data_2R27
# 
_entry.id   2R27 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.350 
_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   2R27         pdb_00002r27 10.2210/pdb2r27/pdb 
RCSB  RCSB044332   ?            ?                   
WWPDB D_1000044332 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2R27 
_pdbx_database_status.recvd_initial_deposition_date   2007-08-24 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Roberts, B.R.' 1 
'Getzoff, E.D.' 2 
'Karplus, P.A.' 3 
'Beckman, J.S.' 4 
'Tainer, J.A.'  5 
# 
_citation.id                        primary 
_citation.title                     
'Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            373 
_citation.page_first                877 
_citation.page_last                 890 
_citation.year                      2007 
_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   17888947 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2007.07.043 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Roberts, B.R.'  1 ? 
primary 'Tainer, J.A.'   2 ? 
primary 'Getzoff, E.D.'  3 ? 
primary 'Malencik, D.A.' 4 ? 
primary 'Anderson, S.R.' 5 ? 
primary 'Bomben, V.C.'   6 ? 
primary 'Meyers, K.R.'   7 ? 
primary 'Karplus, P.A.'  8 ? 
primary 'Beckman, J.S.'  9 ? 
# 
_cell.entry_id           2R27 
_cell.length_a           107.200 
_cell.length_b           35.900 
_cell.length_c           68.300 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.80 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2R27 
_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 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]' 15831.548 2   1.15.1.1 'C7A, H81S, D84S, C112S' ? ? 
2 non-polymer syn 'COPPER (II) ION'              63.546    2   ?        ?                        ? ? 
3 water       nat water                          18.015    190 ?        ?                        ? ? 
# 
_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       
;MATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
SVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
SVGSLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   ALA n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  SER n 
1 82  VAL n 
1 83  GLY n 
1 84  SER n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 SER n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 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   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2R27 A 1 ? 154 ? P00441 1 ? 154 ? 0 153 
2 1 2R27 B 1 ? 154 ? P00441 1 ? 154 ? 0 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2R27 ALA A 7   ? UNP P00441 CYS 7   'engineered mutation' 6   1 
1 2R27 SER A 81  ? UNP P00441 HIS 81  'engineered mutation' 80  2 
1 2R27 SER A 84  ? UNP P00441 ASP 84  'engineered mutation' 83  3 
1 2R27 SER A 112 ? UNP P00441 CYS 112 'engineered mutation' 111 4 
2 2R27 ALA B 7   ? UNP P00441 CYS 7   'engineered mutation' 6   5 
2 2R27 SER B 81  ? UNP P00441 HIS 81  'engineered mutation' 80  6 
2 2R27 SER B 84  ? UNP P00441 ASP 84  'engineered mutation' 83  7 
2 2R27 SER B 112 ? UNP P00441 CYS 112 'engineered mutation' 111 8 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ? 'C4 H7 N O4'     133.103 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          2R27 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.01 
_exptl_crystal.density_percent_sol   38.70 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'2.45 M ammonium sulfate, 200 mM NaCl in 50 mM Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 130 mm' 
_diffrn_detector.pdbx_collection_date   1997-01-15 
_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   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL9-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL9-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.08 
# 
_reflns.entry_id                     2R27 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            2.0 
_reflns.d_resolution_low             19.2 
_reflns.number_all                   15899 
_reflns.number_obs                   15899 
_reflns.percent_possible_obs         91.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.051 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.00 
_reflns_shell.d_res_low              2.07 
_reflns_shell.percent_possible_all   ? 
_reflns_shell.Rmerge_I_obs           .364 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2R27 
_refine.ls_d_res_high                            2.0 
_refine.ls_d_res_low                             19.2 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     15899 
_refine.ls_number_reflns_obs                     15898 
_refine.ls_number_reflns_R_free                  679 
_refine.ls_percent_reflns_obs                    91.9 
_refine.ls_R_factor_all                          .206 
_refine.ls_R_factor_obs                          .187 
_refine.ls_R_factor_R_work                       .184 
_refine.ls_R_factor_R_free                       .246 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1N18 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            Random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_mean                               31.5 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1910 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             190 
_refine_hist.number_atoms_total               2102 
_refine_hist.d_res_high                       2.0 
_refine_hist.d_res_low                        19.2 
# 
_struct.entry_id                  2R27 
_struct.title                     
'Constitutively zinc-deficient mutant of human superoxide dismutase (SOD), C6A, H80S, H83S, C111S' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2R27 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'oxidoreductase, beta barrel, Cu ion, Amyotrophic lateral sclerosis, Antioxidant, Disease mutation, Metal-binding' 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 SER A 108 ? SER A 112 ? SER A 107 SER A 111 5 ? 5 
HELX_P HELX_P3 3 CYS B 58  ? GLY B 62  ? CYS B 57  GLY B 61  5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 58  SG  ? ? ? 1_555 A CYS 147 SG A ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
disulf2 disulf ? ? A CYS 58  SG  ? ? ? 1_555 A CYS 147 SG B ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
disulf3 disulf ? ? B CYS 58  SG  ? ? ? 1_555 B CYS 147 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc1 metalc ? ? A HIS 47  ND1 ? ? ? 1_555 C CU  .   CU A ? A HIS 46  A CU  154 1_555 ? ? ? ? ? ? ? 2.232 ? ? 
metalc2 metalc ? ? A HIS 49  NE2 ? ? ? 1_555 C CU  .   CU A ? A HIS 48  A CU  154 1_555 ? ? ? ? ? ? ? 1.921 ? ? 
metalc3 metalc ? ? A HIS 49  NE2 ? ? ? 1_555 C CU  .   CU B ? A HIS 48  A CU  154 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc4 metalc ? ? A HIS 121 NE2 ? ? ? 1_555 C CU  .   CU A ? A HIS 120 A CU  154 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc5 metalc ? ? A HIS 121 NE2 ? ? ? 1_555 C CU  .   CU B ? A HIS 120 A CU  154 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc6 metalc ? ? B HIS 47  ND1 ? ? ? 1_555 D CU  .   CU ? ? B HIS 46  B CU  154 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc7 metalc ? ? B HIS 49  NE2 ? ? ? 1_555 D CU  .   CU ? ? B HIS 48  B CU  154 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc8 metalc ? ? B HIS 121 NE2 ? ? ? 1_555 D CU  .   CU ? ? B HIS 120 B CU  154 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
# 
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 ? 10 ? 
B ? 5  ? 
C ? 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 
A 5 6  ? anti-parallel 
A 6 7  ? anti-parallel 
A 7 8  ? anti-parallel 
A 8 9  ? anti-parallel 
A 9 10 ? anti-parallel 
B 1 2  ? anti-parallel 
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 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  GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
A 2  LYS A 4   ? GLY A 11  ? LYS A 3   GLY A 10  
A 3  ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
A 4  THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
A 5  GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
A 6  SER A 84  ? ALA A 90  ? SER A 83  ALA A 89  
A 7  ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
A 8  VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
A 9  GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
A 10 LYS A 4   ? GLY A 11  ? LYS A 3   GLY A 10  
B 1  ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
B 2  VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
B 3  GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
B 4  LYS B 4   ? LEU B 9   ? LYS B 3   LEU B 8   
B 5  GLY B 151 ? ILE B 152 ? GLY B 150 ILE B 151 
C 1  SER B 84  ? ALA B 90  ? SER B 83  ALA B 89  
C 2  GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
C 3  THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
C 4  ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  O GLY A 151 ? O GLY A 150 N VAL A 6   ? N VAL A 5   
A 2 3  N LYS A 10  ? N LYS A 9   O CYS A 147 ? O CYS A 146 
A 3 4  O GLY A 148 ? O GLY A 147 N LEU A 118 ? N LEU A 117 
A 4 5  O THR A 117 ? O THR A 116 N HIS A 49  ? N HIS A 48  
A 5 6  N GLY A 42  ? N GLY A 41  O ALA A 90  ? O ALA A 89  
A 6 7  N THR A 89  ? N THR A 88  O ASP A 97  ? O ASP A 96  
A 7 8  O ALA A 96  ? O ALA A 95  N ILE A 36  ? N ILE A 35  
A 8 9  O LYS A 31  ? O LYS A 30  N GLU A 22  ? N GLU A 21  
A 9 10 O GLY A 17  ? O GLY A 16  N LEU A 9   ? N LEU A 8   
B 1 2  O ASP B 102 ? O ASP B 101 N VAL B 30  ? N VAL B 29  
B 2 3  O TRP B 33  ? O TRP B 32  N ASN B 20  ? N ASN B 19  
B 3 4  O PHE B 21  ? O PHE B 20  N ALA B 5   ? N ALA B 4   
B 4 5  N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
C 1 2  O ALA B 90  ? O ALA B 89  N GLY B 42  ? N GLY B 41  
C 2 3  N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
C 3 4  N LEU B 118 ? N LEU B 117 O GLY B 148 ? O GLY B 147 
# 
_database_PDB_matrix.entry_id          2R27 
_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                    2R27 
_atom_sites.fract_transf_matrix[1][1]   0.009328 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002465 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.027855 
_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]   0.015144 
_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  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 2   ? 27.575 0.494   4.300  1.00 49.99 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 2   ? 27.799 1.957   4.558  1.00 49.80 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 2   ? 29.156 2.447   4.060  1.00 44.73 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 2   ? 29.940 1.680   3.546  1.00 50.93 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 2   ? 27.653 2.248   6.033  1.00 51.87 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 3   ? 29.431 3.730   4.219  1.00 43.23 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 3   ? 30.680 4.300   3.748  1.00 43.61 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 3   ? 31.594 4.793   4.867  1.00 39.88 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 3   ? 32.823 4.758   4.733  1.00 34.71 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 3   ? 30.367 5.451   2.755  1.00 44.90 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 3   ? 30.017 4.872   1.496  1.00 48.73 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 3   ? 31.534 6.392   2.585  1.00 51.07 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 4   ? 30.989 5.271   5.949  1.00 32.34 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 4   ? 31.734 5.761   7.109  1.00 35.12 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 4   ? 31.095 5.191   8.359  1.00 30.40 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 4   ? 29.894 4.980   8.409  1.00 27.98 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 4   ? 31.676 7.289   7.254  1.00 36.51 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 4   ? 32.316 8.107   6.161  1.00 47.32 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 4   ? 32.491 9.514   6.663  1.00 56.74 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 4   ? 32.847 10.480  5.543  1.00 65.79 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 4   ? 32.840 11.896  6.046  1.00 65.52 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 5   ? 31.909 5.016   9.385  1.00 30.31 ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 5   ? 31.430 4.507   10.657 1.00 27.60 ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 5   ? 32.295 5.086   11.738 1.00 29.82 ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 5   ? 33.349 5.717   11.462 1.00 28.36 ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 5   ? 31.530 3.033   10.681 1.00 25.95 ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 6   ? 31.879 4.857   12.981 1.00 24.53 ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 6   ? 32.634 5.403   14.082 1.00 21.72 ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 6   ? 32.377 4.546   15.311 1.00 22.77 ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 6   ? 31.287 4.003   15.457 1.00 24.02 ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 6   ? 32.208 6.873   14.413 1.00 23.66 ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 6   ? 30.772 6.908   14.974 1.00 24.56 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 6   ? 33.145 7.482   15.463 1.00 23.29 ? 5   VAL A CG2 1 
ATOM   34   N  N   . ALA A 1 7   ? 33.389 4.415   16.158 1.00 16.62 ? 6   ALA A N   1 
ATOM   35   C  CA  . ALA A 1 7   ? 33.215 3.693   17.447 1.00 24.28 ? 6   ALA A CA  1 
ATOM   36   C  C   . ALA A 1 7   ? 33.759 4.552   18.568 1.00 21.22 ? 6   ALA A C   1 
ATOM   37   O  O   . ALA A 1 7   ? 34.900 5.018   18.498 1.00 24.94 ? 6   ALA A O   1 
ATOM   38   C  CB  . ALA A 1 7   ? 33.908 2.332   17.455 1.00 22.23 ? 6   ALA A CB  1 
ATOM   39   N  N   . VAL A 1 8   ? 32.949 4.804   19.587 1.00 21.88 ? 7   VAL A N   1 
ATOM   40   C  CA  . VAL A 1 8   ? 33.467 5.605   20.722 1.00 26.35 ? 7   VAL A CA  1 
ATOM   41   C  C   . VAL A 1 8   ? 33.891 4.589   21.803 1.00 27.52 ? 7   VAL A C   1 
ATOM   42   O  O   . VAL A 1 8   ? 33.055 3.908   22.365 1.00 24.54 ? 7   VAL A O   1 
ATOM   43   C  CB  . VAL A 1 8   ? 32.397 6.566   21.305 1.00 29.81 ? 7   VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 8   ? 32.939 7.274   22.606 1.00 24.70 ? 7   VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 8   ? 32.063 7.634   20.264 1.00 36.42 ? 7   VAL A CG2 1 
ATOM   46   N  N   . LEU A 1 9   ? 35.196 4.493   22.053 1.00 25.22 ? 8   LEU A N   1 
ATOM   47   C  CA  . LEU A 1 9   ? 35.730 3.529   23.006 1.00 28.49 ? 8   LEU A CA  1 
ATOM   48   C  C   . LEU A 1 9   ? 35.596 4.048   24.431 1.00 28.48 ? 8   LEU A C   1 
ATOM   49   O  O   . LEU A 1 9   ? 36.192 5.073   24.767 1.00 29.11 ? 8   LEU A O   1 
ATOM   50   C  CB  . LEU A 1 9   ? 37.197 3.257   22.707 1.00 26.95 ? 8   LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 9   ? 37.453 2.598   21.328 1.00 34.86 ? 8   LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 9   ? 38.957 2.403   21.100 1.00 28.24 ? 8   LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 9   ? 36.703 1.286   21.237 1.00 33.82 ? 8   LEU A CD2 1 
ATOM   54   N  N   . LYS A 1 10  ? 34.818 3.334   25.243 1.00 29.04 ? 9   LYS A N   1 
ATOM   55   C  CA  . LYS A 1 10  ? 34.605 3.684   26.665 1.00 31.04 ? 9   LYS A CA  1 
ATOM   56   C  C   . LYS A 1 10  ? 34.682 2.421   27.546 1.00 32.19 ? 9   LYS A C   1 
ATOM   57   O  O   . LYS A 1 10  ? 34.302 1.288   27.130 1.00 26.55 ? 9   LYS A O   1 
ATOM   58   C  CB  . LYS A 1 10  ? 33.222 4.298   26.888 1.00 32.20 ? 9   LYS A CB  1 
ATOM   59   C  CG  . LYS A 1 10  ? 32.925 5.588   26.160 1.00 46.71 ? 9   LYS A CG  1 
ATOM   60   C  CD  . LYS A 1 10  ? 31.503 6.034   26.516 1.00 57.67 ? 9   LYS A CD  1 
ATOM   61   C  CE  . LYS A 1 10  ? 31.103 7.342   25.839 1.00 63.57 ? 9   LYS A CE  1 
ATOM   62   N  NZ  . LYS A 1 10  ? 29.678 7.694   26.146 1.00 65.26 ? 9   LYS A NZ  1 
ATOM   63   N  N   . GLY A 1 11  ? 35.148 2.622   28.771 1.00 33.55 ? 10  GLY A N   1 
ATOM   64   C  CA  . GLY A 1 11  ? 35.282 1.507   29.708 1.00 33.17 ? 10  GLY A CA  1 
ATOM   65   C  C   . GLY A 1 11  ? 35.194 2.011   31.141 1.00 31.77 ? 10  GLY A C   1 
ATOM   66   O  O   . GLY A 1 11  ? 34.695 3.113   31.373 1.00 29.74 ? 10  GLY A O   1 
ATOM   67   N  N   . ASP A 1 12  ? 35.715 1.231   32.085 1.00 34.41 ? 11  ASP A N   1 
ATOM   68   C  CA  . ASP A 1 12  ? 35.688 1.557   33.517 1.00 38.93 ? 11  ASP A CA  1 
ATOM   69   C  C   . ASP A 1 12  ? 36.866 2.356   34.024 1.00 34.44 ? 11  ASP A C   1 
ATOM   70   O  O   . ASP A 1 12  ? 36.942 2.607   35.224 1.00 33.91 ? 11  ASP A O   1 
ATOM   71   C  CB  . ASP A 1 12  ? 35.708 0.298   34.377 1.00 48.64 ? 11  ASP A CB  1 
ATOM   72   C  CG  . ASP A 1 12  ? 34.563 -0.603  34.115 1.00 60.06 ? 11  ASP A CG  1 
ATOM   73   O  OD1 . ASP A 1 12  ? 33.445 -0.080  33.926 1.00 60.95 ? 11  ASP A OD1 1 
ATOM   74   O  OD2 . ASP A 1 12  ? 34.792 -1.835  34.121 1.00 64.44 ? 11  ASP A OD2 1 
ATOM   75   N  N   . GLY A 1 13  ? 37.762 2.751   33.140 1.00 30.50 ? 12  GLY A N   1 
ATOM   76   C  CA  . GLY A 1 13  ? 39.016 3.332   33.548 1.00 30.53 ? 12  GLY A CA  1 
ATOM   77   C  C   . GLY A 1 13  ? 39.440 4.568   32.786 1.00 31.78 ? 12  GLY A C   1 
ATOM   78   O  O   . GLY A 1 13  ? 38.644 5.266   32.234 1.00 29.15 ? 12  GLY A O   1 
ATOM   79   N  N   . PRO A 1 14  ? 40.723 4.838   32.769 1.00 30.22 ? 13  PRO A N   1 
ATOM   80   C  CA  . PRO A 1 14  ? 41.229 5.945   31.975 1.00 32.59 ? 13  PRO A CA  1 
ATOM   81   C  C   . PRO A 1 14  ? 41.220 5.689   30.463 1.00 30.60 ? 13  PRO A C   1 
ATOM   82   O  O   . PRO A 1 14  ? 41.342 6.628   29.710 1.00 30.11 ? 13  PRO A O   1 
ATOM   83   C  CB  . PRO A 1 14  ? 42.654 6.078   32.464 1.00 28.81 ? 13  PRO A CB  1 
ATOM   84   C  CG  . PRO A 1 14  ? 42.997 4.738   32.906 1.00 28.28 ? 13  PRO A CG  1 
ATOM   85   C  CD  . PRO A 1 14  ? 41.796 4.187   33.518 1.00 27.56 ? 13  PRO A CD  1 
ATOM   86   N  N   . VAL A 1 15  ? 41.122 4.449   30.020 1.00 30.54 ? 14  VAL A N   1 
ATOM   87   C  CA  . VAL A 1 15  ? 41.186 4.220   28.568 1.00 25.90 ? 14  VAL A CA  1 
ATOM   88   C  C   . VAL A 1 15  ? 39.919 4.665   27.827 1.00 28.56 ? 14  VAL A C   1 
ATOM   89   O  O   . VAL A 1 15  ? 38.823 4.235   28.160 1.00 26.44 ? 14  VAL A O   1 
ATOM   90   C  CB  . VAL A 1 15  ? 41.466 2.715   28.202 1.00 29.87 ? 14  VAL A CB  1 
ATOM   91   C  CG1 . VAL A 1 15  ? 41.473 2.548   26.653 1.00 28.30 ? 14  VAL A CG1 1 
ATOM   92   C  CG2 . VAL A 1 15  ? 42.842 2.271   28.793 1.00 29.50 ? 14  VAL A CG2 1 
ATOM   93   N  N   . GLN A 1 16  ? 40.091 5.523   26.818 1.00 24.33 ? 15  GLN A N   1 
ATOM   94   C  CA  . GLN A 1 16  ? 38.985 6.009   26.008 1.00 31.64 ? 15  GLN A CA  1 
ATOM   95   C  C   . GLN A 1 16  ? 39.552 6.510   24.698 1.00 30.21 ? 15  GLN A C   1 
ATOM   96   O  O   . GLN A 1 16  ? 40.732 6.842   24.615 1.00 33.29 ? 15  GLN A O   1 
ATOM   97   C  CB  . GLN A 1 16  ? 38.263 7.160   26.693 1.00 33.78 ? 15  GLN A CB  1 
ATOM   98   C  CG  . GLN A 1 16  ? 39.201 8.226   27.182 1.00 42.79 ? 15  GLN A CG  1 
ATOM   99   C  CD  . GLN A 1 16  ? 38.446 9.433   27.678 1.00 57.83 ? 15  GLN A CD  1 
ATOM   100  O  OE1 . GLN A 1 16  ? 37.934 10.228  26.882 1.00 64.33 ? 15  GLN A OE1 1 
ATOM   101  N  NE2 . GLN A 1 16  ? 38.348 9.571   29.000 1.00 57.86 ? 15  GLN A NE2 1 
ATOM   102  N  N   . GLY A 1 17  ? 38.713 6.556   23.673 1.00 28.93 ? 16  GLY A N   1 
ATOM   103  C  CA  . GLY A 1 17  ? 39.166 7.047   22.377 1.00 31.73 ? 16  GLY A CA  1 
ATOM   104  C  C   . GLY A 1 17  ? 38.044 7.056   21.357 1.00 31.28 ? 16  GLY A C   1 
ATOM   105  O  O   . GLY A 1 17  ? 36.937 6.589   21.631 1.00 30.70 ? 16  GLY A O   1 
ATOM   106  N  N   . ILE A 1 18  ? 38.322 7.586   20.168 1.00 31.33 ? 17  ILE A N   1 
ATOM   107  C  CA  . ILE A 1 18  ? 37.321 7.608   19.116 1.00 29.40 ? 17  ILE A CA  1 
ATOM   108  C  C   . ILE A 1 18  ? 37.996 7.038   17.863 1.00 25.90 ? 17  ILE A C   1 
ATOM   109  O  O   . ILE A 1 18  ? 39.066 7.456   17.476 1.00 27.09 ? 17  ILE A O   1 
ATOM   110  C  CB  . ILE A 1 18  ? 36.803 9.062   18.897 1.00 32.70 ? 17  ILE A CB  1 
ATOM   111  C  CG1 . ILE A 1 18  ? 36.024 9.509   20.135 1.00 32.99 ? 17  ILE A CG1 1 
ATOM   112  C  CG2 . ILE A 1 18  ? 35.917 9.146   17.620 1.00 25.16 ? 17  ILE A CG2 1 
ATOM   113  C  CD1 . ILE A 1 18  ? 35.691 11.014  20.144 1.00 40.84 ? 17  ILE A CD1 1 
ATOM   114  N  N   . ILE A 1 19  ? 37.396 6.037   17.255 1.00 25.95 ? 18  ILE A N   1 
ATOM   115  C  CA  . ILE A 1 19  ? 38.006 5.456   16.081 1.00 26.00 ? 18  ILE A CA  1 
ATOM   116  C  C   . ILE A 1 19  ? 37.036 5.604   14.911 1.00 26.71 ? 18  ILE A C   1 
ATOM   117  O  O   . ILE A 1 19  ? 35.861 5.238   15.009 1.00 25.34 ? 18  ILE A O   1 
ATOM   118  C  CB  . ILE A 1 19  ? 38.311 3.945   16.296 1.00 21.23 ? 18  ILE A CB  1 
ATOM   119  C  CG1 . ILE A 1 19  ? 39.357 3.760   17.400 1.00 21.81 ? 18  ILE A CG1 1 
ATOM   120  C  CG2 . ILE A 1 19  ? 38.792 3.325   14.980 1.00 23.99 ? 18  ILE A CG2 1 
ATOM   121  C  CD1 . ILE A 1 19  ? 40.810 4.329   17.008 1.00 20.90 ? 18  ILE A CD1 1 
ATOM   122  N  N   . ASN A 1 20  ? 37.539 6.148   13.813 1.00 25.94 ? 19  ASN A N   1 
ATOM   123  C  CA  . ASN A 1 20  ? 36.741 6.325   12.616 1.00 27.81 ? 19  ASN A CA  1 
ATOM   124  C  C   . ASN A 1 20  ? 37.101 5.264   11.608 1.00 28.39 ? 19  ASN A C   1 
ATOM   125  O  O   . ASN A 1 20  ? 38.235 4.737   11.607 1.00 25.52 ? 19  ASN A O   1 
ATOM   126  C  CB  . ASN A 1 20  ? 36.992 7.713   12.015 1.00 26.29 ? 19  ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 20  ? 36.771 8.808   13.031 1.00 33.85 ? 19  ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 20  ? 35.643 9.149   13.368 1.00 31.59 ? 19  ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 20  ? 37.851 9.322   13.568 1.00 31.28 ? 19  ASN A ND2 1 
ATOM   130  N  N   . PHE A 1 21  ? 36.129 4.966   10.749 1.00 26.00 ? 20  PHE A N   1 
ATOM   131  C  CA  . PHE A 1 21  ? 36.275 3.964   9.691  1.00 27.29 ? 20  PHE A CA  1 
ATOM   132  C  C   . PHE A 1 21  ? 35.756 4.570   8.390  1.00 33.62 ? 20  PHE A C   1 
ATOM   133  O  O   . PHE A 1 21  ? 34.771 5.321   8.409  1.00 32.54 ? 20  PHE A O   1 
ATOM   134  C  CB  . PHE A 1 21  ? 35.406 2.748   9.971  1.00 27.55 ? 20  PHE A CB  1 
ATOM   135  C  CG  . PHE A 1 21  ? 35.747 2.020   11.248 1.00 32.50 ? 20  PHE A CG  1 
ATOM   136  C  CD1 . PHE A 1 21  ? 36.540 0.875   11.208 1.00 31.34 ? 20  PHE A CD1 1 
ATOM   137  C  CD2 . PHE A 1 21  ? 35.237 2.453   12.478 1.00 32.34 ? 20  PHE A CD2 1 
ATOM   138  C  CE1 . PHE A 1 21  ? 36.835 0.145   12.384 1.00 29.78 ? 20  PHE A CE1 1 
ATOM   139  C  CE2 . PHE A 1 21  ? 35.524 1.729   13.672 1.00 31.03 ? 20  PHE A CE2 1 
ATOM   140  C  CZ  . PHE A 1 21  ? 36.328 0.576   13.604 1.00 28.14 ? 20  PHE A CZ  1 
ATOM   141  N  N   . GLU A 1 22  ? 36.393 4.239   7.267  1.00 32.51 ? 21  GLU A N   1 
ATOM   142  C  CA  . GLU A 1 22  ? 35.920 4.749   5.969  1.00 33.47 ? 21  GLU A CA  1 
ATOM   143  C  C   . GLU A 1 22  ? 36.280 3.774   4.878  1.00 32.04 ? 21  GLU A C   1 
ATOM   144  O  O   . GLU A 1 22  ? 37.408 3.274   4.827  1.00 30.17 ? 21  GLU A O   1 
ATOM   145  C  CB  . GLU A 1 22  ? 36.544 6.092   5.658  1.00 34.90 ? 21  GLU A CB  1 
ATOM   146  C  CG  . GLU A 1 22  ? 36.088 6.632   4.320  1.00 51.70 ? 21  GLU A CG  1 
ATOM   147  C  CD  . GLU A 1 22  ? 36.563 8.037   4.104  1.00 56.22 ? 21  GLU A CD  1 
ATOM   148  O  OE1 . GLU A 1 22  ? 36.155 8.924   4.892  1.00 64.68 ? 21  GLU A OE1 1 
ATOM   149  O  OE2 . GLU A 1 22  ? 37.349 8.245   3.162  1.00 59.54 ? 21  GLU A OE2 1 
ATOM   150  N  N   . GLN A 1 23  ? 35.303 3.479   4.025  1.00 35.64 ? 22  GLN A N   1 
ATOM   151  C  CA  . GLN A 1 23  ? 35.471 2.515   2.930  1.00 41.01 ? 22  GLN A CA  1 
ATOM   152  C  C   . GLN A 1 23  ? 34.775 3.076   1.709  1.00 44.58 ? 22  GLN A C   1 
ATOM   153  O  O   . GLN A 1 23  ? 33.561 3.224   1.705  1.00 43.00 ? 22  GLN A O   1 
ATOM   154  C  CB  . GLN A 1 23  ? 34.811 1.184   3.291  1.00 35.12 ? 22  GLN A CB  1 
ATOM   155  C  CG  . GLN A 1 23  ? 35.042 0.087   2.258  1.00 34.97 ? 22  GLN A CG  1 
ATOM   156  C  CD  . GLN A 1 23  ? 34.306 -1.190  2.568  1.00 38.76 ? 22  GLN A CD  1 
ATOM   157  O  OE1 . GLN A 1 23  ? 33.218 -1.164  3.147  1.00 45.68 ? 22  GLN A OE1 1 
ATOM   158  N  NE2 . GLN A 1 23  ? 34.880 -2.323  2.167  1.00 36.29 ? 22  GLN A NE2 1 
ATOM   159  N  N   . LYS A 1 24  ? 35.528 3.372   0.667  1.00 51.30 ? 23  LYS A N   1 
ATOM   160  C  CA  . LYS A 1 24  ? 34.909 3.952   -0.515 1.00 55.85 ? 23  LYS A CA  1 
ATOM   161  C  C   . LYS A 1 24  ? 34.398 2.934   -1.517 1.00 57.39 ? 23  LYS A C   1 
ATOM   162  O  O   . LYS A 1 24  ? 33.292 3.066   -2.023 1.00 60.54 ? 23  LYS A O   1 
ATOM   163  C  CB  . LYS A 1 24  ? 35.880 4.932   -1.160 1.00 57.98 ? 23  LYS A CB  1 
ATOM   164  C  CG  . LYS A 1 24  ? 36.250 6.061   -0.215 1.00 59.26 ? 23  LYS A CG  1 
ATOM   165  C  CD  . LYS A 1 24  ? 37.191 7.049   -0.859 1.00 64.69 ? 23  LYS A CD  1 
ATOM   166  C  CE  . LYS A 1 24  ? 37.595 8.131   0.129  1.00 68.16 ? 23  LYS A CE  1 
ATOM   167  N  NZ  . LYS A 1 24  ? 38.580 9.083   -0.462 1.00 73.60 ? 23  LYS A NZ  1 
ATOM   168  N  N   . GLU A 1 25  ? 35.178 1.911   -1.809 1.00 62.07 ? 24  GLU A N   1 
ATOM   169  C  CA  . GLU A 1 25  ? 34.705 0.911   -2.756 1.00 66.91 ? 24  GLU A CA  1 
ATOM   170  C  C   . GLU A 1 25  ? 34.066 -0.206  -1.976 1.00 65.32 ? 24  GLU A C   1 
ATOM   171  O  O   . GLU A 1 25  ? 34.564 -0.581  -0.914 1.00 64.77 ? 24  GLU A O   1 
ATOM   172  C  CB  . GLU A 1 25  ? 35.849 0.325   -3.570 1.00 69.65 ? 24  GLU A CB  1 
ATOM   173  C  CG  . GLU A 1 25  ? 36.685 1.325   -4.307 1.00 78.80 ? 24  GLU A CG  1 
ATOM   174  C  CD  . GLU A 1 25  ? 37.606 0.636   -5.286 1.00 85.99 ? 24  GLU A CD  1 
ATOM   175  O  OE1 . GLU A 1 25  ? 38.355 -0.272  -4.861 1.00 87.31 ? 24  GLU A OE1 1 
ATOM   176  O  OE2 . GLU A 1 25  ? 37.575 0.995   -6.483 1.00 90.38 ? 24  GLU A OE2 1 
ATOM   177  N  N   . SER A 1 26  ? 32.984 -0.755  -2.510 1.00 65.43 ? 25  SER A N   1 
ATOM   178  C  CA  . SER A 1 26  ? 32.297 -1.837  -1.834 1.00 67.08 ? 25  SER A CA  1 
ATOM   179  C  C   . SER A 1 26  ? 33.289 -2.930  -1.466 1.00 67.27 ? 25  SER A C   1 
ATOM   180  O  O   . SER A 1 26  ? 33.303 -3.416  -0.342 1.00 70.80 ? 25  SER A O   1 
ATOM   181  C  CB  . SER A 1 26  ? 31.199 -2.412  -2.724 1.00 66.00 ? 25  SER A CB  1 
ATOM   182  O  OG  . SER A 1 26  ? 31.757 -3.087  -3.832 1.00 67.84 ? 25  SER A OG  1 
ATOM   183  N  N   . ASN A 1 27  ? 34.131 -3.327  -2.401 1.00 68.73 ? 26  ASN A N   1 
ATOM   184  C  CA  . ASN A 1 27  ? 35.089 -4.370  -2.073 1.00 72.04 ? 26  ASN A CA  1 
ATOM   185  C  C   . ASN A 1 27  ? 36.486 -3.774  -1.914 1.00 68.90 ? 26  ASN A C   1 
ATOM   186  O  O   . ASN A 1 27  ? 37.489 -4.425  -2.208 1.00 69.60 ? 26  ASN A O   1 
ATOM   187  C  CB  . ASN A 1 27  ? 35.069 -5.462  -3.153 1.00 78.37 ? 26  ASN A CB  1 
ATOM   188  C  CG  . ASN A 1 27  ? 35.566 -4.968  -4.495 1.00 84.74 ? 26  ASN A CG  1 
ATOM   189  O  OD1 . ASN A 1 27  ? 35.275 -3.837  -4.904 1.00 88.37 ? 26  ASN A OD1 1 
ATOM   190  N  ND2 . ASN A 1 27  ? 36.310 -5.822  -5.201 1.00 86.34 ? 26  ASN A ND2 1 
ATOM   191  N  N   . GLY A 1 28  ? 36.534 -2.531  -1.439 1.00 60.98 ? 27  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 28  ? 37.800 -1.850  -1.242 1.00 55.53 ? 27  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 28  ? 38.269 -1.893  0.206  1.00 49.87 ? 27  GLY A C   1 
ATOM   194  O  O   . GLY A 1 28  ? 37.548 -2.370  1.080  1.00 46.68 ? 27  GLY A O   1 
ATOM   195  N  N   . PRO A 1 29  ? 39.478 -1.399  0.494  1.00 49.49 ? 28  PRO A N   1 
ATOM   196  C  CA  . PRO A 1 29  ? 39.934 -1.446  1.880  1.00 44.57 ? 28  PRO A CA  1 
ATOM   197  C  C   . PRO A 1 29  ? 39.239 -0.413  2.746  1.00 40.69 ? 28  PRO A C   1 
ATOM   198  O  O   . PRO A 1 29  ? 38.673 0.578   2.253  1.00 33.65 ? 28  PRO A O   1 
ATOM   199  C  CB  . PRO A 1 29  ? 41.428 -1.187  1.751  1.00 46.12 ? 28  PRO A CB  1 
ATOM   200  C  CG  . PRO A 1 29  ? 41.458 -0.184  0.652  1.00 52.77 ? 28  PRO A CG  1 
ATOM   201  C  CD  . PRO A 1 29  ? 40.496 -0.768  -0.365 1.00 47.34 ? 28  PRO A CD  1 
ATOM   202  N  N   . VAL A 1 30  ? 39.288 -0.669  4.043  1.00 34.96 ? 29  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 30  ? 38.683 0.199   5.024  1.00 32.89 ? 29  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 30  ? 39.787 0.925   5.745  1.00 32.34 ? 29  VAL A C   1 
ATOM   205  O  O   . VAL A 1 30  ? 40.709 0.299   6.246  1.00 31.55 ? 29  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 30  ? 37.925 -0.605  6.087  1.00 33.83 ? 29  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 30  ? 37.267 0.365   7.089  1.00 22.08 ? 29  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 30  ? 36.907 -1.550  5.411  1.00 29.85 ? 29  VAL A CG2 1 
ATOM   209  N  N   . LYS A 1 31  ? 39.707 2.241   5.785  1.00 32.82 ? 30  LYS A N   1 
ATOM   210  C  CA  . LYS A 1 31  ? 40.700 2.986   6.522  1.00 36.50 ? 30  LYS A CA  1 
ATOM   211  C  C   . LYS A 1 31  ? 40.154 3.189   7.932  1.00 32.15 ? 30  LYS A C   1 
ATOM   212  O  O   . LYS A 1 31  ? 38.969 3.556   8.120  1.00 28.45 ? 30  LYS A O   1 
ATOM   213  C  CB  . LYS A 1 31  ? 41.004 4.330   5.847  1.00 42.86 ? 30  LYS A CB  1 
ATOM   214  C  CG  . LYS A 1 31  ? 42.022 4.176   4.712  1.00 55.88 ? 30  LYS A CG  1 
ATOM   215  C  CD  . LYS A 1 31  ? 42.476 5.524   4.143  1.00 65.57 ? 30  LYS A CD  1 
ATOM   216  C  CE  . LYS A 1 31  ? 43.500 5.343   3.018  1.00 69.03 ? 30  LYS A CE  1 
ATOM   217  N  NZ  . LYS A 1 31  ? 43.881 6.661   2.401  1.00 70.80 ? 30  LYS A NZ  1 
ATOM   218  N  N   . VAL A 1 32  ? 41.029 2.926   8.909  1.00 28.41 ? 31  VAL A N   1 
ATOM   219  C  CA  . VAL A 1 32  ? 40.715 3.036   10.321 1.00 28.04 ? 31  VAL A CA  1 
ATOM   220  C  C   . VAL A 1 32  ? 41.677 4.039   10.941 1.00 29.54 ? 31  VAL A C   1 
ATOM   221  O  O   . VAL A 1 32  ? 42.881 3.883   10.845 1.00 31.90 ? 31  VAL A O   1 
ATOM   222  C  CB  . VAL A 1 32  ? 40.929 1.692   11.021 1.00 27.18 ? 31  VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 32  ? 40.384 1.746   12.438 1.00 22.63 ? 31  VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 32  ? 40.225 0.587   10.237 1.00 26.98 ? 31  VAL A CG2 1 
ATOM   225  N  N   . TRP A 1 33  ? 41.170 5.062   11.604 1.00 30.88 ? 32  TRP A N   1 
ATOM   226  C  CA  . TRP A 1 33  ? 42.095 5.996   12.206 1.00 31.64 ? 32  TRP A CA  1 
ATOM   227  C  C   . TRP A 1 33  ? 41.439 6.682   13.384 1.00 31.48 ? 32  TRP A C   1 
ATOM   228  O  O   . TRP A 1 33  ? 40.216 6.777   13.487 1.00 29.26 ? 32  TRP A O   1 
ATOM   229  C  CB  . TRP A 1 33  ? 42.568 7.015   11.155 1.00 31.61 ? 32  TRP A CB  1 
ATOM   230  C  CG  . TRP A 1 33  ? 41.548 8.046   10.895 1.00 37.85 ? 32  TRP A CG  1 
ATOM   231  C  CD1 . TRP A 1 33  ? 41.410 9.245   11.541 1.00 38.71 ? 32  TRP A CD1 1 
ATOM   232  C  CD2 . TRP A 1 33  ? 40.467 7.959   9.973  1.00 37.41 ? 32  TRP A CD2 1 
ATOM   233  N  NE1 . TRP A 1 33  ? 40.307 9.906   11.077 1.00 39.87 ? 32  TRP A NE1 1 
ATOM   234  C  CE2 . TRP A 1 33  ? 39.706 9.145   10.113 1.00 33.00 ? 32  TRP A CE2 1 
ATOM   235  C  CE3 . TRP A 1 33  ? 40.061 6.996   9.044  1.00 36.47 ? 32  TRP A CE3 1 
ATOM   236  C  CZ2 . TRP A 1 33  ? 38.566 9.396   9.363  1.00 31.96 ? 32  TRP A CZ2 1 
ATOM   237  C  CZ3 . TRP A 1 33  ? 38.912 7.247   8.288  1.00 38.70 ? 32  TRP A CZ3 1 
ATOM   238  C  CH2 . TRP A 1 33  ? 38.181 8.440   8.455  1.00 34.93 ? 32  TRP A CH2 1 
ATOM   239  N  N   . GLY A 1 34  ? 42.276 7.152   14.289 1.00 32.42 ? 33  GLY A N   1 
ATOM   240  C  CA  . GLY A 1 34  ? 41.763 7.784   15.476 1.00 29.24 ? 33  GLY A CA  1 
ATOM   241  C  C   . GLY A 1 34  ? 42.845 7.757   16.526 1.00 34.20 ? 33  GLY A C   1 
ATOM   242  O  O   . GLY A 1 34  ? 44.016 7.540   16.209 1.00 33.98 ? 33  GLY A O   1 
ATOM   243  N  N   . SER A 1 35  ? 42.427 7.934   17.772 1.00 31.18 ? 34  SER A N   1 
ATOM   244  C  CA  . SER A 1 35  ? 43.330 8.018   18.894 1.00 36.10 ? 34  SER A CA  1 
ATOM   245  C  C   . SER A 1 35  ? 42.719 7.393   20.155 1.00 33.77 ? 34  SER A C   1 
ATOM   246  O  O   . SER A 1 35  ? 41.510 7.482   20.389 1.00 31.42 ? 34  SER A O   1 
ATOM   247  C  CB  . SER A 1 35  ? 43.620 9.504   19.172 1.00 35.02 ? 34  SER A CB  1 
ATOM   248  O  OG  . SER A 1 35  ? 44.650 9.626   20.127 1.00 50.20 ? 34  SER A OG  1 
ATOM   249  N  N   . ILE A 1 36  ? 43.571 6.762   20.959 1.00 32.15 ? 35  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 36  ? 43.134 6.173   22.225 1.00 28.88 ? 35  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 36  ? 44.214 6.613   23.210 1.00 28.91 ? 35  ILE A C   1 
ATOM   252  O  O   . ILE A 1 36  ? 45.411 6.583   22.894 1.00 28.14 ? 35  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 36  ? 43.101 4.635   22.177 1.00 23.20 ? 35  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 36  ? 42.357 4.159   20.926 1.00 24.57 ? 35  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 36  ? 42.458 4.086   23.455 1.00 22.98 ? 35  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 36  ? 42.571 2.654   20.633 1.00 22.90 ? 35  ILE A CD1 1 
ATOM   257  N  N   . LYS A 1 37  ? 43.795 7.023   24.393 1.00 27.18 ? 36  LYS A N   1 
ATOM   258  C  CA  . LYS A 1 37  ? 44.736 7.472   25.405 1.00 32.55 ? 36  LYS A CA  1 
ATOM   259  C  C   . LYS A 1 37  ? 44.428 6.690   26.699 1.00 30.69 ? 36  LYS A C   1 
ATOM   260  O  O   . LYS A 1 37  ? 43.461 5.938   26.742 1.00 26.61 ? 36  LYS A O   1 
ATOM   261  C  CB  . LYS A 1 37  ? 44.528 8.973   25.653 1.00 34.47 ? 36  LYS A CB  1 
ATOM   262  C  CG  . LYS A 1 37  ? 43.145 9.258   26.170 1.00 38.88 ? 36  LYS A CG  1 
ATOM   263  C  CD  . LYS A 1 37  ? 42.934 10.737  26.444 1.00 57.17 ? 36  LYS A CD  1 
ATOM   264  C  CE  . LYS A 1 37  ? 41.708 10.955  27.338 1.00 55.26 ? 36  LYS A CE  1 
ATOM   265  N  NZ  . LYS A 1 37  ? 41.373 12.397  27.443 1.00 61.80 ? 36  LYS A NZ  1 
ATOM   266  N  N   . GLY A 1 38  ? 45.262 6.875   27.728 1.00 29.93 ? 37  GLY A N   1 
ATOM   267  C  CA  . GLY A 1 38  ? 45.043 6.203   29.007 1.00 28.91 ? 37  GLY A CA  1 
ATOM   268  C  C   . GLY A 1 38  ? 45.614 4.794   29.054 1.00 27.12 ? 37  GLY A C   1 
ATOM   269  O  O   . GLY A 1 38  ? 45.386 4.052   30.017 1.00 28.96 ? 37  GLY A O   1 
ATOM   270  N  N   . LEU A 1 39  ? 46.411 4.456   28.044 1.00 26.09 ? 38  LEU A N   1 
ATOM   271  C  CA  . LEU A 1 39  ? 46.980 3.110   27.877 1.00 28.69 ? 38  LEU A CA  1 
ATOM   272  C  C   . LEU A 1 39  ? 48.383 2.887   28.459 1.00 32.82 ? 38  LEU A C   1 
ATOM   273  O  O   . LEU A 1 39  ? 49.159 3.833   28.569 1.00 28.85 ? 38  LEU A O   1 
ATOM   274  C  CB  . LEU A 1 39  ? 47.017 2.786   26.380 1.00 27.74 ? 38  LEU A CB  1 
ATOM   275  C  CG  . LEU A 1 39  ? 45.674 2.608   25.635 1.00 27.25 ? 38  LEU A CG  1 
ATOM   276  C  CD1 . LEU A 1 39  ? 45.852 2.663   24.101 1.00 24.84 ? 38  LEU A CD1 1 
ATOM   277  C  CD2 . LEU A 1 39  ? 45.081 1.243   26.036 1.00 26.26 ? 38  LEU A CD2 1 
ATOM   278  N  N   . THR A 1 40  ? 48.692 1.650   28.865 1.00 29.60 ? 39  THR A N   1 
ATOM   279  C  CA  . THR A 1 40  ? 50.029 1.351   29.357 1.00 28.04 ? 39  THR A CA  1 
ATOM   280  C  C   . THR A 1 40  ? 50.884 1.367   28.086 1.00 31.65 ? 39  THR A C   1 
ATOM   281  O  O   . THR A 1 40  ? 50.426 0.965   27.004 1.00 28.71 ? 39  THR A O   1 
ATOM   282  C  CB  . THR A 1 40  ? 50.135 -0.058  30.018 1.00 32.28 ? 39  THR A CB  1 
ATOM   283  O  OG1 . THR A 1 40  ? 49.614 -1.045  29.111 1.00 26.08 ? 39  THR A OG1 1 
ATOM   284  C  CG2 . THR A 1 40  ? 49.383 -0.100  31.383 1.00 24.34 ? 39  THR A CG2 1 
ATOM   285  N  N   . GLU A 1 41  ? 52.112 1.850   28.203 1.00 28.18 ? 40  GLU A N   1 
ATOM   286  C  CA  . GLU A 1 41  ? 52.993 1.923   27.049 1.00 32.27 ? 40  GLU A CA  1 
ATOM   287  C  C   . GLU A 1 41  ? 53.145 0.563   26.328 1.00 26.15 ? 40  GLU A C   1 
ATOM   288  O  O   . GLU A 1 41  ? 53.210 -0.478  26.962 1.00 30.98 ? 40  GLU A O   1 
ATOM   289  C  CB  . GLU A 1 41  ? 54.371 2.456   27.498 1.00 33.70 ? 40  GLU A CB  1 
ATOM   290  C  CG  . GLU A 1 41  ? 55.390 2.565   26.354 1.00 34.78 ? 40  GLU A CG  1 
ATOM   291  C  CD  . GLU A 1 41  ? 56.771 3.084   26.808 1.00 45.29 ? 40  GLU A CD  1 
ATOM   292  O  OE1 . GLU A 1 41  ? 56.972 3.247   28.028 1.00 45.10 ? 40  GLU A OE1 1 
ATOM   293  O  OE2 . GLU A 1 41  ? 57.654 3.329   25.944 1.00 46.13 ? 40  GLU A OE2 1 
ATOM   294  N  N   . GLY A 1 42  ? 53.210 0.564   25.006 1.00 28.71 ? 41  GLY A N   1 
ATOM   295  C  CA  . GLY A 1 42  ? 53.372 -0.723  24.320 1.00 28.68 ? 41  GLY A CA  1 
ATOM   296  C  C   . GLY A 1 42  ? 52.176 -1.148  23.480 1.00 23.56 ? 41  GLY A C   1 
ATOM   297  O  O   . GLY A 1 42  ? 51.226 -0.366  23.295 1.00 26.32 ? 41  GLY A O   1 
ATOM   298  N  N   . LEU A 1 43  ? 52.198 -2.405  23.024 1.00 25.74 ? 42  LEU A N   1 
ATOM   299  C  CA  . LEU A 1 43  ? 51.149 -2.967  22.144 1.00 25.07 ? 42  LEU A CA  1 
ATOM   300  C  C   . LEU A 1 43  ? 49.883 -3.442  22.866 1.00 25.44 ? 42  LEU A C   1 
ATOM   301  O  O   . LEU A 1 43  ? 49.947 -4.039  23.945 1.00 31.09 ? 42  LEU A O   1 
ATOM   302  C  CB  . LEU A 1 43  ? 51.740 -4.139  21.334 1.00 21.10 ? 42  LEU A CB  1 
ATOM   303  C  CG  . LEU A 1 43  ? 52.988 -3.867  20.518 1.00 28.87 ? 42  LEU A CG  1 
ATOM   304  C  CD1 . LEU A 1 43  ? 53.550 -5.183  19.893 1.00 24.51 ? 42  LEU A CD1 1 
ATOM   305  C  CD2 . LEU A 1 43  ? 52.603 -2.819  19.421 1.00 29.40 ? 42  LEU A CD2 1 
ATOM   306  N  N   . HIS A 1 44  ? 48.734 -3.164  22.265 1.00 27.72 ? 43  HIS A N   1 
ATOM   307  C  CA  . HIS A 1 44  ? 47.414 -3.550  22.787 1.00 24.21 ? 43  HIS A CA  1 
ATOM   308  C  C   . HIS A 1 44  ? 46.545 -4.209  21.723 1.00 23.68 ? 43  HIS A C   1 
ATOM   309  O  O   . HIS A 1 44  ? 46.351 -3.619  20.651 1.00 19.93 ? 43  HIS A O   1 
ATOM   310  C  CB  . HIS A 1 44  ? 46.682 -2.313  23.298 1.00 18.30 ? 43  HIS A CB  1 
ATOM   311  C  CG  . HIS A 1 44  ? 47.289 -1.749  24.546 1.00 26.19 ? 43  HIS A CG  1 
ATOM   312  N  ND1 . HIS A 1 44  ? 46.929 -2.187  25.806 1.00 24.45 ? 43  HIS A ND1 1 
ATOM   313  C  CD2 . HIS A 1 44  ? 48.274 -0.838  24.728 1.00 25.87 ? 43  HIS A CD2 1 
ATOM   314  C  CE1 . HIS A 1 44  ? 47.669 -1.567  26.712 1.00 24.89 ? 43  HIS A CE1 1 
ATOM   315  N  NE2 . HIS A 1 44  ? 48.496 -0.748  26.084 1.00 28.57 ? 43  HIS A NE2 1 
ATOM   316  N  N   . GLY A 1 45  ? 46.006 -5.400  22.035 1.00 20.12 ? 44  GLY A N   1 
ATOM   317  C  CA  . GLY A 1 45  ? 45.119 -6.105  21.096 1.00 20.61 ? 44  GLY A CA  1 
ATOM   318  C  C   . GLY A 1 45  ? 43.998 -5.158  20.621 1.00 28.25 ? 44  GLY A C   1 
ATOM   319  O  O   . GLY A 1 45  ? 43.419 -4.446  21.425 1.00 21.40 ? 44  GLY A O   1 
ATOM   320  N  N   . PHE A 1 46  ? 43.663 -5.188  19.331 1.00 22.20 ? 45  PHE A N   1 
ATOM   321  C  CA  . PHE A 1 46  ? 42.683 -4.266  18.753 1.00 20.54 ? 45  PHE A CA  1 
ATOM   322  C  C   . PHE A 1 46  ? 41.822 -5.151  17.872 1.00 23.02 ? 45  PHE A C   1 
ATOM   323  O  O   . PHE A 1 46  ? 42.258 -5.616  16.817 1.00 23.29 ? 45  PHE A O   1 
ATOM   324  C  CB  . PHE A 1 46  ? 43.471 -3.221  17.926 1.00 23.06 ? 45  PHE A CB  1 
ATOM   325  C  CG  . PHE A 1 46  ? 42.659 -1.993  17.524 1.00 26.54 ? 45  PHE A CG  1 
ATOM   326  C  CD1 . PHE A 1 46  ? 41.911 -1.301  18.467 1.00 25.29 ? 45  PHE A CD1 1 
ATOM   327  C  CD2 . PHE A 1 46  ? 42.681 -1.518  16.210 1.00 30.11 ? 45  PHE A CD2 1 
ATOM   328  C  CE1 . PHE A 1 46  ? 41.188 -0.132  18.124 1.00 31.02 ? 45  PHE A CE1 1 
ATOM   329  C  CE2 . PHE A 1 46  ? 41.942 -0.328  15.847 1.00 23.57 ? 45  PHE A CE2 1 
ATOM   330  C  CZ  . PHE A 1 46  ? 41.206 0.352   16.824 1.00 21.37 ? 45  PHE A CZ  1 
ATOM   331  N  N   . HIS A 1 47  ? 40.610 -5.443  18.298 1.00 26.59 ? 46  HIS A N   1 
ATOM   332  C  CA  . HIS A 1 47  ? 39.799 -6.364  17.494 1.00 22.88 ? 46  HIS A CA  1 
ATOM   333  C  C   . HIS A 1 47  ? 38.350 -5.948  17.440 1.00 26.79 ? 46  HIS A C   1 
ATOM   334  O  O   . HIS A 1 47  ? 37.875 -5.153  18.271 1.00 22.66 ? 46  HIS A O   1 
ATOM   335  C  CB  . HIS A 1 47  ? 39.794 -7.794  18.113 1.00 22.77 ? 46  HIS A CB  1 
ATOM   336  C  CG  . HIS A 1 47  ? 41.133 -8.267  18.615 1.00 27.55 ? 46  HIS A CG  1 
ATOM   337  N  ND1 . HIS A 1 47  ? 41.322 -8.716  19.902 1.00 27.41 ? 46  HIS A ND1 1 
ATOM   338  C  CD2 . HIS A 1 47  ? 42.322 -8.421  17.989 1.00 31.28 ? 46  HIS A CD2 1 
ATOM   339  C  CE1 . HIS A 1 47  ? 42.567 -9.124  20.052 1.00 31.19 ? 46  HIS A CE1 1 
ATOM   340  N  NE2 . HIS A 1 47  ? 43.194 -8.957  18.903 1.00 27.88 ? 46  HIS A NE2 1 
ATOM   341  N  N   . VAL A 1 48  ? 37.644 -6.532  16.474 1.00 24.45 ? 47  VAL A N   1 
ATOM   342  C  CA  . VAL A 1 48  ? 36.185 -6.320  16.355 1.00 20.86 ? 47  VAL A CA  1 
ATOM   343  C  C   . VAL A 1 48  ? 35.596 -7.625  16.916 1.00 23.46 ? 47  VAL A C   1 
ATOM   344  O  O   . VAL A 1 48  ? 35.932 -8.745  16.452 1.00 22.41 ? 47  VAL A O   1 
ATOM   345  C  CB  . VAL A 1 48  ? 35.730 -6.164  14.894 1.00 24.79 ? 47  VAL A CB  1 
ATOM   346  C  CG1 . VAL A 1 48  ? 34.191 -6.149  14.827 1.00 21.74 ? 47  VAL A CG1 1 
ATOM   347  C  CG2 . VAL A 1 48  ? 36.288 -4.816  14.275 1.00 19.53 ? 47  VAL A CG2 1 
ATOM   348  N  N   . HIS A 1 49  ? 34.763 -7.490  17.918 1.00 22.12 ? 48  HIS A N   1 
ATOM   349  C  CA  . HIS A 1 49  ? 34.109 -8.612  18.532 1.00 21.16 ? 48  HIS A CA  1 
ATOM   350  C  C   . HIS A 1 49  ? 32.676 -8.684  18.003 1.00 26.44 ? 48  HIS A C   1 
ATOM   351  O  O   . HIS A 1 49  ? 32.165 -7.725  17.501 1.00 23.93 ? 48  HIS A O   1 
ATOM   352  C  CB  . HIS A 1 49  ? 34.181 -8.497  20.062 1.00 21.52 ? 48  HIS A CB  1 
ATOM   353  C  CG  . HIS A 1 49  ? 35.530 -8.812  20.651 1.00 22.66 ? 48  HIS A CG  1 
ATOM   354  N  ND1 . HIS A 1 49  ? 35.704 -9.751  21.636 1.00 26.37 ? 48  HIS A ND1 1 
ATOM   355  C  CD2 . HIS A 1 49  ? 36.755 -8.298  20.411 1.00 20.65 ? 48  HIS A CD2 1 
ATOM   356  C  CE1 . HIS A 1 49  ? 36.977 -9.814  21.969 1.00 28.77 ? 48  HIS A CE1 1 
ATOM   357  N  NE2 . HIS A 1 49  ? 37.642 -8.942  21.238 1.00 30.42 ? 48  HIS A NE2 1 
ATOM   358  N  N   . GLU A 1 50  ? 32.056 -9.841  18.104 1.00 23.80 ? 49  GLU A N   1 
ATOM   359  C  CA  . GLU A 1 50  ? 30.924 -10.199 17.279 1.00 24.84 ? 49  GLU A CA  1 
ATOM   360  C  C   . GLU A 1 50  ? 29.629 -9.400  17.524 1.00 21.72 ? 49  GLU A C   1 
ATOM   361  O  O   . GLU A 1 50  ? 28.927 -9.067  16.594 1.00 25.70 ? 49  GLU A O   1 
ATOM   362  C  CB  . GLU A 1 50  ? 30.664 -11.687 17.378 1.00 26.80 ? 49  GLU A CB  1 
ATOM   363  C  CG  . GLU A 1 50  ? 29.623 -12.212 16.446 1.00 28.83 ? 49  GLU A CG  1 
ATOM   364  C  CD  . GLU A 1 50  ? 29.373 -13.694 16.594 1.00 31.41 ? 49  GLU A CD  1 
ATOM   365  O  OE1 . GLU A 1 50  ? 28.479 -14.178 15.916 1.00 39.20 ? 49  GLU A OE1 1 
ATOM   366  O  OE2 . GLU A 1 50  ? 30.044 -14.356 17.379 1.00 30.85 ? 49  GLU A OE2 1 
ATOM   367  N  N   . PHE A 1 51  ? 29.328 -9.086  18.771 1.00 23.18 ? 50  PHE A N   1 
ATOM   368  C  CA  . PHE A 1 51  ? 28.052 -8.490  19.097 1.00 23.59 ? 50  PHE A CA  1 
ATOM   369  C  C   . PHE A 1 51  ? 28.185 -7.049  19.538 1.00 26.23 ? 50  PHE A C   1 
ATOM   370  O  O   . PHE A 1 51  ? 29.031 -6.742  20.330 1.00 21.94 ? 50  PHE A O   1 
ATOM   371  C  CB  . PHE A 1 51  ? 27.302 -9.321  20.150 1.00 28.49 ? 50  PHE A CB  1 
ATOM   372  C  CG  . PHE A 1 51  ? 27.190 -10.773 19.807 1.00 29.14 ? 50  PHE A CG  1 
ATOM   373  C  CD1 . PHE A 1 51  ? 26.408 -11.183 18.761 1.00 25.63 ? 50  PHE A CD1 1 
ATOM   374  C  CD2 . PHE A 1 51  ? 27.883 -11.720 20.525 1.00 31.74 ? 50  PHE A CD2 1 
ATOM   375  C  CE1 . PHE A 1 51  ? 26.320 -12.495 18.439 1.00 30.06 ? 50  PHE A CE1 1 
ATOM   376  C  CE2 . PHE A 1 51  ? 27.798 -13.028 20.198 1.00 26.06 ? 50  PHE A CE2 1 
ATOM   377  C  CZ  . PHE A 1 51  ? 27.018 -13.418 19.156 1.00 28.17 ? 50  PHE A CZ  1 
ATOM   378  N  N   . GLY A 1 52  ? 27.332 -6.178  19.005 1.00 23.64 ? 51  GLY A N   1 
ATOM   379  C  CA  . GLY A 1 52  ? 27.289 -4.767  19.387 1.00 21.12 ? 51  GLY A CA  1 
ATOM   380  C  C   . GLY A 1 52  ? 26.289 -4.676  20.533 1.00 26.14 ? 51  GLY A C   1 
ATOM   381  O  O   . GLY A 1 52  ? 25.322 -3.908  20.516 1.00 26.20 ? 51  GLY A O   1 
ATOM   382  N  N   . ASP A 1 53  ? 26.524 -5.506  21.544 1.00 27.09 ? 52  ASP A N   1 
ATOM   383  C  CA  . ASP A 1 53  ? 25.637 -5.611  22.707 1.00 23.31 ? 52  ASP A CA  1 
ATOM   384  C  C   . ASP A 1 53  ? 26.340 -4.974  23.885 1.00 27.10 ? 52  ASP A C   1 
ATOM   385  O  O   . ASP A 1 53  ? 27.309 -5.498  24.392 1.00 25.51 ? 52  ASP A O   1 
ATOM   386  C  CB  . ASP A 1 53  ? 25.355 -7.079  22.981 1.00 24.83 ? 52  ASP A CB  1 
ATOM   387  C  CG  . ASP A 1 53  ? 24.405 -7.308  24.157 1.00 26.77 ? 52  ASP A CG  1 
ATOM   388  O  OD1 . ASP A 1 53  ? 23.753 -8.377  24.117 1.00 27.19 ? 52  ASP A OD1 1 
ATOM   389  O  OD2 . ASP A 1 53  ? 24.331 -6.482  25.106 1.00 25.27 ? 52  ASP A OD2 1 
ATOM   390  N  N   . ASN A 1 54  ? 25.801 -3.855  24.334 1.00 26.43 ? 53  ASN A N   1 
ATOM   391  C  CA  . ASN A 1 54  ? 26.377 -3.082  25.421 1.00 29.16 ? 53  ASN A CA  1 
ATOM   392  C  C   . ASN A 1 54  ? 25.579 -3.268  26.724 1.00 28.35 ? 53  ASN A C   1 
ATOM   393  O  O   . ASN A 1 54  ? 25.725 -2.465  27.660 1.00 30.03 ? 53  ASN A O   1 
ATOM   394  C  CB  . ASN A 1 54  ? 26.412 -1.592  24.939 1.00 31.21 ? 53  ASN A CB  1 
ATOM   395  C  CG  . ASN A 1 54  ? 26.896 -0.616  26.000 1.00 39.90 ? 53  ASN A CG  1 
ATOM   396  O  OD1 . ASN A 1 54  ? 26.170 0.307   26.384 1.00 43.91 ? 53  ASN A OD1 1 
ATOM   397  N  ND2 . ASN A 1 54  ? 28.120 -0.800  26.472 1.00 37.89 ? 53  ASN A ND2 1 
ATOM   398  N  N   . THR A 1 55  ? 24.750 -4.319  26.809 1.00 23.31 ? 54  THR A N   1 
ATOM   399  C  CA  . THR A 1 55  ? 23.985 -4.524  28.036 1.00 24.92 ? 54  THR A CA  1 
ATOM   400  C  C   . THR A 1 55  ? 24.873 -4.726  29.284 1.00 28.06 ? 54  THR A C   1 
ATOM   401  O  O   . THR A 1 55  ? 24.482 -4.374  30.383 1.00 26.18 ? 54  THR A O   1 
ATOM   402  C  CB  . THR A 1 55  ? 22.975 -5.720  27.952 1.00 25.06 ? 54  THR A CB  1 
ATOM   403  O  OG1 . THR A 1 55  ? 23.670 -6.944  27.646 1.00 26.45 ? 54  THR A OG1 1 
ATOM   404  C  CG2 . THR A 1 55  ? 21.867 -5.431  26.864 1.00 25.99 ? 54  THR A CG2 1 
ATOM   405  N  N   . ALA A 1 56  ? 26.072 -5.263  29.114 1.00 27.20 ? 55  ALA A N   1 
ATOM   406  C  CA  . ALA A 1 56  ? 26.970 -5.478  30.265 1.00 30.35 ? 55  ALA A CA  1 
ATOM   407  C  C   . ALA A 1 56  ? 28.273 -4.858  29.818 1.00 30.08 ? 55  ALA A C   1 
ATOM   408  O  O   . ALA A 1 56  ? 29.367 -5.421  29.952 1.00 31.15 ? 55  ALA A O   1 
ATOM   409  C  CB  . ALA A 1 56  ? 27.129 -6.991  30.528 1.00 27.01 ? 55  ALA A CB  1 
ATOM   410  N  N   . GLY A 1 57  ? 28.134 -3.694  29.220 1.00 29.78 ? 56  GLY A N   1 
ATOM   411  C  CA  . GLY A 1 57  ? 29.306 -3.028  28.706 1.00 31.41 ? 56  GLY A CA  1 
ATOM   412  C  C   . GLY A 1 57  ? 30.101 -3.926  27.785 1.00 26.32 ? 56  GLY A C   1 
ATOM   413  O  O   . GLY A 1 57  ? 29.568 -4.715  26.979 1.00 28.75 ? 56  GLY A O   1 
ATOM   414  N  N   . CYS A 1 58  ? 31.407 -3.867  27.957 1.00 28.13 ? 57  CYS A N   1 
ATOM   415  C  CA  . CYS A 1 58  ? 32.318 -4.615  27.132 1.00 27.88 ? 57  CYS A CA  1 
ATOM   416  C  C   . CYS A 1 58  ? 32.128 -6.112  27.300 1.00 27.78 ? 57  CYS A C   1 
ATOM   417  O  O   . CYS A 1 58  ? 32.456 -6.883  26.429 1.00 25.87 ? 57  CYS A O   1 
ATOM   418  C  CB  . CYS A 1 58  ? 33.744 -4.230  27.451 1.00 33.37 ? 57  CYS A CB  1 
ATOM   419  S  SG  . CYS A 1 58  ? 34.243 -2.623  26.893 1.00 33.29 ? 57  CYS A SG  1 
ATOM   420  N  N   . THR A 1 59  ? 31.585 -6.513  28.433 1.00 27.18 ? 58  THR A N   1 
ATOM   421  C  CA  . THR A 1 59  ? 31.439 -7.957  28.684 1.00 29.17 ? 58  THR A CA  1 
ATOM   422  C  C   . THR A 1 59  ? 30.515 -8.715  27.721 1.00 26.04 ? 58  THR A C   1 
ATOM   423  O  O   . THR A 1 59  ? 30.772 -9.869  27.412 1.00 25.90 ? 58  THR A O   1 
ATOM   424  C  CB  . THR A 1 59  ? 30.982 -8.202  30.157 1.00 32.48 ? 58  THR A CB  1 
ATOM   425  O  OG1 . THR A 1 59  ? 31.866 -7.489  31.036 1.00 30.14 ? 58  THR A OG1 1 
ATOM   426  C  CG2 . THR A 1 59  ? 31.010 -9.759  30.515 1.00 24.54 ? 58  THR A CG2 1 
ATOM   427  N  N   . SER A 1 60  ? 29.463 -8.069  27.221 1.00 25.75 ? 59  SER A N   1 
ATOM   428  C  CA  . SER A 1 60  ? 28.506 -8.712  26.304 1.00 22.13 ? 59  SER A CA  1 
ATOM   429  C  C   . SER A 1 60  ? 28.906 -8.681  24.829 1.00 21.74 ? 59  SER A C   1 
ATOM   430  O  O   . SER A 1 60  ? 28.119 -9.087  23.983 1.00 22.51 ? 59  SER A O   1 
ATOM   431  C  CB  . SER A 1 60  ? 27.113 -8.056  26.443 1.00 28.99 ? 59  SER A CB  1 
ATOM   432  O  OG  . SER A 1 60  ? 27.234 -6.678  26.791 1.00 25.10 ? 59  SER A OG  1 
ATOM   433  N  N   . ALA A 1 61  ? 30.127 -8.238  24.519 1.00 25.48 ? 60  ALA A N   1 
ATOM   434  C  CA  . ALA A 1 61  ? 30.561 -8.160  23.115 1.00 28.36 ? 60  ALA A CA  1 
ATOM   435  C  C   . ALA A 1 61  ? 30.843 -9.515  22.459 1.00 29.60 ? 60  ALA A C   1 
ATOM   436  O  O   . ALA A 1 61  ? 30.947 -9.605  21.234 1.00 27.48 ? 60  ALA A O   1 
ATOM   437  C  CB  . ALA A 1 61  ? 31.806 -7.275  22.989 1.00 23.18 ? 60  ALA A CB  1 
ATOM   438  N  N   . GLY A 1 62  ? 30.984 -10.568 23.258 1.00 28.79 ? 61  GLY A N   1 
ATOM   439  C  CA  . GLY A 1 62  ? 31.251 -11.880 22.655 1.00 26.87 ? 61  GLY A CA  1 
ATOM   440  C  C   . GLY A 1 62  ? 32.687 -12.083 22.183 1.00 26.31 ? 61  GLY A C   1 
ATOM   441  O  O   . GLY A 1 62  ? 33.603 -11.301 22.516 1.00 25.32 ? 61  GLY A O   1 
ATOM   442  N  N   . PRO A 1 63  ? 32.907 -13.125 21.374 1.00 27.08 ? 62  PRO A N   1 
ATOM   443  C  CA  . PRO A 1 63  ? 34.217 -13.481 20.826 1.00 28.25 ? 62  PRO A CA  1 
ATOM   444  C  C   . PRO A 1 63  ? 34.534 -12.654 19.584 1.00 32.96 ? 62  PRO A C   1 
ATOM   445  O  O   . PRO A 1 63  ? 33.700 -11.851 19.110 1.00 25.04 ? 62  PRO A O   1 
ATOM   446  C  CB  . PRO A 1 63  ? 34.047 -14.979 20.485 1.00 30.37 ? 62  PRO A CB  1 
ATOM   447  C  CG  . PRO A 1 63  ? 32.636 -14.983 19.929 1.00 30.40 ? 62  PRO A CG  1 
ATOM   448  C  CD  . PRO A 1 63  ? 31.875 -14.106 20.973 1.00 22.89 ? 62  PRO A CD  1 
ATOM   449  N  N   . HIS A 1 64  ? 35.741 -12.835 19.057 1.00 23.69 ? 63  HIS A N   1 
ATOM   450  C  CA  . HIS A 1 64  ? 36.087 -12.122 17.837 1.00 28.75 ? 63  HIS A CA  1 
ATOM   451  C  C   . HIS A 1 64  ? 35.100 -12.428 16.720 1.00 29.64 ? 63  HIS A C   1 
ATOM   452  O  O   . HIS A 1 64  ? 34.598 -13.543 16.622 1.00 31.80 ? 63  HIS A O   1 
ATOM   453  C  CB  . HIS A 1 64  ? 37.498 -12.504 17.382 1.00 26.53 ? 63  HIS A CB  1 
ATOM   454  C  CG  . HIS A 1 64  ? 38.563 -11.935 18.251 1.00 32.28 ? 63  HIS A CG  1 
ATOM   455  N  ND1 . HIS A 1 64  ? 39.905 -12.164 18.041 1.00 33.34 ? 63  HIS A ND1 1 
ATOM   456  C  CD2 . HIS A 1 64  ? 38.481 -11.148 19.349 1.00 33.00 ? 63  HIS A CD2 1 
ATOM   457  C  CE1 . HIS A 1 64  ? 40.605 -11.546 18.972 1.00 37.62 ? 63  HIS A CE1 1 
ATOM   458  N  NE2 . HIS A 1 64  ? 39.765 -10.918 19.776 1.00 35.82 ? 63  HIS A NE2 1 
ATOM   459  N  N   . PHE A 1 65  ? 34.833 -11.428 15.883 1.00 28.25 ? 64  PHE A N   1 
ATOM   460  C  CA  . PHE A 1 65  ? 33.956 -11.562 14.728 1.00 27.03 ? 64  PHE A CA  1 
ATOM   461  C  C   . PHE A 1 65  ? 34.723 -12.482 13.763 1.00 33.03 ? 64  PHE A C   1 
ATOM   462  O  O   . PHE A 1 65  ? 35.857 -12.208 13.331 1.00 30.24 ? 64  PHE A O   1 
ATOM   463  C  CB  . PHE A 1 65  ? 33.704 -10.177 14.100 1.00 24.88 ? 64  PHE A CB  1 
ATOM   464  C  CG  . PHE A 1 65  ? 32.976 -10.213 12.760 1.00 26.36 ? 64  PHE A CG  1 
ATOM   465  C  CD1 . PHE A 1 65  ? 33.433 -9.449  11.700 1.00 23.80 ? 64  PHE A CD1 1 
ATOM   466  C  CD2 . PHE A 1 65  ? 31.872 -11.011 12.567 1.00 26.61 ? 64  PHE A CD2 1 
ATOM   467  C  CE1 . PHE A 1 65  ? 32.796 -9.482  10.443 1.00 33.78 ? 64  PHE A CE1 1 
ATOM   468  C  CE2 . PHE A 1 65  ? 31.234 -11.064 11.339 1.00 32.43 ? 64  PHE A CE2 1 
ATOM   469  C  CZ  . PHE A 1 65  ? 31.693 -10.300 10.269 1.00 31.91 ? 64  PHE A CZ  1 
ATOM   470  N  N   . ASN A 1 66  ? 34.101 -13.599 13.459 1.00 35.14 ? 65  ASN A N   1 
ATOM   471  C  CA  . ASN A 1 66  ? 34.734 -14.591 12.621 1.00 40.11 ? 65  ASN A CA  1 
ATOM   472  C  C   . ASN A 1 66  ? 33.659 -15.232 11.758 1.00 45.53 ? 65  ASN A C   1 
ATOM   473  O  O   . ASN A 1 66  ? 33.185 -16.335 12.054 1.00 45.65 ? 65  ASN A O   1 
ATOM   474  C  CB  . ASN A 1 66  ? 35.411 -15.602 13.535 1.00 43.91 ? 65  ASN A CB  1 
ATOM   475  C  CG  . ASN A 1 66  ? 36.022 -16.738 12.789 1.00 49.67 ? 65  ASN A CG  1 
ATOM   476  O  OD1 . ASN A 1 66  ? 36.377 -16.607 11.616 1.00 60.65 ? 65  ASN A OD1 1 
ATOM   477  N  ND2 . ASN A 1 66  ? 36.166 -17.868 13.459 1.00 50.60 ? 65  ASN A ND2 1 
ATOM   478  N  N   . PRO A 1 67  ? 33.247 -14.528 10.686 1.00 45.76 ? 66  PRO A N   1 
ATOM   479  C  CA  . PRO A 1 67  ? 32.217 -15.007 9.758  1.00 53.14 ? 66  PRO A CA  1 
ATOM   480  C  C   . PRO A 1 67  ? 32.526 -16.394 9.150  1.00 60.60 ? 66  PRO A C   1 
ATOM   481  O  O   . PRO A 1 67  ? 31.604 -17.144 8.797  1.00 63.62 ? 66  PRO A O   1 
ATOM   482  C  CB  . PRO A 1 67  ? 32.123 -13.879 8.723  1.00 51.09 ? 66  PRO A CB  1 
ATOM   483  C  CG  . PRO A 1 67  ? 33.493 -13.270 8.730  1.00 48.23 ? 66  PRO A CG  1 
ATOM   484  C  CD  . PRO A 1 67  ? 33.901 -13.302 10.184 1.00 45.85 ? 66  PRO A CD  1 
ATOM   485  N  N   . LEU A 1 68  ? 33.807 -16.743 9.045  1.00 63.66 ? 67  LEU A N   1 
ATOM   486  C  CA  . LEU A 1 68  ? 34.211 -18.068 8.533  1.00 72.38 ? 67  LEU A CA  1 
ATOM   487  C  C   . LEU A 1 68  ? 33.590 -18.514 7.189  1.00 72.03 ? 67  LEU A C   1 
ATOM   488  O  O   . LEU A 1 68  ? 33.311 -19.726 7.093  1.00 75.15 ? 67  LEU A O   1 
ATOM   489  C  CB  . LEU A 1 68  ? 33.866 -19.151 9.574  1.00 73.80 ? 67  LEU A CB  1 
ATOM   490  C  CG  . LEU A 1 68  ? 34.399 -19.219 11.011 1.00 73.47 ? 67  LEU A CG  1 
ATOM   491  C  CD1 . LEU A 1 68  ? 33.296 -19.799 11.910 1.00 69.46 ? 67  LEU A CD1 1 
ATOM   492  C  CD2 . LEU A 1 68  ? 35.676 -20.070 11.082 1.00 69.49 ? 67  LEU A CD2 1 
ATOM   493  N  N   . ARG A 1 80  ? 44.286 -15.430 11.338 1.00 49.71 ? 79  ARG A N   1 
ATOM   494  C  CA  . ARG A 1 80  ? 43.535 -14.703 12.341 1.00 47.44 ? 79  ARG A CA  1 
ATOM   495  C  C   . ARG A 1 80  ? 42.130 -14.358 11.885 1.00 44.31 ? 79  ARG A C   1 
ATOM   496  O  O   . ARG A 1 80  ? 41.878 -14.228 10.698 1.00 54.13 ? 79  ARG A O   1 
ATOM   497  C  CB  . ARG A 1 80  ? 44.250 -13.424 12.708 1.00 45.15 ? 79  ARG A CB  1 
ATOM   498  C  CG  . ARG A 1 80  ? 45.463 -13.622 13.524 1.00 54.57 ? 79  ARG A CG  1 
ATOM   499  C  CD  . ARG A 1 80  ? 46.068 -12.302 13.849 1.00 55.67 ? 79  ARG A CD  1 
ATOM   500  N  NE  . ARG A 1 80  ? 47.057 -11.938 12.860 1.00 55.84 ? 79  ARG A NE  1 
ATOM   501  C  CZ  . ARG A 1 80  ? 47.066 -10.790 12.213 1.00 58.53 ? 79  ARG A CZ  1 
ATOM   502  N  NH1 . ARG A 1 80  ? 48.021 -10.559 11.347 1.00 53.55 ? 79  ARG A NH1 1 
ATOM   503  N  NH2 . ARG A 1 80  ? 46.127 -9.879  12.438 1.00 54.01 ? 79  ARG A NH2 1 
ATOM   504  N  N   . SER A 1 81  ? 41.232 -14.179 12.846 1.00 34.87 ? 80  SER A N   1 
ATOM   505  C  CA  . SER A 1 81  ? 39.797 -13.926 12.545 1.00 34.55 ? 80  SER A CA  1 
ATOM   506  C  C   . SER A 1 81  ? 39.646 -12.663 11.687 1.00 27.61 ? 80  SER A C   1 
ATOM   507  O  O   . SER A 1 81  ? 40.574 -11.850 11.581 1.00 27.59 ? 80  SER A O   1 
ATOM   508  C  CB  . SER A 1 81  ? 39.045 -13.760 13.856 1.00 31.48 ? 80  SER A CB  1 
ATOM   509  O  OG  . SER A 1 81  ? 39.531 -12.615 14.526 1.00 35.22 ? 80  SER A OG  1 
ATOM   510  N  N   . VAL A 1 82  ? 38.476 -12.495 11.083 1.00 29.83 ? 81  VAL A N   1 
ATOM   511  C  CA  . VAL A 1 82  ? 38.223 -11.300 10.284 1.00 32.19 ? 81  VAL A CA  1 
ATOM   512  C  C   . VAL A 1 82  ? 38.249 -10.084 11.238 1.00 31.76 ? 81  VAL A C   1 
ATOM   513  O  O   . VAL A 1 82  ? 38.697 -8.996  10.869 1.00 30.91 ? 81  VAL A O   1 
ATOM   514  C  CB  . VAL A 1 82  ? 36.833 -11.386 9.581  1.00 34.78 ? 81  VAL A CB  1 
ATOM   515  C  CG1 . VAL A 1 82  ? 36.370 -9.972  9.106  1.00 30.58 ? 81  VAL A CG1 1 
ATOM   516  C  CG2 . VAL A 1 82  ? 36.930 -12.354 8.336  1.00 34.84 ? 81  VAL A CG2 1 
ATOM   517  N  N   . GLY A 1 83  ? 37.797 -10.286 12.478 1.00 31.37 ? 82  GLY A N   1 
ATOM   518  C  CA  . GLY A 1 83  ? 37.787 -9.184  13.432 1.00 29.91 ? 82  GLY A CA  1 
ATOM   519  C  C   . GLY A 1 83  ? 39.145 -8.793  14.008 1.00 33.74 ? 82  GLY A C   1 
ATOM   520  O  O   . GLY A 1 83  ? 39.279 -7.749  14.659 1.00 30.82 ? 82  GLY A O   1 
ATOM   521  N  N   . SER A 1 84  ? 40.170 -9.590  13.743 1.00 28.92 ? 83  SER A N   1 
ATOM   522  C  CA  . SER A 1 84  ? 41.489 -9.290  14.311 1.00 35.27 ? 83  SER A CA  1 
ATOM   523  C  C   . SER A 1 84  ? 42.215 -8.212  13.533 1.00 35.70 ? 83  SER A C   1 
ATOM   524  O  O   . SER A 1 84  ? 42.703 -8.444  12.425 1.00 32.68 ? 83  SER A O   1 
ATOM   525  C  CB  . SER A 1 84  ? 42.364 -10.549 14.383 1.00 37.92 ? 83  SER A CB  1 
ATOM   526  O  OG  . SER A 1 84  ? 43.530 -10.286 15.144 1.00 45.45 ? 83  SER A OG  1 
ATOM   527  N  N   . LEU A 1 85  ? 42.276 -7.025  14.133 1.00 23.63 ? 84  LEU A N   1 
ATOM   528  C  CA  . LEU A 1 85  ? 42.926 -5.897  13.497 1.00 31.06 ? 84  LEU A CA  1 
ATOM   529  C  C   . LEU A 1 85  ? 44.405 -5.777  13.864 1.00 31.45 ? 84  LEU A C   1 
ATOM   530  O  O   . LEU A 1 85  ? 45.087 -4.873  13.394 1.00 33.20 ? 84  LEU A O   1 
ATOM   531  C  CB  . LEU A 1 85  ? 42.202 -4.608  13.882 1.00 29.81 ? 84  LEU A CB  1 
ATOM   532  C  CG  . LEU A 1 85  ? 40.780 -4.479  13.304 1.00 36.63 ? 84  LEU A CG  1 
ATOM   533  C  CD1 . LEU A 1 85  ? 40.134 -3.195  13.805 1.00 34.26 ? 84  LEU A CD1 1 
ATOM   534  C  CD2 . LEU A 1 85  ? 40.831 -4.515  11.790 1.00 38.91 ? 84  LEU A CD2 1 
ATOM   535  N  N   . GLY A 1 86  ? 44.882 -6.679  14.706 1.00 25.50 ? 85  GLY A N   1 
ATOM   536  C  CA  . GLY A 1 86  ? 46.275 -6.638  15.135 1.00 25.08 ? 85  GLY A CA  1 
ATOM   537  C  C   . GLY A 1 86  ? 46.400 -5.875  16.454 1.00 22.85 ? 85  GLY A C   1 
ATOM   538  O  O   . GLY A 1 86  ? 45.597 -6.043  17.347 1.00 23.55 ? 85  GLY A O   1 
ATOM   539  N  N   . ASN A 1 87  ? 47.407 -5.027  16.540 1.00 25.78 ? 86  ASN A N   1 
ATOM   540  C  CA  . ASN A 1 87  ? 47.665 -4.218  17.724 1.00 25.91 ? 86  ASN A CA  1 
ATOM   541  C  C   . ASN A 1 87  ? 47.659 -2.725  17.424 1.00 26.15 ? 86  ASN A C   1 
ATOM   542  O  O   . ASN A 1 87  ? 47.944 -2.316  16.331 1.00 27.48 ? 86  ASN A O   1 
ATOM   543  C  CB  . ASN A 1 87  ? 49.009 -4.582  18.354 1.00 30.58 ? 86  ASN A CB  1 
ATOM   544  C  CG  . ASN A 1 87  ? 49.004 -5.937  19.039 1.00 26.79 ? 86  ASN A CG  1 
ATOM   545  O  OD1 . ASN A 1 87  ? 48.296 -6.158  19.988 1.00 24.34 ? 86  ASN A OD1 1 
ATOM   546  N  ND2 . ASN A 1 87  ? 49.820 -6.833  18.546 1.00 27.06 ? 86  ASN A ND2 1 
ATOM   547  N  N   . VAL A 1 88  ? 47.338 -1.921  18.421 1.00 25.75 ? 87  VAL A N   1 
ATOM   548  C  CA  . VAL A 1 88  ? 47.688 -0.522  18.407 1.00 25.67 ? 87  VAL A CA  1 
ATOM   549  C  C   . VAL A 1 88  ? 48.832 -0.288  19.392 1.00 29.61 ? 87  VAL A C   1 
ATOM   550  O  O   . VAL A 1 88  ? 49.053 -1.078  20.278 1.00 26.83 ? 87  VAL A O   1 
ATOM   551  C  CB  . VAL A 1 88  ? 46.470 0.387   18.723 1.00 22.75 ? 87  VAL A CB  1 
ATOM   552  C  CG1 . VAL A 1 88  ? 45.329 0.128   17.777 1.00 20.68 ? 87  VAL A CG1 1 
ATOM   553  C  CG2 . VAL A 1 88  ? 46.014 0.196   20.119 1.00 28.43 ? 87  VAL A CG2 1 
ATOM   554  N  N   . THR A 1 89  ? 49.550 0.803   19.209 1.00 28.15 ? 88  THR A N   1 
ATOM   555  C  CA  . THR A 1 89  ? 50.797 1.046   19.914 1.00 30.37 ? 88  THR A CA  1 
ATOM   556  C  C   . THR A 1 89  ? 50.699 2.301   20.766 1.00 27.18 ? 88  THR A C   1 
ATOM   557  O  O   . THR A 1 89  ? 50.573 3.379   20.246 1.00 28.60 ? 88  THR A O   1 
ATOM   558  C  CB  . THR A 1 89  ? 51.958 1.161   18.920 1.00 31.21 ? 88  THR A CB  1 
ATOM   559  O  OG1 . THR A 1 89  ? 52.066 -0.043  18.176 1.00 28.08 ? 88  THR A OG1 1 
ATOM   560  C  CG2 . THR A 1 89  ? 53.258 1.449   19.622 1.00 38.01 ? 88  THR A CG2 1 
ATOM   561  N  N   . ALA A 1 90  ? 50.730 2.143   22.079 1.00 28.26 ? 89  ALA A N   1 
ATOM   562  C  CA  . ALA A 1 90  ? 50.667 3.285   22.999 1.00 28.16 ? 89  ALA A CA  1 
ATOM   563  C  C   . ALA A 1 90  ? 52.094 3.754   23.316 1.00 33.06 ? 89  ALA A C   1 
ATOM   564  O  O   . ALA A 1 90  ? 52.979 2.921   23.599 1.00 33.19 ? 89  ALA A O   1 
ATOM   565  C  CB  . ALA A 1 90  ? 49.981 2.897   24.297 1.00 23.53 ? 89  ALA A CB  1 
ATOM   566  N  N   . ASP A 1 91  ? 52.303 5.070   23.260 1.00 34.97 ? 90  ASP A N   1 
ATOM   567  C  CA  . ASP A 1 91  ? 53.605 5.672   23.579 1.00 40.26 ? 90  ASP A CA  1 
ATOM   568  C  C   . ASP A 1 91  ? 53.694 5.807   25.116 1.00 40.57 ? 90  ASP A C   1 
ATOM   569  O  O   . ASP A 1 91  ? 52.734 5.459   25.848 1.00 31.45 ? 90  ASP A O   1 
ATOM   570  C  CB  . ASP A 1 91  ? 53.721 7.068   22.928 1.00 42.66 ? 90  ASP A CB  1 
ATOM   571  C  CG  . ASP A 1 91  ? 52.692 8.062   23.481 1.00 44.35 ? 90  ASP A CG  1 
ATOM   572  O  OD1 . ASP A 1 91  ? 52.290 7.930   24.652 1.00 45.43 ? 90  ASP A OD1 1 
ATOM   573  O  OD2 . ASP A 1 91  ? 52.282 8.989   22.745 1.00 51.78 ? 90  ASP A OD2 1 
ATOM   574  N  N   . LYS A 1 92  ? 54.819 6.335   25.604 1.00 39.95 ? 91  LYS A N   1 
ATOM   575  C  CA  . LYS A 1 92  ? 55.023 6.489   27.047 1.00 38.72 ? 91  LYS A CA  1 
ATOM   576  C  C   . LYS A 1 92  ? 54.022 7.424   27.697 1.00 36.55 ? 91  LYS A C   1 
ATOM   577  O  O   . LYS A 1 92  ? 53.825 7.376   28.897 1.00 41.46 ? 91  LYS A O   1 
ATOM   578  C  CB  . LYS A 1 92  ? 56.451 6.970   27.336 1.00 44.50 ? 91  LYS A CB  1 
ATOM   579  C  CG  . LYS A 1 92  ? 56.781 8.301   26.685 1.00 60.36 ? 91  LYS A CG  1 
ATOM   580  C  CD  . LYS A 1 92  ? 58.289 8.491   26.493 1.00 64.64 ? 91  LYS A CD  1 
ATOM   581  C  CE  . LYS A 1 92  ? 58.637 9.962   26.273 1.00 66.40 ? 91  LYS A CE  1 
ATOM   582  N  NZ  . LYS A 1 92  ? 58.463 10.756  27.527 1.00 60.55 ? 91  LYS A NZ  1 
ATOM   583  N  N   . ASP A 1 93  ? 53.388 8.277   26.908 1.00 31.86 ? 92  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 93  ? 52.373 9.191   27.431 1.00 42.26 ? 92  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 93  ? 51.010 8.476   27.529 1.00 40.83 ? 92  ASP A C   1 
ATOM   586  O  O   . ASP A 1 93  ? 50.033 9.062   28.003 1.00 41.79 ? 92  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 93  ? 52.250 10.429  26.522 1.00 45.82 ? 92  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 93  ? 53.538 11.306  26.513 1.00 63.70 ? 92  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 93  ? 54.494 11.013  27.282 1.00 60.15 ? 92  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 93  ? 53.592 12.294  25.735 1.00 66.04 ? 92  ASP A OD2 1 
ATOM   591  N  N   . GLY A 1 94  ? 50.944 7.225   27.052 1.00 37.11 ? 93  GLY A N   1 
ATOM   592  C  CA  . GLY A 1 94  ? 49.713 6.436   27.125 1.00 30.35 ? 93  GLY A CA  1 
ATOM   593  C  C   . GLY A 1 94  ? 48.782 6.576   25.935 1.00 32.80 ? 93  GLY A C   1 
ATOM   594  O  O   . GLY A 1 94  ? 47.651 6.045   25.905 1.00 30.29 ? 93  GLY A O   1 
ATOM   595  N  N   . VAL A 1 95  ? 49.280 7.269   24.920 1.00 31.70 ? 94  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 95  ? 48.519 7.522   23.715 1.00 30.17 ? 94  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 95  ? 48.897 6.652   22.516 1.00 28.11 ? 94  VAL A C   1 
ATOM   598  O  O   . VAL A 1 95  ? 50.081 6.516   22.172 1.00 29.53 ? 94  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 95  ? 48.654 9.009   23.311 1.00 35.17 ? 94  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 95  ? 47.966 9.259   21.961 1.00 32.52 ? 94  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 95  ? 48.062 9.882   24.414 1.00 37.53 ? 94  VAL A CG2 1 
ATOM   602  N  N   . ALA A 1 96  ? 47.883 6.044   21.902 1.00 25.05 ? 95  ALA A N   1 
ATOM   603  C  CA  . ALA A 1 96  ? 48.103 5.247   20.686 1.00 31.44 ? 95  ALA A CA  1 
ATOM   604  C  C   . ALA A 1 96  ? 47.433 6.024   19.533 1.00 32.28 ? 95  ALA A C   1 
ATOM   605  O  O   . ALA A 1 96  ? 46.207 6.280   19.553 1.00 32.94 ? 95  ALA A O   1 
ATOM   606  C  CB  . ALA A 1 96  ? 47.466 3.830   20.812 1.00 28.57 ? 95  ALA A CB  1 
ATOM   607  N  N   . ASP A 1 97  ? 48.234 6.424   18.555 1.00 30.71 ? 96  ASP A N   1 
ATOM   608  C  CA  . ASP A 1 97  ? 47.697 7.125   17.383 1.00 31.46 ? 96  ASP A CA  1 
ATOM   609  C  C   . ASP A 1 97  ? 47.410 6.078   16.366 1.00 33.01 ? 96  ASP A C   1 
ATOM   610  O  O   . ASP A 1 97  ? 48.316 5.358   15.931 1.00 33.81 ? 96  ASP A O   1 
ATOM   611  C  CB  . ASP A 1 97  ? 48.692 8.138   16.880 1.00 39.92 ? 96  ASP A CB  1 
ATOM   612  C  CG  . ASP A 1 97  ? 48.815 9.294   17.832 1.00 47.42 ? 96  ASP A CG  1 
ATOM   613  O  OD1 . ASP A 1 97  ? 47.779 9.929   18.120 1.00 48.33 ? 96  ASP A OD1 1 
ATOM   614  O  OD2 . ASP A 1 97  ? 49.946 9.551   18.315 1.00 61.24 ? 96  ASP A OD2 1 
ATOM   615  N  N   . VAL A 1 98  ? 46.135 5.949   16.007 1.00 31.39 ? 97  VAL A N   1 
ATOM   616  C  CA  . VAL A 1 98  ? 45.758 4.878   15.104 1.00 28.07 ? 97  VAL A CA  1 
ATOM   617  C  C   . VAL A 1 98  ? 45.573 5.249   13.623 1.00 32.98 ? 97  VAL A C   1 
ATOM   618  O  O   . VAL A 1 98  ? 44.878 6.186   13.290 1.00 27.79 ? 97  VAL A O   1 
ATOM   619  C  CB  . VAL A 1 98  ? 44.449 4.195   15.614 1.00 30.07 ? 97  VAL A CB  1 
ATOM   620  C  CG1 . VAL A 1 98  ? 43.987 3.135   14.618 1.00 23.60 ? 97  VAL A CG1 1 
ATOM   621  C  CG2 . VAL A 1 98  ? 44.681 3.585   17.008 1.00 30.46 ? 97  VAL A CG2 1 
ATOM   622  N  N   . SER A 1 99  ? 46.183 4.479   12.740 1.00 32.41 ? 98  SER A N   1 
ATOM   623  C  CA  . SER A 1 99  ? 46.024 4.719   11.323 1.00 35.75 ? 98  SER A CA  1 
ATOM   624  C  C   . SER A 1 99  ? 46.294 3.392   10.639 1.00 38.46 ? 98  SER A C   1 
ATOM   625  O  O   . SER A 1 99  ? 47.447 2.970   10.553 1.00 42.50 ? 98  SER A O   1 
ATOM   626  C  CB  . SER A 1 99  ? 47.004 5.790   10.838 1.00 35.50 ? 98  SER A CB  1 
ATOM   627  O  OG  . SER A 1 99  ? 46.654 6.147   9.515  1.00 39.36 ? 98  SER A OG  1 
ATOM   628  N  N   . ILE A 1 100 ? 45.226 2.755   10.151 1.00 32.61 ? 99  ILE A N   1 
ATOM   629  C  CA  . ILE A 1 100 ? 45.285 1.445   9.500  1.00 32.88 ? 99  ILE A CA  1 
ATOM   630  C  C   . ILE A 1 100 ? 44.484 1.361   8.191  1.00 33.72 ? 99  ILE A C   1 
ATOM   631  O  O   . ILE A 1 100 ? 43.498 2.086   7.989  1.00 32.10 ? 99  ILE A O   1 
ATOM   632  C  CB  . ILE A 1 100 ? 44.680 0.355   10.460 1.00 36.05 ? 99  ILE A CB  1 
ATOM   633  C  CG1 . ILE A 1 100 ? 45.564 0.169   11.694 1.00 40.14 ? 99  ILE A CG1 1 
ATOM   634  C  CG2 . ILE A 1 100 ? 44.508 -0.953  9.756  1.00 42.92 ? 99  ILE A CG2 1 
ATOM   635  C  CD1 . ILE A 1 100 ? 44.854 -0.557  12.858 1.00 33.63 ? 99  ILE A CD1 1 
ATOM   636  N  N   . GLU A 1 101 ? 44.921 0.471   7.303  1.00 36.98 ? 100 GLU A N   1 
ATOM   637  C  CA  . GLU A 1 101 ? 44.199 0.195   6.070  1.00 39.00 ? 100 GLU A CA  1 
ATOM   638  C  C   . GLU A 1 101 ? 44.078 -1.306  6.118  1.00 36.49 ? 100 GLU A C   1 
ATOM   639  O  O   . GLU A 1 101 ? 45.080 -2.010  6.169  1.00 36.38 ? 100 GLU A O   1 
ATOM   640  C  CB  . GLU A 1 101 ? 44.976 0.626   4.838  1.00 42.14 ? 100 GLU A CB  1 
ATOM   641  C  CG  . GLU A 1 101 ? 44.261 0.263   3.574  1.00 51.08 ? 100 GLU A CG  1 
ATOM   642  C  CD  . GLU A 1 101 ? 44.697 1.108   2.389  1.00 58.30 ? 100 GLU A CD  1 
ATOM   643  O  OE1 . GLU A 1 101 ? 44.567 2.356   2.459  1.00 55.37 ? 100 GLU A OE1 1 
ATOM   644  O  OE2 . GLU A 1 101 ? 45.163 0.508   1.398  1.00 61.99 ? 100 GLU A OE2 1 
ATOM   645  N  N   . ASP A 1 102 ? 42.852 -1.806  6.109  1.00 34.06 ? 101 ASP A N   1 
ATOM   646  C  CA  . ASP A 1 102 ? 42.620 -3.245  6.219  1.00 36.82 ? 101 ASP A CA  1 
ATOM   647  C  C   . ASP A 1 102 ? 41.671 -3.665  5.096  1.00 42.81 ? 101 ASP A C   1 
ATOM   648  O  O   . ASP A 1 102 ? 40.672 -2.988  4.841  1.00 44.66 ? 101 ASP A O   1 
ATOM   649  C  CB  . ASP A 1 102 ? 41.999 -3.502  7.599  1.00 35.96 ? 101 ASP A CB  1 
ATOM   650  C  CG  . ASP A 1 102 ? 41.844 -4.965  7.929  1.00 37.47 ? 101 ASP A CG  1 
ATOM   651  O  OD1 . ASP A 1 102 ? 40.941 -5.637  7.388  1.00 30.45 ? 101 ASP A OD1 1 
ATOM   652  O  OD2 . ASP A 1 102 ? 42.642 -5.449  8.759  1.00 40.64 ? 101 ASP A OD2 1 
ATOM   653  N  N   . SER A 1 103 ? 41.962 -4.771  4.424  1.00 45.14 ? 102 SER A N   1 
ATOM   654  C  CA  . SER A 1 103 ? 41.088 -5.185  3.341  1.00 45.81 ? 102 SER A CA  1 
ATOM   655  C  C   . SER A 1 103 ? 40.316 -6.437  3.598  1.00 40.81 ? 102 SER A C   1 
ATOM   656  O  O   . SER A 1 103 ? 39.680 -6.997  2.688  1.00 44.09 ? 102 SER A O   1 
ATOM   657  C  CB  . SER A 1 103 ? 41.861 -5.322  2.032  1.00 52.55 ? 102 SER A CB  1 
ATOM   658  O  OG  . SER A 1 103 ? 41.467 -4.266  1.166  1.00 61.41 ? 102 SER A OG  1 
ATOM   659  N  N   . VAL A 1 104 ? 40.353 -6.881  4.838  1.00 33.44 ? 103 VAL A N   1 
ATOM   660  C  CA  . VAL A 1 104 ? 39.609 -8.079  5.220  1.00 34.75 ? 103 VAL A CA  1 
ATOM   661  C  C   . VAL A 1 104 ? 38.252 -7.666  5.792  1.00 33.47 ? 103 VAL A C   1 
ATOM   662  O  O   . VAL A 1 104 ? 37.237 -8.255  5.447  1.00 33.43 ? 103 VAL A O   1 
ATOM   663  C  CB  . VAL A 1 104 ? 40.402 -8.896  6.250  1.00 38.58 ? 103 VAL A CB  1 
ATOM   664  C  CG1 . VAL A 1 104 ? 39.553 -10.043 6.791  1.00 40.70 ? 103 VAL A CG1 1 
ATOM   665  C  CG2 . VAL A 1 104 ? 41.668 -9.433  5.582  1.00 43.74 ? 103 VAL A CG2 1 
ATOM   666  N  N   . ILE A 1 105 ? 38.233 -6.648  6.670  1.00 28.15 ? 104 ILE A N   1 
ATOM   667  C  CA  . ILE A 1 105 ? 36.965 -6.186  7.220  1.00 27.31 ? 104 ILE A CA  1 
ATOM   668  C  C   . ILE A 1 105 ? 36.271 -5.420  6.120  1.00 32.80 ? 104 ILE A C   1 
ATOM   669  O  O   . ILE A 1 105 ? 36.895 -5.089  5.114  1.00 31.43 ? 104 ILE A O   1 
ATOM   670  C  CB  . ILE A 1 105 ? 37.145 -5.183  8.451  1.00 29.80 ? 104 ILE A CB  1 
ATOM   671  C  CG1 . ILE A 1 105 ? 38.038 -3.987  8.069  1.00 24.19 ? 104 ILE A CG1 1 
ATOM   672  C  CG2 . ILE A 1 105 ? 37.718 -5.918  9.653  1.00 31.25 ? 104 ILE A CG2 1 
ATOM   673  C  CD1 . ILE A 1 105 ? 38.143 -2.895  9.230  1.00 24.17 ? 104 ILE A CD1 1 
ATOM   674  N  N   . SER A 1 106 ? 34.990 -5.134  6.312  1.00 29.26 ? 105 SER A N   1 
ATOM   675  C  CA  . SER A 1 106 ? 34.267 -4.294  5.372  1.00 30.37 ? 105 SER A CA  1 
ATOM   676  C  C   . SER A 1 106 ? 33.210 -3.499  6.169  1.00 32.87 ? 105 SER A C   1 
ATOM   677  O  O   . SER A 1 106 ? 32.982 -3.763  7.387  1.00 25.43 ? 105 SER A O   1 
ATOM   678  C  CB  . SER A 1 106 ? 33.573 -5.166  4.296  1.00 32.39 ? 105 SER A CB  1 
ATOM   679  O  OG  . SER A 1 106 ? 33.266 -4.376  3.153  1.00 37.68 ? 105 SER A OG  1 
ATOM   680  N  N   . LEU A 1 107 ? 32.582 -2.524  5.505  1.00 30.57 ? 106 LEU A N   1 
ATOM   681  C  CA  . LEU A 1 107 ? 31.503 -1.773  6.126  1.00 30.10 ? 106 LEU A CA  1 
ATOM   682  C  C   . LEU A 1 107 ? 30.189 -2.183  5.436  1.00 35.42 ? 106 LEU A C   1 
ATOM   683  O  O   . LEU A 1 107 ? 29.164 -1.540  5.594  1.00 31.90 ? 106 LEU A O   1 
ATOM   684  C  CB  . LEU A 1 107 ? 31.729 -0.258  6.033  1.00 32.12 ? 106 LEU A CB  1 
ATOM   685  C  CG  . LEU A 1 107 ? 32.995 0.228   6.771  1.00 35.14 ? 106 LEU A CG  1 
ATOM   686  C  CD1 . LEU A 1 107 ? 33.094 1.779   6.765  1.00 25.88 ? 106 LEU A CD1 1 
ATOM   687  C  CD2 . LEU A 1 107 ? 32.984 -0.334  8.206  1.00 26.54 ? 106 LEU A CD2 1 
ATOM   688  N  N   . SER A 1 108 ? 30.235 -3.277  4.682  1.00 34.88 ? 107 SER A N   1 
ATOM   689  C  CA  . SER A 1 108 ? 29.057 -3.805  4.008  1.00 40.48 ? 107 SER A CA  1 
ATOM   690  C  C   . SER A 1 108 ? 29.237 -5.277  3.687  1.00 38.64 ? 107 SER A C   1 
ATOM   691  O  O   . SER A 1 108 ? 30.361 -5.735  3.608  1.00 35.25 ? 107 SER A O   1 
ATOM   692  C  CB  . SER A 1 108 ? 28.818 -3.075  2.699  1.00 45.51 ? 107 SER A CB  1 
ATOM   693  O  OG  . SER A 1 108 ? 27.821 -3.786  2.010  1.00 62.04 ? 107 SER A OG  1 
ATOM   694  N  N   . GLY A 1 109 ? 28.143 -6.019  3.505  1.00 37.75 ? 108 GLY A N   1 
ATOM   695  C  CA  . GLY A 1 109 ? 28.276 -7.429  3.158  1.00 43.64 ? 108 GLY A CA  1 
ATOM   696  C  C   . GLY A 1 109 ? 28.560 -8.460  4.257  1.00 43.05 ? 108 GLY A C   1 
ATOM   697  O  O   . GLY A 1 109 ? 28.255 -8.242  5.434  1.00 43.40 ? 108 GLY A O   1 
ATOM   698  N  N   . ASP A 1 110 ? 29.151 -9.591  3.884  1.00 40.19 ? 109 ASP A N   1 
ATOM   699  C  CA  . ASP A 1 110 ? 29.417 -10.628 4.873  1.00 41.90 ? 109 ASP A CA  1 
ATOM   700  C  C   . ASP A 1 110 ? 30.504 -10.246 5.852  1.00 37.72 ? 109 ASP A C   1 
ATOM   701  O  O   . ASP A 1 110 ? 30.585 -10.796 6.969  1.00 32.52 ? 109 ASP A O   1 
ATOM   702  C  CB  . ASP A 1 110 ? 29.811 -11.959 4.221  1.00 48.37 ? 109 ASP A CB  1 
ATOM   703  C  CG  . ASP A 1 110 ? 28.756 -12.492 3.275  1.00 55.87 ? 109 ASP A CG  1 
ATOM   704  O  OD1 . ASP A 1 110 ? 27.553 -12.179 3.451  1.00 54.45 ? 109 ASP A OD1 1 
ATOM   705  O  OD2 . ASP A 1 110 ? 29.151 -13.249 2.355  1.00 63.05 ? 109 ASP A OD2 1 
ATOM   706  N  N   . HIS A 1 111 ? 31.351 -9.321  5.447  1.00 29.66 ? 110 HIS A N   1 
ATOM   707  C  CA  . HIS A 1 111 ? 32.435 -8.927  6.327  1.00 36.88 ? 110 HIS A CA  1 
ATOM   708  C  C   . HIS A 1 111 ? 32.155 -7.629  7.050  1.00 25.41 ? 110 HIS A C   1 
ATOM   709  O  O   . HIS A 1 111 ? 33.050 -7.061  7.645  1.00 29.13 ? 110 HIS A O   1 
ATOM   710  C  CB  . HIS A 1 111 ? 33.766 -8.854  5.530  1.00 33.07 ? 110 HIS A CB  1 
ATOM   711  C  CG  . HIS A 1 111 ? 34.376 -10.206 5.272  1.00 41.58 ? 110 HIS A CG  1 
ATOM   712  N  ND1 . HIS A 1 111 ? 35.730 -10.399 5.071  1.00 44.21 ? 110 HIS A ND1 1 
ATOM   713  C  CD2 . HIS A 1 111 ? 33.817 -11.437 5.228  1.00 42.68 ? 110 HIS A CD2 1 
ATOM   714  C  CE1 . HIS A 1 111 ? 35.974 -11.691 4.919  1.00 36.90 ? 110 HIS A CE1 1 
ATOM   715  N  NE2 . HIS A 1 111 ? 34.831 -12.341 5.011  1.00 41.54 ? 110 HIS A NE2 1 
ATOM   716  N  N   . SER A 1 112 ? 30.911 -7.166  7.026  1.00 29.20 ? 111 SER A N   1 
ATOM   717  C  CA  . SER A 1 112 ? 30.611 -5.875  7.660  1.00 25.85 ? 111 SER A CA  1 
ATOM   718  C  C   . SER A 1 112 ? 30.747 -5.916  9.171  1.00 24.33 ? 111 SER A C   1 
ATOM   719  O  O   . SER A 1 112 ? 30.265 -6.820  9.857  1.00 26.18 ? 111 SER A O   1 
ATOM   720  C  CB  . SER A 1 112 ? 29.214 -5.380  7.311  1.00 30.86 ? 111 SER A CB  1 
ATOM   721  O  OG  . SER A 1 112 ? 28.976 -4.091  7.896  1.00 28.96 ? 111 SER A OG  1 
ATOM   722  N  N   . ILE A 1 113 ? 31.409 -4.905  9.681  1.00 23.92 ? 112 ILE A N   1 
ATOM   723  C  CA  . ILE A 1 113 ? 31.638 -4.790  11.102 1.00 23.58 ? 112 ILE A CA  1 
ATOM   724  C  C   . ILE A 1 113 ? 30.645 -3.773  11.657 1.00 27.68 ? 112 ILE A C   1 
ATOM   725  O  O   . ILE A 1 113 ? 30.682 -3.460  12.822 1.00 29.19 ? 112 ILE A O   1 
ATOM   726  C  CB  . ILE A 1 113 ? 33.068 -4.312  11.370 1.00 20.99 ? 112 ILE A CB  1 
ATOM   727  C  CG1 . ILE A 1 113 ? 33.337 -3.015  10.614 1.00 25.29 ? 112 ILE A CG1 1 
ATOM   728  C  CG2 . ILE A 1 113 ? 34.038 -5.367  10.866 1.00 27.69 ? 112 ILE A CG2 1 
ATOM   729  C  CD1 . ILE A 1 113 ? 34.644 -2.279  11.017 1.00 27.02 ? 112 ILE A CD1 1 
ATOM   730  N  N   . ILE A 1 114 ? 29.741 -3.271  10.818 1.00 24.42 ? 113 ILE A N   1 
ATOM   731  C  CA  . ILE A 1 114 ? 28.767 -2.290  11.310 1.00 27.23 ? 113 ILE A CA  1 
ATOM   732  C  C   . ILE A 1 114 ? 27.861 -2.983  12.347 1.00 24.61 ? 113 ILE A C   1 
ATOM   733  O  O   . ILE A 1 114 ? 27.393 -4.079  12.098 1.00 21.02 ? 113 ILE A O   1 
ATOM   734  C  CB  . ILE A 1 114 ? 27.891 -1.767  10.149 1.00 27.50 ? 113 ILE A CB  1 
ATOM   735  C  CG1 . ILE A 1 114 ? 28.767 -0.980  9.154  1.00 27.62 ? 113 ILE A CG1 1 
ATOM   736  C  CG2 . ILE A 1 114 ? 26.732 -0.939  10.694 1.00 21.70 ? 113 ILE A CG2 1 
ATOM   737  C  CD1 . ILE A 1 114 ? 29.458 0.234   9.748  1.00 27.66 ? 113 ILE A CD1 1 
ATOM   738  N  N   . GLY A 1 115 ? 27.635 -2.352  13.501 1.00 23.01 ? 114 GLY A N   1 
ATOM   739  C  CA  . GLY A 1 115 ? 26.758 -2.947  14.492 1.00 21.91 ? 114 GLY A CA  1 
ATOM   740  C  C   . GLY A 1 115 ? 27.438 -3.948  15.413 1.00 25.56 ? 114 GLY A C   1 
ATOM   741  O  O   . GLY A 1 115 ? 26.771 -4.630  16.234 1.00 22.36 ? 114 GLY A O   1 
ATOM   742  N  N   . ARG A 1 116 ? 28.760 -4.061  15.261 1.00 23.15 ? 115 ARG A N   1 
ATOM   743  C  CA  . ARG A 1 116 ? 29.514 -4.962  16.096 1.00 20.51 ? 115 ARG A CA  1 
ATOM   744  C  C   . ARG A 1 116 ? 30.312 -4.110  17.071 1.00 23.25 ? 115 ARG A C   1 
ATOM   745  O  O   . ARG A 1 116 ? 30.108 -2.885  17.091 1.00 23.80 ? 115 ARG A O   1 
ATOM   746  C  CB  . ARG A 1 116 ? 30.380 -5.870  15.224 1.00 22.32 ? 115 ARG A CB  1 
ATOM   747  C  CG  . ARG A 1 116 ? 29.514 -6.714  14.281 1.00 21.91 ? 115 ARG A CG  1 
ATOM   748  C  CD  . ARG A 1 116 ? 30.338 -7.791  13.580 1.00 25.74 ? 115 ARG A CD  1 
ATOM   749  N  NE  . ARG A 1 116 ? 29.524 -8.455  12.567 1.00 24.66 ? 115 ARG A NE  1 
ATOM   750  C  CZ  . ARG A 1 116 ? 28.648 -9.425  12.797 1.00 24.88 ? 115 ARG A CZ  1 
ATOM   751  N  NH1 . ARG A 1 116 ? 27.978 -9.932  11.773 1.00 23.29 ? 115 ARG A NH1 1 
ATOM   752  N  NH2 . ARG A 1 116 ? 28.463 -9.933  14.019 1.00 22.48 ? 115 ARG A NH2 1 
ATOM   753  N  N   . THR A 1 117 ? 31.197 -4.720  17.870 1.00 21.08 ? 116 THR A N   1 
ATOM   754  C  CA  . THR A 1 117 ? 31.971 -3.968  18.892 1.00 25.05 ? 116 THR A CA  1 
ATOM   755  C  C   . THR A 1 117 ? 33.486 -3.906  18.720 1.00 26.33 ? 116 THR A C   1 
ATOM   756  O  O   . THR A 1 117 ? 34.170 -4.935  18.556 1.00 23.94 ? 116 THR A O   1 
ATOM   757  C  CB  . THR A 1 117 ? 31.680 -4.532  20.352 1.00 25.34 ? 116 THR A CB  1 
ATOM   758  O  OG1 . THR A 1 117 ? 30.283 -4.365  20.646 1.00 26.40 ? 116 THR A OG1 1 
ATOM   759  C  CG2 . THR A 1 117 ? 32.478 -3.779  21.431 1.00 21.22 ? 116 THR A CG2 1 
ATOM   760  N  N   . LEU A 1 118 ? 34.005 -2.684  18.751 1.00 24.69 ? 117 LEU A N   1 
ATOM   761  C  CA  . LEU A 1 118 ? 35.448 -2.481  18.634 1.00 25.84 ? 117 LEU A CA  1 
ATOM   762  C  C   . LEU A 1 118 ? 35.945 -2.547  20.054 1.00 19.82 ? 117 LEU A C   1 
ATOM   763  O  O   . LEU A 1 118 ? 35.351 -1.914  20.918 1.00 22.80 ? 117 LEU A O   1 
ATOM   764  C  CB  . LEU A 1 118 ? 35.773 -1.104  18.038 1.00 19.95 ? 117 LEU A CB  1 
ATOM   765  C  CG  . LEU A 1 118 ? 37.251 -0.840  17.772 1.00 20.24 ? 117 LEU A CG  1 
ATOM   766  C  CD1 . LEU A 1 118 ? 37.799 -1.835  16.729 1.00 18.05 ? 117 LEU A CD1 1 
ATOM   767  C  CD2 . LEU A 1 118 ? 37.395 0.596   17.162 1.00 20.17 ? 117 LEU A CD2 1 
ATOM   768  N  N   . VAL A 1 119 ? 37.014 -3.312  20.289 1.00 21.73 ? 118 VAL A N   1 
ATOM   769  C  CA  . VAL A 1 119 ? 37.587 -3.485  21.637 1.00 18.55 ? 118 VAL A CA  1 
ATOM   770  C  C   . VAL A 1 119 ? 39.091 -3.213  21.645 1.00 19.30 ? 118 VAL A C   1 
ATOM   771  O  O   . VAL A 1 119 ? 39.812 -3.625  20.721 1.00 21.36 ? 118 VAL A O   1 
ATOM   772  C  CB  . VAL A 1 119 ? 37.407 -4.968  22.105 1.00 22.35 ? 118 VAL A CB  1 
ATOM   773  C  CG1 . VAL A 1 119 ? 38.034 -5.176  23.516 1.00 22.28 ? 118 VAL A CG1 1 
ATOM   774  C  CG2 . VAL A 1 119 ? 35.901 -5.372  22.100 1.00 21.00 ? 118 VAL A CG2 1 
ATOM   775  N  N   . VAL A 1 120 ? 39.600 -2.538  22.668 1.00 23.96 ? 119 VAL A N   1 
ATOM   776  C  CA  . VAL A 1 120 ? 41.059 -2.375  22.736 1.00 19.71 ? 119 VAL A CA  1 
ATOM   777  C  C   . VAL A 1 120 ? 41.407 -3.179  24.023 1.00 24.28 ? 119 VAL A C   1 
ATOM   778  O  O   . VAL A 1 120 ? 40.701 -3.063  25.042 1.00 19.92 ? 119 VAL A O   1 
ATOM   779  C  CB  . VAL A 1 120 ? 41.505 -0.841  22.788 1.00 18.15 ? 119 VAL A CB  1 
ATOM   780  C  CG1 . VAL A 1 120 ? 40.835 -0.093  23.943 1.00 16.03 ? 119 VAL A CG1 1 
ATOM   781  C  CG2 . VAL A 1 120 ? 43.026 -0.725  22.925 1.00 25.73 ? 119 VAL A CG2 1 
ATOM   782  N  N   . HIS A 1 121 ? 42.466 -3.996  23.974 1.00 20.86 ? 120 HIS A N   1 
ATOM   783  C  CA  . HIS A 1 121 ? 42.828 -4.848  25.131 1.00 23.18 ? 120 HIS A CA  1 
ATOM   784  C  C   . HIS A 1 121 ? 43.928 -4.375  26.057 1.00 24.39 ? 120 HIS A C   1 
ATOM   785  O  O   . HIS A 1 121 ? 44.762 -3.524  25.724 1.00 22.47 ? 120 HIS A O   1 
ATOM   786  C  CB  . HIS A 1 121 ? 43.182 -6.270  24.641 1.00 21.74 ? 120 HIS A CB  1 
ATOM   787  C  CG  . HIS A 1 121 ? 42.008 -7.028  24.125 1.00 25.70 ? 120 HIS A CG  1 
ATOM   788  N  ND1 . HIS A 1 121 ? 41.294 -7.917  24.901 1.00 24.28 ? 120 HIS A ND1 1 
ATOM   789  C  CD2 . HIS A 1 121 ? 41.396 -7.003  22.914 1.00 23.54 ? 120 HIS A CD2 1 
ATOM   790  C  CE1 . HIS A 1 121 ? 40.297 -8.412  24.187 1.00 24.20 ? 120 HIS A CE1 1 
ATOM   791  N  NE2 . HIS A 1 121 ? 40.337 -7.871  22.982 1.00 26.15 ? 120 HIS A NE2 1 
ATOM   792  N  N   . GLU A 1 122 ? 43.891 -4.951  27.248 1.00 28.52 ? 121 GLU A N   1 
ATOM   793  C  CA  . GLU A 1 122 ? 44.852 -4.690  28.312 1.00 26.20 ? 121 GLU A CA  1 
ATOM   794  C  C   . GLU A 1 122 ? 46.214 -5.173  27.832 1.00 26.34 ? 121 GLU A C   1 
ATOM   795  O  O   . GLU A 1 122 ? 47.219 -4.516  28.031 1.00 26.61 ? 121 GLU A O   1 
ATOM   796  C  CB  . GLU A 1 122 ? 44.425 -5.499  29.578 1.00 35.27 ? 121 GLU A CB  1 
ATOM   797  C  CG  . GLU A 1 122 ? 45.510 -5.639  30.662 1.00 43.94 ? 121 GLU A CG  1 
ATOM   798  C  CD  . GLU A 1 122 ? 45.464 -6.989  31.407 1.00 56.02 ? 121 GLU A CD  1 
ATOM   799  O  OE1 . GLU A 1 122 ? 44.526 -7.814  31.206 1.00 45.51 ? 121 GLU A OE1 1 
ATOM   800  O  OE2 . GLU A 1 122 ? 46.402 -7.217  32.219 1.00 60.17 ? 121 GLU A OE2 1 
ATOM   801  N  N   . LYS A 1 123 ? 46.240 -6.342  27.189 1.00 29.39 ? 122 LYS A N   1 
ATOM   802  C  CA  . LYS A 1 123 ? 47.500 -6.902  26.703 1.00 31.35 ? 122 LYS A CA  1 
ATOM   803  C  C   . LYS A 1 123 ? 47.650 -6.877  25.190 1.00 27.12 ? 122 LYS A C   1 
ATOM   804  O  O   . LYS A 1 123 ? 46.701 -6.642  24.444 1.00 30.44 ? 122 LYS A O   1 
ATOM   805  C  CB  . LYS A 1 123 ? 47.657 -8.365  27.165 1.00 34.87 ? 122 LYS A CB  1 
ATOM   806  C  CG  . LYS A 1 123 ? 47.286 -8.592  28.644 1.00 47.12 ? 122 LYS A CG  1 
ATOM   807  C  CD  . LYS A 1 123 ? 48.265 -9.525  29.325 1.00 48.91 ? 122 LYS A CD  1 
ATOM   808  C  CE  . LYS A 1 123 ? 48.310 -10.879 28.640 1.00 57.92 ? 122 LYS A CE  1 
ATOM   809  N  NZ  . LYS A 1 123 ? 49.380 -11.785 29.190 1.00 63.04 ? 122 LYS A NZ  1 
ATOM   810  N  N   . ALA A 1 124 ? 48.861 -7.155  24.753 1.00 23.57 ? 123 ALA A N   1 
ATOM   811  C  CA  . ALA A 1 124 ? 49.163 -7.209  23.322 1.00 29.12 ? 123 ALA A CA  1 
ATOM   812  C  C   . ALA A 1 124 ? 48.590 -8.492  22.742 1.00 32.11 ? 123 ALA A C   1 
ATOM   813  O  O   . ALA A 1 124 ? 48.407 -9.475  23.473 1.00 30.40 ? 123 ALA A O   1 
ATOM   814  C  CB  . ALA A 1 124 ? 50.674 -7.222  23.107 1.00 28.45 ? 123 ALA A CB  1 
ATOM   815  N  N   . ASP A 1 125 ? 48.283 -8.467  21.448 1.00 25.64 ? 124 ASP A N   1 
ATOM   816  C  CA  . ASP A 1 125 ? 47.863 -9.685  20.751 1.00 30.43 ? 124 ASP A CA  1 
ATOM   817  C  C   . ASP A 1 125 ? 49.235 -10.188 20.203 1.00 26.90 ? 124 ASP A C   1 
ATOM   818  O  O   . ASP A 1 125 ? 49.874 -9.454  19.462 1.00 23.34 ? 124 ASP A O   1 
ATOM   819  C  CB  . ASP A 1 125 ? 46.939 -9.330  19.583 1.00 29.00 ? 124 ASP A CB  1 
ATOM   820  C  CG  . ASP A 1 125 ? 46.424 -10.543 18.868 1.00 35.40 ? 124 ASP A CG  1 
ATOM   821  O  OD1 . ASP A 1 125 ? 45.321 -10.439 18.290 1.00 31.01 ? 124 ASP A OD1 1 
ATOM   822  O  OD2 . ASP A 1 125 ? 47.131 -11.593 18.875 1.00 26.51 ? 124 ASP A OD2 1 
ATOM   823  N  N   . ASP A 1 126 ? 49.679 -11.408 20.534 1.00 22.40 ? 125 ASP A N   1 
ATOM   824  C  CA  . ASP A 1 126 ? 50.998 -11.826 20.050 1.00 26.70 ? 125 ASP A CA  1 
ATOM   825  C  C   . ASP A 1 126 ? 50.950 -12.290 18.616 1.00 27.96 ? 125 ASP A C   1 
ATOM   826  O  O   . ASP A 1 126 ? 51.983 -12.670 18.036 1.00 27.23 ? 125 ASP A O   1 
ATOM   827  C  CB  . ASP A 1 126 ? 51.676 -12.904 20.946 1.00 25.84 ? 125 ASP A CB  1 
ATOM   828  C  CG  . ASP A 1 126 ? 50.953 -14.240 20.928 1.00 29.41 ? 125 ASP A CG  1 
ATOM   829  O  OD1 . ASP A 1 126 ? 50.165 -14.490 19.981 1.00 29.60 ? 125 ASP A OD1 1 
ATOM   830  O  OD2 . ASP A 1 126 ? 51.191 -15.054 21.857 1.00 29.21 ? 125 ASP A OD2 1 
ATOM   831  N  N   . LEU A 1 127 ? 49.747 -12.231 18.044 1.00 27.50 ? 126 LEU A N   1 
ATOM   832  C  CA  . LEU A 1 127 ? 49.526 -12.593 16.654 1.00 30.71 ? 126 LEU A CA  1 
ATOM   833  C  C   . LEU A 1 127 ? 50.018 -13.973 16.247 1.00 36.34 ? 126 LEU A C   1 
ATOM   834  O  O   . LEU A 1 127 ? 50.321 -14.195 15.071 1.00 37.09 ? 126 LEU A O   1 
ATOM   835  C  CB  . LEU A 1 127 ? 50.199 -11.578 15.744 1.00 27.26 ? 126 LEU A CB  1 
ATOM   836  C  CG  . LEU A 1 127 ? 49.779 -10.125 16.004 1.00 33.04 ? 126 LEU A CG  1 
ATOM   837  C  CD1 . LEU A 1 127 ? 50.554 -9.240  15.093 1.00 35.69 ? 126 LEU A CD1 1 
ATOM   838  C  CD2 . LEU A 1 127 ? 48.295 -9.936  15.805 1.00 31.39 ? 126 LEU A CD2 1 
ATOM   839  N  N   . GLY A 1 128 ? 50.103 -14.896 17.192 1.00 30.28 ? 127 GLY A N   1 
ATOM   840  C  CA  . GLY A 1 128 ? 50.586 -16.212 16.829 1.00 33.59 ? 127 GLY A CA  1 
ATOM   841  C  C   . GLY A 1 128 ? 52.102 -16.351 16.894 1.00 36.10 ? 127 GLY A C   1 
ATOM   842  O  O   . GLY A 1 128 ? 52.620 -17.441 16.679 1.00 35.53 ? 127 GLY A O   1 
ATOM   843  N  N   . LYS A 1 129 ? 52.814 -15.272 17.228 1.00 34.73 ? 128 LYS A N   1 
ATOM   844  C  CA  . LYS A 1 129 ? 54.270 -15.312 17.305 1.00 32.98 ? 128 LYS A CA  1 
ATOM   845  C  C   . LYS A 1 129 ? 54.811 -14.891 18.673 1.00 34.28 ? 128 LYS A C   1 
ATOM   846  O  O   . LYS A 1 129 ? 55.760 -14.100 18.743 1.00 34.27 ? 128 LYS A O   1 
ATOM   847  C  CB  . LYS A 1 129 ? 54.885 -14.413 16.233 1.00 32.43 ? 128 LYS A CB  1 
ATOM   848  C  CG  . LYS A 1 129 ? 54.443 -14.771 14.802 1.00 45.93 ? 128 LYS A CG  1 
ATOM   849  C  CD  . LYS A 1 129 ? 53.185 -14.015 14.382 1.00 57.19 ? 128 LYS A CD  1 
ATOM   850  C  CE  . LYS A 1 129 ? 52.934 -14.138 12.869 1.00 64.92 ? 128 LYS A CE  1 
ATOM   851  N  NZ  . LYS A 1 129 ? 51.898 -13.179 12.358 1.00 66.55 ? 128 LYS A NZ  1 
ATOM   852  N  N   . GLY A 1 130 ? 54.197 -15.417 19.735 1.00 28.11 ? 129 GLY A N   1 
ATOM   853  C  CA  . GLY A 1 130 ? 54.605 -15.133 21.102 1.00 30.47 ? 129 GLY A CA  1 
ATOM   854  C  C   . GLY A 1 130 ? 55.821 -15.968 21.526 1.00 31.02 ? 129 GLY A C   1 
ATOM   855  O  O   . GLY A 1 130 ? 56.281 -15.883 22.671 1.00 31.91 ? 129 GLY A O   1 
ATOM   856  N  N   . GLY A 1 131 ? 56.312 -16.809 20.620 1.00 28.38 ? 130 GLY A N   1 
ATOM   857  C  CA  . GLY A 1 131 ? 57.507 -17.596 20.890 1.00 28.01 ? 130 GLY A CA  1 
ATOM   858  C  C   . GLY A 1 131 ? 57.314 -18.586 22.002 1.00 37.79 ? 130 GLY A C   1 
ATOM   859  O  O   . GLY A 1 131 ? 58.259 -19.010 22.696 1.00 33.42 ? 130 GLY A O   1 
ATOM   860  N  N   . ASN A 1 132 ? 56.054 -18.953 22.158 1.00 45.80 ? 131 ASN A N   1 
ATOM   861  C  CA  . ASN A 1 132 ? 55.630 -19.918 23.150 1.00 53.94 ? 131 ASN A CA  1 
ATOM   862  C  C   . ASN A 1 132 ? 54.102 -20.015 23.122 1.00 56.87 ? 131 ASN A C   1 
ATOM   863  O  O   . ASN A 1 132 ? 53.412 -19.056 22.721 1.00 58.49 ? 131 ASN A O   1 
ATOM   864  C  CB  . ASN A 1 132 ? 56.107 -19.491 24.527 1.00 53.09 ? 131 ASN A CB  1 
ATOM   865  C  CG  . ASN A 1 132 ? 55.962 -20.593 25.539 1.00 62.81 ? 131 ASN A CG  1 
ATOM   866  O  OD1 . ASN A 1 132 ? 56.479 -21.707 25.344 1.00 52.59 ? 131 ASN A OD1 1 
ATOM   867  N  ND2 . ASN A 1 132 ? 55.254 -20.301 26.633 1.00 64.16 ? 131 ASN A ND2 1 
ATOM   868  N  N   . ALA A 1 141 ? 44.279 -11.526 24.536 1.00 36.37 ? 140 ALA A N   1 
ATOM   869  C  CA  . ALA A 1 141 ? 44.994 -10.261 24.785 1.00 36.53 ? 140 ALA A CA  1 
ATOM   870  C  C   . ALA A 1 141 ? 44.547 -9.661  26.119 1.00 35.71 ? 140 ALA A C   1 
ATOM   871  O  O   . ALA A 1 141 ? 44.627 -8.431  26.343 1.00 30.72 ? 140 ALA A O   1 
ATOM   872  C  CB  . ALA A 1 141 ? 44.754 -9.244  23.597 1.00 27.04 ? 140 ALA A CB  1 
ATOM   873  N  N   . GLY A 1 142 ? 44.059 -10.532 27.014 1.00 34.37 ? 141 GLY A N   1 
ATOM   874  C  CA  . GLY A 1 142 ? 43.639 -10.058 28.324 1.00 31.29 ? 141 GLY A CA  1 
ATOM   875  C  C   . GLY A 1 142 ? 42.285 -9.393  28.327 1.00 35.51 ? 141 GLY A C   1 
ATOM   876  O  O   . GLY A 1 142 ? 41.503 -9.580  27.371 1.00 37.23 ? 141 GLY A O   1 
ATOM   877  N  N   . SER A 1 143 ? 42.015 -8.574  29.350 1.00 32.81 ? 142 SER A N   1 
ATOM   878  C  CA  . SER A 1 143 ? 40.698 -7.959  29.452 1.00 32.42 ? 142 SER A CA  1 
ATOM   879  C  C   . SER A 1 143 ? 40.383 -6.865  28.417 1.00 30.67 ? 142 SER A C   1 
ATOM   880  O  O   . SER A 1 143 ? 41.274 -6.292  27.786 1.00 27.75 ? 142 SER A O   1 
ATOM   881  C  CB  . SER A 1 143 ? 40.461 -7.407  30.869 1.00 30.58 ? 142 SER A CB  1 
ATOM   882  O  OG  . SER A 1 143 ? 40.974 -6.102  30.990 1.00 41.66 ? 142 SER A OG  1 
ATOM   883  N  N   . ARG A 1 144 ? 39.091 -6.593  28.283 1.00 31.99 ? 143 ARG A N   1 
ATOM   884  C  CA  . ARG A 1 144 ? 38.564 -5.600  27.339 1.00 31.18 ? 143 ARG A CA  1 
ATOM   885  C  C   . ARG A 1 144 ? 38.494 -4.297  28.087 1.00 31.82 ? 143 ARG A C   1 
ATOM   886  O  O   . ARG A 1 144 ? 37.530 -4.060  28.792 1.00 36.57 ? 143 ARG A O   1 
ATOM   887  C  CB  . ARG A 1 144 ? 37.167 -6.028  26.926 1.00 26.69 ? 143 ARG A CB  1 
ATOM   888  C  CG  . ARG A 1 144 ? 37.141 -7.503  26.490 1.00 25.47 ? 143 ARG A CG  1 
ATOM   889  C  CD  . ARG A 1 144 ? 35.792 -7.964  26.005 1.00 28.25 ? 143 ARG A CD  1 
ATOM   890  N  NE  . ARG A 1 144 ? 35.842 -9.390  25.691 1.00 31.63 ? 143 ARG A NE  1 
ATOM   891  C  CZ  . ARG A 1 144 ? 34.786 -10.189 25.693 1.00 34.40 ? 143 ARG A CZ  1 
ATOM   892  N  NH1 . ARG A 1 144 ? 34.933 -11.475 25.404 1.00 39.05 ? 143 ARG A NH1 1 
ATOM   893  N  NH2 . ARG A 1 144 ? 33.585 -9.702  26.001 1.00 26.73 ? 143 ARG A NH2 1 
ATOM   894  N  N   . LEU A 1 145 ? 39.513 -3.461  27.931 1.00 26.89 ? 144 LEU A N   1 
ATOM   895  C  CA  . LEU A 1 145 ? 39.574 -2.175  28.619 1.00 30.69 ? 144 LEU A CA  1 
ATOM   896  C  C   . LEU A 1 145 ? 38.515 -1.150  28.248 1.00 26.01 ? 144 LEU A C   1 
ATOM   897  O  O   . LEU A 1 145 ? 37.991 -0.482  29.120 1.00 28.21 ? 144 LEU A O   1 
ATOM   898  C  CB  . LEU A 1 145 ? 40.945 -1.510  28.390 1.00 35.24 ? 144 LEU A CB  1 
ATOM   899  C  CG  . LEU A 1 145 ? 42.203 -2.160  28.950 1.00 39.69 ? 144 LEU A CG  1 
ATOM   900  C  CD1 . LEU A 1 145 ? 43.468 -1.509  28.353 1.00 36.63 ? 144 LEU A CD1 1 
ATOM   901  C  CD2 . LEU A 1 145 ? 42.150 -2.041  30.449 1.00 39.25 ? 144 LEU A CD2 1 
ATOM   902  N  N   . ALA A 1 146 ? 38.292 -0.961  26.947 1.00 28.69 ? 145 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 146 ? 37.298 0.014   26.432 1.00 28.87 ? 145 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 146 ? 36.751 -0.586  25.154 1.00 26.41 ? 145 ALA A C   1 
ATOM   905  O  O   . ALA A 1 146 ? 37.509 -1.268  24.441 1.00 23.34 ? 145 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 146 ? 37.956 1.361   26.139 1.00 26.14 ? 145 ALA A CB  1 
ATOM   907  N  N   . CYS A 1 147 ? 35.485 -0.349  24.881 1.00 24.78 ? 146 CYS A N   1 
ATOM   908  C  CA  . CYS A 1 147 ? 34.835 -0.879  23.710 1.00 24.21 ? 146 CYS A CA  1 
ATOM   909  C  C   . CYS A 1 147 ? 33.748 0.054   23.240 1.00 26.48 ? 146 CYS A C   1 
ATOM   910  O  O   . CYS A 1 147 ? 33.295 0.893   23.978 1.00 21.88 ? 146 CYS A O   1 
ATOM   911  C  CB  . CYS A 1 147 ? 34.241 -2.245  24.003 1.00 22.90 ? 146 CYS A CB  1 
ATOM   912  S  SG  A CYS A 1 147 ? 32.994 -2.138  25.221 0.55 27.25 ? 146 CYS A SG  1 
ATOM   913  S  SG  B CYS A 1 147 ? 34.964 -3.367  25.037 0.45 28.37 ? 146 CYS A SG  1 
ATOM   914  N  N   . GLY A 1 148 ? 33.321 -0.114  22.006 1.00 25.54 ? 147 GLY A N   1 
ATOM   915  C  CA  . GLY A 1 148 ? 32.255 0.724   21.494 1.00 23.46 ? 147 GLY A CA  1 
ATOM   916  C  C   . GLY A 1 148 ? 31.561 0.043   20.341 1.00 22.13 ? 147 GLY A C   1 
ATOM   917  O  O   . GLY A 1 148 ? 32.188 -0.652  19.527 1.00 22.54 ? 147 GLY A O   1 
ATOM   918  N  N   . VAL A 1 149 ? 30.258 0.216   20.242 1.00 21.59 ? 148 VAL A N   1 
ATOM   919  C  CA  . VAL A 1 149 ? 29.545 -0.361  19.111 1.00 21.56 ? 148 VAL A CA  1 
ATOM   920  C  C   . VAL A 1 149 ? 29.924 0.438   17.870 1.00 27.81 ? 148 VAL A C   1 
ATOM   921  O  O   . VAL A 1 149 ? 30.040 1.680   17.936 1.00 23.96 ? 148 VAL A O   1 
ATOM   922  C  CB  . VAL A 1 149 ? 28.028 -0.249  19.287 1.00 19.80 ? 148 VAL A CB  1 
ATOM   923  C  CG1 . VAL A 1 149 ? 27.312 -0.941  18.111 1.00 20.11 ? 148 VAL A CG1 1 
ATOM   924  C  CG2 . VAL A 1 149 ? 27.634 -0.871  20.660 1.00 28.06 ? 148 VAL A CG2 1 
ATOM   925  N  N   . ILE A 1 150 ? 30.087 -0.243  16.737 1.00 23.56 ? 149 ILE A N   1 
ATOM   926  C  CA  . ILE A 1 150 ? 30.474 0.471   15.532 1.00 22.85 ? 149 ILE A CA  1 
ATOM   927  C  C   . ILE A 1 150 ? 29.235 0.954   14.793 1.00 26.17 ? 149 ILE A C   1 
ATOM   928  O  O   . ILE A 1 150 ? 28.482 0.172   14.228 1.00 22.51 ? 149 ILE A O   1 
ATOM   929  C  CB  . ILE A 1 150 ? 31.321 -0.424  14.627 1.00 29.31 ? 149 ILE A CB  1 
ATOM   930  C  CG1 . ILE A 1 150 ? 32.589 -0.870  15.385 1.00 26.13 ? 149 ILE A CG1 1 
ATOM   931  C  CG2 . ILE A 1 150 ? 31.749 0.323   13.394 1.00 28.21 ? 149 ILE A CG2 1 
ATOM   932  C  CD1 . ILE A 1 150 ? 33.247 -2.094  14.761 1.00 31.70 ? 149 ILE A CD1 1 
ATOM   933  N  N   . GLY A 1 151 ? 29.041 2.260   14.783 1.00 24.61 ? 150 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 151 ? 27.872 2.792   14.118 1.00 21.00 ? 150 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 151 ? 28.147 3.569   12.829 1.00 29.31 ? 150 GLY A C   1 
ATOM   936  O  O   . GLY A 1 151 ? 29.258 4.126   12.593 1.00 25.72 ? 150 GLY A O   1 
ATOM   937  N  N   . ILE A 1 152 ? 27.124 3.590   11.978 1.00 24.39 ? 151 ILE A N   1 
ATOM   938  C  CA  . ILE A 1 152 ? 27.152 4.347   10.706 1.00 25.46 ? 151 ILE A CA  1 
ATOM   939  C  C   . ILE A 1 152 ? 27.315 5.832   11.069 1.00 30.44 ? 151 ILE A C   1 
ATOM   940  O  O   . ILE A 1 152 ? 26.555 6.344   11.889 1.00 25.42 ? 151 ILE A O   1 
ATOM   941  C  CB  . ILE A 1 152 ? 25.809 4.152   9.924  1.00 27.33 ? 151 ILE A CB  1 
ATOM   942  C  CG1 . ILE A 1 152 ? 25.720 2.696   9.467  1.00 30.69 ? 151 ILE A CG1 1 
ATOM   943  C  CG2 . ILE A 1 152 ? 25.742 5.091   8.677  1.00 30.61 ? 151 ILE A CG2 1 
ATOM   944  C  CD1 . ILE A 1 152 ? 24.331 2.265   9.015  1.00 28.54 ? 151 ILE A CD1 1 
ATOM   945  N  N   . ALA A 1 153 ? 28.308 6.506   10.464 1.00 29.00 ? 152 ALA A N   1 
ATOM   946  C  CA  . ALA A 1 153 ? 28.573 7.925   10.721 1.00 30.71 ? 152 ALA A CA  1 
ATOM   947  C  C   . ALA A 1 153 ? 28.360 8.830   9.501  1.00 30.89 ? 152 ALA A C   1 
ATOM   948  O  O   . ALA A 1 153 ? 28.357 8.385   8.362  1.00 29.15 ? 152 ALA A O   1 
ATOM   949  C  CB  . ALA A 1 153 ? 30.023 8.122   11.227 1.00 23.23 ? 152 ALA A CB  1 
ATOM   950  N  N   . GLN A 1 154 ? 28.239 10.113  9.771  1.00 36.39 ? 153 GLN A N   1 
ATOM   951  C  CA  . GLN A 1 154 ? 28.073 11.099  8.719  1.00 45.01 ? 153 GLN A CA  1 
ATOM   952  C  C   . GLN A 1 154 ? 29.452 11.356  8.098  1.00 43.24 ? 153 GLN A C   1 
ATOM   953  O  O   . GLN A 1 154 ? 29.611 11.190  6.890  1.00 47.15 ? 153 GLN A O   1 
ATOM   954  C  CB  . GLN A 1 154 ? 27.532 12.385  9.323  1.00 47.03 ? 153 GLN A CB  1 
ATOM   955  C  CG  . GLN A 1 154 ? 27.080 13.448  8.323  1.00 54.60 ? 153 GLN A CG  1 
ATOM   956  C  CD  . GLN A 1 154 ? 26.613 14.699  9.055  1.00 61.40 ? 153 GLN A CD  1 
ATOM   957  O  OE1 . GLN A 1 154 ? 27.383 15.311  9.816  1.00 68.18 ? 153 GLN A OE1 1 
ATOM   958  N  NE2 . GLN A 1 154 ? 25.351 15.076  8.853  1.00 57.81 ? 153 GLN A NE2 1 
ATOM   959  O  OXT . GLN A 1 154 ? 30.364 11.734  8.863  1.00 48.35 ? 153 GLN A OXT 1 
ATOM   960  N  N   . ALA B 1 2   ? 21.577 -9.259  9.820  1.00 53.50 ? 1   ALA B N   1 
ATOM   961  C  CA  . ALA B 1 2   ? 21.491 -10.018 11.073 1.00 54.68 ? 1   ALA B CA  1 
ATOM   962  C  C   . ALA B 1 2   ? 20.044 -10.402 11.420 1.00 49.78 ? 1   ALA B C   1 
ATOM   963  O  O   . ALA B 1 2   ? 19.102 -9.909  10.828 1.00 46.85 ? 1   ALA B O   1 
ATOM   964  C  CB  . ALA B 1 2   ? 22.116 -9.210  12.221 1.00 50.40 ? 1   ALA B CB  1 
ATOM   965  N  N   . THR B 1 3   ? 19.884 -11.297 12.382 1.00 47.56 ? 2   THR B N   1 
ATOM   966  C  CA  . THR B 1 3   ? 18.557 -11.731 12.772 1.00 45.14 ? 2   THR B CA  1 
ATOM   967  C  C   . THR B 1 3   ? 18.160 -11.195 14.145 1.00 36.20 ? 2   THR B C   1 
ATOM   968  O  O   . THR B 1 3   ? 16.987 -11.218 14.492 1.00 33.49 ? 2   THR B O   1 
ATOM   969  C  CB  . THR B 1 3   ? 18.477 -13.261 12.772 1.00 47.70 ? 2   THR B CB  1 
ATOM   970  O  OG1 . THR B 1 3   ? 18.724 -13.747 11.442 1.00 51.39 ? 2   THR B OG1 1 
ATOM   971  C  CG2 . THR B 1 3   ? 17.122 -13.730 13.240 1.00 53.33 ? 2   THR B CG2 1 
ATOM   972  N  N   . LYS B 1 4   ? 19.133 -10.723 14.924 1.00 31.23 ? 3   LYS B N   1 
ATOM   973  C  CA  . LYS B 1 4   ? 18.824 -10.177 16.257 1.00 34.85 ? 3   LYS B CA  1 
ATOM   974  C  C   . LYS B 1 4   ? 19.629 -8.947  16.570 1.00 31.89 ? 3   LYS B C   1 
ATOM   975  O  O   . LYS B 1 4   ? 20.780 -8.851  16.170 1.00 29.72 ? 3   LYS B O   1 
ATOM   976  C  CB  . LYS B 1 4   ? 19.069 -11.215 17.366 1.00 33.94 ? 3   LYS B CB  1 
ATOM   977  C  CG  . LYS B 1 4   ? 17.785 -11.662 18.060 1.00 53.68 ? 3   LYS B CG  1 
ATOM   978  C  CD  . LYS B 1 4   ? 18.022 -12.769 19.069 1.00 56.50 ? 3   LYS B CD  1 
ATOM   979  C  CE  . LYS B 1 4   ? 18.664 -13.974 18.391 1.00 64.78 ? 3   LYS B CE  1 
ATOM   980  N  NZ  . LYS B 1 4   ? 18.849 -15.130 19.331 1.00 65.15 ? 3   LYS B NZ  1 
ATOM   981  N  N   . ALA B 1 5   ? 19.051 -8.014  17.320 1.00 26.26 ? 4   ALA B N   1 
ATOM   982  C  CA  . ALA B 1 5   ? 19.798 -6.807  17.629 1.00 25.32 ? 4   ALA B CA  1 
ATOM   983  C  C   . ALA B 1 5   ? 19.324 -6.285  18.971 1.00 24.86 ? 4   ALA B C   1 
ATOM   984  O  O   . ALA B 1 5   ? 18.343 -6.788  19.529 1.00 26.08 ? 4   ALA B O   1 
ATOM   985  C  CB  . ALA B 1 5   ? 19.610 -5.748  16.497 1.00 19.92 ? 4   ALA B CB  1 
ATOM   986  N  N   . VAL B 1 6   ? 20.015 -5.275  19.487 1.00 23.22 ? 5   VAL B N   1 
ATOM   987  C  CA  . VAL B 1 6   ? 19.673 -4.734  20.790 1.00 17.67 ? 5   VAL B CA  1 
ATOM   988  C  C   . VAL B 1 6   ? 20.220 -3.315  20.825 1.00 21.32 ? 5   VAL B C   1 
ATOM   989  O  O   . VAL B 1 6   ? 21.158 -2.982  20.108 1.00 20.42 ? 5   VAL B O   1 
ATOM   990  C  CB  . VAL B 1 6   ? 20.374 -5.613  21.914 1.00 20.61 ? 5   VAL B CB  1 
ATOM   991  C  CG1 . VAL B 1 6   ? 21.902 -5.487  21.773 1.00 19.02 ? 5   VAL B CG1 1 
ATOM   992  C  CG2 . VAL B 1 6   ? 19.898 -5.202  23.323 1.00 21.38 ? 5   VAL B CG2 1 
ATOM   993  N  N   . ALA B 1 7   ? 19.592 -2.485  21.640 1.00 18.42 ? 6   ALA B N   1 
ATOM   994  C  CA  . ALA B 1 7   ? 20.028 -1.119  21.818 1.00 21.67 ? 6   ALA B CA  1 
ATOM   995  C  C   . ALA B 1 7   ? 19.811 -0.881  23.278 1.00 19.51 ? 6   ALA B C   1 
ATOM   996  O  O   . ALA B 1 7   ? 18.785 -1.278  23.834 1.00 22.57 ? 6   ALA B O   1 
ATOM   997  C  CB  . ALA B 1 7   ? 19.159 -0.103  20.986 1.00 24.63 ? 6   ALA B CB  1 
ATOM   998  N  N   . VAL B 1 8   ? 20.772 -0.235  23.904 1.00 21.65 ? 7   VAL B N   1 
ATOM   999  C  CA  . VAL B 1 8   ? 20.638 0.119   25.307 1.00 23.44 ? 7   VAL B CA  1 
ATOM   1000 C  C   . VAL B 1 8   ? 20.387 1.630   25.306 1.00 20.88 ? 7   VAL B C   1 
ATOM   1001 O  O   . VAL B 1 8   ? 21.224 2.397   24.822 1.00 23.72 ? 7   VAL B O   1 
ATOM   1002 C  CB  . VAL B 1 8   ? 21.925 -0.217  26.116 1.00 27.21 ? 7   VAL B CB  1 
ATOM   1003 C  CG1 . VAL B 1 8   ? 21.735 0.238   27.577 1.00 28.08 ? 7   VAL B CG1 1 
ATOM   1004 C  CG2 . VAL B 1 8   ? 22.177 -1.742  26.065 1.00 21.96 ? 7   VAL B CG2 1 
ATOM   1005 N  N   . LEU B 1 9   ? 19.219 2.045   25.806 1.00 20.68 ? 8   LEU B N   1 
ATOM   1006 C  CA  . LEU B 1 9   ? 18.871 3.463   25.815 1.00 23.64 ? 8   LEU B CA  1 
ATOM   1007 C  C   . LEU B 1 9   ? 19.384 4.138   27.087 1.00 25.50 ? 8   LEU B C   1 
ATOM   1008 O  O   . LEU B 1 9   ? 19.091 3.676   28.188 1.00 24.91 ? 8   LEU B O   1 
ATOM   1009 C  CB  . LEU B 1 9   ? 17.344 3.664   25.735 1.00 23.98 ? 8   LEU B CB  1 
ATOM   1010 C  CG  . LEU B 1 9   ? 16.616 3.095   24.509 1.00 27.12 ? 8   LEU B CG  1 
ATOM   1011 C  CD1 . LEU B 1 9   ? 15.063 3.269   24.597 1.00 22.51 ? 8   LEU B CD1 1 
ATOM   1012 C  CD2 . LEU B 1 9   ? 17.179 3.770   23.301 1.00 27.48 ? 8   LEU B CD2 1 
ATOM   1013 N  N   . LYS B 1 10  ? 20.136 5.231   26.915 1.00 30.88 ? 9   LYS B N   1 
ATOM   1014 C  CA  . LYS B 1 10  ? 20.699 6.014   28.025 1.00 32.32 ? 9   LYS B CA  1 
ATOM   1015 C  C   . LYS B 1 10  ? 20.691 7.481   27.629 1.00 30.17 ? 9   LYS B C   1 
ATOM   1016 O  O   . LYS B 1 10  ? 20.770 7.821   26.444 1.00 25.31 ? 9   LYS B O   1 
ATOM   1017 C  CB  . LYS B 1 10  ? 22.165 5.639   28.282 1.00 37.72 ? 9   LYS B CB  1 
ATOM   1018 C  CG  . LYS B 1 10  ? 22.432 4.231   28.724 1.00 43.36 ? 9   LYS B CG  1 
ATOM   1019 C  CD  . LYS B 1 10  ? 23.946 4.019   28.815 1.00 50.93 ? 9   LYS B CD  1 
ATOM   1020 C  CE  . LYS B 1 10  ? 24.334 2.572   29.050 1.00 54.21 ? 9   LYS B CE  1 
ATOM   1021 N  NZ  . LYS B 1 10  ? 25.802 2.412   28.840 1.00 59.23 ? 9   LYS B NZ  1 
ATOM   1022 N  N   . GLY B 1 11  ? 20.638 8.356   28.625 1.00 35.86 ? 10  GLY B N   1 
ATOM   1023 C  CA  . GLY B 1 11  ? 20.627 9.772   28.340 1.00 36.26 ? 10  GLY B CA  1 
ATOM   1024 C  C   . GLY B 1 11  ? 21.042 10.581  29.556 1.00 43.41 ? 10  GLY B C   1 
ATOM   1025 O  O   . GLY B 1 11  ? 21.602 10.043  30.517 1.00 40.94 ? 10  GLY B O   1 
ATOM   1026 N  N   . ASP B 1 12  ? 20.740 11.875  29.498 1.00 44.67 ? 11  ASP B N   1 
ATOM   1027 C  CA  . ASP B 1 12  ? 21.058 12.824  30.551 1.00 52.64 ? 11  ASP B CA  1 
ATOM   1028 C  C   . ASP B 1 12  ? 20.276 12.562  31.816 1.00 51.97 ? 11  ASP B C   1 
ATOM   1029 O  O   . ASP B 1 12  ? 20.828 12.609  32.915 1.00 52.67 ? 11  ASP B O   1 
ATOM   1030 C  CB  . ASP B 1 12  ? 20.748 14.243  30.077 1.00 57.82 ? 11  ASP B CB  1 
ATOM   1031 C  CG  . ASP B 1 12  ? 21.953 14.938  29.474 1.00 66.14 ? 11  ASP B CG  1 
ATOM   1032 O  OD1 . ASP B 1 12  ? 22.860 14.236  28.965 1.00 66.82 ? 11  ASP B OD1 1 
ATOM   1033 O  OD2 . ASP B 1 12  ? 21.984 16.192  29.502 1.00 67.04 ? 11  ASP B OD2 1 
ATOM   1034 N  N   . GLY B 1 13  ? 18.986 12.289  31.654 1.00 49.15 ? 12  GLY B N   1 
ATOM   1035 C  CA  . GLY B 1 13  ? 18.127 12.084  32.802 1.00 41.44 ? 12  GLY B CA  1 
ATOM   1036 C  C   . GLY B 1 13  ? 17.927 10.669  33.301 1.00 38.58 ? 12  GLY B C   1 
ATOM   1037 O  O   . GLY B 1 13  ? 18.780 9.792   33.160 1.00 41.95 ? 12  GLY B O   1 
ATOM   1038 N  N   . PRO B 1 14  ? 16.756 10.413  33.874 1.00 36.55 ? 13  PRO B N   1 
ATOM   1039 C  CA  . PRO B 1 14  ? 16.405 9.106   34.418 1.00 34.41 ? 13  PRO B CA  1 
ATOM   1040 C  C   . PRO B 1 14  ? 15.902 8.076   33.391 1.00 30.21 ? 13  PRO B C   1 
ATOM   1041 O  O   . PRO B 1 14  ? 15.648 6.950   33.754 1.00 34.51 ? 13  PRO B O   1 
ATOM   1042 C  CB  . PRO B 1 14  ? 15.300 9.455   35.395 1.00 34.65 ? 13  PRO B CB  1 
ATOM   1043 C  CG  . PRO B 1 14  ? 14.506 10.436  34.576 1.00 33.62 ? 13  PRO B CG  1 
ATOM   1044 C  CD  . PRO B 1 14  ? 15.608 11.338  33.963 1.00 33.75 ? 13  PRO B CD  1 
ATOM   1045 N  N   . VAL B 1 15  ? 15.741 8.441   32.129 1.00 26.40 ? 14  VAL B N   1 
ATOM   1046 C  CA  . VAL B 1 15  ? 15.206 7.460   31.185 1.00 25.74 ? 14  VAL B CA  1 
ATOM   1047 C  C   . VAL B 1 15  ? 16.251 6.418   30.774 1.00 26.12 ? 14  VAL B C   1 
ATOM   1048 O  O   . VAL B 1 15  ? 17.319 6.756   30.280 1.00 25.85 ? 14  VAL B O   1 
ATOM   1049 C  CB  . VAL B 1 15  ? 14.593 8.164   29.941 1.00 25.65 ? 14  VAL B CB  1 
ATOM   1050 C  CG1 . VAL B 1 15  ? 14.134 7.116   28.917 1.00 27.20 ? 14  VAL B CG1 1 
ATOM   1051 C  CG2 . VAL B 1 15  ? 13.367 8.974   30.377 1.00 27.79 ? 14  VAL B CG2 1 
ATOM   1052 N  N   . GLN B 1 16  ? 15.955 5.157   31.057 1.00 25.41 ? 15  GLN B N   1 
ATOM   1053 C  CA  . GLN B 1 16  ? 16.841 4.044   30.715 1.00 31.56 ? 15  GLN B CA  1 
ATOM   1054 C  C   . GLN B 1 16  ? 16.012 2.910   30.162 1.00 24.31 ? 15  GLN B C   1 
ATOM   1055 O  O   . GLN B 1 16  ? 14.872 2.717   30.557 1.00 25.13 ? 15  GLN B O   1 
ATOM   1056 C  CB  . GLN B 1 16  ? 17.529 3.405   31.930 1.00 32.03 ? 15  GLN B CB  1 
ATOM   1057 C  CG  . GLN B 1 16  ? 17.844 4.258   33.094 1.00 48.44 ? 15  GLN B CG  1 
ATOM   1058 C  CD  . GLN B 1 16  ? 18.607 3.472   34.156 1.00 50.00 ? 15  GLN B CD  1 
ATOM   1059 O  OE1 . GLN B 1 16  ? 18.043 3.065   35.174 1.00 55.52 ? 15  GLN B OE1 1 
ATOM   1060 N  NE2 . GLN B 1 16  ? 19.893 3.241   33.906 1.00 51.78 ? 15  GLN B NE2 1 
ATOM   1061 N  N   . GLY B 1 17  ? 16.608 2.108   29.290 1.00 25.47 ? 16  GLY B N   1 
ATOM   1062 C  CA  . GLY B 1 17  ? 15.854 0.965   28.811 1.00 24.39 ? 16  GLY B CA  1 
ATOM   1063 C  C   . GLY B 1 17  ? 16.692 0.024   27.967 1.00 24.01 ? 16  GLY B C   1 
ATOM   1064 O  O   . GLY B 1 17  ? 17.793 0.374   27.553 1.00 25.99 ? 16  GLY B O   1 
ATOM   1065 N  N   . ILE B 1 18  ? 16.184 -1.186  27.749 1.00 22.35 ? 17  ILE B N   1 
ATOM   1066 C  CA  . ILE B 1 18  ? 16.849 -2.141  26.865 1.00 24.71 ? 17  ILE B CA  1 
ATOM   1067 C  C   . ILE B 1 18  ? 15.784 -2.589  25.882 1.00 23.34 ? 17  ILE B C   1 
ATOM   1068 O  O   . ILE B 1 18  ? 14.718 -3.025  26.268 1.00 23.74 ? 17  ILE B O   1 
ATOM   1069 C  CB  . ILE B 1 18  ? 17.408 -3.362  27.627 1.00 25.36 ? 17  ILE B CB  1 
ATOM   1070 C  CG1 . ILE B 1 18  ? 18.613 -2.900  28.477 1.00 30.08 ? 17  ILE B CG1 1 
ATOM   1071 C  CG2 . ILE B 1 18  ? 17.812 -4.469  26.613 1.00 24.96 ? 17  ILE B CG2 1 
ATOM   1072 C  CD1 . ILE B 1 18  ? 19.105 -3.936  29.532 1.00 28.22 ? 17  ILE B CD1 1 
ATOM   1073 N  N   . ILE B 1 19  ? 16.068 -2.423  24.597 1.00 26.29 ? 18  ILE B N   1 
ATOM   1074 C  CA  . ILE B 1 19  ? 15.126 -2.799  23.564 1.00 20.37 ? 18  ILE B CA  1 
ATOM   1075 C  C   . ILE B 1 19  ? 15.785 -3.850  22.644 1.00 25.79 ? 18  ILE B C   1 
ATOM   1076 O  O   . ILE B 1 19  ? 16.896 -3.647  22.144 1.00 22.83 ? 18  ILE B O   1 
ATOM   1077 C  CB  . ILE B 1 19  ? 14.739 -1.560  22.689 1.00 22.40 ? 18  ILE B CB  1 
ATOM   1078 C  CG1 . ILE B 1 19  ? 14.060 -0.475  23.559 1.00 22.61 ? 18  ILE B CG1 1 
ATOM   1079 C  CG2 . ILE B 1 19  ? 13.837 -2.026  21.520 1.00 20.37 ? 18  ILE B CG2 1 
ATOM   1080 C  CD1 . ILE B 1 19  ? 12.741 -0.932  24.262 1.00 19.46 ? 18  ILE B CD1 1 
ATOM   1081 N  N   . ASN B 1 20  ? 15.074 -4.944  22.412 1.00 24.31 ? 19  ASN B N   1 
ATOM   1082 C  CA  . ASN B 1 20  ? 15.546 -6.039  21.544 1.00 25.80 ? 19  ASN B CA  1 
ATOM   1083 C  C   . ASN B 1 20  ? 14.836 -5.996  20.216 1.00 27.91 ? 19  ASN B C   1 
ATOM   1084 O  O   . ASN B 1 20  ? 13.723 -5.475  20.148 1.00 29.27 ? 19  ASN B O   1 
ATOM   1085 C  CB  . ASN B 1 20  ? 15.213 -7.372  22.215 1.00 27.55 ? 19  ASN B CB  1 
ATOM   1086 C  CG  . ASN B 1 20  ? 15.841 -7.482  23.575 1.00 33.17 ? 19  ASN B CG  1 
ATOM   1087 O  OD1 . ASN B 1 20  ? 17.064 -7.465  23.688 1.00 27.92 ? 19  ASN B OD1 1 
ATOM   1088 N  ND2 . ASN B 1 20  ? 15.015 -7.582  24.620 1.00 29.32 ? 19  ASN B ND2 1 
ATOM   1089 N  N   . PHE B 1 21  ? 15.474 -6.570  19.182 1.00 28.36 ? 20  PHE B N   1 
ATOM   1090 C  CA  . PHE B 1 21  ? 14.942 -6.661  17.812 1.00 26.13 ? 20  PHE B CA  1 
ATOM   1091 C  C   . PHE B 1 21  ? 15.267 -8.069  17.335 1.00 31.69 ? 20  PHE B C   1 
ATOM   1092 O  O   . PHE B 1 21  ? 16.321 -8.634  17.687 1.00 27.83 ? 20  PHE B O   1 
ATOM   1093 C  CB  . PHE B 1 21  ? 15.653 -5.717  16.808 1.00 23.37 ? 20  PHE B CB  1 
ATOM   1094 C  CG  . PHE B 1 21  ? 15.630 -4.271  17.196 1.00 21.10 ? 20  PHE B CG  1 
ATOM   1095 C  CD1 . PHE B 1 21  ? 14.708 -3.394  16.616 1.00 28.33 ? 20  PHE B CD1 1 
ATOM   1096 C  CD2 . PHE B 1 21  ? 16.539 -3.786  18.130 1.00 24.53 ? 20  PHE B CD2 1 
ATOM   1097 C  CE1 . PHE B 1 21  ? 14.691 -2.029  16.976 1.00 22.54 ? 20  PHE B CE1 1 
ATOM   1098 C  CE2 . PHE B 1 21  ? 16.531 -2.421  18.497 1.00 23.25 ? 20  PHE B CE2 1 
ATOM   1099 C  CZ  . PHE B 1 21  ? 15.613 -1.560  17.926 1.00 22.61 ? 20  PHE B CZ  1 
ATOM   1100 N  N   . GLU B 1 22  ? 14.377 -8.613  16.508 1.00 25.77 ? 21  GLU B N   1 
ATOM   1101 C  CA  . GLU B 1 22  ? 14.554 -9.948  15.956 1.00 29.10 ? 21  GLU B CA  1 
ATOM   1102 C  C   . GLU B 1 22  ? 13.777 -10.009 14.646 1.00 31.61 ? 21  GLU B C   1 
ATOM   1103 O  O   . GLU B 1 22  ? 12.631 -9.591  14.575 1.00 32.18 ? 21  GLU B O   1 
ATOM   1104 C  CB  . GLU B 1 22  ? 14.008 -10.971 16.928 1.00 35.01 ? 21  GLU B CB  1 
ATOM   1105 C  CG  . GLU B 1 22  ? 13.545 -12.263 16.300 1.00 48.45 ? 21  GLU B CG  1 
ATOM   1106 C  CD  . GLU B 1 22  ? 13.248 -13.307 17.355 1.00 58.02 ? 21  GLU B CD  1 
ATOM   1107 O  OE1 . GLU B 1 22  ? 14.213 -13.972 17.790 1.00 62.31 ? 21  GLU B OE1 1 
ATOM   1108 O  OE2 . GLU B 1 22  ? 12.066 -13.442 17.760 1.00 58.72 ? 21  GLU B OE2 1 
ATOM   1109 N  N   . GLN B 1 23  ? 14.417 -10.518 13.609 1.00 30.33 ? 22  GLN B N   1 
ATOM   1110 C  CA  . GLN B 1 23  ? 13.779 -10.625 12.306 1.00 36.35 ? 22  GLN B CA  1 
ATOM   1111 C  C   . GLN B 1 23  ? 14.084 -12.028 11.841 1.00 41.43 ? 22  GLN B C   1 
ATOM   1112 O  O   . GLN B 1 23  ? 15.238 -12.376 11.619 1.00 37.18 ? 22  GLN B O   1 
ATOM   1113 C  CB  . GLN B 1 23  ? 14.374 -9.608  11.349 1.00 33.97 ? 22  GLN B CB  1 
ATOM   1114 C  CG  . GLN B 1 23  ? 13.818 -9.671  9.914  1.00 36.72 ? 22  GLN B CG  1 
ATOM   1115 C  CD  . GLN B 1 23  ? 14.409 -8.578  9.080  1.00 32.59 ? 22  GLN B CD  1 
ATOM   1116 O  OE1 . GLN B 1 23  ? 15.587 -8.245  9.238  1.00 39.50 ? 22  GLN B OE1 1 
ATOM   1117 N  NE2 . GLN B 1 23  ? 13.612 -8.001  8.184  1.00 39.66 ? 22  GLN B NE2 1 
ATOM   1118 N  N   . LYS B 1 24  ? 13.032 -12.831 11.753 1.00 53.56 ? 23  LYS B N   1 
ATOM   1119 C  CA  . LYS B 1 24  ? 13.118 -14.221 11.354 1.00 59.30 ? 23  LYS B CA  1 
ATOM   1120 C  C   . LYS B 1 24  ? 13.505 -14.363 9.899  1.00 60.44 ? 23  LYS B C   1 
ATOM   1121 O  O   . LYS B 1 24  ? 14.550 -14.920 9.579  1.00 59.82 ? 23  LYS B O   1 
ATOM   1122 C  CB  . LYS B 1 24  ? 11.773 -14.888 11.607 1.00 67.79 ? 23  LYS B CB  1 
ATOM   1123 C  CG  . LYS B 1 24  ? 11.703 -16.358 11.247 1.00 79.60 ? 23  LYS B CG  1 
ATOM   1124 C  CD  . LYS B 1 24  ? 10.288 -16.882 11.494 1.00 85.26 ? 23  LYS B CD  1 
ATOM   1125 C  CE  . LYS B 1 24  ? 10.148 -18.370 11.187 1.00 86.61 ? 23  LYS B CE  1 
ATOM   1126 N  NZ  . LYS B 1 24  ? 8.741  -18.834 11.419 1.00 88.25 ? 23  LYS B NZ  1 
ATOM   1127 N  N   . GLU B 1 25  ? 12.653 -13.863 9.015  1.00 63.38 ? 24  GLU B N   1 
ATOM   1128 C  CA  . GLU B 1 25  ? 12.921 -13.945 7.587  1.00 64.57 ? 24  GLU B CA  1 
ATOM   1129 C  C   . GLU B 1 25  ? 13.604 -12.673 7.094  1.00 63.96 ? 24  GLU B C   1 
ATOM   1130 O  O   . GLU B 1 25  ? 13.213 -11.558 7.452  1.00 56.83 ? 24  GLU B O   1 
ATOM   1131 C  CB  . GLU B 1 25  ? 11.617 -14.193 6.819  1.00 69.49 ? 24  GLU B CB  1 
ATOM   1132 C  CG  . GLU B 1 25  ? 10.963 -15.560 7.095  1.00 77.62 ? 24  GLU B CG  1 
ATOM   1133 C  CD  . GLU B 1 25  ? 11.772 -16.743 6.540  1.00 81.01 ? 24  GLU B CD  1 
ATOM   1134 O  OE1 . GLU B 1 25  ? 12.085 -16.738 5.329  1.00 86.07 ? 24  GLU B OE1 1 
ATOM   1135 O  OE2 . GLU B 1 25  ? 12.090 -17.681 7.304  1.00 79.64 ? 24  GLU B OE2 1 
ATOM   1136 N  N   . SER B 1 26  ? 14.628 -12.875 6.268  1.00 66.80 ? 25  SER B N   1 
ATOM   1137 C  CA  . SER B 1 26  ? 15.451 -11.817 5.695  1.00 68.54 ? 25  SER B CA  1 
ATOM   1138 C  C   . SER B 1 26  ? 14.705 -10.576 5.257  1.00 68.39 ? 25  SER B C   1 
ATOM   1139 O  O   . SER B 1 26  ? 15.251 -9.475  5.315  1.00 71.46 ? 25  SER B O   1 
ATOM   1140 C  CB  . SER B 1 26  ? 16.265 -12.364 4.511  1.00 72.82 ? 25  SER B CB  1 
ATOM   1141 O  OG  . SER B 1 26  ? 17.204 -11.407 4.040  1.00 75.92 ? 25  SER B OG  1 
ATOM   1142 N  N   . ASN B 1 27  ? 13.465 -10.731 4.812  1.00 65.46 ? 26  ASN B N   1 
ATOM   1143 C  CA  . ASN B 1 27  ? 12.718 -9.558  4.391  1.00 65.66 ? 26  ASN B CA  1 
ATOM   1144 C  C   . ASN B 1 27  ? 11.442 -9.426  5.215  1.00 60.58 ? 26  ASN B C   1 
ATOM   1145 O  O   . ASN B 1 27  ? 10.631 -8.541  4.952  1.00 58.77 ? 26  ASN B O   1 
ATOM   1146 C  CB  . ASN B 1 27  ? 12.369 -9.649  2.897  1.00 71.45 ? 26  ASN B CB  1 
ATOM   1147 C  CG  . ASN B 1 27  ? 11.198 -10.590 2.618  1.00 80.10 ? 26  ASN B CG  1 
ATOM   1148 O  OD1 . ASN B 1 27  ? 11.200 -11.754 3.036  1.00 85.08 ? 26  ASN B OD1 1 
ATOM   1149 N  ND2 . ASN B 1 27  ? 10.192 -10.088 1.903  1.00 81.60 ? 26  ASN B ND2 1 
ATOM   1150 N  N   . GLY B 1 28  ? 11.288 -10.290 6.225  1.00 52.97 ? 27  GLY B N   1 
ATOM   1151 C  CA  . GLY B 1 28  ? 10.088 -10.287 7.049  1.00 47.50 ? 27  GLY B CA  1 
ATOM   1152 C  C   . GLY B 1 28  ? 9.924  -9.110  7.986  1.00 45.25 ? 27  GLY B C   1 
ATOM   1153 O  O   . GLY B 1 28  ? 10.690 -8.147  7.915  1.00 41.12 ? 27  GLY B O   1 
ATOM   1154 N  N   . PRO B 1 29  ? 8.893  -9.134  8.850  1.00 43.96 ? 28  PRO B N   1 
ATOM   1155 C  CA  . PRO B 1 29  ? 8.692  -8.024  9.785  1.00 41.67 ? 28  PRO B CA  1 
ATOM   1156 C  C   . PRO B 1 29  ? 9.715  -8.126  10.921 1.00 37.61 ? 28  PRO B C   1 
ATOM   1157 O  O   . PRO B 1 29  ? 10.203 -9.213  11.218 1.00 32.29 ? 28  PRO B O   1 
ATOM   1158 C  CB  . PRO B 1 29  ? 7.268  -8.244  10.284 1.00 43.03 ? 28  PRO B CB  1 
ATOM   1159 C  CG  . PRO B 1 29  ? 7.139  -9.749  10.283 1.00 50.52 ? 28  PRO B CG  1 
ATOM   1160 C  CD  . PRO B 1 29  ? 7.813  -10.136 8.969  1.00 47.41 ? 28  PRO B CD  1 
ATOM   1161 N  N   . VAL B 1 30  ? 10.043 -7.002  11.542 1.00 36.73 ? 29  VAL B N   1 
ATOM   1162 C  CA  . VAL B 1 30  ? 10.987 -7.026  12.664 1.00 33.99 ? 29  VAL B CA  1 
ATOM   1163 C  C   . VAL B 1 30  ? 10.179 -6.881  13.922 1.00 34.27 ? 29  VAL B C   1 
ATOM   1164 O  O   . VAL B 1 30  ? 9.318  -6.003  13.989 1.00 35.16 ? 29  VAL B O   1 
ATOM   1165 C  CB  . VAL B 1 30  ? 12.005 -5.845  12.619 1.00 29.44 ? 29  VAL B CB  1 
ATOM   1166 C  CG1 . VAL B 1 30  ? 12.972 -5.928  13.858 1.00 21.28 ? 29  VAL B CG1 1 
ATOM   1167 C  CG2 . VAL B 1 30  ? 12.842 -5.907  11.302 1.00 28.31 ? 29  VAL B CG2 1 
ATOM   1168 N  N   . LYS B 1 31  ? 10.437 -7.740  14.911 1.00 31.25 ? 30  LYS B N   1 
ATOM   1169 C  CA  . LYS B 1 31  ? 9.728  -7.645  16.191 1.00 32.72 ? 30  LYS B CA  1 
ATOM   1170 C  C   . LYS B 1 31  ? 10.616 -6.842  17.150 1.00 30.85 ? 30  LYS B C   1 
ATOM   1171 O  O   . LYS B 1 31  ? 11.821 -7.111  17.262 1.00 25.78 ? 30  LYS B O   1 
ATOM   1172 C  CB  . LYS B 1 31  ? 9.482  -9.033  16.783 1.00 37.48 ? 30  LYS B CB  1 
ATOM   1173 C  CG  . LYS B 1 31  ? 8.411  -9.839  16.066 1.00 53.96 ? 30  LYS B CG  1 
ATOM   1174 C  CD  . LYS B 1 31  ? 8.342  -11.271 16.604 1.00 60.32 ? 30  LYS B CD  1 
ATOM   1175 C  CE  . LYS B 1 31  ? 7.249  -12.089 15.906 1.00 66.78 ? 30  LYS B CE  1 
ATOM   1176 N  NZ  . LYS B 1 31  ? 7.067  -13.429 16.558 1.00 64.95 ? 30  LYS B NZ  1 
ATOM   1177 N  N   . VAL B 1 32  ? 10.020 -5.881  17.846 1.00 27.73 ? 31  VAL B N   1 
ATOM   1178 C  CA  . VAL B 1 32  ? 10.769 -5.004  18.773 1.00 22.78 ? 31  VAL B CA  1 
ATOM   1179 C  C   . VAL B 1 32  ? 10.144 -5.149  20.153 1.00 27.93 ? 31  VAL B C   1 
ATOM   1180 O  O   . VAL B 1 32  ? 8.900  -5.021  20.296 1.00 31.36 ? 31  VAL B O   1 
ATOM   1181 C  CB  . VAL B 1 32  ? 10.636 -3.510  18.312 1.00 29.86 ? 31  VAL B CB  1 
ATOM   1182 C  CG1 . VAL B 1 32  ? 11.611 -2.605  19.088 1.00 27.82 ? 31  VAL B CG1 1 
ATOM   1183 C  CG2 . VAL B 1 32  ? 10.910 -3.391  16.825 1.00 22.33 ? 31  VAL B CG2 1 
ATOM   1184 N  N   . TRP B 1 33  ? 10.955 -5.428  21.172 1.00 21.46 ? 32  TRP B N   1 
ATOM   1185 C  CA  . TRP B 1 33  ? 10.385 -5.583  22.503 1.00 26.74 ? 32  TRP B CA  1 
ATOM   1186 C  C   . TRP B 1 33  ? 11.396 -5.247  23.572 1.00 30.18 ? 32  TRP B C   1 
ATOM   1187 O  O   . TRP B 1 33  ? 12.610 -5.246  23.315 1.00 32.00 ? 32  TRP B O   1 
ATOM   1188 C  CB  . TRP B 1 33  ? 9.845  -7.009  22.711 1.00 30.06 ? 32  TRP B CB  1 
ATOM   1189 C  CG  . TRP B 1 33  ? 10.894 -8.059  22.961 1.00 30.31 ? 32  TRP B CG  1 
ATOM   1190 C  CD1 . TRP B 1 33  ? 11.293 -8.538  24.176 1.00 37.03 ? 32  TRP B CD1 1 
ATOM   1191 C  CD2 . TRP B 1 33  ? 11.712 -8.720  21.985 1.00 33.13 ? 32  TRP B CD2 1 
ATOM   1192 N  NE1 . TRP B 1 33  ? 12.302 -9.448  24.017 1.00 36.65 ? 32  TRP B NE1 1 
ATOM   1193 C  CE2 . TRP B 1 33  ? 12.578 -9.582  22.683 1.00 35.54 ? 32  TRP B CE2 1 
ATOM   1194 C  CE3 . TRP B 1 33  ? 11.791 -8.672  20.590 1.00 30.68 ? 32  TRP B CE3 1 
ATOM   1195 C  CZ2 . TRP B 1 33  ? 13.521 -10.395 22.031 1.00 38.31 ? 32  TRP B CZ2 1 
ATOM   1196 C  CZ3 . TRP B 1 33  ? 12.730 -9.485  19.938 1.00 34.90 ? 32  TRP B CZ3 1 
ATOM   1197 C  CH2 . TRP B 1 33  ? 13.580 -10.332 20.664 1.00 35.48 ? 32  TRP B CH2 1 
ATOM   1198 N  N   . GLY B 1 34  ? 10.890 -4.949  24.763 1.00 19.92 ? 33  GLY B N   1 
ATOM   1199 C  CA  . GLY B 1 34  ? 11.783 -4.607  25.846 1.00 25.38 ? 33  GLY B CA  1 
ATOM   1200 C  C   . GLY B 1 34  ? 11.075 -3.660  26.785 1.00 23.27 ? 33  GLY B C   1 
ATOM   1201 O  O   . GLY B 1 34  ? 9.849  -3.581  26.773 1.00 25.82 ? 33  GLY B O   1 
ATOM   1202 N  N   . SER B 1 35  ? 11.855 -2.908  27.549 1.00 25.89 ? 34  SER B N   1 
ATOM   1203 C  CA  . SER B 1 35  ? 11.303 -1.983  28.532 1.00 27.51 ? 34  SER B CA  1 
ATOM   1204 C  C   . SER B 1 35  ? 12.107 -0.692  28.669 1.00 24.32 ? 34  SER B C   1 
ATOM   1205 O  O   . SER B 1 35  ? 13.321 -0.642  28.449 1.00 25.87 ? 34  SER B O   1 
ATOM   1206 C  CB  . SER B 1 35  ? 11.265 -2.674  29.895 1.00 31.02 ? 34  SER B CB  1 
ATOM   1207 O  OG  . SER B 1 35  ? 10.203 -2.137  30.668 1.00 43.83 ? 34  SER B OG  1 
ATOM   1208 N  N   . ILE B 1 36  ? 11.409 0.353   29.066 1.00 25.76 ? 35  ILE B N   1 
ATOM   1209 C  CA  . ILE B 1 36  ? 12.039 1.641   29.269 1.00 25.00 ? 35  ILE B CA  1 
ATOM   1210 C  C   . ILE B 1 36  ? 11.413 2.202   30.549 1.00 23.38 ? 35  ILE B C   1 
ATOM   1211 O  O   . ILE B 1 36  ? 10.202 2.150   30.685 1.00 25.71 ? 35  ILE B O   1 
ATOM   1212 C  CB  . ILE B 1 36  ? 11.717 2.609   28.096 1.00 20.83 ? 35  ILE B CB  1 
ATOM   1213 C  CG1 . ILE B 1 36  ? 11.946 1.909   26.756 1.00 22.37 ? 35  ILE B CG1 1 
ATOM   1214 C  CG2 . ILE B 1 36  ? 12.608 3.837   28.179 1.00 23.83 ? 35  ILE B CG2 1 
ATOM   1215 C  CD1 . ILE B 1 36  ? 11.574 2.793   25.524 1.00 22.10 ? 35  ILE B CD1 1 
ATOM   1216 N  N   . LYS B 1 37  ? 12.218 2.729   31.479 1.00 22.18 ? 36  LYS B N   1 
ATOM   1217 C  CA  . LYS B 1 37  ? 11.642 3.304   32.695 1.00 23.76 ? 36  LYS B CA  1 
ATOM   1218 C  C   . LYS B 1 37  ? 12.137 4.732   32.804 1.00 27.86 ? 36  LYS B C   1 
ATOM   1219 O  O   . LYS B 1 37  ? 13.002 5.145   32.023 1.00 25.37 ? 36  LYS B O   1 
ATOM   1220 C  CB  . LYS B 1 37  ? 12.067 2.492   33.939 1.00 31.29 ? 36  LYS B CB  1 
ATOM   1221 C  CG  . LYS B 1 37  ? 13.570 2.392   34.175 1.00 36.57 ? 36  LYS B CG  1 
ATOM   1222 C  CD  . LYS B 1 37  ? 13.862 1.374   35.293 1.00 51.11 ? 36  LYS B CD  1 
ATOM   1223 C  CE  . LYS B 1 37  ? 15.355 1.042   35.396 1.00 54.26 ? 36  LYS B CE  1 
ATOM   1224 N  NZ  . LYS B 1 37  ? 15.843 0.177   34.245 1.00 61.62 ? 36  LYS B NZ  1 
ATOM   1225 N  N   . GLY B 1 38  ? 11.593 5.481   33.773 1.00 35.18 ? 37  GLY B N   1 
ATOM   1226 C  CA  . GLY B 1 38  ? 11.996 6.873   33.992 1.00 25.38 ? 37  GLY B CA  1 
ATOM   1227 C  C   . GLY B 1 38  ? 11.259 7.893   33.148 1.00 26.51 ? 37  GLY B C   1 
ATOM   1228 O  O   . GLY B 1 38  ? 11.630 9.065   33.124 1.00 29.78 ? 37  GLY B O   1 
ATOM   1229 N  N   . LEU B 1 39  ? 10.185 7.471   32.489 1.00 23.23 ? 38  LEU B N   1 
ATOM   1230 C  CA  . LEU B 1 39  ? 9.401  8.355   31.581 1.00 25.28 ? 38  LEU B CA  1 
ATOM   1231 C  C   . LEU B 1 39  ? 8.153  8.938   32.232 1.00 23.79 ? 38  LEU B C   1 
ATOM   1232 O  O   . LEU B 1 39  ? 7.656  8.393   33.217 1.00 29.89 ? 38  LEU B O   1 
ATOM   1233 C  CB  . LEU B 1 39  ? 8.900  7.527   30.379 1.00 23.91 ? 38  LEU B CB  1 
ATOM   1234 C  CG  . LEU B 1 39  ? 9.926  6.909   29.436 1.00 23.23 ? 38  LEU B CG  1 
ATOM   1235 C  CD1 . LEU B 1 39  ? 9.345  5.647   28.634 1.00 19.28 ? 38  LEU B CD1 1 
ATOM   1236 C  CD2 . LEU B 1 39  ? 10.381 8.067   28.499 1.00 20.88 ? 38  LEU B CD2 1 
ATOM   1237 N  N   . THR B 1 40  ? 7.646  10.027  31.656 1.00 22.37 ? 39  THR B N   1 
ATOM   1238 C  CA  . THR B 1 40  ? 6.397  10.638  32.103 1.00 25.07 ? 39  THR B CA  1 
ATOM   1239 C  C   . THR B 1 40  ? 5.279  9.778   31.507 1.00 32.01 ? 39  THR B C   1 
ATOM   1240 O  O   . THR B 1 40  ? 5.397  9.285   30.356 1.00 32.40 ? 39  THR B O   1 
ATOM   1241 C  CB  . THR B 1 40  ? 6.226  12.082  31.552 1.00 26.91 ? 39  THR B CB  1 
ATOM   1242 O  OG1 . THR B 1 40  ? 6.410  12.081  30.134 1.00 30.45 ? 39  THR B OG1 1 
ATOM   1243 C  CG2 . THR B 1 40  ? 7.253  13.059  32.209 1.00 28.38 ? 39  THR B CG2 1 
ATOM   1244 N  N   . GLU B 1 41  ? 4.216  9.563   32.280 1.00 30.26 ? 40  GLU B N   1 
ATOM   1245 C  CA  . GLU B 1 41  ? 3.083  8.766   31.813 1.00 31.14 ? 40  GLU B CA  1 
ATOM   1246 C  C   . GLU B 1 41  ? 2.617  9.223   30.425 1.00 29.93 ? 40  GLU B C   1 
ATOM   1247 O  O   . GLU B 1 41  ? 2.637  10.429  30.104 1.00 26.72 ? 40  GLU B O   1 
ATOM   1248 C  CB  . GLU B 1 41  ? 1.899  8.867   32.782 1.00 34.64 ? 40  GLU B CB  1 
ATOM   1249 C  CG  . GLU B 1 41  ? 0.783  7.865   32.473 1.00 41.95 ? 40  GLU B CG  1 
ATOM   1250 C  CD  . GLU B 1 41  ? -0.374 7.956   33.460 1.00 55.69 ? 40  GLU B CD  1 
ATOM   1251 O  OE1 . GLU B 1 41  ? -0.124 8.266   34.642 1.00 60.55 ? 40  GLU B OE1 1 
ATOM   1252 O  OE2 . GLU B 1 41  ? -1.535 7.701   33.071 1.00 61.10 ? 40  GLU B OE2 1 
ATOM   1253 N  N   . GLY B 1 42  ? 2.217  8.265   29.591 1.00 28.72 ? 41  GLY B N   1 
ATOM   1254 C  CA  . GLY B 1 42  ? 1.750  8.639   28.264 1.00 26.74 ? 41  GLY B CA  1 
ATOM   1255 C  C   . GLY B 1 42  ? 2.616  8.252   27.079 1.00 24.84 ? 41  GLY B C   1 
ATOM   1256 O  O   . GLY B 1 42  ? 3.552  7.467   27.228 1.00 24.26 ? 41  GLY B O   1 
ATOM   1257 N  N   . LEU B 1 43  ? 2.301  8.827   25.902 1.00 27.47 ? 42  LEU B N   1 
ATOM   1258 C  CA  . LEU B 1 43  ? 2.982  8.517   24.643 1.00 30.42 ? 42  LEU B CA  1 
ATOM   1259 C  C   . LEU B 1 43  ? 4.296  9.227   24.424 1.00 26.10 ? 42  LEU B C   1 
ATOM   1260 O  O   . LEU B 1 43  ? 4.446  10.413  24.672 1.00 28.11 ? 42  LEU B O   1 
ATOM   1261 C  CB  . LEU B 1 43  ? 2.066  8.789   23.411 1.00 29.29 ? 42  LEU B CB  1 
ATOM   1262 C  CG  . LEU B 1 43  ? 0.654  8.193   23.411 1.00 31.74 ? 42  LEU B CG  1 
ATOM   1263 C  CD1 . LEU B 1 43  ? -0.077 8.597   22.140 1.00 32.93 ? 42  LEU B CD1 1 
ATOM   1264 C  CD2 . LEU B 1 43  ? 0.730  6.669   23.576 1.00 37.12 ? 42  LEU B CD2 1 
ATOM   1265 N  N   . HIS B 1 44  ? 5.247  8.486   23.891 1.00 25.13 ? 43  HIS B N   1 
ATOM   1266 C  CA  . HIS B 1 44  ? 6.577  9.010   23.634 1.00 25.48 ? 43  HIS B CA  1 
ATOM   1267 C  C   . HIS B 1 44  ? 7.056  8.553   22.259 1.00 25.03 ? 43  HIS B C   1 
ATOM   1268 O  O   . HIS B 1 44  ? 7.093  7.345   21.997 1.00 25.45 ? 43  HIS B O   1 
ATOM   1269 C  CB  . HIS B 1 44  ? 7.543  8.470   24.706 1.00 25.43 ? 43  HIS B CB  1 
ATOM   1270 C  CG  . HIS B 1 44  ? 7.355  9.082   26.060 1.00 26.73 ? 43  HIS B CG  1 
ATOM   1271 N  ND1 . HIS B 1 44  ? 7.986  10.248  26.439 1.00 29.10 ? 43  HIS B ND1 1 
ATOM   1272 C  CD2 . HIS B 1 44  ? 6.581  8.713   27.109 1.00 21.85 ? 43  HIS B CD2 1 
ATOM   1273 C  CE1 . HIS B 1 44  ? 7.607  10.574  27.659 1.00 23.82 ? 43  HIS B CE1 1 
ATOM   1274 N  NE2 . HIS B 1 44  ? 6.754  9.662   28.090 1.00 26.26 ? 43  HIS B NE2 1 
ATOM   1275 N  N   . GLY B 1 45  ? 7.420  9.514   21.403 1.00 19.16 ? 44  GLY B N   1 
ATOM   1276 C  CA  . GLY B 1 45  ? 7.947  9.213   20.085 1.00 25.43 ? 44  GLY B CA  1 
ATOM   1277 C  C   . GLY B 1 45  ? 9.069  8.186   20.143 1.00 25.99 ? 44  GLY B C   1 
ATOM   1278 O  O   . GLY B 1 45  ? 9.949  8.264   20.998 1.00 28.28 ? 44  GLY B O   1 
ATOM   1279 N  N   . PHE B 1 46  ? 9.063  7.234   19.215 1.00 26.55 ? 45  PHE B N   1 
ATOM   1280 C  CA  . PHE B 1 46  ? 10.051 6.144   19.235 1.00 26.48 ? 45  PHE B CA  1 
ATOM   1281 C  C   . PHE B 1 46  ? 10.541 5.983   17.805 1.00 27.07 ? 45  PHE B C   1 
ATOM   1282 O  O   . PHE B 1 46  ? 9.795  5.510   16.948 1.00 22.86 ? 45  PHE B O   1 
ATOM   1283 C  CB  . PHE B 1 46  ? 9.321  4.862   19.746 1.00 23.78 ? 45  PHE B CB  1 
ATOM   1284 C  CG  . PHE B 1 46  ? 10.245 3.748   20.194 1.00 25.94 ? 45  PHE B CG  1 
ATOM   1285 C  CD1 . PHE B 1 46  ? 11.243 3.987   21.131 1.00 25.16 ? 45  PHE B CD1 1 
ATOM   1286 C  CD2 . PHE B 1 46  ? 10.033 2.423   19.751 1.00 23.95 ? 45  PHE B CD2 1 
ATOM   1287 C  CE1 . PHE B 1 46  ? 12.039 2.918   21.652 1.00 25.14 ? 45  PHE B CE1 1 
ATOM   1288 C  CE2 . PHE B 1 46  ? 10.815 1.351   20.261 1.00 25.86 ? 45  PHE B CE2 1 
ATOM   1289 C  CZ  . PHE B 1 46  ? 11.806 1.598   21.203 1.00 20.17 ? 45  PHE B CZ  1 
ATOM   1290 N  N   . HIS B 1 47  ? 11.785 6.382   17.551 1.00 25.57 ? 46  HIS B N   1 
ATOM   1291 C  CA  . HIS B 1 47  ? 12.333 6.338   16.196 1.00 28.67 ? 46  HIS B CA  1 
ATOM   1292 C  C   . HIS B 1 47  ? 13.782 5.905   16.073 1.00 27.53 ? 46  HIS B C   1 
ATOM   1293 O  O   . HIS B 1 47  ? 14.600 6.052   16.997 1.00 27.53 ? 46  HIS B O   1 
ATOM   1294 C  CB  . HIS B 1 47  ? 12.317 7.739   15.527 1.00 32.72 ? 46  HIS B CB  1 
ATOM   1295 C  CG  . HIS B 1 47  ? 11.119 8.582   15.844 1.00 35.20 ? 46  HIS B CG  1 
ATOM   1296 N  ND1 . HIS B 1 47  ? 11.229 9.917   16.166 1.00 33.60 ? 46  HIS B ND1 1 
ATOM   1297 C  CD2 . HIS B 1 47  ? 9.792  8.321   15.775 1.00 37.65 ? 46  HIS B CD2 1 
ATOM   1298 C  CE1 . HIS B 1 47  ? 10.023 10.445  16.278 1.00 37.45 ? 46  HIS B CE1 1 
ATOM   1299 N  NE2 . HIS B 1 47  ? 9.134  9.497   16.045 1.00 34.86 ? 46  HIS B NE2 1 
ATOM   1300 N  N   . VAL B 1 48  ? 14.104 5.438   14.878 1.00 27.87 ? 47  VAL B N   1 
ATOM   1301 C  CA  . VAL B 1 48  ? 15.480 5.094   14.537 1.00 28.95 ? 47  VAL B CA  1 
ATOM   1302 C  C   . VAL B 1 48  ? 15.994 6.348   13.802 1.00 33.00 ? 47  VAL B C   1 
ATOM   1303 O  O   . VAL B 1 48  ? 15.396 6.784   12.794 1.00 27.56 ? 47  VAL B O   1 
ATOM   1304 C  CB  . VAL B 1 48  ? 15.549 3.912   13.538 1.00 34.98 ? 47  VAL B CB  1 
ATOM   1305 C  CG1 . VAL B 1 48  ? 17.028 3.651   13.105 1.00 24.02 ? 47  VAL B CG1 1 
ATOM   1306 C  CG2 . VAL B 1 48  ? 14.903 2.674   14.161 1.00 30.61 ? 47  VAL B CG2 1 
ATOM   1307 N  N   . HIS B 1 49  ? 17.046 6.944   14.322 1.00 28.62 ? 48  HIS B N   1 
ATOM   1308 C  CA  . HIS B 1 49  ? 17.714 8.043   13.670 1.00 30.71 ? 48  HIS B CA  1 
ATOM   1309 C  C   . HIS B 1 49  ? 18.903 7.565   12.832 1.00 31.46 ? 48  HIS B C   1 
ATOM   1310 O  O   . HIS B 1 49  ? 19.392 6.471   13.007 1.00 26.43 ? 48  HIS B O   1 
ATOM   1311 C  CB  . HIS B 1 49  ? 18.136 9.083   14.703 1.00 23.51 ? 48  HIS B CB  1 
ATOM   1312 C  CG  . HIS B 1 49  ? 17.011 9.915   15.229 1.00 34.64 ? 48  HIS B CG  1 
ATOM   1313 N  ND1 . HIS B 1 49  ? 17.018 11.288  15.180 1.00 35.99 ? 48  HIS B ND1 1 
ATOM   1314 C  CD2 . HIS B 1 49  ? 15.846 9.571   15.818 1.00 27.51 ? 48  HIS B CD2 1 
ATOM   1315 C  CE1 . HIS B 1 49  ? 15.907 11.752  15.706 1.00 34.35 ? 48  HIS B CE1 1 
ATOM   1316 N  NE2 . HIS B 1 49  ? 15.178 10.732  16.102 1.00 40.21 ? 48  HIS B NE2 1 
ATOM   1317 N  N   . GLU B 1 50  ? 19.349 8.404   11.910 1.00 31.52 ? 49  GLU B N   1 
ATOM   1318 C  CA  . GLU B 1 50  ? 20.278 8.000   10.863 1.00 28.41 ? 49  GLU B CA  1 
ATOM   1319 C  C   . GLU B 1 50  ? 21.649 7.455   11.301 1.00 21.56 ? 49  GLU B C   1 
ATOM   1320 O  O   . GLU B 1 50  ? 22.080 6.448   10.815 1.00 26.82 ? 49  GLU B O   1 
ATOM   1321 C  CB  . GLU B 1 50  ? 20.428 9.088   9.806  1.00 32.57 ? 49  GLU B CB  1 
ATOM   1322 C  CG  . GLU B 1 50  ? 21.345 8.709   8.676  1.00 33.30 ? 49  GLU B CG  1 
ATOM   1323 C  CD  . GLU B 1 50  ? 21.171 9.553   7.415  1.00 40.74 ? 49  GLU B CD  1 
ATOM   1324 O  OE1 . GLU B 1 50  ? 20.718 10.680  7.504  1.00 37.32 ? 49  GLU B OE1 1 
ATOM   1325 O  OE2 . GLU B 1 50  ? 21.515 9.074   6.338  1.00 42.48 ? 49  GLU B OE2 1 
ATOM   1326 N  N   . PHE B 1 51  ? 22.323 8.126   12.211 1.00 25.34 ? 50  PHE B N   1 
ATOM   1327 C  CA  . PHE B 1 51  ? 23.692 7.770   12.519 1.00 25.30 ? 50  PHE B CA  1 
ATOM   1328 C  C   . PHE B 1 51  ? 23.868 7.117   13.878 1.00 28.63 ? 50  PHE B C   1 
ATOM   1329 O  O   . PHE B 1 51  ? 23.259 7.514   14.845 1.00 26.54 ? 50  PHE B O   1 
ATOM   1330 C  CB  . PHE B 1 51  ? 24.638 8.959   12.341 1.00 27.72 ? 50  PHE B CB  1 
ATOM   1331 C  CG  . PHE B 1 51  ? 24.464 9.671   11.036 1.00 34.51 ? 50  PHE B CG  1 
ATOM   1332 C  CD1 . PHE B 1 51  ? 24.882 9.097   9.863  1.00 34.22 ? 50  PHE B CD1 1 
ATOM   1333 C  CD2 . PHE B 1 51  ? 23.844 10.897  10.983 1.00 36.46 ? 50  PHE B CD2 1 
ATOM   1334 C  CE1 . PHE B 1 51  ? 24.701 9.733   8.683  1.00 34.39 ? 50  PHE B CE1 1 
ATOM   1335 C  CE2 . PHE B 1 51  ? 23.660 11.530  9.799  1.00 29.54 ? 50  PHE B CE2 1 
ATOM   1336 C  CZ  . PHE B 1 51  ? 24.084 10.947  8.655  1.00 36.72 ? 50  PHE B CZ  1 
ATOM   1337 N  N   . GLY B 1 52  ? 24.734 6.124   13.934 1.00 25.81 ? 51  GLY B N   1 
ATOM   1338 C  CA  . GLY B 1 52  ? 25.068 5.470   15.184 1.00 25.95 ? 51  GLY B CA  1 
ATOM   1339 C  C   . GLY B 1 52  ? 26.309 6.175   15.704 1.00 33.76 ? 51  GLY B C   1 
ATOM   1340 O  O   . GLY B 1 52  ? 27.329 5.544   15.978 1.00 27.97 ? 51  GLY B O   1 
ATOM   1341 N  N   . ASP B 1 53  ? 26.203 7.506   15.835 1.00 35.59 ? 52  ASP B N   1 
ATOM   1342 C  CA  . ASP B 1 53  ? 27.295 8.357   16.287 1.00 27.91 ? 52  ASP B CA  1 
ATOM   1343 C  C   . ASP B 1 53  ? 26.940 8.905   17.663 1.00 33.50 ? 52  ASP B C   1 
ATOM   1344 O  O   . ASP B 1 53  ? 25.989 9.666   17.828 1.00 32.39 ? 52  ASP B O   1 
ATOM   1345 C  CB  . ASP B 1 53  ? 27.488 9.472   15.271 1.00 31.93 ? 52  ASP B CB  1 
ATOM   1346 C  CG  . ASP B 1 53  ? 28.711 10.311  15.536 1.00 36.87 ? 52  ASP B CG  1 
ATOM   1347 O  OD1 . ASP B 1 53  ? 29.234 10.839  14.524 1.00 34.28 ? 52  ASP B OD1 1 
ATOM   1348 O  OD2 . ASP B 1 53  ? 29.134 10.445  16.722 1.00 31.05 ? 52  ASP B OD2 1 
ATOM   1349 N  N   . ASN B 1 54  ? 27.718 8.477   18.648 1.00 32.72 ? 53  ASN B N   1 
ATOM   1350 C  CA  . ASN B 1 54  ? 27.536 8.827   20.039 1.00 38.50 ? 53  ASN B CA  1 
ATOM   1351 C  C   . ASN B 1 54  ? 28.521 9.906   20.493 1.00 39.14 ? 53  ASN B C   1 
ATOM   1352 O  O   . ASN B 1 54  ? 28.560 10.264  21.672 1.00 39.20 ? 53  ASN B O   1 
ATOM   1353 C  CB  . ASN B 1 54  ? 27.768 7.563   20.869 1.00 46.29 ? 53  ASN B CB  1 
ATOM   1354 C  CG  . ASN B 1 54  ? 27.008 7.576   22.147 1.00 54.50 ? 53  ASN B CG  1 
ATOM   1355 O  OD1 . ASN B 1 54  ? 27.259 6.769   23.037 1.00 63.51 ? 53  ASN B OD1 1 
ATOM   1356 N  ND2 . ASN B 1 54  ? 26.053 8.492   22.254 1.00 58.11 ? 53  ASN B ND2 1 
ATOM   1357 N  N   . THR B 1 55  ? 29.323 10.431  19.575 1.00 36.07 ? 54  THR B N   1 
ATOM   1358 C  CA  . THR B 1 55  ? 30.287 11.449  19.987 1.00 41.98 ? 54  THR B CA  1 
ATOM   1359 C  C   . THR B 1 55  ? 29.688 12.669  20.707 1.00 42.98 ? 54  THR B C   1 
ATOM   1360 O  O   . THR B 1 55  ? 30.372 13.296  21.520 1.00 44.48 ? 54  THR B O   1 
ATOM   1361 C  CB  . THR B 1 55  ? 31.116 11.899  18.804 1.00 40.87 ? 54  THR B CB  1 
ATOM   1362 O  OG1 . THR B 1 55  ? 30.274 12.534  17.840 1.00 39.71 ? 54  THR B OG1 1 
ATOM   1363 C  CG2 . THR B 1 55  ? 31.755 10.682  18.146 1.00 37.70 ? 54  THR B CG2 1 
ATOM   1364 N  N   . ALA B 1 56  ? 28.421 12.989  20.433 1.00 41.15 ? 55  ALA B N   1 
ATOM   1365 C  CA  . ALA B 1 56  ? 27.742 14.130  21.067 1.00 40.29 ? 55  ALA B CA  1 
ATOM   1366 C  C   . ALA B 1 56  ? 26.370 13.736  21.637 1.00 42.79 ? 55  ALA B C   1 
ATOM   1367 O  O   . ALA B 1 56  ? 25.345 14.364  21.329 1.00 44.24 ? 55  ALA B O   1 
ATOM   1368 C  CB  . ALA B 1 56  ? 27.578 15.307  20.046 1.00 39.93 ? 55  ALA B CB  1 
ATOM   1369 N  N   . GLY B 1 57  ? 26.358 12.693  22.460 1.00 40.06 ? 56  GLY B N   1 
ATOM   1370 C  CA  . GLY B 1 57  ? 25.124 12.243  23.054 1.00 42.60 ? 56  GLY B CA  1 
ATOM   1371 C  C   . GLY B 1 57  ? 24.159 11.842  21.970 1.00 40.53 ? 56  GLY B C   1 
ATOM   1372 O  O   . GLY B 1 57  ? 24.574 11.316  20.927 1.00 40.74 ? 56  GLY B O   1 
ATOM   1373 N  N   . CYS B 1 58  ? 22.879 12.120  22.204 1.00 32.70 ? 57  CYS B N   1 
ATOM   1374 C  CA  . CYS B 1 58  ? 21.846 11.803  21.240 1.00 34.41 ? 57  CYS B CA  1 
ATOM   1375 C  C   . CYS B 1 58  ? 21.860 12.826  20.114 1.00 35.42 ? 57  CYS B C   1 
ATOM   1376 O  O   . CYS B 1 58  ? 21.344 12.559  19.027 1.00 35.79 ? 57  CYS B O   1 
ATOM   1377 C  CB  . CYS B 1 58  ? 20.476 11.790  21.917 1.00 30.45 ? 57  CYS B CB  1 
ATOM   1378 S  SG  . CYS B 1 58  ? 20.347 10.582  23.271 1.00 35.81 ? 57  CYS B SG  1 
ATOM   1379 N  N   . THR B 1 59  ? 22.466 13.988  20.352 1.00 35.96 ? 58  THR B N   1 
ATOM   1380 C  CA  . THR B 1 59  ? 22.528 15.035  19.291 1.00 36.95 ? 58  THR B CA  1 
ATOM   1381 C  C   . THR B 1 59  ? 23.221 14.590  18.008 1.00 33.10 ? 58  THR B C   1 
ATOM   1382 O  O   . THR B 1 59  ? 22.797 14.934  16.897 1.00 37.63 ? 58  THR B O   1 
ATOM   1383 C  CB  . THR B 1 59  ? 23.273 16.283  19.786 1.00 41.88 ? 58  THR B CB  1 
ATOM   1384 O  OG1 . THR B 1 59  ? 22.594 16.801  20.932 1.00 45.59 ? 58  THR B OG1 1 
ATOM   1385 C  CG2 . THR B 1 59  ? 23.343 17.355  18.688 1.00 45.64 ? 58  THR B CG2 1 
ATOM   1386 N  N   . SER B 1 60  ? 24.299 13.829  18.126 1.00 33.36 ? 59  SER B N   1 
ATOM   1387 C  CA  . SER B 1 60  ? 25.006 13.404  16.909 1.00 30.84 ? 59  SER B CA  1 
ATOM   1388 C  C   . SER B 1 60  ? 24.305 12.279  16.126 1.00 29.82 ? 59  SER B C   1 
ATOM   1389 O  O   . SER B 1 60  ? 24.787 11.811  15.076 1.00 30.20 ? 59  SER B O   1 
ATOM   1390 C  CB  . SER B 1 60  ? 26.472 13.032  17.265 1.00 34.99 ? 59  SER B CB  1 
ATOM   1391 O  OG  . SER B 1 60  ? 26.548 12.205  18.417 1.00 29.58 ? 59  SER B OG  1 
ATOM   1392 N  N   . ALA B 1 61  ? 23.142 11.870  16.614 1.00 27.22 ? 60  ALA B N   1 
ATOM   1393 C  CA  . ALA B 1 61  ? 22.392 10.797  15.949 1.00 31.99 ? 60  ALA B CA  1 
ATOM   1394 C  C   . ALA B 1 61  ? 21.781 11.238  14.605 1.00 34.97 ? 60  ALA B C   1 
ATOM   1395 O  O   . ALA B 1 61  ? 21.374 10.413  13.780 1.00 30.13 ? 60  ALA B O   1 
ATOM   1396 C  CB  . ALA B 1 61  ? 21.315 10.274  16.891 1.00 31.01 ? 60  ALA B CB  1 
ATOM   1397 N  N   . GLY B 1 62  ? 21.745 12.546  14.383 1.00 37.22 ? 61  GLY B N   1 
ATOM   1398 C  CA  . GLY B 1 62  ? 21.193 13.067  13.138 1.00 37.41 ? 61  GLY B CA  1 
ATOM   1399 C  C   . GLY B 1 62  ? 19.673 12.999  13.024 1.00 32.65 ? 61  GLY B C   1 
ATOM   1400 O  O   . GLY B 1 62  ? 18.961 12.927  14.031 1.00 36.97 ? 61  GLY B O   1 
ATOM   1401 N  N   . PRO B 1 63  ? 19.147 13.027  11.804 1.00 31.82 ? 62  PRO B N   1 
ATOM   1402 C  CA  . PRO B 1 63  ? 17.692 12.963  11.612 1.00 38.60 ? 62  PRO B CA  1 
ATOM   1403 C  C   . PRO B 1 63  ? 17.146 11.534  11.556 1.00 42.08 ? 62  PRO B C   1 
ATOM   1404 O  O   . PRO B 1 63  ? 17.877 10.561  11.728 1.00 34.77 ? 62  PRO B O   1 
ATOM   1405 C  CB  . PRO B 1 63  ? 17.492 13.690  10.280 1.00 36.10 ? 62  PRO B CB  1 
ATOM   1406 C  CG  . PRO B 1 63  ? 18.733 13.279  9.521  1.00 35.70 ? 62  PRO B CG  1 
ATOM   1407 C  CD  . PRO B 1 63  ? 19.831 13.420  10.553 1.00 31.43 ? 62  PRO B CD  1 
ATOM   1408 N  N   . HIS B 1 64  ? 15.836 11.433  11.327 1.00 39.20 ? 63  HIS B N   1 
ATOM   1409 C  CA  . HIS B 1 64  ? 15.189 10.156  11.205 1.00 39.26 ? 63  HIS B CA  1 
ATOM   1410 C  C   . HIS B 1 64  ? 15.802 9.422   10.043 1.00 39.57 ? 63  HIS B C   1 
ATOM   1411 O  O   . HIS B 1 64  ? 16.105 10.001  8.991  1.00 39.30 ? 63  HIS B O   1 
ATOM   1412 C  CB  . HIS B 1 64  ? 13.691 10.327  10.952 1.00 45.08 ? 63  HIS B CB  1 
ATOM   1413 C  CG  . HIS B 1 64  ? 12.938 10.782  12.154 1.00 54.72 ? 63  HIS B CG  1 
ATOM   1414 N  ND1 . HIS B 1 64  ? 11.573 10.974  12.152 1.00 59.62 ? 63  HIS B ND1 1 
ATOM   1415 C  CD2 . HIS B 1 64  ? 13.361 11.082  13.405 1.00 57.88 ? 63  HIS B CD2 1 
ATOM   1416 C  CE1 . HIS B 1 64  ? 11.188 11.372  13.353 1.00 63.98 ? 63  HIS B CE1 1 
ATOM   1417 N  NE2 . HIS B 1 64  ? 12.255 11.444  14.133 1.00 61.28 ? 63  HIS B NE2 1 
ATOM   1418 N  N   . PHE B 1 65  ? 16.014 8.138   10.244 1.00 35.32 ? 64  PHE B N   1 
ATOM   1419 C  CA  . PHE B 1 65  ? 16.549 7.295   9.194  1.00 40.27 ? 64  PHE B CA  1 
ATOM   1420 C  C   . PHE B 1 65  ? 15.463 7.275   8.104  1.00 46.48 ? 64  PHE B C   1 
ATOM   1421 O  O   . PHE B 1 65  ? 14.270 7.104   8.405  1.00 44.95 ? 64  PHE B O   1 
ATOM   1422 C  CB  . PHE B 1 65  ? 16.751 5.882   9.748  1.00 37.46 ? 64  PHE B CB  1 
ATOM   1423 C  CG  . PHE B 1 65  ? 17.090 4.855   8.708  1.00 34.58 ? 64  PHE B CG  1 
ATOM   1424 C  CD1 . PHE B 1 65  ? 16.444 3.625   8.705  1.00 32.74 ? 64  PHE B CD1 1 
ATOM   1425 C  CD2 . PHE B 1 65  ? 18.106 5.079   7.798  1.00 33.77 ? 64  PHE B CD2 1 
ATOM   1426 C  CE1 . PHE B 1 65  ? 16.826 2.624   7.800  1.00 32.19 ? 64  PHE B CE1 1 
ATOM   1427 C  CE2 . PHE B 1 65  ? 18.494 4.094   6.896  1.00 35.92 ? 64  PHE B CE2 1 
ATOM   1428 C  CZ  . PHE B 1 65  ? 17.858 2.868   6.897  1.00 32.28 ? 64  PHE B CZ  1 
ATOM   1429 N  N   . ASN B 1 66  ? 15.853 7.452   6.851  1.00 48.12 ? 65  ASN B N   1 
ATOM   1430 C  CA  . ASN B 1 66  ? 14.847 7.422   5.809  1.00 54.92 ? 65  ASN B CA  1 
ATOM   1431 C  C   . ASN B 1 66  ? 15.385 7.310   4.401  1.00 55.95 ? 65  ASN B C   1 
ATOM   1432 O  O   . ASN B 1 66  ? 15.768 8.311   3.811  1.00 58.02 ? 65  ASN B O   1 
ATOM   1433 C  CB  . ASN B 1 66  ? 13.955 8.663   5.917  1.00 54.68 ? 65  ASN B CB  1 
ATOM   1434 C  CG  . ASN B 1 66  ? 12.716 8.564   5.058  1.00 58.65 ? 65  ASN B CG  1 
ATOM   1435 O  OD1 . ASN B 1 66  ? 12.077 7.508   4.975  1.00 54.98 ? 65  ASN B OD1 1 
ATOM   1436 N  ND2 . ASN B 1 66  ? 12.351 9.675   4.426  1.00 60.99 ? 65  ASN B ND2 1 
ATOM   1437 N  N   . PRO B 1 67  ? 15.459 6.076   3.866  1.00 59.91 ? 66  PRO B N   1 
ATOM   1438 C  CA  . PRO B 1 67  ? 15.930 5.731   2.508  1.00 62.84 ? 66  PRO B CA  1 
ATOM   1439 C  C   . PRO B 1 67  ? 14.768 5.640   1.467  1.00 63.23 ? 66  PRO B C   1 
ATOM   1440 O  O   . PRO B 1 67  ? 13.780 4.916   1.685  1.00 59.74 ? 66  PRO B O   1 
ATOM   1441 C  CB  . PRO B 1 67  ? 16.634 4.389   2.725  1.00 63.73 ? 66  PRO B CB  1 
ATOM   1442 C  CG  . PRO B 1 67  ? 15.815 3.766   3.838  1.00 57.63 ? 66  PRO B CG  1 
ATOM   1443 C  CD  . PRO B 1 67  ? 15.626 4.926   4.778  1.00 57.61 ? 66  PRO B CD  1 
ATOM   1444 N  N   . LEU B 1 68  ? 14.897 6.355   0.340  1.00 66.38 ? 67  LEU B N   1 
ATOM   1445 C  CA  . LEU B 1 68  ? 13.858 6.378   -0.709 1.00 65.69 ? 67  LEU B CA  1 
ATOM   1446 C  C   . LEU B 1 68  ? 14.395 6.058   -2.104 1.00 66.36 ? 67  LEU B C   1 
ATOM   1447 O  O   . LEU B 1 68  ? 13.666 5.571   -2.971 1.00 61.30 ? 67  LEU B O   1 
ATOM   1448 C  CB  . LEU B 1 68  ? 13.182 7.753   -0.745 1.00 66.89 ? 67  LEU B CB  1 
ATOM   1449 C  CG  . LEU B 1 68  ? 12.743 8.371   0.598  1.00 68.41 ? 67  LEU B CG  1 
ATOM   1450 C  CD1 . LEU B 1 68  ? 12.484 9.847   0.407  1.00 63.92 ? 67  LEU B CD1 1 
ATOM   1451 C  CD2 . LEU B 1 68  ? 11.503 7.665   1.153  1.00 62.38 ? 67  LEU B CD2 1 
ATOM   1452 N  N   . ARG B 1 80  ? 5.150  7.917   6.974  1.00 58.16 ? 79  ARG B N   1 
ATOM   1453 C  CA  . ARG B 1 80  ? 6.185  8.181   7.963  1.00 56.37 ? 79  ARG B CA  1 
ATOM   1454 C  C   . ARG B 1 80  ? 7.530  7.697   7.450  1.00 55.69 ? 79  ARG B C   1 
ATOM   1455 O  O   . ARG B 1 80  ? 7.599  6.846   6.589  1.00 59.78 ? 79  ARG B O   1 
ATOM   1456 C  CB  . ARG B 1 80  ? 5.842  7.494   9.279  1.00 59.24 ? 79  ARG B CB  1 
ATOM   1457 N  N   . SER B 1 81  ? 8.607  8.237   7.984  1.00 53.47 ? 80  SER B N   1 
ATOM   1458 C  CA  . SER B 1 81  ? 9.913  7.737   7.636  1.00 47.91 ? 80  SER B CA  1 
ATOM   1459 C  C   . SER B 1 81  ? 10.011 6.255   7.926  1.00 46.43 ? 80  SER B C   1 
ATOM   1460 O  O   . SER B 1 81  ? 9.256  5.728   8.704  1.00 41.00 ? 80  SER B O   1 
ATOM   1461 C  CB  . SER B 1 81  ? 10.981 8.508   8.377  1.00 53.46 ? 80  SER B CB  1 
ATOM   1462 O  OG  . SER B 1 81  ? 10.624 8.689   9.731  1.00 57.99 ? 80  SER B OG  1 
ATOM   1463 N  N   . VAL B 1 82  ? 10.944 5.592   7.257  1.00 42.84 ? 81  VAL B N   1 
ATOM   1464 C  CA  . VAL B 1 82  ? 11.344 4.237   7.582  1.00 36.87 ? 81  VAL B CA  1 
ATOM   1465 C  C   . VAL B 1 82  ? 11.683 4.104   9.058  1.00 35.81 ? 81  VAL B C   1 
ATOM   1466 O  O   . VAL B 1 82  ? 11.326 3.149   9.701  1.00 30.19 ? 81  VAL B O   1 
ATOM   1467 C  CB  . VAL B 1 82  ? 12.546 3.811   6.728  1.00 38.90 ? 81  VAL B CB  1 
ATOM   1468 C  CG1 . VAL B 1 82  ? 13.194 2.573   7.274  1.00 36.95 ? 81  VAL B CG1 1 
ATOM   1469 C  CG2 . VAL B 1 82  ? 12.134 3.628   5.278  1.00 42.42 ? 81  VAL B CG2 1 
ATOM   1470 N  N   . GLY B 1 83  ? 12.372 5.102   9.577  1.00 35.17 ? 82  GLY B N   1 
ATOM   1471 C  CA  . GLY B 1 83  ? 12.830 5.078   10.957 1.00 39.79 ? 82  GLY B CA  1 
ATOM   1472 C  C   . GLY B 1 83  ? 11.790 5.237   12.044 1.00 43.00 ? 82  GLY B C   1 
ATOM   1473 O  O   . GLY B 1 83  ? 12.028 4.844   13.198 1.00 33.48 ? 82  GLY B O   1 
ATOM   1474 N  N   . SER B 1 84  ? 10.640 5.805   11.698 1.00 38.68 ? 83  SER B N   1 
ATOM   1475 C  CA  . SER B 1 84  ? 9.608  5.982   12.695 1.00 37.60 ? 83  SER B CA  1 
ATOM   1476 C  C   . SER B 1 84  ? 9.015  4.654   13.128 1.00 33.99 ? 83  SER B C   1 
ATOM   1477 O  O   . SER B 1 84  ? 8.601  3.820   12.300 1.00 36.13 ? 83  SER B O   1 
ATOM   1478 C  CB  . SER B 1 84  ? 8.489  6.877   12.169 1.00 39.83 ? 83  SER B CB  1 
ATOM   1479 O  OG  . SER B 1 84  ? 7.467  6.985   13.150 1.00 41.59 ? 83  SER B OG  1 
ATOM   1480 N  N   . LEU B 1 85  ? 8.979  4.438   14.430 1.00 28.23 ? 84  LEU B N   1 
ATOM   1481 C  CA  . LEU B 1 85  ? 8.403  3.207   14.946 1.00 27.77 ? 84  LEU B CA  1 
ATOM   1482 C  C   . LEU B 1 85  ? 7.128  3.559   15.756 1.00 28.98 ? 84  LEU B C   1 
ATOM   1483 O  O   . LEU B 1 85  ? 6.685  2.792   16.608 1.00 28.47 ? 84  LEU B O   1 
ATOM   1484 C  CB  . LEU B 1 85  ? 9.435  2.470   15.825 1.00 26.70 ? 84  LEU B CB  1 
ATOM   1485 C  CG  . LEU B 1 85  ? 10.521 1.639   15.123 1.00 30.47 ? 84  LEU B CG  1 
ATOM   1486 C  CD1 . LEU B 1 85  ? 11.561 1.168   16.160 1.00 27.65 ? 84  LEU B CD1 1 
ATOM   1487 C  CD2 . LEU B 1 85  ? 9.836  0.406   14.434 1.00 27.26 ? 84  LEU B CD2 1 
ATOM   1488 N  N   . GLY B 1 86  ? 6.550  4.729   15.500 1.00 26.56 ? 85  GLY B N   1 
ATOM   1489 C  CA  . GLY B 1 86  ? 5.339  5.112   16.233 1.00 30.30 ? 85  GLY B CA  1 
ATOM   1490 C  C   . GLY B 1 86  ? 5.662  5.701   17.614 1.00 27.69 ? 85  GLY B C   1 
ATOM   1491 O  O   . GLY B 1 86  ? 6.559  6.520   17.750 1.00 24.68 ? 85  GLY B O   1 
ATOM   1492 N  N   . ASN B 1 87  ? 4.923  5.280   18.621 1.00 26.21 ? 86  ASN B N   1 
ATOM   1493 C  CA  . ASN B 1 87  ? 5.123  5.750   19.987 1.00 28.71 ? 86  ASN B CA  1 
ATOM   1494 C  C   . ASN B 1 87  ? 5.219  4.545   20.908 1.00 28.89 ? 86  ASN B C   1 
ATOM   1495 O  O   . ASN B 1 87  ? 4.845  3.428   20.512 1.00 27.08 ? 86  ASN B O   1 
ATOM   1496 C  CB  . ASN B 1 87  ? 3.906  6.561   20.471 1.00 30.45 ? 86  ASN B CB  1 
ATOM   1497 C  CG  . ASN B 1 87  ? 3.841  7.963   19.872 1.00 31.11 ? 86  ASN B CG  1 
ATOM   1498 O  OD1 . ASN B 1 87  ? 4.671  8.835   20.174 1.00 28.02 ? 86  ASN B OD1 1 
ATOM   1499 N  ND2 . ASN B 1 87  ? 2.841  8.194   19.035 1.00 27.91 ? 86  ASN B ND2 1 
ATOM   1500 N  N   . VAL B 1 88  ? 5.786  4.757   22.104 1.00 21.64 ? 87  VAL B N   1 
ATOM   1501 C  CA  . VAL B 1 88  ? 5.761  3.719   23.142 1.00 20.73 ? 87  VAL B CA  1 
ATOM   1502 C  C   . VAL B 1 88  ? 4.874  4.382   24.188 1.00 22.04 ? 87  VAL B C   1 
ATOM   1503 O  O   . VAL B 1 88  ? 4.704  5.611   24.149 1.00 23.75 ? 87  VAL B O   1 
ATOM   1504 C  CB  . VAL B 1 88  ? 7.142  3.362   23.705 1.00 23.45 ? 87  VAL B CB  1 
ATOM   1505 C  CG1 . VAL B 1 88  ? 7.965  2.711   22.581 1.00 22.17 ? 87  VAL B CG1 1 
ATOM   1506 C  CG2 . VAL B 1 88  ? 7.830  4.596   24.291 1.00 24.08 ? 87  VAL B CG2 1 
ATOM   1507 N  N   . THR B 1 89  ? 4.313  3.590   25.098 1.00 21.46 ? 88  THR B N   1 
ATOM   1508 C  CA  . THR B 1 89  ? 3.351  4.054   26.102 1.00 26.45 ? 88  THR B CA  1 
ATOM   1509 C  C   . THR B 1 89  ? 3.833  3.804   27.518 1.00 23.94 ? 88  THR B C   1 
ATOM   1510 O  O   . THR B 1 89  ? 3.895  2.645   27.944 1.00 25.60 ? 88  THR B O   1 
ATOM   1511 C  CB  . THR B 1 89  ? 1.981  3.281   25.901 1.00 29.68 ? 88  THR B CB  1 
ATOM   1512 O  OG1 . THR B 1 89  ? 1.503  3.507   24.563 1.00 27.88 ? 88  THR B OG1 1 
ATOM   1513 C  CG2 . THR B 1 89  ? 0.921  3.731   26.907 1.00 31.06 ? 88  THR B CG2 1 
ATOM   1514 N  N   . ALA B 1 90  ? 4.167  4.875   28.252 1.00 22.74 ? 89  ALA B N   1 
ATOM   1515 C  CA  . ALA B 1 90  ? 4.639  4.699   29.625 1.00 22.55 ? 89  ALA B CA  1 
ATOM   1516 C  C   . ALA B 1 90  ? 3.409  4.615   30.498 1.00 23.75 ? 89  ALA B C   1 
ATOM   1517 O  O   . ALA B 1 90  ? 2.459  5.408   30.324 1.00 26.56 ? 89  ALA B O   1 
ATOM   1518 C  CB  . ALA B 1 90  ? 5.518  5.909   30.106 1.00 20.15 ? 89  ALA B CB  1 
ATOM   1519 N  N   . ASP B 1 91  ? 3.433  3.694   31.449 1.00 27.12 ? 90  ASP B N   1 
ATOM   1520 C  CA  . ASP B 1 91  ? 2.295  3.571   32.348 1.00 30.05 ? 90  ASP B CA  1 
ATOM   1521 C  C   . ASP B 1 91  ? 2.353  4.628   33.481 1.00 31.80 ? 90  ASP B C   1 
ATOM   1522 O  O   . ASP B 1 91  ? 3.217  5.504   33.477 1.00 27.77 ? 90  ASP B O   1 
ATOM   1523 C  CB  . ASP B 1 91  ? 2.241  2.160   32.920 1.00 29.45 ? 90  ASP B CB  1 
ATOM   1524 C  CG  . ASP B 1 91  ? 3.429  1.833   33.820 1.00 31.74 ? 90  ASP B CG  1 
ATOM   1525 O  OD1 . ASP B 1 91  ? 4.127  2.725   34.332 1.00 28.18 ? 90  ASP B OD1 1 
ATOM   1526 O  OD2 . ASP B 1 91  ? 3.644  0.636   34.033 1.00 31.64 ? 90  ASP B OD2 1 
ATOM   1527 N  N   . LYS B 1 92  ? 1.451  4.540   34.455 1.00 32.20 ? 91  LYS B N   1 
ATOM   1528 C  CA  . LYS B 1 92  ? 1.416  5.547   35.548 1.00 36.84 ? 91  LYS B CA  1 
ATOM   1529 C  C   . LYS B 1 92  ? 2.685  5.607   36.397 1.00 37.29 ? 91  LYS B C   1 
ATOM   1530 O  O   . LYS B 1 92  ? 2.887  6.541   37.191 1.00 36.97 ? 91  LYS B O   1 
ATOM   1531 C  CB  . LYS B 1 92  ? 0.224  5.297   36.469 1.00 28.67 ? 91  LYS B CB  1 
ATOM   1532 C  CG  . LYS B 1 92  ? 0.321  4.008   37.251 1.00 23.71 ? 91  LYS B CG  1 
ATOM   1533 C  CD  . LYS B 1 92  ? -0.904 3.897   38.146 1.00 33.60 ? 91  LYS B CD  1 
ATOM   1534 C  CE  . LYS B 1 92  ? -0.937 2.629   38.922 1.00 37.85 ? 91  LYS B CE  1 
ATOM   1535 N  NZ  . LYS B 1 92  ? -2.284 2.516   39.551 1.00 48.18 ? 91  LYS B NZ  1 
ATOM   1536 N  N   . ASP B 1 93  ? 3.539  4.608   36.250 1.00 34.15 ? 92  ASP B N   1 
ATOM   1537 C  CA  . ASP B 1 93  ? 4.780  4.597   37.002 1.00 34.00 ? 92  ASP B CA  1 
ATOM   1538 C  C   . ASP B 1 93  ? 5.974  4.820   36.119 1.00 31.64 ? 92  ASP B C   1 
ATOM   1539 O  O   . ASP B 1 93  ? 7.116  4.553   36.516 1.00 29.16 ? 92  ASP B O   1 
ATOM   1540 C  CB  . ASP B 1 93  ? 4.904  3.302   37.799 1.00 37.02 ? 92  ASP B CB  1 
ATOM   1541 C  CG  . ASP B 1 93  ? 3.828  3.208   38.865 1.00 48.88 ? 92  ASP B CG  1 
ATOM   1542 O  OD1 . ASP B 1 93  ? 3.605  4.235   39.546 1.00 48.59 ? 92  ASP B OD1 1 
ATOM   1543 O  OD2 . ASP B 1 93  ? 3.195  2.142   39.021 1.00 47.72 ? 92  ASP B OD2 1 
ATOM   1544 N  N   . GLY B 1 94  ? 5.698  5.310   34.910 1.00 28.59 ? 93  GLY B N   1 
ATOM   1545 C  CA  . GLY B 1 94  ? 6.766  5.641   33.979 1.00 30.73 ? 93  GLY B CA  1 
ATOM   1546 C  C   . GLY B 1 94  ? 7.436  4.465   33.283 1.00 24.36 ? 93  GLY B C   1 
ATOM   1547 O  O   . GLY B 1 94  ? 8.542  4.604   32.757 1.00 27.30 ? 93  GLY B O   1 
ATOM   1548 N  N   . VAL B 1 95  ? 6.797  3.312   33.283 1.00 24.51 ? 94  VAL B N   1 
ATOM   1549 C  CA  . VAL B 1 95  ? 7.408  2.175   32.602 1.00 24.82 ? 94  VAL B CA  1 
ATOM   1550 C  C   . VAL B 1 95  ? 6.696  1.888   31.279 1.00 26.84 ? 94  VAL B C   1 
ATOM   1551 O  O   . VAL B 1 95  ? 5.461  1.789   31.214 1.00 26.36 ? 94  VAL B O   1 
ATOM   1552 C  CB  . VAL B 1 95  ? 7.461  0.931   33.526 1.00 27.13 ? 94  VAL B CB  1 
ATOM   1553 C  CG1 . VAL B 1 95  ? 8.193  -0.207  32.856 1.00 24.17 ? 94  VAL B CG1 1 
ATOM   1554 C  CG2 . VAL B 1 95  ? 8.291  1.258   34.776 1.00 27.40 ? 94  VAL B CG2 1 
ATOM   1555 N  N   . ALA B 1 96  ? 7.470  1.864   30.192 1.00 25.57 ? 95  ALA B N   1 
ATOM   1556 C  CA  . ALA B 1 96  ? 6.893  1.539   28.880 1.00 27.03 ? 95  ALA B CA  1 
ATOM   1557 C  C   . ALA B 1 96  ? 7.319  0.107   28.556 1.00 27.54 ? 95  ALA B C   1 
ATOM   1558 O  O   . ALA B 1 96  ? 8.504  -0.160  28.327 1.00 28.69 ? 95  ALA B O   1 
ATOM   1559 C  CB  . ALA B 1 96  ? 7.410  2.502   27.790 1.00 22.45 ? 95  ALA B CB  1 
ATOM   1560 N  N   . ASP B 1 97  ? 6.369  -0.816  28.573 1.00 27.20 ? 96  ASP B N   1 
ATOM   1561 C  CA  . ASP B 1 97  ? 6.712  -2.193  28.243 1.00 30.24 ? 96  ASP B CA  1 
ATOM   1562 C  C   . ASP B 1 97  ? 6.458  -2.208  26.745 1.00 24.54 ? 96  ASP B C   1 
ATOM   1563 O  O   . ASP B 1 97  ? 5.352  -1.954  26.266 1.00 27.17 ? 96  ASP B O   1 
ATOM   1564 C  CB  . ASP B 1 97  ? 5.851  -3.152  29.068 1.00 33.40 ? 96  ASP B CB  1 
ATOM   1565 C  CG  . ASP B 1 97  ? 6.328  -3.222  30.532 1.00 43.46 ? 96  ASP B CG  1 
ATOM   1566 O  OD1 . ASP B 1 97  ? 7.536  -3.478  30.763 1.00 37.52 ? 96  ASP B OD1 1 
ATOM   1567 O  OD2 . ASP B 1 97  ? 5.504  -3.016  31.462 1.00 45.28 ? 96  ASP B OD2 1 
ATOM   1568 N  N   . VAL B 1 98  ? 7.521  -2.431  25.991 1.00 25.42 ? 97  VAL B N   1 
ATOM   1569 C  CA  . VAL B 1 98  ? 7.417  -2.300  24.547 1.00 24.57 ? 97  VAL B CA  1 
ATOM   1570 C  C   . VAL B 1 98  ? 7.185  -3.581  23.793 1.00 27.97 ? 97  VAL B C   1 
ATOM   1571 O  O   . VAL B 1 98  ? 7.793  -4.602  24.081 1.00 22.92 ? 97  VAL B O   1 
ATOM   1572 C  CB  . VAL B 1 98  ? 8.686  -1.581  23.949 1.00 20.67 ? 97  VAL B CB  1 
ATOM   1573 C  CG1 . VAL B 1 98  ? 8.476  -1.357  22.424 1.00 26.33 ? 97  VAL B CG1 1 
ATOM   1574 C  CG2 . VAL B 1 98  ? 8.917  -0.171  24.647 1.00 17.12 ? 97  VAL B CG2 1 
ATOM   1575 N  N   . SER B 1 99  ? 6.290  -3.517  22.820 1.00 28.47 ? 98  SER B N   1 
ATOM   1576 C  CA  . SER B 1 99  ? 6.004  -4.664  21.978 1.00 30.26 ? 98  SER B CA  1 
ATOM   1577 C  C   . SER B 1 99  ? 5.527  -4.119  20.636 1.00 36.95 ? 98  SER B C   1 
ATOM   1578 O  O   . SER B 1 99  ? 4.403  -3.621  20.523 1.00 39.01 ? 98  SER B O   1 
ATOM   1579 C  CB  . SER B 1 99  ? 4.922  -5.521  22.606 1.00 37.93 ? 98  SER B CB  1 
ATOM   1580 O  OG  . SER B 1 99  ? 4.505  -6.488  21.668 1.00 43.07 ? 98  SER B OG  1 
ATOM   1581 N  N   . ILE B 1 100 ? 6.375  -4.216  19.622 1.00 31.38 ? 99  ILE B N   1 
ATOM   1582 C  CA  . ILE B 1 100 ? 6.038  -3.688  18.307 1.00 35.02 ? 99  ILE B CA  1 
ATOM   1583 C  C   . ILE B 1 100 ? 6.439  -4.666  17.213 1.00 35.71 ? 99  ILE B C   1 
ATOM   1584 O  O   . ILE B 1 100 ? 7.352  -5.467  17.395 1.00 29.73 ? 99  ILE B O   1 
ATOM   1585 C  CB  . ILE B 1 100 ? 6.802  -2.351  18.037 1.00 32.52 ? 99  ILE B CB  1 
ATOM   1586 C  CG1 . ILE B 1 100 ? 6.335  -1.251  18.995 1.00 31.43 ? 99  ILE B CG1 1 
ATOM   1587 C  CG2 . ILE B 1 100 ? 6.599  -1.906  16.603 1.00 37.44 ? 99  ILE B CG2 1 
ATOM   1588 C  CD1 . ILE B 1 100 ? 7.231  0.016   18.982 1.00 26.38 ? 99  ILE B CD1 1 
ATOM   1589 N  N   . GLU B 1 101 ? 5.726  -4.605  16.093 1.00 37.21 ? 100 GLU B N   1 
ATOM   1590 C  CA  . GLU B 1 101 ? 6.046  -5.408  14.922 1.00 34.68 ? 100 GLU B CA  1 
ATOM   1591 C  C   . GLU B 1 101 ? 6.078  -4.394  13.770 1.00 35.44 ? 100 GLU B C   1 
ATOM   1592 O  O   . GLU B 1 101 ? 5.168  -3.601  13.632 1.00 32.54 ? 100 GLU B O   1 
ATOM   1593 C  CB  . GLU B 1 101 ? 4.987  -6.453  14.664 1.00 44.07 ? 100 GLU B CB  1 
ATOM   1594 C  CG  . GLU B 1 101 ? 5.460  -7.436  13.619 1.00 58.69 ? 100 GLU B CG  1 
ATOM   1595 C  CD  . GLU B 1 101 ? 4.777  -8.778  13.744 1.00 67.14 ? 100 GLU B CD  1 
ATOM   1596 O  OE1 . GLU B 1 101 ? 4.731  -9.305  14.888 1.00 72.21 ? 100 GLU B OE1 1 
ATOM   1597 O  OE2 . GLU B 1 101 ? 4.296  -9.298  12.709 1.00 69.11 ? 100 GLU B OE2 1 
ATOM   1598 N  N   . ASP B 1 102 ? 7.126  -4.402  12.958 1.00 32.43 ? 101 ASP B N   1 
ATOM   1599 C  CA  . ASP B 1 102 ? 7.223  -3.437  11.890 1.00 35.32 ? 101 ASP B CA  1 
ATOM   1600 C  C   . ASP B 1 102 ? 7.814  -4.133  10.647 1.00 36.85 ? 101 ASP B C   1 
ATOM   1601 O  O   . ASP B 1 102 ? 8.830  -4.818  10.746 1.00 35.02 ? 101 ASP B O   1 
ATOM   1602 C  CB  . ASP B 1 102 ? 8.112  -2.263  12.375 1.00 32.60 ? 101 ASP B CB  1 
ATOM   1603 C  CG  . ASP B 1 102 ? 8.159  -1.091  11.398 1.00 37.83 ? 101 ASP B CG  1 
ATOM   1604 O  OD1 . ASP B 1 102 ? 8.771  -1.197  10.313 1.00 39.04 ? 101 ASP B OD1 1 
ATOM   1605 O  OD2 . ASP B 1 102 ? 7.592  -0.034  11.726 1.00 43.02 ? 101 ASP B OD2 1 
ATOM   1606 N  N   . SER B 1 103 ? 7.175  -3.941  9.490  1.00 35.99 ? 102 SER B N   1 
ATOM   1607 C  CA  . SER B 1 103 ? 7.620  -4.555  8.232  1.00 39.84 ? 102 SER B CA  1 
ATOM   1608 C  C   . SER B 1 103 ? 8.413  -3.604  7.339  1.00 41.22 ? 102 SER B C   1 
ATOM   1609 O  O   . SER B 1 103 ? 8.875  -4.002  6.265  1.00 41.32 ? 102 SER B O   1 
ATOM   1610 C  CB  . SER B 1 103 ? 6.412  -5.073  7.422  1.00 41.46 ? 102 SER B CB  1 
ATOM   1611 O  OG  . SER B 1 103 ? 5.575  -5.914  8.200  1.00 46.56 ? 102 SER B OG  1 
ATOM   1612 N  N   . VAL B 1 104 ? 8.556  -2.349  7.752  1.00 33.01 ? 103 VAL B N   1 
ATOM   1613 C  CA  . VAL B 1 104 ? 9.303  -1.394  6.948  1.00 31.63 ? 103 VAL B CA  1 
ATOM   1614 C  C   . VAL B 1 104 ? 10.778 -1.386  7.347  1.00 34.11 ? 103 VAL B C   1 
ATOM   1615 O  O   . VAL B 1 104 ? 11.655 -1.430  6.482  1.00 34.56 ? 103 VAL B O   1 
ATOM   1616 C  CB  . VAL B 1 104 ? 8.695  0.023   7.055  1.00 35.72 ? 103 VAL B CB  1 
ATOM   1617 C  CG1 . VAL B 1 104 ? 9.528  1.024   6.258  1.00 40.02 ? 103 VAL B CG1 1 
ATOM   1618 C  CG2 . VAL B 1 104 ? 7.270  0.011   6.500  1.00 37.01 ? 103 VAL B CG2 1 
ATOM   1619 N  N   . ILE B 1 105 ? 11.080 -1.305  8.642  1.00 35.11 ? 104 ILE B N   1 
ATOM   1620 C  CA  . ILE B 1 105 ? 12.486 -1.361  9.023  1.00 29.07 ? 104 ILE B CA  1 
ATOM   1621 C  C   . ILE B 1 105 ? 12.951 -2.805  8.779  1.00 29.45 ? 104 ILE B C   1 
ATOM   1622 O  O   . ILE B 1 105 ? 12.146 -3.707  8.658  1.00 26.96 ? 104 ILE B O   1 
ATOM   1623 C  CB  . ILE B 1 105 ? 12.711 -1.083  10.514 1.00 25.07 ? 104 ILE B CB  1 
ATOM   1624 C  CG1 . ILE B 1 105 ? 11.905 -2.078  11.365 1.00 26.10 ? 104 ILE B CG1 1 
ATOM   1625 C  CG2 . ILE B 1 105 ? 12.369 0.328   10.827 1.00 28.30 ? 104 ILE B CG2 1 
ATOM   1626 C  CD1 . ILE B 1 105 ? 12.384 -2.190  12.876 1.00 24.47 ? 104 ILE B CD1 1 
ATOM   1627 N  N   . SER B 1 106 ? 14.254 -3.020  8.719  1.00 31.63 ? 105 SER B N   1 
ATOM   1628 C  CA  . SER B 1 106 ? 14.776 -4.367  8.551  1.00 29.04 ? 105 SER B CA  1 
ATOM   1629 C  C   . SER B 1 106 ? 16.119 -4.417  9.328  1.00 32.80 ? 105 SER B C   1 
ATOM   1630 O  O   . SER B 1 106 ? 16.628 -3.360  9.769  1.00 28.94 ? 105 SER B O   1 
ATOM   1631 C  CB  . SER B 1 106 ? 15.008 -4.631  7.052  1.00 30.24 ? 105 SER B CB  1 
ATOM   1632 O  OG  . SER B 1 106 ? 15.812 -5.758  6.859  1.00 31.76 ? 105 SER B OG  1 
ATOM   1633 N  N   . LEU B 1 107 ? 16.655 -5.629  9.510  1.00 25.80 ? 106 LEU B N   1 
ATOM   1634 C  CA  . LEU B 1 107 ? 17.950 -5.843  10.157 1.00 31.47 ? 106 LEU B CA  1 
ATOM   1635 C  C   . LEU B 1 107 ? 19.048 -6.202  9.115  1.00 36.15 ? 106 LEU B C   1 
ATOM   1636 O  O   . LEU B 1 107 ? 20.103 -6.674  9.489  1.00 33.52 ? 106 LEU B O   1 
ATOM   1637 C  CB  . LEU B 1 107 ? 17.844 -6.943  11.244 1.00 35.21 ? 106 LEU B CB  1 
ATOM   1638 C  CG  . LEU B 1 107 ? 16.758 -6.677  12.316 1.00 23.49 ? 106 LEU B CG  1 
ATOM   1639 C  CD1 . LEU B 1 107 ? 16.835 -7.691  13.399 1.00 29.96 ? 106 LEU B CD1 1 
ATOM   1640 C  CD2 . LEU B 1 107 ? 16.968 -5.284  12.889 1.00 32.51 ? 106 LEU B CD2 1 
ATOM   1641 N  N   . SER B 1 108 ? 18.780 -5.970  7.823  1.00 37.88 ? 107 SER B N   1 
ATOM   1642 C  CA  . SER B 1 108 ? 19.737 -6.185  6.712  1.00 41.73 ? 107 SER B CA  1 
ATOM   1643 C  C   . SER B 1 108 ? 19.199 -5.481  5.454  1.00 46.11 ? 107 SER B C   1 
ATOM   1644 O  O   . SER B 1 108 ? 18.004 -5.211  5.354  1.00 43.58 ? 107 SER B O   1 
ATOM   1645 C  CB  . SER B 1 108 ? 19.927 -7.670  6.393  1.00 41.46 ? 107 SER B CB  1 
ATOM   1646 O  OG  . SER B 1 108 ? 18.726 -8.238  5.921  1.00 39.47 ? 107 SER B OG  1 
ATOM   1647 N  N   . GLY B 1 109 ? 20.067 -5.172  4.496  1.00 46.60 ? 108 GLY B N   1 
ATOM   1648 C  CA  . GLY B 1 109 ? 19.574 -4.507  3.298  1.00 49.12 ? 108 GLY B CA  1 
ATOM   1649 C  C   . GLY B 1 109 ? 19.527 -2.991  3.432  1.00 49.50 ? 108 GLY B C   1 
ATOM   1650 O  O   . GLY B 1 109 ? 20.053 -2.423  4.399  1.00 48.46 ? 108 GLY B O   1 
ATOM   1651 N  N   . ASP B 1 110 ? 18.882 -2.324  2.481  1.00 46.18 ? 109 ASP B N   1 
ATOM   1652 C  CA  . ASP B 1 110 ? 18.823 -0.858  2.491  1.00 47.94 ? 109 ASP B CA  1 
ATOM   1653 C  C   . ASP B 1 110 ? 18.037 -0.255  3.646  1.00 42.67 ? 109 ASP B C   1 
ATOM   1654 O  O   . ASP B 1 110 ? 18.268 0.903   4.019  1.00 42.08 ? 109 ASP B O   1 
ATOM   1655 C  CB  . ASP B 1 110 ? 18.244 -0.340  1.174  1.00 58.25 ? 109 ASP B CB  1 
ATOM   1656 C  CG  . ASP B 1 110 ? 18.842 -1.026  -0.027 1.00 70.91 ? 109 ASP B CG  1 
ATOM   1657 O  OD1 . ASP B 1 110 ? 18.475 -2.203  -0.268 1.00 77.76 ? 109 ASP B OD1 1 
ATOM   1658 O  OD2 . ASP B 1 110 ? 19.683 -0.399  -0.720 1.00 77.44 ? 109 ASP B OD2 1 
ATOM   1659 N  N   . HIS B 1 111 ? 17.100 -1.028  4.194  1.00 36.64 ? 110 HIS B N   1 
ATOM   1660 C  CA  . HIS B 1 111 ? 16.294 -0.568  5.326  1.00 39.26 ? 110 HIS B CA  1 
ATOM   1661 C  C   . HIS B 1 111 ? 16.868 -1.081  6.664  1.00 38.83 ? 110 HIS B C   1 
ATOM   1662 O  O   . HIS B 1 111 ? 16.194 -1.028  7.694  1.00 38.04 ? 110 HIS B O   1 
ATOM   1663 C  CB  . HIS B 1 111 ? 14.828 -1.046  5.188  1.00 41.78 ? 110 HIS B CB  1 
ATOM   1664 C  CG  . HIS B 1 111 ? 13.994 -0.213  4.256  1.00 53.64 ? 110 HIS B CG  1 
ATOM   1665 N  ND1 . HIS B 1 111 ? 12.617 -0.295  4.217  1.00 58.06 ? 110 HIS B ND1 1 
ATOM   1666 C  CD2 . HIS B 1 111 ? 14.335 0.760   3.375  1.00 52.76 ? 110 HIS B CD2 1 
ATOM   1667 C  CE1 . HIS B 1 111 ? 12.147 0.596   3.360  1.00 56.45 ? 110 HIS B CE1 1 
ATOM   1668 N  NE2 . HIS B 1 111 ? 13.168 1.251   2.838  1.00 54.77 ? 110 HIS B NE2 1 
ATOM   1669 N  N   . SER B 1 112 ? 18.100 -1.577  6.658  1.00 32.62 ? 111 SER B N   1 
ATOM   1670 C  CA  . SER B 1 112 ? 18.672 -2.065  7.911  1.00 32.06 ? 111 SER B CA  1 
ATOM   1671 C  C   . SER B 1 112 ? 18.897 -0.914  8.900  1.00 32.74 ? 111 SER B C   1 
ATOM   1672 O  O   . SER B 1 112 ? 19.403 0.161   8.542  1.00 29.58 ? 111 SER B O   1 
ATOM   1673 C  CB  . SER B 1 112 ? 20.000 -2.805  7.675  1.00 28.32 ? 111 SER B CB  1 
ATOM   1674 O  OG  . SER B 1 112 ? 20.639 -3.107  8.926  1.00 31.78 ? 111 SER B OG  1 
ATOM   1675 N  N   . ILE B 1 113 ? 18.462 -1.135  10.135 1.00 25.87 ? 112 ILE B N   1 
ATOM   1676 C  CA  . ILE B 1 113 ? 18.655 -0.154  11.182 1.00 25.07 ? 112 ILE B CA  1 
ATOM   1677 C  C   . ILE B 1 113 ? 19.899 -0.535  12.008 1.00 26.69 ? 112 ILE B C   1 
ATOM   1678 O  O   . ILE B 1 113 ? 20.199 0.092   12.987 1.00 27.18 ? 112 ILE B O   1 
ATOM   1679 C  CB  . ILE B 1 113 ? 17.428 -0.078  12.096 1.00 28.24 ? 112 ILE B CB  1 
ATOM   1680 C  CG1 . ILE B 1 113 ? 17.173 -1.429  12.755 1.00 29.34 ? 112 ILE B CG1 1 
ATOM   1681 C  CG2 . ILE B 1 113 ? 16.186 0.302   11.257 1.00 28.58 ? 112 ILE B CG2 1 
ATOM   1682 C  CD1 . ILE B 1 113 ? 16.133 -1.381  13.815 1.00 20.34 ? 112 ILE B CD1 1 
ATOM   1683 N  N   . ILE B 1 114 ? 20.621 -1.572  11.602 1.00 26.24 ? 113 ILE B N   1 
ATOM   1684 C  CA  . ILE B 1 114 ? 21.837 -1.977  12.328 1.00 23.94 ? 113 ILE B CA  1 
ATOM   1685 C  C   . ILE B 1 114 ? 22.901 -0.881  12.231 1.00 25.38 ? 113 ILE B C   1 
ATOM   1686 O  O   . ILE B 1 114 ? 23.189 -0.379  11.155 1.00 24.53 ? 113 ILE B O   1 
ATOM   1687 C  CB  . ILE B 1 114 ? 22.401 -3.288  11.740 1.00 27.08 ? 113 ILE B CB  1 
ATOM   1688 C  CG1 . ILE B 1 114 ? 21.365 -4.403  11.931 1.00 29.44 ? 113 ILE B CG1 1 
ATOM   1689 C  CG2 . ILE B 1 114 ? 23.728 -3.660  12.428 1.00 24.80 ? 113 ILE B CG2 1 
ATOM   1690 C  CD1 . ILE B 1 114 ? 21.143 -4.822  13.414 1.00 27.77 ? 113 ILE B CD1 1 
ATOM   1691 N  N   . GLY B 1 115 ? 23.496 -0.505  13.357 1.00 23.12 ? 114 GLY B N   1 
ATOM   1692 C  CA  . GLY B 1 115 ? 24.495 0.531   13.310 1.00 23.76 ? 114 GLY B CA  1 
ATOM   1693 C  C   . GLY B 1 115 ? 23.884 1.930   13.329 1.00 22.17 ? 114 GLY B C   1 
ATOM   1694 O  O   . GLY B 1 115 ? 24.596 2.913   13.170 1.00 21.67 ? 114 GLY B O   1 
ATOM   1695 N  N   . ARG B 1 116 ? 22.575 2.024   13.512 1.00 22.86 ? 115 ARG B N   1 
ATOM   1696 C  CA  . ARG B 1 116 ? 21.931 3.333   13.568 1.00 23.91 ? 115 ARG B CA  1 
ATOM   1697 C  C   . ARG B 1 116 ? 21.512 3.641   15.021 1.00 25.83 ? 115 ARG B C   1 
ATOM   1698 O  O   . ARG B 1 116 ? 21.894 2.915   15.946 1.00 22.83 ? 115 ARG B O   1 
ATOM   1699 C  CB  . ARG B 1 116 ? 20.757 3.365   12.562 1.00 27.74 ? 115 ARG B CB  1 
ATOM   1700 C  CG  . ARG B 1 116 ? 21.277 3.131   11.126 1.00 26.22 ? 115 ARG B CG  1 
ATOM   1701 C  CD  . ARG B 1 116 ? 20.214 3.486   10.042 1.00 29.39 ? 115 ARG B CD  1 
ATOM   1702 N  NE  . ARG B 1 116 ? 20.671 3.079   8.717  1.00 28.31 ? 115 ARG B NE  1 
ATOM   1703 C  CZ  . ARG B 1 116 ? 21.460 3.801   7.925  1.00 30.58 ? 115 ARG B CZ  1 
ATOM   1704 N  NH1 . ARG B 1 116 ? 21.818 3.322   6.739  1.00 29.99 ? 115 ARG B NH1 1 
ATOM   1705 N  NH2 . ARG B 1 116 ? 21.869 4.997   8.301  1.00 26.75 ? 115 ARG B NH2 1 
ATOM   1706 N  N   . THR B 1 117 ? 20.767 4.710   15.270 1.00 28.24 ? 116 THR B N   1 
ATOM   1707 C  CA  . THR B 1 117 ? 20.443 4.989   16.665 1.00 26.22 ? 116 THR B CA  1 
ATOM   1708 C  C   . THR B 1 117 ? 18.959 4.901   16.986 1.00 31.83 ? 116 THR B C   1 
ATOM   1709 O  O   . THR B 1 117 ? 18.142 5.432   16.230 1.00 28.20 ? 116 THR B O   1 
ATOM   1710 C  CB  . THR B 1 117 ? 20.926 6.401   17.065 1.00 28.47 ? 116 THR B CB  1 
ATOM   1711 O  OG1 . THR B 1 117 ? 22.352 6.489   16.926 1.00 31.66 ? 116 THR B OG1 1 
ATOM   1712 C  CG2 . THR B 1 117 ? 20.522 6.716   18.519 1.00 23.79 ? 116 THR B CG2 1 
ATOM   1713 N  N   . LEU B 1 118 ? 18.615 4.251   18.108 1.00 23.67 ? 117 LEU B N   1 
ATOM   1714 C  CA  . LEU B 1 118 ? 17.217 4.170   18.544 1.00 20.74 ? 117 LEU B CA  1 
ATOM   1715 C  C   . LEU B 1 118 ? 17.082 5.317   19.559 1.00 22.39 ? 117 LEU B C   1 
ATOM   1716 O  O   . LEU B 1 118 ? 17.960 5.548   20.396 1.00 23.93 ? 117 LEU B O   1 
ATOM   1717 C  CB  . LEU B 1 118 ? 16.894 2.803   19.228 1.00 21.16 ? 117 LEU B CB  1 
ATOM   1718 C  CG  . LEU B 1 118 ? 15.450 2.665   19.764 1.00 19.60 ? 117 LEU B CG  1 
ATOM   1719 C  CD1 . LEU B 1 118 ? 14.433 2.567   18.603 1.00 23.78 ? 117 LEU B CD1 1 
ATOM   1720 C  CD2 . LEU B 1 118 ? 15.342 1.418   20.641 1.00 24.96 ? 117 LEU B CD2 1 
ATOM   1721 N  N   . VAL B 1 119 ? 15.994 6.067   19.448 1.00 20.64 ? 118 VAL B N   1 
ATOM   1722 C  CA  . VAL B 1 119 ? 15.752 7.232   20.302 1.00 24.14 ? 118 VAL B CA  1 
ATOM   1723 C  C   . VAL B 1 119 ? 14.370 7.254   20.941 1.00 22.04 ? 118 VAL B C   1 
ATOM   1724 O  O   . VAL B 1 119 ? 13.380 6.971   20.267 1.00 23.54 ? 118 VAL B O   1 
ATOM   1725 C  CB  . VAL B 1 119 ? 15.851 8.543   19.442 1.00 26.48 ? 118 VAL B CB  1 
ATOM   1726 C  CG1 . VAL B 1 119 ? 15.466 9.781   20.286 1.00 25.22 ? 118 VAL B CG1 1 
ATOM   1727 C  CG2 . VAL B 1 119 ? 17.277 8.681   18.863 1.00 30.08 ? 118 VAL B CG2 1 
ATOM   1728 N  N   . VAL B 1 120 ? 14.273 7.562   22.226 1.00 20.05 ? 119 VAL B N   1 
ATOM   1729 C  CA  . VAL B 1 120 ? 12.942 7.718   22.794 1.00 21.07 ? 119 VAL B CA  1 
ATOM   1730 C  C   . VAL B 1 120 ? 12.804 9.242   23.123 1.00 26.41 ? 119 VAL B C   1 
ATOM   1731 O  O   . VAL B 1 120 ? 13.707 9.857   23.746 1.00 20.71 ? 119 VAL B O   1 
ATOM   1732 C  CB  . VAL B 1 120 ? 12.689 6.752   24.007 1.00 24.15 ? 119 VAL B CB  1 
ATOM   1733 C  CG1 . VAL B 1 120 ? 13.746 6.914   25.074 1.00 26.44 ? 119 VAL B CG1 1 
ATOM   1734 C  CG2 . VAL B 1 120 ? 11.253 6.969   24.556 1.00 23.77 ? 119 VAL B CG2 1 
ATOM   1735 N  N   . HIS B 1 121 ? 11.713 9.845   22.627 1.00 23.86 ? 120 HIS B N   1 
ATOM   1736 C  CA  . HIS B 1 121 ? 11.472 11.293  22.755 1.00 27.66 ? 120 HIS B CA  1 
ATOM   1737 C  C   . HIS B 1 121 ? 10.615 11.766  23.921 1.00 28.09 ? 120 HIS B C   1 
ATOM   1738 O  O   . HIS B 1 121 ? 9.834  11.033  24.534 1.00 24.81 ? 120 HIS B O   1 
ATOM   1739 C  CB  . HIS B 1 121 ? 10.834 11.858  21.477 1.00 25.33 ? 120 HIS B CB  1 
ATOM   1740 C  CG  . HIS B 1 121 ? 11.719 11.825  20.273 1.00 32.49 ? 120 HIS B CG  1 
ATOM   1741 N  ND1 . HIS B 1 121 ? 12.519 12.887  19.911 1.00 29.92 ? 120 HIS B ND1 1 
ATOM   1742 C  CD2 . HIS B 1 121 ? 11.886 10.885  19.315 1.00 30.67 ? 120 HIS B CD2 1 
ATOM   1743 C  CE1 . HIS B 1 121 ? 13.134 12.608  18.778 1.00 33.40 ? 120 HIS B CE1 1 
ATOM   1744 N  NE2 . HIS B 1 121 ? 12.771 11.401  18.395 1.00 28.97 ? 120 HIS B NE2 1 
ATOM   1745 N  N   . GLU B 1 122 ? 10.774 13.046  24.186 1.00 30.41 ? 121 GLU B N   1 
ATOM   1746 C  CA  . GLU B 1 122 ? 10.059 13.744  25.244 1.00 31.05 ? 121 GLU B CA  1 
ATOM   1747 C  C   . GLU B 1 122 ? 8.546  13.782  25.002 1.00 26.48 ? 121 GLU B C   1 
ATOM   1748 O  O   . GLU B 1 122 ? 7.785  13.505  25.904 1.00 28.03 ? 121 GLU B O   1 
ATOM   1749 C  CB  . GLU B 1 122 ? 10.628 15.147  25.289 1.00 36.70 ? 121 GLU B CB  1 
ATOM   1750 C  CG  . GLU B 1 122 ? 10.126 16.035  26.352 1.00 42.40 ? 121 GLU B CG  1 
ATOM   1751 C  CD  . GLU B 1 122 ? 10.916 17.313  26.311 1.00 55.39 ? 121 GLU B CD  1 
ATOM   1752 O  OE1 . GLU B 1 122 ? 10.698 18.103  25.356 1.00 49.97 ? 121 GLU B OE1 1 
ATOM   1753 O  OE2 . GLU B 1 122 ? 11.788 17.495  27.208 1.00 61.28 ? 121 GLU B OE2 1 
ATOM   1754 N  N   . LYS B 1 123 ? 8.119  14.102  23.776 1.00 31.13 ? 122 LYS B N   1 
ATOM   1755 C  CA  . LYS B 1 123 ? 6.679  14.185  23.459 1.00 30.93 ? 122 LYS B CA  1 
ATOM   1756 C  C   . LYS B 1 123 ? 6.277  13.066  22.540 1.00 30.24 ? 122 LYS B C   1 
ATOM   1757 O  O   . LYS B 1 123 ? 7.128  12.307  22.069 1.00 27.02 ? 122 LYS B O   1 
ATOM   1758 C  CB  . LYS B 1 123 ? 6.350  15.517  22.759 1.00 37.86 ? 122 LYS B CB  1 
ATOM   1759 C  CG  . LYS B 1 123 ? 6.830  16.750  23.525 1.00 45.90 ? 122 LYS B CG  1 
ATOM   1760 C  CD  . LYS B 1 123 ? 6.962  17.997  22.643 1.00 54.02 ? 122 LYS B CD  1 
ATOM   1761 C  CE  . LYS B 1 123 ? 5.653  18.728  22.490 1.00 61.61 ? 122 LYS B CE  1 
ATOM   1762 N  NZ  . LYS B 1 123 ? 5.849  20.073  21.852 1.00 68.96 ? 122 LYS B NZ  1 
ATOM   1763 N  N   . ALA B 1 124 ? 4.979  12.943  22.319 1.00 29.11 ? 123 ALA B N   1 
ATOM   1764 C  CA  . ALA B 1 124 ? 4.408  12.005  21.375 1.00 29.01 ? 123 ALA B CA  1 
ATOM   1765 C  C   . ALA B 1 124 ? 4.761  12.383  19.948 1.00 28.02 ? 123 ALA B C   1 
ATOM   1766 O  O   . ALA B 1 124 ? 4.925  13.520  19.645 1.00 29.23 ? 123 ALA B O   1 
ATOM   1767 C  CB  . ALA B 1 124 ? 2.910  11.918  21.562 1.00 27.56 ? 123 ALA B CB  1 
ATOM   1768 N  N   . ASP B 1 125 ? 4.909  11.399  19.093 1.00 27.19 ? 124 ASP B N   1 
ATOM   1769 C  CA  . ASP B 1 125 ? 4.824  11.575  17.653 1.00 29.02 ? 124 ASP B CA  1 
ATOM   1770 C  C   . ASP B 1 125 ? 3.349  11.644  17.265 1.00 25.53 ? 124 ASP B C   1 
ATOM   1771 O  O   . ASP B 1 125 ? 2.617  10.759  17.566 1.00 24.10 ? 124 ASP B O   1 
ATOM   1772 C  CB  . ASP B 1 125 ? 5.489  10.358  17.009 1.00 34.10 ? 124 ASP B CB  1 
ATOM   1773 C  CG  . ASP B 1 125 ? 5.783  10.535  15.546 1.00 37.18 ? 124 ASP B CG  1 
ATOM   1774 O  OD1 . ASP B 1 125 ? 5.004  11.176  14.841 1.00 34.62 ? 124 ASP B OD1 1 
ATOM   1775 O  OD2 . ASP B 1 125 ? 6.789  9.982   15.108 1.00 31.57 ? 124 ASP B OD2 1 
ATOM   1776 N  N   . ASP B 1 126 ? 2.914  12.710  16.616 1.00 28.84 ? 125 ASP B N   1 
ATOM   1777 C  CA  . ASP B 1 126 ? 1.508  12.783  16.254 1.00 31.05 ? 125 ASP B CA  1 
ATOM   1778 C  C   . ASP B 1 126 ? 1.181  11.945  15.022 1.00 31.88 ? 125 ASP B C   1 
ATOM   1779 O  O   . ASP B 1 126 ? 0.047  11.826  14.641 1.00 32.64 ? 125 ASP B O   1 
ATOM   1780 C  CB  . ASP B 1 126 ? 1.022  14.218  16.109 1.00 29.76 ? 125 ASP B CB  1 
ATOM   1781 C  CG  . ASP B 1 126 ? 1.648  14.929  14.940 1.00 28.20 ? 125 ASP B CG  1 
ATOM   1782 O  OD1 . ASP B 1 126 ? 2.144  14.273  14.030 1.00 34.75 ? 125 ASP B OD1 1 
ATOM   1783 O  OD2 . ASP B 1 126 ? 1.652  16.148  14.935 1.00 34.88 ? 125 ASP B OD2 1 
ATOM   1784 N  N   . LEU B 1 127 ? 2.209  11.351  14.435 1.00 31.15 ? 126 LEU B N   1 
ATOM   1785 C  CA  . LEU B 1 127 ? 2.100  10.532  13.230 1.00 31.62 ? 126 LEU B CA  1 
ATOM   1786 C  C   . LEU B 1 127 ? 1.389  11.243  12.066 1.00 36.53 ? 126 LEU B C   1 
ATOM   1787 O  O   . LEU B 1 127 ? 0.743  10.587  11.252 1.00 38.59 ? 126 LEU B O   1 
ATOM   1788 C  CB  . LEU B 1 127 ? 1.349  9.237   13.511 1.00 35.50 ? 126 LEU B CB  1 
ATOM   1789 C  CG  . LEU B 1 127 ? 1.622  8.510   14.828 1.00 44.33 ? 126 LEU B CG  1 
ATOM   1790 C  CD1 . LEU B 1 127 ? 0.429  7.627   15.186 1.00 41.82 ? 126 LEU B CD1 1 
ATOM   1791 C  CD2 . LEU B 1 127 ? 2.876  7.721   14.707 1.00 36.00 ? 126 LEU B CD2 1 
ATOM   1792 N  N   . GLY B 1 128 ? 1.516  12.564  11.983 1.00 35.80 ? 127 GLY B N   1 
ATOM   1793 C  CA  . GLY B 1 128 ? 0.872  13.291  10.904 1.00 35.60 ? 127 GLY B CA  1 
ATOM   1794 C  C   . GLY B 1 128 ? -0.600 13.554  11.164 1.00 39.70 ? 127 GLY B C   1 
ATOM   1795 O  O   . GLY B 1 128 ? -1.287 14.131  10.332 1.00 36.92 ? 127 GLY B O   1 
ATOM   1796 N  N   . LYS B 1 129 ? -1.087 13.148  12.333 1.00 36.62 ? 128 LYS B N   1 
ATOM   1797 C  CA  . LYS B 1 129 ? -2.494 13.319  12.658 1.00 37.39 ? 128 LYS B CA  1 
ATOM   1798 C  C   . LYS B 1 129 ? -2.682 14.127  13.955 1.00 36.67 ? 128 LYS B C   1 
ATOM   1799 O  O   . LYS B 1 129 ? -3.440 13.737  14.840 1.00 36.57 ? 128 LYS B O   1 
ATOM   1800 C  CB  . LYS B 1 129 ? -3.139 11.934  12.757 1.00 42.89 ? 128 LYS B CB  1 
ATOM   1801 C  CG  . LYS B 1 129 ? -3.657 11.370  11.433 1.00 50.44 ? 128 LYS B CG  1 
ATOM   1802 C  CD  . LYS B 1 129 ? -2.746 11.617  10.240 1.00 60.88 ? 128 LYS B CD  1 
ATOM   1803 C  CE  . LYS B 1 129 ? -3.395 11.103  8.946  1.00 65.18 ? 128 LYS B CE  1 
ATOM   1804 N  NZ  . LYS B 1 129 ? -2.648 11.443  7.689  1.00 63.46 ? 128 LYS B NZ  1 
ATOM   1805 N  N   . GLY B 1 130 ? -1.986 15.263  14.022 1.00 32.06 ? 129 GLY B N   1 
ATOM   1806 C  CA  . GLY B 1 130 ? -2.019 16.145  15.175 1.00 28.53 ? 129 GLY B CA  1 
ATOM   1807 C  C   . GLY B 1 130 ? -3.188 17.122  15.237 1.00 29.33 ? 129 GLY B C   1 
ATOM   1808 O  O   . GLY B 1 130 ? -3.308 17.865  16.186 1.00 30.32 ? 129 GLY B O   1 
ATOM   1809 N  N   . GLY B 1 131 ? -4.042 17.134  14.219 1.00 33.20 ? 130 GLY B N   1 
ATOM   1810 C  CA  . GLY B 1 131 ? -5.214 17.993  14.259 1.00 30.85 ? 130 GLY B CA  1 
ATOM   1811 C  C   . GLY B 1 131 ? -5.013 19.400  13.768 1.00 34.04 ? 130 GLY B C   1 
ATOM   1812 O  O   . GLY B 1 131 ? -5.897 20.233  13.940 1.00 37.49 ? 130 GLY B O   1 
ATOM   1813 N  N   . ASN B 1 132 ? -3.859 19.681  13.170 1.00 37.54 ? 131 ASN B N   1 
ATOM   1814 C  CA  . ASN B 1 132 ? -3.594 21.024  12.661 1.00 39.78 ? 131 ASN B CA  1 
ATOM   1815 C  C   . ASN B 1 132 ? -2.646 21.012  11.461 1.00 43.91 ? 131 ASN B C   1 
ATOM   1816 O  O   . ASN B 1 132 ? -2.015 22.023  11.163 1.00 49.50 ? 131 ASN B O   1 
ATOM   1817 C  CB  . ASN B 1 132 ? -3.020 21.890  13.771 1.00 42.67 ? 131 ASN B CB  1 
ATOM   1818 C  CG  . ASN B 1 132 ? -2.843 23.348  13.349 1.00 55.30 ? 131 ASN B CG  1 
ATOM   1819 O  OD1 . ASN B 1 132 ? -3.770 23.981  12.833 1.00 54.34 ? 131 ASN B OD1 1 
ATOM   1820 N  ND2 . ASN B 1 132 ? -1.654 23.890  13.586 1.00 58.22 ? 131 ASN B ND2 1 
ATOM   1821 N  N   . ALA B 1 141 ? 8.100  15.647  18.059 1.00 49.13 ? 140 ALA B N   1 
ATOM   1822 C  CA  . ALA B 1 141 ? 8.189  14.753  19.224 1.00 46.15 ? 140 ALA B CA  1 
ATOM   1823 C  C   . ALA B 1 141 ? 9.105  15.300  20.312 1.00 43.18 ? 140 ALA B C   1 
ATOM   1824 O  O   . ALA B 1 141 ? 9.294  14.671  21.347 1.00 41.83 ? 140 ALA B O   1 
ATOM   1825 C  CB  . ALA B 1 141 ? 8.661  13.340  18.795 1.00 41.48 ? 140 ALA B CB  1 
ATOM   1826 N  N   . GLY B 1 142 ? 9.691  16.470  20.081 1.00 42.39 ? 141 GLY B N   1 
ATOM   1827 C  CA  . GLY B 1 142 ? 10.536 17.042  21.111 1.00 40.84 ? 141 GLY B CA  1 
ATOM   1828 C  C   . GLY B 1 142 ? 11.946 16.496  21.302 1.00 41.21 ? 141 GLY B C   1 
ATOM   1829 O  O   . GLY B 1 142 ? 12.515 15.821  20.422 1.00 41.75 ? 141 GLY B O   1 
ATOM   1830 N  N   . SER B 1 143 ? 12.515 16.797  22.469 1.00 34.55 ? 142 SER B N   1 
ATOM   1831 C  CA  . SER B 1 143 ? 13.879 16.391  22.766 1.00 42.54 ? 142 SER B CA  1 
ATOM   1832 C  C   . SER B 1 143 ? 14.110 14.878  22.865 1.00 39.92 ? 142 SER B C   1 
ATOM   1833 O  O   . SER B 1 143 ? 13.175 14.084  23.032 1.00 37.43 ? 142 SER B O   1 
ATOM   1834 C  CB  . SER B 1 143 ? 14.399 17.109  24.027 1.00 38.98 ? 142 SER B CB  1 
ATOM   1835 O  OG  . SER B 1 143 ? 13.847 16.609  25.231 1.00 47.49 ? 142 SER B OG  1 
ATOM   1836 N  N   . ARG B 1 144 ? 15.376 14.511  22.733 1.00 36.04 ? 143 ARG B N   1 
ATOM   1837 C  CA  . ARG B 1 144 ? 15.818 13.115  22.761 1.00 32.66 ? 143 ARG B CA  1 
ATOM   1838 C  C   . ARG B 1 144 ? 16.170 12.752  24.217 1.00 28.17 ? 143 ARG B C   1 
ATOM   1839 O  O   . ARG B 1 144 ? 17.213 13.161  24.727 1.00 34.16 ? 143 ARG B O   1 
ATOM   1840 C  CB  . ARG B 1 144 ? 17.026 13.009  21.801 1.00 30.82 ? 143 ARG B CB  1 
ATOM   1841 C  CG  . ARG B 1 144 ? 16.699 13.627  20.420 1.00 26.53 ? 143 ARG B CG  1 
ATOM   1842 C  CD  . ARG B 1 144 ? 17.791 13.403  19.370 1.00 27.88 ? 143 ARG B CD  1 
ATOM   1843 N  NE  . ARG B 1 144 ? 17.394 13.965  18.082 1.00 31.74 ? 143 ARG B NE  1 
ATOM   1844 C  CZ  . ARG B 1 144 ? 18.148 14.013  16.983 1.00 36.13 ? 143 ARG B CZ  1 
ATOM   1845 N  NH1 . ARG B 1 144 ? 17.641 14.562  15.890 1.00 30.53 ? 143 ARG B NH1 1 
ATOM   1846 N  NH2 . ARG B 1 144 ? 19.393 13.510  16.954 1.00 31.75 ? 143 ARG B NH2 1 
ATOM   1847 N  N   . LEU B 1 145 ? 15.291 12.019  24.898 1.00 26.24 ? 144 LEU B N   1 
ATOM   1848 C  CA  . LEU B 1 145 ? 15.502 11.659  26.296 1.00 28.58 ? 144 LEU B CA  1 
ATOM   1849 C  C   . LEU B 1 145 ? 16.568 10.601  26.502 1.00 29.09 ? 144 LEU B C   1 
ATOM   1850 O  O   . LEU B 1 145 ? 17.275 10.625  27.502 1.00 25.84 ? 144 LEU B O   1 
ATOM   1851 C  CB  . LEU B 1 145 ? 14.200 11.192  26.987 1.00 24.56 ? 144 LEU B CB  1 
ATOM   1852 C  CG  . LEU B 1 145 ? 12.985 12.147  26.909 1.00 37.35 ? 144 LEU B CG  1 
ATOM   1853 C  CD1 . LEU B 1 145 ? 11.818 11.616  27.727 1.00 30.49 ? 144 LEU B CD1 1 
ATOM   1854 C  CD2 . LEU B 1 145 ? 13.396 13.491  27.429 1.00 37.15 ? 144 LEU B CD2 1 
ATOM   1855 N  N   . ALA B 1 146 ? 16.665 9.658   25.576 1.00 25.07 ? 145 ALA B N   1 
ATOM   1856 C  CA  . ALA B 1 146 ? 17.666 8.617   25.701 1.00 29.51 ? 145 ALA B CA  1 
ATOM   1857 C  C   . ALA B 1 146 ? 17.821 7.995   24.334 1.00 28.70 ? 145 ALA B C   1 
ATOM   1858 O  O   . ALA B 1 146 ? 16.897 8.074   23.511 1.00 28.23 ? 145 ALA B O   1 
ATOM   1859 C  CB  . ALA B 1 146 ? 17.220 7.577   26.723 1.00 26.71 ? 145 ALA B CB  1 
ATOM   1860 N  N   . CYS B 1 147 ? 18.984 7.397   24.091 1.00 23.19 ? 146 CYS B N   1 
ATOM   1861 C  CA  . CYS B 1 147 ? 19.266 6.762   22.803 1.00 24.96 ? 146 CYS B CA  1 
ATOM   1862 C  C   . CYS B 1 147 ? 20.330 5.713   22.969 1.00 24.53 ? 146 CYS B C   1 
ATOM   1863 O  O   . CYS B 1 147 ? 20.971 5.621   24.023 1.00 24.30 ? 146 CYS B O   1 
ATOM   1864 C  CB  . CYS B 1 147 ? 19.799 7.791   21.796 1.00 29.07 ? 146 CYS B CB  1 
ATOM   1865 S  SG  . CYS B 1 147 ? 21.284 8.697   22.380 1.00 35.43 ? 146 CYS B SG  1 
ATOM   1866 N  N   . GLY B 1 148 ? 20.528 4.935   21.917 1.00 27.33 ? 147 GLY B N   1 
ATOM   1867 C  CA  . GLY B 1 148 ? 21.562 3.918   21.945 1.00 29.30 ? 147 GLY B CA  1 
ATOM   1868 C  C   . GLY B 1 148 ? 21.744 3.346   20.558 1.00 26.31 ? 147 GLY B C   1 
ATOM   1869 O  O   . GLY B 1 148 ? 20.777 3.174   19.798 1.00 24.09 ? 147 GLY B O   1 
ATOM   1870 N  N   . VAL B 1 149 ? 22.986 3.056   20.225 1.00 22.09 ? 148 VAL B N   1 
ATOM   1871 C  CA  . VAL B 1 149 ? 23.294 2.473   18.920 1.00 20.67 ? 148 VAL B CA  1 
ATOM   1872 C  C   . VAL B 1 149 ? 22.708 1.065   18.872 1.00 26.29 ? 148 VAL B C   1 
ATOM   1873 O  O   . VAL B 1 149 ? 22.764 0.318   19.861 1.00 27.30 ? 148 VAL B O   1 
ATOM   1874 C  CB  . VAL B 1 149 ? 24.836 2.426   18.719 1.00 24.05 ? 148 VAL B CB  1 
ATOM   1875 C  CG1 . VAL B 1 149 ? 25.215 1.759   17.366 1.00 21.74 ? 148 VAL B CG1 1 
ATOM   1876 C  CG2 . VAL B 1 149 ? 25.371 3.826   18.774 1.00 25.47 ? 148 VAL B CG2 1 
ATOM   1877 N  N   . ILE B 1 150 ? 22.151 0.703   17.728 1.00 23.89 ? 149 ILE B N   1 
ATOM   1878 C  CA  . ILE B 1 150 ? 21.560 -0.603  17.520 1.00 22.59 ? 149 ILE B CA  1 
ATOM   1879 C  C   . ILE B 1 150 ? 22.666 -1.557  17.057 1.00 26.85 ? 149 ILE B C   1 
ATOM   1880 O  O   . ILE B 1 150 ? 23.245 -1.370  15.984 1.00 21.67 ? 149 ILE B O   1 
ATOM   1881 C  CB  . ILE B 1 150 ? 20.427 -0.477  16.463 1.00 26.97 ? 149 ILE B CB  1 
ATOM   1882 C  CG1 . ILE B 1 150 ? 19.373 0.481   17.011 1.00 25.62 ? 149 ILE B CG1 1 
ATOM   1883 C  CG2 . ILE B 1 150 ? 19.745 -1.825  16.182 1.00 28.47 ? 149 ILE B CG2 1 
ATOM   1884 C  CD1 . ILE B 1 150 ? 18.336 0.892   15.960 1.00 26.95 ? 149 ILE B CD1 1 
ATOM   1885 N  N   . GLY B 1 151 ? 22.969 -2.570  17.885 1.00 27.83 ? 150 GLY B N   1 
ATOM   1886 C  CA  . GLY B 1 151 ? 24.026 -3.513  17.538 1.00 23.05 ? 150 GLY B CA  1 
ATOM   1887 C  C   . GLY B 1 151 ? 23.562 -4.966  17.355 1.00 26.51 ? 150 GLY B C   1 
ATOM   1888 O  O   . GLY B 1 151 ? 22.510 -5.380  17.846 1.00 24.12 ? 150 GLY B O   1 
ATOM   1889 N  N   . ILE B 1 152 ? 24.356 -5.746  16.630 1.00 26.42 ? 151 ILE B N   1 
ATOM   1890 C  CA  . ILE B 1 152 ? 24.034 -7.151  16.401 1.00 24.44 ? 151 ILE B CA  1 
ATOM   1891 C  C   . ILE B 1 152 ? 24.106 -7.881  17.767 1.00 27.83 ? 151 ILE B C   1 
ATOM   1892 O  O   . ILE B 1 152 ? 25.023 -7.661  18.559 1.00 25.84 ? 151 ILE B O   1 
ATOM   1893 C  CB  . ILE B 1 152 ? 25.037 -7.738  15.372 1.00 26.47 ? 151 ILE B CB  1 
ATOM   1894 C  CG1 . ILE B 1 152 ? 24.916 -6.921  14.063 1.00 29.87 ? 151 ILE B CG1 1 
ATOM   1895 C  CG2 . ILE B 1 152 ? 24.786 -9.265  15.174 1.00 24.88 ? 151 ILE B CG2 1 
ATOM   1896 C  CD1 . ILE B 1 152 ? 25.866 -7.333  12.921 1.00 31.46 ? 151 ILE B CD1 1 
ATOM   1897 N  N   . ALA B 1 153 ? 23.104 -8.707  18.045 1.00 27.40 ? 152 ALA B N   1 
ATOM   1898 C  CA  . ALA B 1 153 ? 23.021 -9.447  19.300 1.00 26.70 ? 152 ALA B CA  1 
ATOM   1899 C  C   . ALA B 1 153 ? 22.923 -10.946 19.039 1.00 26.88 ? 152 ALA B C   1 
ATOM   1900 O  O   . ALA B 1 153 ? 22.561 -11.378 17.946 1.00 28.62 ? 152 ALA B O   1 
ATOM   1901 C  CB  . ALA B 1 153 ? 21.800 -8.998  20.097 1.00 29.56 ? 152 ALA B CB  1 
ATOM   1902 N  N   . GLN B 1 154 ? 23.212 -11.739 20.066 1.00 30.88 ? 153 GLN B N   1 
ATOM   1903 C  CA  . GLN B 1 154 ? 23.163 -13.189 19.943 1.00 33.42 ? 153 GLN B CA  1 
ATOM   1904 C  C   . GLN B 1 154 ? 21.743 -13.738 20.112 1.00 37.83 ? 153 GLN B C   1 
ATOM   1905 O  O   . GLN B 1 154 ? 21.013 -13.276 20.996 1.00 33.57 ? 153 GLN B O   1 
ATOM   1906 C  CB  . GLN B 1 154 ? 24.067 -13.812 21.000 1.00 37.20 ? 153 GLN B CB  1 
ATOM   1907 C  CG  . GLN B 1 154 ? 24.362 -15.262 20.729 1.00 37.51 ? 153 GLN B CG  1 
ATOM   1908 C  CD  . GLN B 1 154 ? 25.296 -15.858 21.755 1.00 43.84 ? 153 GLN B CD  1 
ATOM   1909 O  OE1 . GLN B 1 154 ? 26.059 -16.770 21.447 1.00 52.21 ? 153 GLN B OE1 1 
ATOM   1910 N  NE2 . GLN B 1 154 ? 25.236 -15.354 22.984 1.00 44.62 ? 153 GLN B NE2 1 
ATOM   1911 O  OXT . GLN B 1 154 ? 21.398 -14.668 19.353 1.00 43.63 ? 153 GLN B OXT 1 
HETATM 1912 CU CU  A CU  C 2 .   ? 39.563 -8.982  21.250 0.83 29.81 ? 154 CU  A CU  1 
HETATM 1913 CU CU  B CU  C 2 .   ? 39.403 -7.677  21.052 0.17 31.26 ? 154 CU  A CU  1 
HETATM 1914 CU CU  . CU  D 2 .   ? 13.009 10.901  16.493 1.00 42.39 ? 154 CU  B CU  1 
HETATM 1915 O  O   . HOH E 3 .   ? 41.978 -14.499 16.434 1.00 29.97 ? 155 HOH A O   1 
HETATM 1916 O  O   . HOH E 3 .   ? 45.337 1.628   31.133 1.00 23.18 ? 156 HOH A O   1 
HETATM 1917 O  O   . HOH E 3 .   ? 23.843 -2.568  22.625 1.00 24.30 ? 157 HOH A O   1 
HETATM 1918 O  O   . HOH E 3 .   ? 54.198 -4.625  24.369 1.00 33.03 ? 158 HOH A O   1 
HETATM 1919 O  O   . HOH E 3 .   ? 58.672 -17.206 25.092 1.00 31.83 ? 159 HOH A O   1 
HETATM 1920 O  O   . HOH E 3 .   ? 38.079 -10.976 25.192 1.00 27.88 ? 160 HOH A O   1 
HETATM 1921 O  O   . HOH E 3 .   ? 40.655 1.645   31.441 1.00 26.25 ? 161 HOH A O   1 
HETATM 1922 O  O   . HOH E 3 .   ? 41.932 -8.141  9.370  1.00 37.79 ? 162 HOH A O   1 
HETATM 1923 O  O   . HOH E 3 .   ? 37.156 -13.312 23.803 1.00 35.96 ? 163 HOH A O   1 
HETATM 1924 O  O   . HOH E 3 .   ? 32.150 -4.687  31.522 1.00 31.42 ? 164 HOH A O   1 
HETATM 1925 O  O   . HOH E 3 .   ? 27.112 -12.745 14.209 1.00 32.92 ? 165 HOH A O   1 
HETATM 1926 O  O   . HOH E 3 .   ? 28.722 2.101   22.043 1.00 37.77 ? 166 HOH A O   1 
HETATM 1927 O  O   . HOH E 3 .   ? 47.068 -3.108  13.768 1.00 30.12 ? 167 HOH A O   1 
HETATM 1928 O  O   . HOH E 3 .   ? 24.104 -10.319 22.553 1.00 32.37 ? 168 HOH A O   1 
HETATM 1929 O  O   . HOH E 3 .   ? 46.686 0.630   33.394 1.00 32.50 ? 169 HOH A O   1 
HETATM 1930 O  O   . HOH E 3 .   ? 51.663 -2.347  28.016 1.00 30.46 ? 170 HOH A O   1 
HETATM 1931 O  O   . HOH E 3 .   ? 38.744 -0.632  31.667 1.00 33.81 ? 171 HOH A O   1 
HETATM 1932 O  O   . HOH E 3 .   ? 51.421 -7.688  26.658 1.00 34.30 ? 172 HOH A O   1 
HETATM 1933 O  O   . HOH E 3 .   ? 42.981 -12.840 6.173  1.00 37.56 ? 173 HOH A O   1 
HETATM 1934 O  O   . HOH E 3 .   ? 26.495 -3.721  7.261  1.00 40.40 ? 174 HOH A O   1 
HETATM 1935 O  O   . HOH E 3 .   ? 30.341 3.722   19.634 1.00 31.29 ? 175 HOH A O   1 
HETATM 1936 O  O   . HOH E 3 .   ? 46.392 -0.049  29.139 1.00 30.05 ? 176 HOH A O   1 
HETATM 1937 O  O   . HOH E 3 .   ? 46.237 -1.790  32.514 1.00 33.94 ? 177 HOH A O   1 
HETATM 1938 O  O   . HOH E 3 .   ? 26.710 -5.294  10.014 1.00 35.60 ? 178 HOH A O   1 
HETATM 1939 O  O   . HOH E 3 .   ? 47.270 9.031   28.061 1.00 31.28 ? 179 HOH A O   1 
HETATM 1940 O  O   . HOH E 3 .   ? 42.203 -10.135 9.722  1.00 45.39 ? 180 HOH A O   1 
HETATM 1941 O  O   . HOH E 3 .   ? 30.263 -11.880 25.753 1.00 30.38 ? 181 HOH A O   1 
HETATM 1942 O  O   . HOH E 3 .   ? 23.844 -5.847  4.426  1.00 49.17 ? 182 HOH A O   1 
HETATM 1943 O  O   . HOH E 3 .   ? 29.179 -16.729 18.826 1.00 35.78 ? 183 HOH A O   1 
HETATM 1944 O  O   . HOH E 3 .   ? 36.147 5.379   29.314 1.00 39.63 ? 184 HOH A O   1 
HETATM 1945 O  O   . HOH E 3 .   ? 37.988 2.526   30.244 1.00 34.65 ? 185 HOH A O   1 
HETATM 1946 O  O   . HOH E 3 .   ? 46.963 -2.513  30.088 1.00 38.00 ? 186 HOH A O   1 
HETATM 1947 O  O   . HOH E 3 .   ? 29.602 -9.946  0.916  1.00 45.37 ? 187 HOH A O   1 
HETATM 1948 O  O   . HOH E 3 .   ? 33.048 -2.445  30.164 1.00 37.60 ? 188 HOH A O   1 
HETATM 1949 O  O   . HOH E 3 .   ? 25.201 -4.182  3.402  1.00 51.26 ? 189 HOH A O   1 
HETATM 1950 O  O   . HOH E 3 .   ? 47.966 -13.152 22.645 1.00 39.25 ? 190 HOH A O   1 
HETATM 1951 O  O   . HOH E 3 .   ? 30.656 3.835   23.310 1.00 41.57 ? 191 HOH A O   1 
HETATM 1952 O  O   . HOH E 3 .   ? 50.341 -4.437  26.678 1.00 43.33 ? 192 HOH A O   1 
HETATM 1953 O  O   . HOH E 3 .   ? 37.468 1.530   -0.243 1.00 39.57 ? 193 HOH A O   1 
HETATM 1954 O  O   . HOH E 3 .   ? 48.757 -2.437  11.866 1.00 37.83 ? 194 HOH A O   1 
HETATM 1955 O  O   . HOH E 3 .   ? 25.189 -0.687  29.657 1.00 43.66 ? 195 HOH A O   1 
HETATM 1956 O  O   . HOH E 3 .   ? 52.740 14.253  27.370 1.00 50.50 ? 196 HOH A O   1 
HETATM 1957 O  O   . HOH E 3 .   ? 52.431 -17.101 20.187 1.00 38.89 ? 197 HOH A O   1 
HETATM 1958 O  O   . HOH E 3 .   ? 37.971 10.384  23.363 1.00 49.36 ? 198 HOH A O   1 
HETATM 1959 O  O   . HOH E 3 .   ? 24.464 -8.830  29.180 1.00 38.27 ? 199 HOH A O   1 
HETATM 1960 O  O   . HOH E 3 .   ? 35.324 -15.952 17.094 1.00 39.25 ? 200 HOH A O   1 
HETATM 1961 O  O   . HOH E 3 .   ? 37.618 -14.593 20.457 1.00 41.57 ? 201 HOH A O   1 
HETATM 1962 O  O   . HOH E 3 .   ? 39.484 -14.227 6.148  1.00 50.22 ? 202 HOH A O   1 
HETATM 1963 O  O   . HOH E 3 .   ? 31.259 0.975   26.027 1.00 47.60 ? 203 HOH A O   1 
HETATM 1964 O  O   . HOH E 3 .   ? 43.881 -17.164 19.243 1.00 55.77 ? 204 HOH A O   1 
HETATM 1965 O  O   . HOH E 3 .   ? 25.905 -12.562 11.631 1.00 53.77 ? 205 HOH A O   1 
HETATM 1966 O  O   . HOH E 3 .   ? 28.924 -11.928 8.116  1.00 46.99 ? 206 HOH A O   1 
HETATM 1967 O  O   . HOH E 3 .   ? 47.808 8.197   30.555 1.00 40.94 ? 207 HOH A O   1 
HETATM 1968 O  O   . HOH E 3 .   ? 37.226 -14.720 10.655 1.00 44.33 ? 208 HOH A O   1 
HETATM 1969 O  O   . HOH E 3 .   ? 34.038 11.330  14.766 1.00 49.06 ? 209 HOH A O   1 
HETATM 1970 O  O   . HOH E 3 .   ? 28.246 -16.814 15.251 1.00 40.17 ? 210 HOH A O   1 
HETATM 1971 O  O   . HOH E 3 .   ? 48.764 2.510   16.988 1.00 35.83 ? 211 HOH A O   1 
HETATM 1972 O  O   . HOH E 3 .   ? 39.145 -12.957 24.771 1.00 50.14 ? 212 HOH A O   1 
HETATM 1973 O  O   . HOH E 3 .   ? 21.260 -9.003  25.529 1.00 45.60 ? 213 HOH A O   1 
HETATM 1974 O  O   . HOH E 3 .   ? 54.525 -0.244  17.099 1.00 38.22 ? 214 HOH A O   1 
HETATM 1975 O  O   . HOH E 3 .   ? 28.211 7.017   6.051  1.00 48.60 ? 215 HOH A O   1 
HETATM 1976 O  O   . HOH E 3 .   ? 54.141 -17.887 27.433 1.00 46.57 ? 216 HOH A O   1 
HETATM 1977 O  O   . HOH E 3 .   ? 31.239 0.258   28.307 1.00 46.82 ? 217 HOH A O   1 
HETATM 1978 O  O   . HOH E 3 .   ? 29.671 -2.973  22.859 1.00 41.94 ? 218 HOH A O   1 
HETATM 1979 O  O   . HOH E 3 .   ? 43.746 -12.497 16.952 1.00 49.81 ? 219 HOH A O   1 
HETATM 1980 O  O   . HOH E 3 .   ? 38.821 -10.771 27.869 1.00 49.46 ? 220 HOH A O   1 
HETATM 1981 O  O   . HOH E 3 .   ? 45.830 10.163  -1.341 1.00 56.97 ? 221 HOH A O   1 
HETATM 1982 O  O   . HOH E 3 .   ? 28.490 -8.986  8.937  1.00 39.05 ? 222 HOH A O   1 
HETATM 1983 O  O   . HOH E 3 .   ? 40.003 -11.243 22.690 1.00 44.86 ? 223 HOH A O   1 
HETATM 1984 O  O   . HOH E 3 .   ? 21.656 -1.366  30.915 1.00 54.88 ? 224 HOH A O   1 
HETATM 1985 O  O   . HOH E 3 .   ? 50.659 5.591   18.552 1.00 50.06 ? 225 HOH A O   1 
HETATM 1986 O  O   . HOH E 3 .   ? 34.021 8.540   11.350 1.00 47.91 ? 226 HOH A O   1 
HETATM 1987 O  O   . HOH E 3 .   ? 54.088 5.169   30.339 1.00 49.63 ? 227 HOH A O   1 
HETATM 1988 O  O   . HOH E 3 .   ? 31.124 -1.727  34.224 1.00 54.88 ? 228 HOH A O   1 
HETATM 1989 O  O   . HOH E 3 .   ? 55.344 9.914   24.330 1.00 46.57 ? 229 HOH A O   1 
HETATM 1990 O  O   . HOH E 3 .   ? 54.987 -21.579 20.968 1.00 57.91 ? 230 HOH A O   1 
HETATM 1991 O  O   . HOH E 3 .   ? 27.396 5.197   4.949  1.00 49.48 ? 231 HOH A O   1 
HETATM 1992 O  O   . HOH E 3 .   ? 35.481 -1.971  30.424 1.00 49.69 ? 232 HOH A O   1 
HETATM 1993 O  O   . HOH E 3 .   ? 49.665 -13.669 24.519 1.00 53.94 ? 233 HOH A O   1 
HETATM 1994 O  O   . HOH E 3 .   ? 34.920 9.340   8.914  1.00 65.89 ? 234 HOH A O   1 
HETATM 1995 O  O   . HOH E 3 .   ? 44.902 7.537   0.234  1.00 64.26 ? 235 HOH A O   1 
HETATM 1996 O  O   . HOH E 3 .   ? 46.389 -14.219 18.359 1.00 50.43 ? 236 HOH A O   1 
HETATM 1997 O  O   . HOH E 3 .   ? 35.613 5.596   32.348 1.00 47.11 ? 237 HOH A O   1 
HETATM 1998 O  O   . HOH E 3 .   ? 44.457 -4.402  10.584 1.00 48.66 ? 238 HOH A O   1 
HETATM 1999 O  O   . HOH E 3 .   ? 31.943 4.111   30.584 1.00 46.97 ? 239 HOH A O   1 
HETATM 2000 O  O   . HOH E 3 .   ? 38.599 7.836   30.933 1.00 48.71 ? 240 HOH A O   1 
HETATM 2001 O  O   . HOH E 3 .   ? 22.355 -3.468  31.562 1.00 61.26 ? 241 HOH A O   1 
HETATM 2002 O  O   . HOH E 3 .   ? 26.328 -11.368 23.970 1.00 50.03 ? 242 HOH A O   1 
HETATM 2003 O  O   . HOH E 3 .   ? 37.086 -4.468  2.430  1.00 47.71 ? 243 HOH A O   1 
HETATM 2004 O  O   . HOH E 3 .   ? 41.791 -11.388 25.040 1.00 47.68 ? 244 HOH A O   1 
HETATM 2005 O  O   . HOH E 3 .   ? 49.653 6.153   30.461 1.00 49.45 ? 245 HOH A O   1 
HETATM 2006 O  O   . HOH E 3 .   ? 36.030 -4.517  31.530 1.00 68.44 ? 246 HOH A O   1 
HETATM 2007 O  O   . HOH E 3 .   ? 38.936 -3.035  33.125 1.00 52.52 ? 247 HOH A O   1 
HETATM 2008 O  O   . HOH E 3 .   ? 43.049 -12.032 8.429  1.00 47.78 ? 248 HOH A O   1 
HETATM 2009 O  O   . HOH E 3 .   ? 45.477 9.531   14.923 1.00 59.28 ? 249 HOH A O   1 
HETATM 2010 O  O   . HOH E 3 .   ? 52.047 6.805   31.031 1.00 49.89 ? 250 HOH A O   1 
HETATM 2011 O  O   . HOH E 3 .   ? 29.109 0.448   23.539 1.00 50.25 ? 251 HOH A O   1 
HETATM 2012 O  O   . HOH E 3 .   ? 29.970 -4.739  24.430 1.00 46.15 ? 252 HOH A O   1 
HETATM 2013 O  O   . HOH E 3 .   ? 25.338 1.191   24.015 1.00 55.31 ? 253 HOH A O   1 
HETATM 2014 O  O   . HOH E 3 .   ? 47.596 -8.696  8.544  1.00 52.22 ? 254 HOH A O   1 
HETATM 2015 O  O   . HOH E 3 .   ? 57.454 8.217   23.100 1.00 54.68 ? 255 HOH A O   1 
HETATM 2016 O  O   . HOH F 3 .   ? 16.794 9.362   -1.438 1.00 51.46 ? 155 HOH B O   1 
HETATM 2017 O  O   . HOH F 3 .   ? 23.297 0.215   22.479 1.00 24.63 ? 156 HOH B O   1 
HETATM 2018 O  O   . HOH F 3 .   ? 0.284  11.040  25.792 1.00 29.00 ? 157 HOH B O   1 
HETATM 2019 O  O   . HOH F 3 .   ? 9.753  4.686   36.059 1.00 27.76 ? 158 HOH B O   1 
HETATM 2020 O  O   . HOH F 3 .   ? -1.087 2.797   33.993 1.00 39.04 ? 159 HOH B O   1 
HETATM 2021 O  O   . HOH F 3 .   ? 25.269 3.033   22.283 1.00 30.84 ? 160 HOH B O   1 
HETATM 2022 O  O   . HOH F 3 .   ? 9.574  11.463  30.054 1.00 32.44 ? 161 HOH B O   1 
HETATM 2023 O  O   . HOH F 3 .   ? -1.914 12.306  16.556 1.00 33.44 ? 162 HOH B O   1 
HETATM 2024 O  O   . HOH F 3 .   ? 29.236 5.882   18.134 1.00 30.85 ? 163 HOH B O   1 
HETATM 2025 O  O   . HOH F 3 .   ? 4.660  2.038   18.126 1.00 32.38 ? 164 HOH B O   1 
HETATM 2026 O  O   . HOH F 3 .   ? -1.137 3.233   24.172 1.00 28.93 ? 165 HOH B O   1 
HETATM 2027 O  O   . HOH F 3 .   ? 4.054  12.318  28.744 1.00 34.03 ? 166 HOH B O   1 
HETATM 2028 O  O   . HOH F 3 .   ? 5.916  0.787   13.651 1.00 37.64 ? 167 HOH B O   1 
HETATM 2029 O  O   . HOH F 3 .   ? 26.368 12.998  13.318 1.00 44.68 ? 168 HOH B O   1 
HETATM 2030 O  O   . HOH F 3 .   ? 23.164 -1.268  8.644  1.00 38.81 ? 169 HOH B O   1 
HETATM 2031 O  O   . HOH F 3 .   ? 9.170  13.806  28.625 1.00 39.45 ? 170 HOH B O   1 
HETATM 2032 O  O   . HOH F 3 .   ? 3.148  14.836  23.797 1.00 33.69 ? 171 HOH B O   1 
HETATM 2033 O  O   . HOH F 3 .   ? 22.951 -4.136  8.293  1.00 44.59 ? 172 HOH B O   1 
HETATM 2034 O  O   . HOH F 3 .   ? 22.013 -12.158 15.573 1.00 43.21 ? 173 HOH B O   1 
HETATM 2035 O  O   . HOH F 3 .   ? 22.998 6.726   5.923  1.00 37.63 ? 174 HOH B O   1 
HETATM 2036 O  O   . HOH F 3 .   ? 18.206 -8.696  21.389 1.00 37.71 ? 175 HOH B O   1 
HETATM 2037 O  O   . HOH F 3 .   ? -1.843 23.070  8.820  1.00 43.60 ? 176 HOH B O   1 
HETATM 2038 O  O   . HOH F 3 .   ? 19.452 16.167  13.028 1.00 46.44 ? 177 HOH B O   1 
HETATM 2039 O  O   . HOH F 3 .   ? 3.904  -0.863  31.619 1.00 38.33 ? 178 HOH B O   1 
HETATM 2040 O  O   . HOH F 3 .   ? 16.166 17.419  19.335 1.00 50.20 ? 179 HOH B O   1 
HETATM 2041 O  O   . HOH F 3 .   ? 1.164  8.926   36.930 1.00 32.82 ? 180 HOH B O   1 
HETATM 2042 O  O   . HOH F 3 .   ? 0.760  6.587   18.974 1.00 47.32 ? 181 HOH B O   1 
HETATM 2043 O  O   . HOH F 3 .   ? 18.789 -8.001  26.089 1.00 44.33 ? 182 HOH B O   1 
HETATM 2044 O  O   . HOH F 3 .   ? 11.452 11.464  32.292 1.00 42.59 ? 183 HOH B O   1 
HETATM 2045 O  O   . HOH F 3 .   ? 9.484  7.840   35.927 1.00 44.38 ? 184 HOH B O   1 
HETATM 2046 O  O   . HOH F 3 .   ? 31.956 11.021  13.505 1.00 45.50 ? 185 HOH B O   1 
HETATM 2047 O  O   . HOH F 3 .   ? 8.562  2.531   10.146 1.00 37.19 ? 186 HOH B O   1 
HETATM 2048 O  O   . HOH F 3 .   ? 23.257 7.351   24.687 1.00 50.32 ? 187 HOH B O   1 
HETATM 2049 O  O   . HOH F 3 .   ? 10.660 -11.686 10.146 1.00 48.51 ? 188 HOH B O   1 
HETATM 2050 O  O   . HOH F 3 .   ? 4.128  0.091   28.981 1.00 43.42 ? 189 HOH B O   1 
HETATM 2051 O  O   . HOH F 3 .   ? 23.599 3.197   25.094 1.00 48.55 ? 190 HOH B O   1 
HETATM 2052 O  O   . HOH F 3 .   ? 13.838 -1.000  32.465 1.00 53.49 ? 191 HOH B O   1 
HETATM 2053 O  O   . HOH F 3 .   ? 2.774  -3.420  16.426 1.00 47.34 ? 192 HOH B O   1 
HETATM 2054 O  O   . HOH F 3 .   ? 14.677 15.436  17.084 1.00 52.95 ? 193 HOH B O   1 
HETATM 2055 O  O   . HOH F 3 .   ? 8.810  -5.936  29.188 1.00 49.06 ? 194 HOH B O   1 
HETATM 2056 O  O   . HOH F 3 .   ? 21.674 14.403  24.045 1.00 48.83 ? 195 HOH B O   1 
HETATM 2057 O  O   . HOH F 3 .   ? 8.811  -4.359  33.003 1.00 50.70 ? 196 HOH B O   1 
HETATM 2058 O  O   . HOH F 3 .   ? 16.809 10.719  30.378 1.00 41.13 ? 197 HOH B O   1 
HETATM 2059 O  O   . HOH F 3 .   ? -0.206 5.026   30.208 1.00 40.51 ? 198 HOH B O   1 
HETATM 2060 O  O   . HOH F 3 .   ? 18.240 0.194   36.951 1.00 50.46 ? 199 HOH B O   1 
HETATM 2061 O  O   . HOH F 3 .   ? 17.288 -1.223  32.341 1.00 64.19 ? 200 HOH B O   1 
HETATM 2062 O  O   . HOH F 3 .   ? 19.319 7.474   31.729 1.00 41.69 ? 201 HOH B O   1 
HETATM 2063 O  O   . HOH F 3 .   ? 22.460 -6.874  5.733  1.00 56.18 ? 202 HOH B O   1 
HETATM 2064 O  O   . HOH F 3 .   ? 16.149 17.043  14.777 1.00 50.05 ? 203 HOH B O   1 
HETATM 2065 O  O   . HOH F 3 .   ? 2.317  17.018  22.531 1.00 46.17 ? 204 HOH B O   1 
HETATM 2066 O  O   . HOH F 3 .   ? -0.548 16.421  12.362 1.00 43.48 ? 205 HOH B O   1 
HETATM 2067 O  O   . HOH F 3 .   ? 15.895 -4.115  3.850  1.00 44.09 ? 206 HOH B O   1 
HETATM 2068 O  O   . HOH F 3 .   ? 13.997 -4.649  28.417 1.00 48.85 ? 207 HOH B O   1 
HETATM 2069 O  O   . HOH F 3 .   ? 6.886  3.710   8.485  1.00 56.58 ? 208 HOH B O   1 
HETATM 2070 O  O   . HOH F 3 .   ? 4.906  -0.430  36.145 1.00 49.39 ? 209 HOH B O   1 
HETATM 2071 O  O   . HOH F 3 .   ? 4.785  14.990  16.346 1.00 45.39 ? 210 HOH B O   1 
HETATM 2072 O  O   . HOH F 3 .   ? 18.292 -7.922  28.605 1.00 44.85 ? 211 HOH B O   1 
HETATM 2073 O  O   . HOH F 3 .   ? 11.004 -5.786  7.167  1.00 43.00 ? 212 HOH B O   1 
HETATM 2074 O  O   . HOH F 3 .   ? 15.335 -2.313  30.929 1.00 48.46 ? 213 HOH B O   1 
HETATM 2075 O  O   . HOH F 3 .   ? 4.712  12.481  26.303 1.00 42.75 ? 214 HOH B O   1 
HETATM 2076 O  O   . HOH F 3 .   ? 15.653 8.275   1.424  1.00 60.77 ? 215 HOH B O   1 
HETATM 2077 O  O   . HOH F 3 .   ? 33.859 13.904  18.276 1.00 52.53 ? 216 HOH B O   1 
HETATM 2078 O  O   . HOH F 3 .   ? -1.669 8.962   36.478 1.00 50.02 ? 217 HOH B O   1 
HETATM 2079 O  O   . HOH F 3 .   ? 13.693 16.778  29.145 1.00 60.33 ? 218 HOH B O   1 
HETATM 2080 O  O   . HOH F 3 .   ? 4.587  1.747   4.842  1.00 54.69 ? 219 HOH B O   1 
HETATM 2081 O  O   . HOH F 3 .   ? 2.075  3.066   41.739 1.00 44.82 ? 220 HOH B O   1 
HETATM 2082 O  O   . HOH F 3 .   ? 2.250  12.615  32.159 1.00 40.45 ? 221 HOH B O   1 
HETATM 2083 O  O   . HOH F 3 .   ? 21.748 10.043  33.951 1.00 56.53 ? 222 HOH B O   1 
HETATM 2084 O  O   . HOH F 3 .   ? 20.886 2.080   30.277 1.00 50.16 ? 223 HOH B O   1 
HETATM 2085 O  O   . HOH F 3 .   ? 1.646  11.245  35.826 1.00 48.28 ? 224 HOH B O   1 
HETATM 2086 O  O   . HOH F 3 .   ? 20.699 0.797   6.102  1.00 41.55 ? 225 HOH B O   1 
HETATM 2087 O  O   . HOH F 3 .   ? 18.115 8.948   6.232  1.00 50.38 ? 226 HOH B O   1 
HETATM 2088 O  O   . HOH F 3 .   ? 8.341  10.262  10.282 1.00 64.33 ? 227 HOH B O   1 
HETATM 2089 O  O   . HOH F 3 .   ? 27.989 11.336  12.350 1.00 43.12 ? 228 HOH B O   1 
HETATM 2090 O  O   . HOH F 3 .   ? 8.128  6.535   38.302 1.00 51.76 ? 229 HOH B O   1 
HETATM 2091 O  O   . HOH F 3 .   ? 5.679  3.231   12.382 1.00 53.63 ? 230 HOH B O   1 
HETATM 2092 O  O   . HOH F 3 .   ? -0.186 11.367  7.667  1.00 60.37 ? 231 HOH B O   1 
HETATM 2093 O  O   . HOH F 3 .   ? 10.895 -12.185 13.770 1.00 58.35 ? 232 HOH B O   1 
HETATM 2094 O  O   . HOH F 3 .   ? -3.287 7.468   34.712 1.00 52.65 ? 233 HOH B O   1 
HETATM 2095 O  O   . HOH F 3 .   ? 12.566 13.527  15.646 1.00 52.84 ? 234 HOH B O   1 
HETATM 2096 O  O   . HOH F 3 .   ? 23.684 9.480   19.351 1.00 45.17 ? 235 HOH B O   1 
HETATM 2097 O  O   . HOH F 3 .   ? 28.196 3.231   27.113 1.00 52.87 ? 236 HOH B O   1 
HETATM 2098 O  O   . HOH F 3 .   ? 23.942 7.189   19.187 1.00 54.10 ? 237 HOH B O   1 
HETATM 2099 O  O   . HOH F 3 .   ? 16.531 -12.528 9.107  1.00 60.83 ? 238 HOH B O   1 
HETATM 2100 O  O   . HOH F 3 .   ? 10.526 -7.350  27.866 1.00 61.80 ? 239 HOH B O   1 
HETATM 2101 O  O   . HOH F 3 .   ? 3.474  16.537  25.633 1.00 55.03 ? 240 HOH B O   1 
HETATM 2102 O  O   . HOH F 3 .   ? 10.473 1.859   37.246 1.00 60.72 ? 241 HOH B O   1 
HETATM 2103 O  O   . HOH F 3 .   ? 15.779 -6.530  4.210  1.00 52.13 ? 242 HOH B O   1 
HETATM 2104 O  O   . HOH F 3 .   ? 17.650 -9.656  8.060  1.00 55.63 ? 243 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   ALA 7   6   6   ALA ALA A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  ?   ?   ?   A . n 
A 1 70  ARG 70  69  ?   ?   ?   A . n 
A 1 71  LYS 71  70  ?   ?   ?   A . n 
A 1 72  HIS 72  71  ?   ?   ?   A . n 
A 1 73  GLY 73  72  ?   ?   ?   A . n 
A 1 74  GLY 74  73  ?   ?   ?   A . n 
A 1 75  PRO 75  74  ?   ?   ?   A . n 
A 1 76  LYS 76  75  ?   ?   ?   A . n 
A 1 77  ASP 77  76  ?   ?   ?   A . n 
A 1 78  GLU 78  77  ?   ?   ?   A . n 
A 1 79  GLU 79  78  ?   ?   ?   A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  SER 81  80  80  SER SER A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  SER 84  83  83  SER SER A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 ?   ?   ?   A . n 
A 1 134 GLU 134 133 ?   ?   ?   A . n 
A 1 135 SER 135 134 ?   ?   ?   A . n 
A 1 136 THR 136 135 ?   ?   ?   A . n 
A 1 137 LYS 137 136 ?   ?   ?   A . n 
A 1 138 THR 138 137 ?   ?   ?   A . n 
A 1 139 GLY 139 138 ?   ?   ?   A . n 
A 1 140 ASN 140 139 ?   ?   ?   A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   ALA 7   6   6   ALA ALA B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  ?   ?   ?   B . n 
B 1 70  ARG 70  69  ?   ?   ?   B . n 
B 1 71  LYS 71  70  ?   ?   ?   B . n 
B 1 72  HIS 72  71  ?   ?   ?   B . n 
B 1 73  GLY 73  72  ?   ?   ?   B . n 
B 1 74  GLY 74  73  ?   ?   ?   B . n 
B 1 75  PRO 75  74  ?   ?   ?   B . n 
B 1 76  LYS 76  75  ?   ?   ?   B . n 
B 1 77  ASP 77  76  ?   ?   ?   B . n 
B 1 78  GLU 78  77  ?   ?   ?   B . n 
B 1 79  GLU 79  78  ?   ?   ?   B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  SER 81  80  80  SER SER B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  SER 84  83  83  SER SER B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 SER 112 111 111 SER SER B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 ?   ?   ?   B . n 
B 1 134 GLU 134 133 ?   ?   ?   B . n 
B 1 135 SER 135 134 ?   ?   ?   B . n 
B 1 136 THR 136 135 ?   ?   ?   B . n 
B 1 137 LYS 137 136 ?   ?   ?   B . n 
B 1 138 THR 138 137 ?   ?   ?   B . n 
B 1 139 GLY 139 138 ?   ?   ?   B . n 
B 1 140 ASN 140 139 ?   ?   ?   B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU  1   154 154 CU  CU  A . 
D 2 CU  1   154 154 CU  CU  B . 
E 3 HOH 1   155 1   HOH HOH A . 
E 3 HOH 2   156 2   HOH HOH A . 
E 3 HOH 3   157 3   HOH HOH A . 
E 3 HOH 4   158 4   HOH HOH A . 
E 3 HOH 5   159 8   HOH HOH A . 
E 3 HOH 6   160 9   HOH HOH A . 
E 3 HOH 7   161 10  HOH HOH A . 
E 3 HOH 8   162 11  HOH HOH A . 
E 3 HOH 9   163 12  HOH HOH A . 
E 3 HOH 10  164 14  HOH HOH A . 
E 3 HOH 11  165 15  HOH HOH A . 
E 3 HOH 12  166 17  HOH HOH A . 
E 3 HOH 13  167 19  HOH HOH A . 
E 3 HOH 14  168 20  HOH HOH A . 
E 3 HOH 15  169 21  HOH HOH A . 
E 3 HOH 16  170 22  HOH HOH A . 
E 3 HOH 17  171 25  HOH HOH A . 
E 3 HOH 18  172 28  HOH HOH A . 
E 3 HOH 19  173 29  HOH HOH A . 
E 3 HOH 20  174 30  HOH HOH A . 
E 3 HOH 21  175 33  HOH HOH A . 
E 3 HOH 22  176 34  HOH HOH A . 
E 3 HOH 23  177 36  HOH HOH A . 
E 3 HOH 24  178 40  HOH HOH A . 
E 3 HOH 25  179 41  HOH HOH A . 
E 3 HOH 26  180 42  HOH HOH A . 
E 3 HOH 27  181 43  HOH HOH A . 
E 3 HOH 28  182 47  HOH HOH A . 
E 3 HOH 29  183 49  HOH HOH A . 
E 3 HOH 30  184 50  HOH HOH A . 
E 3 HOH 31  185 52  HOH HOH A . 
E 3 HOH 32  186 53  HOH HOH A . 
E 3 HOH 33  187 54  HOH HOH A . 
E 3 HOH 34  188 55  HOH HOH A . 
E 3 HOH 35  189 57  HOH HOH A . 
E 3 HOH 36  190 58  HOH HOH A . 
E 3 HOH 37  191 62  HOH HOH A . 
E 3 HOH 38  192 69  HOH HOH A . 
E 3 HOH 39  193 70  HOH HOH A . 
E 3 HOH 40  194 72  HOH HOH A . 
E 3 HOH 41  195 73  HOH HOH A . 
E 3 HOH 42  196 75  HOH HOH A . 
E 3 HOH 43  197 78  HOH HOH A . 
E 3 HOH 44  198 79  HOH HOH A . 
E 3 HOH 45  199 80  HOH HOH A . 
E 3 HOH 46  200 82  HOH HOH A . 
E 3 HOH 47  201 83  HOH HOH A . 
E 3 HOH 48  202 84  HOH HOH A . 
E 3 HOH 49  203 85  HOH HOH A . 
E 3 HOH 50  204 86  HOH HOH A . 
E 3 HOH 51  205 87  HOH HOH A . 
E 3 HOH 52  206 90  HOH HOH A . 
E 3 HOH 53  207 91  HOH HOH A . 
E 3 HOH 54  208 92  HOH HOH A . 
E 3 HOH 55  209 95  HOH HOH A . 
E 3 HOH 56  210 97  HOH HOH A . 
E 3 HOH 57  211 99  HOH HOH A . 
E 3 HOH 58  212 100 HOH HOH A . 
E 3 HOH 59  213 104 HOH HOH A . 
E 3 HOH 60  214 106 HOH HOH A . 
E 3 HOH 61  215 107 HOH HOH A . 
E 3 HOH 62  216 109 HOH HOH A . 
E 3 HOH 63  217 112 HOH HOH A . 
E 3 HOH 64  218 114 HOH HOH A . 
E 3 HOH 65  219 115 HOH HOH A . 
E 3 HOH 66  220 119 HOH HOH A . 
E 3 HOH 67  221 120 HOH HOH A . 
E 3 HOH 68  222 124 HOH HOH A . 
E 3 HOH 69  223 125 HOH HOH A . 
E 3 HOH 70  224 127 HOH HOH A . 
E 3 HOH 71  225 132 HOH HOH A . 
E 3 HOH 72  226 134 HOH HOH A . 
E 3 HOH 73  227 135 HOH HOH A . 
E 3 HOH 74  228 136 HOH HOH A . 
E 3 HOH 75  229 137 HOH HOH A . 
E 3 HOH 76  230 141 HOH HOH A . 
E 3 HOH 77  231 143 HOH HOH A . 
E 3 HOH 78  232 144 HOH HOH A . 
E 3 HOH 79  233 147 HOH HOH A . 
E 3 HOH 80  234 148 HOH HOH A . 
E 3 HOH 81  235 152 HOH HOH A . 
E 3 HOH 82  236 153 HOH HOH A . 
E 3 HOH 83  237 156 HOH HOH A . 
E 3 HOH 84  238 157 HOH HOH A . 
E 3 HOH 85  239 158 HOH HOH A . 
E 3 HOH 86  240 159 HOH HOH A . 
E 3 HOH 87  241 161 HOH HOH A . 
E 3 HOH 88  242 162 HOH HOH A . 
E 3 HOH 89  243 165 HOH HOH A . 
E 3 HOH 90  244 166 HOH HOH A . 
E 3 HOH 91  245 168 HOH HOH A . 
E 3 HOH 92  246 176 HOH HOH A . 
E 3 HOH 93  247 177 HOH HOH A . 
E 3 HOH 94  248 178 HOH HOH A . 
E 3 HOH 95  249 179 HOH HOH A . 
E 3 HOH 96  250 180 HOH HOH A . 
E 3 HOH 97  251 186 HOH HOH A . 
E 3 HOH 98  252 189 HOH HOH A . 
E 3 HOH 99  253 190 HOH HOH A . 
E 3 HOH 100 254 26  HOH HOH A . 
E 3 HOH 101 255 66  HOH HOH A . 
F 3 HOH 1   155 61  HOH HOH B . 
F 3 HOH 2   156 5   HOH HOH B . 
F 3 HOH 3   157 6   HOH HOH B . 
F 3 HOH 4   158 7   HOH HOH B . 
F 3 HOH 5   159 13  HOH HOH B . 
F 3 HOH 6   160 16  HOH HOH B . 
F 3 HOH 7   161 18  HOH HOH B . 
F 3 HOH 8   162 23  HOH HOH B . 
F 3 HOH 9   163 24  HOH HOH B . 
F 3 HOH 10  164 27  HOH HOH B . 
F 3 HOH 11  165 31  HOH HOH B . 
F 3 HOH 12  166 32  HOH HOH B . 
F 3 HOH 13  167 35  HOH HOH B . 
F 3 HOH 14  168 37  HOH HOH B . 
F 3 HOH 15  169 38  HOH HOH B . 
F 3 HOH 16  170 39  HOH HOH B . 
F 3 HOH 17  171 44  HOH HOH B . 
F 3 HOH 18  172 45  HOH HOH B . 
F 3 HOH 19  173 46  HOH HOH B . 
F 3 HOH 20  174 48  HOH HOH B . 
F 3 HOH 21  175 51  HOH HOH B . 
F 3 HOH 22  176 56  HOH HOH B . 
F 3 HOH 23  177 59  HOH HOH B . 
F 3 HOH 24  178 60  HOH HOH B . 
F 3 HOH 25  179 63  HOH HOH B . 
F 3 HOH 26  180 64  HOH HOH B . 
F 3 HOH 27  181 65  HOH HOH B . 
F 3 HOH 28  182 67  HOH HOH B . 
F 3 HOH 29  183 68  HOH HOH B . 
F 3 HOH 30  184 71  HOH HOH B . 
F 3 HOH 31  185 74  HOH HOH B . 
F 3 HOH 32  186 76  HOH HOH B . 
F 3 HOH 33  187 77  HOH HOH B . 
F 3 HOH 34  188 81  HOH HOH B . 
F 3 HOH 35  189 88  HOH HOH B . 
F 3 HOH 36  190 89  HOH HOH B . 
F 3 HOH 37  191 93  HOH HOH B . 
F 3 HOH 38  192 94  HOH HOH B . 
F 3 HOH 39  193 96  HOH HOH B . 
F 3 HOH 40  194 98  HOH HOH B . 
F 3 HOH 41  195 101 HOH HOH B . 
F 3 HOH 42  196 102 HOH HOH B . 
F 3 HOH 43  197 103 HOH HOH B . 
F 3 HOH 44  198 105 HOH HOH B . 
F 3 HOH 45  199 108 HOH HOH B . 
F 3 HOH 46  200 110 HOH HOH B . 
F 3 HOH 47  201 111 HOH HOH B . 
F 3 HOH 48  202 113 HOH HOH B . 
F 3 HOH 49  203 116 HOH HOH B . 
F 3 HOH 50  204 117 HOH HOH B . 
F 3 HOH 51  205 118 HOH HOH B . 
F 3 HOH 52  206 121 HOH HOH B . 
F 3 HOH 53  207 122 HOH HOH B . 
F 3 HOH 54  208 123 HOH HOH B . 
F 3 HOH 55  209 126 HOH HOH B . 
F 3 HOH 56  210 128 HOH HOH B . 
F 3 HOH 57  211 129 HOH HOH B . 
F 3 HOH 58  212 130 HOH HOH B . 
F 3 HOH 59  213 131 HOH HOH B . 
F 3 HOH 60  214 133 HOH HOH B . 
F 3 HOH 61  215 138 HOH HOH B . 
F 3 HOH 62  216 139 HOH HOH B . 
F 3 HOH 63  217 140 HOH HOH B . 
F 3 HOH 64  218 142 HOH HOH B . 
F 3 HOH 65  219 145 HOH HOH B . 
F 3 HOH 66  220 146 HOH HOH B . 
F 3 HOH 67  221 149 HOH HOH B . 
F 3 HOH 68  222 150 HOH HOH B . 
F 3 HOH 69  223 151 HOH HOH B . 
F 3 HOH 70  224 154 HOH HOH B . 
F 3 HOH 71  225 155 HOH HOH B . 
F 3 HOH 72  226 160 HOH HOH B . 
F 3 HOH 73  227 163 HOH HOH B . 
F 3 HOH 74  228 164 HOH HOH B . 
F 3 HOH 75  229 167 HOH HOH B . 
F 3 HOH 76  230 169 HOH HOH B . 
F 3 HOH 77  231 170 HOH HOH B . 
F 3 HOH 78  232 171 HOH HOH B . 
F 3 HOH 79  233 172 HOH HOH B . 
F 3 HOH 80  234 173 HOH HOH B . 
F 3 HOH 81  235 174 HOH HOH B . 
F 3 HOH 82  236 175 HOH HOH B . 
F 3 HOH 83  237 181 HOH HOH B . 
F 3 HOH 84  238 182 HOH HOH B . 
F 3 HOH 85  239 183 HOH HOH B . 
F 3 HOH 86  240 184 HOH HOH B . 
F 3 HOH 87  241 185 HOH HOH B . 
F 3 HOH 88  242 187 HOH HOH B . 
F 3 HOH 89  243 188 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 
# 
_pdbx_struct_assembly_prop.biol_id   1 
_pdbx_struct_assembly_prop.type      'ABSA (A^2)' 
_pdbx_struct_assembly_prop.value     1540 
_pdbx_struct_assembly_prop.details   ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU A C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 49  ? A HIS 48  ? 1_555 141.4 ? 
2 ND1 ? A HIS 47 ? A HIS 46 ? 1_555 CU A C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 97.9  ? 
3 NE2 ? A HIS 49 ? A HIS 48 ? 1_555 CU A C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 110.3 ? 
4 NE2 ? A HIS 49 ? A HIS 48 ? 1_555 CU B C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 121 ? A HIS 120 ? 1_555 102.8 ? 
5 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? D CU . ? B CU 154 ? 1_555 NE2 ? B HIS 49  ? B HIS 48  ? 1_555 141.6 ? 
6 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 CU ? D CU . ? B CU 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 99.7  ? 
7 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 CU ? D CU . ? B CU 154 ? 1_555 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 107.9 ? 
# 
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 2007-12-11 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2021-10-20 
# 
_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' 'Atomic model'              
2 2 'Structure model' 'Version format compliance' 
3 3 'Structure model' 'Database references'       
4 3 '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 3 'Structure model' database_2             
2 3 'Structure model' pdbx_struct_conn_angle 
3 3 'Structure model' struct_conn            
4 3 'Structure model' struct_ref_seq_dif     
# 
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  3 'Structure model' '_database_2.pdbx_DOI'                        
2  3 'Structure model' '_database_2.pdbx_database_accession'         
3  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
4  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_alt_id'  
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 3 'Structure model' '_pdbx_struct_conn_angle.value'               
16 3 'Structure model' '_struct_conn.pdbx_dist_value'                
17 3 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
18 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
19 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
23 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
24 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
25 3 'Structure model' '_struct_ref_seq_dif.details'                 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345dtb 'data collection' . ? 1 
CNS       refinement        . ? 2 
DENZO     'data reduction'  . ? 3 
SCALEPACK 'data scaling'    . ? 4 
CNS       phasing           . ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 162 ? ? O A HOH 180 ? ? 2.04 
2 1 O A HOH 182 ? ? O B HOH 202 ? ? 2.16 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             146 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            SG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             146 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.688 
_pdbx_validate_rmsd_bond.bond_target_value         1.812 
_pdbx_validate_rmsd_bond.bond_deviation            -0.124 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              146 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              146 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              146 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                123.27 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            9.07 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 25 ? ? -40.00  -31.84 
2 1 ASN B 65 ? ? -166.49 95.16  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B ARG 79 ? CG  ? B ARG 80 CG  
2 1 Y 1 B ARG 79 ? CD  ? B ARG 80 CD  
3 1 Y 1 B ARG 79 ? NE  ? B ARG 80 NE  
4 1 Y 1 B ARG 79 ? CZ  ? B ARG 80 CZ  
5 1 Y 1 B ARG 79 ? NH1 ? B ARG 80 NH1 
6 1 Y 1 B ARG 79 ? NH2 ? B ARG 80 NH2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0   ? A MET 1   
2  1 Y 1 A SER 68  ? A SER 69  
3  1 Y 1 A ARG 69  ? A ARG 70  
4  1 Y 1 A LYS 70  ? A LYS 71  
5  1 Y 1 A HIS 71  ? A HIS 72  
6  1 Y 1 A GLY 72  ? A GLY 73  
7  1 Y 1 A GLY 73  ? A GLY 74  
8  1 Y 1 A PRO 74  ? A PRO 75  
9  1 Y 1 A LYS 75  ? A LYS 76  
10 1 Y 1 A ASP 76  ? A ASP 77  
11 1 Y 1 A GLU 77  ? A GLU 78  
12 1 Y 1 A GLU 78  ? A GLU 79  
13 1 Y 1 A GLU 132 ? A GLU 133 
14 1 Y 1 A GLU 133 ? A GLU 134 
15 1 Y 1 A SER 134 ? A SER 135 
16 1 Y 1 A THR 135 ? A THR 136 
17 1 Y 1 A LYS 136 ? A LYS 137 
18 1 Y 1 A THR 137 ? A THR 138 
19 1 Y 1 A GLY 138 ? A GLY 139 
20 1 Y 1 A ASN 139 ? A ASN 140 
21 1 Y 1 B MET 0   ? B MET 1   
22 1 Y 1 B SER 68  ? B SER 69  
23 1 Y 1 B ARG 69  ? B ARG 70  
24 1 Y 1 B LYS 70  ? B LYS 71  
25 1 Y 1 B HIS 71  ? B HIS 72  
26 1 Y 1 B GLY 72  ? B GLY 73  
27 1 Y 1 B GLY 73  ? B GLY 74  
28 1 Y 1 B PRO 74  ? B PRO 75  
29 1 Y 1 B LYS 75  ? B LYS 76  
30 1 Y 1 B ASP 76  ? B ASP 77  
31 1 Y 1 B GLU 77  ? B GLU 78  
32 1 Y 1 B GLU 78  ? B GLU 79  
33 1 Y 1 B GLU 132 ? B GLU 133 
34 1 Y 1 B GLU 133 ? B GLU 134 
35 1 Y 1 B SER 134 ? B SER 135 
36 1 Y 1 B THR 135 ? B THR 136 
37 1 Y 1 B LYS 136 ? B LYS 137 
38 1 Y 1 B THR 137 ? B THR 138 
39 1 Y 1 B GLY 138 ? B GLY 139 
40 1 Y 1 B ASN 139 ? B ASN 140 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 water             HOH 
# 
