30.84 ? 36  LYS A CG  1 
ATOM   263  C  CD  . LYS A 1 36  ? 39.455 17.979  -0.161  1.00 35.94 ? 36  LYS A CD  1 
ATOM   264  C  CE  . LYS A 1 36  ? 39.419 18.058  1.359   1.00 39.55 ? 36  LYS A CE  1 
ATOM   265  N  NZ  . LYS A 1 36  ? 38.730 16.879  1.965   1.00 42.76 ? 36  LYS A NZ  1 
ATOM   266  N  N   . GLY A 1 37  ? 43.193 16.584  -2.768  1.00 25.75 ? 37  GLY A N   1 
ATOM   267  C  CA  . GLY A 1 37  ? 44.585 16.755  -2.392  1.00 25.89 ? 37  GLY A CA  1 
ATOM   268  C  C   . GLY A 1 37  ? 45.544 15.911  -3.211  1.00 24.73 ? 37  GLY A C   1 
ATOM   269  O  O   . GLY A 1 37  ? 46.728 15.812  -2.886  1.00 24.74 ? 37  GLY A O   1 
ATOM   270  N  N   . LEU A 1 38  ? 45.036 15.303  -4.279  1.00 23.82 ? 38  LEU A N   1 
ATOM   271  C  CA  . LEU A 1 38  ? 45.853 14.461  -5.145  1.00 24.20 ? 38  LEU A CA  1 
ATOM   272  C  C   . LEU A 1 38  ? 46.450 15.254  -6.296  1.00 25.62 ? 38  LEU A C   1 
ATOM   273  O  O   . LEU A 1 38  ? 46.083 16.408  -6.531  1.00 25.57 ? 38  LEU A O   1 
ATOM   274  C  CB  . LEU A 1 38  ? 45.009 13.323  -5.730  1.00 23.83 ? 38  LEU A CB  1 
ATOM   275  C  CG  . LEU A 1 38  ? 44.454 12.235  -4.803  1.00 23.22 ? 38  LEU A CG  1 
ATOM   276  C  CD1 . LEU A 1 38  ? 43.429 11.396  -5.561  1.00 24.71 ? 38  LEU A CD1 1 
ATOM   277  C  CD2 . LEU A 1 38  ? 45.592 11.359  -4.294  1.00 20.93 ? 38  LEU A CD2 1 
ATOM   278  N  N   . THR A 1 39  ? 47.377 14.623  -7.008  1.00 25.15 ? 39  THR A N   1 
ATOM   279  C  CA  . THR A 1 39  ? 48.002 15.230  -8.172  1.00 25.71 ? 39  THR A CA  1 
ATOM   280  C  C   . THR A 1 39  ? 47.224 14.710  -9.373  1.00 25.54 ? 39  THR A C   1 
ATOM   281  O  O   . THR A 1 39  ? 46.947 13.513  -9.463  1.00 25.50 ? 39  THR A O   1 
ATOM   282  C  CB  . THR A 1 39  ? 49.478 14.809  -8.303  1.00 26.50 ? 39  THR A CB  1 
ATOM   283  O  OG1 . THR A 1 39  ? 50.237 15.406  -7.244  1.00 28.18 ? 39  THR A OG1 1 
ATOM   284  C  CG2 . THR A 1 39  ? 50.048 15.247  -9.648  1.00 27.28 ? 39  THR A CG2 1 
ATOM   285  N  N   . GLU A 1 40  ? 46.861 15.608  -10.285 1.00 25.41 ? 40  GLU A N   1 
ATOM   286  C  CA  . GLU A 1 40  ? 46.104 15.235  -11.478 1.00 25.14 ? 40  GLU A CA  1 
ATOM   287  C  C   . GLU A 1 40  ? 46.665 13.977  -12.137 1.00 23.93 ? 40  GLU A C   1 
ATOM   288  O  O   . GLU A 1 40  ? 47.874 13.845  -12.317 1.00 22.60 ? 40  GLU A O   1 
ATOM   289  C  CB  . GLU A 1 40  ? 46.109 16.389  -12.494 1.00 27.80 ? 40  GLU A CB  1 
ATOM   290  C  CG  . GLU A 1 40  ? 45.308 16.095  -13.757 1.00 30.43 ? 40  GLU A CG  1 
ATOM   291  C  CD  . GLU A 1 40  ? 45.352 17.227  -14.779 1.00 36.60 ? 40  GLU A CD  1 
ATOM   292  O  OE1 . GLU A 1 40  ? 44.728 17.078  -15.851 1.00 37.97 ? 40  GLU A OE1 1 
ATOM   293  O  OE2 . GLU A 1 40  ? 46.005 18.263  -14.520 1.00 37.25 ? 40  GLU A OE2 1 
ATOM   294  N  N   . GLY A 1 41  ? 45.780 13.050  -12.492 1.00 23.67 ? 41  GLY A N   1 
ATOM   295  C  CA  . GLY A 1 41  ? 46.219 11.824  -13.132 1.00 22.74 ? 41  GLY A CA  1 
ATOM   296  C  C   . GLY A 1 41  ? 45.755 10.558  -12.430 1.00 21.65 ? 41  GLY A C   1 
ATOM   297  O  O   . GLY A 1 41  ? 45.003 10.612  -11.455 1.00 20.08 ? 41  GLY A O   1 
ATOM   298  N  N   . LEU A 1 42  ? 46.214 9.416   -12.932 1.00 19.79 ? 42  LEU A N   1 
ATOM   299  C  CA  . LEU A 1 42  ? 45.853 8.111   -12.376 1.00 19.74 ? 42  LEU A CA  1 
ATOM   300  C  C   . LEU A 1 42  ? 46.587 7.816   -11.074 1.00 19.84 ? 42  LEU A C   1 
ATOM   301  O  O   . LEU A 1 42  ? 47.793 8.056   -10.968 1.00 20.24 ? 42  LEU A O   1 
ATOM   302  C  CB  . LEU A 1 42  ? 46.172 7.007   -13.393 1.00 19.45 ? 42  LEU A CB  1 
ATOM   303  C  CG  . LEU A 1 42  ? 45.425 7.064   -14.730 1.00 20.36 ? 42  LEU A CG  1 
ATOM   304  C  CD1 . LEU A 1 42  ? 46.046 6.075   -15.712 1.00 19.48 ? 42  LEU A CD1 1 
ATOM   305  C  CD2 . LEU A 1 42  ? 43.951 6.751   -14.506 1.00 20.35 ? 42  LEU A CD2 1 
ATOM   306  N  N   . ARG A 1 43  ? 45.861 7.288   -10.091 1.00 17.56 ? 43  ARG A N   1 
ATOM   307  C  CA  . ARG A 1 43  ? 46.446 6.943   -8.794  1.00 18.04 ? 43  ARG A CA  1 
ATOM   308  C  C   . ARG A 1 43  ? 45.926 5.572   -8.342  1.00 16.43 ? 43  ARG A C   1 
ATOM   309  O  O   . ARG A 1 43  ? 44.718 5.337   -8.343  1.00 17.99 ? 43  ARG A O   1 
ATOM   310  C  CB  . ARG A 1 43  ? 46.075 8.000   -7.745  1.00 16.79 ? 43  ARG A CB  1 
ATOM   311  C  CG  . ARG A 1 43  ? 46.445 9.426   -8.130  1.00 17.41 ? 43  ARG A CG  1 
ATOM   312  C  CD  . ARG A 1 43  ? 47.947 9.593   -8.274  1.00 14.81 ? 43  ARG A CD  1 
ATOM   313  N  NE  . ARG A 1 43  ? 48.266 10.809  -9.019  1.00 19.02 ? 43  ARG A NE  1 
ATOM   314  C  CZ  . ARG A 1 43  ? 49.364 10.980  -9.747  1.00 19.61 ? 43  ARG A CZ  1 
ATOM   315  N  NH1 . ARG A 1 43  ? 49.557 12.123  -10.393 1.00 22.84 ? 43  ARG A NH1 1 
ATOM   316  N  NH2 . ARG A 1 43  ? 50.271 10.016  -9.833  1.00 21.58 ? 43  ARG A NH2 1 
ATOM   317  N  N   . GLY A 1 44  ? 46.841 4.682   -7.959  1.00 17.94 ? 44  GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? 46.465 3.347   -7.509  1.00 16.65 ? 44  GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? 45.391 3.368   -6.432  1.00 16.52 ? 44  GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? 45.384 4.249   -5.575  1.00 15.98 ? 44  GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? 44.504 2.373   -6.459  1.00 17.18 ? 45  PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? 43.376 2.292   -5.528  1.00 17.14 ? 45  PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? 43.108 0.822   -5.163  1.00 17.66 ? 45  PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? 42.575 0.072   -5.986  1.00 16.58 ? 45  PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? 42.161 2.896   -6.244  1.00 19.12 ? 45  PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? 40.982 3.173   -5.363  1.00 16.80 ? 45  PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? 41.087 4.027   -4.275  1.00 21.26 ? 45  PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? 39.735 2.637   -5.677  1.00 17.58 ? 45  PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? 39.965 4.349   -3.511  1.00 19.08 ? 45  PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? 38.614 2.951   -4.922  1.00 19.33 ? 45  PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? 38.730 3.813   -3.837  1.00 18.95 ? 45  PHE A CZ  1 
ATOM   332  N  N   . HIS A 1 46  ? 43.466 0.412   -3.945  1.00 16.03 ? 46  HIS A N   1 
ATOM   333  C  CA  . HIS A 1 46  ? 43.261 -0.982  -3.536  1.00 17.21 ? 46  HIS A CA  1 
ATOM   334  C  C   . HIS A 1 46  ? 42.806 -1.192  -2.098  1.00 16.74 ? 46  HIS A C   1 
ATOM   335  O  O   . HIS A 1 46  ? 42.906 -0.301  -1.250  1.00 15.50 ? 46  HIS A O   1 
ATOM   336  C  CB  . HIS A 1 46  ? 44.549 -1.806  -3.696  1.00 17.96 ? 46  HIS A CB  1 
ATOM   337  C  CG  . HIS A 1 46  ? 45.453 -1.337  -4.792  1.00 19.36 ? 46  HIS A CG  1 
ATOM   338  N  ND1 . HIS A 1 46  ? 46.637 -0.677  -4.545  1.00 18.45 ? 46  HIS A ND1 1 
ATOM   339  C  CD2 . HIS A 1 46  ? 45.355 -1.445  -6.139  1.00 18.04 ? 46  HIS A CD2 1 
ATOM   340  C  CE1 . HIS A 1 46  ? 47.229 -0.397  -5.691  1.00 17.33 ? 46  HIS A CE1 1 
ATOM   341  N  NE2 . HIS A 1 46  ? 46.472 -0.851  -6.674  1.00 19.62 ? 46  HIS A NE2 1 
ATOM   342  N  N   . VAL A 1 47  ? 42.321 -2.402  -1.834  1.00 16.07 ? 47  VAL A N   1 
ATOM   343  C  CA  . VAL A 1 47  ? 41.919 -2.790  -0.491  1.00 16.24 ? 47  VAL A CA  1 
ATOM   344  C  C   . VAL A 1 47  ? 43.096 -3.632  -0.006  1.00 17.90 ? 47  VAL A C   1 
ATOM   345  O  O   . VAL A 1 47  ? 43.461 -4.625  -0.646  1.00 16.25 ? 47  VAL A O   1 
ATOM   346  C  CB  . VAL A 1 47  ? 40.660 -3.690  -0.480  1.00 16.82 ? 47  VAL A CB  1 
ATOM   347  C  CG1 . VAL A 1 47  ? 40.398 -4.187  0.937   1.00 18.50 ? 47  VAL A CG1 1 
ATOM   348  C  CG2 . VAL A 1 47  ? 39.450 -2.922  -0.998  1.00 15.61 ? 47  VAL A CG2 1 
ATOM   349  N  N   . HIS A 1 48  ? 43.710 -3.216  1.094   1.00 17.10 ? 48  HIS A N   1 
ATOM   350  C  CA  . HIS A 1 48  ? 44.829 -3.950  1.654   1.00 17.60 ? 48  HIS A CA  1 
ATOM   351  C  C   . HIS A 1 48  ? 44.311 -4.888  2.739   1.00 18.84 ? 48  HIS A C   1 
ATOM   352  O  O   . HIS A 1 48  ? 43.233 -4.680  3.289   1.00 18.40 ? 48  HIS A O   1 
ATOM   353  C  CB  . HIS A 1 48  ? 45.890 -2.980  2.173   1.00 17.15 ? 48  HIS A CB  1 
ATOM   354  C  CG  . HIS A 1 48  ? 46.654 -2.307  1.073   1.00 15.42 ? 48  HIS A CG  1 
ATOM   355  N  ND1 . HIS A 1 48  ? 48.027 -2.376  0.965   1.00 14.99 ? 48  HIS A ND1 1 
ATOM   356  C  CD2 . HIS A 1 48  ? 46.229 -1.577  0.012   1.00 17.29 ? 48  HIS A CD2 1 
ATOM   357  C  CE1 . HIS A 1 48  ? 48.415 -1.719  -0.114  1.00 15.73 ? 48  HIS A CE1 1 
ATOM   358  N  NE2 . HIS A 1 48  ? 47.344 -1.225  -0.709  1.00 16.74 ? 48  HIS A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? 45.087 -5.922  3.030   1.00 16.57 ? 49  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? 44.691 -6.958  3.974   1.00 16.44 ? 49  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? 44.245 -6.591  5.385   1.00 16.54 ? 49  GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? 43.189 -7.036  5.834   1.00 15.80 ? 49  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? 45.807 -8.002  4.056   1.00 18.04 ? 49  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? 45.441 -9.251  4.848   1.00 18.23 ? 49  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? 46.561 -10.269 4.854   1.00 20.65 ? 49  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? 46.361 -11.364 5.415   1.00 24.70 ? 49  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? 47.640 -9.967  4.301   1.00 20.72 ? 49  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? 45.028 -5.780  6.083   1.00 16.37 ? 50  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 44.704 -5.444  7.463   1.00 15.43 ? 50  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 44.152 -4.056  7.734   1.00 15.92 ? 50  PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 44.617 -3.070  7.170   1.00 16.04 ? 50  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 45.946 -5.651  8.331   1.00 17.27 ? 50  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 46.560 -7.012  8.188   1.00 19.66 ? 50  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 45.862 -8.146  8.584   1.00 20.29 ? 50  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 47.829 -7.162  7.634   1.00 20.56 ? 50  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 46.418 -9.411  8.433   1.00 22.05 ? 50  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 48.395 -8.425  7.476   1.00 21.79 ? 50  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 47.689 -9.550  7.876   1.00 23.71 ? 50  PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? 43.159 -3.991  8.619   1.00 16.63 ? 51  GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? 42.590 -2.712  8.999   1.00 16.10 ? 51  GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? 43.375 -2.279  10.223  1.00 18.06 ? 51  GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? 42.805 -1.961  11.270  1.00 18.67 ? 51  GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? 44.697 -2.268  10.072  1.00 17.76 ? 52  ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? 45.636 -1.933  11.146  1.00 19.47 ? 52  ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? 46.348 -0.614  10.859  1.00 18.55 ? 52  ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? 47.211 -0.539  9.982   1.00 19.34 ? 52  ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? 46.654 -3.076  11.275  1.00 18.65 ? 52  ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? 47.603 -2.905  12.447  1.00 21.67 ? 52  ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? 48.138 -3.935  12.914  1.00 22.14 ? 52  ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? 47.829 -1.762  12.894  1.00 19.30 ? 52  ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? 45.985 0.418   11.613  1.00 19.07 ? 53  ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? 46.563 1.745   11.431  1.00 20.41 ? 53  ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? 47.535 2.107   12.554  1.00 19.73 ? 53  ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? 47.789 3.286   12.805  1.00 18.51 ? 53  ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? 45.444 2.787   11.378  1.00 23.98 ? 53  ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? 45.909 4.115   10.816  1.00 28.05 ? 53  ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? 45.559 5.175   11.331  1.00 33.78 ? 53  ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? 46.690 4.064   9.746   1.00 31.42 ? 53  ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? 48.084 1.101   13.228  1.00 18.52 ? 54  THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? 49.008 1.371   14.325  1.00 18.77 ? 54  THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? 50.277 2.059   13.832  1.00 20.35 ? 54  THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? 50.931 2.782   14.586  1.00 22.46 ? 54  THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? 49.375 0.081   15.080  1.00 19.98 ? 54  THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? 49.905 -0.885  14.163  1.00 19.82 ? 54  THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? 48.137 -0.498  15.775  1.00 20.60 ? 54  THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? 50.621 1.838   12.568  1.00 19.87 ? 55  ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? 51.804 2.459   11.974  1.00 20.65 ? 55  ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? 51.391 3.185   10.701  1.00 21.64 ? 55  ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? 52.024 3.045   9.655   1.00 24.26 ? 55  ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? 52.857 1.406   11.656  1.00 19.03 ? 55  ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? 50.321 3.962   10.789  1.00 20.91 ? 56  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? 49.857 4.681   9.618   1.00 21.08 ? 56  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? 49.365 3.712   8.561   1.00 20.36 ? 56  GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? 48.871 2.634   8.887   1.00 22.62 ? 56  GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? 49.516 4.064   7.292   1.00 17.83 ? 57  CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? 49.044 3.181   6.233   1.00 18.74 ? 57  CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? 49.939 1.976   5.971   1.00 16.08 ? 57  CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? 49.510 1.028   5.318   1.00 16.72 ? 57  CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? 48.849 3.972   4.933   1.00 18.82 ? 57  CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? 47.686 5.357   5.149   1.00 20.67 ? 57  CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? 51.168 1.997   6.476   1.00 15.80 ? 58  THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? 52.071 0.876   6.233   1.00 17.29 ? 58  THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? 51.615 -0.407  6.911   1.00 17.29 ? 58  THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? 51.763 -1.494  6.349   1.00 17.69 ? 58  THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? 53.524 1.180   6.684   1.00 18.54 ? 58  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? 53.571 1.365   8.101   1.00 21.40 ? 58  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? 54.040 2.427   5.998   1.00 19.71 ? 58  THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? 51.047 -0.291  8.108   1.00 17.11 ? 59  SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? 50.605 -1.478  8.826   1.00 17.62 ? 59  SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? 49.407 -2.179  8.192   1.00 18.00 ? 59  SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? 48.992 -3.239  8.653   1.00 18.32 ? 59  SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? 50.326 -1.148  10.303  1.00 16.84 ? 59  SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? 49.648 0.086   10.459  1.00 19.77 ? 59  SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? 48.865 -1.606  7.122   1.00 17.67 ? 60  ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? 47.735 -2.229  6.432   1.00 16.78 ? 60  ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? 48.211 -3.467  5.672   1.00 15.98 ? 60  ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? 47.408 -4.298  5.247   1.00 17.00 ? 60  ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? 47.103 -1.243  5.469   1.00 16.04 ? 60  ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? 49.521 -3.581  5.483   1.00 17.13 ? 61  GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? 50.053 -4.739  4.782   1.00 17.29 ? 61  GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? 49.875 -4.721  3.275   1.00 16.94 ? 61  GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? 49.659 -3.665  2.685   1.00 17.99 ? 61  GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? 49.951 -5.891  2.622   1.00 16.94 ? 62  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? 49.809 -6.037  1.173   1.00 18.08 ? 62  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? 48.358 -6.007  0.702   1.00 17.32 ? 62  PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? 47.438 -5.875  1.506   1.00 19.30 ? 62  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? 50.466 -7.383  0.915   1.00 18.72 ? 62  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? 49.970 -8.176  2.087   1.00 18.13 ? 62  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? 50.155 -7.207  3.258   1.00 19.67 ? 62  PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? 48.153 -6.131  -0.604  1.00 17.88 ? 63  HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? 46.798 -6.124  -1.141  1.00 17.24 ? 63  HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? 46.064 -7.362  -0.638  1.00 18.36 ? 63  HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? 46.664 -8.429  -0.507  1.00 18.75 ? 63  HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? 46.830 -6.139  -2.674  1.00 17.16 ? 63  HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? 47.497 -4.942  -3.280  1.00 20.04 ? 63  HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? 47.670 -4.795  -4.639  1.00 19.47 ? 63  HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? 48.041 -3.841  -2.711  1.00 21.60 ? 63  HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? 48.291 -3.655  -4.882  1.00 21.23 ? 63  HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? 48.528 -3.057  -3.729  1.00 22.35 ? 63  HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? 44.774 -7.211  -0.351  1.00 18.43 ? 64  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? 43.947 -8.325  0.119   1.00 18.82 ? 64  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? 44.003 -9.390  -0.979  1.00 18.54 ? 64  PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? 43.569 -9.154  -2.107  1.00 16.72 ? 64  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? 42.508 -7.843  0.329   1.00 20.29 ? 64  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? 41.583 -8.894  0.876   1.00 18.91 ? 64  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? 40.248 -8.918  0.496   1.00 19.89 ? 64  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? 42.041 -9.852  1.773   1.00 19.84 ? 64  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? 39.378 -9.883  0.999   1.00 21.27 ? 64  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? 41.180 -10.821 2.283   1.00 19.42 ? 64  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? 39.846 -10.837 1.894   1.00 21.00 ? 64  PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? 44.525 -10.567 -0.649  1.00 19.10 ? 65  ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? 44.683 -11.615 -1.654  1.00 19.61 ? 65  ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? 44.459 -13.026 -1.094  1.00 21.81 ? 65  ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? 45.381 -13.838 -1.036  1.00 22.15 ? 65  ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? 46.089 -11.464 -2.250  1.00 21.04 ? 65  ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? 46.441 -12.542 -3.248  1.00 21.80 ? 65  ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? 45.625 -12.937 -4.084  1.00 20.47 ? 65  ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? 47.688 -13.005 -3.187  1.00 23.37 ? 65  ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? 43.217 -13.332 -0.686  1.00 21.93 ? 66  PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? 42.869 -14.644 -0.127  1.00 22.86 ? 66  PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? 42.976 -15.816 -1.103  1.00 24.31 ? 66  PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? 43.012 -16.972 -0.679  1.00 25.34 ? 66  PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? 41.444 -14.435 0.370   1.00 21.06 ? 66  PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? 40.897 -13.456 -0.618  1.00 22.06 ? 66  PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? 42.032 -12.458 -0.738  1.00 20.83 ? 66  PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? 43.018 -15.529 -2.399  1.00 23.36 ? 67  LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? 43.126 -16.592 -3.395  1.00 25.83 ? 67  LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? 44.565 -16.798 -3.859  1.00 26.19 ? 67  LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? 44.832 -17.607 -4.746  1.00 27.44 ? 67  LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? 42.226 -16.295 -4.596  1.00 26.42 ? 67  LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? 40.724 -16.359 -4.296  1.00 28.35 ? 67  LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? 39.934 -16.067 -5.559  1.00 30.14 ? 67  LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? 40.371 -17.740 -3.760  1.00 31.58 ? 67  LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? 45.488 -16.058 -3.256  1.00 26.05 ? 68  SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? 46.907 -16.165 -3.589  1.00 26.23 ? 68  SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? 47.214 -16.058 -5.082  1.00 26.45 ? 68  SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? 47.884 -16.924 -5.658  1.00 26.02 ? 68  SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? 47.470 -17.481 -3.041  1.00 28.48 ? 68  SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? 47.365 -17.527 -1.628  1.00 30.04 ? 68  SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? 46.731 -14.990 -5.707  1.00 24.67 ? 69  ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? 46.976 -14.759 -7.125  1.00 24.45 ? 69  ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? 47.912 -13.567 -7.288  1.00 22.71 ? 69  ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? 48.270 -12.922 -6.307  1.00 20.44 ? 69  ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? 45.660 -14.497 -7.860  1.00 25.58 ? 69  ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? 44.752 -15.723 -7.929  1.00 31.30 ? 69  ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? 43.449 -15.416 -8.647  1.00 35.02 ? 69  ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? 42.589 -16.594 -8.740  1.00 37.99 ? 69  ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? 41.354 -16.581 -9.231  1.00 39.52 ? 69  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? 40.645 -17.701 -9.279  1.00 40.18 ? 69  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? 40.826 -15.449 -9.673  1.00 40.21 ? 69  ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? 48.313 -13.287 -8.523  1.00 21.30 ? 70  LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? 49.207 -12.169 -8.791  1.00 23.16 ? 70  LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? 48.420 -10.879 -8.918  1.00 20.62 ? 70  LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? 47.203 -10.905 -9.086  1.00 20.19 ? 70  LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? 50.004 -12.409 -10.077 1.00 25.19 ? 70  LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? 50.905 -13.639 -10.030 1.00 30.44 ? 70  LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? 51.618 -13.776 -8.686  1.00 35.80 ? 70  LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? 52.328 -12.489 -8.278  1.00 38.05 ? 70  LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? 52.772 -12.531 -6.856  1.00 37.55 ? 70  LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? 49.122 -9.754  -8.824  1.00 20.47 ? 71  HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? 48.490 -8.451  -8.939  1.00 20.10 ? 71  HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? 48.011 -8.247  -10.370 1.00 21.07 ? 71  HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? 48.675 -8.660  -11.321 1.00 21.06 ? 71  HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? 49.483 -7.343  -8.575  1.00 18.64 ? 71  HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? 48.921 -5.961  -8.718  1.00 19.24 ? 71  HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? 48.023 -5.424  -7.820  1.00 17.95 ? 71  HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? 49.077 -5.034  -9.693  1.00 18.96 ? 71  HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? 47.648 -4.229  -8.238  1.00 16.80 ? 71  HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? 48.272 -3.969  -9.373  1.00 17.51 ? 71  HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? 46.855 -7.612  -10.520 1.00 20.09 ? 72  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? 46.326 -7.347  -11.843 1.00 18.64 ? 72  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? 45.387 -6.161  -11.806 1.00 18.91 ? 72  GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? 45.308 -5.455  -10.795 1.00 18.81 ? 72  GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? 44.689 -5.940  -12.916 1.00 19.13 ? 73  GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? 43.724 -4.858  -13.000 1.00 18.89 ? 73  GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? 42.382 -5.428  -12.577 1.00 19.83 ? 73  GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? 42.211 -6.649  -12.583 1.00 21.36 ? 73  GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? 41.408 -4.585  -12.208 1.00 19.31 ? 74  PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 40.097 -5.085  -11.784 1.00 20.78 ? 74  PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 39.353 -5.934  -12.817 1.00 21.99 ? 74  PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 38.571 -6.805  -12.447 1.00 21.63 ? 74  PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 39.346 -3.806  -11.403 1.00 20.74 ? 74  PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 39.973 -2.765  -12.275 1.00 21.86 ? 74  PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 41.437 -3.112  -12.207 1.00 20.35 ? 74  PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? 39.595 -5.692  -14.102 1.00 23.57 ? 75  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? 38.924 -6.467  -15.148 1.00 26.19 ? 75  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? 39.606 -7.813  -15.409 1.00 25.78 ? 75  LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? 39.068 -8.663  -16.121 1.00 26.48 ? 75  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? 38.865 -5.672  -16.456 1.00 28.23 ? 75  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? 37.795 -4.587  -16.498 1.00 34.50 ? 75  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? 38.134 -3.400  -15.611 1.00 35.59 ? 75  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? 37.074 -2.309  -15.738 1.00 37.92 ? 75  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? 37.438 -1.069  -14.996 1.00 35.88 ? 75  LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? 40.787 -8.006  -14.833 1.00 25.38 ? 76  ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? 41.530 -9.253  -15.013 1.00 25.99 ? 76  ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? 41.032 -10.348 -14.076 1.00 27.08 ? 76  ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? 40.615 -10.070 -12.956 1.00 24.98 ? 76  ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? 43.013 -9.028  -14.735 1.00 25.98 ? 76  ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? 43.615 -7.957  -15.609 1.00 28.36 ? 76  ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? 44.689 -7.437  -15.245 1.00 28.16 ? 76  ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? 43.024 -7.640  -16.662 1.00 30.32 ? 76  ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? 41.080 -11.595 -14.529 1.00 28.29 ? 77  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? 40.662 -12.698 -13.681 1.00 29.53 ? 77  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? 41.820 -12.965 -12.732 1.00 27.81 ? 77  GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? 41.617 -13.314 -11.572 1.00 28.11 ? 77  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? 40.344 -13.950 -14.500 1.00 35.12 ? 77  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? 40.035 -15.170 -13.632 1.00 41.16 ? 77  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? 38.865 -14.950 -12.676 1.00 46.33 ? 77  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? 38.575 -13.785 -12.328 1.00 50.44 ? 77  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? 38.242 -15.950 -12.256 1.00 49.31 ? 77  GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? 43.040 -12.796 -13.232 1.00 26.48 ? 78  GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? 44.212 -12.982 -12.395 1.00 26.31 ? 78  GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? 44.453 -11.630 -11.735 1.00 24.21 ? 78  GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? 45.064 -10.739 -12.323 1.00 24.34 ? 78  GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? 45.432 -13.380 -13.229 1.00 27.85 ? 78  GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? 46.688 -13.657 -12.398 1.00 31.33 ? 78  GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? 46.584 -14.920 -11.546 1.00 33.15 ? 78  GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? 47.524 -15.190 -10.766 1.00 30.90 ? 78  GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? 45.572 -15.645 -11.654 1.00 34.35 ? 78  GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? 43.934 -11.480 -10.522 1.00 22.89 ? 79  ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? 44.076 -10.244 -9.754  1.00 20.44 ? 79  ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? 43.894 -10.571 -8.284  1.00 20.50 ? 79  ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? 43.429 -11.656 -7.932  1.00 22.22 ? 79  ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? 42.991 -9.234  -10.148 1.00 20.25 ? 79  ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? 41.578 -9.784  -9.960  1.00 19.62 ? 79  ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? 40.481 -8.714  -10.044 1.00 20.85 ? 79  ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? 40.170 -8.118  -8.743  1.00 19.63 ? 79  ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? 39.136 -7.309  -8.518  1.00 20.86 ? 79  ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? 38.924 -6.818  -7.308  1.00 19.16 ? 79  ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? 38.311 -6.987  -9.506  1.00 21.26 ? 79  ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? 44.270 -9.629  -7.428  1.00 19.74 ? 80  HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? 44.087 -9.785  -5.991  1.00 18.89 ? 80  HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? 42.646 -9.341  -5.767  1.00 18.67 ? 80  HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? 42.130 -8.531  -6.534  1.00 17.22 ? 80  HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? 45.015 -8.839  -5.229  1.00 17.55 ? 80  HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? 46.469 -9.124  -5.427  1.00 16.93 ? 80  HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? 47.423 -8.129  -5.465  1.00 15.66 ? 80  HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? 47.141 -10.295 -5.537  1.00 17.41 ? 80  HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? 48.620 -8.675  -5.587  1.00 19.21 ? 80  HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? 48.477 -9.988  -5.633  1.00 18.58 ? 80  HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? 41.990 -9.863  -4.737  1.00 18.28 ? 81  VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? 40.621 -9.447  -4.462  1.00 16.79 ? 81  VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? 40.585 -7.933  -4.255  1.00 17.65 ? 81  VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? 39.629 -7.270  -4.636  1.00 17.75 ? 81  VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? 40.064 -10.145 -3.202  1.00 17.10 ? 81  VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? 38.765 -9.481  -2.754  1.00 16.76 ? 81  VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? 39.816 -11.620 -3.502  1.00 15.28 ? 81  VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? 41.642 -7.383  -3.666  1.00 17.94 ? 82  GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? 41.666 -5.954  -3.410  1.00 18.51 ? 82  GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? 42.075 -5.040  -4.552  1.00 18.84 ? 82  GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? 42.161 -3.826  -4.363  1.00 17.54 ? 82  GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? 42.315 -5.599  -5.735  1.00 16.30 ? 83  ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? 42.738 -4.786  -6.873  1.00 16.47 ? 83  ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? 41.613 -4.020  -7.552  1.00 17.73 ? 83  ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? 40.875 -4.576  -8.366  1.00 18.24 ? 83  ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? 43.458 -5.658  -7.906  1.00 16.83 ? 83  ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? 44.767 -6.203  -7.389  1.00 18.97 ? 83  ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? 45.314 -5.612  -6.428  1.00 18.65 ? 83  ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? 45.258 -7.209  -7.947  1.00 19.89 ? 83  ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? 41.492 -2.735  -7.222  1.00 17.12 ? 84  LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? 40.454 -1.899  -7.809  1.00 17.05 ? 84  LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? 41.018 -0.908  -8.830  1.00 18.27 ? 84  LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? 40.389 0.107   -9.148  1.00 18.93 ? 84  LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? 39.688 -1.167  -6.705  1.00 18.16 ? 84  LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? 38.947 -2.102  -5.745  1.00 18.39 ? 84  LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? 38.255 -1.289  -4.668  1.00 19.10 ? 84  LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? 37.932 -2.941  -6.516  1.00 18.62 ? 84  LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? 42.210 -1.217  -9.334  1.00 17.44 ? 85  GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? 42.848 -0.391  -10.349 1.00 18.95 ? 85  GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? 43.263 1.021   -9.983  1.00 18.99 ? 85  GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? 44.000 1.236   -9.019  1.00 17.59 ? 85  GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? 42.794 1.986   -10.769 1.00 17.62 ? 86  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? 43.120 3.393   -10.556 1.00 18.72 ? 86  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? 41.908 4.308   -10.489 1.00 18.36 ? 86  ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? 40.855 4.013   -11.057 1.00 19.34 ? 86  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? 44.002 3.914   -11.696 1.00 19.16 ? 86  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? 45.349 3.234   -11.758 1.00 19.51 ? 86  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? 46.164 3.370   -10.852 1.00 22.93 ? 86  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? 45.590 2.497   -12.832 1.00 18.16 ? 86  ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? 42.068 5.422   -9.783  1.00 18.12 ? 87  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? 41.038 6.447   -9.720  1.00 18.89 ? 87  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? 41.701 7.589   -10.491 1.00 20.36 ? 87  VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? 42.925 7.592   -10.659 1.00 19.43 ? 87  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? 40.730 6.894   -8.275  1.00 19.94 ? 87  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? 40.044 5.761   -7.519  1.00 19.84 ? 87  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? 42.009 7.312   -7.571  1.00 21.04 ? 87  VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? 40.918 8.552   -10.966 1.00 20.75 ? 88  THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? 41.493 9.651   -11.735 1.00 21.62 ? 88  THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? 41.259 11.009  -11.101 1.00 20.84 ? 88  THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? 40.118 11.450  -10.967 1.00 20.44 ? 88  THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? 40.919 9.681   -13.161 1.00 21.92 ? 88  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? 41.160 8.420   -13.798 1.00 23.16 ? 88  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? 41.568 10.798  -13.974 1.00 23.69 ? 88  THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? 42.347 11.668  -10.718 1.00 20.46 ? 89  ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? 42.270 12.991  -10.110 1.00 20.78 ? 89  ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? 42.198 14.027  -11.227 1.00 23.41 ? 89  ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? 42.941 13.935  -12.205 1.00 22.33 ? 89  ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? 43.501 13.241  -9.250  1.00 20.44 ? 89  ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? 41.306 15.006  -11.085 1.00 25.02 ? 90  ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? 41.165 16.044  -12.101 1.00 26.66 ? 90  ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? 42.240 17.111  -11.918 1.00 27.35 ? 90  ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? 43.116 16.969  -11.065 1.00 26.30 ? 90  ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? 39.750 16.654  -12.060 1.00 27.90 ? 90  ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? 39.436 17.366  -10.753 1.00 26.47 ? 90  ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? 38.233 17.577  -10.477 1.00 26.68 ? 90  ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? 40.371 17.730  -10.010 1.00 27.26 ? 90  ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? 42.188 18.170  -12.719 1.00 29.12 ? 91  LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? 43.192 19.223  -12.625 1.00 32.05 ? 91  LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? 43.142 19.961  -11.292 1.00 32.12 ? 91  LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? 44.071 20.688  -10.944 1.00 33.89 ? 91  LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? 43.035 20.213  -13.785 1.00 33.56 ? 91  LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? 41.707 20.946  -13.819 1.00 37.26 ? 91  LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? 41.568 21.744  -15.110 1.00 40.86 ? 91  LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? 40.245 22.491  -15.169 1.00 42.82 ? 91  LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? 40.129 23.501  -14.082 1.00 44.69 ? 91  LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? 42.056 19.766  -10.551 1.00 31.53 ? 92  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? 41.889 20.400  -9.250  1.00 32.13 ? 92  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? 42.342 19.455  -8.136  1.00 30.95 ? 92  ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? 42.228 19.775  -6.954  1.00 32.27 ? 92  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? 40.423 20.795  -9.046  1.00 35.02 ? 92  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? 39.973 21.882  -10.009 1.00 38.64 ? 92  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? 38.754 22.149  -10.085 1.00 41.63 ? 92  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? 40.839 22.475  -10.688 1.00 40.29 ? 92  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? 42.858 18.292  -8.526  1.00 28.91 ? 93  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? 43.337 17.320  -7.558  1.00 26.44 ? 93  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? 42.247 16.480  -6.922  1.00 26.05 ? 93  GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? 42.477 15.809  -5.915  1.00 24.32 ? 93  GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? 41.057 16.509  -7.512  1.00 24.29 ? 94  VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? 39.932 15.754  -6.982  1.00 24.29 ? 94  VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? 39.580 14.555  -7.841  1.00 24.46 ? 94  VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? 39.413 14.676  -9.054  1.00 25.53 ? 94  VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? 38.670 16.629  -6.870  1.00 23.76 ? 94  VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? 37.504 15.788  -6.369  1.00 23.82 ? 94  VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? 38.929 17.801  -5.936  1.00 25.09 ? 94  VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? 39.459 13.399  -7.201  1.00 24.27 ? 95  ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? 39.102 12.182  -7.904  1.00 24.98 ? 95  ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? 37.715 11.746  -7.462  1.00 26.35 ? 95  ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? 37.529 11.302  -6.326  1.00 25.92 ? 95  ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? 40.114 11.081  -7.606  1.00 27.40 ? 95  ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? 36.734 11.901  -8.345  1.00 25.28 ? 96  ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? 35.383 11.473  -8.024  1.00 27.20 ? 96  ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? 35.340 10.012  -8.432  1.00 26.57 ? 96  ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? 35.470 9.679   -9.607  1.00 27.33 ? 96  ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 34.347 12.299  -8.789  1.00 30.07 ? 96  ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 34.287 13.737  -8.305  1.00 33.07 ? 96  ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 34.752 14.639  -9.032  1.00 35.31 ? 96  ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 33.785 13.963  -7.183  1.00 35.94 ? 96  ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? 35.174 9.146   -7.441  1.00 24.96 ? 97  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? 35.168 7.708   -7.656  1.00 23.54 ? 97  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? 33.783 7.110   -7.858  1.00 23.40 ? 97  VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? 32.854 7.396   -7.109  1.00 21.47 ? 97  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? 35.852 6.995   -6.466  1.00 24.17 ? 97  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? 35.959 5.503   -6.733  1.00 23.19 ? 97  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? 37.231 7.608   -6.222  1.00 23.56 ? 97  VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? 33.661 6.279   -8.887  1.00 24.58 ? 98  SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? 32.411 5.600   -9.204  1.00 25.31 ? 98  SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? 32.817 4.279   -9.842  1.00 26.60 ? 98  SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? 33.037 4.197   -11.054 1.00 26.33 ? 98  SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? 31.574 6.425   -10.183 1.00 28.45 ? 98  SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 30.281 5.860   -10.330 1.00 29.69 ? 98  SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? 32.927 3.253   -9.004  1.00 24.79 ? 99  ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? 33.338 1.925   -9.431  1.00 24.27 ? 99  ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? 32.292 0.872   -9.073  1.00 23.93 ? 99  ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? 31.484 1.055   -8.168  1.00 22.64 ? 99  ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? 34.680 1.527   -8.740  1.00 24.39 ? 99  ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? 35.811 2.454   -9.198  1.00 25.82 ? 99  ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? 35.031 0.081   -9.046  1.00 27.49 ? 99  ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? 37.132 2.228   -8.461  1.00 24.67 ? 99  ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? 32.308 -0.228  -9.810  1.00 23.38 ? 100 GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? 31.421 -1.341  -9.533  1.00 23.62 ? 100 GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? 32.336 -2.545  -9.656  1.00 22.52 ? 100 GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? 33.034 -2.697  -10.659 1.00 22.84 ? 100 GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? 30.285 -1.415  -10.551 1.00 28.47 ? 100 GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? 29.310 -2.546  -10.283 1.00 35.61 ? 100 GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? 27.872 -2.167  -10.593 1.00 39.33 ? 100 GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? 26.996 -3.053  -10.532 1.00 41.67 ? 100 GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? 27.614 -0.980  -10.887 1.00 44.07 ? 100 GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? 32.363 -3.380  -8.627  1.00 21.35 ? 101 ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? 33.232 -4.550  -8.650  1.00 21.43 ? 101 ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? 32.523 -5.746  -8.039  1.00 21.15 ? 101 ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? 31.831 -5.618  -7.029  1.00 21.46 ? 101 ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? 34.523 -4.246  -7.891  1.00 20.87 ? 101 ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? 35.588 -5.299  -8.112  1.00 21.22 ? 101 ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? 35.700 -6.220  -7.281  1.00 21.05 ? 101 ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? 36.308 -5.210  -9.129  1.00 23.01 ? 101 ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? 32.703 -6.909  -8.654  1.00 21.51 ? 102 SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? 32.053 -8.124  -8.180  1.00 21.57 ? 102 SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? 32.985 -9.103  -7.490  1.00 22.52 ? 102 SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? 32.553 -10.173 -7.063  1.00 23.44 ? 102 SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? 31.357 -8.827  -9.347  1.00 24.63 ? 102 SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? 30.350 -7.995  -9.888  1.00 27.81 ? 102 SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? 34.262 -8.750  -7.378  1.00 21.17 ? 103 VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? 35.214 -9.634  -6.722  1.00 22.13 ? 103 VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? 35.264 -9.318  -5.230  1.00 22.08 ? 103 VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? 35.263 -10.229 -4.394  1.00 22.50 ? 103 VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? 36.611 -9.515  -7.363  1.00 21.15 ? 103 VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? 37.624 -10.341 -6.586  1.00 22.20 ? 103 VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? 36.546 -10.005 -8.805  1.00 22.30 ? 103 VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? 35.308 -8.034  -4.887  1.00 21.31 ? 104 ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? 35.300 -7.664  -3.481  1.00 19.57 ? 104 ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? 33.880 -7.939  -2.990  1.00 20.82 ? 104 ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? 32.959 -8.081  -3.794  1.00 20.70 ? 104 ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? 35.614 -6.165  -3.250  1.00 18.44 ? 104 ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? 34.623 -5.286  -4.013  1.00 16.65 ? 104 ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? 37.038 -5.860  -3.660  1.00 19.63 ? 104 ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? 34.675 -3.814  -3.590  1.00 18.46 ? 104 ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? 33.711 -8.027  -1.677  1.00 20.43 ? 105 SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? 32.401 -8.270  -1.082  1.00 20.79 ? 105 SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? 32.350 -7.608  0.292   1.00 20.41 ? 105 SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? 33.390 -7.300  0.871   1.00 20.40 ? 105 SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? 32.155 -9.774  -0.931  1.00 20.68 ? 105 SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? 30.846 -10.022 -0.448  1.00 22.62 ? 105 SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? 31.145 -7.379  0.806   1.00 21.04 ? 106 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? 30.990 -6.773  2.123   1.00 21.62 ? 106 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? 30.583 -7.834  3.149   1.00 23.87 ? 106 LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? 30.208 -7.522  4.276   1.00 23.54 ? 106 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? 29.958 -5.637  2.077   1.00 20.25 ? 106 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? 30.321 -4.446  1.180   1.00 19.88 ? 106 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? 29.359 -3.293  1.456   1.00 20.03 ? 106 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? 31.756 -3.997  1.451   1.00 19.08 ? 106 LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? 30.671 -9.096  2.742   1.00 26.76 ? 107 SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? 30.346 -10.216 3.620   1.00 29.32 ? 107 SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? 30.978 -11.468 3.028   1.00 29.50 ? 107 SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? 31.400 -11.468 1.874   1.00 29.44 ? 107 SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? 28.832 -10.405 3.725   1.00 31.03 ? 107 SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? 28.297 -10.837 2.489   1.00 30.24 ? 107 SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? 31.053 -12.532 3.817   1.00 30.46 ? 108 GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? 31.646 -13.757 3.315   1.00 30.43 ? 108 GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? 33.164 -13.760 3.367   1.00 31.09 ? 108 GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? 33.782 -12.851 3.923   1.00 30.80 ? 108 GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? 33.764 -14.785 2.770   1.00 30.62 ? 109 ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? 35.216 -14.944 2.753   1.00 31.71 ? 109 ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? 35.995 -13.793 2.119   1.00 30.61 ? 109 ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? 37.120 -13.504 2.526   1.00 30.82 ? 109 ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? 35.585 -16.250 2.043   1.00 34.52 ? 109 ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? 35.090 -17.476 2.786   1.00 37.19 ? 109 ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? 35.275 -18.596 2.265   1.00 38.56 ? 109 ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? 34.521 -17.320 3.889   1.00 37.78 ? 109 ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? 35.405 -13.142 1.123   1.00 28.75 ? 110 HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? 36.077 -12.039 0.448   1.00 27.83 ? 110 HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? 35.636 -10.676 0.964   1.00 26.01 ? 110 HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? 35.853 -9.655  0.312   1.00 26.45 ? 110 HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? 35.850 -12.141 -1.064  1.00 30.83 ? 110 HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? 36.493 -13.344 -1.684  1.00 34.40 ? 110 HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? 36.386 -13.641 -3.025  1.00 35.81 ? 110 HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? 37.262 -14.319 -1.143  1.00 36.77 ? 110 HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? 37.062 -14.747 -3.284  1.00 37.50 ? 110 HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? 37.604 -15.178 -2.159  1.00 37.91 ? 110 HIS A NE2 1 
ATOM   809  N  N   . SER A 1 111 ? 35.021 -10.662 2.142   1.00 24.17 ? 111 SER A N   1 
ATOM   810  C  CA  . SER A 1 111 ? 34.571 -9.411  2.732   1.00 21.92 ? 111 SER A CA  1 
ATOM   811  C  C   . SER A 1 111 ? 35.755 -8.491  2.988   1.00 21.46 ? 111 SER A C   1 
ATOM   812  O  O   . SER A 1 111 ? 36.819 -8.932  3.432   1.00 21.10 ? 111 SER A O   1 
ATOM   813  C  CB  . SER A 1 111 ? 33.846 -9.664  4.051   1.00 22.19 ? 111 SER A CB  1 
ATOM   814  O  OG  . SER A 1 111 ? 33.454 -8.435  4.639   1.00 21.68 ? 111 SER A OG  1 
ATOM   815  N  N   . ILE A 1 112 ? 35.568 -7.209  2.700   1.00 19.84 ? 112 ILE A N   1 
ATOM   816  C  CA  . ILE A 1 112 ? 36.618 -6.225  2.917   1.00 18.91 ? 112 ILE A CA  1 
ATOM   817  C  C   . ILE A 1 112 ? 36.335 -5.423  4.192   1.00 19.08 ? 112 ILE A C   1 
ATOM   818  O  O   . ILE A 1 112 ? 37.065 -4.490  4.527   1.00 17.52 ? 112 ILE A O   1 
ATOM   819  C  CB  . ILE A 1 112 ? 36.733 -5.257  1.719   1.00 19.04 ? 112 ILE A CB  1 
ATOM   820  C  CG1 . ILE A 1 112 ? 35.410 -4.520  1.512   1.00 19.45 ? 112 ILE A CG1 1 
ATOM   821  C  CG2 . ILE A 1 112 ? 37.118 -6.033  0.462   1.00 18.89 ? 112 ILE A CG2 1 
ATOM   822  C  CD1 . ILE A 1 112 ? 35.436 -3.524  0.377   1.00 21.84 ? 112 ILE A CD1 1 
ATOM   823  N  N   . ILE A 1 113 ? 35.268 -5.783  4.899   1.00 19.76 ? 113 ILE A N   1 
ATOM   824  C  CA  . ILE A 1 113 ? 34.939 -5.082  6.137   1.00 19.08 ? 113 ILE A CA  1 
ATOM   825  C  C   . ILE A 1 113 ? 36.061 -5.320  7.140   1.00 17.64 ? 113 ILE A C   1 
ATOM   826  O  O   . ILE A 1 113 ? 36.475 -6.459  7.371   1.00 18.27 ? 113 ILE A O   1 
ATOM   827  C  CB  . ILE A 1 113 ? 33.608 -5.580  6.747   1.00 19.74 ? 113 ILE A CB  1 
ATOM   828  C  CG1 . ILE A 1 113 ? 32.445 -5.265  5.797   1.00 18.57 ? 113 ILE A CG1 1 
ATOM   829  C  CG2 . ILE A 1 113 ? 33.367 -4.908  8.094   1.00 18.46 ? 113 ILE A CG2 1 
ATOM   830  C  CD1 . ILE A 1 113 ? 32.268 -3.783  5.495   1.00 20.90 ? 113 ILE A CD1 1 
ATOM   831  N  N   . GLY A 1 114 ? 36.557 -4.241  7.731   1.00 17.20 ? 114 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 114 ? 37.634 -4.369  8.696   1.00 17.04 ? 114 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 114 ? 39.004 -4.343  8.041   1.00 18.00 ? 114 GLY A C   1 
ATOM   834  O  O   . GLY A 1 114 ? 40.020 -4.504  8.713   1.00 17.66 ? 114 GLY A O   1 
ATOM   835  N  N   . ARG A 1 115 ? 39.048 -4.154  6.728   1.00 17.60 ? 115 ARG A N   1 
ATOM   836  C  CA  . ARG A 1 115 ? 40.334 -4.095  6.047   1.00 17.06 ? 115 ARG A CA  1 
ATOM   837  C  C   . ARG A 1 115 ? 40.637 -2.639  5.718   1.00 18.57 ? 115 ARG A C   1 
ATOM   838  O  O   . ARG A 1 115 ? 39.965 -1.743  6.230   1.00 20.72 ? 115 ARG A O   1 
ATOM   839  C  CB  . ARG A 1 115 ? 40.322 -5.009  4.816   1.00 17.01 ? 115 ARG A CB  1 
ATOM   840  C  CG  . ARG A 1 115 ? 40.079 -6.468  5.241   1.00 15.83 ? 115 ARG A CG  1 
ATOM   841  C  CD  . ARG A 1 115 ? 40.206 -7.482  4.117   1.00 18.35 ? 115 ARG A CD  1 
ATOM   842  N  NE  . ARG A 1 115 ? 39.766 -8.806  4.558   1.00 18.55 ? 115 ARG A NE  1 
ATOM   843  C  CZ  . ARG A 1 115 ? 40.485 -9.642  5.307   1.00 22.17 ? 115 ARG A CZ  1 
ATOM   844  N  NH1 . ARG A 1 115 ? 39.978 -10.820 5.652   1.00 20.92 ? 115 ARG A NH1 1 
ATOM   845  N  NH2 . ARG A 1 115 ? 41.712 -9.318  5.693   1.00 19.84 ? 115 ARG A NH2 1 
ATOM   846  N  N   . THR A 1 116 ? 41.636 -2.384  4.884   1.00 16.24 ? 116 THR A N   1 
ATOM   847  C  CA  . THR A 1 116 ? 42.005 -1.001  4.603   1.00 17.59 ? 116 THR A CA  1 
ATOM   848  C  C   . THR A 1 116 ? 41.961 -0.588  3.142   1.00 16.16 ? 116 THR A C   1 
ATOM   849  O  O   . THR A 1 116 ? 42.458 -1.300  2.274   1.00 16.82 ? 116 THR A O   1 
ATOM   850  C  CB  . THR A 1 116 ? 43.432 -0.708  5.137   1.00 17.15 ? 116 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 116 ? 43.452 -0.845  6.564   1.00 17.85 ? 116 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 116 ? 43.878 0.704   4.757   1.00 17.47 ? 116 THR A CG2 1 
ATOM   853  N  N   . LEU A 1 117 ? 41.366 0.572   2.882   1.00 16.87 ? 117 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 117 ? 41.296 1.106   1.528   1.00 16.80 ? 117 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 117 ? 42.457 2.088   1.432   1.00 16.66 ? 117 LEU A C   1 
ATOM   856  O  O   . LEU A 1 117 ? 42.643 2.930   2.317   1.00 16.45 ? 117 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 117 ? 39.969 1.836   1.294   1.00 17.21 ? 117 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 117 ? 39.761 2.434   -0.100  1.00 15.14 ? 117 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 117 ? 39.735 1.328   -1.157  1.00 16.34 ? 117 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 117 ? 38.456 3.215   -0.113  1.00 15.06 ? 117 LEU A CD2 1 
ATOM   861  N  N   . VAL A 1 118 ? 43.243 1.979   0.368   1.00 15.95 ? 118 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 118 ? 44.397 2.853   0.193   1.00 15.87 ? 118 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 118 ? 44.421 3.529   -1.172  1.00 15.45 ? 118 VAL A C   1 
ATOM   864  O  O   . VAL A 1 118 ? 44.077 2.914   -2.182  1.00 16.67 ? 118 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 118 ? 45.717 2.047   0.343   1.00 18.49 ? 118 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 118 ? 46.924 2.965   0.160   1.00 17.26 ? 118 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 118 ? 45.770 1.380   1.708   1.00 15.92 ? 118 VAL A CG2 1 
ATOM   868  N  N   . VAL A 1 119 ? 44.807 4.802   -1.195  1.00 15.09 ? 119 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 119 ? 44.965 5.516   -2.455  1.00 15.82 ? 119 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 119 ? 46.467 5.808   -2.512  1.00 15.56 ? 119 VAL A C   1 
ATOM   871  O  O   . VAL A 1 119 ? 47.071 6.227   -1.516  1.00 15.20 ? 119 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 119 ? 44.123 6.809   -2.529  1.00 16.16 ? 119 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 119 ? 44.501 7.771   -1.416  1.00 16.97 ? 119 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 119 ? 44.309 7.444   -3.903  1.00 15.26 ? 119 VAL A CG2 1 
ATOM   875  N  N   . HIS A 1 120 ? 47.061 5.562   -3.678  1.00 15.75 ? 120 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 120 ? 48.502 5.687   -3.886  1.00 16.93 ? 120 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 120 ? 49.030 6.919   -4.598  1.00 17.37 ? 120 HIS A C   1 
ATOM   878  O  O   . HIS A 1 120 ? 48.286 7.665   -5.224  1.00 16.69 ? 120 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 120 ? 48.998 4.448   -4.628  1.00 16.73 ? 120 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 120 ? 48.911 3.190   -3.824  1.00 16.16 ? 120 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 120 ? 49.925 2.772   -2.988  1.00 16.06 ? 120 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 120 ? 47.925 2.266   -3.712  1.00 16.64 ? 120 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 120 ? 49.568 1.645   -2.397  1.00 16.77 ? 120 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 120 ? 48.360 1.317   -2.818  1.00 15.23 ? 120 HIS A NE2 1 
ATOM   885  N  N   . GLU A 1 121 ? 50.342 7.103   -4.499  1.00 18.75 ? 121 GLU A N   1 
ATOM   886  C  CA  . GLU A 1 121 ? 51.022 8.243   -5.102  1.00 19.85 ? 121 GLU A CA  1 
ATOM   887  C  C   . GLU A 1 121 ? 51.175 8.107   -6.607  1.00 19.68 ? 121 GLU A C   1 
ATOM   888  O  O   . GLU A 1 121 ? 51.170 9.103   -7.330  1.00 18.38 ? 121 GLU A O   1 
ATOM   889  C  CB  . GLU A 1 121 ? 52.404 8.415   -4.468  1.00 23.46 ? 121 GLU A CB  1 
ATOM   890  C  CG  . GLU A 1 121 ? 53.287 9.445   -5.157  1.00 29.18 ? 121 GLU A CG  1 
ATOM   891  C  CD  . GLU A 1 121 ? 54.544 9.752   -4.368  1.00 33.77 ? 121 GLU A CD  1 
ATOM   892  O  OE1 . GLU A 1 121 ? 54.450 10.486  -3.361  1.00 39.08 ? 121 GLU A OE1 1 
ATOM   893  O  OE2 . GLU A 1 121 ? 55.624 9.254   -4.747  1.00 38.12 ? 121 GLU A OE2 1 
ATOM   894  N  N   . LYS A 1 122 ? 51.316 6.873   -7.075  1.00 19.47 ? 122 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 122 ? 51.493 6.625   -8.498  1.00 20.26 ? 122 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 122 ? 50.399 5.759   -9.092  1.00 19.63 ? 122 LYS A C   1 
ATOM   897  O  O   . LYS A 1 122 ? 49.613 5.136   -8.373  1.00 19.77 ? 122 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 122 ? 52.845 5.953   -8.751  1.00 21.91 ? 122 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 122 ? 54.031 6.703   -8.167  1.00 22.88 ? 122 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 122 ? 55.337 6.101   -8.642  1.00 27.49 ? 122 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 122 ? 55.421 4.623   -8.288  1.00 28.02 ? 122 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 122 ? 56.622 3.967   -8.876  1.00 24.32 ? 122 LYS A NZ  1 
ATOM   903  N  N   . ALA A 1 123 ? 50.367 5.719   -10.419 1.00 19.42 ? 123 ALA A N   1 
ATOM   904  C  CA  . ALA A 1 123 ? 49.391 4.917   -11.135 1.00 20.49 ? 123 ALA A CA  1 
ATOM   905  C  C   . ALA A 1 123 ? 49.732 3.437   -10.985 1.00 20.53 ? 123 ALA A C   1 
ATOM   906  O  O   . ALA A 1 123 ? 50.900 3.058   -10.917 1.00 22.28 ? 123 ALA A O   1 
ATOM   907  C  CB  . ALA A 1 123 ? 49.383 5.302   -12.612 1.00 20.88 ? 123 ALA A CB  1 
ATOM   908  N  N   . ASP A 1 124 ? 48.698 2.609   -10.922 1.00 19.92 ? 124 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 124 ? 48.850 1.162   -10.809 1.00 18.20 ? 124 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 124 ? 49.048 0.696   -12.252 1.00 20.31 ? 124 ASP A C   1 
ATOM   911  O  O   . ASP A 1 124 ? 48.201 0.969   -13.106 1.00 19.31 ? 124 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 124 ? 47.556 0.604   -10.201 1.00 17.06 ? 124 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 124 ? 47.554 -0.902  -10.051 1.00 19.13 ? 124 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 124 ? 46.737 -1.395  -9.242  1.00 18.27 ? 124 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 124 ? 48.333 -1.596  -10.732 1.00 18.71 ? 124 ASP A OD2 1 
ATOM   916  N  N   . ASP A 1 125 ? 50.157 0.018   -12.547 1.00 19.23 ? 125 ASP A N   1 
ATOM   917  C  CA  . ASP A 1 125 ? 50.384 -0.417  -13.925 1.00 21.37 ? 125 ASP A CA  1 
ATOM   918  C  C   . ASP A 1 125 ? 49.594 -1.672  -14.302 1.00 20.56 ? 125 ASP A C   1 
ATOM   919  O  O   . ASP A 1 125 ? 49.771 -2.242  -15.380 1.00 21.59 ? 125 ASP A O   1 
ATOM   920  C  CB  . ASP A 1 125 ? 51.888 -0.584  -14.207 1.00 20.90 ? 125 ASP A CB  1 
ATOM   921  C  CG  . ASP A 1 125 ? 52.515 -1.732  -13.454 1.00 21.45 ? 125 ASP A CG  1 
ATOM   922  O  OD1 . ASP A 1 125 ? 53.759 -1.727  -13.323 1.00 21.15 ? 125 ASP A OD1 1 
ATOM   923  O  OD2 . ASP A 1 125 ? 51.790 -2.644  -13.009 1.00 19.82 ? 125 ASP A OD2 1 
ATOM   924  N  N   . LEU A 1 126 ? 48.712 -2.078  -13.398 1.00 21.06 ? 126 LEU A N   1 
ATOM   925  C  CA  . LEU A 1 126 ? 47.831 -3.222  -13.605 1.00 20.93 ? 126 LEU A CA  1 
ATOM   926  C  C   . LEU A 1 126 ? 48.547 -4.528  -13.931 1.00 21.36 ? 126 LEU A C   1 
ATOM   927  O  O   . LEU A 1 126 ? 47.968 -5.407  -14.560 1.00 21.53 ? 126 LEU A O   1 
ATOM   928  C  CB  . LEU A 1 126 ? 46.827 -2.886  -14.717 1.00 20.63 ? 126 LEU A CB  1 
ATOM   929  C  CG  . LEU A 1 126 ? 46.172 -1.503  -14.585 1.00 22.54 ? 126 LEU A CG  1 
ATOM   930  C  CD1 . LEU A 1 126 ? 45.171 -1.288  -15.723 1.00 23.63 ? 126 LEU A CD1 1 
ATOM   931  C  CD2 . LEU A 1 126 ? 45.475 -1.391  -13.232 1.00 23.25 ? 126 LEU A CD2 1 
ATOM   932  N  N   . GLY A 1 127 ? 49.799 -4.653  -13.497 1.00 20.64 ? 127 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 127 ? 50.556 -5.869  -13.748 1.00 23.27 ? 127 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 127 ? 51.169 -5.952  -15.133 1.00 23.74 ? 127 GLY A C   1 
ATOM   935  O  O   . GLY A 1 127 ? 51.719 -6.986  -15.515 1.00 25.16 ? 127 GLY A O   1 
ATOM   936  N  N   . LYS A 1 128 ? 51.084 -4.862  -15.887 1.00 24.72 ? 128 LYS A N   1 
ATOM   937  C  CA  . LYS A 1 128 ? 51.632 -4.825  -17.239 1.00 27.53 ? 128 LYS A CA  1 
ATOM   938  C  C   . LYS A 1 128 ? 52.977 -4.103  -17.300 1.00 27.28 ? 128 LYS A C   1 
ATOM   939  O  O   . LYS A 1 128 ? 53.458 -3.750  -18.377 1.00 27.86 ? 128 LYS A O   1 
ATOM   940  C  CB  . LYS A 1 128 ? 50.627 -4.153  -18.180 1.00 28.91 ? 128 LYS A CB  1 
ATOM   941  C  CG  . LYS A 1 128 ? 49.345 -4.959  -18.375 1.00 29.81 ? 128 LYS A CG  1 
ATOM   942  C  CD  . LYS A 1 128 ? 48.307 -4.202  -19.189 1.00 33.84 ? 128 LYS A CD  1 
ATOM   943  C  CE  . LYS A 1 128 ? 48.781 -3.926  -20.610 1.00 34.08 ? 128 LYS A CE  1 
ATOM   944  N  NZ  . LYS A 1 128 ? 47.753 -3.168  -21.385 1.00 36.37 ? 128 LYS A NZ  1 
ATOM   945  N  N   . GLY A 1 129 ? 53.587 -3.898  -16.135 1.00 27.73 ? 129 GLY A N   1 
ATOM   946  C  CA  . GLY A 1 129 ? 54.867 -3.216  -16.075 1.00 26.83 ? 129 GLY A CA  1 
ATOM   947  C  C   . GLY A 1 129 ? 56.044 -4.096  -16.459 1.00 27.82 ? 129 GLY A C   1 
ATOM   948  O  O   . GLY A 1 129 ? 55.989 -5.319  -16.336 1.00 26.89 ? 129 GLY A O   1 
ATOM   949  N  N   . GLY A 1 130 ? 57.119 -3.466  -16.921 1.00 27.75 ? 130 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 130 ? 58.293 -4.214  -17.324 1.00 28.20 ? 130 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 130 ? 59.240 -4.527  -16.182 1.00 28.26 ? 130 GLY A C   1 
ATOM   952  O  O   . GLY A 1 130 ? 60.423 -4.187  -16.246 1.00 29.37 ? 130 GLY A O   1 
ATOM   953  N  N   . ASN A 1 131 ? 58.725 -5.170  -15.137 1.00 26.13 ? 131 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 131 ? 59.545 -5.531  -13.980 1.00 25.36 ? 131 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 131 ? 58.808 -6.506  -13.067 1.00 24.91 ? 131 ASN A C   1 
ATOM   956  O  O   . ASN A 1 131 ? 57.608 -6.726  -13.223 1.00 25.44 ? 131 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 131 ? 59.937 -4.278  -13.192 1.00 23.08 ? 131 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 131 ? 58.749 -3.402  -12.865 1.00 24.05 ? 131 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 131 ? 57.791 -3.844  -12.224 1.00 21.63 ? 131 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 131 ? 58.800 -2.148  -13.310 1.00 24.84 ? 131 ASN A ND2 1 
ATOM   961  N  N   . GLU A 1 132 ? 59.530 -7.082  -12.110 1.00 24.40 ? 132 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 132 ? 58.949 -8.047  -11.182 1.00 25.17 ? 132 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 132 ? 57.915 -7.463  -10.220 1.00 23.99 ? 132 GLU A C   1 
ATOM   964  O  O   . GLU A 1 132 ? 56.964 -8.144  -9.837  1.00 24.03 ? 132 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 132 ? 60.055 -8.719  -10.365 1.00 27.60 ? 132 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 132 ? 60.992 -9.598  -11.179 1.00 29.69 ? 132 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 132 ? 60.280 -10.781 -11.810 1.00 32.73 ? 132 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 132 ? 59.592 -11.518 -11.073 1.00 34.08 ? 132 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 132 ? 60.409 -10.976 -13.039 1.00 34.67 ? 132 GLU A OE2 1 
ATOM   970  N  N   . GLU A 1 133 ? 58.102 -6.208  -9.825  1.00 22.09 ? 133 GLU A N   1 
ATOM   971  C  CA  . GLU A 1 133 ? 57.184 -5.570  -8.886  1.00 21.58 ? 133 GLU A CA  1 
ATOM   972  C  C   . GLU A 1 133 ? 55.786 -5.361  -9.456  1.00 22.14 ? 133 GLU A C   1 
ATOM   973  O  O   . GLU A 1 133 ? 54.809 -5.293  -8.708  1.00 23.48 ? 133 GLU A O   1 
ATOM   974  C  CB  . GLU A 1 133 ? 57.737 -4.216  -8.430  1.00 21.49 ? 133 GLU A CB  1 
ATOM   975  C  CG  . GLU A 1 133 ? 56.882 -3.536  -7.367  1.00 18.98 ? 133 GLU A CG  1 
ATOM   976  C  CD  . GLU A 1 133 ? 56.865 -4.312  -6.067  1.00 21.41 ? 133 GLU A CD  1 
ATOM   977  O  OE1 . GLU A 1 133 ? 55.955 -4.086  -5.240  1.00 17.73 ? 133 GLU A OE1 1 
ATOM   978  O  OE2 . GLU A 1 133 ? 57.774 -5.148  -5.870  1.00 20.22 ? 133 GLU A OE2 1 
ATOM   979  N  N   . SER A 1 134 ? 55.691 -5.254  -10.775 1.00 21.50 ? 134 SER A N   1 
ATOM   980  C  CA  . SER A 1 134 ? 54.404 -5.031  -11.424 1.00 21.37 ? 134 SER A CA  1 
ATOM   981  C  C   . SER A 1 134 ? 53.340 -6.037  -11.002 1.00 21.71 ? 134 SER A C   1 
ATOM   982  O  O   . SER A 1 134 ? 52.194 -5.665  -10.759 1.00 22.13 ? 134 SER A O   1 
ATOM   983  C  CB  . SER A 1 134 ? 54.561 -5.069  -12.945 1.00 22.76 ? 134 SER A CB  1 
ATOM   984  O  OG  . SER A 1 134 ? 53.336 -4.758  -13.596 1.00 21.82 ? 134 SER A OG  1 
ATOM   985  N  N   . THR A 1 135 ? 53.706 -7.310  -10.917 1.00 21.60 ? 135 THR A N   1 
ATOM   986  C  CA  . THR A 1 135 ? 52.724 -8.319  -10.531 1.00 22.15 ? 135 THR A CA  1 
ATOM   987  C  C   . THR A 1 135 ? 52.596 -8.521  -9.025  1.00 22.54 ? 135 THR A C   1 
ATOM   988  O  O   . THR A 1 135 ? 52.065 -9.542  -8.569  1.00 22.22 ? 135 THR A O   1 
ATOM   989  C  CB  . THR A 1 135 ? 53.004 -9.669  -11.225 1.00 25.01 ? 135 THR A CB  1 
ATOM   990  O  OG1 . THR A 1 135 ? 54.405 -9.957  -11.186 1.00 23.40 ? 135 THR A OG1 1 
ATOM   991  C  CG2 . THR A 1 135 ? 52.535 -9.612  -12.674 1.00 26.96 ? 135 THR A CG2 1 
ATOM   992  N  N   . LYS A 1 136 ? 53.071 -7.532  -8.264  1.00 21.40 ? 136 LYS A N   1 
ATOM   993  C  CA  . LYS A 1 136 ? 52.995 -7.552  -6.803  1.00 22.25 ? 136 LYS A CA  1 
ATOM   994  C  C   . LYS A 1 136 ? 52.145 -6.388  -6.313  1.00 21.53 ? 136 LYS A C   1 
ATOM   995  O  O   . LYS A 1 136 ? 51.166 -6.582  -5.592  1.00 18.83 ? 136 LYS A O   1 
ATOM   996  C  CB  . LYS A 1 136 ? 54.388 -7.438  -6.151  1.00 24.47 ? 136 LYS A CB  1 
ATOM   997  C  CG  . LYS A 1 136 ? 55.305 -8.652  -6.295  1.00 30.47 ? 136 LYS A CG  1 
ATOM   998  C  CD  . LYS A 1 136 ? 54.578 -9.858  -6.862  1.00 36.35 ? 136 LYS A CD  1 
ATOM   999  C  CE  . LYS A 1 136 ? 55.564 -10.863 -7.457  1.00 41.61 ? 136 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A 1 136 ? 54.902 -11.788 -8.419  1.00 44.87 ? 136 LYS A NZ  1 
ATOM   1001 N  N   . THR A 1 137 ? 52.528 -5.178  -6.711  1.00 19.62 ? 137 THR A N   1 
ATOM   1002 C  CA  . THR A 1 137 ? 51.817 -3.978  -6.290  1.00 20.63 ? 137 THR A CA  1 
ATOM   1003 C  C   . THR A 1 137 ? 51.446 -3.062  -7.443  1.00 19.03 ? 137 THR A C   1 
ATOM   1004 O  O   . THR A 1 137 ? 50.863 -2.004  -7.220  1.00 18.94 ? 137 THR A O   1 
ATOM   1005 C  CB  . THR A 1 137 ? 52.672 -3.143  -5.320  1.00 21.84 ? 137 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 137 ? 53.844 -2.681  -6.006  1.00 22.37 ? 137 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 137 ? 53.087 -3.973  -4.110  1.00 24.13 ? 137 THR A CG2 1 
ATOM   1008 N  N   . GLY A 1 138 ? 51.782 -3.460  -8.666  1.00 20.56 ? 138 GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 138 ? 51.491 -2.621  -9.816  1.00 18.63 ? 138 GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 138 ? 52.341 -1.359  -9.794  1.00 19.28 ? 138 GLY A C   1 
ATOM   1011 O  O   . GLY A 1 138 ? 52.093 -0.425  -10.555 1.00 17.50 ? 138 GLY A O   1 
ATOM   1012 N  N   . ASN A 1 139 ? 53.348 -1.332  -8.919  1.00 19.22 ? 139 ASN A N   1 
ATOM   1013 C  CA  . ASN A 1 139 ? 54.244 -0.178  -8.785  1.00 18.20 ? 139 ASN A CA  1 
ATOM   1014 C  C   . ASN A 1 139 ? 53.504 1.101   -8.391  1.00 19.62 ? 139 ASN A C   1 
ATOM   1015 O  O   . ASN A 1 139 ? 53.933 2.206   -8.737  1.00 17.82 ? 139 ASN A O   1 
ATOM   1016 C  CB  . ASN A 1 139 ? 55.017 0.051   -10.093 1.00 20.05 ? 139 ASN A CB  1 
ATOM   1017 C  CG  . ASN A 1 139 ? 56.098 -0.996  -10.322 1.00 21.33 ? 139 ASN A CG  1 
ATOM   1018 O  OD1 . ASN A 1 139 ? 57.086 -1.053  -9.590  1.00 18.53 ? 139 ASN A OD1 1 
ATOM   1019 N  ND2 . ASN A 1 139 ? 55.909 -1.832  -11.333 1.00 20.41 ? 139 ASN A ND2 1 
ATOM   1020 N  N   . ALA A 1 140 ? 52.413 0.942   -7.641  1.00 18.16 ? 140 ALA A N   1 
ATOM   1021 C  CA  . ALA A 1 140 ? 51.589 2.068   -7.199  1.00 20.18 ? 140 ALA A CA  1 
ATOM   1022 C  C   . ALA A 1 140 ? 52.317 3.009   -6.244  1.00 19.38 ? 140 ALA A C   1 
ATOM   1023 O  O   . ALA A 1 140 ? 51.890 4.145   -6.034  1.00 19.76 ? 140 ALA A O   1 
ATOM   1024 C  CB  . ALA A 1 140 ? 50.306 1.549   -6.546  1.00 18.49 ? 140 ALA A CB  1 
ATOM   1025 N  N   . GLY A 1 141 ? 53.404 2.533   -5.649  1.00 20.66 ? 141 GLY A N   1 
ATOM   1026 C  CA  . GLY A 1 141 ? 54.170 3.383   -4.755  1.00 19.44 ? 141 GLY A CA  1 
ATOM   1027 C  C   . GLY A 1 141 ? 53.599 3.701   -3.384  1.00 20.64 ? 141 GLY A C   1 
ATOM   1028 O  O   . GLY A 1 141 ? 52.786 2.951   -2.836  1.00 18.27 ? 141 GLY A O   1 
ATOM   1029 N  N   . SER A 1 142 ? 54.021 4.839   -2.837  1.00 20.41 ? 142 SER A N   1 
ATOM   1030 C  CA  . SER A 1 142 ? 53.605 5.251   -1.500  1.00 21.21 ? 142 SER A CA  1 
ATOM   1031 C  C   . SER A 1 142 ? 52.106 5.351   -1.296  1.00 19.63 ? 142 SER A C   1 
ATOM   1032 O  O   . SER A 1 142 ? 51.341 5.641   -2.220  1.00 19.97 ? 142 SER A O   1 
ATOM   1033 C  CB  . SER A 1 142 ? 54.257 6.583   -1.108  1.00 22.03 ? 142 SER A CB  1 
ATOM   1034 O  OG  . SER A 1 142 ? 53.589 7.684   -1.693  1.00 27.18 ? 142 SER A OG  1 
ATOM   1035 N  N   . ARG A 1 143 ? 51.704 5.113   -0.054  1.00 18.03 ? 143 ARG A N   1 
ATOM   1036 C  CA  . ARG A 1 143 ? 50.309 5.151   0.348   1.00 16.83 ? 143 ARG A CA  1 
ATOM   1037 C  C   . ARG A 1 143 ? 50.041 6.556   0.861   1.00 17.09 ? 143 ARG A C   1 
ATOM   1038 O  O   . ARG A 1 143 ? 50.443 6.909   1.971   1.00 17.98 ? 143 ARG A O   1 
ATOM   1039 C  CB  . ARG A 1 143 ? 50.094 4.104   1.440   1.00 19.04 ? 143 ARG A CB  1 
ATOM   1040 C  CG  . ARG A 1 143 ? 50.718 2.767   1.042   1.00 19.64 ? 143 ARG A CG  1 
ATOM   1041 C  CD  . ARG A 1 143 ? 50.673 1.704   2.128   1.00 19.10 ? 143 ARG A CD  1 
ATOM   1042 N  NE  . ARG A 1 143 ? 51.201 0.444   1.605   1.00 18.96 ? 143 ARG A NE  1 
ATOM   1043 C  CZ  . ARG A 1 143 ? 51.009 -0.750  2.159   1.00 18.14 ? 143 ARG A CZ  1 
ATOM   1044 N  NH1 . ARG A 1 143 ? 51.532 -1.830  1.589   1.00 17.33 ? 143 ARG A NH1 1 
ATOM   1045 N  NH2 . ARG A 1 143 ? 50.299 -0.869  3.273   1.00 14.32 ? 143 ARG A NH2 1 
ATOM   1046 N  N   . LEU A 1 144 ? 49.365 7.359   0.042   1.00 16.30 ? 144 LEU A N   1 
ATOM   1047 C  CA  . LEU A 1 144 ? 49.072 8.745   0.396   1.00 17.20 ? 144 LEU A CA  1 
ATOM   1048 C  C   . LEU A 1 144 ? 48.011 8.910   1.472   1.00 18.51 ? 144 LEU A C   1 
ATOM   1049 O  O   . LEU A 1 144 ? 48.094 9.816   2.301   1.00 19.16 ? 144 LEU A O   1 
ATOM   1050 C  CB  . LEU A 1 144 ? 48.656 9.531   -0.850  1.00 17.06 ? 144 LEU A CB  1 
ATOM   1051 C  CG  . LEU A 1 144 ? 49.702 9.610   -1.966  1.00 16.95 ? 144 LEU A CG  1 
ATOM   1052 C  CD1 . LEU A 1 144 ? 49.169 10.506  -3.071  1.00 20.95 ? 144 LEU A CD1 1 
ATOM   1053 C  CD2 . LEU A 1 144 ? 51.016 10.161  -1.431  1.00 19.93 ? 144 LEU A CD2 1 
ATOM   1054 N  N   . ALA A 1 145 ? 47.006 8.044   1.450   1.00 17.11 ? 145 ALA A N   1 
ATOM   1055 C  CA  . ALA A 1 145 ? 45.941 8.106   2.436   1.00 15.89 ? 145 ALA A CA  1 
ATOM   1056 C  C   . ALA A 1 145 ? 45.280 6.744   2.529   1.00 15.93 ? 145 ALA A C   1 
ATOM   1057 O  O   . ALA A 1 145 ? 45.316 5.958   1.582   1.00 15.30 ? 145 ALA A O   1 
ATOM   1058 C  CB  . ALA A 1 145 ? 44.914 9.166   2.047   1.00 17.44 ? 145 ALA A CB  1 
ATOM   1059 N  N   . CYS A 1 146 ? 44.683 6.464   3.680   1.00 16.91 ? 146 CYS A N   1 
ATOM   1060 C  CA  . CYS A 1 146 ? 44.020 5.190   3.889   1.00 17.04 ? 146 CYS A CA  1 
ATOM   1061 C  C   . CYS A 1 146 ? 42.981 5.300   4.993   1.00 15.94 ? 146 CYS A C   1 
ATOM   1062 O  O   . CYS A 1 146 ? 42.930 6.284   5.734   1.00 15.35 ? 146 CYS A O   1 
ATOM   1063 C  CB  . CYS A 1 146 ? 45.048 4.111   4.246   1.00 16.71 ? 146 CYS A CB  1 
ATOM   1064 S  SG  . CYS A 1 146 ? 45.985 4.432   5.779   1.00 19.68 ? 146 CYS A SG  1 
ATOM   1065 N  N   . GLY A 1 147 ? 42.136 4.286   5.086   1.00 14.52 ? 147 GLY A N   1 
ATOM   1066 C  CA  . GLY A 1 147 ? 41.123 4.274   6.114   1.00 13.65 ? 147 GLY A CA  1 
ATOM   1067 C  C   . GLY A 1 147 ? 40.596 2.868   6.262   1.00 16.31 ? 147 GLY A C   1 
ATOM   1068 O  O   . GLY A 1 147 ? 40.537 2.119   5.283   1.00 15.01 ? 147 GLY A O   1 
ATOM   1069 N  N   . VAL A 1 148 ? 40.230 2.499   7.482   1.00 15.36 ? 148 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 148 ? 39.694 1.169   7.720   1.00 16.75 ? 148 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 148 ? 38.271 1.175   7.185   1.00 16.52 ? 148 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 148 ? 37.532 2.154   7.359   1.00 18.21 ? 148 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 148 ? 39.700 0.828   9.220   1.00 15.55 ? 148 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 148 ? 39.166 -0.586  9.446   1.00 16.21 ? 148 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 148 ? 41.111 0.945   9.760   1.00 17.29 ? 148 VAL A CG2 1 
ATOM   1076 N  N   . ILE A 1 149 ? 37.894 0.092   6.516   1.00 16.92 ? 149 ILE A N   1 
ATOM   1077 C  CA  . ILE A 1 149 ? 36.565 -0.025  5.936   1.00 17.02 ? 149 ILE A CA  1 
ATOM   1078 C  C   . ILE A 1 149 ? 35.608 -0.470  7.030   1.00 17.87 ? 149 ILE A C   1 
ATOM   1079 O  O   . ILE A 1 149 ? 35.705 -1.597  7.526   1.00 19.31 ? 149 ILE A O   1 
ATOM   1080 C  CB  . ILE A 1 149 ? 36.564 -1.055  4.792   1.00 17.62 ? 149 ILE A CB  1 
ATOM   1081 C  CG1 . ILE A 1 149 ? 37.523 -0.593  3.688   1.00 19.77 ? 149 ILE A CG1 1 
ATOM   1082 C  CG2 . ILE A 1 149 ? 35.147 -1.234  4.240   1.00 16.30 ? 149 ILE A CG2 1 
ATOM   1083 C  CD1 . ILE A 1 149 ? 37.799 -1.646  2.632   1.00 18.47 ? 149 ILE A CD1 1 
ATOM   1084 N  N   . GLY A 1 150 ? 34.688 0.415   7.401   1.00 18.63 ? 150 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 150 ? 33.752 0.097   8.462   1.00 19.62 ? 150 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 150 ? 32.306 -0.020  8.034   1.00 18.46 ? 150 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 150 ? 31.919 0.457   6.974   1.00 17.58 ? 150 GLY A O   1 
ATOM   1088 N  N   . ILE A 1 151 ? 31.510 -0.672  8.874   1.00 20.31 ? 151 ILE A N   1 
ATOM   1089 C  CA  . ILE A 1 151 ? 30.094 -0.853  8.608   1.00 20.82 ? 151 ILE A CA  1 
ATOM   1090 C  C   . ILE A 1 151 ? 29.393 0.498   8.704   1.00 20.77 ? 151 ILE A C   1 
ATOM   1091 O  O   . ILE A 1 151 ? 29.612 1.250   9.655   1.00 22.11 ? 151 ILE A O   1 
ATOM   1092 C  CB  . ILE A 1 151 ? 29.474 -1.828  9.625   1.00 20.50 ? 151 ILE A CB  1 
ATOM   1093 C  CG1 . ILE A 1 151 ? 30.138 -3.200  9.486   1.00 22.04 ? 151 ILE A CG1 1 
ATOM   1094 C  CG2 . ILE A 1 151 ? 27.972 -1.938  9.393   1.00 22.43 ? 151 ILE A CG2 1 
ATOM   1095 C  CD1 . ILE A 1 151 ? 29.807 -4.162  10.610  1.00 22.32 ? 151 ILE A CD1 1 
ATOM   1096 N  N   . ALA A 1 152 ? 28.554 0.801   7.719   1.00 21.69 ? 152 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 152 ? 27.831 2.069   7.695   1.00 23.65 ? 152 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 152 ? 26.322 1.858   7.728   1.00 25.22 ? 152 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 152 ? 25.823 0.792   7.367   1.00 24.66 ? 152 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 152 ? 28.217 2.863   6.453   1.00 24.23 ? 152 ALA A CB  1 
ATOM   1101 N  N   . GLN A 1 153 ? 25.602 2.889   8.156   1.00 28.76 ? 153 GLN A N   1 
ATOM   1102 C  CA  . GLN A 1 153 ? 24.150 2.831   8.240   1.00 30.27 ? 153 GLN A CA  1 
ATOM   1103 C  C   . GLN A 1 153 ? 23.502 2.913   6.860   1.00 31.08 ? 153 GLN A C   1 
ATOM   1104 O  O   . GLN A 1 153 ? 24.041 3.624   5.985   1.00 31.48 ? 153 GLN A O   1 
ATOM   1105 C  CB  . GLN A 1 153 ? 23.645 3.973   9.122   1.00 31.33 ? 153 GLN A CB  1 
ATOM   1106 C  CG  . GLN A 1 153 ? 22.142 4.190   9.085   1.00 34.92 ? 153 GLN A CG  1 
ATOM   1107 C  CD  . GLN A 1 153 ? 21.688 5.234   10.084  1.00 35.78 ? 153 GLN A CD  1 
ATOM   1108 O  OE1 . GLN A 1 153 ? 21.620 4.973   11.284  1.00 38.78 ? 153 GLN A OE1 1 
ATOM   1109 N  NE2 . GLN A 1 153 ? 21.389 6.430   9.595   1.00 38.00 ? 153 GLN A NE2 1 
ATOM   1110 O  OXT . GLN A 1 153 ? 22.447 2.273   6.686   1.00 31.62 ? 153 GLN A OXT 1 
ATOM   1111 N  N   . ALA B 1 1   ? 39.722 -11.670 12.269  1.00 37.98 ? 1   ALA B N   1 
ATOM   1112 C  CA  . ALA B 1 1   ? 39.924 -13.145 12.371  1.00 37.03 ? 1   ALA B CA  1 
ATOM   1113 C  C   . ALA B 1 1   ? 40.129 -13.549 13.828  1.00 35.22 ? 1   ALA B C   1 
ATOM   1114 O  O   . ALA B 1 1   ? 39.168 -13.795 14.556  1.00 34.94 ? 1   ALA B O   1 
ATOM   1115 C  CB  . ALA B 1 1   ? 41.128 -13.561 11.535  1.00 38.98 ? 1   ALA B CB  1 
ATOM   1116 N  N   . THR B 1 2   ? 41.390 -13.623 14.243  1.00 33.41 ? 2   THR B N   1 
ATOM   1117 C  CA  . THR B 1 2   ? 41.722 -13.983 15.614  1.00 29.95 ? 2   THR B CA  1 
ATOM   1118 C  C   . THR B 1 2   ? 42.279 -12.762 16.327  1.00 26.20 ? 2   THR B C   1 
ATOM   1119 O  O   . THR B 1 2   ? 42.399 -12.749 17.547  1.00 24.12 ? 2   THR B O   1 
ATOM   1120 C  CB  . THR B 1 2   ? 42.780 -15.107 15.673  1.00 32.61 ? 2   THR B CB  1 
ATOM   1121 O  OG1 . THR B 1 2   ? 44.006 -14.644 15.091  1.00 35.63 ? 2   THR B OG1 1 
ATOM   1122 C  CG2 . THR B 1 2   ? 42.299 -16.332 14.916  1.00 33.18 ? 2   THR B CG2 1 
ATOM   1123 N  N   . LYS B 1 3   ? 42.613 -11.730 15.559  1.00 24.33 ? 3   LYS B N   1 
ATOM   1124 C  CA  . LYS B 1 3   ? 43.164 -10.512 16.137  1.00 23.81 ? 3   LYS B CA  1 
ATOM   1125 C  C   . LYS B 1 3   ? 42.646 -9.257  15.436  1.00 21.11 ? 3   LYS B C   1 
ATOM   1126 O  O   . LYS B 1 3   ? 42.469 -9.241  14.223  1.00 20.34 ? 3   LYS B O   1 
ATOM   1127 C  CB  . LYS B 1 3   ? 44.691 -10.575 16.072  1.00 27.58 ? 3   LYS B CB  1 
ATOM   1128 C  CG  . LYS B 1 3   ? 45.407 -9.493  16.849  1.00 32.29 ? 3   LYS B CG  1 
ATOM   1129 C  CD  . LYS B 1 3   ? 46.882 -9.847  17.008  1.00 35.60 ? 3   LYS B CD  1 
ATOM   1130 C  CE  . LYS B 1 3   ? 47.048 -11.123 17.822  1.00 38.96 ? 3   LYS B CE  1 
ATOM   1131 N  NZ  . LYS B 1 3   ? 47.845 -12.160 17.108  1.00 38.97 ? 3   LYS B NZ  1 
ATOM   1132 N  N   . ALA B 1 4   ? 42.392 -8.210  16.213  1.00 19.46 ? 4   ALA B N   1 
ATOM   1133 C  CA  . ALA B 1 4   ? 41.897 -6.953  15.665  1.00 19.63 ? 4   ALA B CA  1 
ATOM   1134 C  C   . ALA B 1 4   ? 42.524 -5.801  16.436  1.00 20.80 ? 4   ALA B C   1 
ATOM   1135 O  O   . ALA B 1 4   ? 43.111 -6.005  17.501  1.00 21.19 ? 4   ALA B O   1 
ATOM   1136 C  CB  . ALA B 1 4   ? 40.378 -6.897  15.769  1.00 18.94 ? 4   ALA B CB  1 
ATOM   1137 N  N   . VAL B 1 5   ? 42.403 -4.592  15.901  1.00 19.98 ? 5   VAL B N   1 
ATOM   1138 C  CA  . VAL B 1 5   ? 42.980 -3.426  16.553  1.00 19.63 ? 5   VAL B CA  1 
ATOM   1139 C  C   . VAL B 1 5   ? 42.196 -2.169  16.214  1.00 20.50 ? 5   VAL B C   1 
ATOM   1140 O  O   . VAL B 1 5   ? 41.543 -2.089  15.174  1.00 19.82 ? 5   VAL B O   1 
ATOM   1141 C  CB  . VAL B 1 5   ? 44.463 -3.226  16.121  1.00 20.56 ? 5   VAL B CB  1 
ATOM   1142 C  CG1 . VAL B 1 5   ? 44.533 -2.828  14.643  1.00 17.68 ? 5   VAL B CG1 1 
ATOM   1143 C  CG2 . VAL B 1 5   ? 45.133 -2.167  16.992  1.00 19.83 ? 5   VAL B CG2 1 
ATOM   1144 N  N   . ALA B 1 6   ? 42.253 -1.194  17.112  1.00 18.84 ? 6   ALA B N   1 
ATOM   1145 C  CA  . ALA B 1 6   ? 41.581 0.076   16.905  1.00 18.39 ? 6   ALA B CA  1 
ATOM   1146 C  C   . ALA B 1 6   ? 42.525 1.175   17.363  1.00 18.61 ? 6   ALA B C   1 
ATOM   1147 O  O   . ALA B 1 6   ? 43.101 1.100   18.449  1.00 20.39 ? 6   ALA B O   1 
ATOM   1148 C  CB  . ALA B 1 6   ? 40.283 0.131   17.700  1.00 19.73 ? 6   ALA B CB  1 
ATOM   1149 N  N   . VAL B 1 7   ? 42.705 2.176   16.514  1.00 17.39 ? 7   VAL B N   1 
ATOM   1150 C  CA  . VAL B 1 7   ? 43.558 3.306   16.835  1.00 19.35 ? 7   VAL B CA  1 
ATOM   1151 C  C   . VAL B 1 7   ? 42.613 4.449   17.176  1.00 19.96 ? 7   VAL B C   1 
ATOM   1152 O  O   . VAL B 1 7   ? 41.897 4.954   16.313  1.00 20.68 ? 7   VAL B O   1 
ATOM   1153 C  CB  . VAL B 1 7   ? 44.440 3.689   15.637  1.00 19.26 ? 7   VAL B CB  1 
ATOM   1154 C  CG1 . VAL B 1 7   ? 45.285 4.901   15.977  1.00 21.91 ? 7   VAL B CG1 1 
ATOM   1155 C  CG2 . VAL B 1 7   ? 45.325 2.513   15.258  1.00 21.33 ? 7   VAL B CG2 1 
ATOM   1156 N  N   . LEU B 1 8   ? 42.605 4.844   18.444  1.00 19.75 ? 8   LEU B N   1 
ATOM   1157 C  CA  . LEU B 1 8   ? 41.713 5.899   18.903  1.00 20.44 ? 8   LEU B CA  1 
ATOM   1158 C  C   . LEU B 1 8   ? 42.266 7.297   18.675  1.00 20.81 ? 8   LEU B C   1 
ATOM   1159 O  O   . LEU B 1 8   ? 43.395 7.604   19.056  1.00 21.98 ? 8   LEU B O   1 
ATOM   1160 C  CB  . LEU B 1 8   ? 41.399 5.702   20.391  1.00 20.86 ? 8   LEU B CB  1 
ATOM   1161 C  CG  . LEU B 1 8   ? 40.840 4.328   20.783  1.00 23.54 ? 8   LEU B CG  1 
ATOM   1162 C  CD1 . LEU B 1 8   ? 40.743 4.231   22.297  1.00 24.67 ? 8   LEU B CD1 1 
ATOM   1163 C  CD2 . LEU B 1 8   ? 39.478 4.117   20.145  1.00 24.44 ? 8   LEU B CD2 1 
ATOM   1164 N  N   . LYS B 1 9   ? 41.453 8.137   18.047  1.00 21.64 ? 9   LYS B N   1 
ATOM   1165 C  CA  . LYS B 1 9   ? 41.825 9.515   17.767  1.00 23.48 ? 9   LYS B CA  1 
ATOM   1166 C  C   . LYS B 1 9   ? 40.575 10.376  17.865  1.00 22.81 ? 9   LYS B C   1 
ATOM   1167 O  O   . LYS B 1 9   ? 39.468 9.897   17.639  1.00 20.92 ? 9   LYS B O   1 
ATOM   1168 C  CB  . LYS B 1 9   ? 42.441 9.618   16.370  1.00 25.85 ? 9   LYS B CB  1 
ATOM   1169 C  CG  . LYS B 1 9   ? 43.702 8.778   16.210  1.00 30.70 ? 9   LYS B CG  1 
ATOM   1170 C  CD  . LYS B 1 9   ? 44.322 8.923   14.830  1.00 35.37 ? 9   LYS B CD  1 
ATOM   1171 C  CE  . LYS B 1 9   ? 45.608 8.112   14.731  1.00 37.26 ? 9   LYS B CE  1 
ATOM   1172 N  NZ  . LYS B 1 9   ? 46.200 8.154   13.367  1.00 41.31 ? 9   LYS B NZ  1 
ATOM   1173 N  N   . GLY B 1 10  ? 40.752 11.643  18.218  1.00 25.35 ? 10  GLY B N   1 
ATOM   1174 C  CA  . GLY B 1 10  ? 39.613 12.535  18.334  1.00 28.98 ? 10  GLY B CA  1 
ATOM   1175 C  C   . GLY B 1 10  ? 39.988 13.957  17.976  1.00 30.49 ? 10  GLY B C   1 
ATOM   1176 O  O   . GLY B 1 10  ? 41.013 14.185  17.331  1.00 30.13 ? 10  GLY B O   1 
ATOM   1177 N  N   . ASP B 1 11  ? 39.162 14.913  18.389  1.00 33.46 ? 11  ASP B N   1 
ATOM   1178 C  CA  . ASP B 1 11  ? 39.426 16.322  18.108  1.00 36.67 ? 11  ASP B CA  1 
ATOM   1179 C  C   . ASP B 1 11  ? 40.352 16.913  19.157  1.00 36.64 ? 11  ASP B C   1 
ATOM   1180 O  O   . ASP B 1 11  ? 40.950 17.968  18.950  1.00 37.59 ? 11  ASP B O   1 
ATOM   1181 C  CB  . ASP B 1 11  ? 38.122 17.123  18.079  1.00 40.20 ? 11  ASP B CB  1 
ATOM   1182 C  CG  . ASP B 1 11  ? 37.229 16.740  16.919  1.00 43.26 ? 11  ASP B CG  1 
ATOM   1183 O  OD1 . ASP B 1 11  ? 37.738 16.645  15.780  1.00 46.54 ? 11  ASP B OD1 1 
ATOM   1184 O  OD2 . ASP B 1 11  ? 36.016 16.543  17.145  1.00 46.61 ? 11  ASP B OD2 1 
ATOM   1185 N  N   . GLY B 1 12  ? 40.460 16.226  20.288  1.00 35.97 ? 12  GLY B N   1 
ATOM   1186 C  CA  . GLY B 1 12  ? 41.320 16.695  21.356  1.00 33.83 ? 12  GLY B CA  1 
ATOM   1187 C  C   . GLY B 1 12  ? 42.608 15.898  21.430  1.00 33.50 ? 12  GLY B C   1 
ATOM   1188 O  O   . GLY B 1 12  ? 43.019 15.286  20.445  1.00 33.38 ? 12  GLY B O   1 
ATOM   1189 N  N   . PRO B 1 13  ? 43.265 15.883  22.597  1.00 33.52 ? 13  PRO B N   1 
ATOM   1190 C  CA  . PRO B 1 13  ? 44.521 15.169  22.839  1.00 32.38 ? 13  PRO B CA  1 
ATOM   1191 C  C   . PRO B 1 13  ? 44.385 13.676  23.141  1.00 31.47 ? 13  PRO B C   1 
ATOM   1192 O  O   . PRO B 1 13  ? 45.392 12.978  23.250  1.00 31.10 ? 13  PRO B O   1 
ATOM   1193 C  CB  . PRO B 1 13  ? 45.104 15.922  24.022  1.00 33.00 ? 13  PRO B CB  1 
ATOM   1194 C  CG  . PRO B 1 13  ? 43.878 16.204  24.827  1.00 33.87 ? 13  PRO B CG  1 
ATOM   1195 C  CD  . PRO B 1 13  ? 42.907 16.704  23.769  1.00 34.32 ? 13  PRO B CD  1 
ATOM   1196 N  N   . VAL B 1 14  ? 43.157 13.185  23.284  1.00 28.71 ? 14  VAL B N   1 
ATOM   1197 C  CA  . VAL B 1 14  ? 42.956 11.772  23.599  1.00 27.20 ? 14  VAL B CA  1 
ATOM   1198 C  C   . VAL B 1 14  ? 43.354 10.858  22.446  1.00 27.01 ? 14  VAL B C   1 
ATOM   1199 O  O   . VAL B 1 14  ? 42.837 10.978  21.337  1.00 24.99 ? 14  VAL B O   1 
ATOM   1200 C  CB  . VAL B 1 14  ? 41.489 11.484  23.984  1.00 26.00 ? 14  VAL B CB  1 
ATOM   1201 C  CG1 . VAL B 1 14  ? 41.350 10.038  24.446  1.00 25.74 ? 14  VAL B CG1 1 
ATOM   1202 C  CG2 . VAL B 1 14  ? 41.045 12.437  25.084  1.00 26.47 ? 14  VAL B CG2 1 
ATOM   1203 N  N   . GLN B 1 15  ? 44.281 9.946   22.719  1.00 27.77 ? 15  GLN B N   1 
ATOM   1204 C  CA  . GLN B 1 15  ? 44.754 9.005   21.709  1.00 29.40 ? 15  GLN B CA  1 
ATOM   1205 C  C   . GLN B 1 15  ? 45.057 7.668   22.363  1.00 29.55 ? 15  GLN B C   1 
ATOM   1206 O  O   . GLN B 1 15  ? 45.272 7.598   23.572  1.00 31.31 ? 15  GLN B O   1 
ATOM   1207 C  CB  . GLN B 1 15  ? 46.030 9.525   21.044  1.00 31.42 ? 15  GLN B CB  1 
ATOM   1208 C  CG  . GLN B 1 15  ? 45.882 10.861  20.346  1.00 37.39 ? 15  GLN B CG  1 
ATOM   1209 C  CD  . GLN B 1 15  ? 47.198 11.367  19.785  1.00 40.06 ? 15  GLN B CD  1 
ATOM   1210 O  OE1 . GLN B 1 15  ? 48.262 10.813  20.072  1.00 41.47 ? 15  GLN B OE1 1 
ATOM   1211 N  NE2 . GLN B 1 15  ? 47.135 12.430  18.990  1.00 42.57 ? 15  GLN B NE2 1 
ATOM   1212 N  N   . GLY B 1 16  ? 45.079 6.609   21.563  1.00 28.02 ? 16  GLY B N   1 
ATOM   1213 C  CA  . GLY B 1 16  ? 45.377 5.301   22.110  1.00 26.84 ? 16  GLY B CA  1 
ATOM   1214 C  C   . GLY B 1 16  ? 45.259 4.172   21.108  1.00 25.00 ? 16  GLY B C   1 
ATOM   1215 O  O   . GLY B 1 16  ? 44.718 4.342   20.014  1.00 25.19 ? 16  GLY B O   1 
ATOM   1216 N  N   . ILE B 1 17  ? 45.789 3.015   21.490  1.00 24.04 ? 17  ILE B N   1 
ATOM   1217 C  CA  . ILE B 1 17  ? 45.743 1.821   20.658  1.00 22.05 ? 17  ILE B CA  1 
ATOM   1218 C  C   . ILE B 1 17  ? 45.185 0.691   21.511  1.00 21.26 ? 17  ILE B C   1 
ATOM   1219 O  O   . ILE B 1 17  ? 45.719 0.394   22.580  1.00 19.79 ? 17  ILE B O   1 
ATOM   1220 C  CB  . ILE B 1 17  ? 47.147 1.421   20.158  1.00 22.51 ? 17  ILE B CB  1 
ATOM   1221 C  CG1 . ILE B 1 17  ? 47.704 2.511   19.239  1.00 22.69 ? 17  ILE B CG1 1 
ATOM   1222 C  CG2 . ILE B 1 17  ? 47.074 0.095   19.414  1.00 22.82 ? 17  ILE B CG2 1 
ATOM   1223 C  CD1 . ILE B 1 17  ? 49.088 2.211   18.694  1.00 24.23 ? 17  ILE B CD1 1 
ATOM   1224 N  N   . ILE B 1 18  ? 44.102 0.076   21.043  1.00 19.17 ? 18  ILE B N   1 
ATOM   1225 C  CA  . ILE B 1 18  ? 43.470 -1.018  21.768  1.00 19.31 ? 18  ILE B CA  1 
ATOM   1226 C  C   . ILE B 1 18  ? 43.496 -2.272  20.904  1.00 19.21 ? 18  ILE B C   1 
ATOM   1227 O  O   . ILE B 1 18  ? 43.013 -2.271  19.772  1.00 20.06 ? 18  ILE B O   1 
ATOM   1228 C  CB  . ILE B 1 18  ? 42.003 -0.673  22.140  1.00 16.82 ? 18  ILE B CB  1 
ATOM   1229 C  CG1 . ILE B 1 18  ? 41.974 0.533   23.083  1.00 17.96 ? 18  ILE B CG1 1 
ATOM   1230 C  CG2 . ILE B 1 18  ? 41.327 -1.880  22.787  1.00 16.77 ? 18  ILE B CG2 1 
ATOM   1231 C  CD1 . ILE B 1 18  ? 42.637 0.288   24.431  1.00 20.56 ? 18  ILE B CD1 1 
ATOM   1232 N  N   . ASN B 1 19  ? 44.065 -3.341  21.450  1.00 20.40 ? 19  ASN B N   1 
ATOM   1233 C  CA  . ASN B 1 19  ? 44.177 -4.608  20.740  1.00 20.44 ? 19  ASN B CA  1 
ATOM   1234 C  C   . ASN B 1 19  ? 43.092 -5.582  21.178  1.00 20.55 ? 19  ASN B C   1 
ATOM   1235 O  O   . ASN B 1 19  ? 42.651 -5.551  22.326  1.00 20.95 ? 19  ASN B O   1 
ATOM   1236 C  CB  . ASN B 1 19  ? 45.546 -5.230  21.014  1.00 22.55 ? 19  ASN B CB  1 
ATOM   1237 C  CG  . ASN B 1 19  ? 46.691 -4.297  20.667  1.00 24.36 ? 19  ASN B CG  1 
ATOM   1238 O  OD1 . ASN B 1 19  ? 47.053 -4.146  19.501  1.00 25.10 ? 19  ASN B OD1 1 
ATOM   1239 N  ND2 . ASN B 1 19  ? 47.257 -3.655  21.682  1.00 24.76 ? 19  ASN B ND2 1 
ATOM   1240 N  N   . PHE B 1 20  ? 42.677 -6.441  20.251  1.00 19.86 ? 20  PHE B N   1 
ATOM   1241 C  CA  . PHE B 1 20  ? 41.659 -7.464  20.497  1.00 20.58 ? 20  PHE B CA  1 
ATOM   1242 C  C   . PHE B 1 20  ? 42.202 -8.818  20.048  1.00 21.23 ? 20  PHE B C   1 
ATOM   1243 O  O   . PHE B 1 20  ? 42.817 -8.929  18.991  1.00 20.40 ? 20  PHE B O   1 
ATOM   1244 C  CB  . PHE B 1 20  ? 40.389 -7.181  19.688  1.00 19.90 ? 20  PHE B CB  1 
ATOM   1245 C  CG  . PHE B 1 20  ? 39.705 -5.898  20.048  1.00 22.32 ? 20  PHE B CG  1 
ATOM   1246 C  CD1 . PHE B 1 20  ? 38.687 -5.880  20.999  1.00 21.11 ? 20  PHE B CD1 1 
ATOM   1247 C  CD2 . PHE B 1 20  ? 40.072 -4.706  19.430  1.00 21.38 ? 20  PHE B CD2 1 
ATOM   1248 C  CE1 . PHE B 1 20  ? 38.040 -4.688  21.327  1.00 21.03 ? 20  PHE B CE1 1 
ATOM   1249 C  CE2 . PHE B 1 20  ? 39.434 -3.512  19.750  1.00 20.35 ? 20  PHE B CE2 1 
ATOM   1250 C  CZ  . PHE B 1 20  ? 38.415 -3.504  20.701  1.00 22.17 ? 20  PHE B CZ  1 
ATOM   1251 N  N   . GLU B 1 21  ? 41.973 -9.850  20.848  1.00 20.90 ? 21  GLU B N   1 
ATOM   1252 C  CA  . GLU B 1 21  ? 42.426 -11.178 20.480  1.00 22.90 ? 21  GLU B CA  1 
ATOM   1253 C  C   . GLU B 1 21  ? 41.408 -12.209 20.926  1.00 22.32 ? 21  GLU B C   1 
ATOM   1254 O  O   . GLU B 1 21  ? 40.910 -12.158 22.049  1.00 21.59 ? 21  GLU B O   1 
ATOM   1255 C  CB  . GLU B 1 21  ? 43.783 -11.487 21.110  1.00 25.30 ? 21  GLU B CB  1 
ATOM   1256 C  CG  . GLU B 1 21  ? 44.251 -12.919 20.880  1.00 30.99 ? 21  GLU B CG  1 
ATOM   1257 C  CD  . GLU B 1 21  ? 45.599 -13.202 21.521  1.00 36.32 ? 21  GLU B CD  1 
ATOM   1258 O  OE1 . GLU B 1 21  ? 46.614 -12.680 21.023  1.00 37.66 ? 21  GLU B OE1 1 
ATOM   1259 O  OE2 . GLU B 1 21  ? 45.639 -13.936 22.532  1.00 40.02 ? 21  GLU B OE2 1 
ATOM   1260 N  N   . GLN B 1 22  ? 41.094 -13.136 20.031  1.00 23.61 ? 22  GLN B N   1 
ATOM   1261 C  CA  . GLN B 1 22  ? 40.145 -14.195 20.328  1.00 24.81 ? 22  GLN B CA  1 
ATOM   1262 C  C   . GLN B 1 22  ? 40.716 -15.495 19.768  1.00 28.57 ? 22  GLN B C   1 
ATOM   1263 O  O   . GLN B 1 22  ? 40.630 -15.764 18.571  1.00 29.42 ? 22  GLN B O   1 
ATOM   1264 C  CB  . GLN B 1 22  ? 38.782 -13.872 19.707  1.00 22.52 ? 22  GLN B CB  1 
ATOM   1265 C  CG  . GLN B 1 22  ? 37.698 -14.909 19.988  1.00 21.47 ? 22  GLN B CG  1 
ATOM   1266 C  CD  . GLN B 1 22  ? 36.348 -14.529 19.397  1.00 22.02 ? 22  GLN B CD  1 
ATOM   1267 O  OE1 . GLN B 1 22  ? 36.273 -13.923 18.326  1.00 19.05 ? 22  GLN B OE1 1 
ATOM   1268 N  NE2 . GLN B 1 22  ? 35.270 -14.903 20.088  1.00 21.15 ? 22  GLN B NE2 1 
ATOM   1269 N  N   . LYS B 1 23  ? 41.320 -16.280 20.654  1.00 32.59 ? 23  LYS B N   1 
ATOM   1270 C  CA  . LYS B 1 23  ? 41.934 -17.555 20.298  1.00 36.50 ? 23  LYS B CA  1 
ATOM   1271 C  C   . LYS B 1 23  ? 40.945 -18.489 19.604  1.00 37.37 ? 23  LYS B C   1 
ATOM   1272 O  O   . LYS B 1 23  ? 41.195 -18.963 18.494  1.00 39.25 ? 23  LYS B O   1 
ATOM   1273 C  CB  . LYS B 1 23  ? 42.462 -18.252 21.557  1.00 39.88 ? 23  LYS B CB  1 
ATOM   1274 C  CG  . LYS B 1 23  ? 43.375 -17.411 22.438  1.00 43.32 ? 23  LYS B CG  1 
ATOM   1275 C  CD  . LYS B 1 23  ? 44.785 -17.299 21.881  1.00 45.92 ? 23  LYS B CD  1 
ATOM   1276 C  CE  . LYS B 1 23  ? 45.733 -16.737 22.938  1.00 46.93 ? 23  LYS B CE  1 
ATOM   1277 N  NZ  . LYS B 1 23  ? 47.123 -16.552 22.433  1.00 47.78 ? 23  LYS B NZ  1 
ATOM   1278 N  N   . GLU B 1 24  ? 39.826 -18.752 20.272  1.00 37.60 ? 24  GLU B N   1 
ATOM   1279 C  CA  . GLU B 1 24  ? 38.802 -19.648 19.745  1.00 37.04 ? 24  GLU B CA  1 
ATOM   1280 C  C   . GLU B 1 24  ? 37.583 -18.897 19.227  1.00 36.28 ? 24  GLU B C   1 
ATOM   1281 O  O   . GLU B 1 24  ? 37.243 -17.824 19.730  1.00 35.55 ? 24  GLU B O   1 
ATOM   1282 C  CB  . GLU B 1 24  ? 38.377 -20.634 20.834  1.00 40.29 ? 24  GLU B CB  1 
ATOM   1283 C  CG  . GLU B 1 24  ? 39.529 -21.459 21.392  1.00 44.12 ? 24  GLU B CG  1 
ATOM   1284 C  CD  . GLU B 1 24  ? 40.083 -22.454 20.384  1.00 46.89 ? 24  GLU B CD  1 
ATOM   1285 O  OE1 . GLU B 1 24  ? 41.134 -23.068 20.671  1.00 48.79 ? 24  GLU B OE1 1 
ATOM   1286 O  OE2 . GLU B 1 24  ? 39.467 -22.628 19.310  1.00 47.41 ? 24  GLU B OE2 1 
ATOM   1287 N  N   . SER B 1 25  ? 36.921 -19.478 18.229  1.00 33.37 ? 25  SER B N   1 
ATOM   1288 C  CA  . SER B 1 25  ? 35.743 -18.869 17.618  1.00 32.48 ? 25  SER B CA  1 
ATOM   1289 C  C   . SER B 1 25  ? 34.644 -18.517 18.622  1.00 30.83 ? 25  SER B C   1 
ATOM   1290 O  O   . SER B 1 25  ? 33.879 -17.577 18.402  1.00 29.45 ? 25  SER B O   1 
ATOM   1291 C  CB  . SER B 1 25  ? 35.171 -19.793 16.541  1.00 33.63 ? 25  SER B CB  1 
ATOM   1292 O  OG  . SER B 1 25  ? 34.753 -21.025 17.101  1.00 37.51 ? 25  SER B OG  1 
ATOM   1293 N  N   . ASN B 1 26  ? 34.549 -19.279 19.707  1.00 28.00 ? 26  ASN B N   1 
ATOM   1294 C  CA  . ASN B 1 26  ? 33.547 -19.003 20.727  1.00 27.28 ? 26  ASN B CA  1 
ATOM   1295 C  C   . ASN B 1 26  ? 34.203 -18.771 22.084  1.00 26.77 ? 26  ASN B C   1 
ATOM   1296 O  O   . ASN B 1 26  ? 33.597 -18.993 23.132  1.00 28.58 ? 26  ASN B O   1 
ATOM   1297 C  CB  . ASN B 1 26  ? 32.519 -20.144 20.817  1.00 27.73 ? 26  ASN B CB  1 
ATOM   1298 C  CG  . ASN B 1 26  ? 33.146 -21.481 21.164  1.00 28.46 ? 26  ASN B CG  1 
ATOM   1299 O  OD1 . ASN B 1 26  ? 34.339 -21.569 21.459  1.00 29.30 ? 26  ASN B OD1 1 
ATOM   1300 N  ND2 . ASN B 1 26  ? 32.336 -22.534 21.133  1.00 28.71 ? 26  ASN B ND2 1 
ATOM   1301 N  N   . GLY B 1 27  ? 35.451 -18.320 22.054  1.00 25.12 ? 27  GLY B N   1 
ATOM   1302 C  CA  . GLY B 1 27  ? 36.168 -18.044 23.282  1.00 22.68 ? 27  GLY B CA  1 
ATOM   1303 C  C   . GLY B 1 27  ? 36.051 -16.570 23.626  1.00 23.60 ? 27  GLY B C   1 
ATOM   1304 O  O   . GLY B 1 27  ? 35.514 -15.793 22.830  1.00 22.26 ? 27  GLY B O   1 
ATOM   1305 N  N   . PRO B 1 28  ? 36.530 -16.153 24.807  1.00 22.25 ? 28  PRO B N   1 
ATOM   1306 C  CA  . PRO B 1 28  ? 36.460 -14.750 25.216  1.00 21.82 ? 28  PRO B CA  1 
ATOM   1307 C  C   . PRO B 1 28  ? 37.400 -13.884 24.385  1.00 21.13 ? 28  PRO B C   1 
ATOM   1308 O  O   . PRO B 1 28  ? 38.364 -14.382 23.800  1.00 21.20 ? 28  PRO B O   1 
ATOM   1309 C  CB  . PRO B 1 28  ? 36.879 -14.801 26.680  1.00 23.71 ? 28  PRO B CB  1 
ATOM   1310 C  CG  . PRO B 1 28  ? 37.879 -15.922 26.690  1.00 23.51 ? 28  PRO B CG  1 
ATOM   1311 C  CD  . PRO B 1 28  ? 37.196 -16.968 25.842  1.00 23.01 ? 28  PRO B CD  1 
ATOM   1312 N  N   . VAL B 1 29  ? 37.112 -12.591 24.321  1.00 18.86 ? 29  VAL B N   1 
ATOM   1313 C  CA  . VAL B 1 29  ? 37.965 -11.683 23.576  1.00 19.71 ? 29  VAL B CA  1 
ATOM   1314 C  C   . VAL B 1 29  ? 38.800 -10.893 24.570  1.00 19.75 ? 29  VAL B C   1 
ATOM   1315 O  O   . VAL B 1 29  ? 38.264 -10.270 25.483  1.00 20.45 ? 29  VAL B O   1 
ATOM   1316 C  CB  . VAL B 1 29  ? 37.141 -10.699 22.712  1.00 20.39 ? 29  VAL B CB  1 
ATOM   1317 C  CG1 . VAL B 1 29  ? 38.075 -9.758  21.956  1.00 21.17 ? 29  VAL B CG1 1 
ATOM   1318 C  CG2 . VAL B 1 29  ? 36.277 -11.470 21.730  1.00 19.94 ? 29  VAL B CG2 1 
ATOM   1319 N  N   . LYS B 1 30  ? 40.117 -10.942 24.410  1.00 20.15 ? 30  LYS B N   1 
ATOM   1320 C  CA  . LYS B 1 30  ? 41.005 -10.197 25.291  1.00 22.28 ? 30  LYS B CA  1 
ATOM   1321 C  C   . LYS B 1 30  ? 41.127 -8.798  24.695  1.00 20.65 ? 30  LYS B C   1 
ATOM   1322 O  O   . LYS B 1 30  ? 41.325 -8.653  23.492  1.00 20.72 ? 30  LYS B O   1 
ATOM   1323 C  CB  . LYS B 1 30  ? 42.382 -10.865 25.347  1.00 24.93 ? 30  LYS B CB  1 
ATOM   1324 C  CG  . LYS B 1 30  ? 42.342 -12.303 25.836  1.00 30.94 ? 30  LYS B CG  1 
ATOM   1325 C  CD  . LYS B 1 30  ? 43.667 -13.016 25.603  1.00 34.90 ? 30  LYS B CD  1 
ATOM   1326 C  CE  . LYS B 1 30  ? 43.561 -14.487 25.977  1.00 38.13 ? 30  LYS B CE  1 
ATOM   1327 N  NZ  . LYS B 1 30  ? 44.767 -15.258 25.556  1.00 40.71 ? 30  LYS B NZ  1 
ATOM   1328 N  N   . VAL B 1 31  ? 40.991 -7.778  25.535  1.00 20.19 ? 31  VAL B N   1 
ATOM   1329 C  CA  . VAL B 1 31  ? 41.083 -6.386  25.098  1.00 19.58 ? 31  VAL B CA  1 
ATOM   1330 C  C   . VAL B 1 31  ? 42.172 -5.707  25.920  1.00 20.24 ? 31  VAL B C   1 
ATOM   1331 O  O   . VAL B 1 31  ? 42.089 -5.671  27.145  1.00 21.45 ? 31  VAL B O   1 
ATOM   1332 C  CB  . VAL B 1 31  ? 39.749 -5.643  25.335  1.00 19.69 ? 31  VAL B CB  1 
ATOM   1333 C  CG1 . VAL B 1 31  ? 39.839 -4.207  24.818  1.00 18.86 ? 31  VAL B CG1 1 
ATOM   1334 C  CG2 . VAL B 1 31  ? 38.621 -6.395  24.656  1.00 19.06 ? 31  VAL B CG2 1 
ATOM   1335 N  N   . TRP B 1 32  ? 43.185 -5.160  25.259  1.00 20.08 ? 32  TRP B N   1 
ATOM   1336 C  CA  . TRP B 1 32  ? 44.264 -4.519  26.000  1.00 21.26 ? 32  TRP B CA  1 
ATOM   1337 C  C   . TRP B 1 32  ? 44.963 -3.422  25.213  1.00 20.92 ? 32  TRP B C   1 
ATOM   1338 O  O   . TRP B 1 32  ? 45.023 -3.456  23.986  1.00 20.20 ? 32  TRP B O   1 
ATOM   1339 C  CB  . TRP B 1 32  ? 45.284 -5.574  26.432  1.00 22.91 ? 32  TRP B CB  1 
ATOM   1340 C  CG  . TRP B 1 32  ? 46.192 -6.023  25.336  1.00 26.50 ? 32  TRP B CG  1 
ATOM   1341 C  CD1 . TRP B 1 32  ? 47.435 -5.527  25.048  1.00 27.38 ? 32  TRP B CD1 1 
ATOM   1342 C  CD2 . TRP B 1 32  ? 45.938 -7.053  24.375  1.00 28.12 ? 32  TRP B CD2 1 
ATOM   1343 N  NE1 . TRP B 1 32  ? 47.969 -6.189  23.970  1.00 29.73 ? 32  TRP B NE1 1 
ATOM   1344 C  CE2 . TRP B 1 32  ? 47.072 -7.131  23.537  1.00 28.30 ? 32  TRP B CE2 1 
ATOM   1345 C  CE3 . TRP B 1 32  ? 44.861 -7.920  24.139  1.00 29.77 ? 32  TRP B CE3 1 
ATOM   1346 C  CZ2 . TRP B 1 32  ? 47.163 -8.041  22.479  1.00 30.59 ? 32  TRP B CZ2 1 
ATOM   1347 C  CZ3 . TRP B 1 32  ? 44.951 -8.828  23.085  1.00 30.65 ? 32  TRP B CZ3 1 
ATOM   1348 C  CH2 . TRP B 1 32  ? 46.097 -8.880  22.269  1.00 31.66 ? 32  TRP B CH2 1 
ATOM   1349 N  N   . GLY B 1 33  ? 45.490 -2.447  25.939  1.00 21.45 ? 33  GLY B N   1 
ATOM   1350 C  CA  . GLY B 1 33  ? 46.183 -1.348  25.301  1.00 21.05 ? 33  GLY B CA  1 
ATOM   1351 C  C   . GLY B 1 33  ? 46.282 -0.184  26.258  1.00 22.13 ? 33  GLY B C   1 
ATOM   1352 O  O   . GLY B 1 33  ? 46.196 -0.359  27.475  1.00 20.65 ? 33  GLY B O   1 
ATOM   1353 N  N   . SER B 1 34  ? 46.460 1.009   25.711  1.00 22.69 ? 34  SER B N   1 
ATOM   1354 C  CA  . SER B 1 34  ? 46.574 2.202   26.530  1.00 24.60 ? 34  SER B CA  1 
ATOM   1355 C  C   . SER B 1 34  ? 45.910 3.383   25.845  1.00 23.50 ? 34  SER B C   1 
ATOM   1356 O  O   . SER B 1 34  ? 45.826 3.434   24.619  1.00 25.74 ? 34  SER B O   1 
ATOM   1357 C  CB  . SER B 1 34  ? 48.051 2.521   26.783  1.00 24.63 ? 34  SER B CB  1 
ATOM   1358 O  OG  . SER B 1 34  ? 48.177 3.639   27.643  1.00 29.04 ? 34  SER B OG  1 
ATOM   1359 N  N   . ILE B 1 35  ? 45.430 4.326   26.648  1.00 23.54 ? 35  ILE B N   1 
ATOM   1360 C  CA  . ILE B 1 35  ? 44.786 5.531   26.144  1.00 22.82 ? 35  ILE B CA  1 
ATOM   1361 C  C   . ILE B 1 35  ? 45.348 6.705   26.945  1.00 24.04 ? 35  ILE B C   1 
ATOM   1362 O  O   . ILE B 1 35  ? 45.361 6.669   28.172  1.00 25.08 ? 35  ILE B O   1 
ATOM   1363 C  CB  . ILE B 1 35  ? 43.255 5.477   26.338  1.00 22.39 ? 35  ILE B CB  1 
ATOM   1364 C  CG1 . ILE B 1 35  ? 42.685 4.224   25.664  1.00 19.61 ? 35  ILE B CG1 1 
ATOM   1365 C  CG2 . ILE B 1 35  ? 42.617 6.723   25.752  1.00 21.09 ? 35  ILE B CG2 1 
ATOM   1366 C  CD1 . ILE B 1 35  ? 41.210 3.989   25.931  1.00 20.51 ? 35  ILE B CD1 1 
ATOM   1367 N  N   . LYS B 1 36  ? 45.815 7.738   26.251  1.00 25.89 ? 36  LYS B N   1 
ATOM   1368 C  CA  . LYS B 1 36  ? 46.390 8.907   26.911  1.00 26.57 ? 36  LYS B CA  1 
ATOM   1369 C  C   . LYS B 1 36  ? 45.602 10.185  26.648  1.00 26.03 ? 36  LYS B C   1 
ATOM   1370 O  O   . LYS B 1 36  ? 44.726 10.222  25.784  1.00 24.81 ? 36  LYS B O   1 
ATOM   1371 C  CB  . LYS B 1 36  ? 47.843 9.094   26.458  1.00 29.63 ? 36  LYS B CB  1 
ATOM   1372 C  CG  . LYS B 1 36  ? 48.022 9.032   24.952  1.00 33.40 ? 36  LYS B CG  1 
ATOM   1373 C  CD  . LYS B 1 36  ? 49.483 9.154   24.532  1.00 36.79 ? 36  LYS B CD  1 
ATOM   1374 C  CE  . LYS B 1 36  ? 50.017 10.565  24.738  1.00 38.95 ? 36  LYS B CE  1 
ATOM   1375 N  NZ  . LYS B 1 36  ? 51.397 10.723  24.194  1.00 40.03 ? 36  LYS B NZ  1 
ATOM   1376 N  N   . GLY B 1 37  ? 45.917 11.231  27.407  1.00 26.31 ? 37  GLY B N   1 
ATOM   1377 C  CA  . GLY B 1 37  ? 45.237 12.503  27.242  1.00 26.12 ? 37  GLY B CA  1 
ATOM   1378 C  C   . GLY B 1 37  ? 43.907 12.609  27.964  1.00 26.42 ? 37  GLY B C   1 
ATOM   1379 O  O   . GLY B 1 37  ? 43.179 13.589  27.796  1.00 26.86 ? 37  GLY B O   1 
ATOM   1380 N  N   . LEU B 1 38  ? 43.585 11.607  28.776  1.00 25.92 ? 38  LEU B N   1 
ATOM   1381 C  CA  . LEU B 1 38  ? 42.324 11.601  29.512  1.00 26.31 ? 38  LEU B CA  1 
ATOM   1382 C  C   . LEU B 1 38  ? 42.425 12.299  30.861  1.00 27.11 ? 38  LEU B C   1 
ATOM   1383 O  O   . LEU B 1 38  ? 43.512 12.449  31.413  1.00 28.28 ? 38  LEU B O   1 
ATOM   1384 C  CB  . LEU B 1 38  ? 41.859 10.163  29.749  1.00 26.65 ? 38  LEU B CB  1 
ATOM   1385 C  CG  . LEU B 1 38  ? 41.552 9.297   28.527  1.00 26.88 ? 38  LEU B CG  1 
ATOM   1386 C  CD1 . LEU B 1 38  ? 41.338 7.862   28.967  1.00 26.55 ? 38  LEU B CD1 1 
ATOM   1387 C  CD2 . LEU B 1 38  ? 40.333 9.836   27.813  1.00 24.98 ? 38  LEU B CD2 1 
ATOM   1388 N  N   . THR B 1 39  ? 41.281 12.729  31.382  1.00 28.59 ? 39  THR B N   1 
ATOM   1389 C  CA  . THR B 1 39  ? 41.237 13.361  32.694  1.00 27.38 ? 39  THR B CA  1 
ATOM   1390 C  C   . THR B 1 39  ? 41.147 12.202  33.686  1.00 27.60 ? 39  THR B C   1 
ATOM   1391 O  O   . THR B 1 39  ? 40.404 11.245  33.460  1.00 24.99 ? 39  THR B O   1 
ATOM   1392 C  CB  . THR B 1 39  ? 39.993 14.253  32.853  1.00 28.41 ? 39  THR B CB  1 
ATOM   1393 O  OG1 . THR B 1 39  ? 40.048 15.329  31.909  1.00 28.02 ? 39  THR B OG1 1 
ATOM   1394 C  CG2 . THR B 1 39  ? 39.926 14.826  34.263  1.00 29.19 ? 39  THR B CG2 1 
ATOM   1395 N  N   . GLU B 1 40  ? 41.910 12.279  34.770  1.00 25.52 ? 40  GLU B N   1 
ATOM   1396 C  CA  . GLU B 1 40  ? 41.910 11.225  35.777  1.00 25.65 ? 40  GLU B CA  1 
ATOM   1397 C  C   . GLU B 1 40  ? 40.486 10.827  36.165  1.00 24.30 ? 40  GLU B C   1 
ATOM   1398 O  O   . GLU B 1 40  ? 39.629 11.686  36.371  1.00 23.06 ? 40  GLU B O   1 
ATOM   1399 C  CB  . GLU B 1 40  ? 42.678 11.693  37.018  1.00 27.71 ? 40  GLU B CB  1 
ATOM   1400 C  CG  . GLU B 1 40  ? 42.857 10.622  38.081  1.00 29.43 ? 40  GLU B CG  1 
ATOM   1401 C  CD  . GLU B 1 40  ? 43.680 11.103  39.262  1.00 32.14 ? 40  GLU B CD  1 
ATOM   1402 O  OE1 . GLU B 1 40  ? 43.953 10.287  40.168  1.00 33.82 ? 40  GLU B OE1 1 
ATOM   1403 O  OE2 . GLU B 1 40  ? 44.050 12.295  39.282  1.00 31.83 ? 40  GLU B OE2 1 
ATOM   1404 N  N   . GLY B 1 41  ? 40.237 9.522   36.253  1.00 22.94 ? 41  GLY B N   1 
ATOM   1405 C  CA  . GLY B 1 41  ? 38.911 9.050   36.619  1.00 22.22 ? 41  GLY B CA  1 
ATOM   1406 C  C   . GLY B 1 41  ? 38.312 8.063   35.631  1.00 22.17 ? 41  GLY B C   1 
ATOM   1407 O  O   . GLY B 1 41  ? 38.978 7.622   34.692  1.00 20.57 ? 41  GLY B O   1 
ATOM   1408 N  N   . LEU B 1 42  ? 37.045 7.719   35.843  1.00 21.14 ? 42  LEU B N   1 
ATOM   1409 C  CA  . LEU B 1 42  ? 36.338 6.772   34.982  1.00 21.44 ? 42  LEU B CA  1 
ATOM   1410 C  C   . LEU B 1 42  ? 35.857 7.395   33.672  1.00 21.62 ? 42  LEU B C   1 
ATOM   1411 O  O   . LEU B 1 42  ? 35.343 8.514   33.665  1.00 22.32 ? 42  LEU B O   1 
ATOM   1412 C  CB  . LEU B 1 42  ? 35.125 6.202   35.722  1.00 20.49 ? 42  LEU B CB  1 
ATOM   1413 C  CG  . LEU B 1 42  ? 35.350 5.379   36.989  1.00 19.98 ? 42  LEU B CG  1 
ATOM   1414 C  CD1 . LEU B 1 42  ? 34.019 5.145   37.680  1.00 21.70 ? 42  LEU B CD1 1 
ATOM   1415 C  CD2 . LEU B 1 42  ? 36.008 4.060   36.637  1.00 23.03 ? 42  LEU B CD2 1 
ATOM   1416 N  N   . ARG B 1 43  ? 36.011 6.660   32.572  1.00 21.56 ? 43  ARG B N   1 
ATOM   1417 C  CA  . ARG B 1 43  ? 35.568 7.131   31.260  1.00 21.02 ? 43  ARG B CA  1 
ATOM   1418 C  C   . ARG B 1 43  ? 34.879 5.988   30.508  1.00 21.49 ? 43  ARG B C   1 
ATOM   1419 O  O   . ARG B 1 43  ? 35.422 4.886   30.414  1.00 20.42 ? 43  ARG B O   1 
ATOM   1420 C  CB  . ARG B 1 43  ? 36.758 7.646   30.440  1.00 21.60 ? 43  ARG B CB  1 
ATOM   1421 C  CG  . ARG B 1 43  ? 37.622 8.683   31.159  1.00 21.56 ? 43  ARG B CG  1 
ATOM   1422 C  CD  . ARG B 1 43  ? 36.845 9.953   31.492  1.00 24.36 ? 43  ARG B CD  1 
ATOM   1423 N  NE  . ARG B 1 43  ? 37.484 10.694  32.578  1.00 24.64 ? 43  ARG B NE  1 
ATOM   1424 C  CZ  . ARG B 1 43  ? 36.878 11.620  33.314  1.00 23.68 ? 43  ARG B CZ  1 
ATOM   1425 N  NH1 . ARG B 1 43  ? 35.611 11.937  33.085  1.00 25.78 ? 43  ARG B NH1 1 
ATOM   1426 N  NH2 . ARG B 1 43  ? 37.530 12.211  34.304  1.00 25.13 ? 43  ARG B NH2 1 
ATOM   1427 N  N   . GLY B 1 44  ? 33.683 6.257   29.987  1.00 20.27 ? 44  GLY B N   1 
ATOM   1428 C  CA  . GLY B 1 44  ? 32.931 5.249   29.254  1.00 21.07 ? 44  GLY B CA  1 
ATOM   1429 C  C   . GLY B 1 44  ? 33.749 4.615   28.148  1.00 19.20 ? 44  GLY B C   1 
ATOM   1430 O  O   . GLY B 1 44  ? 34.542 5.289   27.490  1.00 19.15 ? 44  GLY B O   1 
ATOM   1431 N  N   . PHE B 1 45  ? 33.541 3.321   27.924  1.00 16.75 ? 45  PHE B N   1 
ATOM   1432 C  CA  . PHE B 1 45  ? 34.305 2.589   26.920  1.00 16.30 ? 45  PHE B CA  1 
ATOM   1433 C  C   . PHE B 1 45  ? 33.400 1.561   26.243  1.00 17.55 ? 45  PHE B C   1 
ATOM   1434 O  O   . PHE B 1 45  ? 33.063 0.543   26.844  1.00 17.05 ? 45  PHE B O   1 
ATOM   1435 C  CB  . PHE B 1 45  ? 35.477 1.904   27.635  1.00 18.16 ? 45  PHE B CB  1 
ATOM   1436 C  CG  . PHE B 1 45  ? 36.486 1.266   26.725  1.00 17.64 ? 45  PHE B CG  1 
ATOM   1437 C  CD1 . PHE B 1 45  ? 37.155 2.017   25.761  1.00 19.91 ? 45  PHE B CD1 1 
ATOM   1438 C  CD2 . PHE B 1 45  ? 36.827 -0.077  26.889  1.00 17.17 ? 45  PHE B CD2 1 
ATOM   1439 C  CE1 . PHE B 1 45  ? 38.155 1.441   24.975  1.00 19.79 ? 45  PHE B CE1 1 
ATOM   1440 C  CE2 . PHE B 1 45  ? 37.823 -0.664  26.110  1.00 18.36 ? 45  PHE B CE2 1 
ATOM   1441 C  CZ  . PHE B 1 45  ? 38.491 0.095   25.152  1.00 18.68 ? 45  PHE B CZ  1 
ATOM   1442 N  N   . HIS B 1 46  ? 32.987 1.830   25.005  1.00 18.14 ? 46  HIS B N   1 
ATOM   1443 C  CA  . HIS B 1 46  ? 32.112 0.887   24.306  1.00 17.97 ? 46  HIS B CA  1 
ATOM   1444 C  C   . HIS B 1 46  ? 32.352 0.770   22.810  1.00 18.27 ? 46  HIS B C   1 
ATOM   1445 O  O   . HIS B 1 46  ? 33.037 1.593   22.195  1.00 15.21 ? 46  HIS B O   1 
ATOM   1446 C  CB  . HIS B 1 46  ? 30.631 1.253   24.471  1.00 21.73 ? 46  HIS B CB  1 
ATOM   1447 C  CG  . HIS B 1 46  ? 30.325 2.097   25.667  1.00 20.06 ? 46  HIS B CG  1 
ATOM   1448 N  ND1 . HIS B 1 46  ? 30.201 3.467   25.596  1.00 22.25 ? 46  HIS B ND1 1 
ATOM   1449 C  CD2 . HIS B 1 46  ? 30.063 1.761   26.952  1.00 20.07 ? 46  HIS B CD2 1 
ATOM   1450 C  CE1 . HIS B 1 46  ? 29.869 3.939   26.785  1.00 20.58 ? 46  HIS B CE1 1 
ATOM   1451 N  NE2 . HIS B 1 46  ? 29.779 2.924   27.625  1.00 20.85 ? 46  HIS B NE2 1 
ATOM   1452 N  N   . VAL B 1 47  ? 31.763 -0.270  22.233  1.00 17.65 ? 47  VAL B N   1 
ATOM   1453 C  CA  . VAL B 1 47  ? 31.841 -0.481  20.802  1.00 19.03 ? 47  VAL B CA  1 
ATOM   1454 C  C   . VAL B 1 47  ? 30.532 0.062   20.257  1.00 20.19 ? 47  VAL B C   1 
ATOM   1455 O  O   . VAL B 1 47  ? 29.449 -0.338  20.697  1.00 20.23 ? 47  VAL B O   1 
ATOM   1456 C  CB  . VAL B 1 47  ? 31.944 -1.967  20.437  1.00 19.82 ? 47  VAL B CB  1 
ATOM   1457 C  CG1 . VAL B 1 47  ? 31.898 -2.123  18.925  1.00 19.60 ? 47  VAL B CG1 1 
ATOM   1458 C  CG2 . VAL B 1 47  ? 33.243 -2.550  20.989  1.00 19.62 ? 47  VAL B CG2 1 
ATOM   1459 N  N   . HIS B 1 48  ? 30.632 0.991   19.318  1.00 19.75 ? 48  HIS B N   1 
ATOM   1460 C  CA  . HIS B 1 48  ? 29.452 1.573   18.714  1.00 20.21 ? 48  HIS B CA  1 
ATOM   1461 C  C   . HIS B 1 48  ? 29.146 0.887   17.395  1.00 20.60 ? 48  HIS B C   1 
ATOM   1462 O  O   . HIS B 1 48  ? 30.029 0.327   16.748  1.00 19.64 ? 48  HIS B O   1 
ATOM   1463 C  CB  . HIS B 1 48  ? 29.640 3.076   18.544  1.00 18.50 ? 48  HIS B CB  1 
ATOM   1464 C  CG  . HIS B 1 48  ? 29.507 3.829   19.829  1.00 18.64 ? 48  HIS B CG  1 
ATOM   1465 N  ND1 . HIS B 1 48  ? 28.586 4.837   20.010  1.00 19.77 ? 48  HIS B ND1 1 
ATOM   1466 C  CD2 . HIS B 1 48  ? 30.158 3.696   21.010  1.00 20.18 ? 48  HIS B CD2 1 
ATOM   1467 C  CE1 . HIS B 1 48  ? 28.675 5.294   21.247  1.00 21.05 ? 48  HIS B CE1 1 
ATOM   1468 N  NE2 . HIS B 1 48  ? 29.621 4.619   21.874  1.00 20.06 ? 48  HIS B NE2 1 
ATOM   1469 N  N   . GLU B 1 49  ? 27.878 0.940   17.014  1.00 20.87 ? 49  GLU B N   1 
ATOM   1470 C  CA  . GLU B 1 49  ? 27.380 0.277   15.822  1.00 20.67 ? 49  GLU B CA  1 
ATOM   1471 C  C   . GLU B 1 49  ? 28.085 0.491   14.487  1.00 21.41 ? 49  GLU B C   1 
ATOM   1472 O  O   . GLU B 1 49  ? 28.397 -0.478  13.791  1.00 22.22 ? 49  GLU B O   1 
ATOM   1473 C  CB  . GLU B 1 49  ? 25.893 0.595   15.653  1.00 21.64 ? 49  GLU B CB  1 
ATOM   1474 C  CG  . GLU B 1 49  ? 25.197 -0.280  14.623  1.00 22.01 ? 49  GLU B CG  1 
ATOM   1475 C  CD  . GLU B 1 49  ? 23.724 0.037   14.500  1.00 25.73 ? 49  GLU B CD  1 
ATOM   1476 O  OE1 . GLU B 1 49  ? 23.028 -0.672  13.738  1.00 26.22 ? 49  GLU B OE1 1 
ATOM   1477 O  OE2 . GLU B 1 49  ? 23.267 0.996   15.166  1.00 23.10 ? 49  GLU B OE2 1 
ATOM   1478 N  N   . PHE B 1 50  ? 28.335 1.740   14.116  1.00 21.00 ? 50  PHE B N   1 
ATOM   1479 C  CA  . PHE B 1 50  ? 28.956 1.996   12.821  1.00 22.39 ? 50  PHE B CA  1 
ATOM   1480 C  C   . PHE B 1 50  ? 30.430 2.375   12.834  1.00 21.29 ? 50  PHE B C   1 
ATOM   1481 O  O   . PHE B 1 50  ? 30.880 3.167   13.665  1.00 20.64 ? 50  PHE B O   1 
ATOM   1482 C  CB  . PHE B 1 50  ? 28.160 3.073   12.081  1.00 24.28 ? 50  PHE B CB  1 
ATOM   1483 C  CG  . PHE B 1 50  ? 26.692 2.779   12.000  1.00 26.45 ? 50  PHE B CG  1 
ATOM   1484 C  CD1 . PHE B 1 50  ? 26.233 1.652   11.327  1.00 27.63 ? 50  PHE B CD1 1 
ATOM   1485 C  CD2 . PHE B 1 50  ? 25.770 3.609   12.631  1.00 27.20 ? 50  PHE B CD2 1 
ATOM   1486 C  CE1 . PHE B 1 50  ? 24.872 1.351   11.285  1.00 29.26 ? 50  PHE B CE1 1 
ATOM   1487 C  CE2 . PHE B 1 50  ? 24.409 3.320   12.597  1.00 27.92 ? 50  PHE B CE2 1 
ATOM   1488 C  CZ  . PHE B 1 50  ? 23.959 2.189   11.923  1.00 29.31 ? 50  PHE B CZ  1 
ATOM   1489 N  N   . GLY B 1 51  ? 31.175 1.785   11.901  1.00 21.00 ? 51  GLY B N   1 
ATOM   1490 C  CA  . GLY B 1 51  ? 32.590 2.084   11.771  1.00 21.26 ? 51  GLY B CA  1 
ATOM   1491 C  C   . GLY B 1 51  ? 32.681 3.218   10.771  1.00 21.26 ? 51  GLY B C   1 
ATOM   1492 O  O   . GLY B 1 51  ? 33.401 3.144   9.773   1.00 21.98 ? 51  GLY B O   1 
ATOM   1493 N  N   . ASP B 1 52  ? 31.928 4.275   11.054  1.00 21.85 ? 52  ASP B N   1 
ATOM   1494 C  CA  . ASP B 1 52  ? 31.851 5.450   10.199  1.00 21.96 ? 52  ASP B CA  1 
ATOM   1495 C  C   . ASP B 1 52  ? 32.356 6.689   10.938  1.00 23.69 ? 52  ASP B C   1 
ATOM   1496 O  O   . ASP B 1 52  ? 31.790 7.092   11.954  1.00 23.92 ? 52  ASP B O   1 
ATOM   1497 C  CB  . ASP B 1 52  ? 30.394 5.631   9.758   1.00 25.19 ? 52  ASP B CB  1 
ATOM   1498 C  CG  . ASP B 1 52  ? 30.188 6.841   8.869   1.00 25.65 ? 52  ASP B CG  1 
ATOM   1499 O  OD1 . ASP B 1 52  ? 29.099 6.938   8.266   1.00 28.93 ? 52  ASP B OD1 1 
ATOM   1500 O  OD2 . ASP B 1 52  ? 31.096 7.691   8.779   1.00 27.88 ? 52  ASP B OD2 1 
ATOM   1501 N  N   . ASN B 1 53  ? 33.422 7.293   10.418  1.00 23.03 ? 53  ASN B N   1 
ATOM   1502 C  CA  . ASN B 1 53  ? 34.014 8.474   11.042  1.00 24.99 ? 53  ASN B CA  1 
ATOM   1503 C  C   . ASN B 1 53  ? 33.946 9.688   10.116  1.00 25.01 ? 53  ASN B C   1 
ATOM   1504 O  O   . ASN B 1 53  ? 34.794 10.580  10.178  1.00 25.23 ? 53  ASN B O   1 
ATOM   1505 C  CB  . ASN B 1 53  ? 35.473 8.179   11.406  1.00 28.04 ? 53  ASN B CB  1 
ATOM   1506 C  CG  . ASN B 1 53  ? 36.040 9.173   12.400  1.00 30.36 ? 53  ASN B CG  1 
ATOM   1507 O  OD1 . ASN B 1 53  ? 35.499 9.353   13.493  1.00 31.89 ? 53  ASN B OD1 1 
ATOM   1508 N  ND2 . ASN B 1 53  ? 37.138 9.819   12.029  1.00 32.45 ? 53  ASN B ND2 1 
ATOM   1509 N  N   . THR B 1 54  ? 32.926 9.719   9.267   1.00 26.02 ? 54  THR B N   1 
ATOM   1510 C  CA  . THR B 1 54  ? 32.750 10.808  8.315   1.00 27.62 ? 54  THR B CA  1 
ATOM   1511 C  C   . THR B 1 54  ? 32.660 12.174  8.991   1.00 28.22 ? 54  THR B C   1 
ATOM   1512 O  O   . THR B 1 54  ? 33.258 13.145  8.523   1.00 28.77 ? 54  THR B O   1 
ATOM   1513 C  CB  . THR B 1 54  ? 31.490 10.586  7.451   1.00 29.02 ? 54  THR B CB  1 
ATOM   1514 O  OG1 . THR B 1 54  ? 30.362 10.365  8.301   1.00 35.25 ? 54  THR B OG1 1 
ATOM   1515 C  CG2 . THR B 1 54  ? 31.670 9.380   6.547   1.00 28.25 ? 54  THR B CG2 1 
ATOM   1516 N  N   . ALA B 1 55  ? 31.920 12.248  10.093  1.00 26.25 ? 55  ALA B N   1 
ATOM   1517 C  CA  . ALA B 1 55  ? 31.768 13.506  10.823  1.00 28.64 ? 55  ALA B CA  1 
ATOM   1518 C  C   . ALA B 1 55  ? 32.348 13.371  12.226  1.00 28.65 ? 55  ALA B C   1 
ATOM   1519 O  O   . ALA B 1 55  ? 31.830 13.945  13.183  1.00 30.85 ? 55  ALA B O   1 
ATOM   1520 C  CB  . ALA B 1 55  ? 30.299 13.888  10.905  1.00 28.25 ? 55  ALA B CB  1 
ATOM   1521 N  N   . GLY B 1 56  ? 33.433 12.618  12.340  1.00 28.30 ? 56  GLY B N   1 
ATOM   1522 C  CA  . GLY B 1 56  ? 34.043 12.413  13.639  1.00 27.57 ? 56  GLY B CA  1 
ATOM   1523 C  C   . GLY B 1 56  ? 33.366 11.252  14.340  1.00 25.84 ? 56  GLY B C   1 
ATOM   1524 O  O   . GLY B 1 56  ? 32.624 10.495  13.717  1.00 25.48 ? 56  GLY B O   1 
ATOM   1525 N  N   . CYS B 1 57  ? 33.604 11.114  15.638  1.00 25.87 ? 57  CYS B N   1 
ATOM   1526 C  CA  . CYS B 1 57  ? 33.021 10.021  16.406  1.00 25.93 ? 57  CYS B CA  1 
ATOM   1527 C  C   . CYS B 1 57  ? 31.498 10.031  16.473  1.00 26.12 ? 57  CYS B C   1 
ATOM   1528 O  O   . CYS B 1 57  ? 30.888 9.027   16.827  1.00 26.90 ? 57  CYS B O   1 
ATOM   1529 C  CB  . CYS B 1 57  ? 33.601 10.016  17.820  1.00 26.97 ? 57  CYS B CB  1 
ATOM   1530 S  SG  . CYS B 1 57  ? 35.413 9.905   17.820  1.00 27.27 ? 57  CYS B SG  1 
ATOM   1531 N  N   . THR B 1 58  ? 30.877 11.154  16.127  1.00 26.18 ? 58  THR B N   1 
ATOM   1532 C  CA  . THR B 1 58  ? 29.422 11.236  16.168  1.00 26.74 ? 58  THR B CA  1 
ATOM   1533 C  C   . THR B 1 58  ? 28.796 10.270  15.168  1.00 25.59 ? 58  THR B C   1 
ATOM   1534 O  O   . THR B 1 58  ? 27.715 9.733   15.404  1.00 24.80 ? 58  THR B O   1 
ATOM   1535 C  CB  . THR B 1 58  ? 28.928 12.660  15.840  1.00 28.72 ? 58  THR B CB  1 
ATOM   1536 O  OG1 . THR B 1 58  ? 29.505 13.594  16.759  1.00 33.96 ? 58  THR B OG1 1 
ATOM   1537 C  CG2 . THR B 1 58  ? 27.419 12.732  15.956  1.00 30.57 ? 58  THR B CG2 1 
ATOM   1538 N  N   . SER B 1 59  ? 29.496 10.034  14.062  1.00 24.38 ? 59  SER B N   1 
ATOM   1539 C  CA  . SER B 1 59  ? 29.008 9.158   13.001  1.00 24.34 ? 59  SER B CA  1 
ATOM   1540 C  C   . SER B 1 59  ? 28.983 7.674   13.343  1.00 22.32 ? 59  SER B C   1 
ATOM   1541 O  O   . SER B 1 59  ? 28.450 6.869   12.576  1.00 21.35 ? 59  SER B O   1 
ATOM   1542 C  CB  . SER B 1 59  ? 29.853 9.359   11.742  1.00 25.41 ? 59  SER B CB  1 
ATOM   1543 O  OG  . SER B 1 59  ? 29.902 10.727  11.383  1.00 27.95 ? 59  SER B OG  1 
ATOM   1544 N  N   . ALA B 1 60  ? 29.558 7.312   14.484  1.00 21.92 ? 60  ALA B N   1 
ATOM   1545 C  CA  . ALA B 1 60  ? 29.604 5.912   14.902  1.00 21.41 ? 60  ALA B CA  1 
ATOM   1546 C  C   . ALA B 1 60  ? 28.242 5.385   15.340  1.00 22.71 ? 60  ALA B C   1 
ATOM   1547 O  O   . ALA B 1 60  ? 28.065 4.178   15.526  1.00 22.29 ? 60  ALA B O   1 
ATOM   1548 C  CB  . ALA B 1 60  ? 30.614 5.737   16.028  1.00 21.65 ? 60  ALA B CB  1 
ATOM   1549 N  N   . GLY B 1 61  ? 27.281 6.286   15.514  1.00 22.11 ? 61  GLY B N   1 
ATOM   1550 C  CA  . GLY B 1 61  ? 25.956 5.859   15.921  1.00 22.31 ? 61  GLY B CA  1 
ATOM   1551 C  C   . GLY B 1 61  ? 25.889 5.445   17.378  1.00 21.82 ? 61  GLY B C   1 
ATOM   1552 O  O   . GLY B 1 61  ? 26.789 5.764   18.159  1.00 21.23 ? 61  GLY B O   1 
ATOM   1553 N  N   . PRO B 1 62  ? 24.830 4.721   17.775  1.00 20.78 ? 62  PRO B N   1 
ATOM   1554 C  CA  . PRO B 1 62  ? 24.662 4.271   19.160  1.00 20.41 ? 62  PRO B CA  1 
ATOM   1555 C  C   . PRO B 1 62  ? 25.519 3.055   19.476  1.00 21.48 ? 62  PRO B C   1 
ATOM   1556 O  O   . PRO B 1 62  ? 26.294 2.603   18.634  1.00 18.74 ? 62  PRO B O   1 
ATOM   1557 C  CB  . PRO B 1 62  ? 23.178 3.955   19.229  1.00 22.05 ? 62  PRO B CB  1 
ATOM   1558 C  CG  . PRO B 1 62  ? 22.927 3.356   17.875  1.00 21.39 ? 62  PRO B CG  1 
ATOM   1559 C  CD  . PRO B 1 62  ? 23.688 4.291   16.944  1.00 21.02 ? 62  PRO B CD  1 
ATOM   1560 N  N   . HIS B 1 63  ? 25.378 2.531   20.692  1.00 20.65 ? 63  HIS B N   1 
ATOM   1561 C  CA  . HIS B 1 63  ? 26.139 1.352   21.096  1.00 21.17 ? 63  HIS B CA  1 
ATOM   1562 C  C   . HIS B 1 63  ? 25.740 0.161   20.234  1.00 21.08 ? 63  HIS B C   1 
ATOM   1563 O  O   . HIS B 1 63  ? 24.566 0.003   19.893  1.00 21.63 ? 63  HIS B O   1 
ATOM   1564 C  CB  . HIS B 1 63  ? 25.865 1.010   22.565  1.00 21.91 ? 63  HIS B CB  1 
ATOM   1565 C  CG  . HIS B 1 63  ? 26.341 2.046   23.533  1.00 21.12 ? 63  HIS B CG  1 
ATOM   1566 N  ND1 . HIS B 1 63  ? 26.235 1.890   24.898  1.00 19.34 ? 63  HIS B ND1 1 
ATOM   1567 C  CD2 . HIS B 1 63  ? 26.929 3.251   23.337  1.00 22.27 ? 63  HIS B CD2 1 
ATOM   1568 C  CE1 . HIS B 1 63  ? 26.737 2.951   25.503  1.00 21.14 ? 63  HIS B CE1 1 
ATOM   1569 N  NE2 . HIS B 1 63  ? 27.165 3.792   24.578  1.00 21.67 ? 63  HIS B NE2 1 
ATOM   1570 N  N   . PHE B 1 64  ? 26.722 -0.665  19.880  1.00 20.64 ? 64  PHE B N   1 
ATOM   1571 C  CA  . PHE B 1 64  ? 26.486 -1.865  19.081  1.00 21.30 ? 64  PHE B CA  1 
ATOM   1572 C  C   . PHE B 1 64  ? 25.459 -2.664  19.876  1.00 20.98 ? 64  PHE B C   1 
ATOM   1573 O  O   . PHE B 1 64  ? 25.725 -3.069  21.005  1.00 21.28 ? 64  PHE B O   1 
ATOM   1574 C  CB  . PHE B 1 64  ? 27.797 -2.646  18.940  1.00 20.31 ? 64  PHE B CB  1 
ATOM   1575 C  CG  . PHE B 1 64  ? 27.678 -3.908  18.138  1.00 20.64 ? 64  PHE B CG  1 
ATOM   1576 C  CD1 . PHE B 1 64  ? 28.570 -4.954  18.343  1.00 21.24 ? 64  PHE B CD1 1 
ATOM   1577 C  CD2 . PHE B 1 64  ? 26.684 -4.055  17.178  1.00 22.81 ? 64  PHE B CD2 1 
ATOM   1578 C  CE1 . PHE B 1 64  ? 28.475 -6.135  17.604  1.00 22.13 ? 64  PHE B CE1 1 
ATOM   1579 C  CE2 . PHE B 1 64  ? 26.581 -5.234  16.431  1.00 22.57 ? 64  PHE B CE2 1 
ATOM   1580 C  CZ  . PHE B 1 64  ? 27.478 -6.273  16.647  1.00 22.82 ? 64  PHE B CZ  1 
ATOM   1581 N  N   . ASN B 1 65  ? 24.290 -2.896  19.288  1.00 22.67 ? 65  ASN B N   1 
ATOM   1582 C  CA  . ASN B 1 65  ? 23.217 -3.585  19.997  1.00 23.56 ? 65  ASN B CA  1 
ATOM   1583 C  C   . ASN B 1 65  ? 22.212 -4.227  19.027  1.00 25.22 ? 65  ASN B C   1 
ATOM   1584 O  O   . ASN B 1 65  ? 21.107 -3.727  18.829  1.00 25.73 ? 65  ASN B O   1 
ATOM   1585 C  CB  . ASN B 1 65  ? 22.555 -2.545  20.915  1.00 23.60 ? 65  ASN B CB  1 
ATOM   1586 C  CG  . ASN B 1 65  ? 21.363 -3.079  21.673  1.00 23.07 ? 65  ASN B CG  1 
ATOM   1587 O  OD1 . ASN B 1 65  ? 21.312 -4.245  22.047  1.00 21.89 ? 65  ASN B OD1 1 
ATOM   1588 N  ND2 . ASN B 1 65  ? 20.399 -2.199  21.936  1.00 25.45 ? 65  ASN B ND2 1 
ATOM   1589 N  N   . PRO B 1 66  ? 22.592 -5.363  18.418  1.00 25.54 ? 66  PRO B N   1 
ATOM   1590 C  CA  . PRO B 1 66  ? 21.762 -6.098  17.461  1.00 28.02 ? 66  PRO B CA  1 
ATOM   1591 C  C   . PRO B 1 66  ? 20.285 -6.302  17.795  1.00 29.16 ? 66  PRO B C   1 
ATOM   1592 O  O   . PRO B 1 66  ? 19.417 -5.946  16.996  1.00 29.20 ? 66  PRO B O   1 
ATOM   1593 C  CB  . PRO B 1 66  ? 22.507 -7.420  17.317  1.00 27.01 ? 66  PRO B CB  1 
ATOM   1594 C  CG  . PRO B 1 66  ? 23.920 -6.991  17.410  1.00 26.13 ? 66  PRO B CG  1 
ATOM   1595 C  CD  . PRO B 1 66  ? 23.888 -6.042  18.596  1.00 25.61 ? 66  PRO B CD  1 
ATOM   1596 N  N   . LEU B 1 67  ? 19.991 -6.869  18.961  1.00 30.50 ? 67  LEU B N   1 
ATOM   1597 C  CA  . LEU B 1 67  ? 18.601 -7.134  19.329  1.00 32.26 ? 67  LEU B CA  1 
ATOM   1598 C  C   . LEU B 1 67  ? 17.904 -6.130  20.238  1.00 32.33 ? 67  LEU B C   1 
ATOM   1599 O  O   . LEU B 1 67  ? 16.943 -6.472  20.932  1.00 30.92 ? 67  LEU B O   1 
ATOM   1600 C  CB  . LEU B 1 67  ? 18.480 -8.540  19.922  1.00 34.99 ? 67  LEU B CB  1 
ATOM   1601 C  CG  . LEU B 1 67  ? 18.282 -9.658  18.888  1.00 38.18 ? 67  LEU B CG  1 
ATOM   1602 C  CD1 . LEU B 1 67  ? 16.937 -9.477  18.191  1.00 40.17 ? 67  LEU B CD1 1 
ATOM   1603 C  CD2 . LEU B 1 67  ? 19.408 -9.643  17.873  1.00 40.01 ? 67  LEU B CD2 1 
ATOM   1604 N  N   . SER B 1 68  ? 18.387 -4.895  20.226  1.00 30.42 ? 68  SER B N   1 
ATOM   1605 C  CA  . SER B 1 68  ? 17.793 -3.824  21.010  1.00 30.50 ? 68  SER B CA  1 
ATOM   1606 C  C   . SER B 1 68  ? 17.630 -4.121  22.498  1.00 30.38 ? 68  SER B C   1 
ATOM   1607 O  O   . SER B 1 68  ? 16.516 -4.125  23.020  1.00 31.01 ? 68  SER B O   1 
ATOM   1608 C  CB  . SER B 1 68  ? 16.433 -3.455  20.409  1.00 32.22 ? 68  SER B CB  1 
ATOM   1609 O  OG  . SER B 1 68  ? 16.559 -3.127  19.034  1.00 31.42 ? 68  SER B OG  1 
ATOM   1610 N  N   . ARG B 1 69  ? 18.739 -4.370  23.182  1.00 26.53 ? 69  ARG B N   1 
ATOM   1611 C  CA  . ARG B 1 69  ? 18.695 -4.628  24.613  1.00 25.76 ? 69  ARG B CA  1 
ATOM   1612 C  C   . ARG B 1 69  ? 18.969 -3.291  25.285  1.00 24.46 ? 69  ARG B C   1 
ATOM   1613 O  O   . ARG B 1 69  ? 19.264 -2.312  24.603  1.00 23.64 ? 69  ARG B O   1 
ATOM   1614 C  CB  . ARG B 1 69  ? 19.776 -5.635  25.003  1.00 26.54 ? 69  ARG B CB  1 
ATOM   1615 C  CG  . ARG B 1 69  ? 19.726 -6.912  24.186  1.00 28.96 ? 69  ARG B CG  1 
ATOM   1616 C  CD  . ARG B 1 69  ? 20.790 -7.906  24.623  1.00 29.12 ? 69  ARG B CD  1 
ATOM   1617 N  NE  . ARG B 1 69  ? 20.833 -9.051  23.718  1.00 31.42 ? 69  ARG B NE  1 
ATOM   1618 C  CZ  . ARG B 1 69  ? 20.806 -10.319 24.114  1.00 31.14 ? 69  ARG B CZ  1 
ATOM   1619 N  NH1 . ARG B 1 69  ? 20.845 -11.293 23.217  1.00 31.09 ? 69  ARG B NH1 1 
ATOM   1620 N  NH2 . ARG B 1 69  ? 20.735 -10.610 25.405  1.00 28.01 ? 69  ARG B NH2 1 
ATOM   1621 N  N   . LYS B 1 70  ? 18.863 -3.246  26.611  1.00 23.37 ? 70  LYS B N   1 
ATOM   1622 C  CA  . LYS B 1 70  ? 19.123 -2.020  27.355  1.00 22.88 ? 70  LYS B CA  1 
ATOM   1623 C  C   . LYS B 1 70  ? 20.598 -1.979  27.735  1.00 20.41 ? 70  LYS B C   1 
ATOM   1624 O  O   . LYS B 1 70  ? 21.263 -3.017  27.788  1.00 20.84 ? 70  LYS B O   1 
ATOM   1625 C  CB  . LYS B 1 70  ? 18.284 -1.976  28.633  1.00 23.77 ? 70  LYS B CB  1 
ATOM   1626 C  CG  . LYS B 1 70  ? 16.787 -2.020  28.414  1.00 30.68 ? 70  LYS B CG  1 
ATOM   1627 C  CD  . LYS B 1 70  ? 16.293 -0.787  27.689  1.00 35.37 ? 70  LYS B CD  1 
ATOM   1628 C  CE  . LYS B 1 70  ? 14.774 -0.699  27.765  1.00 39.10 ? 70  LYS B CE  1 
ATOM   1629 N  NZ  . LYS B 1 70  ? 14.311 -0.648  29.183  1.00 40.37 ? 70  LYS B NZ  1 
ATOM   1630 N  N   . HIS B 1 71  ? 21.099 -0.780  28.016  1.00 20.08 ? 71  HIS B N   1 
ATOM   1631 C  CA  . HIS B 1 71  ? 22.495 -0.587  28.395  1.00 19.12 ? 71  HIS B CA  1 
ATOM   1632 C  C   . HIS B 1 71  ? 22.810 -1.195  29.760  1.00 19.92 ? 71  HIS B C   1 
ATOM   1633 O  O   . HIS B 1 71  ? 21.967 -1.215  30.658  1.00 20.35 ? 71  HIS B O   1 
ATOM   1634 C  CB  . HIS B 1 71  ? 22.825 0.909   28.429  1.00 19.51 ? 71  HIS B CB  1 
ATOM   1635 C  CG  . HIS B 1 71  ? 24.246 1.209   28.794  1.00 19.55 ? 71  HIS B CG  1 
ATOM   1636 N  ND1 . HIS B 1 71  ? 25.293 1.058   27.909  1.00 21.11 ? 71  HIS B ND1 1 
ATOM   1637 C  CD2 . HIS B 1 71  ? 24.797 1.622   29.960  1.00 20.69 ? 71  HIS B CD2 1 
ATOM   1638 C  CE1 . HIS B 1 71  ? 26.427 1.362   28.516  1.00 18.92 ? 71  HIS B CE1 1 
ATOM   1639 N  NE2 . HIS B 1 71  ? 26.154 1.707   29.761  1.00 19.40 ? 71  HIS B NE2 1 
ATOM   1640 N  N   . GLY B 1 72  ? 24.034 -1.685  29.910  1.00 19.18 ? 72  GLY B N   1 
ATOM   1641 C  CA  . GLY B 1 72  ? 24.446 -2.263  31.175  1.00 19.55 ? 72  GLY B CA  1 
ATOM   1642 C  C   . GLY B 1 72  ? 25.954 -2.294  31.303  1.00 19.84 ? 72  GLY B C   1 
ATOM   1643 O  O   . GLY B 1 72  ? 26.664 -1.841  30.407  1.00 20.22 ? 72  GLY B O   1 
ATOM   1644 N  N   . GLY B 1 73  ? 26.443 -2.806  32.428  1.00 20.39 ? 73  GLY B N   1 
ATOM   1645 C  CA  . GLY B 1 73  ? 27.873 -2.918  32.634  1.00 21.53 ? 73  GLY B CA  1 
ATOM   1646 C  C   . GLY B 1 73  ? 28.307 -4.207  31.961  1.00 22.87 ? 73  GLY B C   1 
ATOM   1647 O  O   . GLY B 1 73  ? 27.464 -5.064  31.690  1.00 24.42 ? 73  GLY B O   1 
ATOM   1648 N  N   . PRO B 1 74  ? 29.604 -4.389  31.684  1.00 22.42 ? 74  PRO B N   1 
ATOM   1649 C  CA  . PRO B 1 74  ? 30.061 -5.619  31.028  1.00 23.42 ? 74  PRO B CA  1 
ATOM   1650 C  C   . PRO B 1 74  ? 29.700 -6.913  31.765  1.00 25.50 ? 74  PRO B C   1 
ATOM   1651 O  O   . PRO B 1 74  ? 29.536 -7.970  31.144  1.00 23.57 ? 74  PRO B O   1 
ATOM   1652 C  CB  . PRO B 1 74  ? 31.569 -5.401  30.901  1.00 22.62 ? 74  PRO B CB  1 
ATOM   1653 C  CG  . PRO B 1 74  ? 31.885 -4.500  32.067  1.00 25.22 ? 74  PRO B CG  1 
ATOM   1654 C  CD  . PRO B 1 74  ? 30.742 -3.522  32.040  1.00 23.58 ? 74  PRO B CD  1 
ATOM   1655 N  N   . LYS B 1 75  ? 29.560 -6.828  33.085  1.00 26.24 ? 75  LYS B N   1 
ATOM   1656 C  CA  . LYS B 1 75  ? 29.219 -7.998  33.887  1.00 28.94 ? 75  LYS B CA  1 
ATOM   1657 C  C   . LYS B 1 75  ? 27.721 -8.138  34.139  1.00 30.27 ? 75  LYS B C   1 
ATOM   1658 O  O   . LYS B 1 75  ? 27.287 -9.036  34.861  1.00 30.61 ? 75  LYS B O   1 
ATOM   1659 C  CB  . LYS B 1 75  ? 29.969 -7.954  35.218  1.00 31.07 ? 75  LYS B CB  1 
ATOM   1660 C  CG  . LYS B 1 75  ? 31.472 -8.109  35.068  1.00 33.73 ? 75  LYS B CG  1 
ATOM   1661 C  CD  . LYS B 1 75  ? 32.160 -8.164  36.419  1.00 37.65 ? 75  LYS B CD  1 
ATOM   1662 C  CE  . LYS B 1 75  ? 33.600 -8.635  36.284  1.00 39.14 ? 75  LYS B CE  1 
ATOM   1663 N  NZ  . LYS B 1 75  ? 34.399 -7.775  35.372  1.00 41.67 ? 75  LYS B NZ  1 
ATOM   1664 N  N   . ASP B 1 76  ? 26.932 -7.254  33.538  1.00 30.05 ? 76  ASP B N   1 
ATOM   1665 C  CA  . ASP B 1 76  ? 25.483 -7.285  33.702  1.00 29.85 ? 76  ASP B CA  1 
ATOM   1666 C  C   . ASP B 1 76  ? 24.809 -8.249  32.734  1.00 30.50 ? 76  ASP B C   1 
ATOM   1667 O  O   . ASP B 1 76  ? 25.214 -8.370  31.575  1.00 29.75 ? 76  ASP B O   1 
ATOM   1668 C  CB  . ASP B 1 76  ? 24.904 -5.881  33.514  1.00 30.88 ? 76  ASP B CB  1 
ATOM   1669 C  CG  . ASP B 1 76  ? 25.081 -5.014  34.744  1.00 32.12 ? 76  ASP B CG  1 
ATOM   1670 O  OD1 . ASP B 1 76  ? 25.127 -3.774  34.606  1.00 31.45 ? 76  ASP B OD1 1 
ATOM   1671 O  OD2 . ASP B 1 76  ? 25.161 -5.579  35.854  1.00 32.45 ? 76  ASP B OD2 1 
ATOM   1672 N  N   . GLU B 1 77  ? 23.777 -8.931  33.220  1.00 30.53 ? 77  GLU B N   1 
ATOM   1673 C  CA  . GLU B 1 77  ? 23.039 -9.880  32.397  1.00 31.46 ? 77  GLU B CA  1 
ATOM   1674 C  C   . GLU B 1 77  ? 22.402 -9.144  31.224  1.00 28.71 ? 77  GLU B C   1 
ATOM   1675 O  O   . GLU B 1 77  ? 22.394 -9.643  30.103  1.00 28.58 ? 77  GLU B O   1 
ATOM   1676 C  CB  . GLU B 1 77  ? 21.971 -10.589 33.235  1.00 34.34 ? 77  GLU B CB  1 
ATOM   1677 C  CG  . GLU B 1 77  ? 21.062 -11.509 32.431  1.00 37.66 ? 77  GLU B CG  1 
ATOM   1678 C  CD  . GLU B 1 77  ? 20.508 -12.651 33.262  1.00 38.94 ? 77  GLU B CD  1 
ATOM   1679 O  OE1 . GLU B 1 77  ? 21.209 -13.676 33.407  1.00 41.00 ? 77  GLU B OE1 1 
ATOM   1680 O  OE2 . GLU B 1 77  ? 19.378 -12.517 33.777  1.00 40.58 ? 77  GLU B OE2 1 
ATOM   1681 N  N   . GLU B 1 78  ? 21.866 -7.957  31.491  1.00 27.07 ? 78  GLU B N   1 
ATOM   1682 C  CA  . GLU B 1 78  ? 21.264 -7.139  30.445  1.00 25.82 ? 78  GLU B CA  1 
ATOM   1683 C  C   . GLU B 1 78  ? 22.260 -6.050  30.063  1.00 23.32 ? 78  GLU B C   1 
ATOM   1684 O  O   . GLU B 1 78  ? 22.612 -5.199  30.884  1.00 22.17 ? 78  GLU B O   1 
ATOM   1685 C  CB  . GLU B 1 78  ? 19.961 -6.492  30.926  1.00 28.82 ? 78  GLU B CB  1 
ATOM   1686 C  CG  . GLU B 1 78  ? 19.503 -5.349  30.033  1.00 33.50 ? 78  GLU B CG  1 
ATOM   1687 C  CD  . GLU B 1 78  ? 18.100 -5.531  29.494  1.00 37.22 ? 78  GLU B CD  1 
ATOM   1688 O  OE1 . GLU B 1 78  ? 17.149 -5.568  30.305  1.00 39.14 ? 78  GLU B OE1 1 
ATOM   1689 O  OE2 . GLU B 1 78  ? 17.944 -5.633  28.256  1.00 36.65 ? 78  GLU B OE2 1 
ATOM   1690 N  N   . ARG B 1 79  ? 22.713 -6.089  28.814  1.00 22.34 ? 79  ARG B N   1 
ATOM   1691 C  CA  . ARG B 1 79  ? 23.676 -5.119  28.302  1.00 19.97 ? 79  ARG B CA  1 
ATOM   1692 C  C   . ARG B 1 79  ? 23.717 -5.171  26.782  1.00 19.86 ? 79  ARG B C   1 
ATOM   1693 O  O   . ARG B 1 79  ? 23.228 -6.118  26.165  1.00 19.80 ? 79  ARG B O   1 
ATOM   1694 C  CB  . ARG B 1 79  ? 25.083 -5.429  28.828  1.00 18.23 ? 79  ARG B CB  1 
ATOM   1695 C  CG  . ARG B 1 79  ? 25.563 -6.834  28.465  1.00 17.03 ? 79  ARG B CG  1 
ATOM   1696 C  CD  . ARG B 1 79  ? 27.069 -7.032  28.677  1.00 16.22 ? 79  ARG B CD  1 
ATOM   1697 N  NE  . ARG B 1 79  ? 27.847 -6.692  27.482  1.00 17.46 ? 79  ARG B NE  1 
ATOM   1698 C  CZ  . ARG B 1 79  ? 29.128 -7.012  27.310  1.00 18.00 ? 79  ARG B CZ  1 
ATOM   1699 N  NH1 . ARG B 1 79  ? 29.760 -6.674  26.193  1.00 19.39 ? 79  ARG B NH1 1 
ATOM   1700 N  NH2 . ARG B 1 79  ? 29.782 -7.669  28.258  1.00 18.48 ? 79  ARG B NH2 1 
ATOM   1701 N  N   . HIS B 1 80  ? 24.302 -4.137  26.186  1.00 19.01 ? 80  HIS B N   1 
ATOM   1702 C  CA  . HIS B 1 80  ? 24.465 -4.075  24.740  1.00 18.26 ? 80  HIS B CA  1 
ATOM   1703 C  C   . HIS B 1 80  ? 25.720 -4.897  24.472  1.00 17.72 ? 80  HIS B C   1 
ATOM   1704 O  O   . HIS B 1 80  ? 26.596 -4.987  25.332  1.00 17.76 ? 80  HIS B O   1 
ATOM   1705 C  CB  . HIS B 1 80  ? 24.735 -2.641  24.289  1.00 17.30 ? 80  HIS B CB  1 
ATOM   1706 C  CG  . HIS B 1 80  ? 23.610 -1.694  24.558  1.00 18.37 ? 80  HIS B CG  1 
ATOM   1707 N  ND1 . HIS B 1 80  ? 23.820 -0.389  24.947  1.00 18.84 ? 80  HIS B ND1 1 
ATOM   1708 C  CD2 . HIS B 1 80  ? 22.271 -1.837  24.421  1.00 18.29 ? 80  HIS B CD2 1 
ATOM   1709 C  CE1 . HIS B 1 80  ? 22.658 0.234   25.034  1.00 16.95 ? 80  HIS B CE1 1 
ATOM   1710 N  NE2 . HIS B 1 80  ? 21.702 -0.622  24.719  1.00 18.55 ? 80  HIS B NE2 1 
ATOM   1711 N  N   . VAL B 1 81  ? 25.819 -5.490  23.292  1.00 18.53 ? 81  VAL B N   1 
ATOM   1712 C  CA  . VAL B 1 81  ? 27.011 -6.263  22.973  1.00 19.04 ? 81  VAL B CA  1 
ATOM   1713 C  C   . VAL B 1 81  ? 28.257 -5.383  23.136  1.00 18.67 ? 81  VAL B C   1 
ATOM   1714 O  O   . VAL B 1 81  ? 29.292 -5.841  23.622  1.00 19.51 ? 81  VAL B O   1 
ATOM   1715 C  CB  . VAL B 1 81  ? 26.958 -6.810  21.531  1.00 20.24 ? 81  VAL B CB  1 
ATOM   1716 C  CG1 . VAL B 1 81  ? 28.290 -7.470  21.172  1.00 19.17 ? 81  VAL B CG1 1 
ATOM   1717 C  CG2 . VAL B 1 81  ? 25.818 -7.817  21.396  1.00 21.45 ? 81  VAL B CG2 1 
ATOM   1718 N  N   . GLY B 1 82  ? 28.150 -4.112  22.763  1.00 17.99 ? 82  GLY B N   1 
ATOM   1719 C  CA  . GLY B 1 82  ? 29.298 -3.219  22.861  1.00 17.25 ? 82  GLY B CA  1 
ATOM   1720 C  C   . GLY B 1 82  ? 29.628 -2.579  24.203  1.00 18.85 ? 82  GLY B C   1 
ATOM   1721 O  O   . GLY B 1 82  ? 30.540 -1.753  24.284  1.00 18.83 ? 82  GLY B O   1 
ATOM   1722 N  N   . ASP B 1 83  ? 28.907 -2.947  25.258  1.00 17.95 ? 83  ASP B N   1 
ATOM   1723 C  CA  . ASP B 1 83  ? 29.148 -2.371  26.581  1.00 17.98 ? 83  ASP B CA  1 
ATOM   1724 C  C   . ASP B 1 83  ? 30.359 -2.945  27.320  1.00 18.23 ? 83  ASP B C   1 
ATOM   1725 O  O   . ASP B 1 83  ? 30.285 -4.026  27.908  1.00 20.85 ? 83  ASP B O   1 
ATOM   1726 C  CB  . ASP B 1 83  ? 27.894 -2.522  27.448  1.00 18.22 ? 83  ASP B CB  1 
ATOM   1727 C  CG  . ASP B 1 83  ? 26.744 -1.683  26.939  1.00 17.53 ? 83  ASP B CG  1 
ATOM   1728 O  OD1 . ASP B 1 83  ? 27.018 -0.674  26.255  1.00 18.06 ? 83  ASP B OD1 1 
ATOM   1729 O  OD2 . ASP B 1 83  ? 25.576 -2.012  27.228  1.00 19.20 ? 83  ASP B OD2 1 
ATOM   1730 N  N   . LEU B 1 84  ? 31.470 -2.210  27.295  1.00 19.08 ? 84  LEU B N   1 
ATOM   1731 C  CA  . LEU B 1 84  ? 32.692 -2.644  27.968  1.00 18.41 ? 84  LEU B CA  1 
ATOM   1732 C  C   . LEU B 1 84  ? 32.994 -1.839  29.239  1.00 19.60 ? 84  LEU B C   1 
ATOM   1733 O  O   . LEU B 1 84  ? 34.133 -1.791  29.707  1.00 19.33 ? 84  LEU B O   1 
ATOM   1734 C  CB  . LEU B 1 84  ? 33.873 -2.575  26.999  1.00 18.20 ? 84  LEU B CB  1 
ATOM   1735 C  CG  . LEU B 1 84  ? 33.691 -3.414  25.727  1.00 17.93 ? 84  LEU B CG  1 
ATOM   1736 C  CD1 . LEU B 1 84  ? 34.910 -3.264  24.836  1.00 18.49 ? 84  LEU B CD1 1 
ATOM   1737 C  CD2 . LEU B 1 84  ? 33.475 -4.874  26.088  1.00 21.72 ? 84  LEU B CD2 1 
ATOM   1738 N  N   . GLY B 1 85  ? 31.960 -1.203  29.785  1.00 19.27 ? 85  GLY B N   1 
ATOM   1739 C  CA  . GLY B 1 85  ? 32.098 -0.439  31.012  1.00 20.60 ? 85  GLY B CA  1 
ATOM   1740 C  C   . GLY B 1 85  ? 32.951 0.815   30.975  1.00 19.49 ? 85  GLY B C   1 
ATOM   1741 O  O   . GLY B 1 85  ? 32.783 1.679   30.110  1.00 19.25 ? 85  GLY B O   1 
ATOM   1742 N  N   . ASN B 1 86  ? 33.866 0.911   31.935  1.00 19.00 ? 86  ASN B N   1 
ATOM   1743 C  CA  . ASN B 1 86  ? 34.757 2.061   32.055  1.00 19.28 ? 86  ASN B CA  1 
ATOM   1744 C  C   . ASN B 1 86  ? 36.217 1.674   32.060  1.00 20.58 ? 86  ASN B C   1 
ATOM   1745 O  O   . ASN B 1 86  ? 36.583 0.562   32.446  1.00 20.95 ? 86  ASN B O   1 
ATOM   1746 C  CB  . ASN B 1 86  ? 34.520 2.815   33.371  1.00 19.73 ? 86  ASN B CB  1 
ATOM   1747 C  CG  . ASN B 1 86  ? 33.200 3.544   33.414  1.00 20.17 ? 86  ASN B CG  1 
ATOM   1748 O  OD1 . ASN B 1 86  ? 32.974 4.496   32.664  1.00 20.10 ? 86  ASN B OD1 1 
ATOM   1749 N  ND2 . ASN B 1 86  ? 32.319 3.107   34.305  1.00 20.02 ? 86  ASN B ND2 1 
ATOM   1750 N  N   . VAL B 1 87  ? 37.043 2.619   31.630  1.00 20.31 ? 87  VAL B N   1 
ATOM   1751 C  CA  . VAL B 1 87  ? 38.486 2.470   31.666  1.00 21.10 ? 87  VAL B CA  1 
ATOM   1752 C  C   . VAL B 1 87  ? 38.817 3.522   32.722  1.00 21.80 ? 87  VAL B C   1 
ATOM   1753 O  O   . VAL B 1 87  ? 38.067 4.491   32.886  1.00 18.98 ? 87  VAL B O   1 
ATOM   1754 C  CB  . VAL B 1 87  ? 39.156 2.834   30.322  1.00 22.18 ? 87  VAL B CB  1 
ATOM   1755 C  CG1 . VAL B 1 87  ? 38.669 1.894   29.234  1.00 24.20 ? 87  VAL B CG1 1 
ATOM   1756 C  CG2 . VAL B 1 87  ? 38.867 4.277   29.958  1.00 22.70 ? 87  VAL B CG2 1 
ATOM   1757 N  N   . THR B 1 88  ? 39.906 3.337   33.456  1.00 22.10 ? 88  THR B N   1 
ATOM   1758 C  CA  . THR B 1 88  ? 40.257 4.297   34.496  1.00 21.16 ? 88  THR B CA  1 
ATOM   1759 C  C   . THR B 1 88  ? 41.583 4.977   34.217  1.00 22.77 ? 88  THR B C   1 
ATOM   1760 O  O   . THR B 1 88  ? 42.634 4.334   34.211  1.00 20.65 ? 88  THR B O   1 
ATOM   1761 C  CB  . THR B 1 88  ? 40.347 3.620   35.870  1.00 22.68 ? 88  THR B CB  1 
ATOM   1762 O  OG1 . THR B 1 88  ? 39.139 2.892   36.123  1.00 23.35 ? 88  THR B OG1 1 
ATOM   1763 C  CG2 . THR B 1 88  ? 40.545 4.667   36.962  1.00 23.04 ? 88  THR B CG2 1 
ATOM   1764 N  N   . ALA B 1 89  ? 41.524 6.287   33.998  1.00 23.04 ? 89  ALA B N   1 
ATOM   1765 C  CA  . ALA B 1 89  ? 42.715 7.075   33.720  1.00 24.47 ? 89  ALA B CA  1 
ATOM   1766 C  C   . ALA B 1 89  ? 43.380 7.445   35.039  1.00 25.56 ? 89  ALA B C   1 
ATOM   1767 O  O   . ALA B 1 89  ? 42.700 7.805   36.000  1.00 24.49 ? 89  ALA B O   1 
ATOM   1768 C  CB  . ALA B 1 89  ? 42.331 8.331   32.954  1.00 24.69 ? 89  ALA B CB  1 
ATOM   1769 N  N   . ASP B 1 90  ? 44.707 7.355   35.087  1.00 26.66 ? 90  ASP B N   1 
ATOM   1770 C  CA  . ASP B 1 90  ? 45.437 7.686   36.305  1.00 29.11 ? 90  ASP B CA  1 
ATOM   1771 C  C   . ASP B 1 90  ? 45.752 9.176   36.373  1.00 29.74 ? 90  ASP B C   1 
ATOM   1772 O  O   . ASP B 1 90  ? 45.313 9.949   35.520  1.00 28.67 ? 90  ASP B O   1 
ATOM   1773 C  CB  . ASP B 1 90  ? 46.727 6.861   36.394  1.00 28.89 ? 90  ASP B CB  1 
ATOM   1774 C  CG  . ASP B 1 90  ? 47.733 7.214   35.309  1.00 30.53 ? 90  ASP B CG  1 
ATOM   1775 O  OD1 . ASP B 1 90  ? 48.738 6.484   35.187  1.00 31.76 ? 90  ASP B OD1 1 
ATOM   1776 O  OD2 . ASP B 1 90  ? 47.533 8.214   34.587  1.00 31.27 ? 90  ASP B OD2 1 
ATOM   1777 N  N   . LYS B 1 91  ? 46.512 9.573   37.391  1.00 31.05 ? 91  LYS B N   1 
ATOM   1778 C  CA  . LYS B 1 91  ? 46.876 10.974  37.590  1.00 32.60 ? 91  LYS B CA  1 
ATOM   1779 C  C   . LYS B 1 91  ? 47.541 11.614  36.375  1.00 33.20 ? 91  LYS B C   1 
ATOM   1780 O  O   . LYS B 1 91  ? 47.423 12.820  36.159  1.00 33.79 ? 91  LYS B O   1 
ATOM   1781 C  CB  . LYS B 1 91  ? 47.807 11.111  38.797  1.00 34.98 ? 91  LYS B CB  1 
ATOM   1782 C  CG  . LYS B 1 91  ? 49.109 10.330  38.664  1.00 37.65 ? 91  LYS B CG  1 
ATOM   1783 C  CD  . LYS B 1 91  ? 50.091 10.668  39.781  1.00 40.40 ? 91  LYS B CD  1 
ATOM   1784 C  CE  . LYS B 1 91  ? 49.557 10.285  41.150  1.00 41.11 ? 91  LYS B CE  1 
ATOM   1785 N  NZ  . LYS B 1 91  ? 50.553 10.577  42.219  1.00 42.22 ? 91  LYS B NZ  1 
ATOM   1786 N  N   . ASP B 1 92  ? 48.248 10.807  35.592  1.00 33.36 ? 92  ASP B N   1 
ATOM   1787 C  CA  . ASP B 1 92  ? 48.936 11.303  34.404  1.00 33.36 ? 92  ASP B CA  1 
ATOM   1788 C  C   . ASP B 1 92  ? 48.051 11.262  33.162  1.00 32.36 ? 92  ASP B C   1 
ATOM   1789 O  O   . ASP B 1 92  ? 48.508 11.543  32.053  1.00 32.94 ? 92  ASP B O   1 
ATOM   1790 C  CB  . ASP B 1 92  ? 50.212 10.495  34.176  1.00 35.15 ? 92  ASP B CB  1 
ATOM   1791 C  CG  . ASP B 1 92  ? 51.230 10.698  35.286  1.00 37.69 ? 92  ASP B CG  1 
ATOM   1792 O  OD1 . ASP B 1 92  ? 51.942 9.733   35.630  1.00 40.38 ? 92  ASP B OD1 1 
ATOM   1793 O  OD2 . ASP B 1 92  ? 51.318 11.827  35.813  1.00 39.40 ? 92  ASP B OD2 1 
ATOM   1794 N  N   . GLY B 1 93  ? 46.784 10.912  33.359  1.00 30.60 ? 93  GLY B N   1 
ATOM   1795 C  CA  . GLY B 1 93  ? 45.843 10.862  32.255  1.00 29.47 ? 93  GLY B CA  1 
ATOM   1796 C  C   . GLY B 1 93  ? 45.924 9.633   31.370  1.00 28.62 ? 93  GLY B C   1 
ATOM   1797 O  O   . GLY B 1 93  ? 45.411 9.633   30.248  1.00 27.94 ? 93  GLY B O   1 
ATOM   1798 N  N   . VAL B 1 94  ? 46.557 8.579   31.866  1.00 27.61 ? 94  VAL B N   1 
ATOM   1799 C  CA  . VAL B 1 94  ? 46.686 7.360   31.087  1.00 26.29 ? 94  VAL B CA  1 
ATOM   1800 C  C   . VAL B 1 94  ? 45.844 6.229   31.658  1.00 26.17 ? 94  VAL B C   1 
ATOM   1801 O  O   . VAL B 1 94  ? 45.825 5.995   32.867  1.00 26.21 ? 94  VAL B O   1 
ATOM   1802 C  CB  . VAL B 1 94  ? 48.155 6.896   31.013  1.00 26.95 ? 94  VAL B CB  1 
ATOM   1803 C  CG1 . VAL B 1 94  ? 48.250 5.579   30.260  1.00 25.40 ? 94  VAL B CG1 1 
ATOM   1804 C  CG2 . VAL B 1 94  ? 48.996 7.957   30.324  1.00 28.17 ? 94  VAL B CG2 1 
ATOM   1805 N  N   . ALA B 1 95  ? 45.132 5.540   30.777  1.00 24.46 ? 95  ALA B N   1 
ATOM   1806 C  CA  . ALA B 1 95  ? 44.308 4.421   31.189  1.00 24.98 ? 95  ALA B CA  1 
ATOM   1807 C  C   . ALA B 1 95  ? 44.908 3.165   30.576  1.00 25.55 ? 95  ALA B C   1 
ATOM   1808 O  O   . ALA B 1 95  ? 44.972 3.032   29.356  1.00 26.15 ? 95  ALA B O   1 
ATOM   1809 C  CB  . ALA B 1 95  ? 42.873 4.611   30.711  1.00 24.96 ? 95  ALA B CB  1 
ATOM   1810 N  N   . ASP B 1 96  ? 45.383 2.263   31.427  1.00 25.87 ? 96  ASP B N   1 
ATOM   1811 C  CA  . ASP B 1 96  ? 45.958 1.011   30.958  1.00 28.23 ? 96  ASP B CA  1 
ATOM   1812 C  C   . ASP B 1 96  ? 44.822 -0.003  30.932  1.00 28.08 ? 96  ASP B C   1 
ATOM   1813 O  O   . ASP B 1 96  ? 44.281 -0.378  31.974  1.00 29.42 ? 96  ASP B O   1 
ATOM   1814 C  CB  . ASP B 1 96  ? 47.082 0.573   31.895  1.00 30.23 ? 96  ASP B CB  1 
ATOM   1815 C  CG  . ASP B 1 96  ? 48.332 1.415   31.722  1.00 34.35 ? 96  ASP B CG  1 
ATOM   1816 O  OD1 . ASP B 1 96  ? 48.937 1.803   32.742  1.00 38.24 ? 96  ASP B OD1 1 
ATOM   1817 O  OD2 . ASP B 1 96  ? 48.711 1.686   30.561  1.00 36.19 ? 96  ASP B OD2 1 
ATOM   1818 N  N   . VAL B 1 97  ? 44.457 -0.425  29.726  1.00 26.31 ? 97  VAL B N   1 
ATOM   1819 C  CA  . VAL B 1 97  ? 43.353 -1.355  29.533  1.00 23.73 ? 97  VAL B CA  1 
ATOM   1820 C  C   . VAL B 1 97  ? 43.754 -2.821  29.463  1.00 23.82 ? 97  VAL B C   1 
ATOM   1821 O  O   . VAL B 1 97  ? 44.648 -3.200  28.716  1.00 20.79 ? 97  VAL B O   1 
ATOM   1822 C  CB  . VAL B 1 97  ? 42.578 -1.005  28.248  1.00 23.63 ? 97  VAL B CB  1 
ATOM   1823 C  CG1 . VAL B 1 97  ? 41.348 -1.891  28.125  1.00 22.32 ? 97  VAL B CG1 1 
ATOM   1824 C  CG2 . VAL B 1 97  ? 42.186 0.463   28.263  1.00 23.47 ? 97  VAL B CG2 1 
ATOM   1825 N  N   . SER B 1 98  ? 43.076 -3.642  30.255  1.00 26.42 ? 98  SER B N   1 
ATOM   1826 C  CA  . SER B 1 98  ? 43.325 -5.076  30.277  1.00 29.35 ? 98  SER B CA  1 
ATOM   1827 C  C   . SER B 1 98  ? 42.021 -5.732  30.707  1.00 30.73 ? 98  SER B C   1 
ATOM   1828 O  O   . SER B 1 98  ? 41.760 -5.902  31.900  1.00 31.00 ? 98  SER B O   1 
ATOM   1829 C  CB  . SER B 1 98  ? 44.441 -5.419  31.265  1.00 31.87 ? 98  SER B CB  1 
ATOM   1830 O  OG  . SER B 1 98  ? 44.827 -6.778  31.130  1.00 34.97 ? 98  SER B OG  1 
ATOM   1831 N  N   . ILE B 1 99  ? 41.205 -6.088  29.721  1.00 29.53 ? 99  ILE B N   1 
ATOM   1832 C  CA  . ILE B 1 99  ? 39.905 -6.694  29.967  1.00 29.88 ? 99  ILE B CA  1 
ATOM   1833 C  C   . ILE B 1 99  ? 39.721 -7.953  29.138  1.00 27.92 ? 99  ILE B C   1 
ATOM   1834 O  O   . ILE B 1 99  ? 40.435 -8.183  28.167  1.00 25.22 ? 99  ILE B O   1 
ATOM   1835 C  CB  . ILE B 1 99  ? 38.760 -5.735  29.555  1.00 32.38 ? 99  ILE B CB  1 
ATOM   1836 C  CG1 . ILE B 1 99  ? 38.968 -4.353  30.172  1.00 35.24 ? 99  ILE B CG1 1 
ATOM   1837 C  CG2 . ILE B 1 99  ? 37.416 -6.308  29.986  1.00 35.85 ? 99  ILE B CG2 1 
ATOM   1838 C  CD1 . ILE B 1 99  ? 37.966 -3.317  29.675  1.00 34.35 ? 99  ILE B CD1 1 
ATOM   1839 N  N   . GLU B 1 100 ? 38.758 -8.766  29.553  1.00 26.67 ? 100 GLU B N   1 
ATOM   1840 C  CA  . GLU B 1 100 ? 38.376 -9.971  28.840  1.00 26.09 ? 100 GLU B CA  1 
ATOM   1841 C  C   . GLU B 1 100 ? 36.857 -9.923  28.841  1.00 24.63 ? 100 GLU B C   1 
ATOM   1842 O  O   . GLU B 1 100 ? 36.238 -9.698  29.883  1.00 22.73 ? 100 GLU B O   1 
ATOM   1843 C  CB  . GLU B 1 100 ? 38.895 -11.231 29.538  1.00 31.01 ? 100 GLU B CB  1 
ATOM   1844 C  CG  . GLU B 1 100 ? 40.301 -11.612 29.084  1.00 35.11 ? 100 GLU B CG  1 
ATOM   1845 C  CD  . GLU B 1 100 ? 40.731 -12.987 29.565  1.00 39.72 ? 100 GLU B CD  1 
ATOM   1846 O  OE1 . GLU B 1 100 ? 39.915 -13.931 29.477  1.00 41.29 ? 100 GLU B OE1 1 
ATOM   1847 O  OE2 . GLU B 1 100 ? 41.889 -13.127 30.015  1.00 39.78 ? 100 GLU B OE2 1 
ATOM   1848 N  N   . ASP B 1 101 ? 36.262 -10.094 27.667  1.00 22.84 ? 101 ASP B N   1 
ATOM   1849 C  CA  . ASP B 1 101 ? 34.816 -10.040 27.541  1.00 22.50 ? 101 ASP B CA  1 
ATOM   1850 C  C   . ASP B 1 101 ? 34.298 -11.287 26.841  1.00 21.43 ? 101 ASP B C   1 
ATOM   1851 O  O   . ASP B 1 101 ? 34.959 -11.835 25.960  1.00 21.91 ? 101 ASP B O   1 
ATOM   1852 C  CB  . ASP B 1 101 ? 34.413 -8.781  26.767  1.00 20.66 ? 101 ASP B CB  1 
ATOM   1853 C  CG  . ASP B 1 101 ? 32.936 -8.471  26.890  1.00 20.24 ? 101 ASP B CG  1 
ATOM   1854 O  OD1 . ASP B 1 101 ? 32.188 -8.679  25.913  1.00 18.80 ? 101 ASP B OD1 1 
ATOM   1855 O  OD2 . ASP B 1 101 ? 32.524 -8.020  27.975  1.00 21.01 ? 101 ASP B OD2 1 
ATOM   1856 N  N   . SER B 1 102 ? 33.110 -11.727 27.245  1.00 20.59 ? 102 SER B N   1 
ATOM   1857 C  CA  . SER B 1 102 ? 32.500 -12.925 26.687  1.00 19.07 ? 102 SER B CA  1 
ATOM   1858 C  C   . SER B 1 102 ? 31.392 -12.625 25.687  1.00 18.61 ? 102 SER B C   1 
ATOM   1859 O  O   . SER B 1 102 ? 30.920 -13.521 24.991  1.00 19.81 ? 102 SER B O   1 
ATOM   1860 C  CB  . SER B 1 102 ? 31.920 -13.776 27.820  1.00 21.52 ? 102 SER B CB  1 
ATOM   1861 O  OG  . SER B 1 102 ? 32.891 -14.025 28.819  1.00 24.31 ? 102 SER B OG  1 
ATOM   1862 N  N   . VAL B 1 103 ? 30.975 -11.369 25.603  1.00 17.60 ? 103 VAL B N   1 
ATOM   1863 C  CA  . VAL B 1 103 ? 29.880 -11.017 24.708  1.00 18.67 ? 103 VAL B CA  1 
ATOM   1864 C  C   . VAL B 1 103 ? 30.336 -10.551 23.328  1.00 19.16 ? 103 VAL B C   1 
ATOM   1865 O  O   . VAL B 1 103 ? 29.781 -10.983 22.316  1.00 19.40 ? 103 VAL B O   1 
ATOM   1866 C  CB  . VAL B 1 103 ? 28.972 -9.956  25.365  1.00 16.89 ? 103 VAL B CB  1 
ATOM   1867 C  CG1 . VAL B 1 103 ? 27.776 -9.655  24.475  1.00 19.20 ? 103 VAL B CG1 1 
ATOM   1868 C  CG2 . VAL B 1 103 ? 28.499 -10.465 26.714  1.00 20.57 ? 103 VAL B CG2 1 
ATOM   1869 N  N   . ILE B 1 104 ? 31.332 -9.669  23.277  1.00 18.26 ? 104 ILE B N   1 
ATOM   1870 C  CA  . ILE B 1 104 ? 31.835 -9.220  21.985  1.00 18.43 ? 104 ILE B CA  1 
ATOM   1871 C  C   . ILE B 1 104 ? 32.554 -10.401 21.344  1.00 18.76 ? 104 ILE B C   1 
ATOM   1872 O  O   . ILE B 1 104 ? 32.899 -11.363 22.025  1.00 19.24 ? 104 ILE B O   1 
ATOM   1873 C  CB  . ILE B 1 104 ? 32.828 -8.044  22.111  1.00 17.65 ? 104 ILE B CB  1 
ATOM   1874 C  CG1 . ILE B 1 104 ? 34.012 -8.434  22.997  1.00 18.05 ? 104 ILE B CG1 1 
ATOM   1875 C  CG2 . ILE B 1 104 ? 32.114 -6.826  22.681  1.00 18.48 ? 104 ILE B CG2 1 
ATOM   1876 C  CD1 . ILE B 1 104 ? 35.138 -7.414  22.989  1.00 18.28 ? 104 ILE B CD1 1 
ATOM   1877 N  N   . SER B 1 105 ? 32.761 -10.331 20.036  1.00 19.01 ? 105 SER B N   1 
ATOM   1878 C  CA  . SER B 1 105 ? 33.440 -11.394 19.307  1.00 20.07 ? 105 SER B CA  1 
ATOM   1879 C  C   . SER B 1 105 ? 34.095 -10.796 18.075  1.00 20.18 ? 105 SER B C   1 
ATOM   1880 O  O   . SER B 1 105 ? 33.865 -9.634  17.752  1.00 18.71 ? 105 SER B O   1 
ATOM   1881 C  CB  . SER B 1 105 ? 32.436 -12.470 18.880  1.00 19.91 ? 105 SER B CB  1 
ATOM   1882 O  OG  . SER B 1 105 ? 33.070 -13.485 18.118  1.00 22.90 ? 105 SER B OG  1 
ATOM   1883 N  N   . LEU B 1 106 ? 34.916 -11.588 17.393  1.00 21.36 ? 106 LEU B N   1 
ATOM   1884 C  CA  . LEU B 1 106 ? 35.571 -11.114 16.183  1.00 20.67 ? 106 LEU B CA  1 
ATOM   1885 C  C   . LEU B 1 106 ? 34.967 -11.821 14.972  1.00 22.41 ? 106 LEU B C   1 
ATOM   1886 O  O   . LEU B 1 106 ? 35.532 -11.806 13.883  1.00 21.62 ? 106 LEU B O   1 
ATOM   1887 C  CB  . LEU B 1 106 ? 37.082 -11.361 16.251  1.00 19.81 ? 106 LEU B CB  1 
ATOM   1888 C  CG  . LEU B 1 106 ? 37.835 -10.654 17.386  1.00 21.26 ? 106 LEU B CG  1 
ATOM   1889 C  CD1 . LEU B 1 106 ? 39.322 -10.842 17.176  1.00 22.69 ? 106 LEU B CD1 1 
ATOM   1890 C  CD2 . LEU B 1 106 ? 37.494 -9.158  17.419  1.00 21.08 ? 106 LEU B CD2 1 
ATOM   1891 N  N   . SER B 1 107 ? 33.809 -12.443 15.176  1.00 23.81 ? 107 SER B N   1 
ATOM   1892 C  CA  . SER B 1 107 ? 33.108 -13.132 14.097  1.00 25.53 ? 107 SER B CA  1 
ATOM   1893 C  C   . SER B 1 107 ? 31.644 -13.331 14.474  1.00 25.91 ? 107 SER B C   1 
ATOM   1894 O  O   . SER B 1 107 ? 31.290 -13.276 15.650  1.00 26.12 ? 107 SER B O   1 
ATOM   1895 C  CB  . SER B 1 107 ? 33.754 -14.494 13.813  1.00 27.83 ? 107 SER B CB  1 
ATOM   1896 O  OG  . SER B 1 107 ? 33.408 -15.451 14.801  1.00 28.76 ? 107 SER B OG  1 
ATOM   1897 N  N   . GLY B 1 108 ? 30.795 -13.552 13.474  1.00 27.06 ? 108 GLY B N   1 
ATOM   1898 C  CA  . GLY B 1 108 ? 29.384 -13.775 13.736  1.00 26.55 ? 108 GLY B CA  1 
ATOM   1899 C  C   . GLY B 1 108 ? 28.565 -12.548 14.091  1.00 26.48 ? 108 GLY B C   1 
ATOM   1900 O  O   . GLY B 1 108 ? 29.005 -11.408 13.920  1.00 25.68 ? 108 GLY B O   1 
ATOM   1901 N  N   . ASP B 1 109 ? 27.360 -12.795 14.596  1.00 25.75 ? 109 ASP B N   1 
ATOM   1902 C  CA  . ASP B 1 109 ? 26.435 -11.734 14.982  1.00 26.54 ? 109 ASP B CA  1 
ATOM   1903 C  C   . ASP B 1 109 ? 27.030 -10.697 15.927  1.00 24.77 ? 109 ASP B C   1 
ATOM   1904 O  O   . ASP B 1 109 ? 26.711 -9.512  15.831  1.00 23.33 ? 109 ASP B O   1 
ATOM   1905 C  CB  . ASP B 1 109 ? 25.190 -12.338 15.640  1.00 28.71 ? 109 ASP B CB  1 
ATOM   1906 C  CG  . ASP B 1 109 ? 24.335 -13.129 14.668  1.00 33.75 ? 109 ASP B CG  1 
ATOM   1907 O  OD1 . ASP B 1 109 ? 23.326 -13.718 15.116  1.00 34.96 ? 109 ASP B OD1 1 
ATOM   1908 O  OD2 . ASP B 1 109 ? 24.661 -13.158 13.462  1.00 35.81 ? 109 ASP B OD2 1 
ATOM   1909 N  N   . HIS B 1 110 ? 27.880 -11.139 16.847  1.00 23.60 ? 110 HIS B N   1 
ATOM   1910 C  CA  . HIS B 1 110 ? 28.483 -10.225 17.811  1.00 23.50 ? 110 HIS B CA  1 
ATOM   1911 C  C   . HIS B 1 110 ? 29.818 -9.634  17.366  1.00 22.44 ? 110 HIS B C   1 
ATOM   1912 O  O   . HIS B 1 110 ? 30.490 -8.962  18.149  1.00 22.27 ? 110 HIS B O   1 
ATOM   1913 C  CB  . HIS B 1 110 ? 28.679 -10.925 19.159  1.00 24.62 ? 110 HIS B CB  1 
ATOM   1914 C  CG  . HIS B 1 110 ? 27.400 -11.275 19.858  1.00 26.80 ? 110 HIS B CG  1 
ATOM   1915 N  ND1 . HIS B 1 110 ? 27.350 -11.585 21.200  1.00 28.04 ? 110 HIS B ND1 1 
ATOM   1916 C  CD2 . HIS B 1 110 ? 26.130 -11.378 19.400  1.00 27.49 ? 110 HIS B CD2 1 
ATOM   1917 C  CE1 . HIS B 1 110 ? 26.103 -11.863 21.540  1.00 28.64 ? 110 HIS B CE1 1 
ATOM   1918 N  NE2 . HIS B 1 110 ? 25.343 -11.745 20.466  1.00 28.28 ? 110 HIS B NE2 1 
ATOM   1919 N  N   . SER B 1 111 ? 30.201 -9.868  16.114  1.00 22.57 ? 111 SER B N   1 
ATOM   1920 C  CA  . SER B 1 111 ? 31.477 -9.359  15.628  1.00 20.81 ? 111 SER B CA  1 
ATOM   1921 C  C   . SER B 1 111 ? 31.564 -7.844  15.681  1.00 20.80 ? 111 SER B C   1 
ATOM   1922 O  O   . SER B 1 111 ? 30.649 -7.141  15.253  1.00 21.33 ? 111 SER B O   1 
ATOM   1923 C  CB  . SER B 1 111 ? 31.741 -9.820  14.196  1.00 22.68 ? 111 SER B CB  1 
ATOM   1924 O  OG  . SER B 1 111 ? 33.014 -9.358  13.768  1.00 21.99 ? 111 SER B OG  1 
ATOM   1925 N  N   . ILE B 1 112 ? 32.680 -7.347  16.197  1.00 19.75 ? 112 ILE B N   1 
ATOM   1926 C  CA  . ILE B 1 112 ? 32.893 -5.915  16.299  1.00 18.06 ? 112 ILE B CA  1 
ATOM   1927 C  C   . ILE B 1 112 ? 33.803 -5.433  15.176  1.00 18.82 ? 112 ILE B C   1 
ATOM   1928 O  O   . ILE B 1 112 ? 34.145 -4.259  15.113  1.00 17.65 ? 112 ILE B O   1 
ATOM   1929 C  CB  . ILE B 1 112 ? 33.502 -5.542  17.663  1.00 18.31 ? 112 ILE B CB  1 
ATOM   1930 C  CG1 . ILE B 1 112 ? 34.844 -6.253  17.857  1.00 20.76 ? 112 ILE B CG1 1 
ATOM   1931 C  CG2 . ILE B 1 112 ? 32.544 -5.940  18.772  1.00 18.09 ? 112 ILE B CG2 1 
ATOM   1932 C  CD1 . ILE B 1 112 ? 35.536 -5.912  19.173  1.00 21.61 ? 112 ILE B CD1 1 
ATOM   1933 N  N   . ILE B 1 113 ? 34.191 -6.345  14.289  1.00 18.43 ? 113 ILE B N   1 
ATOM   1934 C  CA  . ILE B 1 113 ? 35.044 -5.974  13.161  1.00 19.33 ? 113 ILE B CA  1 
ATOM   1935 C  C   . ILE B 1 113 ? 34.283 -4.988  12.271  1.00 17.63 ? 113 ILE B C   1 
ATOM   1936 O  O   . ILE B 1 113 ? 33.141 -5.238  11.885  1.00 19.21 ? 113 ILE B O   1 
ATOM   1937 C  CB  . ILE B 1 113 ? 35.427 -7.214  12.311  1.00 18.72 ? 113 ILE B CB  1 
ATOM   1938 C  CG1 . ILE B 1 113 ? 36.234 -8.201  13.158  1.00 20.09 ? 113 ILE B CG1 1 
ATOM   1939 C  CG2 . ILE B 1 113 ? 36.236 -6.789  11.084  1.00 19.10 ? 113 ILE B CG2 1 
ATOM   1940 C  CD1 . ILE B 1 113 ? 37.560 -7.672  13.642  1.00 20.51 ? 113 ILE B CD1 1 
ATOM   1941 N  N   . GLY B 1 114 ? 34.916 -3.867  11.944  1.00 16.39 ? 114 GLY B N   1 
ATOM   1942 C  CA  . GLY B 1 114 ? 34.260 -2.887  11.099  1.00 17.54 ? 114 GLY B CA  1 
ATOM   1943 C  C   . GLY B 1 114 ? 33.382 -1.927  11.877  1.00 17.54 ? 114 GLY B C   1 
ATOM   1944 O  O   . GLY B 1 114 ? 32.693 -1.093  11.288  1.00 18.04 ? 114 GLY B O   1 
ATOM   1945 N  N   . ARG B 1 115 ? 33.385 -2.044  13.201  1.00 18.02 ? 115 ARG B N   1 
ATOM   1946 C  CA  . ARG B 1 115 ? 32.584 -1.144  14.023  1.00 19.77 ? 115 ARG B CA  1 
ATOM   1947 C  C   . ARG B 1 115 ? 33.524 -0.174  14.738  1.00 21.64 ? 115 ARG B C   1 
ATOM   1948 O  O   . ARG B 1 115 ? 34.734 -0.221  14.523  1.00 22.68 ? 115 ARG B O   1 
ATOM   1949 C  CB  . ARG B 1 115 ? 31.708 -1.953  14.991  1.00 21.07 ? 115 ARG B CB  1 
ATOM   1950 C  CG  . ARG B 1 115 ? 30.694 -2.816  14.230  1.00 21.27 ? 115 ARG B CG  1 
ATOM   1951 C  CD  . ARG B 1 115 ? 29.769 -3.621  15.116  1.00 23.17 ? 115 ARG B CD  1 
ATOM   1952 N  NE  . ARG B 1 115 ? 29.004 -4.594  14.336  1.00 22.89 ? 115 ARG B NE  1 
ATOM   1953 C  CZ  . ARG B 1 115 ? 27.956 -4.305  13.566  1.00 23.97 ? 115 ARG B CZ  1 
ATOM   1954 N  NH1 . ARG B 1 115 ? 27.340 -5.272  12.900  1.00 24.50 ? 115 ARG B NH1 1 
ATOM   1955 N  NH2 . ARG B 1 115 ? 27.507 -3.060  13.471  1.00 23.96 ? 115 ARG B NH2 1 
ATOM   1956 N  N   . THR B 1 116 ? 32.985 0.703   15.578  1.00 21.30 ? 116 THR B N   1 
ATOM   1957 C  CA  . THR B 1 116 ? 33.818 1.700   16.240  1.00 20.05 ? 116 THR B CA  1 
ATOM   1958 C  C   . THR B 1 116 ? 33.952 1.593   17.750  1.00 20.24 ? 116 THR B C   1 
ATOM   1959 O  O   . THR B 1 116 ? 32.960 1.437   18.460  1.00 21.19 ? 116 THR B O   1 
ATOM   1960 C  CB  . THR B 1 116 ? 33.302 3.115   15.917  1.00 20.92 ? 116 THR B CB  1 
ATOM   1961 O  OG1 . THR B 1 116 ? 33.300 3.303   14.499  1.00 20.82 ? 116 THR B OG1 1 
ATOM   1962 C  CG2 . THR B 1 116 ? 34.185 4.175   16.562  1.00 19.73 ? 116 THR B CG2 1 
ATOM   1963 N  N   . LEU B 1 117 ? 35.192 1.691   18.227  1.00 18.62 ? 117 LEU B N   1 
ATOM   1964 C  CA  . LEU B 1 117 ? 35.490 1.657   19.654  1.00 17.44 ? 117 LEU B CA  1 
ATOM   1965 C  C   . LEU B 1 117 ? 35.538 3.121   20.082  1.00 19.15 ? 117 LEU B C   1 
ATOM   1966 O  O   . LEU B 1 117 ? 36.207 3.938   19.442  1.00 17.72 ? 117 LEU B O   1 
ATOM   1967 C  CB  . LEU B 1 117 ? 36.853 1.004   19.910  1.00 16.46 ? 117 LEU B CB  1 
ATOM   1968 C  CG  . LEU B 1 117 ? 37.302 0.909   21.375  1.00 15.52 ? 117 LEU B CG  1 
ATOM   1969 C  CD1 . LEU B 1 117 ? 36.349 0.018   22.154  1.00 16.41 ? 117 LEU B CD1 1 
ATOM   1970 C  CD2 . LEU B 1 117 ? 38.721 0.360   21.450  1.00 15.65 ? 117 LEU B CD2 1 
ATOM   1971 N  N   . VAL B 1 118 ? 34.836 3.448   21.162  1.00 18.24 ? 118 VAL B N   1 
ATOM   1972 C  CA  . VAL B 1 118 ? 34.784 4.823   21.645  1.00 18.72 ? 118 VAL B CA  1 
ATOM   1973 C  C   . VAL B 1 118 ? 35.117 4.959   23.133  1.00 16.92 ? 118 VAL B C   1 
ATOM   1974 O  O   . VAL B 1 118 ? 34.768 4.096   23.938  1.00 17.37 ? 118 VAL B O   1 
ATOM   1975 C  CB  . VAL B 1 118 ? 33.368 5.423   21.421  1.00 20.27 ? 118 VAL B CB  1 
ATOM   1976 C  CG1 . VAL B 1 118 ? 33.323 6.874   21.888  1.00 20.36 ? 118 VAL B CG1 1 
ATOM   1977 C  CG2 . VAL B 1 118 ? 32.984 5.325   19.952  1.00 19.81 ? 118 VAL B CG2 1 
ATOM   1978 N  N   . VAL B 1 119 ? 35.810 6.040   23.486  1.00 17.24 ? 119 VAL B N   1 
ATOM   1979 C  CA  . VAL B 1 119 ? 36.123 6.331   24.883  1.00 18.09 ? 119 VAL B CA  1 
ATOM   1980 C  C   . VAL B 1 119 ? 35.443 7.678   25.127  1.00 19.72 ? 119 VAL B C   1 
ATOM   1981 O  O   . VAL B 1 119 ? 35.643 8.632   24.372  1.00 17.63 ? 119 VAL B O   1 
ATOM   1982 C  CB  . VAL B 1 119 ? 37.652 6.404   25.163  1.00 20.64 ? 119 VAL B CB  1 
ATOM   1983 C  CG1 . VAL B 1 119 ? 38.325 7.441   24.277  1.00 20.31 ? 119 VAL B CG1 1 
ATOM   1984 C  CG2 . VAL B 1 119 ? 37.883 6.727   26.642  1.00 20.51 ? 119 VAL B CG2 1 
ATOM   1985 N  N   . HIS B 1 120 ? 34.623 7.732   26.174  1.00 19.29 ? 120 HIS B N   1 
ATOM   1986 C  CA  . HIS B 1 120 ? 33.829 8.912   26.504  1.00 20.18 ? 120 HIS B CA  1 
ATOM   1987 C  C   . HIS B 1 120 ? 34.365 9.958   27.472  1.00 21.45 ? 120 HIS B C   1 
ATOM   1988 O  O   . HIS B 1 120 ? 35.331 9.740   28.207  1.00 22.13 ? 120 HIS B O   1 
ATOM   1989 C  CB  . HIS B 1 120 ? 32.464 8.457   27.016  1.00 20.16 ? 120 HIS B CB  1 
ATOM   1990 C  CG  . HIS B 1 120 ? 31.621 7.793   25.974  1.00 21.44 ? 120 HIS B CG  1 
ATOM   1991 N  ND1 . HIS B 1 120 ? 30.760 8.493   25.157  1.00 20.71 ? 120 HIS B ND1 1 
ATOM   1992 C  CD2 . HIS B 1 120 ? 31.524 6.496   25.600  1.00 21.10 ? 120 HIS B CD2 1 
ATOM   1993 C  CE1 . HIS B 1 120 ? 30.165 7.654   24.327  1.00 21.65 ? 120 HIS B CE1 1 
ATOM   1994 N  NE2 . HIS B 1 120 ? 30.611 6.436   24.575  1.00 20.98 ? 120 HIS B NE2 1 
ATOM   1995 N  N   . GLU B 1 121 ? 33.667 11.090  27.458  1.00 21.76 ? 121 GLU B N   1 
ATOM   1996 C  CA  . GLU B 1 121 ? 33.935 12.264  28.280  1.00 23.23 ? 121 GLU B CA  1 
ATOM   1997 C  C   . GLU B 1 121 ? 33.709 11.989  29.770  1.00 23.15 ? 121 GLU B C   1 
ATOM   1998 O  O   . GLU B 1 121 ? 34.519 12.373  30.620  1.00 22.52 ? 121 GLU B O   1 
ATOM   1999 C  CB  . GLU B 1 121 ? 32.996 13.390  27.829  1.00 24.99 ? 121 GLU B CB  1 
ATOM   2000 C  CG  . GLU B 1 121 ? 33.013 14.660  28.667  1.00 31.34 ? 121 GLU B CG  1 
ATOM   2001 C  CD  . GLU B 1 121 ? 31.768 15.512  28.449  1.00 34.80 ? 121 GLU B CD  1 
ATOM   2002 O  OE1 . GLU B 1 121 ? 31.747 16.673  28.912  1.00 37.02 ? 121 GLU B OE1 1 
ATOM   2003 O  OE2 . GLU B 1 121 ? 30.803 15.014  27.824  1.00 35.62 ? 121 GLU B OE2 1 
ATOM   2004 N  N   . LYS B 1 122 ? 32.603 11.318  30.074  1.00 23.05 ? 122 LYS B N   1 
ATOM   2005 C  CA  . LYS B 1 122 ? 32.236 11.020  31.452  1.00 22.15 ? 122 LYS B CA  1 
ATOM   2006 C  C   . LYS B 1 122 ? 32.149 9.526   31.746  1.00 21.37 ? 122 LYS B C   1 
ATOM   2007 O  O   . LYS B 1 122 ? 32.247 8.691   30.847  1.00 21.19 ? 122 LYS B O   1 
ATOM   2008 C  CB  . LYS B 1 122 ? 30.889 11.676  31.774  1.00 21.54 ? 122 LYS B CB  1 
ATOM   2009 C  CG  . LYS B 1 122 ? 30.841 13.176  31.516  1.00 23.02 ? 122 LYS B CG  1 
ATOM   2010 C  CD  . LYS B 1 122 ? 31.781 13.934  32.447  1.00 21.43 ? 122 LYS B CD  1 
ATOM   2011 C  CE  . LYS B 1 122 ? 31.736 15.435  32.186  1.00 23.50 ? 122 LYS B CE  1 
ATOM   2012 N  NZ  . LYS B 1 122 ? 32.733 16.166  33.033  1.00 22.18 ? 122 LYS B NZ  1 
ATOM   2013 N  N   . ALA B 1 123 ? 31.951 9.204   33.021  1.00 21.81 ? 123 ALA B N   1 
ATOM   2014 C  CA  . ALA B 1 123 ? 31.843 7.818   33.455  1.00 20.18 ? 123 ALA B CA  1 
ATOM   2015 C  C   . ALA B 1 123 ? 30.545 7.167   32.994  1.00 20.49 ? 123 ALA B C   1 
ATOM   2016 O  O   . ALA B 1 123 ? 29.515 7.828   32.833  1.00 18.16 ? 123 ALA B O   1 
ATOM   2017 C  CB  . ALA B 1 123 ? 31.940 7.739   34.972  1.00 19.06 ? 123 ALA B CB  1 
ATOM   2018 N  N   . ASP B 1 124 ? 30.615 5.858   32.782  1.00 18.97 ? 124 ASP B N   1 
ATOM   2019 C  CA  . ASP B 1 124 ? 29.466 5.060   32.380  1.00 19.55 ? 124 ASP B CA  1 
ATOM   2020 C  C   . ASP B 1 124 ? 28.839 4.596   33.699  1.00 20.28 ? 124 ASP B C   1 
ATOM   2021 O  O   . ASP B 1 124 ? 29.511 3.959   34.508  1.00 21.27 ? 124 ASP B O   1 
ATOM   2022 C  CB  . ASP B 1 124 ? 29.954 3.865   31.554  1.00 18.47 ? 124 ASP B CB  1 
ATOM   2023 C  CG  . ASP B 1 124 ? 28.830 2.964   31.084  1.00 19.16 ? 124 ASP B CG  1 
ATOM   2024 O  OD1 . ASP B 1 124 ? 29.067 2.171   30.145  1.00 19.04 ? 124 ASP B OD1 1 
ATOM   2025 O  OD2 . ASP B 1 124 ? 27.719 3.029   31.646  1.00 20.11 ? 124 ASP B OD2 1 
ATOM   2026 N  N   . ASP B 1 125 ? 27.570 4.930   33.928  1.00 20.67 ? 125 ASP B N   1 
ATOM   2027 C  CA  . ASP B 1 125 ? 26.909 4.538   35.172  1.00 20.97 ? 125 ASP B CA  1 
ATOM   2028 C  C   . ASP B 1 125 ? 26.405 3.101   35.146  1.00 21.52 ? 125 ASP B C   1 
ATOM   2029 O  O   . ASP B 1 125 ? 25.664 2.668   36.031  1.00 22.92 ? 125 ASP B O   1 
ATOM   2030 C  CB  . ASP B 1 125 ? 25.772 5.516   35.519  1.00 20.43 ? 125 ASP B CB  1 
ATOM   2031 C  CG  . ASP B 1 125 ? 24.602 5.459   34.546  1.00 20.43 ? 125 ASP B CG  1 
ATOM   2032 O  OD1 . ASP B 1 125 ? 23.858 6.460   34.483  1.00 20.16 ? 125 ASP B OD1 1 
ATOM   2033 O  OD2 . ASP B 1 125 ? 24.400 4.430   33.869  1.00 19.14 ? 125 ASP B OD2 1 
ATOM   2034 N  N   . LEU B 1 126 ? 26.825 2.373   34.119  1.00 20.95 ? 126 LEU B N   1 
ATOM   2035 C  CA  . LEU B 1 126 ? 26.483 0.970   33.941  1.00 21.40 ? 126 LEU B CA  1 
ATOM   2036 C  C   . LEU B 1 126 ? 24.986 0.680   33.855  1.00 21.57 ? 126 LEU B C   1 
ATOM   2037 O  O   . LEU B 1 126 ? 24.546 -0.440  34.121  1.00 22.25 ? 126 LEU B O   1 
ATOM   2038 C  CB  . LEU B 1 126 ? 27.131 0.145   35.059  1.00 19.82 ? 126 LEU B CB  1 
ATOM   2039 C  CG  . LEU B 1 126 ? 28.629 0.426   35.254  1.00 19.60 ? 126 LEU B CG  1 
ATOM   2040 C  CD1 . LEU B 1 126 ? 29.173 -0.460  36.364  1.00 24.43 ? 126 LEU B CD1 1 
ATOM   2041 C  CD2 . LEU B 1 126 ? 29.393 0.176   33.958  1.00 20.00 ? 126 LEU B CD2 1 
ATOM   2042 N  N   . GLY B 1 127 ? 24.210 1.691   33.475  1.00 21.08 ? 127 GLY B N   1 
ATOM   2043 C  CA  . GLY B 1 127 ? 22.776 1.519   33.316  1.00 23.02 ? 127 GLY B CA  1 
ATOM   2044 C  C   . GLY B 1 127 ? 21.950 1.360   34.577  1.00 24.53 ? 127 GLY B C   1 
ATOM   2045 O  O   . GLY B 1 127 ? 20.827 0.855   34.524  1.00 26.40 ? 127 GLY B O   1 
ATOM   2046 N  N   . LYS B 1 128 ? 22.489 1.793   35.710  1.00 25.70 ? 128 LYS B N   1 
ATOM   2047 C  CA  . LYS B 1 128 ? 21.769 1.683   36.969  1.00 28.30 ? 128 LYS B CA  1 
ATOM   2048 C  C   . LYS B 1 128 ? 21.212 3.035   37.407  1.00 29.28 ? 128 LYS B C   1 
ATOM   2049 O  O   . LYS B 1 128 ? 20.708 3.178   38.521  1.00 29.43 ? 128 LYS B O   1 
ATOM   2050 C  CB  . LYS B 1 128 ? 22.690 1.106   38.050  1.00 30.57 ? 128 LYS B CB  1 
ATOM   2051 C  CG  . LYS B 1 128 ? 23.374 -0.191  37.624  1.00 32.93 ? 128 LYS B CG  1 
ATOM   2052 C  CD  . LYS B 1 128 ? 22.400 -1.091  36.869  1.00 34.47 ? 128 LYS B CD  1 
ATOM   2053 C  CE  . LYS B 1 128 ? 23.125 -2.152  36.056  1.00 37.16 ? 128 LYS B CE  1 
ATOM   2054 N  NZ  . LYS B 1 128 ? 22.262 -2.664  34.949  1.00 34.46 ? 128 LYS B NZ  1 
ATOM   2055 N  N   . GLY B 1 129 ? 21.292 4.019   36.515  1.00 27.97 ? 129 GLY B N   1 
ATOM   2056 C  CA  . GLY B 1 129 ? 20.795 5.346   36.827  1.00 27.39 ? 129 GLY B CA  1 
ATOM   2057 C  C   . GLY B 1 129 ? 19.283 5.437   36.795  1.00 27.02 ? 129 GLY B C   1 
ATOM   2058 O  O   . GLY B 1 129 ? 18.616 4.703   36.064  1.00 26.57 ? 129 GLY B O   1 
ATOM   2059 N  N   . GLY B 1 130 ? 18.738 6.352   37.589  1.00 26.46 ? 130 GLY B N   1 
ATOM   2060 C  CA  . GLY B 1 130 ? 17.299 6.519   37.639  1.00 25.30 ? 130 GLY B CA  1 
ATOM   2061 C  C   . GLY B 1 130 ? 16.766 7.402   36.533  1.00 25.12 ? 130 GLY B C   1 
ATOM   2062 O  O   . GLY B 1 130 ? 16.025 8.344   36.788  1.00 26.17 ? 130 GLY B O   1 
ATOM   2063 N  N   . ASN B 1 131 ? 17.151 7.105   35.297  1.00 24.51 ? 131 ASN B N   1 
ATOM   2064 C  CA  . ASN B 1 131 ? 16.700 7.876   34.147  1.00 23.33 ? 131 ASN B CA  1 
ATOM   2065 C  C   . ASN B 1 131 ? 16.834 7.022   32.903  1.00 22.18 ? 131 ASN B C   1 
ATOM   2066 O  O   . ASN B 1 131 ? 17.604 6.064   32.881  1.00 21.89 ? 131 ASN B O   1 
ATOM   2067 C  CB  . ASN B 1 131 ? 17.520 9.162   34.002  1.00 21.77 ? 131 ASN B CB  1 
ATOM   2068 C  CG  . ASN B 1 131 ? 19.007 8.917   34.093  1.00 24.34 ? 131 ASN B CG  1 
ATOM   2069 O  OD1 . ASN B 1 131 ? 19.625 8.385   33.169  1.00 21.02 ? 131 ASN B OD1 1 
ATOM   2070 N  ND2 . ASN B 1 131 ? 19.596 9.300   35.222  1.00 22.53 ? 131 ASN B ND2 1 
ATOM   2071 N  N   . GLU B 1 132 ? 16.081 7.366   31.867  1.00 22.96 ? 132 GLU B N   1 
ATOM   2072 C  CA  . GLU B 1 132 ? 16.113 6.597   30.636  1.00 22.76 ? 132 GLU B CA  1 
ATOM   2073 C  C   . GLU B 1 132 ? 17.458 6.643   29.914  1.00 23.32 ? 132 GLU B C   1 
ATOM   2074 O  O   . GLU B 1 132 ? 17.873 5.654   29.311  1.00 22.40 ? 132 GLU B O   1 
ATOM   2075 C  CB  . GLU B 1 132 ? 14.997 7.066   29.703  1.00 25.44 ? 132 GLU B CB  1 
ATOM   2076 C  CG  . GLU B 1 132 ? 14.939 6.303   28.396  1.00 27.97 ? 132 GLU B CG  1 
ATOM   2077 C  CD  . GLU B 1 132 ? 13.659 6.555   27.641  1.00 31.21 ? 132 GLU B CD  1 
ATOM   2078 O  OE1 . GLU B 1 132 ? 12.788 5.659   27.633  1.00 35.18 ? 132 GLU B OE1 1 
ATOM   2079 O  OE2 . GLU B 1 132 ? 13.518 7.651   27.065  1.00 32.86 ? 132 GLU B OE2 1 
ATOM   2080 N  N   . GLU B 1 133 ? 18.146 7.778   29.977  1.00 21.66 ? 133 GLU B N   1 
ATOM   2081 C  CA  . GLU B 1 133 ? 19.438 7.888   29.305  1.00 22.07 ? 133 GLU B CA  1 
ATOM   2082 C  C   . GLU B 1 133 ? 20.432 6.857   29.845  1.00 19.79 ? 133 GLU B C   1 
ATOM   2083 O  O   . GLU B 1 133 ? 21.300 6.382   29.111  1.00 19.58 ? 133 GLU B O   1 
ATOM   2084 C  CB  . GLU B 1 133 ? 20.017 9.290   29.470  1.00 23.24 ? 133 GLU B CB  1 
ATOM   2085 C  CG  . GLU B 1 133 ? 21.200 9.567   28.554  1.00 26.05 ? 133 GLU B CG  1 
ATOM   2086 C  CD  . GLU B 1 133 ? 20.809 9.637   27.085  1.00 29.04 ? 133 GLU B CD  1 
ATOM   2087 O  OE1 . GLU B 1 133 ? 21.718 9.725   26.237  1.00 34.11 ? 133 GLU B OE1 1 
ATOM   2088 O  OE2 . GLU B 1 133 ? 19.597 9.611   26.774  1.00 32.27 ? 133 GLU B OE2 1 
ATOM   2089 N  N   . SER B 1 134 ? 20.309 6.514   31.125  1.00 18.61 ? 134 SER B N   1 
ATOM   2090 C  CA  . SER B 1 134 ? 21.203 5.523   31.725  1.00 19.19 ? 134 SER B CA  1 
ATOM   2091 C  C   . SER B 1 134 ? 21.068 4.189   30.996  1.00 18.76 ? 134 SER B C   1 
ATOM   2092 O  O   . SER B 1 134 ? 22.062 3.504   30.750  1.00 18.81 ? 134 SER B O   1 
ATOM   2093 C  CB  . SER B 1 134 ? 20.875 5.322   33.210  1.00 18.92 ? 134 SER B CB  1 
ATOM   2094 O  OG  . SER B 1 134 ? 21.673 4.294   33.776  1.00 18.51 ? 134 SER B OG  1 
ATOM   2095 N  N   . THR B 1 135 ? 19.834 3.839   30.639  1.00 20.70 ? 135 THR B N   1 
ATOM   2096 C  CA  . THR B 1 135 ? 19.541 2.580   29.953  1.00 20.98 ? 135 THR B CA  1 
ATOM   2097 C  C   . THR B 1 135 ? 19.925 2.593   28.472  1.00 21.30 ? 135 THR B C   1 
ATOM   2098 O  O   . THR B 1 135 ? 19.765 1.591   27.775  1.00 20.38 ? 135 THR B O   1 
ATOM   2099 C  CB  . THR B 1 135 ? 18.040 2.227   30.064  1.00 21.88 ? 135 THR B CB  1 
ATOM   2100 O  OG1 . THR B 1 135 ? 17.285 3.042   29.159  1.00 20.48 ? 135 THR B OG1 1 
ATOM   2101 C  CG2 . THR B 1 135 ? 17.540 2.480   31.479  1.00 22.02 ? 135 THR B CG2 1 
ATOM   2102 N  N   . LYS B 1 136 ? 20.438 3.720   27.991  1.00 21.92 ? 136 LYS B N   1 
ATOM   2103 C  CA  . LYS B 1 136 ? 20.838 3.820   26.593  1.00 21.85 ? 136 LYS B CA  1 
ATOM   2104 C  C   . LYS B 1 136 ? 22.341 4.024   26.412  1.00 21.84 ? 136 LYS B C   1 
ATOM   2105 O  O   . LYS B 1 136 ? 22.983 3.315   25.636  1.00 21.83 ? 136 LYS B O   1 
ATOM   2106 C  CB  . LYS B 1 136 ? 20.084 4.965   25.907  1.00 24.93 ? 136 LYS B CB  1 
ATOM   2107 C  CG  . LYS B 1 136 ? 18.570 4.815   25.941  1.00 27.84 ? 136 LYS B CG  1 
ATOM   2108 C  CD  . LYS B 1 136 ? 17.886 5.766   24.968  1.00 32.88 ? 136 LYS B CD  1 
ATOM   2109 C  CE  . LYS B 1 136 ? 18.198 7.222   25.271  1.00 35.30 ? 136 LYS B CE  1 
ATOM   2110 N  NZ  . LYS B 1 136 ? 17.559 8.147   24.284  1.00 38.68 ? 136 LYS B NZ  1 
ATOM   2111 N  N   . THR B 1 137 ? 22.903 4.977   27.147  1.00 20.92 ? 137 THR B N   1 
ATOM   2112 C  CA  . THR B 1 137 ? 24.319 5.298   27.027  1.00 20.04 ? 137 THR B CA  1 
ATOM   2113 C  C   . THR B 1 137 ? 25.089 5.246   28.340  1.00 20.03 ? 137 THR B C   1 
ATOM   2114 O  O   . THR B 1 137 ? 26.299 5.457   28.351  1.00 18.99 ? 137 THR B O   1 
ATOM   2115 C  CB  . THR B 1 137 ? 24.493 6.717   26.487  1.00 21.27 ? 137 THR B CB  1 
ATOM   2116 O  OG1 . THR B 1 137 ? 23.960 7.643   27.445  1.00 20.15 ? 137 THR B OG1 1 
ATOM   2117 C  CG2 . THR B 1 137 ? 23.754 6.884   25.167  1.00 22.89 ? 137 THR B CG2 1 
ATOM   2118 N  N   . GLY B 1 138 ? 24.396 4.973   29.440  1.00 19.00 ? 138 GLY B N   1 
ATOM   2119 C  CA  . GLY B 1 138 ? 25.063 4.966   30.728  1.00 18.93 ? 138 GLY B CA  1 
ATOM   2120 C  C   . GLY B 1 138 ? 25.446 6.388   31.112  1.00 18.09 ? 138 GLY B C   1 
ATOM   2121 O  O   . GLY B 1 138 ? 26.213 6.600   32.055  1.00 18.71 ? 138 GLY B O   1 
ATOM   2122 N  N   . ASN B 1 139 ? 24.922 7.365   30.371  1.00 17.57 ? 139 ASN B N   1 
ATOM   2123 C  CA  . ASN B 1 139 ? 25.201 8.781   30.629  1.00 18.45 ? 139 ASN B CA  1 
ATOM   2124 C  C   . ASN B 1 139 ? 26.680 9.137   30.463  1.00 19.23 ? 139 ASN B C   1 
ATOM   2125 O  O   . ASN B 1 139 ? 27.166 10.085  31.081  1.00 19.57 ? 139 ASN B O   1 
ATOM   2126 C  CB  . ASN B 1 139 ? 24.744 9.166   32.046  1.00 20.04 ? 139 ASN B CB  1 
ATOM   2127 C  CG  . ASN B 1 139 ? 23.236 9.330   32.155  1.00 21.32 ? 139 ASN B CG  1 
ATOM   2128 O  OD1 . ASN B 1 139 ? 22.645 10.174  31.481  1.00 21.63 ? 139 ASN B OD1 1 
ATOM   2129 N  ND2 . ASN B 1 139 ? 22.609 8.528   33.008  1.00 20.67 ? 139 ASN B ND2 1 
ATOM   2130 N  N   . ALA B 1 140 ? 27.390 8.396   29.615  1.00 19.48 ? 140 ALA B N   1 
ATOM   2131 C  CA  . ALA B 1 140 ? 28.823 8.634   29.404  1.00 19.94 ? 140 ALA B CA  1 
ATOM   2132 C  C   . ALA B 1 140 ? 29.172 9.931   28.673  1.00 20.77 ? 140 ALA B C   1 
ATOM   2133 O  O   . ALA B 1 140 ? 30.344 10.298  28.591  1.00 21.38 ? 140 ALA B O   1 
ATOM   2134 C  CB  . ALA B 1 140 ? 29.448 7.448   28.683  1.00 19.15 ? 140 ALA B CB  1 
ATOM   2135 N  N   . GLY B 1 141 ? 28.164 10.617  28.140  1.00 20.83 ? 141 GLY B N   1 
ATOM   2136 C  CA  . GLY B 1 141 ? 28.412 11.879  27.463  1.00 20.22 ? 141 GLY B CA  1 
ATOM   2137 C  C   . GLY B 1 141 ? 29.078 11.844  26.099  1.00 21.56 ? 141 GLY B C   1 
ATOM   2138 O  O   . GLY B 1 141 ? 28.958 10.870  25.348  1.00 18.64 ? 141 GLY B O   1 
ATOM   2139 N  N   . SER B 1 142 ? 29.799 12.921  25.789  1.00 22.25 ? 142 SER B N   1 
ATOM   2140 C  CA  . SER B 1 142 ? 30.467 13.060  24.501  1.00 23.10 ? 142 SER B CA  1 
ATOM   2141 C  C   . SER B 1 142 ? 31.570 12.045  24.245  1.00 23.42 ? 142 SER B C   1 
ATOM   2142 O  O   . SER B 1 142 ? 32.046 11.361  25.156  1.00 22.04 ? 142 SER B O   1 
ATOM   2143 C  CB  . SER B 1 142 ? 31.018 14.486  24.329  1.00 22.53 ? 142 SER B CB  1 
ATOM   2144 O  OG  . SER B 1 142 ? 32.141 14.724  25.157  1.00 26.23 ? 142 SER B OG  1 
ATOM   2145 N  N   . ARG B 1 143 ? 31.970 11.966  22.981  1.00 22.91 ? 143 ARG B N   1 
ATOM   2146 C  CA  . ARG B 1 143 ? 32.997 11.034  22.535  1.00 23.09 ? 143 ARG B CA  1 
ATOM   2147 C  C   . ARG B 1 143 ? 34.328 11.773  22.388  1.00 22.85 ? 143 ARG B C   1 
ATOM   2148 O  O   . ARG B 1 143 ? 34.455 12.692  21.572  1.00 23.45 ? 143 ARG B O   1 
ATOM   2149 C  CB  . ARG B 1 143 ? 32.521 10.424  21.216  1.00 23.02 ? 143 ARG B CB  1 
ATOM   2150 C  CG  . ARG B 1 143 ? 31.068 9.976   21.339  1.00 22.11 ? 143 ARG B CG  1 
ATOM   2151 C  CD  . ARG B 1 143 ? 30.421 9.500   20.052  1.00 21.25 ? 143 ARG B CD  1 
ATOM   2152 N  NE  . ARG B 1 143 ? 29.028 9.139   20.315  1.00 23.11 ? 143 ARG B NE  1 
ATOM   2153 C  CZ  . ARG B 1 143 ? 28.264 8.404   19.512  1.00 23.93 ? 143 ARG B CZ  1 
ATOM   2154 N  NH1 . ARG B 1 143 ? 27.010 8.138   19.858  1.00 24.99 ? 143 ARG B NH1 1 
ATOM   2155 N  NH2 . ARG B 1 143 ? 28.745 7.931   18.370  1.00 23.45 ? 143 ARG B NH2 1 
ATOM   2156 N  N   . LEU B 1 144 ? 35.308 11.382  23.199  1.00 21.26 ? 144 LEU B N   1 
ATOM   2157 C  CA  . LEU B 1 144 ? 36.621 12.023  23.186  1.00 21.34 ? 144 LEU B CA  1 
ATOM   2158 C  C   . LEU B 1 144 ? 37.514 11.518  22.067  1.00 21.80 ? 144 LEU B C   1 
ATOM   2159 O  O   . LEU B 1 144 ? 38.238 12.291  21.441  1.00 23.01 ? 144 LEU B O   1 
ATOM   2160 C  CB  . LEU B 1 144 ? 37.323 11.816  24.529  1.00 22.68 ? 144 LEU B CB  1 
ATOM   2161 C  CG  . LEU B 1 144 ? 36.588 12.329  25.771  1.00 23.10 ? 144 LEU B CG  1 
ATOM   2162 C  CD1 . LEU B 1 144 ? 37.499 12.183  26.977  1.00 24.39 ? 144 LEU B CD1 1 
ATOM   2163 C  CD2 . LEU B 1 144 ? 36.191 13.786  25.591  1.00 25.17 ? 144 LEU B CD2 1 
ATOM   2164 N  N   . ALA B 1 145 ? 37.474 10.213  21.833  1.00 21.53 ? 145 ALA B N   1 
ATOM   2165 C  CA  . ALA B 1 145 ? 38.269 9.599   20.781  1.00 20.91 ? 145 ALA B CA  1 
ATOM   2166 C  C   . ALA B 1 145 ? 37.607 8.305   20.348  1.00 20.18 ? 145 ALA B C   1 
ATOM   2167 O  O   . ALA B 1 145 ? 36.856 7.691   21.108  1.00 19.91 ? 145 ALA B O   1 
ATOM   2168 C  CB  . ALA B 1 145 ? 39.680 9.320   21.273  1.00 19.30 ? 145 ALA B CB  1 
ATOM   2169 N  N   . CYS B 1 146 ? 37.884 7.894   19.119  1.00 21.31 ? 146 CYS B N   1 
ATOM   2170 C  CA  . CYS B 1 146 ? 37.309 6.668   18.589  1.00 20.92 ? 146 CYS B CA  1 
ATOM   2171 C  C   . CYS B 1 146 ? 38.146 6.150   17.431  1.00 21.31 ? 146 CYS B C   1 
ATOM   2172 O  O   . CYS B 1 146 ? 39.001 6.859   16.896  1.00 19.99 ? 146 CYS B O   1 
ATOM   2173 C  CB  . CYS B 1 146 ? 35.880 6.919   18.107  1.00 23.24 ? 146 CYS B CB  1 
ATOM   2174 S  SG  . CYS B 1 146 ? 35.788 8.181   16.803  1.00 25.41 ? 146 CYS B SG  1 
ATOM   2175 N  N   . GLY B 1 147 ? 37.897 4.902   17.056  1.00 20.03 ? 147 GLY B N   1 
ATOM   2176 C  CA  . GLY B 1 147 ? 38.626 4.302   15.959  1.00 20.49 ? 147 GLY B CA  1 
ATOM   2177 C  C   . GLY B 1 147 ? 37.901 3.075   15.455  1.00 21.60 ? 147 GLY B C   1 
ATOM   2178 O  O   . GLY B 1 147 ? 37.286 2.351   16.240  1.00 18.86 ? 147 GLY B O   1 
ATOM   2179 N  N   . VAL B 1 148 ? 37.961 2.842   14.148  1.00 20.12 ? 148 VAL B N   1 
ATOM   2180 C  CA  . VAL B 1 148 ? 37.310 1.678   13.568  1.00 19.74 ? 148 VAL B CA  1 
ATOM   2181 C  C   . VAL B 1 148 ? 38.112 0.440   13.926  1.00 20.26 ? 148 VAL B C   1 
ATOM   2182 O  O   . VAL B 1 148 ? 39.344 0.446   13.868  1.00 19.96 ? 148 VAL B O   1 
ATOM   2183 C  CB  . VAL B 1 148 ? 37.218 1.787   12.038  1.00 18.91 ? 148 VAL B CB  1 
ATOM   2184 C  CG1 . VAL B 1 148 ? 36.503 0.558   11.472  1.00 18.79 ? 148 VAL B CG1 1 
ATOM   2185 C  CG2 . VAL B 1 148 ? 36.479 3.062   11.661  1.00 19.07 ? 148 VAL B CG2 1 
ATOM   2186 N  N   . ILE B 1 149 ? 37.409 -0.619  14.305  1.00 19.25 ? 149 ILE B N   1 
ATOM   2187 C  CA  . ILE B 1 149 ? 38.053 -1.868  14.678  1.00 18.79 ? 149 ILE B CA  1 
ATOM   2188 C  C   . ILE B 1 149 ? 38.356 -2.668  13.415  1.00 18.89 ? 149 ILE B C   1 
ATOM   2189 O  O   . ILE B 1 149 ? 37.448 -3.075  12.689  1.00 17.79 ? 149 ILE B O   1 
ATOM   2190 C  CB  . ILE B 1 149 ? 37.139 -2.661  15.621  1.00 18.97 ? 149 ILE B CB  1 
ATOM   2191 C  CG1 . ILE B 1 149 ? 36.866 -1.812  16.869  1.00 16.82 ? 149 ILE B CG1 1 
ATOM   2192 C  CG2 . ILE B 1 149 ? 37.775 -4.005  15.978  1.00 17.16 ? 149 ILE B CG2 1 
ATOM   2193 C  CD1 . ILE B 1 149 ? 35.697 -2.303  17.722  1.00 20.91 ? 149 ILE B CD1 1 
ATOM   2194 N  N   . GLY B 1 150 ? 39.641 -2.884  13.154  1.00 18.29 ? 150 GLY B N   1 
ATOM   2195 C  CA  . GLY B 1 150 ? 40.029 -3.599  11.952  1.00 18.03 ? 150 GLY B CA  1 
ATOM   2196 C  C   . GLY B 1 150 ? 40.744 -4.910  12.194  1.00 18.92 ? 150 GLY B C   1 
ATOM   2197 O  O   . GLY B 1 150 ? 41.241 -5.158  13.287  1.00 18.11 ? 150 GLY B O   1 
ATOM   2198 N  N   . ILE B 1 151 ? 40.788 -5.748  11.161  1.00 18.45 ? 151 ILE B N   1 
ATOM   2199 C  CA  . ILE B 1 151 ? 41.449 -7.048  11.234  1.00 19.11 ? 151 ILE B CA  1 
ATOM   2200 C  C   . ILE B 1 151 ? 42.954 -6.821  11.311  1.00 19.44 ? 151 ILE B C   1 
ATOM   2201 O  O   . ILE B 1 151 ? 43.518 -6.096  10.496  1.00 20.47 ? 151 ILE B O   1 
ATOM   2202 C  CB  . ILE B 1 151 ? 41.116 -7.891  9.990   1.00 18.45 ? 151 ILE B CB  1 
ATOM   2203 C  CG1 . ILE B 1 151 ? 39.601 -8.084  9.901   1.00 19.25 ? 151 ILE B CG1 1 
ATOM   2204 C  CG2 . ILE B 1 151 ? 41.823 -9.242  10.057  1.00 20.77 ? 151 ILE B CG2 1 
ATOM   2205 C  CD1 . ILE B 1 151 ? 39.141 -8.789  8.652   1.00 19.25 ? 151 ILE B CD1 1 
ATOM   2206 N  N   . ALA B 1 152 ? 43.605 -7.444  12.289  1.00 19.01 ? 152 ALA B N   1 
ATOM   2207 C  CA  . ALA B 1 152 ? 45.041 -7.270  12.468  1.00 20.11 ? 152 ALA B CA  1 
ATOM   2208 C  C   . ALA B 1 152 ? 45.824 -8.559  12.262  1.00 23.16 ? 152 ALA B C   1 
ATOM   2209 O  O   . ALA B 1 152 ? 47.057 -8.558  12.269  1.00 22.59 ? 152 ALA B O   1 
ATOM   2210 C  CB  . ALA B 1 152 ? 45.317 -6.711  13.849  1.00 19.87 ? 152 ALA B CB  1 
ATOM   2211 N  N   . GLN B 1 153 ? 45.095 -9.657  12.100  1.00 26.30 ? 153 GLN B N   1 
ATOM   2212 C  CA  . GLN B 1 153 ? 45.689 -10.966 11.872  1.00 32.08 ? 153 GLN B CA  1 
ATOM   2213 C  C   . GLN B 1 153 ? 44.570 -11.983 11.663  1.00 33.65 ? 153 GLN B C   1 
ATOM   2214 O  O   . GLN B 1 153 ? 43.477 -11.795 12.246  1.00 34.34 ? 153 GLN B O   1 
ATOM   2215 C  CB  . GLN B 1 153 ? 46.538 -11.389 13.072  1.00 33.75 ? 153 GLN B CB  1 
ATOM   2216 C  CG  . GLN B 1 153 ? 47.276 -12.696 12.860  1.00 37.22 ? 153 GLN B CG  1 
ATOM   2217 C  CD  . GLN B 1 153 ? 47.842 -13.253 14.146  1.00 39.71 ? 153 GLN B CD  1 
ATOM   2218 O  OE1 . GLN B 1 153 ? 47.096 -13.650 15.040  1.00 41.78 ? 153 GLN B OE1 1 
ATOM   2219 N  NE2 . GLN B 1 153 ? 49.165 -13.278 14.252  1.00 41.01 ? 153 GLN B NE2 1 
ATOM   2220 O  OXT . GLN B 1 153 ? 44.806 -12.967 10.935  1.00 35.51 ? 153 GLN B OXT 1 
HETATM 2221 CU CU  . CU1 C 2 .   ? 47.312 -0.405  -2.539  1.00 22.88 ? 200 CU1 A CU  1 
HETATM 2222 ZN ZN  . ZN  D 3 .   ? 47.196 -6.137  -6.081  1.00 18.83 ? 201 ZN  A ZN  1 
HETATM 2223 S  S   . SO4 E 4 .   ? 42.471 -12.151 -17.761 0.77 67.58 ? 600 SO4 A S   1 
HETATM 2224 O  O1  . SO4 E 4 .   ? 43.515 -12.933 -17.065 0.77 66.09 ? 600 SO4 A O1  1 
HETATM 2225 O  O2  . SO4 E 4 .   ? 41.374 -11.843 -16.831 0.77 66.28 ? 600 SO4 A O2  1 
HETATM 2226 O  O3  . SO4 E 4 .   ? 41.924 -12.933 -18.886 0.77 66.12 ? 600 SO4 A O3  1 
HETATM 2227 O  O4  . SO4 E 4 .   ? 43.057 -10.894 -18.265 0.77 66.23 ? 600 SO4 A O4  1 
HETATM 2228 CU CU  . CU1 F 2 .   ? 29.968 4.662   23.769  1.00 26.80 ? 200 CU1 B CU  1 
HETATM 2229 ZN ZN  . ZN  G 3 .   ? 25.435 0.406   25.934  1.00 20.05 ? 201 ZN  B ZN  1 
HETATM 2230 O  O   . HOH H 5 .   ? 43.716 2.186   -15.399 1.00 14.32 ? 302 HOH A O   1 
HETATM 2231 O  O   . HOH H 5 .   ? 52.582 0.249   -3.210  1.00 19.43 ? 304 HOH A O   1 
HETATM 2232 O  O   . HOH H 5 .   ? 38.612 0.839   -11.178 1.00 19.73 ? 305 HOH A O   1 
HETATM 2233 O  O   . HOH H 5 .   ? 40.149 4.694   9.700   1.00 14.38 ? 306 HOH A O   1 
HETATM 2234 O  O   . HOH H 5 .   ? 40.915 1.226   -12.903 1.00 18.53 ? 308 HOH A O   1 
HETATM 2235 O  O   . HOH H 5 .   ? 43.630 0.154   13.100  1.00 18.50 ? 310 HOH A O   1 
HETATM 2236 O  O   . HOH H 5 .   ? 54.559 -0.253  -5.110  1.00 18.92 ? 311 HOH A O   1 
HETATM 2237 O  O   . HOH H 5 .   ? 51.044 11.666  -6.665  1.00 28.56 ? 312 HOH A O   1 
HETATM 2238 O  O   . HOH H 5 .   ? 43.013 -12.985 -3.999  1.00 21.86 ? 313 HOH A O   1 
HETATM 2239 O  O   . HOH H 5 .   ? 38.021 8.356   -10.598 1.00 24.36 ? 318 HOH A O   1 
HETATM 2240 O  O   . HOH H 5 .   ? 37.505 4.801   7.934   1.00 16.76 ? 319 HOH A O   1 
HETATM 2241 O  O   . HOH H 5 .   ? 40.623 8.380   -16.585 1.00 25.24 ? 320 HOH A O   1 
HETATM 2242 O  O   . HOH H 5 .   ? 44.589 -2.966  -9.490  1.00 21.09 ? 322 HOH A O   1 
HETATM 2243 O  O   . HOH H 5 .   ? 52.047 7.761   -12.028 1.00 27.22 ? 323 HOH A O   1 
HETATM 2244 O  O   . HOH H 5 .   ? 48.679 12.562  -5.650  1.00 29.64 ? 325 HOH A O   1 
HETATM 2245 O  O   . HOH H 5 .   ? 35.761 -3.309  -10.967 1.00 24.21 ? 328 HOH A O   1 
HETATM 2246 O  O   . HOH H 5 .   ? 40.211 5.918   -13.327 1.00 27.02 ? 329 HOH A O   1 
HETATM 2247 O  O   . HOH H 5 .   ? 47.815 9.707   -15.628 1.00 23.33 ? 331 HOH A O   1 
HETATM 2248 O  O   . HOH H 5 .   ? 48.787 -6.293  11.670  1.00 23.20 ? 333 HOH A O   1 
HETATM 2249 O  O   . HOH H 5 .   ? 56.569 -2.945  -2.874  1.00 27.71 ? 334 HOH A O   1 
HETATM 2250 O  O   . HOH H 5 .   ? 20.789 -10.812 -0.472  1.00 25.33 ? 335 HOH A O   1 
HETATM 2251 O  O   . HOH H 5 .   ? 45.414 -11.383 1.978   1.00 23.81 ? 338 HOH A O   1 
HETATM 2252 O  O   . HOH H 5 .   ? 36.794 -1.055  -12.069 1.00 23.47 ? 341 HOH A O   1 
HETATM 2253 O  O   . HOH H 5 .   ? 35.602 -8.957  7.670   1.00 23.55 ? 342 HOH A O   1 
HETATM 2254 O  O   . HOH H 5 .   ? 52.783 -4.517  1.839   1.00 26.41 ? 343 HOH A O   1 
HETATM 2255 O  O   . HOH H 5 .   ? 30.685 -9.697  -4.082  1.00 24.66 ? 347 HOH A O   1 
HETATM 2256 O  O   . HOH H 5 .   ? 50.668 -1.686  -2.501  1.00 24.97 ? 350 HOH A O   1 
HETATM 2257 O  O   . HOH H 5 .   ? 51.131 -11.071 -5.507  1.00 23.97 ? 351 HOH A O   1 
HETATM 2258 O  O   . HOH H 5 .   ? 57.331 -6.642  -3.486  1.00 28.27 ? 356 HOH A O   1 
HETATM 2259 O  O   . HOH H 5 .   ? 49.622 8.999   -12.811 1.00 21.19 ? 359 HOH A O   1 
HETATM 2260 O  O   . HOH H 5 .   ? 46.209 -5.940  -16.717 1.00 28.54 ? 360 HOH A O   1 
HETATM 2261 O  O   . HOH H 5 .   ? 25.273 -2.016  6.474   1.00 31.37 ? 361 HOH A O   1 
HETATM 2262 O  O   . HOH H 5 .   ? 55.589 6.698   -4.630  1.00 28.47 ? 363 HOH A O   1 
HETATM 2263 O  O   . HOH H 5 .   ? 42.244 18.982  -4.426  1.00 30.86 ? 365 HOH A O   1 
HETATM 2264 O  O   . HOH H 5 .   ? 41.674 -13.130 -6.452  1.00 24.46 ? 366 HOH A O   1 
HETATM 2265 O  O   . HOH H 5 .   ? 37.288 -11.316 4.518   1.00 31.84 ? 369 HOH A O   1 
HETATM 2266 O  O   . HOH H 5 .   ? 53.078 -0.578  -0.598  1.00 31.63 ? 370 HOH A O   1 
HETATM 2267 O  O   . HOH H 5 .   ? 24.736 -6.340  -4.910  1.00 29.40 ? 371 HOH A O   1 
HETATM 2268 O  O   . HOH H 5 .   ? 48.387 2.303   -15.466 1.00 33.72 ? 373 HOH A O   1 
HETATM 2269 O  O   . HOH H 5 .   ? 44.144 1.524   8.147   1.00 31.11 ? 374 HOH A O   1 
HETATM 2270 O  O   . HOH H 5 .   ? 47.673 18.324  -9.920  1.00 27.91 ? 375 HOH A O   1 
HETATM 2271 O  O   . HOH H 5 .   ? 38.305 3.565   -11.480 1.00 26.92 ? 377 HOH A O   1 
HETATM 2272 O  O   . HOH H 5 .   ? 49.658 7.260   7.257   1.00 27.87 ? 378 HOH A O   1 
HETATM 2273 O  O   . HOH H 5 .   ? 39.189 -12.368 -10.335 1.00 34.94 ? 379 HOH A O   1 
HETATM 2274 O  O   . HOH H 5 .   ? 48.248 5.955   13.549  1.00 34.42 ? 381 HOH A O   1 
HETATM 2275 O  O   . HOH H 5 .   ? 48.325 -5.008  15.327  1.00 29.34 ? 383 HOH A O   1 
HETATM 2276 O  O   . HOH H 5 .   ? 40.502 17.957  -15.311 1.00 32.66 ? 385 HOH A O   1 
HETATM 2277 O  O   . HOH H 5 .   ? 28.921 4.987   3.153   1.00 29.68 ? 386 HOH A O   1 
HETATM 2278 O  O   . HOH H 5 .   ? 46.793 1.336   7.917   1.00 27.48 ? 387 HOH A O   1 
HETATM 2279 O  O   . HOH H 5 .   ? 25.447 -3.432  -5.035  1.00 41.04 ? 388 HOH A O   1 
HETATM 2280 O  O   . HOH H 5 .   ? 43.571 -11.738 6.419   1.00 26.93 ? 390 HOH A O   1 
HETATM 2281 O  O   . HOH H 5 .   ? 32.349 -9.121  6.969   1.00 29.47 ? 392 HOH A O   1 
HETATM 2282 O  O   . HOH H 5 .   ? 44.443 6.622   8.299   1.00 25.17 ? 393 HOH A O   1 
HETATM 2283 O  O   . HOH H 5 .   ? 49.064 14.331  -3.561  1.00 39.14 ? 397 HOH A O   1 
HETATM 2284 O  O   . HOH H 5 .   ? 40.935 7.407   8.664   1.00 26.98 ? 398 HOH A O   1 
HETATM 2285 O  O   . HOH H 5 .   ? 29.786 -10.817 -6.979  1.00 31.48 ? 399 HOH A O   1 
HETATM 2286 O  O   . HOH H 5 .   ? 45.335 13.368  4.994   1.00 29.17 ? 400 HOH A O   1 
HETATM 2287 O  O   . HOH H 5 .   ? 50.319 -9.213  -15.957 1.00 34.75 ? 404 HOH A O   1 
HETATM 2288 O  O   . HOH H 5 .   ? 38.117 -10.673 -12.282 1.00 35.32 ? 405 HOH A O   1 
HETATM 2289 O  O   . HOH H 5 .   ? 37.596 12.395  -11.342 1.00 39.82 ? 406 HOH A O   1 
HETATM 2290 O  O   . HOH H 5 .   ? 25.005 -11.811 3.459   1.00 30.68 ? 408 HOH A O   1 
HETATM 2291 O  O   . HOH H 5 .   ? 50.447 10.152  3.767   1.00 31.09 ? 412 HOH A O   1 
HETATM 2292 O  O   . HOH H 5 .   ? 31.901 12.278  -6.377  1.00 36.30 ? 413 HOH A O   1 
HETATM 2293 O  O   . HOH H 5 .   ? 31.471 9.747   -7.655  1.00 30.08 ? 414 HOH A O   1 
HETATM 2294 O  O   . HOH H 5 .   ? 48.487 -1.883  -23.774 1.00 30.23 ? 419 HOH A O   1 
HETATM 2295 O  O   . HOH H 5 .   ? 42.572 -19.233 -7.392  1.00 51.13 ? 421 HOH A O   1 
HETATM 2296 O  O   . HOH H 5 .   ? 55.881 -8.599  -13.398 1.00 42.72 ? 422 HOH A O   1 
HETATM 2297 O  O   . HOH H 5 .   ? 32.747 -13.111 -0.133  1.00 32.56 ? 426 HOH A O   1 
HETATM 2298 O  O   . HOH H 5 .   ? 34.223 -7.011  -11.107 1.00 32.30 ? 427 HOH A O   1 
HETATM 2299 O  O   . HOH H 5 .   ? 25.827 -14.520 -4.204  1.00 40.55 ? 429 HOH A O   1 
HETATM 2300 O  O   . HOH H 5 .   ? 52.286 7.276   8.527   1.00 40.41 ? 434 HOH A O   1 
HETATM 2301 O  O   . HOH H 5 .   ? 27.465 3.254   1.698   1.00 42.86 ? 435 HOH A O   1 
HETATM 2302 O  O   . HOH H 5 .   ? 18.002 -10.342 -5.161  1.00 39.15 ? 437 HOH A O   1 
HETATM 2303 O  O   . HOH H 5 .   ? 20.080 2.292   11.872  1.00 47.69 ? 439 HOH A O   1 
HETATM 2304 O  O   . HOH H 5 .   ? 50.222 -11.679 -2.008  1.00 38.05 ? 441 HOH A O   1 
HETATM 2305 O  O   . HOH H 5 .   ? 54.957 0.853   -14.499 1.00 42.02 ? 443 HOH A O   1 
HETATM 2306 O  O   . HOH H 5 .   ? 48.470 12.573  2.454   1.00 36.93 ? 444 HOH A O   1 
HETATM 2307 O  O   . HOH H 5 .   ? 28.176 6.943   -11.879 1.00 48.83 ? 451 HOH A O   1 
HETATM 2308 O  O   . HOH H 5 .   ? 48.166 -11.649 1.766   1.00 40.81 ? 453 HOH A O   1 
HETATM 2309 O  O   . HOH H 5 .   ? 54.422 -7.364  -16.062 1.00 31.26 ? 454 HOH A O   1 
HETATM 2310 O  O   . HOH H 5 .   ? 50.763 15.076  9.224   1.00 48.08 ? 455 HOH A O   1 
HETATM 2311 O  O   . HOH H 5 .   ? 48.549 -17.216 -9.450  1.00 41.99 ? 457 HOH A O   1 
HETATM 2312 O  O   . HOH H 5 .   ? 34.932 2.915   -12.565 1.00 46.38 ? 459 HOH A O   1 
HETATM 2313 O  O   . HOH H 5 .   ? 28.644 -8.921  -11.383 1.00 32.92 ? 463 HOH A O   1 
HETATM 2314 O  O   . HOH H 5 .   ? 49.944 -11.241 4.560   1.00 42.73 ? 464 HOH A O   1 
HETATM 2315 O  O   . HOH H 5 .   ? 48.899 -10.022 -0.612  1.00 36.10 ? 467 HOH A O   1 
HETATM 2316 O  O   . HOH H 5 .   ? 43.562 6.816   12.732  1.00 40.35 ? 469 HOH A O   1 
HETATM 2317 O  O   . HOH H 5 .   ? 56.808 -10.978 -10.035 1.00 44.81 ? 471 HOH A O   1 
HETATM 2318 O  O   . HOH H 5 .   ? 49.015 -0.202  -17.470 1.00 39.11 ? 476 HOH A O   1 
HETATM 2319 O  O   . HOH H 5 .   ? 41.268 14.725  6.893   1.00 48.89 ? 478 HOH A O   1 
HETATM 2320 O  O   . HOH H 5 .   ? 39.698 12.410  6.002   1.00 29.56 ? 481 HOH A O   1 
HETATM 2321 O  O   . HOH H 5 .   ? 53.178 11.063  -12.402 1.00 39.91 ? 482 HOH A O   1 
HETATM 2322 O  O   . HOH H 5 .   ? 43.370 3.961   8.676   1.00 24.39 ? 483 HOH A O   1 
HETATM 2323 O  O   . HOH H 5 .   ? 53.964 4.364   2.107   1.00 11.35 ? 484 HOH A O   1 
HETATM 2324 O  O   . HOH H 5 .   ? 54.361 -0.281  3.636   1.00 26.77 ? 486 HOH A O   1 
HETATM 2325 O  O   . HOH H 5 .   ? 50.507 -6.492  -2.502  1.00 26.25 ? 487 HOH A O   1 
HETATM 2326 O  O   . HOH H 5 .   ? 43.744 -13.431 3.256   1.00 37.73 ? 488 HOH A O   1 
HETATM 2327 O  O   . HOH H 5 .   ? 36.817 -14.428 -6.986  1.00 36.57 ? 489 HOH A O   1 
HETATM 2328 O  O   . HOH H 5 .   ? 41.645 -3.625  -15.427 1.00 19.25 ? 490 HOH A O   1 
HETATM 2329 O  O   . HOH H 5 .   ? 43.519 0.433   -18.370 1.00 34.75 ? 491 HOH A O   1 
HETATM 2330 O  O   . HOH H 5 .   ? 40.965 3.369   -14.706 1.00 27.01 ? 492 HOH A O   1 
HETATM 2331 O  O   . HOH H 5 .   ? 37.174 3.475   -13.927 1.00 34.65 ? 493 HOH A O   1 
HETATM 2332 O  O   . HOH H 5 .   ? 34.010 -0.019  -12.461 1.00 30.60 ? 494 HOH A O   1 
HETATM 2333 O  O   . HOH H 5 .   ? 38.458 6.887   -17.204 1.00 27.64 ? 495 HOH A O   1 
HETATM 2334 O  O   . HOH H 5 .   ? 39.559 10.753  -17.414 1.00 32.30 ? 496 HOH A O   1 
HETATM 2335 O  O   . HOH H 5 .   ? 36.520 5.830   -10.468 1.00 14.13 ? 498 HOH A O   1 
HETATM 2336 O  O   . HOH H 5 .   ? 27.579 -9.785  0.483   1.00 38.99 ? 499 HOH A O   1 
HETATM 2337 O  O   . HOH H 5 .   ? 39.855 -12.745 8.334   1.00 41.76 ? 500 HOH A O   1 
HETATM 2338 O  O   . HOH H 5 .   ? 51.108 -3.861  -1.147  1.00 26.96 ? 506 HOH A O   1 
HETATM 2339 O  O   . HOH H 5 .   ? 50.854 3.826   -15.844 1.00 40.21 ? 507 HOH A O   1 
HETATM 2340 O  O   . HOH H 5 .   ? 39.106 -13.300 -7.968  1.00 42.01 ? 508 HOH A O   1 
HETATM 2341 O  O   . HOH H 5 .   ? 50.849 13.228  0.887   1.00 25.88 ? 509 HOH A O   1 
HETATM 2342 O  O   . HOH H 5 .   ? 28.447 -4.765  -12.000 1.00 34.22 ? 510 HOH A O   1 
HETATM 2343 O  O   . HOH H 5 .   ? 30.566 -7.465  8.404   1.00 38.67 ? 511 HOH A O   1 
HETATM 2344 O  O   . HOH H 5 .   ? 47.431 7.322   9.069   1.00 37.96 ? 513 HOH A O   1 
HETATM 2345 O  O   . HOH H 5 .   ? 44.872 10.637  -16.156 1.00 29.17 ? 514 HOH A O   1 
HETATM 2346 O  O   . HOH H 5 .   ? 37.732 5.937   -14.545 1.00 38.61 ? 515 HOH A O   1 
HETATM 2347 O  O   . HOH H 5 .   ? 36.392 8.332   -18.122 1.00 35.74 ? 516 HOH A O   1 
HETATM 2348 O  O   . HOH H 5 .   ? 50.272 -5.478  9.541   1.00 21.17 ? 518 HOH A O   1 
HETATM 2349 O  O   . HOH H 5 .   ? 51.464 -6.841  7.130   1.00 18.69 ? 519 HOH A O   1 
HETATM 2350 O  O   . HOH H 5 .   ? 52.202 4.791   4.697   1.00 26.81 ? 520 HOH A O   1 
HETATM 2351 O  O   . HOH H 5 .   ? 54.426 1.442   1.199   1.00 35.52 ? 521 HOH A O   1 
HETATM 2352 O  O   . HOH H 5 .   ? 39.058 -17.354 -0.122  1.00 43.93 ? 522 HOH A O   1 
HETATM 2353 O  O   . HOH H 5 .   ? 39.051 -14.654 3.795   1.00 50.06 ? 523 HOH A O   1 
HETATM 2354 O  O   . HOH I 5 .   ? 22.106 -8.564  20.837  1.00 17.21 ? 300 HOH B O   1 
HETATM 2355 O  O   . HOH I 5 .   ? 20.658 7.794   39.699  1.00 21.64 ? 301 HOH B O   1 
HETATM 2356 O  O   . HOH I 5 .   ? 29.614 -4.508  35.179  1.00 21.97 ? 303 HOH B O   1 
HETATM 2357 O  O   . HOH I 5 .   ? 41.375 0.766   32.635  1.00 26.63 ? 307 HOH B O   1 
HETATM 2358 O  O   . HOH I 5 .   ? 29.135 -0.530  29.829  1.00 18.70 ? 309 HOH B O   1 
HETATM 2359 O  O   . HOH I 5 .   ? 32.237 11.343  35.204  1.00 21.93 ? 314 HOH B O   1 
HETATM 2360 O  O   . HOH I 5 .   ? 25.115 10.177  27.468  1.00 19.60 ? 315 HOH B O   1 
HETATM 2361 O  O   . HOH I 5 .   ? 33.815 -1.420  34.130  1.00 21.06 ? 316 HOH B O   1 
HETATM 2362 O  O   . HOH I 5 .   ? 35.486 8.947   38.069  1.00 20.77 ? 317 HOH B O   1 
HETATM 2363 O  O   . HOH I 5 .   ? 33.190 1.159   36.371  1.00 23.18 ? 321 HOH B O   1 
HETATM 2364 O  O   . HOH I 5 .   ? 23.522 -2.256  16.751  1.00 25.19 ? 324 HOH B O   1 
HETATM 2365 O  O   . HOH I 5 .   ? 41.578 2.007   13.831  1.00 18.31 ? 326 HOH B O   1 
HETATM 2366 O  O   . HOH I 5 .   ? 27.073 8.838   25.436  1.00 25.89 ? 327 HOH B O   1 
HETATM 2367 O  O   . HOH I 5 .   ? 21.332 -3.374  32.468  1.00 24.63 ? 330 HOH B O   1 
HETATM 2368 O  O   . HOH I 5 .   ? 23.048 -6.219  22.180  1.00 24.24 ? 332 HOH B O   1 
HETATM 2369 O  O   . HOH I 5 .   ? 40.413 14.103  22.245  1.00 35.61 ? 336 HOH B O   1 
HETATM 2370 O  O   . HOH I 5 .   ? 23.514 3.683   22.841  1.00 22.61 ? 337 HOH B O   1 
HETATM 2371 O  O   . HOH I 5 .   ? 33.300 -9.947  11.292  1.00 28.53 ? 339 HOH B O   1 
HETATM 2372 O  O   . HOH I 5 .   ? 34.737 10.246  35.747  1.00 23.15 ? 340 HOH B O   1 
HETATM 2373 O  O   . HOH I 5 .   ? 33.414 -14.023 23.177  1.00 21.04 ? 344 HOH B O   1 
HETATM 2374 O  O   . HOH I 5 .   ? 34.198 -7.720  30.212  1.00 28.59 ? 345 HOH B O   1 
HETATM 2375 O  O   . HOH I 5 .   ? 19.655 -0.130  31.779  1.00 21.53 ? 346 HOH B O   1 
HETATM 2376 O  O   . HOH I 5 .   ? 23.970 12.064  30.194  1.00 27.60 ? 348 HOH B O   1 
HETATM 2377 O  O   . HOH I 5 .   ? 19.370 1.021   24.364  1.00 23.40 ? 349 HOH B O   1 
HETATM 2378 O  O   . HOH I 5 .   ? 30.275 4.436   37.346  1.00 26.21 ? 352 HOH B O   1 
HETATM 2379 O  O   . HOH I 5 .   ? 22.480 -12.830 20.438  1.00 27.08 ? 353 HOH B O   1 
HETATM 2380 O  O   . HOH I 5 .   ? 31.890 -10.734 29.778  1.00 26.85 ? 354 HOH B O   1 
HETATM 2381 O  O   . HOH I 5 .   ? 33.346 7.535   14.275  1.00 27.82 ? 355 HOH B O   1 
HETATM 2382 O  O   . HOH I 5 .   ? 22.020 -9.093  27.633  1.00 27.92 ? 357 HOH B O   1 
HETATM 2383 O  O   . HOH I 5 .   ? 34.799 5.394   8.752   1.00 22.67 ? 358 HOH B O   1 
HETATM 2384 O  O   . HOH I 5 .   ? 36.614 14.053  30.415  1.00 26.00 ? 362 HOH B O   1 
HETATM 2385 O  O   . HOH I 5 .   ? 39.834 4.443   12.520  1.00 25.37 ? 364 HOH B O   1 
HETATM 2386 O  O   . HOH I 5 .   ? 38.687 8.835   14.818  1.00 27.22 ? 367 HOH B O   1 
HETATM 2387 O  O   . HOH I 5 .   ? 31.152 13.784  20.692  1.00 31.70 ? 368 HOH B O   1 
HETATM 2388 O  O   . HOH I 5 .   ? 29.049 -13.725 17.390  1.00 27.08 ? 372 HOH B O   1 
HETATM 2389 O  O   . HOH I 5 .   ? 18.544 2.263   35.298  1.00 29.24 ? 376 HOH B O   1 
HETATM 2390 O  O   . HOH I 5 .   ? 41.345 6.442   14.183  1.00 28.00 ? 380 HOH B O   1 
HETATM 2391 O  O   . HOH I 5 .   ? 21.685 13.111  25.914  1.00 29.48 ? 382 HOH B O   1 
HETATM 2392 O  O   . HOH I 5 .   ? 40.417 14.454  27.843  1.00 33.60 ? 384 HOH B O   1 
HETATM 2393 O  O   . HOH I 5 .   ? 44.030 1.964   34.213  1.00 30.54 ? 389 HOH B O   1 
HETATM 2394 O  O   . HOH I 5 .   ? 34.914 -15.868 16.827  1.00 32.61 ? 391 HOH B O   1 
HETATM 2395 O  O   . HOH I 5 .   ? 37.242 6.574   13.360  1.00 28.24 ? 394 HOH B O   1 
HETATM 2396 O  O   . HOH I 5 .   ? 21.063 2.529   14.561  1.00 37.56 ? 395 HOH B O   1 
HETATM 2397 O  O   . HOH I 5 .   ? 35.441 -2.786  31.681  1.00 28.92 ? 396 HOH B O   1 
HETATM 2398 O  O   . HOH I 5 .   ? 38.284 2.254   38.501  1.00 32.94 ? 401 HOH B O   1 
HETATM 2399 O  O   . HOH I 5 .   ? 36.497 12.742  9.641   1.00 38.05 ? 402 HOH B O   1 
HETATM 2400 O  O   . HOH I 5 .   ? 43.655 14.527  35.215  1.00 34.90 ? 407 HOH B O   1 
HETATM 2401 O  O   . HOH I 5 .   ? 43.102 12.518  19.298  1.00 33.01 ? 409 HOH B O   1 
HETATM 2402 O  O   . HOH I 5 .   ? 48.567 0.187   23.261  1.00 41.18 ? 410 HOH B O   1 
HETATM 2403 O  O   . HOH I 5 .   ? 42.117 7.163   38.916  1.00 35.48 ? 411 HOH B O   1 
HETATM 2404 O  O   . HOH I 5 .   ? 46.818 -13.074 9.517   1.00 34.94 ? 415 HOH B O   1 
HETATM 2405 O  O   . HOH I 5 .   ? 31.599 -12.561 10.548  1.00 41.47 ? 416 HOH B O   1 
HETATM 2406 O  O   . HOH I 5 .   ? 27.198 6.464   23.595  1.00 32.64 ? 417 HOH B O   1 
HETATM 2407 O  O   . HOH I 5 .   ? 41.313 -7.096  34.296  1.00 40.81 ? 418 HOH B O   1 
HETATM 2408 O  O   . HOH I 5 .   ? 26.182 6.936   11.110  1.00 36.08 ? 420 HOH B O   1 
HETATM 2409 O  O   . HOH I 5 .   ? 47.133 7.725   39.667  1.00 35.33 ? 423 HOH B O   1 
HETATM 2410 O  O   . HOH I 5 .   ? 31.766 -7.404  11.080  1.00 27.60 ? 424 HOH B O   1 
HETATM 2411 O  O   . HOH I 5 .   ? 48.126 11.565  29.211  1.00 32.62 ? 428 HOH B O   1 
HETATM 2412 O  O   . HOH I 5 .   ? 46.341 -6.033  17.618  1.00 30.97 ? 430 HOH B O   1 
HETATM 2413 O  O   . HOH I 5 .   ? 34.231 -21.125 24.619  1.00 47.33 ? 431 HOH B O   1 
HETATM 2414 O  O   . HOH I 5 .   ? 32.176 13.825  16.735  1.00 42.11 ? 432 HOH B O   1 
HETATM 2415 O  O   . HOH I 5 .   ? 34.753 5.523   13.744  1.00 35.78 ? 433 HOH B O   1 
HETATM 2416 O  O   . HOH I 5 .   ? 49.278 -3.316  18.399  1.00 32.92 ? 436 HOH B O   1 
HETATM 2417 O  O   . HOH I 5 .   ? 27.737 9.247   6.792   1.00 44.82 ? 438 HOH B O   1 
HETATM 2418 O  O   . HOH I 5 .   ? 39.090 12.865  29.739  1.00 34.83 ? 440 HOH B O   1 
HETATM 2419 O  O   . HOH I 5 .   ? 32.121 -20.745 17.203  1.00 37.99 ? 442 HOH B O   1 
HETATM 2420 O  O   . HOH I 5 .   ? 21.406 9.374   23.685  1.00 47.69 ? 445 HOH B O   1 
HETATM 2421 O  O   . HOH I 5 .   ? 32.878 15.753  8.491   1.00 47.12 ? 446 HOH B O   1 
HETATM 2422 O  O   . HOH I 5 .   ? 43.844 -11.379 29.794  1.00 41.42 ? 447 HOH B O   1 
HETATM 2423 O  O   . HOH I 5 .   ? 39.516 9.152   10.550  1.00 30.19 ? 448 HOH B O   1 
HETATM 2424 O  O   . HOH I 5 .   ? 27.287 -3.517  36.556  1.00 44.15 ? 449 HOH B O   1 
HETATM 2425 O  O   . HOH I 5 .   ? 24.136 8.119   18.312  1.00 32.03 ? 450 HOH B O   1 
HETATM 2426 O  O   . HOH I 5 .   ? 43.097 -12.808 8.653   1.00 45.34 ? 452 HOH B O   1 
HETATM 2427 O  O   . HOH I 5 .   ? 43.774 16.607  28.449  1.00 47.59 ? 456 HOH B O   1 
HETATM 2428 O  O   . HOH I 5 .   ? 48.798 -8.114  14.620  1.00 34.33 ? 458 HOH B O   1 
HETATM 2429 O  O   . HOH I 5 .   ? 24.572 -8.143  25.011  1.00 32.12 ? 460 HOH B O   1 
HETATM 2430 O  O   . HOH I 5 .   ? 39.378 -16.908 22.819  1.00 33.13 ? 461 HOH B O   1 
HETATM 2431 O  O   . HOH I 5 .   ? 26.948 5.297   8.953   1.00 34.67 ? 462 HOH B O   1 
HETATM 2432 O  O   . HOH I 5 .   ? 24.632 8.672   36.347  1.00 38.96 ? 465 HOH B O   1 
HETATM 2433 O  O   . HOH I 5 .   ? 49.432 -1.926  21.748  1.00 34.69 ? 466 HOH B O   1 
HETATM 2434 O  O   . HOH I 5 .   ? 26.396 2.144   38.560  1.00 39.70 ? 468 HOH B O   1 
HETATM 2435 O  O   . HOH I 5 .   ? 48.101 -16.466 19.886  1.00 55.15 ? 470 HOH B O   1 
HETATM 2436 O  O   . HOH I 5 .   ? 38.325 16.473  22.919  1.00 40.59 ? 472 HOH B O   1 
HETATM 2437 O  O   . HOH I 5 .   ? 21.846 0.783   20.971  1.00 33.91 ? 474 HOH B O   1 
HETATM 2438 O  O   . HOH I 5 .   ? 33.626 -5.237  35.671  1.00 49.85 ? 475 HOH B O   1 
HETATM 2439 O  O   . HOH I 5 .   ? 28.149 6.425   5.683   1.00 39.95 ? 477 HOH B O   1 
HETATM 2440 O  O   . HOH I 5 .   ? 26.779 -12.080 11.538  1.00 44.70 ? 479 HOH B O   1 
HETATM 2441 O  O   . HOH I 5 .   ? 37.821 11.927  14.982  1.00 32.41 ? 485 HOH B O   1 
HETATM 2442 O  O   . HOH I 5 .   ? 24.574 -2.657  12.015  1.00 29.58 ? 501 HOH B O   1 
HETATM 2443 O  O   . HOH I 5 .   ? 33.936 14.034  35.443  1.00 39.76 ? 502 HOH B O   1 
HETATM 2444 O  O   . HOH I 5 .   ? 35.157 -5.990  31.952  1.00 28.31 ? 503 HOH B O   1 
HETATM 2445 O  O   . HOH I 5 .   ? 38.021 -8.266  32.715  1.00 33.73 ? 504 HOH B O   1 
HETATM 2446 O  O   . HOH I 5 .   ? 23.352 13.829  28.493  1.00 34.07 ? 505 HOH B O   1 
HETATM 2447 O  O   . HOH I 5 .   ? 23.520 -6.039  13.565  1.00 37.99 ? 512 HOH B O   1 
HETATM 2448 O  O   . HOH I 5 .   ? 22.829 -10.813 18.699  1.00 37.62 ? 517 HOH B O   1 
HETATM 2449 O  O   . HOH I 5 .   ? 35.573 13.083  16.537  1.00 38.76 ? 524 HOH B O   1 
HETATM 2450 O  O   . HOH I 5 .   ? 25.151 6.015   22.175  1.00 29.78 ? 525 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  ARG 43  43  43  ARG ARG B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU1 1   200 200 CU1 CU  A . 
D 3 ZN  1   201 201 ZN  ZN  A . 
E 4 SO4 1   600 600 SO4 SO4 A . 
F 2 CU1 1   200 200 CU1 CU  B . 
G 3 ZN  1   201 201 ZN  ZN  B . 
H 5 HOH 1   302 302 HOH HOH A . 
H 5 HOH 2   304 304 HOH HOH A . 
H 5 HOH 3   305 305 HOH HOH A . 
H 5 HOH 4   306 306 HOH HOH A . 
H 5 HOH 5   308 308 HOH HOH A . 
H 5 HOH 6   310 310 HOH HOH A . 
H 5 HOH 7   311 311 HOH HOH A . 
H 5 HOH 8   312 312 HOH HOH A . 
H 5 HOH 9   313 313 HOH HOH A . 
H 5 HOH 10  318 318 HOH HOH A . 
H 5 HOH 11  319 319 HOH HOH A . 
H 5 HOH 12  320 320 HOH HOH A . 
H 5 HOH 13  322 322 HOH HOH A . 
H 5 HOH 14  323 323 HOH HOH A . 
H 5 HOH 15  325 325 HOH HOH A . 
H 5 HOH 16  328 328 HOH HOH A . 
H 5 HOH 17  329 329 HOH HOH A . 
H 5 HOH 18  331 331 HOH HOH A . 
H 5 HOH 19  333 333 HOH HOH A . 
H 5 HOH 20  334 334 HOH HOH A . 
H 5 HOH 21  335 335 HOH HOH A . 
H 5 HOH 22  338 338 HOH HOH A . 
H 5 HOH 23  341 341 HOH HOH A . 
H 5 HOH 24  342 342 HOH HOH A . 
H 5 HOH 25  343 343 HOH HOH A . 
H 5 HOH 26  347 347 HOH HOH A . 
H 5 HOH 27  350 350 HOH HOH A . 
H 5 HOH 28  351 351 HOH HOH A . 
H 5 HOH 29  356 356 HOH HOH A . 
H 5 HOH 30  359 359 HOH HOH A . 
H 5 HOH 31  360 360 HOH HOH A . 
H 5 HOH 32  361 361 HOH HOH A . 
H 5 HOH 33  363 363 HOH HOH A . 
H 5 HOH 34  365 365 HOH HOH A . 
H 5 HOH 35  366 366 HOH HOH A . 
H 5 HOH 36  369 369 HOH HOH A . 
H 5 HOH 37  370 370 HOH HOH A . 
H 5 HOH 38  371 371 HOH HOH A . 
H 5 HOH 39  373 373 HOH HOH A . 
H 5 HOH 40  374 374 HOH HOH A . 
H 5 HOH 41  375 375 HOH HOH A . 
H 5 HOH 42  377 377 HOH HOH A . 
H 5 HOH 43  378 378 HOH HOH A . 
H 5 HOH 44  379 379 HOH HOH A . 
H 5 HOH 45  381 381 HOH HOH A . 
H 5 HOH 46  383 383 HOH HOH A . 
H 5 HOH 47  385 385 HOH HOH A . 
H 5 HOH 48  386 386 HOH HOH A . 
H 5 HOH 49  387 387 HOH HOH A . 
H 5 HOH 50  388 388 HOH HOH A . 
H 5 HOH 51  390 390 HOH HOH A . 
H 5 HOH 52  392 392 HOH HOH A . 
H 5 HOH 53  393 393 HOH HOH A . 
H 5 HOH 54  397 397 HOH HOH A . 
H 5 HOH 55  398 398 HOH HOH A . 
H 5 HOH 56  399 399 HOH HOH A . 
H 5 HOH 57  400 400 HOH HOH A . 
H 5 HOH 58  404 404 HOH HOH A . 
H 5 HOH 59  405 405 HOH HOH A . 
H 5 HOH 60  406 406 HOH HOH A . 
H 5 HOH 61  408 408 HOH HOH A . 
H 5 HOH 62  412 412 HOH HOH A . 
H 5 HOH 63  413 413 HOH HOH A . 
H 5 HOH 64  414 414 HOH HOH A . 
H 5 HOH 65  419 419 HOH HOH A . 
H 5 HOH 66  421 421 HOH HOH A . 
H 5 HOH 67  422 422 HOH HOH A . 
H 5 HOH 68  426 426 HOH HOH A . 
H 5 HOH 69  427 427 HOH HOH A . 
H 5 HOH 70  429 429 HOH HOH A . 
H 5 HOH 71  434 434 HOH HOH A . 
H 5 HOH 72  435 435 HOH HOH A . 
H 5 HOH 73  437 437 HOH HOH A . 
H 5 HOH 74  439 439 HOH HOH A . 
H 5 HOH 75  441 441 HOH HOH A . 
H 5 HOH 76  443 443 HOH HOH A . 
H 5 HOH 77  444 444 HOH HOH A . 
H 5 HOH 78  451 451 HOH HOH A . 
H 5 HOH 79  453 453 HOH HOH A . 
H 5 HOH 80  454 454 HOH HOH A . 
H 5 HOH 81  455 455 HOH HOH A . 
H 5 HOH 82  457 457 HOH HOH A . 
H 5 HOH 83  459 459 HOH HOH A . 
H 5 HOH 84  463 463 HOH HOH A . 
H 5 HOH 85  464 464 HOH HOH A . 
H 5 HOH 86  467 467 HOH HOH A . 
H 5 HOH 87  469 469 HOH HOH A . 
H 5 HOH 88  471 471 HOH HOH A . 
H 5 HOH 89  476 476 HOH HOH A . 
H 5 HOH 90  478 478 HOH HOH A . 
H 5 HOH 91  481 481 HOH HOH A . 
H 5 HOH 92  482 482 HOH HOH A . 
H 5 HOH 93  483 483 HOH HOH A . 
H 5 HOH 94  484 484 HOH HOH A . 
H 5 HOH 95  486 486 HOH HOH A . 
H 5 HOH 96  487 487 HOH HOH A . 
H 5 HOH 97  488 488 HOH HOH A . 
H 5 HOH 98  489 489 HOH HOH A . 
H 5 HOH 99  490 490 HOH HOH A . 
H 5 HOH 100 491 491 HOH HOH A . 
H 5 HOH 101 492 492 HOH HOH A . 
H 5 HOH 102 493 493 HOH HOH A . 
H 5 HOH 103 494 494 HOH HOH A . 
H 5 HOH 104 495 495 HOH HOH A . 
H 5 HOH 105 496 496 HOH HOH A . 
H 5 HOH 106 498 498 HOH HOH A . 
H 5 HOH 107 499 499 HOH HOH A . 
H 5 HOH 108 500 500 HOH HOH A . 
H 5 HOH 109 506 506 HOH HOH A . 
H 5 HOH 110 507 507 HOH HOH A . 
H 5 HOH 111 508 508 HOH HOH A . 
H 5 HOH 112 509 509 HOH HOH A . 
H 5 HOH 113 510 510 HOH HOH A . 
H 5 HOH 114 511 511 HOH HOH A . 
H 5 HOH 115 513 513 HOH HOH A . 
H 5 HOH 116 514 514 HOH HOH A . 
H 5 HOH 117 515 515 HOH HOH A . 
H 5 HOH 118 516 516 HOH HOH A . 
H 5 HOH 119 518 518 HOH HOH A . 
H 5 HOH 120 519 519 HOH HOH A . 
H 5 HOH 121 520 520 HOH HOH A . 
H 5 HOH 122 521 521 HOH HOH A . 
H 5 HOH 123 522 522 HOH HOH A . 
H 5 HOH 124 523 523 HOH HOH A . 
I 5 HOH 1   300 300 HOH HOH B . 
I 5 HOH 2   301 301 HOH HOH B . 
I 5 HOH 3   303 303 HOH HOH B . 
I 5 HOH 4   307 307 HOH HOH B . 
I 5 HOH 5   309 309 HOH HOH B . 
I 5 HOH 6   314 314 HOH HOH B . 
I 5 HOH 7   315 315 HOH HOH B . 
I 5 HOH 8   316 316 HOH HOH B . 
I 5 HOH 9   317 317 HOH HOH B . 
I 5 HOH 10  321 321 HOH HOH B . 
I 5 HOH 11  324 324 HOH HOH B . 
I 5 HOH 12  326 326 HOH HOH B . 
I 5 HOH 13  327 327 HOH HOH B . 
I 5 HOH 14  330 330 HOH HOH B . 
I 5 HOH 15  332 332 HOH HOH B . 
I 5 HOH 16  336 336 HOH HOH B . 
I 5 HOH 17  337 337 HOH HOH B . 
I 5 HOH 18  339 339 HOH HOH B . 
I 5 HOH 19  340 340 HOH HOH B . 
I 5 HOH 20  344 344 HOH HOH B . 
I 5 HOH 21  345 345 HOH HOH B . 
I 5 HOH 22  346 346 HOH HOH B . 
I 5 HOH 23  348 348 HOH HOH B . 
I 5 HOH 24  349 349 HOH HOH B . 
I 5 HOH 25  352 352 HOH HOH B . 
I 5 HOH 26  353 353 HOH HOH B . 
I 5 HOH 27  354 354 HOH HOH B . 
I 5 HOH 28  355 355 HOH HOH B . 
I 5 HOH 29  357 357 HOH HOH B . 
I 5 HOH 30  358 358 HOH HOH B . 
I 5 HOH 31  362 362 HOH HOH B . 
I 5 HOH 32  364 364 HOH HOH B . 
I 5 HOH 33  367 367 HOH HOH B . 
I 5 HOH 34  368 368 HOH HOH B . 
I 5 HOH 35  372 372 HOH HOH B . 
I 5 HOH 36  376 376 HOH HOH B . 
I 5 HOH 37  380 380 HOH HOH B . 
I 5 HOH 38  382 382 HOH HOH B . 
I 5 HOH 39  384 384 HOH HOH B . 
I 5 HOH 40  389 389 HOH HOH B . 
I 5 HOH 41  391 391 HOH HOH B . 
I 5 HOH 42  394 394 HOH HOH B . 
I 5 HOH 43  395 395 HOH HOH B . 
I 5 HOH 44  396 396 HOH HOH B . 
I 5 HOH 45  401 401 HOH HOH B . 
I 5 HOH 46  402 402 HOH HOH B . 
I 5 HOH 47  407 407 HOH HOH B . 
I 5 HOH 48  409 409 HOH HOH B . 
I 5 HOH 49  410 410 HOH HOH B . 
I 5 HOH 50  411 411 HOH HOH B . 
I 5 HOH 51  415 415 HOH HOH B . 
I 5 HOH 52  416 416 HOH HOH B . 
I 5 HOH 53  417 417 HOH HOH B . 
I 5 HOH 54  418 418 HOH HOH B . 
I 5 HOH 55  420 420 HOH HOH B . 
I 5 HOH 56  423 423 HOH HOH B . 
I 5 HOH 57  424 424 HOH HOH B . 
I 5 HOH 58  428 428 HOH HOH B . 
I 5 HOH 59  430 430 HOH HOH B . 
I 5 HOH 60  431 431 HOH HOH B . 
I 5 HOH 61  432 432 HOH HOH B . 
I 5 HOH 62  433 433 HOH HOH B . 
I 5 HOH 63  436 436 HOH HOH B . 
I 5 HOH 64  438 438 HOH HOH B . 
I 5 HOH 65  440 440 HOH HOH B . 
I 5 HOH 66  442 442 HOH HOH B . 
I 5 HOH 67  445 445 HOH HOH B . 
I 5 HOH 68  446 446 HOH HOH B . 
I 5 HOH 69  447 447 HOH HOH B . 
I 5 HOH 70  448 448 HOH HOH B . 
I 5 HOH 71  449 449 HOH HOH B . 
I 5 HOH 72  450 450 HOH HOH B . 
I 5 HOH 73  452 452 HOH HOH B . 
I 5 HOH 74  456 456 HOH HOH B . 
I 5 HOH 75  458 458 HOH HOH B . 
I 5 HOH 76  460 460 HOH HOH B . 
I 5 HOH 77  461 461 HOH HOH B . 
I 5 HOH 78  462 462 HOH HOH B . 
I 5 HOH 79  465 465 HOH HOH B . 
I 5 HOH 80  466 466 HOH HOH B . 
I 5 HOH 81  468 468 HOH HOH B . 
I 5 HOH 82  470 470 HOH HOH B . 
I 5 HOH 83  472 472 HOH HOH B . 
I 5 HOH 84  474 474 HOH HOH B . 
I 5 HOH 85  475 475 HOH HOH B . 
I 5 HOH 86  477 477 HOH HOH B . 
I 5 HOH 87  479 479 HOH HOH B . 
I 5 HOH 88  485 485 HOH HOH B . 
I 5 HOH 89  501 501 HOH HOH B . 
I 5 HOH 90  502 502 HOH HOH B . 
I 5 HOH 91  503 503 HOH HOH B . 
I 5 HOH 92  504 504 HOH HOH B . 
I 5 HOH 93  505 505 HOH HOH B . 
I 5 HOH 94  512 512 HOH HOH B . 
I 5 HOH 95  517 517 HOH HOH B . 
I 5 HOH 96  524 524 HOH HOH B . 
I 5 HOH 97  525 525 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)' 1500  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  13690 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 144.2 ? 
2  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? C CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 98.2  ? 
3  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? C CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 117.6 ? 
4  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 106.2 ? 
5  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 113.2 ? 
6  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 122.3 ? 
7  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 99.9  ? 
8  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 98.2  ? 
9  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? D ZN  . ? A ZN  201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 113.9 ? 
10 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? F CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 145.6 ? 
11 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? F CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 96.3  ? 
12 NE2 ? B HIS 48 ? B HIS 48 ? 1_555 CU ? F CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 117.5 ? 
13 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 106.8 ? 
14 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 110.9 ? 
15 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 121.5 ? 
16 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 100.0 ? 
17 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 94.2  ? 
18 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 120.3 ? 
19 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 152.4 ? 
20 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 80.4  ? 
21 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 85.8  ? 
22 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? G ZN  . ? B ZN  201 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 52.5  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2003-09-09 
2 'Structure model' 1 1 2008-04-29 
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.ptnr2_auth_comp_id'  
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_atom_id' 
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_comp_id' 
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 4 'Structure model' '_pdbx_struct_conn_angle.value'               
19 4 'Structure model' '_struct_conn.pdbx_dist_value'                
20 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
21 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
22 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
23 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
24 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
25 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
26 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
27 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
28 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
29 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
30 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
31 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
32 4 'Structure model' '_struct_ref_seq_dif.details'                 
33 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
34 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
35 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       1.1 ? 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 ARG A 115 ? ? -104.02 -167.81 
2 1 ASN B 65  ? ? -157.60 76.18   
# 
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 
# 
