data_3K91
# 
_entry.id   3K91 
# 
_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   3K91         pdb_00003k91 10.2210/pdb3k91/pdb 
RCSB  RCSB055698   ?            ?                   
WWPDB D_1000055698 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3GQF . unspecified 
PDB 2NNX . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3K91 
_pdbx_database_status.recvd_initial_deposition_date   2009-10-15 
_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.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'You, Z.'      1 
'Cao, X.'      2 
'Taylor, A.B.' 3 
'Hart, P.J.'   4 
'Levine, R.L.' 5 
# 
_citation.id                        primary 
_citation.title                     'Characterization of a covalent polysulfane bridge in copper-zinc superoxide dismutase .' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            49 
_citation.page_first                1191 
_citation.page_last                 1198 
_citation.year                      2010 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20052996 
_citation.pdbx_database_id_DOI      10.1021/bi901844d 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'You, Z.'      1 ? 
primary 'Cao, X.'      2 ? 
primary 'Taylor, A.B.' 3 ? 
primary 'Hart, P.J.'   4 ? 
primary 'Levine, R.L.' 5 ? 
# 
_cell.entry_id           3K91 
_cell.length_a           40.049 
_cell.length_b           57.925 
_cell.length_c           104.988 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_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                         3K91 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_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]' 15836.590 2   1.15.1.1 'H46R, H48Q' ? ? 
2 non-polymer syn PENTASULFIDE-SULFUR            160.325   1   ?        ?            ? ? 
3 water       nat water                          18.015    255 ?        ?            ? ? 
# 
_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       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFRVQEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFRVQEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  ARG n 
1 47  VAL n 
1 48  GLN n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_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      'Saccharomyces Cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     ? 
_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               EG118 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       YEP351 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_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 3K91 A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 3K91 B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3K91 ARG A 46 ? UNP P00441 HIS 47 'engineered mutation' 46 1 
1 3K91 GLN A 48 ? UNP P00441 HIS 49 'engineered mutation' 48 2 
2 3K91 ARG B 46 ? UNP P00441 HIS 47 'engineered mutation' 46 3 
2 3K91 GLN B 48 ? UNP P00441 HIS 49 'engineered mutation' 48 4 
# 
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 
CYS 'L-peptide linking' y CYSTEINE            ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE           ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'     ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE             ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE           ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER               ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE          ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE             ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE              ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE       ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE             ? 'C5 H9 N O2'     115.130 
PS5 non-polymer         . PENTASULFIDE-SULFUR ? 'S5 -2'          160.325 
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          3K91 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.92 
_exptl_crystal.density_percent_sol   36.02 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pdbx_details    
;0.17 M ammonium sulfate, 0.085 M sodium acetate, 25.5% PEG 4000, 15% glycerol, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K
;
_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               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS HTC' 
_diffrn_detector.pdbx_collection_date   2007-04-20 
_diffrn_detector.details                mirrors 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'confocal optics' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
# 
_reflns.entry_id                     3K91 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             27.92 
_reflns.d_resolution_high            1.75 
_reflns.number_obs                   24379 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         95.8 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.059 
_reflns.pdbx_netI_over_sigmaI        15.8 
_reflns.B_iso_Wilson_estimate        19.9 
_reflns.pdbx_redundancy              2.8 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.75 
_reflns_shell.d_res_low              1.81 
_reflns_shell.percent_possible_all   94.9 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.351 
_reflns_shell.meanI_over_sigI_obs    3.0 
_reflns_shell.pdbx_redundancy        2.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2384 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3K91 
_refine.ls_number_reflns_obs                     24337 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             27.92 
_refine.ls_d_res_high                            1.75 
_refine.ls_percent_reflns_obs                    95.69 
_refine.ls_R_factor_obs                          0.1892 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1876 
_refine.ls_R_factor_R_free                       0.2183 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_number_reflns_R_free                  1248 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               25.7 
_refine.aniso_B[1][1]                            -3.5794 
_refine.aniso_B[2][2]                            12.2064 
_refine.aniso_B[3][3]                            -7.7542 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.369 
_refine.solvent_model_param_bsol                 38.892 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1OZU 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.16 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.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_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        1999 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.number_atoms_solvent             255 
_refine_hist.number_atoms_total               2259 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        27.92 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.010  ? ? 2054 'X-RAY DIFFRACTION' ? 
f_angle_d          0.925  ? ? 2771 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 15.023 ? ? 738  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.058  ? ? 315  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 369  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 1.75   1.8186 2462 0.2506 93.00 0.2810 . . 131 . . . . 'X-RAY DIFFRACTION' 
. 1.8186 1.9014 2516 0.2128 96.00 0.2907 . . 146 . . . . 'X-RAY DIFFRACTION' 
. 1.9014 2.0016 2540 0.1977 96.00 0.2022 . . 141 . . . . 'X-RAY DIFFRACTION' 
. 2.0016 2.1270 2542 0.1647 97.00 0.2327 . . 134 . . . . 'X-RAY DIFFRACTION' 
. 2.1270 2.2911 2562 0.1797 96.00 0.2279 . . 131 . . . . 'X-RAY DIFFRACTION' 
. 2.2911 2.5215 2583 0.1923 96.00 0.2556 . . 140 . . . . 'X-RAY DIFFRACTION' 
. 2.5215 2.8861 2566 0.1977 96.00 0.2165 . . 139 . . . . 'X-RAY DIFFRACTION' 
. 2.8861 3.6349 2619 0.1728 96.00 0.2168 . . 143 . . . . 'X-RAY DIFFRACTION' 
. 3.6349 27.92  2699 0.1761 95.00 0.1771 . . 143 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3K91 
_struct.title                     'Polysulfane Bridge in Cu-Zn Superoxide Dismutase' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3K91 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;human cu-zn superoxide dismutase, amyotrophic lateral sclerosis, antioxidant, oxidoreductase, sulfur, polysulfane, Disease mutation, Disulfide bond, Metal-binding, Neurodegeneration, Phosphoprotein
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 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 55  ? ALA A 60  ? ALA A 55  ALA A 60  5 ? 6 
HELX_P HELX_P2 2 ALA B 55  ? ALA B 60  ? ALA B 55  ALA B 60  5 ? 6 
HELX_P HELX_P3 3 SER B 107 ? CYS B 111 ? SER B 107 CYS B 111 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 57 SG ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf2 disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 150 ? ILE A 151 ? GLY A 150 ILE A 151 
A 2  THR A 2   ? GLY A 10  ? THR A 2   GLY A 10  
A 3  ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
A 4  THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
A 5  GLY A 41  ? GLN A 48  ? GLY A 41  GLN A 48  
A 6  ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
A 7  ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 8  VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 9  GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 10 THR A 2   ? GLY A 10  ? THR A 2   GLY A 10  
B 1  ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
B 2  VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
B 3  GLN B 15  ? GLU B 21  ? GLN B 15  GLU B 21  
B 4  LYS B 3   ? LEU B 8   ? LYS B 3   LEU B 8   
B 5  GLY B 150 ? GLN B 153 ? GLY B 150 GLN B 153 
C 1  ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
C 2  GLY B 41  ? GLN B 48  ? GLY B 41  GLN B 48  
C 3  THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
C 4  ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  O GLY A 150 ? O GLY A 150 N VAL A 5   ? N VAL A 5   
A 2 3  N LYS A 9   ? N LYS A 9   O CYS A 146 ? O CYS A 146 
A 3 4  O GLY A 147 ? O GLY A 147 N LEU A 117 ? N LEU A 117 
A 4 5  O THR A 116 ? O THR A 116 N GLN A 48  ? N GLN A 48  
A 5 6  N GLY A 41  ? N GLY A 41  O ALA A 89  ? O ALA A 89  
A 6 7  N THR A 88  ? N THR A 88  O ASP A 96  ? O ASP A 96  
A 7 8  O ILE A 99  ? O ILE A 99  N VAL A 31  ? N VAL A 31  
A 8 9  O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 9 10 O GLN A 22  ? O GLN A 22  N THR A 2   ? N THR A 2   
B 1 2  O ALA B 95  ? O ALA B 95  N ILE B 35  ? N ILE B 35  
B 2 3  O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
B 3 4  O PHE B 20  ? O PHE B 20  N ALA B 4   ? N ALA B 4   
B 4 5  N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
C 1 2  O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
C 2 3  N GLN B 48  ? N GLN B 48  O THR B 116 ? O THR B 116 
C 3 4  N LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_struct_site.pdbx_auth_asym_id    A 
_struct_site.pdbx_auth_comp_id    PS5 
_struct_site.pdbx_auth_seq_id     154 
_struct_site.pdbx_auth_ins_code   ? 
_struct_site.pdbx_num_residues    4 
_struct_site.details              'BINDING SITE FOR RESIDUE PS5 A 154' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1 AC1 4 LEU A 106 ? LEU A 106 . ? 1_555 ? 
2 AC1 4 CYS A 111 ? CYS A 111 . ? 1_555 ? 
3 AC1 4 CYS B 111 ? CYS B 111 . ? 1_555 ? 
4 AC1 4 HOH E .   ? HOH B 181 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3K91 
_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                    3K91 
_atom_sites.fract_transf_matrix[1][1]   0.024969 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017264 
_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]   0.009525 
_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 
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 1   ? 13.336  18.712  -16.433 1.00 45.81 ? 1   ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 12.292  19.720  -16.289 1.00 36.96 ? 1   ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 10.920  19.080  -16.101 1.00 33.03 ? 1   ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? 10.608  18.058  -16.714 1.00 39.53 ? 1   ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 12.284  20.657  -17.490 1.00 32.91 ? 1   ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? 10.103  19.687  -15.249 1.00 31.58 ? 2   THR A N   1 
ATOM   7    C CA  . THR A 1 2   ? 8.753   19.196  -15.020 1.00 22.10 ? 2   THR A CA  1 
ATOM   8    C C   . THR A 1 2   ? 7.818   19.801  -16.062 1.00 25.71 ? 2   THR A C   1 
ATOM   9    O O   . THR A 1 2   ? 7.944   20.974  -16.419 1.00 19.04 ? 2   THR A O   1 
ATOM   10   C CB  . THR A 1 2   ? 8.263   19.523  -13.597 1.00 31.56 ? 2   THR A CB  1 
ATOM   11   O OG1 . THR A 1 2   ? 9.221   19.043  -12.645 1.00 37.27 ? 2   THR A OG1 1 
ATOM   12   C CG2 . THR A 1 2   ? 6.925   18.863  -13.324 1.00 31.79 ? 2   THR A CG2 1 
ATOM   13   N N   . LYS A 1 3   ? 6.899   18.986  -16.564 1.00 17.86 ? 3   LYS A N   1 
ATOM   14   C CA  . LYS A 1 3   ? 5.934   19.434  -17.555 1.00 13.65 ? 3   LYS A CA  1 
ATOM   15   C C   . LYS A 1 3   ? 4.536   18.980  -17.167 1.00 19.18 ? 3   LYS A C   1 
ATOM   16   O O   . LYS A 1 3   ? 4.363   17.931  -16.549 1.00 15.98 ? 3   LYS A O   1 
ATOM   17   C CB  . LYS A 1 3   ? 6.283   18.879  -18.933 1.00 23.93 ? 3   LYS A CB  1 
ATOM   18   C CG  . LYS A 1 3   ? 7.619   19.360  -19.460 1.00 22.39 ? 3   LYS A CG  1 
ATOM   19   C CD  . LYS A 1 3   ? 7.915   18.778  -20.830 1.00 32.36 ? 3   LYS A CD  1 
ATOM   20   C CE  . LYS A 1 3   ? 6.915   19.262  -21.862 1.00 37.57 ? 3   LYS A CE  1 
ATOM   21   N NZ  . LYS A 1 3   ? 7.297   18.860  -23.246 1.00 45.72 ? 3   LYS A NZ  1 
ATOM   22   N N   . ALA A 1 4   ? 3.543   19.771  -17.552 1.00 15.99 ? 4   ALA A N   1 
ATOM   23   C CA  . ALA A 1 4   ? 2.147   19.436  -17.293 1.00 12.17 ? 4   ALA A CA  1 
ATOM   24   C C   . ALA A 1 4   ? 1.277   19.895  -18.462 1.00 15.33 ? 4   ALA A C   1 
ATOM   25   O O   . ALA A 1 4   ? 1.731   20.627  -19.341 1.00 14.17 ? 4   ALA A O   1 
ATOM   26   C CB  . ALA A 1 4   ? 1.683   20.077  -15.996 1.00 15.12 ? 4   ALA A CB  1 
ATOM   27   N N   . VAL A 1 5   ? 0.022   19.468  -18.463 1.00 14.25 ? 5   VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? -0.882  19.812  -19.550 1.00 11.33 ? 5   VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? -2.316  19.778  -19.035 1.00 15.48 ? 5   VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? -2.619  19.098  -18.054 1.00 12.77 ? 5   VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? -0.698  18.848  -20.739 1.00 14.45 ? 5   VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? -1.168  17.450  -20.370 1.00 18.23 ? 5   VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? -1.428  19.362  -21.981 1.00 15.85 ? 5   VAL A CG2 1 
ATOM   34   N N   . CYS A 1 6   ? -3.191  20.532  -19.686 1.00 11.02 ? 6   CYS A N   1 
ATOM   35   C CA  . CYS A 1 6   ? -4.581  20.614  -19.267 1.00 13.91 ? 6   CYS A CA  1 
ATOM   36   C C   . CYS A 1 6   ? -5.463  20.760  -20.490 1.00 17.49 ? 6   CYS A C   1 
ATOM   37   O O   . CYS A 1 6   ? -5.207  21.601  -21.351 1.00 15.37 ? 6   CYS A O   1 
ATOM   38   C CB  . CYS A 1 6   ? -4.799  21.816  -18.350 1.00 12.72 ? 6   CYS A CB  1 
ATOM   39   S SG  . CYS A 1 6   ? -6.495  21.924  -17.730 1.00 16.79 ? 6   CYS A SG  1 
ATOM   40   N N   . VAL A 1 7   ? -6.496  19.932  -20.565 1.00 13.11 ? 7   VAL A N   1 
ATOM   41   C CA  . VAL A 1 7   ? -7.481  20.048  -21.630 1.00 14.28 ? 7   VAL A CA  1 
ATOM   42   C C   . VAL A 1 7   ? -8.703  20.756  -21.053 1.00 16.01 ? 7   VAL A C   1 
ATOM   43   O O   . VAL A 1 7   ? -9.333  20.265  -20.114 1.00 12.59 ? 7   VAL A O   1 
ATOM   44   C CB  . VAL A 1 7   ? -7.896  18.662  -22.166 1.00 16.64 ? 7   VAL A CB  1 
ATOM   45   C CG1 . VAL A 1 7   ? -9.001  18.800  -23.212 1.00 17.91 ? 7   VAL A CG1 1 
ATOM   46   C CG2 . VAL A 1 7   ? -6.690  17.928  -22.732 1.00 19.55 ? 7   VAL A CG2 1 
ATOM   47   N N   . LEU A 1 8   ? -9.014  21.927  -21.596 1.00 16.56 ? 8   LEU A N   1 
ATOM   48   C CA  . LEU A 1 8   ? -10.152 22.709  -21.143 1.00 17.15 ? 8   LEU A CA  1 
ATOM   49   C C   . LEU A 1 8   ? -11.397 22.316  -21.926 1.00 18.23 ? 8   LEU A C   1 
ATOM   50   O O   . LEU A 1 8   ? -11.396 22.356  -23.154 1.00 17.13 ? 8   LEU A O   1 
ATOM   51   C CB  . LEU A 1 8   ? -9.878  24.203  -21.337 1.00 14.68 ? 8   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 8   ? -8.734  24.820  -20.532 1.00 20.00 ? 8   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 8   ? -8.511  26.278  -20.930 1.00 20.04 ? 8   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 8   ? -9.024  24.713  -19.056 1.00 17.84 ? 8   LEU A CD2 1 
ATOM   55   N N   . LYS A 1 9   ? -12.453 21.937  -21.212 1.00 19.69 ? 9   LYS A N   1 
ATOM   56   C CA  . LYS A 1 9   ? -13.726 21.609  -21.846 1.00 27.62 ? 9   LYS A CA  1 
ATOM   57   C C   . LYS A 1 9   ? -14.876 22.246  -21.079 1.00 22.13 ? 9   LYS A C   1 
ATOM   58   O O   . LYS A 1 9   ? -14.809 22.400  -19.864 1.00 21.55 ? 9   LYS A O   1 
ATOM   59   C CB  . LYS A 1 9   ? -13.924 20.095  -21.918 1.00 27.97 ? 9   LYS A CB  1 
ATOM   60   C CG  . LYS A 1 9   ? -12.949 19.375  -22.832 1.00 29.72 ? 9   LYS A CG  1 
ATOM   61   C CD  . LYS A 1 9   ? -13.310 17.901  -22.953 1.00 37.33 ? 9   LYS A CD  1 
ATOM   62   C CE  . LYS A 1 9   ? -12.326 17.161  -23.843 1.00 36.79 ? 9   LYS A CE  1 
ATOM   63   N NZ  . LYS A 1 9   ? -12.287 17.716  -25.225 1.00 49.55 ? 9   LYS A NZ  1 
ATOM   64   N N   . GLY A 1 10  ? -15.934 22.607  -21.797 1.00 20.39 ? 10  GLY A N   1 
ATOM   65   C CA  . GLY A 1 10  ? -17.086 23.245  -21.190 1.00 24.47 ? 10  GLY A CA  1 
ATOM   66   C C   . GLY A 1 10  ? -18.391 22.704  -21.733 1.00 32.07 ? 10  GLY A C   1 
ATOM   67   O O   . GLY A 1 10  ? -18.425 21.626  -22.326 1.00 33.89 ? 10  GLY A O   1 
ATOM   68   N N   . ASP A 1 11  ? -19.469 23.453  -21.527 1.00 38.23 ? 11  ASP A N   1 
ATOM   69   C CA  . ASP A 1 11  ? -20.790 23.044  -21.993 1.00 42.53 ? 11  ASP A CA  1 
ATOM   70   C C   . ASP A 1 11  ? -21.147 23.672  -23.333 1.00 41.19 ? 11  ASP A C   1 
ATOM   71   O O   . ASP A 1 11  ? -22.272 23.531  -23.812 1.00 50.30 ? 11  ASP A O   1 
ATOM   72   C CB  . ASP A 1 11  ? -21.861 23.388  -20.956 1.00 39.05 ? 11  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 11  ? -22.016 22.311  -19.904 1.00 53.64 ? 11  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 11  ? -21.335 21.268  -20.020 1.00 43.44 ? 11  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 11  ? -22.818 22.503  -18.966 1.00 60.20 ? 11  ASP A OD2 1 
ATOM   76   N N   . GLY A 1 12  ? -20.187 24.365  -23.936 1.00 31.74 ? 12  GLY A N   1 
ATOM   77   C CA  . GLY A 1 12  ? -20.400 24.979  -25.233 1.00 36.99 ? 12  GLY A CA  1 
ATOM   78   C C   . GLY A 1 12  ? -19.235 24.783  -26.187 1.00 31.75 ? 12  GLY A C   1 
ATOM   79   O O   . GLY A 1 12  ? -18.615 23.718  -26.208 1.00 26.25 ? 12  GLY A O   1 
ATOM   80   N N   . PRO A 1 13  ? -18.926 25.822  -26.977 1.00 27.68 ? 13  PRO A N   1 
ATOM   81   C CA  . PRO A 1 13  ? -17.908 25.803  -28.033 1.00 23.51 ? 13  PRO A CA  1 
ATOM   82   C C   . PRO A 1 13  ? -16.497 25.929  -27.475 1.00 20.35 ? 13  PRO A C   1 
ATOM   83   O O   . PRO A 1 13  ? -15.530 25.636  -28.181 1.00 20.42 ? 13  PRO A O   1 
ATOM   84   C CB  . PRO A 1 13  ? -18.227 27.062  -28.855 1.00 24.06 ? 13  PRO A CB  1 
ATOM   85   C CG  . PRO A 1 13  ? -19.451 27.669  -28.237 1.00 30.43 ? 13  PRO A CG  1 
ATOM   86   C CD  . PRO A 1 13  ? -19.551 27.146  -26.856 1.00 31.00 ? 13  PRO A CD  1 
ATOM   87   N N   . VAL A 1 14  ? -16.391 26.366  -26.224 1.00 20.56 ? 14  VAL A N   1 
ATOM   88   C CA  . VAL A 1 14  ? -15.090 26.655  -25.622 1.00 20.46 ? 14  VAL A CA  1 
ATOM   89   C C   . VAL A 1 14  ? -14.281 25.389  -25.380 1.00 23.78 ? 14  VAL A C   1 
ATOM   90   O O   . VAL A 1 14  ? -14.734 24.470  -24.703 1.00 26.13 ? 14  VAL A O   1 
ATOM   91   C CB  . VAL A 1 14  ? -15.224 27.420  -24.289 1.00 19.37 ? 14  VAL A CB  1 
ATOM   92   C CG1 . VAL A 1 14  ? -13.847 27.731  -23.709 1.00 17.41 ? 14  VAL A CG1 1 
ATOM   93   C CG2 . VAL A 1 14  ? -16.029 28.699  -24.479 1.00 24.93 ? 14  VAL A CG2 1 
ATOM   94   N N   . GLN A 1 15  ? -13.078 25.345  -25.940 1.00 19.22 ? 15  GLN A N   1 
ATOM   95   C CA  . GLN A 1 15  ? -12.156 24.260  -25.652 1.00 17.64 ? 15  GLN A CA  1 
ATOM   96   C C   . GLN A 1 15  ? -10.722 24.706  -25.897 1.00 15.50 ? 15  GLN A C   1 
ATOM   97   O O   . GLN A 1 15  ? -10.467 25.630  -26.670 1.00 19.61 ? 15  GLN A O   1 
ATOM   98   C CB  . GLN A 1 15  ? -12.496 23.019  -26.474 1.00 22.92 ? 15  GLN A CB  1 
ATOM   99   C CG  . GLN A 1 15  ? -12.574 23.261  -27.971 1.00 26.56 ? 15  GLN A CG  1 
ATOM   100  C CD  . GLN A 1 15  ? -13.280 22.131  -28.695 1.00 34.60 ? 15  GLN A CD  1 
ATOM   101  O OE1 . GLN A 1 15  ? -13.346 22.108  -29.924 1.00 51.26 ? 15  GLN A OE1 1 
ATOM   102  N NE2 . GLN A 1 15  ? -13.816 21.186  -27.932 1.00 47.14 ? 15  GLN A NE2 1 
ATOM   103  N N   . GLY A 1 16  ? -9.784  24.056  -25.226 1.00 15.64 ? 16  GLY A N   1 
ATOM   104  C CA  . GLY A 1 16  ? -8.399  24.454  -25.347 1.00 15.75 ? 16  GLY A CA  1 
ATOM   105  C C   . GLY A 1 16  ? -7.452  23.423  -24.786 1.00 14.67 ? 16  GLY A C   1 
ATOM   106  O O   . GLY A 1 16  ? -7.864  22.495  -24.094 1.00 16.94 ? 16  GLY A O   1 
ATOM   107  N N   . ILE A 1 17  ? -6.177  23.595  -25.114 1.00 17.46 ? 17  ILE A N   1 
ATOM   108  C CA  . ILE A 1 17  ? -5.102  22.795  -24.557 1.00 16.25 ? 17  ILE A CA  1 
ATOM   109  C C   . ILE A 1 17  ? -4.032  23.758  -24.078 1.00 15.89 ? 17  ILE A C   1 
ATOM   110  O O   . ILE A 1 17  ? -3.561  24.613  -24.837 1.00 16.45 ? 17  ILE A O   1 
ATOM   111  C CB  . ILE A 1 17  ? -4.489  21.856  -25.609 1.00 20.33 ? 17  ILE A CB  1 
ATOM   112  C CG1 . ILE A 1 17  ? -5.497  20.782  -26.019 1.00 19.80 ? 17  ILE A CG1 1 
ATOM   113  C CG2 . ILE A 1 17  ? -3.210  21.210  -25.079 1.00 18.54 ? 17  ILE A CG2 1 
ATOM   114  C CD1 . ILE A 1 17  ? -4.949  19.806  -27.028 1.00 22.41 ? 17  ILE A CD1 1 
ATOM   115  N N   . ILE A 1 18  ? -3.647  23.608  -22.817 1.00 14.83 ? 18  ILE A N   1 
ATOM   116  C CA  . ILE A 1 18  ? -2.695  24.505  -22.187 1.00 14.92 ? 18  ILE A CA  1 
ATOM   117  C C   . ILE A 1 18  ? -1.537  23.680  -21.652 1.00 19.62 ? 18  ILE A C   1 
ATOM   118  O O   . ILE A 1 18  ? -1.739  22.675  -20.982 1.00 16.75 ? 18  ILE A O   1 
ATOM   119  C CB  . ILE A 1 18  ? -3.349  25.280  -21.025 1.00 17.03 ? 18  ILE A CB  1 
ATOM   120  C CG1 . ILE A 1 18  ? -4.594  26.030  -21.511 1.00 15.59 ? 18  ILE A CG1 1 
ATOM   121  C CG2 . ILE A 1 18  ? -2.341  26.224  -20.359 1.00 16.82 ? 18  ILE A CG2 1 
ATOM   122  C CD1 . ILE A 1 18  ? -4.317  27.018  -22.637 1.00 18.11 ? 18  ILE A CD1 1 
ATOM   123  N N   . ASN A 1 19  ? -0.324  24.107  -21.972 1.00 16.71 ? 19  ASN A N   1 
ATOM   124  C CA  . ASN A 1 19  ? 0.876   23.396  -21.571 1.00 17.01 ? 19  ASN A CA  1 
ATOM   125  C C   . ASN A 1 19  ? 1.599   24.145  -20.468 1.00 15.52 ? 19  ASN A C   1 
ATOM   126  O O   . ASN A 1 19  ? 1.546   25.376  -20.398 1.00 14.77 ? 19  ASN A O   1 
ATOM   127  C CB  . ASN A 1 19  ? 1.805   23.231  -22.775 1.00 18.48 ? 19  ASN A CB  1 
ATOM   128  C CG  . ASN A 1 19  ? 1.128   22.522  -23.940 1.00 20.42 ? 19  ASN A CG  1 
ATOM   129  O OD1 . ASN A 1 19  ? 0.742   23.150  -24.930 1.00 25.74 ? 19  ASN A OD1 1 
ATOM   130  N ND2 . ASN A 1 19  ? 0.970   21.207  -23.819 1.00 17.27 ? 19  ASN A ND2 1 
ATOM   131  N N   . PHE A 1 20  ? 2.290   23.399  -19.615 1.00 13.62 ? 20  PHE A N   1 
ATOM   132  C CA  . PHE A 1 20  ? 3.091   23.991  -18.548 1.00 14.18 ? 20  PHE A CA  1 
ATOM   133  C C   . PHE A 1 20  ? 4.481   23.382  -18.553 1.00 15.34 ? 20  PHE A C   1 
ATOM   134  O O   . PHE A 1 20  ? 4.631   22.185  -18.791 1.00 15.67 ? 20  PHE A O   1 
ATOM   135  C CB  . PHE A 1 20  ? 2.457   23.738  -17.178 1.00 11.07 ? 20  PHE A CB  1 
ATOM   136  C CG  . PHE A 1 20  ? 1.036   24.207  -17.067 1.00 17.10 ? 20  PHE A CG  1 
ATOM   137  C CD1 . PHE A 1 20  ? -0.004  23.428  -17.546 1.00 16.96 ? 20  PHE A CD1 1 
ATOM   138  C CD2 . PHE A 1 20  ? 0.741   25.418  -16.465 1.00 17.98 ? 20  PHE A CD2 1 
ATOM   139  C CE1 . PHE A 1 20  ? -1.316  23.855  -17.433 1.00 20.70 ? 20  PHE A CE1 1 
ATOM   140  C CE2 . PHE A 1 20  ? -0.565  25.851  -16.348 1.00 16.80 ? 20  PHE A CE2 1 
ATOM   141  C CZ  . PHE A 1 20  ? -1.594  25.074  -16.834 1.00 14.88 ? 20  PHE A CZ  1 
ATOM   142  N N   . GLU A 1 21  ? 5.491   24.206  -18.294 1.00 20.04 ? 21  GLU A N   1 
ATOM   143  C CA  . GLU A 1 21  ? 6.868   23.722  -18.166 1.00 17.59 ? 21  GLU A CA  1 
ATOM   144  C C   . GLU A 1 21  ? 7.637   24.516  -17.122 1.00 18.52 ? 21  GLU A C   1 
ATOM   145  O O   . GLU A 1 21  ? 7.603   25.743  -17.112 1.00 17.65 ? 21  GLU A O   1 
ATOM   146  C CB  . GLU A 1 21  ? 7.609   23.787  -19.508 1.00 21.71 ? 21  GLU A CB  1 
ATOM   147  C CG  . GLU A 1 21  ? 9.096   23.440  -19.391 1.00 20.96 ? 21  GLU A CG  1 
ATOM   148  C CD  . GLU A 1 21  ? 9.845   23.557  -20.707 1.00 37.56 ? 21  GLU A CD  1 
ATOM   149  O OE1 . GLU A 1 21  ? 9.252   23.262  -21.764 1.00 30.82 ? 21  GLU A OE1 1 
ATOM   150  O OE2 . GLU A 1 21  ? 11.035  23.936  -20.682 1.00 55.45 ? 21  GLU A OE2 1 
ATOM   151  N N   . GLN A 1 22  ? 8.340   23.811  -16.240 1.00 15.19 ? 22  GLN A N   1 
ATOM   152  C CA  . GLN A 1 22  ? 9.160   24.467  -15.233 1.00 16.19 ? 22  GLN A CA  1 
ATOM   153  C C   . GLN A 1 22  ? 10.544  23.819  -15.193 1.00 22.72 ? 22  GLN A C   1 
ATOM   154  O O   . GLN A 1 22  ? 10.665  22.622  -14.948 1.00 20.85 ? 22  GLN A O   1 
ATOM   155  C CB  . GLN A 1 22  ? 8.474   24.385  -13.864 1.00 15.52 ? 22  GLN A CB  1 
ATOM   156  C CG  . GLN A 1 22  ? 9.185   25.153  -12.757 1.00 17.07 ? 22  GLN A CG  1 
ATOM   157  C CD  . GLN A 1 22  ? 8.497   24.977  -11.423 1.00 18.01 ? 22  GLN A CD  1 
ATOM   158  O OE1 . GLN A 1 22  ? 7.895   23.938  -11.169 1.00 15.38 ? 22  GLN A OE1 1 
ATOM   159  N NE2 . GLN A 1 22  ? 8.569   25.994  -10.570 1.00 14.84 ? 22  GLN A NE2 1 
ATOM   160  N N   . LYS A 1 23  ? 11.582  24.609  -15.455 1.00 20.65 ? 23  LYS A N   1 
ATOM   161  C CA  . LYS A 1 23  ? 12.942  24.082  -15.546 1.00 23.58 ? 23  LYS A CA  1 
ATOM   162  C C   . LYS A 1 23  ? 13.532  23.738  -14.182 1.00 26.54 ? 23  LYS A C   1 
ATOM   163  O O   . LYS A 1 23  ? 14.237  22.739  -14.038 1.00 25.16 ? 23  LYS A O   1 
ATOM   164  C CB  . LYS A 1 23  ? 13.854  25.071  -16.278 1.00 26.59 ? 23  LYS A CB  1 
ATOM   165  C CG  . LYS A 1 23  ? 13.479  25.284  -17.736 1.00 36.44 ? 23  LYS A CG  1 
ATOM   166  C CD  . LYS A 1 23  ? 14.560  26.054  -18.480 1.00 52.43 ? 23  LYS A CD  1 
ATOM   167  C CE  . LYS A 1 23  ? 15.894  25.317  -18.441 1.00 60.14 ? 23  LYS A CE  1 
ATOM   168  N NZ  . LYS A 1 23  ? 16.944  26.008  -19.244 1.00 58.47 ? 23  LYS A NZ  1 
ATOM   169  N N   . GLU A 1 24  ? 13.250  24.573  -13.188 1.00 19.67 ? 24  GLU A N   1 
ATOM   170  C CA  . GLU A 1 24  ? 13.735  24.328  -11.829 1.00 27.66 ? 24  GLU A CA  1 
ATOM   171  C C   . GLU A 1 24  ? 12.674  24.652  -10.777 1.00 24.03 ? 24  GLU A C   1 
ATOM   172  O O   . GLU A 1 24  ? 11.867  25.560  -10.953 1.00 18.49 ? 24  GLU A O   1 
ATOM   173  C CB  . GLU A 1 24  ? 15.032  25.095  -11.559 1.00 32.12 ? 24  GLU A CB  1 
ATOM   174  C CG  . GLU A 1 24  ? 14.960  26.581  -11.850 1.00 41.18 ? 24  GLU A CG  1 
ATOM   175  C CD  . GLU A 1 24  ? 16.335  27.192  -12.057 1.00 51.69 ? 24  GLU A CD  1 
ATOM   176  O OE1 . GLU A 1 24  ? 17.270  26.445  -12.417 1.00 49.29 ? 24  GLU A OE1 1 
ATOM   177  O OE2 . GLU A 1 24  ? 16.480  28.417  -11.865 1.00 57.10 ? 24  GLU A OE2 1 
ATOM   178  N N   . SER A 1 25  ? 12.691  23.911  -9.674  1.00 18.65 ? 25  SER A N   1 
ATOM   179  C CA  A SER A 1 25  ? 11.633  24.022  -8.676  0.24 22.37 ? 25  SER A CA  1 
ATOM   180  C CA  B SER A 1 25  ? 11.658  24.015  -8.644  0.76 22.35 ? 25  SER A CA  1 
ATOM   181  C C   . SER A 1 25  ? 11.442  25.443  -8.146  1.00 20.33 ? 25  SER A C   1 
ATOM   182  O O   . SER A 1 25  ? 10.341  25.814  -7.751  1.00 25.30 ? 25  SER A O   1 
ATOM   183  C CB  A SER A 1 25  ? 11.864  23.038  -7.524  0.24 21.89 ? 25  SER A CB  1 
ATOM   184  C CB  B SER A 1 25  ? 11.997  23.105  -7.458  0.76 21.76 ? 25  SER A CB  1 
ATOM   185  O OG  A SER A 1 25  ? 11.621  21.709  -7.952  0.24 21.43 ? 25  SER A OG  1 
ATOM   186  O OG  B SER A 1 25  ? 13.180  23.539  -6.811  0.76 19.11 ? 25  SER A OG  1 
ATOM   187  N N   . ASN A 1 26  ? 12.503  26.240  -8.159  1.00 22.02 ? 26  ASN A N   1 
ATOM   188  C CA  . ASN A 1 26  ? 12.417  27.610  -7.668  1.00 30.51 ? 26  ASN A CA  1 
ATOM   189  C C   . ASN A 1 26  ? 12.166  28.603  -8.796  1.00 29.13 ? 26  ASN A C   1 
ATOM   190  O O   . ASN A 1 26  ? 12.081  29.810  -8.568  1.00 36.70 ? 26  ASN A O   1 
ATOM   191  C CB  . ASN A 1 26  ? 13.692  27.986  -6.909  1.00 33.56 ? 26  ASN A CB  1 
ATOM   192  C CG  . ASN A 1 26  ? 14.947  27.787  -7.744  1.00 40.43 ? 26  ASN A CG  1 
ATOM   193  O OD1 . ASN A 1 26  ? 15.291  26.528  -8.014  1.00 44.77 ? 26  ASN A OD1 1 
ATOM   194  N ND2 . ASN A 1 26  ? 15.596  28.754  -8.148  1.00 36.90 ? 26  ASN A ND2 1 
ATOM   195  N N   . GLY A 1 27  ? 12.037  28.087  -10.012 1.00 29.53 ? 27  GLY A N   1 
ATOM   196  C CA  . GLY A 1 27  ? 11.960  28.932  -11.188 1.00 27.86 ? 27  GLY A CA  1 
ATOM   197  C C   . GLY A 1 27  ? 10.554  29.187  -11.697 1.00 22.67 ? 27  GLY A C   1 
ATOM   198  O O   . GLY A 1 27  ? 9.588   28.594  -11.211 1.00 20.67 ? 27  GLY A O   1 
ATOM   199  N N   . PRO A 1 28  ? 10.435  30.073  -12.696 1.00 22.32 ? 28  PRO A N   1 
ATOM   200  C CA  . PRO A 1 28  ? 9.134   30.411  -13.284 1.00 25.02 ? 28  PRO A CA  1 
ATOM   201  C C   . PRO A 1 28  ? 8.524   29.235  -14.032 1.00 19.37 ? 28  PRO A C   1 
ATOM   202  O O   . PRO A 1 28  ? 9.245   28.375  -14.541 1.00 18.25 ? 28  PRO A O   1 
ATOM   203  C CB  . PRO A 1 28  ? 9.473   31.536  -14.270 1.00 23.82 ? 28  PRO A CB  1 
ATOM   204  C CG  . PRO A 1 28  ? 10.850  32.007  -13.886 1.00 34.91 ? 28  PRO A CG  1 
ATOM   205  C CD  . PRO A 1 28  ? 11.536  30.798  -13.348 1.00 28.13 ? 28  PRO A CD  1 
ATOM   206  N N   . VAL A 1 29  ? 7.196   29.202  -14.087 1.00 18.48 ? 29  VAL A N   1 
ATOM   207  C CA  . VAL A 1 29  ? 6.483   28.225  -14.896 1.00 21.30 ? 29  VAL A CA  1 
ATOM   208  C C   . VAL A 1 29  ? 6.046   28.860  -16.222 1.00 17.03 ? 29  VAL A C   1 
ATOM   209  O O   . VAL A 1 29  ? 5.379   29.894  -16.226 1.00 18.26 ? 29  VAL A O   1 
ATOM   210  C CB  . VAL A 1 29  ? 5.227   27.706  -14.172 1.00 15.97 ? 29  VAL A CB  1 
ATOM   211  C CG1 . VAL A 1 29  ? 4.533   26.651  -15.020 1.00 17.47 ? 29  VAL A CG1 1 
ATOM   212  C CG2 . VAL A 1 29  ? 5.584   27.146  -12.788 1.00 16.10 ? 29  VAL A CG2 1 
ATOM   213  N N   . LYS A 1 30  ? 6.436   28.256  -17.340 1.00 15.87 ? 30  LYS A N   1 
ATOM   214  C CA  . LYS A 1 30  ? 5.975   28.726  -18.646 1.00 21.50 ? 30  LYS A CA  1 
ATOM   215  C C   . LYS A 1 30  ? 4.622   28.108  -18.977 1.00 19.33 ? 30  LYS A C   1 
ATOM   216  O O   . LYS A 1 30  ? 4.468   26.888  -18.949 1.00 17.13 ? 30  LYS A O   1 
ATOM   217  C CB  . LYS A 1 30  ? 6.984   28.383  -19.746 1.00 20.68 ? 30  LYS A CB  1 
ATOM   218  C CG  . LYS A 1 30  ? 8.277   29.187  -19.694 1.00 28.02 ? 30  LYS A CG  1 
ATOM   219  C CD  . LYS A 1 30  ? 9.125   28.931  -20.930 1.00 40.16 ? 30  LYS A CD  1 
ATOM   220  C CE  . LYS A 1 30  ? 10.294  29.898  -21.014 1.00 50.21 ? 30  LYS A CE  1 
ATOM   221  N NZ  . LYS A 1 30  ? 11.007  29.785  -22.318 1.00 55.89 ? 30  LYS A NZ  1 
ATOM   222  N N   . VAL A 1 31  ? 3.646   28.953  -19.300 1.00 16.45 ? 31  VAL A N   1 
ATOM   223  C CA  . VAL A 1 31  ? 2.308   28.487  -19.644 1.00 14.86 ? 31  VAL A CA  1 
ATOM   224  C C   . VAL A 1 31  ? 1.979   28.910  -21.064 1.00 20.35 ? 31  VAL A C   1 
ATOM   225  O O   . VAL A 1 31  ? 2.018   30.099  -21.387 1.00 19.92 ? 31  VAL A O   1 
ATOM   226  C CB  . VAL A 1 31  ? 1.252   29.095  -18.701 1.00 15.12 ? 31  VAL A CB  1 
ATOM   227  C CG1 . VAL A 1 31  ? -0.158  28.593  -19.065 1.00 15.02 ? 31  VAL A CG1 1 
ATOM   228  C CG2 . VAL A 1 31  ? 1.603   28.801  -17.237 1.00 15.19 ? 31  VAL A CG2 1 
ATOM   229  N N   . TRP A 1 32  ? 1.666   27.946  -21.923 1.00 14.71 ? 32  TRP A N   1 
ATOM   230  C CA  . TRP A 1 32  ? 1.332   28.281  -23.301 1.00 17.84 ? 32  TRP A CA  1 
ATOM   231  C C   . TRP A 1 32  ? 0.358   27.302  -23.938 1.00 16.40 ? 32  TRP A C   1 
ATOM   232  O O   . TRP A 1 32  ? 0.357   26.110  -23.629 1.00 15.91 ? 32  TRP A O   1 
ATOM   233  C CB  . TRP A 1 32  ? 2.600   28.408  -24.153 1.00 19.97 ? 32  TRP A CB  1 
ATOM   234  C CG  . TRP A 1 32  ? 3.179   27.105  -24.604 1.00 19.90 ? 32  TRP A CG  1 
ATOM   235  C CD1 . TRP A 1 32  ? 3.100   26.561  -25.856 1.00 22.51 ? 32  TRP A CD1 1 
ATOM   236  C CD2 . TRP A 1 32  ? 3.944   26.185  -23.815 1.00 18.99 ? 32  TRP A CD2 1 
ATOM   237  N NE1 . TRP A 1 32  ? 3.763   25.354  -25.892 1.00 21.85 ? 32  TRP A NE1 1 
ATOM   238  C CE2 . TRP A 1 32  ? 4.290   25.102  -24.653 1.00 20.65 ? 32  TRP A CE2 1 
ATOM   239  C CE3 . TRP A 1 32  ? 4.369   26.169  -22.481 1.00 24.20 ? 32  TRP A CE3 1 
ATOM   240  C CZ2 . TRP A 1 32  ? 5.037   24.015  -24.200 1.00 25.03 ? 32  TRP A CZ2 1 
ATOM   241  C CZ3 . TRP A 1 32  ? 5.115   25.087  -22.033 1.00 20.21 ? 32  TRP A CZ3 1 
ATOM   242  C CH2 . TRP A 1 32  ? 5.441   24.027  -22.892 1.00 20.30 ? 32  TRP A CH2 1 
ATOM   243  N N   . GLY A 1 33  ? -0.448  27.823  -24.857 1.00 18.67 ? 33  GLY A N   1 
ATOM   244  C CA  . GLY A 1 33  ? -1.423  27.026  -25.571 1.00 13.00 ? 33  GLY A CA  1 
ATOM   245  C C   . GLY A 1 33  ? -2.454  27.921  -26.225 1.00 18.95 ? 33  GLY A C   1 
ATOM   246  O O   . GLY A 1 33  ? -2.212  29.103  -26.457 1.00 15.66 ? 33  GLY A O   1 
ATOM   247  N N   . SER A 1 34  ? -3.622  27.365  -26.507 1.00 18.65 ? 34  SER A N   1 
ATOM   248  C CA  . SER A 1 34  ? -4.667  28.141  -27.157 1.00 19.29 ? 34  SER A CA  1 
ATOM   249  C C   . SER A 1 34  ? -6.047  27.701  -26.693 1.00 17.72 ? 34  SER A C   1 
ATOM   250  O O   . SER A 1 34  ? -6.239  26.553  -26.289 1.00 16.03 ? 34  SER A O   1 
ATOM   251  C CB  . SER A 1 34  ? -4.544  28.020  -28.675 1.00 22.35 ? 34  SER A CB  1 
ATOM   252  O OG  . SER A 1 34  ? -4.444  26.661  -29.061 1.00 33.82 ? 34  SER A OG  1 
ATOM   253  N N   . ILE A 1 35  ? -6.994  28.632  -26.739 1.00 15.34 ? 35  ILE A N   1 
ATOM   254  C CA  . ILE A 1 35  ? -8.378  28.352  -26.373 1.00 12.25 ? 35  ILE A CA  1 
ATOM   255  C C   . ILE A 1 35  ? -9.281  28.892  -27.476 1.00 21.83 ? 35  ILE A C   1 
ATOM   256  O O   . ILE A 1 35  ? -9.110  30.025  -27.934 1.00 18.71 ? 35  ILE A O   1 
ATOM   257  C CB  . ILE A 1 35  ? -8.777  29.013  -25.041 1.00 16.70 ? 35  ILE A CB  1 
ATOM   258  C CG1 . ILE A 1 35  ? -7.701  28.790  -23.971 1.00 15.34 ? 35  ILE A CG1 1 
ATOM   259  C CG2 . ILE A 1 35  ? -10.133 28.482  -24.567 1.00 15.53 ? 35  ILE A CG2 1 
ATOM   260  C CD1 . ILE A 1 35  ? -7.985  29.492  -22.662 1.00 24.17 ? 35  ILE A CD1 1 
ATOM   261  N N   . LYS A 1 36  ? -10.236 28.085  -27.915 1.00 15.68 ? 36  LYS A N   1 
ATOM   262  C CA  . LYS A 1 36  ? -11.148 28.537  -28.959 1.00 14.00 ? 36  LYS A CA  1 
ATOM   263  C C   . LYS A 1 36  ? -12.580 28.595  -28.439 1.00 18.37 ? 36  LYS A C   1 
ATOM   264  O O   . LYS A 1 36  ? -12.862 28.178  -27.312 1.00 17.06 ? 36  LYS A O   1 
ATOM   265  C CB  . LYS A 1 36  ? -11.048 27.655  -30.205 1.00 25.55 ? 36  LYS A CB  1 
ATOM   266  C CG  . LYS A 1 36  ? -11.382 26.195  -29.978 1.00 30.70 ? 36  LYS A CG  1 
ATOM   267  C CD  . LYS A 1 36  ? -11.383 25.436  -31.298 1.00 36.44 ? 36  LYS A CD  1 
ATOM   268  C CE  . LYS A 1 36  ? -11.375 23.934  -31.078 1.00 44.04 ? 36  LYS A CE  1 
ATOM   269  N NZ  . LYS A 1 36  ? -10.223 23.506  -30.232 1.00 47.72 ? 36  LYS A NZ  1 
ATOM   270  N N   . GLY A 1 37  ? -13.478 29.143  -29.251 1.00 17.37 ? 37  GLY A N   1 
ATOM   271  C CA  . GLY A 1 37  ? -14.878 29.241  -28.871 1.00 19.08 ? 37  GLY A CA  1 
ATOM   272  C C   . GLY A 1 37  ? -15.238 30.367  -27.919 1.00 15.47 ? 37  GLY A C   1 
ATOM   273  O O   . GLY A 1 37  ? -16.337 30.375  -27.352 1.00 17.93 ? 37  GLY A O   1 
ATOM   274  N N   . LEU A 1 38  ? -14.333 31.330  -27.760 1.00 16.56 ? 38  LEU A N   1 
ATOM   275  C CA  . LEU A 1 38  ? -14.513 32.440  -26.821 1.00 16.28 ? 38  LEU A CA  1 
ATOM   276  C C   . LEU A 1 38  ? -15.073 33.700  -27.479 1.00 17.01 ? 38  LEU A C   1 
ATOM   277  O O   . LEU A 1 38  ? -14.943 33.885  -28.686 1.00 21.12 ? 38  LEU A O   1 
ATOM   278  C CB  . LEU A 1 38  ? -13.172 32.798  -26.166 1.00 16.00 ? 38  LEU A CB  1 
ATOM   279  C CG  . LEU A 1 38  ? -12.511 31.785  -25.220 1.00 15.63 ? 38  LEU A CG  1 
ATOM   280  C CD1 . LEU A 1 38  ? -11.101 32.250  -24.840 1.00 15.62 ? 38  LEU A CD1 1 
ATOM   281  C CD2 . LEU A 1 38  ? -13.360 31.568  -23.985 1.00 18.01 ? 38  LEU A CD2 1 
ATOM   282  N N   . THR A 1 39  ? -15.693 34.567  -26.681 1.00 19.77 ? 39  THR A N   1 
ATOM   283  C CA  . THR A 1 39  ? -16.082 35.888  -27.170 1.00 18.50 ? 39  THR A CA  1 
ATOM   284  C C   . THR A 1 39  ? -14.839 36.744  -27.348 1.00 16.54 ? 39  THR A C   1 
ATOM   285  O O   . THR A 1 39  ? -13.874 36.613  -26.593 1.00 16.22 ? 39  THR A O   1 
ATOM   286  C CB  . THR A 1 39  ? -17.073 36.614  -26.227 1.00 21.03 ? 39  THR A CB  1 
ATOM   287  O OG1 . THR A 1 39  ? -16.541 36.677  -24.897 1.00 17.36 ? 39  THR A OG1 1 
ATOM   288  C CG2 . THR A 1 39  ? -18.414 35.901  -26.201 1.00 20.93 ? 39  THR A CG2 1 
ATOM   289  N N   . GLU A 1 40  ? -14.849 37.608  -28.360 1.00 19.58 ? 40  GLU A N   1 
ATOM   290  C CA  . GLU A 1 40  ? -13.705 38.483  -28.595 1.00 19.07 ? 40  GLU A CA  1 
ATOM   291  C C   . GLU A 1 40  ? -13.440 39.308  -27.340 1.00 20.99 ? 40  GLU A C   1 
ATOM   292  O O   . GLU A 1 40  ? -14.369 39.827  -26.726 1.00 21.98 ? 40  GLU A O   1 
ATOM   293  C CB  . GLU A 1 40  ? -13.955 39.403  -29.791 1.00 19.83 ? 40  GLU A CB  1 
ATOM   294  C CG  . GLU A 1 40  ? -12.775 40.286  -30.146 1.00 24.86 ? 40  GLU A CG  1 
ATOM   295  C CD  . GLU A 1 40  ? -13.150 41.385  -31.119 1.00 33.45 ? 40  GLU A CD  1 
ATOM   296  O OE1 . GLU A 1 40  ? -14.287 41.361  -31.638 1.00 31.20 ? 40  GLU A OE1 1 
ATOM   297  O OE2 . GLU A 1 40  ? -12.308 42.276  -31.358 1.00 35.35 ? 40  GLU A OE2 1 
ATOM   298  N N   . GLY A 1 41  ? -12.176 39.416  -26.946 1.00 19.14 ? 41  GLY A N   1 
ATOM   299  C CA  . GLY A 1 41  ? -11.825 40.212  -25.780 1.00 17.72 ? 41  GLY A CA  1 
ATOM   300  C C   . GLY A 1 41  ? -11.240 39.441  -24.609 1.00 20.50 ? 41  GLY A C   1 
ATOM   301  O O   . GLY A 1 41  ? -10.783 38.309  -24.755 1.00 21.24 ? 41  GLY A O   1 
ATOM   302  N N   . LEU A 1 42  ? -11.281 40.059  -23.433 1.00 17.42 ? 42  LEU A N   1 
ATOM   303  C CA  . LEU A 1 42  ? -10.601 39.533  -22.245 1.00 18.57 ? 42  LEU A CA  1 
ATOM   304  C C   . LEU A 1 42  ? -11.393 38.476  -21.473 1.00 23.30 ? 42  LEU A C   1 
ATOM   305  O O   . LEU A 1 42  ? -12.613 38.582  -21.314 1.00 19.95 ? 42  LEU A O   1 
ATOM   306  C CB  . LEU A 1 42  ? -10.214 40.685  -21.314 1.00 23.38 ? 42  LEU A CB  1 
ATOM   307  C CG  . LEU A 1 42  ? -8.848  41.343  -21.540 1.00 24.16 ? 42  LEU A CG  1 
ATOM   308  C CD1 . LEU A 1 42  ? -8.433  41.305  -23.002 1.00 37.69 ? 42  LEU A CD1 1 
ATOM   309  C CD2 . LEU A 1 42  ? -8.848  42.769  -21.001 1.00 29.20 ? 42  LEU A CD2 1 
ATOM   310  N N   . HIS A 1 43  ? -10.676 37.465  -20.986 1.00 21.24 ? 43  HIS A N   1 
ATOM   311  C CA  . HIS A 1 43  ? -11.267 36.374  -20.219 1.00 18.79 ? 43  HIS A CA  1 
ATOM   312  C C   . HIS A 1 43  ? -10.388 35.978  -19.042 1.00 19.77 ? 43  HIS A C   1 
ATOM   313  O O   . HIS A 1 43  ? -9.200  35.709  -19.212 1.00 17.11 ? 43  HIS A O   1 
ATOM   314  C CB  . HIS A 1 43  ? -11.491 35.160  -21.112 1.00 16.54 ? 43  HIS A CB  1 
ATOM   315  C CG  . HIS A 1 43  ? -12.521 35.387  -22.170 1.00 19.37 ? 43  HIS A CG  1 
ATOM   316  N ND1 . HIS A 1 43  ? -13.860 35.138  -21.967 1.00 20.12 ? 43  HIS A ND1 1 
ATOM   317  C CD2 . HIS A 1 43  ? -12.412 35.875  -23.428 1.00 18.14 ? 43  HIS A CD2 1 
ATOM   318  C CE1 . HIS A 1 43  ? -14.533 35.447  -23.062 1.00 18.23 ? 43  HIS A CE1 1 
ATOM   319  N NE2 . HIS A 1 43  ? -13.678 35.900  -23.961 1.00 16.49 ? 43  HIS A NE2 1 
ATOM   320  N N   . GLY A 1 44  ? -10.981 35.933  -17.853 1.00 15.77 ? 44  GLY A N   1 
ATOM   321  C CA  . GLY A 1 44  ? -10.257 35.525  -16.657 1.00 16.26 ? 44  GLY A CA  1 
ATOM   322  C C   . GLY A 1 44  ? -9.691  34.124  -16.792 1.00 16.00 ? 44  GLY A C   1 
ATOM   323  O O   . GLY A 1 44  ? -10.333 33.234  -17.349 1.00 17.97 ? 44  GLY A O   1 
ATOM   324  N N   . PHE A 1 45  ? -8.484  33.932  -16.268 1.00 17.53 ? 45  PHE A N   1 
ATOM   325  C CA  . PHE A 1 45  ? -7.742  32.692  -16.431 1.00 15.54 ? 45  PHE A CA  1 
ATOM   326  C C   . PHE A 1 45  ? -7.135  32.358  -15.069 1.00 19.38 ? 45  PHE A C   1 
ATOM   327  O O   . PHE A 1 45  ? -6.305  33.108  -14.556 1.00 22.07 ? 45  PHE A O   1 
ATOM   328  C CB  . PHE A 1 45  ? -6.654  32.928  -17.488 1.00 19.57 ? 45  PHE A CB  1 
ATOM   329  C CG  . PHE A 1 45  ? -5.962  31.684  -17.973 1.00 21.30 ? 45  PHE A CG  1 
ATOM   330  C CD1 . PHE A 1 45  ? -6.683  30.608  -18.457 1.00 16.38 ? 45  PHE A CD1 1 
ATOM   331  C CD2 . PHE A 1 45  ? -4.573  31.620  -17.996 1.00 21.07 ? 45  PHE A CD2 1 
ATOM   332  C CE1 . PHE A 1 45  ? -6.033  29.474  -18.920 1.00 21.30 ? 45  PHE A CE1 1 
ATOM   333  C CE2 . PHE A 1 45  ? -3.918  30.493  -18.463 1.00 18.73 ? 45  PHE A CE2 1 
ATOM   334  C CZ  . PHE A 1 45  ? -4.647  29.419  -18.923 1.00 17.21 ? 45  PHE A CZ  1 
ATOM   335  N N   . ARG A 1 46  ? -7.561  31.258  -14.458 1.00 16.57 ? 46  ARG A N   1 
ATOM   336  C CA  . ARG A 1 46  ? -7.099  30.974  -13.099 1.00 16.83 ? 46  ARG A CA  1 
ATOM   337  C C   . ARG A 1 46  ? -7.116  29.501  -12.714 1.00 17.97 ? 46  ARG A C   1 
ATOM   338  O O   . ARG A 1 46  ? -7.744  28.681  -13.368 1.00 17.20 ? 46  ARG A O   1 
ATOM   339  C CB  . ARG A 1 46  ? -7.893  31.793  -12.079 1.00 23.02 ? 46  ARG A CB  1 
ATOM   340  C CG  . ARG A 1 46  ? -9.365  31.452  -12.039 1.00 25.08 ? 46  ARG A CG  1 
ATOM   341  C CD  . ARG A 1 46  ? -10.133 32.377  -11.106 1.00 32.37 ? 46  ARG A CD  1 
ATOM   342  N NE  . ARG A 1 46  ? -10.041 33.769  -11.533 1.00 31.57 ? 46  ARG A NE  1 
ATOM   343  C CZ  . ARG A 1 46  ? -10.960 34.694  -11.276 1.00 35.83 ? 46  ARG A CZ  1 
ATOM   344  N NH1 . ARG A 1 46  ? -12.054 34.375  -10.596 1.00 34.24 ? 46  ARG A NH1 1 
ATOM   345  N NH2 . ARG A 1 46  ? -10.788 35.936  -11.709 1.00 32.90 ? 46  ARG A NH2 1 
ATOM   346  N N   . VAL A 1 47  ? -6.399  29.184  -11.641 1.00 17.31 ? 47  VAL A N   1 
ATOM   347  C CA  . VAL A 1 47  ? -6.364  27.832  -11.106 1.00 15.83 ? 47  VAL A CA  1 
ATOM   348  C C   . VAL A 1 47  ? -7.188  27.784  -9.813  1.00 18.41 ? 47  VAL A C   1 
ATOM   349  O O   . VAL A 1 47  ? -7.026  28.635  -8.938  1.00 18.46 ? 47  VAL A O   1 
ATOM   350  C CB  . VAL A 1 47  ? -4.913  27.389  -10.809 1.00 15.42 ? 47  VAL A CB  1 
ATOM   351  C CG1 . VAL A 1 47  ? -4.881  25.939  -10.344 1.00 16.71 ? 47  VAL A CG1 1 
ATOM   352  C CG2 . VAL A 1 47  ? -4.027  27.581  -12.048 1.00 19.85 ? 47  VAL A CG2 1 
ATOM   353  N N   . GLN A 1 48  ? -8.082  26.803  -9.717  1.00 24.35 ? 48  GLN A N   1 
ATOM   354  C CA  . GLN A 1 48  ? -8.912  26.600  -8.528  1.00 22.01 ? 48  GLN A CA  1 
ATOM   355  C C   . GLN A 1 48  ? -8.239  25.578  -7.630  1.00 23.67 ? 48  GLN A C   1 
ATOM   356  O O   . GLN A 1 48  ? -7.364  24.845  -8.076  1.00 21.77 ? 48  GLN A O   1 
ATOM   357  C CB  . GLN A 1 48  ? -10.293 26.084  -8.927  1.00 19.19 ? 48  GLN A CB  1 
ATOM   358  C CG  . GLN A 1 48  ? -10.932 26.845  -10.057 1.00 22.98 ? 48  GLN A CG  1 
ATOM   359  C CD  . GLN A 1 48  ? -11.131 28.307  -9.729  1.00 27.42 ? 48  GLN A CD  1 
ATOM   360  O OE1 . GLN A 1 48  ? -10.827 29.181  -10.539 1.00 37.58 ? 48  GLN A OE1 1 
ATOM   361  N NE2 . GLN A 1 48  ? -11.637 28.583  -8.533  1.00 33.27 ? 48  GLN A NE2 1 
ATOM   362  N N   . GLU A 1 49  ? -8.655  25.504  -6.368  1.00 21.44 ? 49  GLU A N   1 
ATOM   363  C CA  . GLU A 1 49  ? -7.969  24.631  -5.430  1.00 21.14 ? 49  GLU A CA  1 
ATOM   364  C C   . GLU A 1 49  ? -8.110  23.147  -5.768  1.00 19.44 ? 49  GLU A C   1 
ATOM   365  O O   . GLU A 1 49  ? -7.144  22.388  -5.689  1.00 23.89 ? 49  GLU A O   1 
ATOM   366  C CB  . GLU A 1 49  ? -8.440  24.887  -4.001  1.00 24.60 ? 49  GLU A CB  1 
ATOM   367  C CG  . GLU A 1 49  ? -7.652  24.095  -2.980  1.00 26.27 ? 49  GLU A CG  1 
ATOM   368  C CD  . GLU A 1 49  ? -8.018  24.452  -1.557  1.00 36.83 ? 49  GLU A CD  1 
ATOM   369  O OE1 . GLU A 1 49  ? -8.776  25.425  -1.366  1.00 33.83 ? 49  GLU A OE1 1 
ATOM   370  O OE2 . GLU A 1 49  ? -7.544  23.758  -0.635  1.00 37.27 ? 49  GLU A OE2 1 
ATOM   371  N N   . PHE A 1 50  ? -9.309  22.729  -6.150  1.00 16.53 ? 50  PHE A N   1 
ATOM   372  C CA  . PHE A 1 50  ? -9.549  21.307  -6.344  1.00 17.39 ? 50  PHE A CA  1 
ATOM   373  C C   . PHE A 1 50  ? -9.584  20.901  -7.808  1.00 17.09 ? 50  PHE A C   1 
ATOM   374  O O   . PHE A 1 50  ? -10.015 21.668  -8.671  1.00 22.10 ? 50  PHE A O   1 
ATOM   375  C CB  . PHE A 1 50  ? -10.833 20.879  -5.640  1.00 18.43 ? 50  PHE A CB  1 
ATOM   376  C CG  . PHE A 1 50  ? -10.841 21.199  -4.175  1.00 19.68 ? 50  PHE A CG  1 
ATOM   377  C CD1 . PHE A 1 50  ? -9.756  20.868  -3.376  1.00 23.30 ? 50  PHE A CD1 1 
ATOM   378  C CD2 . PHE A 1 50  ? -11.925 21.840  -3.596  1.00 25.36 ? 50  PHE A CD2 1 
ATOM   379  C CE1 . PHE A 1 50  ? -9.756  21.164  -2.018  1.00 24.30 ? 50  PHE A CE1 1 
ATOM   380  C CE2 . PHE A 1 50  ? -11.929 22.139  -2.237  1.00 25.73 ? 50  PHE A CE2 1 
ATOM   381  C CZ  . PHE A 1 50  ? -10.844 21.800  -1.452  1.00 25.20 ? 50  PHE A CZ  1 
ATOM   382  N N   . GLY A 1 51  ? -9.131  19.682  -8.074  1.00 13.48 ? 51  GLY A N   1 
ATOM   383  C CA  . GLY A 1 51  ? -9.208  19.105  -9.404  1.00 12.67 ? 51  GLY A CA  1 
ATOM   384  C C   . GLY A 1 51  ? -10.403 18.185  -9.475  1.00 15.09 ? 51  GLY A C   1 
ATOM   385  O O   . GLY A 1 51  ? -10.308 17.041  -9.916  1.00 15.67 ? 51  GLY A O   1 
ATOM   386  N N   . ASP A 1 52  ? -11.538 18.699  -9.013  1.00 14.23 ? 52  ASP A N   1 
ATOM   387  C CA  . ASP A 1 52  ? -12.769 17.936  -8.954  1.00 17.31 ? 52  ASP A CA  1 
ATOM   388  C C   . ASP A 1 52  ? -13.695 18.387  -10.078 1.00 15.96 ? 52  ASP A C   1 
ATOM   389  O O   . ASP A 1 52  ? -14.195 19.510  -10.078 1.00 15.16 ? 52  ASP A O   1 
ATOM   390  C CB  . ASP A 1 52  ? -13.423 18.146  -7.592  1.00 14.06 ? 52  ASP A CB  1 
ATOM   391  C CG  . ASP A 1 52  ? -14.651 17.283  -7.384  1.00 16.48 ? 52  ASP A CG  1 
ATOM   392  O OD1 . ASP A 1 52  ? -15.385 17.031  -8.356  1.00 12.73 ? 52  ASP A OD1 1 
ATOM   393  O OD2 . ASP A 1 52  ? -14.890 16.877  -6.225  1.00 17.85 ? 52  ASP A OD2 1 
ATOM   394  N N   . ASN A 1 53  ? -13.903 17.520  -11.057 1.00 13.75 ? 53  ASN A N   1 
ATOM   395  C CA  . ASN A 1 53  ? -14.750 17.890  -12.181 1.00 17.70 ? 53  ASN A CA  1 
ATOM   396  C C   . ASN A 1 53  ? -15.998 17.025  -12.255 1.00 18.65 ? 53  ASN A C   1 
ATOM   397  O O   . ASN A 1 53  ? -16.583 16.855  -13.325 1.00 18.87 ? 53  ASN A O   1 
ATOM   398  C CB  . ASN A 1 53  ? -13.956 17.872  -13.487 1.00 27.02 ? 53  ASN A CB  1 
ATOM   399  C CG  . ASN A 1 53  ? -12.946 19.015  -13.569 1.00 27.90 ? 53  ASN A CG  1 
ATOM   400  O OD1 . ASN A 1 53  ? -12.879 19.829  -12.515 1.00 27.73 ? 53  ASN A OD1 1 
ATOM   401  N ND2 . ASN A 1 53  ? -12.240 19.163  -14.563 1.00 27.66 ? 53  ASN A ND2 1 
ATOM   402  N N   . THR A 1 54  ? -16.414 16.501  -11.101 1.00 13.56 ? 54  THR A N   1 
ATOM   403  C CA  . THR A 1 54  ? -17.599 15.648  -11.025 1.00 21.07 ? 54  THR A CA  1 
ATOM   404  C C   . THR A 1 54  ? -18.861 16.403  -11.432 1.00 19.53 ? 54  THR A C   1 
ATOM   405  O O   . THR A 1 54  ? -19.843 15.803  -11.861 1.00 21.80 ? 54  THR A O   1 
ATOM   406  C CB  . THR A 1 54  ? -17.793 15.032  -9.615  1.00 18.62 ? 54  THR A CB  1 
ATOM   407  O OG1 . THR A 1 54  ? -17.921 16.075  -8.639  1.00 18.66 ? 54  THR A OG1 1 
ATOM   408  C CG2 . THR A 1 54  ? -16.617 14.146  -9.257  1.00 20.71 ? 54  THR A CG2 1 
ATOM   409  N N   . ALA A 1 55  ? -18.829 17.725  -11.298 1.00 18.35 ? 55  ALA A N   1 
ATOM   410  C CA  . ALA A 1 55  ? -19.941 18.563  -11.735 1.00 17.51 ? 55  ALA A CA  1 
ATOM   411  C C   . ALA A 1 55  ? -19.434 19.623  -12.704 1.00 20.85 ? 55  ALA A C   1 
ATOM   412  O O   . ALA A 1 55  ? -19.757 20.802  -12.575 1.00 23.97 ? 55  ALA A O   1 
ATOM   413  C CB  . ALA A 1 55  ? -20.620 19.217  -10.532 1.00 22.39 ? 55  ALA A CB  1 
ATOM   414  N N   . GLY A 1 56  ? -18.621 19.198  -13.663 1.00 23.34 ? 56  GLY A N   1 
ATOM   415  C CA  . GLY A 1 56  ? -17.998 20.128  -14.585 1.00 22.26 ? 56  GLY A CA  1 
ATOM   416  C C   . GLY A 1 56  ? -17.185 21.139  -13.809 1.00 20.07 ? 56  GLY A C   1 
ATOM   417  O O   . GLY A 1 56  ? -16.505 20.791  -12.850 1.00 21.32 ? 56  GLY A O   1 
ATOM   418  N N   . CYS A 1 57  ? -17.263 22.402  -14.210 1.00 21.08 ? 57  CYS A N   1 
ATOM   419  C CA  . CYS A 1 57  ? -16.455 23.433  -13.578 1.00 20.03 ? 57  CYS A CA  1 
ATOM   420  C C   . CYS A 1 57  ? -17.051 23.878  -12.248 1.00 24.27 ? 57  CYS A C   1 
ATOM   421  O O   . CYS A 1 57  ? -16.402 24.566  -11.465 1.00 22.24 ? 57  CYS A O   1 
ATOM   422  C CB  . CYS A 1 57  ? -16.303 24.625  -14.519 1.00 30.48 ? 57  CYS A CB  1 
ATOM   423  S SG  . CYS A 1 57  ? -15.642 24.165  -16.131 1.00 25.22 ? 57  CYS A SG  1 
ATOM   424  N N   . THR A 1 58  ? -18.290 23.467  -12.005 1.00 22.82 ? 58  THR A N   1 
ATOM   425  C CA  . THR A 1 58  ? -19.040 23.899  -10.833 1.00 27.69 ? 58  THR A CA  1 
ATOM   426  C C   . THR A 1 58  ? -18.456 23.340  -9.542  1.00 26.65 ? 58  THR A C   1 
ATOM   427  O O   . THR A 1 58  ? -18.725 23.857  -8.461  1.00 27.52 ? 58  THR A O   1 
ATOM   428  C CB  . THR A 1 58  ? -20.513 23.467  -10.938 1.00 31.24 ? 58  THR A CB  1 
ATOM   429  O OG1 . THR A 1 58  ? -20.977 23.661  -12.280 1.00 26.40 ? 58  THR A OG1 1 
ATOM   430  C CG2 . THR A 1 58  ? -21.381 24.271  -9.979  1.00 34.80 ? 58  THR A CG2 1 
ATOM   431  N N   . SER A 1 59  ? -17.647 22.290  -9.662  1.00 18.46 ? 59  SER A N   1 
ATOM   432  C CA  . SER A 1 59  ? -17.115 21.585  -8.502  1.00 17.79 ? 59  SER A CA  1 
ATOM   433  C C   . SER A 1 59  ? -15.630 21.861  -8.248  1.00 17.60 ? 59  SER A C   1 
ATOM   434  O O   . SER A 1 59  ? -15.017 21.225  -7.399  1.00 21.82 ? 59  SER A O   1 
ATOM   435  C CB  . SER A 1 59  ? -17.341 20.081  -8.674  1.00 15.79 ? 59  SER A CB  1 
ATOM   436  O OG  . SER A 1 59  ? -16.957 19.665  -9.977  1.00 17.05 ? 59  SER A OG  1 
ATOM   437  N N   . ALA A 1 60  ? -15.060 22.812  -8.979  1.00 21.21 ? 60  ALA A N   1 
ATOM   438  C CA  . ALA A 1 60  ? -13.624 23.074  -8.890  1.00 20.71 ? 60  ALA A CA  1 
ATOM   439  C C   . ALA A 1 60  ? -13.259 23.789  -7.594  1.00 22.24 ? 60  ALA A C   1 
ATOM   440  O O   . ALA A 1 60  ? -12.085 23.914  -7.262  1.00 21.98 ? 60  ALA A O   1 
ATOM   441  C CB  . ALA A 1 60  ? -13.139 23.867  -10.096 1.00 20.33 ? 60  ALA A CB  1 
ATOM   442  N N   . GLY A 1 61  ? -14.270 24.262  -6.872  1.00 26.05 ? 61  GLY A N   1 
ATOM   443  C CA  . GLY A 1 61  ? -14.061 24.799  -5.540  1.00 21.46 ? 61  GLY A CA  1 
ATOM   444  C C   . GLY A 1 61  ? -13.506 26.209  -5.507  1.00 25.65 ? 61  GLY A C   1 
ATOM   445  O O   . GLY A 1 61  ? -13.538 26.924  -6.505  1.00 31.27 ? 61  GLY A O   1 
ATOM   446  N N   . PRO A 1 62  ? -12.987 26.615  -4.340  1.00 35.89 ? 62  PRO A N   1 
ATOM   447  C CA  . PRO A 1 62  ? -12.459 27.960  -4.096  1.00 38.22 ? 62  PRO A CA  1 
ATOM   448  C C   . PRO A 1 62  ? -11.219 28.234  -4.940  1.00 42.52 ? 62  PRO A C   1 
ATOM   449  O O   . PRO A 1 62  ? -10.648 27.309  -5.520  1.00 29.83 ? 62  PRO A O   1 
ATOM   450  C CB  . PRO A 1 62  ? -12.068 27.923  -2.612  1.00 36.44 ? 62  PRO A CB  1 
ATOM   451  C CG  . PRO A 1 62  ? -12.719 26.698  -2.046  1.00 41.83 ? 62  PRO A CG  1 
ATOM   452  C CD  . PRO A 1 62  ? -12.811 25.732  -3.176  1.00 33.56 ? 62  PRO A CD  1 
ATOM   453  N N   . HIS A 1 63  ? -10.815 29.498  -5.005  1.00 36.76 ? 63  HIS A N   1 
ATOM   454  C CA  . HIS A 1 63  ? -9.595  29.880  -5.696  1.00 41.65 ? 63  HIS A CA  1 
ATOM   455  C C   . HIS A 1 63  ? -8.404  29.250  -4.987  1.00 30.80 ? 63  HIS A C   1 
ATOM   456  O O   . HIS A 1 63  ? -8.422  29.074  -3.770  1.00 26.35 ? 63  HIS A O   1 
ATOM   457  C CB  . HIS A 1 63  ? -9.448  31.403  -5.703  1.00 41.91 ? 63  HIS A CB  1 
ATOM   458  C CG  . HIS A 1 63  ? -10.690 32.127  -6.119  1.00 53.05 ? 63  HIS A CG  1 
ATOM   459  N ND1 . HIS A 1 63  ? -11.741 32.357  -5.257  1.00 55.64 ? 63  HIS A ND1 1 
ATOM   460  C CD2 . HIS A 1 63  ? -11.050 32.671  -7.306  1.00 54.09 ? 63  HIS A CD2 1 
ATOM   461  C CE1 . HIS A 1 63  ? -12.696 33.011  -5.895  1.00 49.99 ? 63  HIS A CE1 1 
ATOM   462  N NE2 . HIS A 1 63  ? -12.301 33.216  -7.139  1.00 54.57 ? 63  HIS A NE2 1 
ATOM   463  N N   . PHE A 1 64  ? -7.372  28.901  -5.745  1.00 26.00 ? 64  PHE A N   1 
ATOM   464  C CA  . PHE A 1 64  ? -6.172  28.345  -5.136  1.00 24.12 ? 64  PHE A CA  1 
ATOM   465  C C   . PHE A 1 64  ? -5.419  29.471  -4.439  1.00 28.50 ? 64  PHE A C   1 
ATOM   466  O O   . PHE A 1 64  ? -4.831  30.332  -5.097  1.00 29.16 ? 64  PHE A O   1 
ATOM   467  C CB  . PHE A 1 64  ? -5.301  27.652  -6.181  1.00 22.20 ? 64  PHE A CB  1 
ATOM   468  C CG  . PHE A 1 64  ? -4.078  26.987  -5.606  1.00 21.15 ? 64  PHE A CG  1 
ATOM   469  C CD1 . PHE A 1 64  ? -4.157  26.272  -4.419  1.00 25.40 ? 64  PHE A CD1 1 
ATOM   470  C CD2 . PHE A 1 64  ? -2.861  27.069  -6.253  1.00 20.95 ? 64  PHE A CD2 1 
ATOM   471  C CE1 . PHE A 1 64  ? -3.043  25.656  -3.890  1.00 22.54 ? 64  PHE A CE1 1 
ATOM   472  C CE2 . PHE A 1 64  ? -1.735  26.455  -5.726  1.00 24.30 ? 64  PHE A CE2 1 
ATOM   473  C CZ  . PHE A 1 64  ? -1.829  25.747  -4.544  1.00 18.97 ? 64  PHE A CZ  1 
ATOM   474  N N   . ASN A 1 65  ? -5.448  29.457  -3.107  1.00 31.08 ? 65  ASN A N   1 
ATOM   475  C CA  . ASN A 1 65  ? -5.004  30.593  -2.301  1.00 32.88 ? 65  ASN A CA  1 
ATOM   476  C C   . ASN A 1 65  ? -4.376  30.172  -0.969  1.00 32.98 ? 65  ASN A C   1 
ATOM   477  O O   . ASN A 1 65  ? -4.880  30.520  0.092   1.00 29.70 ? 65  ASN A O   1 
ATOM   478  C CB  . ASN A 1 65  ? -6.201  31.515  -2.038  1.00 34.01 ? 65  ASN A CB  1 
ATOM   479  C CG  . ASN A 1 65  ? -5.821  32.783  -1.298  1.00 34.36 ? 65  ASN A CG  1 
ATOM   480  O OD1 . ASN A 1 65  ? -4.669  33.208  -1.317  1.00 36.73 ? 65  ASN A OD1 1 
ATOM   481  N ND2 . ASN A 1 65  ? -6.802  33.400  -0.647  1.00 38.25 ? 65  ASN A ND2 1 
ATOM   482  N N   . PRO A 1 66  ? -3.265  29.423  -1.025  1.00 31.89 ? 66  PRO A N   1 
ATOM   483  C CA  . PRO A 1 66  ? -2.615  28.872  0.171   1.00 40.53 ? 66  PRO A CA  1 
ATOM   484  C C   . PRO A 1 66  ? -2.275  29.924  1.228   1.00 47.06 ? 66  PRO A C   1 
ATOM   485  O O   . PRO A 1 66  ? -2.283  29.614  2.420   1.00 42.91 ? 66  PRO A O   1 
ATOM   486  C CB  . PRO A 1 66  ? -1.322  28.265  -0.383  1.00 36.66 ? 66  PRO A CB  1 
ATOM   487  C CG  . PRO A 1 66  ? -1.619  27.967  -1.799  1.00 35.82 ? 66  PRO A CG  1 
ATOM   488  C CD  . PRO A 1 66  ? -2.559  29.045  -2.260  1.00 29.72 ? 66  PRO A CD  1 
ATOM   489  N N   . LEU A 1 67  ? -1.981  31.147  0.798   1.00 44.78 ? 67  LEU A N   1 
ATOM   490  C CA  . LEU A 1 67  ? -1.553  32.194  1.724   1.00 46.66 ? 67  LEU A CA  1 
ATOM   491  C C   . LEU A 1 67  ? -2.703  33.049  2.268   1.00 48.86 ? 67  LEU A C   1 
ATOM   492  O O   . LEU A 1 67  ? -2.478  33.984  3.038   1.00 42.57 ? 67  LEU A O   1 
ATOM   493  C CB  . LEU A 1 67  ? -0.493  33.081  1.067   1.00 55.35 ? 67  LEU A CB  1 
ATOM   494  C CG  . LEU A 1 67  ? 0.803   32.368  0.671   1.00 53.95 ? 67  LEU A CG  1 
ATOM   495  C CD1 . LEU A 1 67  ? 1.739   33.316  -0.062  1.00 56.84 ? 67  LEU A CD1 1 
ATOM   496  C CD2 . LEU A 1 67  ? 1.483   31.774  1.898   1.00 52.08 ? 67  LEU A CD2 1 
ATOM   497  N N   . SER A 1 68  ? -3.930  32.723  1.870   1.00 40.31 ? 68  SER A N   1 
ATOM   498  C CA  . SER A 1 68  ? -5.109  33.453  2.335   1.00 46.43 ? 68  SER A CA  1 
ATOM   499  C C   . SER A 1 68  ? -4.996  34.950  2.058   1.00 47.34 ? 68  SER A C   1 
ATOM   500  O O   . SER A 1 68  ? -5.244  35.775  2.939   1.00 52.43 ? 68  SER A O   1 
ATOM   501  C CB  . SER A 1 68  ? -5.340  33.214  3.830   1.00 47.65 ? 68  SER A CB  1 
ATOM   502  O OG  . SER A 1 68  ? -5.627  31.851  4.091   1.00 55.99 ? 68  SER A OG  1 
ATOM   503  N N   . ARG A 1 69  ? -4.626  35.294  0.830   1.00 43.94 ? 69  ARG A N   1 
ATOM   504  C CA  . ARG A 1 69  ? -4.461  36.688  0.446   1.00 41.16 ? 69  ARG A CA  1 
ATOM   505  C C   . ARG A 1 69  ? -5.672  37.182  -0.343  1.00 49.61 ? 69  ARG A C   1 
ATOM   506  O O   . ARG A 1 69  ? -6.605  36.421  -0.603  1.00 44.99 ? 69  ARG A O   1 
ATOM   507  C CB  . ARG A 1 69  ? -3.179  36.858  -0.370  1.00 48.84 ? 69  ARG A CB  1 
ATOM   508  C CG  . ARG A 1 69  ? -2.540  38.229  -0.249  1.00 55.21 ? 69  ARG A CG  1 
ATOM   509  C CD  . ARG A 1 69  ? -1.026  38.129  -0.340  1.00 64.61 ? 69  ARG A CD  1 
ATOM   510  N NE  . ARG A 1 69  ? -0.501  37.099  0.554   1.00 64.77 ? 69  ARG A NE  1 
ATOM   511  C CZ  . ARG A 1 69  ? -0.364  37.249  1.868   1.00 68.41 ? 69  ARG A CZ  1 
ATOM   512  N NH1 . ARG A 1 69  ? -0.716  38.389  2.448   1.00 72.63 ? 69  ARG A NH1 1 
ATOM   513  N NH2 . ARG A 1 69  ? 0.121   36.259  2.604   1.00 67.58 ? 69  ARG A NH2 1 
ATOM   514  N N   . LYS A 1 70  ? -5.659  38.459  -0.712  1.00 50.63 ? 70  LYS A N   1 
ATOM   515  C CA  . LYS A 1 70  ? -6.725  39.030  -1.527  1.00 42.56 ? 70  LYS A CA  1 
ATOM   516  C C   . LYS A 1 70  ? -6.474  38.779  -3.012  1.00 43.21 ? 70  LYS A C   1 
ATOM   517  O O   . LYS A 1 70  ? -5.331  38.671  -3.448  1.00 44.10 ? 70  LYS A O   1 
ATOM   518  C CB  . LYS A 1 70  ? -6.862  40.532  -1.266  1.00 52.07 ? 70  LYS A CB  1 
ATOM   519  C CG  . LYS A 1 70  ? -7.541  40.880  0.051   1.00 51.87 ? 70  LYS A CG  1 
ATOM   520  C CD  . LYS A 1 70  ? -7.747  42.382  0.186   1.00 60.72 ? 70  LYS A CD  1 
ATOM   521  C CE  . LYS A 1 70  ? -8.552  42.725  1.432   1.00 63.90 ? 70  LYS A CE  1 
ATOM   522  N NZ  . LYS A 1 70  ? -9.928  42.156  1.382   1.00 65.31 ? 70  LYS A NZ  1 
ATOM   523  N N   . HIS A 1 71  ? -7.553  38.686  -3.782  1.00 38.35 ? 71  HIS A N   1 
ATOM   524  C CA  . HIS A 1 71  ? -7.451  38.476  -5.221  1.00 41.30 ? 71  HIS A CA  1 
ATOM   525  C C   . HIS A 1 71  ? -6.768  39.663  -5.889  1.00 40.50 ? 71  HIS A C   1 
ATOM   526  O O   . HIS A 1 71  ? -7.008  40.814  -5.525  1.00 36.85 ? 71  HIS A O   1 
ATOM   527  C CB  . HIS A 1 71  ? -8.841  38.252  -5.824  1.00 39.25 ? 71  HIS A CB  1 
ATOM   528  C CG  . HIS A 1 71  ? -8.846  38.169  -7.319  1.00 41.65 ? 71  HIS A CG  1 
ATOM   529  N ND1 . HIS A 1 71  ? -8.341  37.087  -8.006  1.00 40.74 ? 71  HIS A ND1 1 
ATOM   530  C CD2 . HIS A 1 71  ? -9.305  39.030  -8.258  1.00 36.02 ? 71  HIS A CD2 1 
ATOM   531  C CE1 . HIS A 1 71  ? -8.480  37.288  -9.305  1.00 39.05 ? 71  HIS A CE1 1 
ATOM   532  N NE2 . HIS A 1 71  ? -9.062  38.459  -9.484  1.00 39.58 ? 71  HIS A NE2 1 
ATOM   533  N N   . GLY A 1 72  ? -5.912  39.378  -6.867  1.00 39.24 ? 72  GLY A N   1 
ATOM   534  C CA  . GLY A 1 72  ? -5.215  40.427  -7.586  1.00 38.83 ? 72  GLY A CA  1 
ATOM   535  C C   . GLY A 1 72  ? -4.727  39.980  -8.949  1.00 43.70 ? 72  GLY A C   1 
ATOM   536  O O   . GLY A 1 72  ? -5.156  38.947  -9.468  1.00 32.71 ? 72  GLY A O   1 
ATOM   537  N N   . GLY A 1 73  ? -3.831  40.771  -9.531  1.00 43.03 ? 73  GLY A N   1 
ATOM   538  C CA  . GLY A 1 73  ? -3.232  40.438  -10.808 1.00 47.17 ? 73  GLY A CA  1 
ATOM   539  C C   . GLY A 1 73  ? -2.006  39.571  -10.612 1.00 40.50 ? 73  GLY A C   1 
ATOM   540  O O   . GLY A 1 73  ? -1.471  39.496  -9.505  1.00 48.14 ? 73  GLY A O   1 
ATOM   541  N N   . PRO A 1 74  ? -1.556  38.907  -11.687 1.00 41.63 ? 74  PRO A N   1 
ATOM   542  C CA  . PRO A 1 74  ? -0.404  37.999  -11.653 1.00 41.68 ? 74  PRO A CA  1 
ATOM   543  C C   . PRO A 1 74  ? 0.877   38.711  -11.229 1.00 47.30 ? 74  PRO A C   1 
ATOM   544  O O   . PRO A 1 74  ? 1.807   38.069  -10.735 1.00 43.46 ? 74  PRO A O   1 
ATOM   545  C CB  . PRO A 1 74  ? -0.284  37.531  -13.107 1.00 36.04 ? 74  PRO A CB  1 
ATOM   546  C CG  . PRO A 1 74  ? -1.641  37.737  -13.685 1.00 41.92 ? 74  PRO A CG  1 
ATOM   547  C CD  . PRO A 1 74  ? -2.175  38.962  -13.021 1.00 35.23 ? 74  PRO A CD  1 
ATOM   548  N N   . LYS A 1 75  ? 0.921   40.025  -11.421 1.00 47.36 ? 75  LYS A N   1 
ATOM   549  C CA  . LYS A 1 75  ? 2.108   40.802  -11.089 1.00 51.77 ? 75  LYS A CA  1 
ATOM   550  C C   . LYS A 1 75  ? 1.975   41.502  -9.740  1.00 52.85 ? 75  LYS A C   1 
ATOM   551  O O   . LYS A 1 75  ? 2.919   42.134  -9.267  1.00 65.52 ? 75  LYS A O   1 
ATOM   552  C CB  . LYS A 1 75  ? 2.407   41.821  -12.191 1.00 53.16 ? 75  LYS A CB  1 
ATOM   553  C CG  . LYS A 1 75  ? 2.728   41.198  -13.540 1.00 52.55 ? 75  LYS A CG  1 
ATOM   554  C CD  . LYS A 1 75  ? 3.150   42.257  -14.547 1.00 73.04 ? 75  LYS A CD  1 
ATOM   555  C CE  . LYS A 1 75  ? 2.086   43.337  -14.692 1.00 76.57 ? 75  LYS A CE  1 
ATOM   556  N NZ  . LYS A 1 75  ? 2.502   44.409  -15.639 1.00 76.63 ? 75  LYS A NZ  1 
ATOM   557  N N   . ASP A 1 76  ? 0.802   41.387  -9.126  1.00 51.74 ? 76  ASP A N   1 
ATOM   558  C CA  . ASP A 1 76  ? 0.565   41.968  -7.807  1.00 51.57 ? 76  ASP A CA  1 
ATOM   559  C C   . ASP A 1 76  ? 1.198   41.116  -6.711  1.00 52.92 ? 76  ASP A C   1 
ATOM   560  O O   . ASP A 1 76  ? 0.978   39.906  -6.648  1.00 49.04 ? 76  ASP A O   1 
ATOM   561  C CB  . ASP A 1 76  ? -0.936  42.126  -7.545  1.00 58.77 ? 76  ASP A CB  1 
ATOM   562  C CG  . ASP A 1 76  ? -1.544  43.287  -8.310  1.00 63.17 ? 76  ASP A CG  1 
ATOM   563  O OD1 . ASP A 1 76  ? -0.787  44.199  -8.705  1.00 71.06 ? 76  ASP A OD1 1 
ATOM   564  O OD2 . ASP A 1 76  ? -2.778  43.290  -8.510  1.00 61.09 ? 76  ASP A OD2 1 
ATOM   565  N N   . ARG A 1 79  ? -2.038  38.784  -4.367  1.00 39.21 ? 79  ARG A N   1 
ATOM   566  C CA  . ARG A 1 79  ? -2.732  37.896  -5.296  1.00 38.67 ? 79  ARG A CA  1 
ATOM   567  C C   . ARG A 1 79  ? -2.861  36.503  -4.706  1.00 39.36 ? 79  ARG A C   1 
ATOM   568  O O   . ARG A 1 79  ? -2.072  36.110  -3.845  1.00 38.34 ? 79  ARG A O   1 
ATOM   569  C CB  . ARG A 1 79  ? -1.973  37.800  -6.622  1.00 34.85 ? 79  ARG A CB  1 
ATOM   570  C CG  . ARG A 1 79  ? -0.639  37.059  -6.525  1.00 37.76 ? 79  ARG A CG  1 
ATOM   571  C CD  . ARG A 1 79  ? -0.019  36.768  -7.898  1.00 39.20 ? 79  ARG A CD  1 
ATOM   572  N NE  . ARG A 1 79  ? -0.354  35.438  -8.408  1.00 26.56 ? 79  ARG A NE  1 
ATOM   573  C CZ  . ARG A 1 79  ? 0.240   34.864  -9.451  1.00 31.55 ? 79  ARG A CZ  1 
ATOM   574  N NH1 . ARG A 1 79  ? 1.205   35.502  -10.102 1.00 29.79 ? 79  ARG A NH1 1 
ATOM   575  N NH2 . ARG A 1 79  ? -0.126  33.652  -9.847  1.00 25.57 ? 79  ARG A NH2 1 
ATOM   576  N N   . HIS A 1 80  ? -3.859  35.758  -5.168  1.00 33.09 ? 80  HIS A N   1 
ATOM   577  C CA  . HIS A 1 80  ? -3.928  34.339  -4.868  1.00 33.69 ? 80  HIS A CA  1 
ATOM   578  C C   . HIS A 1 80  ? -2.909  33.656  -5.757  1.00 26.85 ? 80  HIS A C   1 
ATOM   579  O O   . HIS A 1 80  ? -2.564  34.169  -6.821  1.00 27.98 ? 80  HIS A O   1 
ATOM   580  C CB  . HIS A 1 80  ? -5.314  33.758  -5.160  1.00 25.87 ? 80  HIS A CB  1 
ATOM   581  C CG  . HIS A 1 80  ? -6.440  34.487  -4.496  1.00 31.56 ? 80  HIS A CG  1 
ATOM   582  N ND1 . HIS A 1 80  ? -7.719  34.497  -5.008  1.00 37.42 ? 80  HIS A ND1 1 
ATOM   583  C CD2 . HIS A 1 80  ? -6.479  35.234  -3.368  1.00 35.10 ? 80  HIS A CD2 1 
ATOM   584  C CE1 . HIS A 1 80  ? -8.500  35.214  -4.221  1.00 38.59 ? 80  HIS A CE1 1 
ATOM   585  N NE2 . HIS A 1 80  ? -7.772  35.673  -3.219  1.00 38.50 ? 80  HIS A NE2 1 
ATOM   586  N N   . VAL A 1 81  ? -2.428  32.497  -5.331  1.00 26.54 ? 81  VAL A N   1 
ATOM   587  C CA  . VAL A 1 81  ? -1.507  31.740  -6.156  1.00 24.92 ? 81  VAL A CA  1 
ATOM   588  C C   . VAL A 1 81  ? -2.150  31.429  -7.509  1.00 24.54 ? 81  VAL A C   1 
ATOM   589  O O   . VAL A 1 81  ? -1.471  31.393  -8.528  1.00 25.09 ? 81  VAL A O   1 
ATOM   590  C CB  . VAL A 1 81  ? -1.067  30.438  -5.467  1.00 23.50 ? 81  VAL A CB  1 
ATOM   591  C CG1 . VAL A 1 81  ? -0.176  29.627  -6.390  1.00 20.06 ? 81  VAL A CG1 1 
ATOM   592  C CG2 . VAL A 1 81  ? -0.344  30.752  -4.156  1.00 27.47 ? 81  VAL A CG2 1 
ATOM   593  N N   . GLY A 1 82  ? -3.465  31.231  -7.515  1.00 20.21 ? 82  GLY A N   1 
ATOM   594  C CA  . GLY A 1 82  ? -4.167  30.829  -8.725  1.00 21.27 ? 82  GLY A CA  1 
ATOM   595  C C   . GLY A 1 82  ? -4.495  31.924  -9.729  1.00 22.60 ? 82  GLY A C   1 
ATOM   596  O O   . GLY A 1 82  ? -4.918  31.630  -10.850 1.00 25.03 ? 82  GLY A O   1 
ATOM   597  N N   . ASP A 1 83  ? -4.305  33.181  -9.340  1.00 22.05 ? 83  ASP A N   1 
ATOM   598  C CA  . ASP A 1 83  ? -4.606  34.313  -10.219 1.00 24.79 ? 83  ASP A CA  1 
ATOM   599  C C   . ASP A 1 83  ? -3.617  34.404  -11.376 1.00 24.94 ? 83  ASP A C   1 
ATOM   600  O O   . ASP A 1 83  ? -2.474  34.825  -11.181 1.00 31.02 ? 83  ASP A O   1 
ATOM   601  C CB  . ASP A 1 83  ? -4.564  35.629  -9.431  1.00 27.07 ? 83  ASP A CB  1 
ATOM   602  C CG  . ASP A 1 83  ? -5.647  35.719  -8.375  1.00 30.27 ? 83  ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 83  ? -6.702  35.073  -8.541  1.00 32.13 ? 83  ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 83  ? -5.441  36.447  -7.380  1.00 34.34 ? 83  ASP A OD2 1 
ATOM   605  N N   . LEU A 1 84  ? -4.053  34.019  -12.575 1.00 22.14 ? 84  LEU A N   1 
ATOM   606  C CA  . LEU A 1 84  ? -3.177  34.058  -13.744 1.00 17.32 ? 84  LEU A CA  1 
ATOM   607  C C   . LEU A 1 84  ? -3.552  35.172  -14.721 1.00 22.56 ? 84  LEU A C   1 
ATOM   608  O O   . LEU A 1 84  ? -3.055  35.216  -15.845 1.00 28.32 ? 84  LEU A O   1 
ATOM   609  C CB  . LEU A 1 84  ? -3.165  32.708  -14.464 1.00 18.82 ? 84  LEU A CB  1 
ATOM   610  C CG  . LEU A 1 84  ? -2.426  31.573  -13.758 1.00 24.39 ? 84  LEU A CG  1 
ATOM   611  C CD1 . LEU A 1 84  ? -2.489  30.306  -14.586 1.00 21.52 ? 84  LEU A CD1 1 
ATOM   612  C CD2 . LEU A 1 84  ? -0.971  31.964  -13.484 1.00 24.17 ? 84  LEU A CD2 1 
ATOM   613  N N   . GLY A 1 85  ? -4.431  36.066  -14.287 1.00 23.36 ? 85  GLY A N   1 
ATOM   614  C CA  . GLY A 1 85  ? -4.782  37.232  -15.076 1.00 23.86 ? 85  GLY A CA  1 
ATOM   615  C C   . GLY A 1 85  ? -5.814  36.960  -16.152 1.00 23.23 ? 85  GLY A C   1 
ATOM   616  O O   . GLY A 1 85  ? -6.785  36.236  -15.935 1.00 22.64 ? 85  GLY A O   1 
ATOM   617  N N   . ASN A 1 86  ? -5.595  37.559  -17.316 1.00 18.69 ? 86  ASN A N   1 
ATOM   618  C CA  . ASN A 1 86  ? -6.522  37.464  -18.441 1.00 21.40 ? 86  ASN A CA  1 
ATOM   619  C C   . ASN A 1 86  ? -5.851  36.909  -19.685 1.00 22.79 ? 86  ASN A C   1 
ATOM   620  O O   . ASN A 1 86  ? -4.661  37.131  -19.906 1.00 21.34 ? 86  ASN A O   1 
ATOM   621  C CB  . ASN A 1 86  ? -7.075  38.848  -18.783 1.00 22.09 ? 86  ASN A CB  1 
ATOM   622  C CG  . ASN A 1 86  ? -8.088  39.334  -17.777 1.00 27.00 ? 86  ASN A CG  1 
ATOM   623  O OD1 . ASN A 1 86  ? -9.151  38.739  -17.621 1.00 22.58 ? 86  ASN A OD1 1 
ATOM   624  N ND2 . ASN A 1 86  ? -7.769  40.429  -17.095 1.00 27.71 ? 86  ASN A ND2 1 
ATOM   625  N N   . VAL A 1 87  ? -6.622  36.193  -20.499 1.00 19.93 ? 87  VAL A N   1 
ATOM   626  C CA  . VAL A 1 87  ? -6.207  35.868  -21.855 1.00 17.50 ? 87  VAL A CA  1 
ATOM   627  C C   . VAL A 1 87  ? -7.096  36.667  -22.797 1.00 19.02 ? 87  VAL A C   1 
ATOM   628  O O   . VAL A 1 87  ? -8.194  37.073  -22.423 1.00 18.35 ? 87  VAL A O   1 
ATOM   629  C CB  . VAL A 1 87  ? -6.349  34.365  -22.176 1.00 20.21 ? 87  VAL A CB  1 
ATOM   630  C CG1 . VAL A 1 87  ? -5.408  33.536  -21.303 1.00 21.27 ? 87  VAL A CG1 1 
ATOM   631  C CG2 . VAL A 1 87  ? -7.795  33.913  -22.016 1.00 20.46 ? 87  VAL A CG2 1 
ATOM   632  N N   . THR A 1 88  ? -6.618  36.896  -24.012 1.00 16.93 ? 88  THR A N   1 
ATOM   633  C CA  . THR A 1 88  ? -7.358  37.697  -24.985 1.00 21.17 ? 88  THR A CA  1 
ATOM   634  C C   . THR A 1 88  ? -7.736  36.875  -26.212 1.00 23.01 ? 88  THR A C   1 
ATOM   635  O O   . THR A 1 88  ? -6.880  36.249  -26.832 1.00 20.61 ? 88  THR A O   1 
ATOM   636  C CB  . THR A 1 88  ? -6.538  38.928  -25.435 1.00 24.19 ? 88  THR A CB  1 
ATOM   637  O OG1 . THR A 1 88  ? -6.136  39.682  -24.286 1.00 30.14 ? 88  THR A OG1 1 
ATOM   638  C CG2 . THR A 1 88  ? -7.362  39.812  -26.352 1.00 24.12 ? 88  THR A CG2 1 
ATOM   639  N N   . ALA A 1 89  ? -9.024  36.876  -26.548 1.00 15.19 ? 89  ALA A N   1 
ATOM   640  C CA  . ALA A 1 89  ? -9.515  36.188  -27.739 1.00 17.56 ? 89  ALA A CA  1 
ATOM   641  C C   . ALA A 1 89  ? -9.703  37.168  -28.895 1.00 16.72 ? 89  ALA A C   1 
ATOM   642  O O   . ALA A 1 89  ? -10.132 38.306  -28.691 1.00 19.50 ? 89  ALA A O   1 
ATOM   643  C CB  . ALA A 1 89  ? -10.822 35.454  -27.430 1.00 17.54 ? 89  ALA A CB  1 
ATOM   644  N N   . ASP A 1 90  ? -9.357  36.726  -30.100 1.00 14.35 ? 90  ASP A N   1 
ATOM   645  C CA  . ASP A 1 90  ? -9.512  37.538  -31.307 1.00 14.85 ? 90  ASP A CA  1 
ATOM   646  C C   . ASP A 1 90  ? -10.931 37.479  -31.856 1.00 16.78 ? 90  ASP A C   1 
ATOM   647  O O   . ASP A 1 90  ? -11.832 36.928  -31.220 1.00 17.06 ? 90  ASP A O   1 
ATOM   648  C CB  . ASP A 1 90  ? -8.504  37.117  -32.386 1.00 15.21 ? 90  ASP A CB  1 
ATOM   649  C CG  . ASP A 1 90  ? -8.726  35.698  -32.885 1.00 15.75 ? 90  ASP A CG  1 
ATOM   650  O OD1 . ASP A 1 90  ? -9.804  35.129  -32.617 1.00 20.09 ? 90  ASP A OD1 1 
ATOM   651  O OD2 . ASP A 1 90  ? -7.825  35.161  -33.573 1.00 18.89 ? 90  ASP A OD2 1 
ATOM   652  N N   . LYS A 1 91  ? -11.122 38.039  -33.049 1.00 19.77 ? 91  LYS A N   1 
ATOM   653  C CA  . LYS A 1 91  ? -12.449 38.138  -33.654 1.00 19.47 ? 91  LYS A CA  1 
ATOM   654  C C   . LYS A 1 91  ? -13.015 36.783  -34.065 1.00 20.67 ? 91  LYS A C   1 
ATOM   655  O O   . LYS A 1 91  ? -14.202 36.671  -34.385 1.00 22.73 ? 91  LYS A O   1 
ATOM   656  C CB  . LYS A 1 91  ? -12.404 39.061  -34.876 1.00 25.78 ? 91  LYS A CB  1 
ATOM   657  C CG  . LYS A 1 91  ? -12.151 40.520  -34.545 1.00 35.47 ? 91  LYS A CG  1 
ATOM   658  C CD  . LYS A 1 91  ? -13.449 41.302  -34.430 1.00 44.87 ? 91  LYS A CD  1 
ATOM   659  C CE  . LYS A 1 91  ? -14.078 41.537  -35.795 1.00 48.72 ? 91  LYS A CE  1 
ATOM   660  N NZ  . LYS A 1 91  ? -15.278 42.416  -35.709 1.00 54.99 ? 91  LYS A NZ  1 
ATOM   661  N N   . ASP A 1 92  ? -12.159 35.767  -34.087 1.00 15.63 ? 92  ASP A N   1 
ATOM   662  C CA  . ASP A 1 92  ? -12.587 34.409  -34.407 1.00 19.13 ? 92  ASP A CA  1 
ATOM   663  C C   . ASP A 1 92  ? -12.782 33.597  -33.125 1.00 14.91 ? 92  ASP A C   1 
ATOM   664  O O   . ASP A 1 92  ? -13.031 32.390  -33.176 1.00 17.90 ? 92  ASP A O   1 
ATOM   665  C CB  . ASP A 1 92  ? -11.575 33.712  -35.322 1.00 21.94 ? 92  ASP A CB  1 
ATOM   666  C CG  . ASP A 1 92  ? -11.569 34.275  -36.744 1.00 27.82 ? 92  ASP A CG  1 
ATOM   667  O OD1 . ASP A 1 92  ? -12.524 34.985  -37.121 1.00 23.74 ? 92  ASP A OD1 1 
ATOM   668  O OD2 . ASP A 1 92  ? -10.605 33.994  -37.490 1.00 25.86 ? 92  ASP A OD2 1 
ATOM   669  N N   . GLY A 1 93  ? -12.647 34.261  -31.982 1.00 16.11 ? 93  GLY A N   1 
ATOM   670  C CA  . GLY A 1 93  ? -12.825 33.617  -30.690 1.00 18.15 ? 93  GLY A CA  1 
ATOM   671  C C   . GLY A 1 93  ? -11.659 32.746  -30.243 1.00 17.78 ? 93  GLY A C   1 
ATOM   672  O O   . GLY A 1 93  ? -11.820 31.865  -29.394 1.00 15.72 ? 93  GLY A O   1 
ATOM   673  N N   . VAL A 1 94  ? -10.482 32.986  -30.812 1.00 18.92 ? 94  VAL A N   1 
ATOM   674  C CA  . VAL A 1 94  ? -9.302  32.194  -30.487 1.00 17.69 ? 94  VAL A CA  1 
ATOM   675  C C   . VAL A 1 94  ? -8.348  33.010  -29.632 1.00 20.46 ? 94  VAL A C   1 
ATOM   676  O O   . VAL A 1 94  ? -7.961  34.118  -30.008 1.00 16.27 ? 94  VAL A O   1 
ATOM   677  C CB  . VAL A 1 94  ? -8.554  31.731  -31.758 1.00 15.77 ? 94  VAL A CB  1 
ATOM   678  C CG1 . VAL A 1 94  ? -7.284  30.961  -31.379 1.00 18.92 ? 94  VAL A CG1 1 
ATOM   679  C CG2 . VAL A 1 94  ? -9.468  30.892  -32.648 1.00 18.31 ? 94  VAL A CG2 1 
ATOM   680  N N   . ALA A 1 95  ? -7.992  32.469  -28.469 1.00 17.11 ? 95  ALA A N   1 
ATOM   681  C CA  . ALA A 1 95  ? -7.040  33.123  -27.583 1.00 15.71 ? 95  ALA A CA  1 
ATOM   682  C C   . ALA A 1 95  ? -5.722  32.367  -27.553 1.00 18.84 ? 95  ALA A C   1 
ATOM   683  O O   . ALA A 1 95  ? -5.685  31.158  -27.309 1.00 20.14 ? 95  ALA A O   1 
ATOM   684  C CB  . ALA A 1 95  ? -7.604  33.252  -26.177 1.00 20.33 ? 95  ALA A CB  1 
ATOM   685  N N   . ASP A 1 96  ? -4.640  33.084  -27.823 1.00 17.56 ? 96  ASP A N   1 
ATOM   686  C CA  . ASP A 1 96  ? -3.314  32.544  -27.597 1.00 19.85 ? 96  ASP A CA  1 
ATOM   687  C C   . ASP A 1 96  ? -2.986  32.704  -26.120 1.00 18.74 ? 96  ASP A C   1 
ATOM   688  O O   . ASP A 1 96  ? -3.266  33.741  -25.523 1.00 23.74 ? 96  ASP A O   1 
ATOM   689  C CB  . ASP A 1 96  ? -2.275  33.288  -28.428 1.00 20.47 ? 96  ASP A CB  1 
ATOM   690  C CG  . ASP A 1 96  ? -0.877  32.740  -28.231 1.00 20.99 ? 96  ASP A CG  1 
ATOM   691  O OD1 . ASP A 1 96  ? -0.681  31.541  -28.501 1.00 20.57 ? 96  ASP A OD1 1 
ATOM   692  O OD2 . ASP A 1 96  ? 0.020   33.508  -27.813 1.00 19.54 ? 96  ASP A OD2 1 
ATOM   693  N N   . VAL A 1 97  ? -2.392  31.676  -25.531 1.00 16.95 ? 97  VAL A N   1 
ATOM   694  C CA  . VAL A 1 97  ? -1.941  31.768  -24.152 1.00 15.61 ? 97  VAL A CA  1 
ATOM   695  C C   . VAL A 1 97  ? -0.420  31.706  -24.109 1.00 15.51 ? 97  VAL A C   1 
ATOM   696  O O   . VAL A 1 97  ? 0.189   30.736  -24.552 1.00 18.88 ? 97  VAL A O   1 
ATOM   697  C CB  . VAL A 1 97  ? -2.543  30.645  -23.274 1.00 15.30 ? 97  VAL A CB  1 
ATOM   698  C CG1 . VAL A 1 97  ? -2.075  30.792  -21.843 1.00 18.98 ? 97  VAL A CG1 1 
ATOM   699  C CG2 . VAL A 1 97  ? -4.064  30.677  -23.347 1.00 18.45 ? 97  VAL A CG2 1 
ATOM   700  N N   . SER A 1 98  ? 0.197   32.766  -23.612 1.00 14.20 ? 98  SER A N   1 
ATOM   701  C CA  . SER A 1 98  ? 1.645   32.754  -23.433 1.00 17.00 ? 98  SER A CA  1 
ATOM   702  C C   . SER A 1 98  ? 1.978   33.524  -22.174 1.00 23.42 ? 98  SER A C   1 
ATOM   703  O O   . SER A 1 98  ? 2.020   34.754  -22.181 1.00 20.39 ? 98  SER A O   1 
ATOM   704  C CB  . SER A 1 98  ? 2.361   33.357  -24.646 1.00 19.93 ? 98  SER A CB  1 
ATOM   705  O OG  . SER A 1 98  ? 3.772   33.307  -24.480 1.00 22.53 ? 98  SER A OG  1 
ATOM   706  N N   . ILE A 1 99  ? 2.195   32.787  -21.088 1.00 18.99 ? 99  ILE A N   1 
ATOM   707  C CA  . ILE A 1 99  ? 2.431   33.376  -19.782 1.00 20.42 ? 99  ILE A CA  1 
ATOM   708  C C   . ILE A 1 99  ? 3.658   32.763  -19.122 1.00 20.69 ? 99  ILE A C   1 
ATOM   709  O O   . ILE A 1 99  ? 3.892   31.561  -19.220 1.00 20.17 ? 99  ILE A O   1 
ATOM   710  C CB  . ILE A 1 99  ? 1.232   33.121  -18.847 1.00 20.46 ? 99  ILE A CB  1 
ATOM   711  C CG1 . ILE A 1 99  ? -0.044  33.728  -19.435 1.00 28.28 ? 99  ILE A CG1 1 
ATOM   712  C CG2 . ILE A 1 99  ? 1.513   33.664  -17.450 1.00 29.64 ? 99  ILE A CG2 1 
ATOM   713  C CD1 . ILE A 1 99  ? -1.296  33.364  -18.671 1.00 23.34 ? 99  ILE A CD1 1 
ATOM   714  N N   . GLU A 1 100 ? 4.443   33.597  -18.457 1.00 20.08 ? 100 GLU A N   1 
ATOM   715  C CA  . GLU A 1 100 ? 5.502   33.103  -17.592 1.00 22.24 ? 100 GLU A CA  1 
ATOM   716  C C   . GLU A 1 100 ? 5.202   33.596  -16.185 1.00 22.38 ? 100 GLU A C   1 
ATOM   717  O O   . GLU A 1 100 ? 5.098   34.800  -15.946 1.00 26.04 ? 100 GLU A O   1 
ATOM   718  C CB  . GLU A 1 100 ? 6.873   33.578  -18.071 1.00 29.68 ? 100 GLU A CB  1 
ATOM   719  C CG  . GLU A 1 100 ? 8.030   32.918  -17.347 1.00 30.97 ? 100 GLU A CG  1 
ATOM   720  C CD  . GLU A 1 100 ? 9.352   33.108  -18.066 1.00 39.65 ? 100 GLU A CD  1 
ATOM   721  O OE1 . GLU A 1 100 ? 10.400  33.137  -17.389 1.00 43.59 ? 100 GLU A OE1 1 
ATOM   722  O OE2 . GLU A 1 100 ? 9.342   33.231  -19.309 1.00 42.57 ? 100 GLU A OE2 1 
ATOM   723  N N   . ASP A 1 101 ? 5.026   32.667  -15.256 1.00 20.51 ? 101 ASP A N   1 
ATOM   724  C CA  . ASP A 1 101 ? 4.610   33.046  -13.912 1.00 18.35 ? 101 ASP A CA  1 
ATOM   725  C C   . ASP A 1 101 ? 5.513   32.436  -12.855 1.00 17.86 ? 101 ASP A C   1 
ATOM   726  O O   . ASP A 1 101 ? 5.857   31.259  -12.926 1.00 18.40 ? 101 ASP A O   1 
ATOM   727  C CB  . ASP A 1 101 ? 3.159   32.640  -13.652 1.00 22.70 ? 101 ASP A CB  1 
ATOM   728  C CG  . ASP A 1 101 ? 2.621   33.221  -12.354 1.00 27.72 ? 101 ASP A CG  1 
ATOM   729  O OD1 . ASP A 1 101 ? 2.157   34.381  -12.369 1.00 33.28 ? 101 ASP A OD1 1 
ATOM   730  O OD2 . ASP A 1 101 ? 2.665   32.521  -11.321 1.00 25.18 ? 101 ASP A OD2 1 
ATOM   731  N N   . SER A 1 102 ? 5.890   33.244  -11.873 1.00 23.64 ? 102 SER A N   1 
ATOM   732  C CA  . SER A 1 102 ? 6.833   32.806  -10.849 1.00 27.81 ? 102 SER A CA  1 
ATOM   733  C C   . SER A 1 102 ? 6.166   32.453  -9.524  1.00 29.43 ? 102 SER A C   1 
ATOM   734  O O   . SER A 1 102 ? 6.848   32.131  -8.553  1.00 25.85 ? 102 SER A O   1 
ATOM   735  C CB  . SER A 1 102 ? 7.894   33.883  -10.618 1.00 30.42 ? 102 SER A CB  1 
ATOM   736  O OG  . SER A 1 102 ? 7.303   35.072  -10.120 1.00 39.27 ? 102 SER A OG  1 
ATOM   737  N N   . VAL A 1 103 ? 4.838   32.507  -9.474  1.00 21.17 ? 103 VAL A N   1 
ATOM   738  C CA  . VAL A 1 103 ? 4.141   32.235  -8.220  1.00 20.57 ? 103 VAL A CA  1 
ATOM   739  C C   . VAL A 1 103 ? 3.555   30.827  -8.206  1.00 19.79 ? 103 VAL A C   1 
ATOM   740  O O   . VAL A 1 103 ? 3.644   30.119  -7.201  1.00 21.76 ? 103 VAL A O   1 
ATOM   741  C CB  . VAL A 1 103 ? 3.054   33.287  -7.919  1.00 24.41 ? 103 VAL A CB  1 
ATOM   742  C CG1 . VAL A 1 103 ? 2.183   32.834  -6.767  1.00 26.41 ? 103 VAL A CG1 1 
ATOM   743  C CG2 . VAL A 1 103 ? 3.701   34.634  -7.611  1.00 27.54 ? 103 VAL A CG2 1 
ATOM   744  N N   . ILE A 1 104 ? 2.959   30.417  -9.320  1.00 20.18 ? 104 ILE A N   1 
ATOM   745  C CA  . ILE A 1 104 ? 2.556   29.024  -9.462  1.00 16.70 ? 104 ILE A CA  1 
ATOM   746  C C   . ILE A 1 104 ? 3.805   28.163  -9.595  1.00 15.75 ? 104 ILE A C   1 
ATOM   747  O O   . ILE A 1 104 ? 4.906   28.673  -9.793  1.00 16.76 ? 104 ILE A O   1 
ATOM   748  C CB  . ILE A 1 104 ? 1.637   28.797  -10.676 1.00 18.16 ? 104 ILE A CB  1 
ATOM   749  C CG1 . ILE A 1 104 ? 2.361   29.157  -11.979 1.00 17.19 ? 104 ILE A CG1 1 
ATOM   750  C CG2 . ILE A 1 104 ? 0.346   29.596  -10.528 1.00 21.11 ? 104 ILE A CG2 1 
ATOM   751  C CD1 . ILE A 1 104 ? 1.634   28.674  -13.210 1.00 16.03 ? 104 ILE A CD1 1 
ATOM   752  N N   . SER A 1 105 ? 3.634   26.852  -9.484  1.00 17.60 ? 105 SER A N   1 
ATOM   753  C CA  . SER A 1 105 ? 4.765   25.942  -9.534  1.00 16.83 ? 105 SER A CA  1 
ATOM   754  C C   . SER A 1 105 ? 4.249   24.562  -9.890  1.00 15.19 ? 105 SER A C   1 
ATOM   755  O O   . SER A 1 105 ? 3.057   24.287  -9.766  1.00 15.57 ? 105 SER A O   1 
ATOM   756  C CB  . SER A 1 105 ? 5.457   25.897  -8.164  1.00 18.80 ? 105 SER A CB  1 
ATOM   757  O OG  . SER A 1 105 ? 6.674   25.168  -8.214  1.00 16.88 ? 105 SER A OG  1 
ATOM   758  N N   . LEU A 1 106 ? 5.149   23.696  -10.320 1.00 14.22 ? 106 LEU A N   1 
ATOM   759  C CA  . LEU A 1 106 ? 4.801   22.311  -10.601 1.00 15.84 ? 106 LEU A CA  1 
ATOM   760  C C   . LEU A 1 106 ? 5.327   21.395  -9.494  1.00 19.30 ? 106 LEU A C   1 
ATOM   761  O O   . LEU A 1 106 ? 5.329   20.170  -9.625  1.00 22.28 ? 106 LEU A O   1 
ATOM   762  C CB  . LEU A 1 106 ? 5.336   21.903  -11.977 1.00 15.64 ? 106 LEU A CB  1 
ATOM   763  C CG  . LEU A 1 106 ? 4.814   22.770  -13.132 1.00 17.15 ? 106 LEU A CG  1 
ATOM   764  C CD1 . LEU A 1 106 ? 5.275   22.222  -14.476 1.00 17.54 ? 106 LEU A CD1 1 
ATOM   765  C CD2 . LEU A 1 106 ? 3.297   22.866  -13.085 1.00 16.92 ? 106 LEU A CD2 1 
ATOM   766  N N   . SER A 1 107 ? 5.779   22.013  -8.407  1.00 17.96 ? 107 SER A N   1 
ATOM   767  C CA  . SER A 1 107 ? 6.150   21.285  -7.193  1.00 18.56 ? 107 SER A CA  1 
ATOM   768  C C   . SER A 1 107 ? 6.051   22.213  -5.984  1.00 21.43 ? 107 SER A C   1 
ATOM   769  O O   . SER A 1 107 ? 5.888   23.424  -6.132  1.00 20.02 ? 107 SER A O   1 
ATOM   770  C CB  . SER A 1 107 ? 7.560   20.709  -7.316  1.00 26.65 ? 107 SER A CB  1 
ATOM   771  O OG  . SER A 1 107 ? 8.539   21.720  -7.173  1.00 28.57 ? 107 SER A OG  1 
ATOM   772  N N   . GLY A 1 108 ? 6.143   21.652  -4.784  1.00 20.38 ? 108 GLY A N   1 
ATOM   773  C CA  . GLY A 1 108 ? 6.070   22.458  -3.576  1.00 26.45 ? 108 GLY A CA  1 
ATOM   774  C C   . GLY A 1 108 ? 4.656   22.859  -3.195  1.00 21.22 ? 108 GLY A C   1 
ATOM   775  O O   . GLY A 1 108 ? 3.687   22.316  -3.721  1.00 22.07 ? 108 GLY A O   1 
ATOM   776  N N   . ASP A 1 109 ? 4.536   23.815  -2.279  1.00 22.59 ? 109 ASP A N   1 
ATOM   777  C CA  . ASP A 1 109 ? 3.226   24.216  -1.759  1.00 26.85 ? 109 ASP A CA  1 
ATOM   778  C C   . ASP A 1 109 ? 2.377   24.972  -2.781  1.00 20.84 ? 109 ASP A C   1 
ATOM   779  O O   . ASP A 1 109 ? 1.154   25.042  -2.654  1.00 23.23 ? 109 ASP A O   1 
ATOM   780  C CB  . ASP A 1 109 ? 3.368   25.045  -0.479  1.00 22.42 ? 109 ASP A CB  1 
ATOM   781  C CG  . ASP A 1 109 ? 4.300   26.228  -0.645  1.00 23.30 ? 109 ASP A CG  1 
ATOM   782  O OD1 . ASP A 1 109 ? 5.347   26.089  -1.315  1.00 28.21 ? 109 ASP A OD1 1 
ATOM   783  O OD2 . ASP A 1 109 ? 3.994   27.301  -0.085  1.00 30.06 ? 109 ASP A OD2 1 
ATOM   784  N N   . HIS A 1 110 ? 3.028   25.546  -3.783  1.00 20.46 ? 110 HIS A N   1 
ATOM   785  C CA  . HIS A 1 110 ? 2.317   26.274  -4.831  1.00 20.22 ? 110 HIS A CA  1 
ATOM   786  C C   . HIS A 1 110 ? 2.081   25.396  -6.056  1.00 17.66 ? 110 HIS A C   1 
ATOM   787  O O   . HIS A 1 110 ? 1.764   25.892  -7.136  1.00 15.90 ? 110 HIS A O   1 
ATOM   788  C CB  . HIS A 1 110 ? 3.094   27.533  -5.219  1.00 22.24 ? 110 HIS A CB  1 
ATOM   789  C CG  . HIS A 1 110 ? 3.048   28.610  -4.182  1.00 23.49 ? 110 HIS A CG  1 
ATOM   790  N ND1 . HIS A 1 110 ? 3.409   29.915  -4.445  1.00 22.86 ? 110 HIS A ND1 1 
ATOM   791  C CD2 . HIS A 1 110 ? 2.663   28.581  -2.884  1.00 24.74 ? 110 HIS A CD2 1 
ATOM   792  C CE1 . HIS A 1 110 ? 3.258   30.640  -3.351  1.00 27.35 ? 110 HIS A CE1 1 
ATOM   793  N NE2 . HIS A 1 110 ? 2.806   29.855  -2.389  1.00 25.78 ? 110 HIS A NE2 1 
ATOM   794  N N   . CYS A 1 111 ? 2.245   24.088  -5.885  1.00 18.98 ? 111 CYS A N   1 
ATOM   795  C CA  . CYS A 1 111 ? 2.034   23.154  -6.982  1.00 17.19 ? 111 CYS A CA  1 
ATOM   796  C C   . CYS A 1 111 ? 0.591   23.198  -7.483  1.00 15.75 ? 111 CYS A C   1 
ATOM   797  O O   . CYS A 1 111 ? -0.352  23.189  -6.684  1.00 18.55 ? 111 CYS A O   1 
ATOM   798  C CB  . CYS A 1 111 ? 2.384   21.725  -6.564  1.00 18.90 ? 111 CYS A CB  1 
ATOM   799  S SG  . CYS A 1 111 ? 2.453   20.643  -7.992  1.00 21.19 ? 111 CYS A SG  1 
ATOM   800  N N   . ILE A 1 112 ? 0.427   23.241  -8.803  1.00 15.20 ? 112 ILE A N   1 
ATOM   801  C CA  . ILE A 1 112 ? -0.907  23.287  -9.413  1.00 14.37 ? 112 ILE A CA  1 
ATOM   802  C C   . ILE A 1 112 ? -1.308  21.988  -10.112 1.00 17.60 ? 112 ILE A C   1 
ATOM   803  O O   . ILE A 1 112 ? -2.428  21.863  -10.625 1.00 16.43 ? 112 ILE A O   1 
ATOM   804  C CB  . ILE A 1 112 ? -1.047  24.461  -10.396 1.00 13.03 ? 112 ILE A CB  1 
ATOM   805  C CG1 . ILE A 1 112 ? -0.005  24.370  -11.515 1.00 16.05 ? 112 ILE A CG1 1 
ATOM   806  C CG2 . ILE A 1 112 ? -0.932  25.790  -9.656  1.00 14.38 ? 112 ILE A CG2 1 
ATOM   807  C CD1 . ILE A 1 112 ? -0.178  25.434  -12.592 1.00 17.15 ? 112 ILE A CD1 1 
ATOM   808  N N   . ILE A 1 113 ? -0.398  21.022  -10.142 1.00 17.21 ? 113 ILE A N   1 
ATOM   809  C CA  . ILE A 1 113 ? -0.722  19.700  -10.669 1.00 15.09 ? 113 ILE A CA  1 
ATOM   810  C C   . ILE A 1 113 ? -1.850  19.060  -9.848  1.00 15.62 ? 113 ILE A C   1 
ATOM   811  O O   . ILE A 1 113 ? -1.795  19.029  -8.613  1.00 15.24 ? 113 ILE A O   1 
ATOM   812  C CB  . ILE A 1 113 ? 0.521   18.792  -10.687 1.00 20.39 ? 113 ILE A CB  1 
ATOM   813  C CG1 . ILE A 1 113 ? 1.498   19.274  -11.766 1.00 19.22 ? 113 ILE A CG1 1 
ATOM   814  C CG2 . ILE A 1 113 ? 0.129   17.338  -10.916 1.00 14.37 ? 113 ILE A CG2 1 
ATOM   815  C CD1 . ILE A 1 113 ? 2.832   18.549  -11.762 1.00 30.53 ? 113 ILE A CD1 1 
ATOM   816  N N   . GLY A 1 114 ? -2.881  18.565  -10.532 1.00 11.91 ? 114 GLY A N   1 
ATOM   817  C CA  . GLY A 1 114 ? -4.020  17.974  -9.853  1.00 14.11 ? 114 GLY A CA  1 
ATOM   818  C C   . GLY A 1 114 ? -5.111  18.973  -9.507  1.00 12.94 ? 114 GLY A C   1 
ATOM   819  O O   . GLY A 1 114 ? -6.151  18.601  -8.960  1.00 12.80 ? 114 GLY A O   1 
ATOM   820  N N   . ARG A 1 115 ? -4.879  20.244  -9.816  1.00 11.23 ? 115 ARG A N   1 
ATOM   821  C CA  . ARG A 1 115 ? -5.893  21.273  -9.603  1.00 13.78 ? 115 ARG A CA  1 
ATOM   822  C C   . ARG A 1 115 ? -6.608  21.641  -10.911 1.00 16.60 ? 115 ARG A C   1 
ATOM   823  O O   . ARG A 1 115 ? -6.228  21.183  -11.983 1.00 16.10 ? 115 ARG A O   1 
ATOM   824  C CB  . ARG A 1 115 ? -5.268  22.492  -8.926  1.00 13.83 ? 115 ARG A CB  1 
ATOM   825  C CG  . ARG A 1 115 ? -4.470  22.098  -7.682  1.00 16.25 ? 115 ARG A CG  1 
ATOM   826  C CD  . ARG A 1 115 ? -4.136  23.267  -6.775  1.00 19.62 ? 115 ARG A CD  1 
ATOM   827  N NE  . ARG A 1 115 ? -3.169  22.872  -5.748  1.00 18.58 ? 115 ARG A NE  1 
ATOM   828  C CZ  . ARG A 1 115 ? -3.491  22.409  -4.544  1.00 20.56 ? 115 ARG A CZ  1 
ATOM   829  N NH1 . ARG A 1 115 ? -4.762  22.284  -4.187  1.00 19.00 ? 115 ARG A NH1 1 
ATOM   830  N NH2 . ARG A 1 115 ? -2.532  22.081  -3.684  1.00 28.11 ? 115 ARG A NH2 1 
ATOM   831  N N   . THR A 1 116 ? -7.656  22.451  -10.818 1.00 15.34 ? 116 THR A N   1 
ATOM   832  C CA  . THR A 1 116 ? -8.457  22.774  -11.995 1.00 11.24 ? 116 THR A CA  1 
ATOM   833  C C   . THR A 1 116 ? -8.081  24.120  -12.608 1.00 14.95 ? 116 THR A C   1 
ATOM   834  O O   . THR A 1 116 ? -8.041  25.134  -11.914 1.00 16.45 ? 116 THR A O   1 
ATOM   835  C CB  . THR A 1 116 ? -9.966  22.782  -11.640 1.00 18.17 ? 116 THR A CB  1 
ATOM   836  O OG1 . THR A 1 116 ? -10.395 21.448  -11.343 1.00 15.79 ? 116 THR A OG1 1 
ATOM   837  C CG2 . THR A 1 116 ? -10.790 23.320  -12.799 1.00 17.73 ? 116 THR A CG2 1 
ATOM   838  N N   . LEU A 1 117 ? -7.806  24.120  -13.911 1.00 17.51 ? 117 LEU A N   1 
ATOM   839  C CA  . LEU A 1 117 ? -7.595  25.352  -14.667 1.00 14.46 ? 117 LEU A CA  1 
ATOM   840  C C   . LEU A 1 117 ? -8.930  25.790  -15.268 1.00 14.17 ? 117 LEU A C   1 
ATOM   841  O O   . LEU A 1 117 ? -9.668  24.967  -15.784 1.00 13.65 ? 117 LEU A O   1 
ATOM   842  C CB  . LEU A 1 117 ? -6.589  25.110  -15.792 1.00 12.93 ? 117 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 117 ? -6.143  26.310  -16.628 1.00 14.21 ? 117 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 117 ? -5.413  27.320  -15.760 1.00 16.78 ? 117 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 117 ? -5.254  25.845  -17.770 1.00 14.00 ? 117 LEU A CD2 1 
ATOM   846  N N   . VAL A 1 118 ? -9.234  27.084  -15.201 1.00 14.33 ? 118 VAL A N   1 
ATOM   847  C CA  . VAL A 1 118 ? -10.536 27.579  -15.647 1.00 14.93 ? 118 VAL A CA  1 
ATOM   848  C C   . VAL A 1 118 ? -10.394 28.828  -16.501 1.00 14.37 ? 118 VAL A C   1 
ATOM   849  O O   . VAL A 1 118 ? -9.562  29.692  -16.219 1.00 15.68 ? 118 VAL A O   1 
ATOM   850  C CB  . VAL A 1 118 ? -11.449 27.937  -14.448 1.00 17.31 ? 118 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 118 ? -12.784 28.483  -14.935 1.00 19.40 ? 118 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 118 ? -11.665 26.730  -13.540 1.00 22.17 ? 118 VAL A CG2 1 
ATOM   853  N N   . VAL A 1 119 ? -11.204 28.921  -17.552 1.00 15.74 ? 119 VAL A N   1 
ATOM   854  C CA  . VAL A 1 119 ? -11.316 30.171  -18.290 1.00 15.52 ? 119 VAL A CA  1 
ATOM   855  C C   . VAL A 1 119 ? -12.721 30.747  -18.088 1.00 18.86 ? 119 VAL A C   1 
ATOM   856  O O   . VAL A 1 119 ? -13.718 30.020  -18.117 1.00 16.09 ? 119 VAL A O   1 
ATOM   857  C CB  . VAL A 1 119 ? -10.951 30.003  -19.787 1.00 16.47 ? 119 VAL A CB  1 
ATOM   858  C CG1 . VAL A 1 119 ? -11.863 28.993  -20.450 1.00 14.42 ? 119 VAL A CG1 1 
ATOM   859  C CG2 . VAL A 1 119 ? -10.983 31.349  -20.501 1.00 16.47 ? 119 VAL A CG2 1 
ATOM   860  N N   . HIS A 1 120 ? -12.790 32.056  -17.870 1.00 15.49 ? 120 HIS A N   1 
ATOM   861  C CA  . HIS A 1 120 ? -14.028 32.689  -17.445 1.00 20.93 ? 120 HIS A CA  1 
ATOM   862  C C   . HIS A 1 120 ? -14.765 33.450  -18.533 1.00 19.49 ? 120 HIS A C   1 
ATOM   863  O O   . HIS A 1 120 ? -14.215 33.752  -19.587 1.00 19.21 ? 120 HIS A O   1 
ATOM   864  C CB  . HIS A 1 120 ? -13.763 33.627  -16.273 1.00 18.53 ? 120 HIS A CB  1 
ATOM   865  C CG  . HIS A 1 120 ? -13.569 32.918  -14.969 1.00 23.04 ? 120 HIS A CG  1 
ATOM   866  N ND1 . HIS A 1 120 ? -14.590 32.734  -14.064 1.00 23.76 ? 120 HIS A ND1 1 
ATOM   867  C CD2 . HIS A 1 120 ? -12.474 32.336  -14.426 1.00 23.13 ? 120 HIS A CD2 1 
ATOM   868  C CE1 . HIS A 1 120 ? -14.131 32.076  -13.014 1.00 23.57 ? 120 HIS A CE1 1 
ATOM   869  N NE2 . HIS A 1 120 ? -12.850 31.823  -13.209 1.00 26.28 ? 120 HIS A NE2 1 
ATOM   870  N N   . GLU A 1 121 ? -16.014 33.780  -18.221 1.00 18.58 ? 121 GLU A N   1 
ATOM   871  C CA  . GLU A 1 121 ? -16.929 34.447  -19.135 1.00 20.53 ? 121 GLU A CA  1 
ATOM   872  C C   . GLU A 1 121 ? -16.498 35.877  -19.438 1.00 23.79 ? 121 GLU A C   1 
ATOM   873  O O   . GLU A 1 121 ? -16.574 36.330  -20.585 1.00 19.45 ? 121 GLU A O   1 
ATOM   874  C CB  . GLU A 1 121 ? -18.334 34.440  -18.528 1.00 21.73 ? 121 GLU A CB  1 
ATOM   875  C CG  . GLU A 1 121 ? -19.350 35.324  -19.225 1.00 26.23 ? 121 GLU A CG  1 
ATOM   876  C CD  . GLU A 1 121 ? -20.585 35.548  -18.364 1.00 30.13 ? 121 GLU A CD  1 
ATOM   877  O OE1 . GLU A 1 121 ? -20.515 35.274  -17.147 1.00 25.16 ? 121 GLU A OE1 1 
ATOM   878  O OE2 . GLU A 1 121 ? -21.618 36.003  -18.898 1.00 31.24 ? 121 GLU A OE2 1 
ATOM   879  N N   . LYS A 1 122 ? -16.043 36.578  -18.405 1.00 23.13 ? 122 LYS A N   1 
ATOM   880  C CA  . LYS A 1 122 ? -15.685 37.984  -18.528 1.00 26.73 ? 122 LYS A CA  1 
ATOM   881  C C   . LYS A 1 122 ? -14.237 38.220  -18.135 1.00 27.08 ? 122 LYS A C   1 
ATOM   882  O O   . LYS A 1 122 ? -13.526 37.292  -17.766 1.00 21.58 ? 122 LYS A O   1 
ATOM   883  C CB  . LYS A 1 122 ? -16.584 38.836  -17.638 1.00 27.80 ? 122 LYS A CB  1 
ATOM   884  C CG  . LYS A 1 122 ? -18.069 38.623  -17.861 1.00 33.48 ? 122 LYS A CG  1 
ATOM   885  C CD  . LYS A 1 122 ? -18.880 39.309  -16.778 1.00 35.43 ? 122 LYS A CD  1 
ATOM   886  C CE  . LYS A 1 122 ? -20.365 39.036  -16.955 1.00 39.86 ? 122 LYS A CE  1 
ATOM   887  N NZ  . LYS A 1 122 ? -21.167 39.580  -15.823 1.00 45.09 ? 122 LYS A NZ  1 
ATOM   888  N N   . ALA A 1 123 ? -13.809 39.475  -18.217 1.00 22.31 ? 123 ALA A N   1 
ATOM   889  C CA  . ALA A 1 123 ? -12.468 39.860  -17.811 1.00 22.71 ? 123 ALA A CA  1 
ATOM   890  C C   . ALA A 1 123 ? -12.330 39.813  -16.292 1.00 23.63 ? 123 ALA A C   1 
ATOM   891  O O   . ALA A 1 123 ? -13.256 40.153  -15.561 1.00 28.25 ? 123 ALA A O   1 
ATOM   892  C CB  . ALA A 1 123 ? -12.145 41.254  -18.319 1.00 23.74 ? 123 ALA A CB  1 
ATOM   893  N N   . ASP A 1 124 ? -11.163 39.386  -15.831 1.00 26.75 ? 124 ASP A N   1 
ATOM   894  C CA  . ASP A 1 124 ? -10.823 39.440  -14.415 1.00 22.20 ? 124 ASP A CA  1 
ATOM   895  C C   . ASP A 1 124 ? -10.306 40.849  -14.123 1.00 27.37 ? 124 ASP A C   1 
ATOM   896  O O   . ASP A 1 124 ? -9.370  41.314  -14.774 1.00 34.46 ? 124 ASP A O   1 
ATOM   897  C CB  . ASP A 1 124 ? -9.746  38.398  -14.123 1.00 24.36 ? 124 ASP A CB  1 
ATOM   898  C CG  . ASP A 1 124 ? -9.241  38.453  -12.698 1.00 34.82 ? 124 ASP A CG  1 
ATOM   899  O OD1 . ASP A 1 124 ? -9.743  39.282  -11.911 1.00 35.36 ? 124 ASP A OD1 1 
ATOM   900  O OD2 . ASP A 1 124 ? -8.332  37.661  -12.374 1.00 25.74 ? 124 ASP A OD2 1 
ATOM   901  N N   . ASP A 1 125 ? -10.921 41.540  -13.167 1.00 27.69 ? 125 ASP A N   1 
ATOM   902  C CA  . ASP A 1 125 ? -10.562 42.936  -12.917 1.00 29.26 ? 125 ASP A CA  1 
ATOM   903  C C   . ASP A 1 125 ? -9.294  43.078  -12.076 1.00 39.29 ? 125 ASP A C   1 
ATOM   904  O O   . ASP A 1 125 ? -8.874  44.190  -11.748 1.00 38.82 ? 125 ASP A O   1 
ATOM   905  C CB  . ASP A 1 125 ? -11.733 43.722  -12.310 1.00 34.13 ? 125 ASP A CB  1 
ATOM   906  C CG  . ASP A 1 125 ? -12.145 43.210  -10.944 1.00 35.26 ? 125 ASP A CG  1 
ATOM   907  O OD1 . ASP A 1 125 ? -11.341 42.509  -10.294 1.00 35.17 ? 125 ASP A OD1 1 
ATOM   908  O OD2 . ASP A 1 125 ? -13.278 43.520  -10.517 1.00 35.78 ? 125 ASP A OD2 1 
ATOM   909  N N   . LEU A 1 126 ? -8.691  41.940  -11.739 1.00 33.32 ? 126 LEU A N   1 
ATOM   910  C CA  . LEU A 1 126 ? -7.416  41.912  -11.028 1.00 38.01 ? 126 LEU A CA  1 
ATOM   911  C C   . LEU A 1 126 ? -7.534  42.488  -9.619  1.00 41.51 ? 126 LEU A C   1 
ATOM   912  O O   . LEU A 1 126 ? -6.541  42.918  -9.029  1.00 37.43 ? 126 LEU A O   1 
ATOM   913  C CB  . LEU A 1 126 ? -6.340  42.666  -11.816 1.00 38.33 ? 126 LEU A CB  1 
ATOM   914  C CG  . LEU A 1 126 ? -6.156  42.281  -13.285 1.00 38.79 ? 126 LEU A CG  1 
ATOM   915  C CD1 . LEU A 1 126 ? -5.058  43.121  -13.927 1.00 32.43 ? 126 LEU A CD1 1 
ATOM   916  C CD2 . LEU A 1 126 ? -5.857  40.793  -13.429 1.00 38.02 ? 126 LEU A CD2 1 
ATOM   917  N N   . GLY A 1 127 ? -8.751  42.490  -9.086  1.00 37.38 ? 127 GLY A N   1 
ATOM   918  C CA  . GLY A 1 127 ? -9.002  43.020  -7.759  1.00 41.03 ? 127 GLY A CA  1 
ATOM   919  C C   . GLY A 1 127 ? -8.964  44.537  -7.707  1.00 46.49 ? 127 GLY A C   1 
ATOM   920  O O   . GLY A 1 127 ? -8.812  45.124  -6.636  1.00 44.15 ? 127 GLY A O   1 
ATOM   921  N N   . LYS A 1 128 ? -9.106  45.173  -8.867  1.00 45.96 ? 128 LYS A N   1 
ATOM   922  C CA  . LYS A 1 128 ? -9.081  46.630  -8.950  1.00 42.37 ? 128 LYS A CA  1 
ATOM   923  C C   . LYS A 1 128 ? -10.459 47.214  -9.262  1.00 45.40 ? 128 LYS A C   1 
ATOM   924  O O   . LYS A 1 128 ? -10.588 48.402  -9.557  1.00 46.62 ? 128 LYS A O   1 
ATOM   925  C CB  . LYS A 1 128 ? -8.065  47.087  -9.997  1.00 47.81 ? 128 LYS A CB  1 
ATOM   926  C CG  . LYS A 1 128 ? -6.626  46.738  -9.657  1.00 44.41 ? 128 LYS A CG  1 
ATOM   927  C CD  . LYS A 1 128 ? -5.673  47.278  -10.710 1.00 60.54 ? 128 LYS A CD  1 
ATOM   928  C CE  . LYS A 1 128 ? -4.224  47.037  -10.321 1.00 74.31 ? 128 LYS A CE  1 
ATOM   929  N NZ  . LYS A 1 128 ? -3.281  47.589  -11.333 1.00 72.03 ? 128 LYS A NZ  1 
ATOM   930  N N   . GLY A 1 129 ? -11.486 46.374  -9.191  1.00 41.52 ? 129 GLY A N   1 
ATOM   931  C CA  . GLY A 1 129 ? -12.846 46.808  -9.452  1.00 38.24 ? 129 GLY A CA  1 
ATOM   932  C C   . GLY A 1 129 ? -13.497 47.436  -8.234  1.00 44.66 ? 129 GLY A C   1 
ATOM   933  O O   . GLY A 1 129 ? -14.661 47.835  -8.277  1.00 49.88 ? 129 GLY A O   1 
ATOM   934  N N   . GLU A 1 133 ? -16.580 41.754  -4.432  1.00 48.31 ? 133 GLU A N   1 
ATOM   935  C CA  . GLU A 1 133 ? -16.426 40.691  -5.420  1.00 51.14 ? 133 GLU A CA  1 
ATOM   936  C C   . GLU A 1 133 ? -15.108 40.802  -6.177  1.00 47.07 ? 133 GLU A C   1 
ATOM   937  O O   . GLU A 1 133 ? -14.546 39.796  -6.607  1.00 42.13 ? 133 GLU A O   1 
ATOM   938  C CB  . GLU A 1 133 ? -17.597 40.690  -6.404  1.00 51.76 ? 133 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 133 ? -18.806 39.918  -5.912  1.00 67.34 ? 133 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 133 ? -18.500 38.449  -5.689  1.00 69.97 ? 133 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 133 ? -17.651 37.902  -6.423  1.00 61.37 ? 133 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 133 ? -19.108 37.842  -4.782  1.00 77.29 ? 133 GLU A OE2 1 
ATOM   943  N N   . SER A 1 134 ? -14.622 42.028  -6.338  1.00 47.17 ? 134 SER A N   1 
ATOM   944  C CA  . SER A 1 134 ? -13.368 42.264  -7.044  1.00 40.57 ? 134 SER A CA  1 
ATOM   945  C C   . SER A 1 134 ? -12.190 41.606  -6.330  1.00 49.22 ? 134 SER A C   1 
ATOM   946  O O   . SER A 1 134 ? -11.348 40.968  -6.962  1.00 41.80 ? 134 SER A O   1 
ATOM   947  C CB  . SER A 1 134 ? -13.118 43.764  -7.200  1.00 44.02 ? 134 SER A CB  1 
ATOM   948  O OG  . SER A 1 134 ? -11.898 44.005  -7.879  1.00 43.34 ? 134 SER A OG  1 
ATOM   949  N N   . THR A 1 135 ? -12.135 41.771  -5.011  1.00 50.19 ? 135 THR A N   1 
ATOM   950  C CA  . THR A 1 135 ? -11.081 41.171  -4.198  1.00 50.41 ? 135 THR A CA  1 
ATOM   951  C C   . THR A 1 135 ? -11.388 39.707  -3.901  1.00 50.54 ? 135 THR A C   1 
ATOM   952  O O   . THR A 1 135 ? -10.747 39.087  -3.053  1.00 51.05 ? 135 THR A O   1 
ATOM   953  C CB  . THR A 1 135 ? -10.907 41.914  -2.860  1.00 47.20 ? 135 THR A CB  1 
ATOM   954  O OG1 . THR A 1 135 ? -12.149 41.911  -2.146  1.00 51.30 ? 135 THR A OG1 1 
ATOM   955  C CG2 . THR A 1 135 ? -10.467 43.350  -3.098  1.00 55.47 ? 135 THR A CG2 1 
ATOM   956  N N   . LYS A 1 136 ? -12.373 39.160  -4.606  1.00 51.82 ? 136 LYS A N   1 
ATOM   957  C CA  . LYS A 1 136 ? -12.781 37.777  -4.401  1.00 48.46 ? 136 LYS A CA  1 
ATOM   958  C C   . LYS A 1 136 ? -12.589 36.952  -5.673  1.00 49.62 ? 136 LYS A C   1 
ATOM   959  O O   . LYS A 1 136 ? -11.720 36.081  -5.736  1.00 45.47 ? 136 LYS A O   1 
ATOM   960  C CB  . LYS A 1 136 ? -14.244 37.720  -3.956  1.00 53.28 ? 136 LYS A CB  1 
ATOM   961  C CG  . LYS A 1 136 ? -14.623 36.447  -3.219  1.00 67.49 ? 136 LYS A CG  1 
ATOM   962  C CD  . LYS A 1 136 ? -13.913 36.357  -1.877  1.00 63.71 ? 136 LYS A CD  1 
ATOM   963  C CE  . LYS A 1 136 ? -14.217 37.569  -1.006  1.00 68.11 ? 136 LYS A CE  1 
ATOM   964  N NZ  . LYS A 1 136 ? -15.668 37.685  -0.691  1.00 64.14 ? 136 LYS A NZ  1 
ATOM   965  N N   . THR A 1 137 ? -13.400 37.240  -6.686  1.00 47.13 ? 137 THR A N   1 
ATOM   966  C CA  . THR A 1 137 ? -13.374 36.480  -7.931  1.00 38.98 ? 137 THR A CA  1 
ATOM   967  C C   . THR A 1 137 ? -12.992 37.349  -9.126  1.00 42.94 ? 137 THR A C   1 
ATOM   968  O O   . THR A 1 137 ? -12.986 36.882  -10.265 1.00 35.98 ? 137 THR A O   1 
ATOM   969  C CB  . THR A 1 137 ? -14.743 35.845  -8.215  1.00 44.86 ? 137 THR A CB  1 
ATOM   970  O OG1 . THR A 1 137 ? -14.641 34.966  -9.343  1.00 56.83 ? 137 THR A OG1 1 
ATOM   971  C CG2 . THR A 1 137 ? -15.773 36.925  -8.510  1.00 45.35 ? 137 THR A CG2 1 
ATOM   972  N N   . GLY A 1 138 ? -12.685 38.615  -8.866  1.00 39.82 ? 138 GLY A N   1 
ATOM   973  C CA  . GLY A 1 138 ? -12.322 39.543  -9.922  1.00 37.07 ? 138 GLY A CA  1 
ATOM   974  C C   . GLY A 1 138 ? -13.471 39.874  -10.856 1.00 34.14 ? 138 GLY A C   1 
ATOM   975  O O   . GLY A 1 138 ? -13.260 40.450  -11.925 1.00 34.34 ? 138 GLY A O   1 
ATOM   976  N N   . ASN A 1 139 ? -14.689 39.509  -10.458 1.00 31.46 ? 139 ASN A N   1 
ATOM   977  C CA  . ASN A 1 139 ? -15.878 39.767  -11.269 1.00 33.07 ? 139 ASN A CA  1 
ATOM   978  C C   . ASN A 1 139 ? -15.792 39.161  -12.673 1.00 29.59 ? 139 ASN A C   1 
ATOM   979  O O   . ASN A 1 139 ? -16.323 39.722  -13.632 1.00 30.92 ? 139 ASN A O   1 
ATOM   980  C CB  . ASN A 1 139 ? -16.148 41.274  -11.367 1.00 34.21 ? 139 ASN A CB  1 
ATOM   981  C CG  . ASN A 1 139 ? -16.671 41.863  -10.067 1.00 37.96 ? 139 ASN A CG  1 
ATOM   982  O OD1 . ASN A 1 139 ? -17.806 41.352  -9.600  1.00 42.98 ? 139 ASN A OD1 1 
ATOM   983  N ND2 . ASN A 1 139 ? -16.060 42.761  -9.487  1.00 41.41 ? 139 ASN A ND2 1 
ATOM   984  N N   . ALA A 1 140 ? -15.135 38.009  -12.781 1.00 24.86 ? 140 ALA A N   1 
ATOM   985  C CA  . ALA A 1 140 ? -14.900 37.365  -14.071 1.00 29.18 ? 140 ALA A CA  1 
ATOM   986  C C   . ALA A 1 140 ? -16.097 36.550  -14.560 1.00 28.14 ? 140 ALA A C   1 
ATOM   987  O O   . ALA A 1 140 ? -16.054 35.955  -15.636 1.00 21.17 ? 140 ALA A O   1 
ATOM   988  C CB  . ALA A 1 140 ? -13.642 36.495  -14.015 1.00 25.98 ? 140 ALA A CB  1 
ATOM   989  N N   . GLY A 1 141 ? -17.163 36.518  -13.767 1.00 29.92 ? 141 GLY A N   1 
ATOM   990  C CA  . GLY A 1 141 ? -18.374 35.824  -14.164 1.00 26.20 ? 141 GLY A CA  1 
ATOM   991  C C   . GLY A 1 141 ? -18.245 34.312  -14.158 1.00 20.50 ? 141 GLY A C   1 
ATOM   992  O O   . GLY A 1 141 ? -17.411 33.751  -13.446 1.00 25.28 ? 141 GLY A O   1 
ATOM   993  N N   A SER A 1 142 ? -19.069 33.655  -14.971 0.50 28.57 ? 142 SER A N   1 
ATOM   994  N N   B SER A 1 142 ? -18.969 33.655  -14.971 0.50 28.57 ? 142 SER A N   1 
ATOM   995  C CA  A SER A 1 142 ? -19.171 32.198  -14.974 0.50 22.98 ? 142 SER A CA  1 
ATOM   996  C CA  B SER A 1 142 ? -19.071 32.198  -14.974 0.50 22.98 ? 142 SER A CA  1 
ATOM   997  C C   A SER A 1 142 ? -17.942 31.498  -15.542 0.50 30.38 ? 142 SER A C   1 
ATOM   998  C C   B SER A 1 142 ? -17.842 31.498  -15.542 0.50 30.38 ? 142 SER A C   1 
ATOM   999  O O   A SER A 1 142 ? -17.158 32.087  -16.291 0.50 23.35 ? 142 SER A O   1 
ATOM   1000 O O   B SER A 1 142 ? -17.058 32.087  -16.291 0.50 23.35 ? 142 SER A O   1 
ATOM   1001 C CB  A SER A 1 142 ? -20.410 31.754  -15.756 0.50 34.94 ? 142 SER A CB  1 
ATOM   1002 C CB  B SER A 1 142 ? -20.310 31.754  -15.756 0.50 34.94 ? 142 SER A CB  1 
ATOM   1003 O OG  A SER A 1 142 ? -21.595 32.237  -15.149 0.50 49.18 ? 142 SER A OG  1 
ATOM   1004 O OG  B SER A 1 142 ? -20.207 32.117  -17.121 0.50 49.18 ? 142 SER A OG  1 
ATOM   1005 N N   . ARG A 1 143 ? -17.802 30.224  -15.189 1.00 24.69 ? 143 ARG A N   1 
ATOM   1006 C CA  . ARG A 1 143 ? -16.723 29.380  -15.693 1.00 24.53 ? 143 ARG A CA  1 
ATOM   1007 C C   . ARG A 1 143 ? -17.135 28.716  -17.004 1.00 24.66 ? 143 ARG A C   1 
ATOM   1008 O O   . ARG A 1 143 ? -18.058 27.905  -17.037 1.00 22.56 ? 143 ARG A O   1 
ATOM   1009 C CB  . ARG A 1 143 ? -16.360 28.322  -14.647 1.00 21.92 ? 143 ARG A CB  1 
ATOM   1010 C CG  . ARG A 1 143 ? -15.927 28.924  -13.320 1.00 20.53 ? 143 ARG A CG  1 
ATOM   1011 C CD  . ARG A 1 143 ? -15.862 27.899  -12.192 1.00 27.63 ? 143 ARG A CD  1 
ATOM   1012 N NE  . ARG A 1 143 ? -15.639 28.565  -10.911 1.00 27.19 ? 143 ARG A NE  1 
ATOM   1013 C CZ  . ARG A 1 143 ? -15.572 27.949  -9.734  1.00 32.73 ? 143 ARG A CZ  1 
ATOM   1014 N NH1 . ARG A 1 143 ? -15.707 26.631  -9.652  1.00 30.35 ? 143 ARG A NH1 1 
ATOM   1015 N NH2 . ARG A 1 143 ? -15.368 28.659  -8.632  1.00 29.48 ? 143 ARG A NH2 1 
ATOM   1016 N N   . LEU A 1 144 ? -16.445 29.059  -18.087 1.00 21.61 ? 144 LEU A N   1 
ATOM   1017 C CA  . LEU A 1 144 ? -16.831 28.578  -19.409 1.00 14.64 ? 144 LEU A CA  1 
ATOM   1018 C C   . LEU A 1 144 ? -16.284 27.193  -19.712 1.00 17.77 ? 144 LEU A C   1 
ATOM   1019 O O   . LEU A 1 144 ? -16.934 26.384  -20.362 1.00 21.35 ? 144 LEU A O   1 
ATOM   1020 C CB  . LEU A 1 144 ? -16.364 29.553  -20.489 1.00 21.73 ? 144 LEU A CB  1 
ATOM   1021 C CG  . LEU A 1 144 ? -16.849 30.991  -20.323 1.00 22.20 ? 144 LEU A CG  1 
ATOM   1022 C CD1 . LEU A 1 144 ? -16.347 31.851  -21.467 1.00 28.62 ? 144 LEU A CD1 1 
ATOM   1023 C CD2 . LEU A 1 144 ? -18.367 31.019  -20.250 1.00 24.57 ? 144 LEU A CD2 1 
ATOM   1024 N N   . ALA A 1 145 ? -15.066 26.932  -19.264 1.00 19.10 ? 145 ALA A N   1 
ATOM   1025 C CA  . ALA A 1 145 ? -14.433 25.655  -19.542 1.00 15.15 ? 145 ALA A CA  1 
ATOM   1026 C C   . ALA A 1 145 ? -13.328 25.439  -18.531 1.00 13.56 ? 145 ALA A C   1 
ATOM   1027 O O   . ALA A 1 145 ? -12.842 26.388  -17.925 1.00 14.46 ? 145 ALA A O   1 
ATOM   1028 C CB  . ALA A 1 145 ? -13.886 25.629  -20.959 1.00 15.86 ? 145 ALA A CB  1 
ATOM   1029 N N   . CYS A 1 146 ? -12.942 24.185  -18.343 1.00 14.37 ? 146 CYS A N   1 
ATOM   1030 C CA  . CYS A 1 146 ? -11.996 23.850  -17.299 1.00 12.21 ? 146 CYS A CA  1 
ATOM   1031 C C   . CYS A 1 146 ? -11.506 22.430  -17.494 1.00 15.29 ? 146 CYS A C   1 
ATOM   1032 O O   . CYS A 1 146 ? -12.096 21.660  -18.246 1.00 16.85 ? 146 CYS A O   1 
ATOM   1033 C CB  . CYS A 1 146 ? -12.684 23.951  -15.940 1.00 16.09 ? 146 CYS A CB  1 
ATOM   1034 S SG  . CYS A 1 146 ? -14.109 22.848  -15.793 1.00 23.29 ? 146 CYS A SG  1 
ATOM   1035 N N   . GLY A 1 147 ? -10.429 22.082  -16.801 1.00 14.95 ? 147 GLY A N   1 
ATOM   1036 C CA  . GLY A 1 147 ? -9.911  20.729  -16.860 1.00 11.97 ? 147 GLY A CA  1 
ATOM   1037 C C   . GLY A 1 147 ? -8.933  20.542  -15.724 1.00 12.56 ? 147 GLY A C   1 
ATOM   1038 O O   . GLY A 1 147 ? -8.489  21.515  -15.130 1.00 15.13 ? 147 GLY A O   1 
ATOM   1039 N N   . VAL A 1 148 ? -8.595  19.297  -15.417 1.00 11.62 ? 148 VAL A N   1 
ATOM   1040 C CA  . VAL A 1 148 ? -7.614  19.038  -14.372 1.00 10.57 ? 148 VAL A CA  1 
ATOM   1041 C C   . VAL A 1 148 ? -6.201  19.085  -14.959 1.00 9.11  ? 148 VAL A C   1 
ATOM   1042 O O   . VAL A 1 148 ? -5.941  18.522  -16.017 1.00 13.99 ? 148 VAL A O   1 
ATOM   1043 C CB  . VAL A 1 148 ? -7.869  17.680  -13.697 1.00 12.94 ? 148 VAL A CB  1 
ATOM   1044 C CG1 . VAL A 1 148 ? -6.872  17.447  -12.563 1.00 15.45 ? 148 VAL A CG1 1 
ATOM   1045 C CG2 . VAL A 1 148 ? -9.306  17.613  -13.180 1.00 16.05 ? 148 VAL A CG2 1 
ATOM   1046 N N   . ILE A 1 149 ? -5.289  19.758  -14.266 1.00 11.01 ? 149 ILE A N   1 
ATOM   1047 C CA  . ILE A 1 149 ? -3.900  19.858  -14.728 1.00 13.64 ? 149 ILE A CA  1 
ATOM   1048 C C   . ILE A 1 149 ? -3.171  18.538  -14.462 1.00 13.23 ? 149 ILE A C   1 
ATOM   1049 O O   . ILE A 1 149 ? -3.122  18.068  -13.327 1.00 14.23 ? 149 ILE A O   1 
ATOM   1050 C CB  . ILE A 1 149 ? -3.180  21.035  -14.033 1.00 14.28 ? 149 ILE A CB  1 
ATOM   1051 C CG1 . ILE A 1 149 ? -3.859  22.350  -14.418 1.00 13.06 ? 149 ILE A CG1 1 
ATOM   1052 C CG2 . ILE A 1 149 ? -1.721  21.092  -14.424 1.00 14.84 ? 149 ILE A CG2 1 
ATOM   1053 C CD1 . ILE A 1 149 ? -3.420  23.527  -13.587 1.00 13.74 ? 149 ILE A CD1 1 
ATOM   1054 N N   . GLY A 1 150 ? -2.607  17.936  -15.508 1.00 13.49 ? 150 GLY A N   1 
ATOM   1055 C CA  . GLY A 1 150 ? -2.010  16.619  -15.375 1.00 11.02 ? 150 GLY A CA  1 
ATOM   1056 C C   . GLY A 1 150 ? -0.536  16.611  -15.715 1.00 17.92 ? 150 GLY A C   1 
ATOM   1057 O O   . GLY A 1 150 ? -0.055  17.510  -16.389 1.00 13.79 ? 150 GLY A O   1 
ATOM   1058 N N   . ILE A 1 151 ? 0.183   15.603  -15.230 1.00 14.33 ? 151 ILE A N   1 
ATOM   1059 C CA  . ILE A 1 151 ? 1.601   15.463  -15.538 1.00 16.80 ? 151 ILE A CA  1 
ATOM   1060 C C   . ILE A 1 151 ? 1.782   15.050  -16.995 1.00 13.02 ? 151 ILE A C   1 
ATOM   1061 O O   . ILE A 1 151 ? 1.045   14.201  -17.507 1.00 15.65 ? 151 ILE A O   1 
ATOM   1062 C CB  . ILE A 1 151 ? 2.261   14.428  -14.614 1.00 13.46 ? 151 ILE A CB  1 
ATOM   1063 C CG1 . ILE A 1 151 ? 2.091   14.843  -13.153 1.00 15.96 ? 151 ILE A CG1 1 
ATOM   1064 C CG2 . ILE A 1 151 ? 3.742   14.274  -14.950 1.00 22.16 ? 151 ILE A CG2 1 
ATOM   1065 C CD1 . ILE A 1 151 ? 2.528   13.780  -12.180 1.00 19.33 ? 151 ILE A CD1 1 
ATOM   1066 N N   . ALA A 1 152 ? 2.764   15.645  -17.668 1.00 14.44 ? 152 ALA A N   1 
ATOM   1067 C CA  . ALA A 1 152 ? 2.953   15.411  -19.094 1.00 18.55 ? 152 ALA A CA  1 
ATOM   1068 C C   . ALA A 1 152 ? 4.417   15.193  -19.455 1.00 19.40 ? 152 ALA A C   1 
ATOM   1069 O O   . ALA A 1 152 ? 5.295   15.353  -18.618 1.00 16.85 ? 152 ALA A O   1 
ATOM   1070 C CB  . ALA A 1 152 ? 2.395   16.580  -19.893 1.00 16.52 ? 152 ALA A CB  1 
ATOM   1071 N N   . GLN A 1 153 ? 4.655   14.828  -20.712 1.00 23.05 ? 153 GLN A N   1 
ATOM   1072 C CA  . GLN A 1 153 ? 6.002   14.736  -21.270 1.00 28.27 ? 153 GLN A CA  1 
ATOM   1073 C C   . GLN A 1 153 ? 6.060   15.550  -22.560 1.00 36.47 ? 153 GLN A C   1 
ATOM   1074 O O   . GLN A 1 153 ? 7.079   16.155  -22.894 1.00 38.08 ? 153 GLN A O   1 
ATOM   1075 C CB  . GLN A 1 153 ? 6.369   13.279  -21.564 1.00 26.03 ? 153 GLN A CB  1 
ATOM   1076 C CG  . GLN A 1 153 ? 5.294   12.521  -22.331 1.00 30.42 ? 153 GLN A CG  1 
ATOM   1077 C CD  . GLN A 1 153 ? 5.739   11.134  -22.769 1.00 34.50 ? 153 GLN A CD  1 
ATOM   1078 O OE1 . GLN A 1 153 ? 6.809   10.660  -22.387 1.00 31.37 ? 153 GLN A OE1 1 
ATOM   1079 N NE2 . GLN A 1 153 ? 4.913   10.479  -23.579 1.00 41.10 ? 153 GLN A NE2 1 
ATOM   1080 O OXT . GLN A 1 153 ? 5.078   15.621  -23.304 1.00 32.64 ? 153 GLN A OXT 1 
ATOM   1081 N N   . ALA B 1 1   ? -2.405  16.434  -0.053  1.00 33.42 ? 1   ALA B N   1 
ATOM   1082 C CA  . ALA B 1 1   ? -3.810  16.079  -0.209  1.00 26.22 ? 1   ALA B CA  1 
ATOM   1083 C C   . ALA B 1 1   ? -4.119  14.780  0.521   1.00 19.97 ? 1   ALA B C   1 
ATOM   1084 O O   . ALA B 1 1   ? -3.260  13.908  0.640   1.00 26.10 ? 1   ALA B O   1 
ATOM   1085 C CB  . ALA B 1 1   ? -4.160  15.946  -1.680  1.00 26.38 ? 1   ALA B CB  1 
ATOM   1086 N N   . THR B 1 2   ? -5.349  14.653  1.003   1.00 16.84 ? 2   THR B N   1 
ATOM   1087 C CA  . THR B 1 2   ? -5.789  13.422  1.641   1.00 16.90 ? 2   THR B CA  1 
ATOM   1088 C C   . THR B 1 2   ? -6.870  12.719  0.828   1.00 15.44 ? 2   THR B C   1 
ATOM   1089 O O   . THR B 1 2   ? -7.201  11.566  1.098   1.00 17.01 ? 2   THR B O   1 
ATOM   1090 C CB  . THR B 1 2   ? -6.311  13.676  3.069   1.00 18.01 ? 2   THR B CB  1 
ATOM   1091 O OG1 . THR B 1 2   ? -7.396  14.613  3.027   1.00 25.15 ? 2   THR B OG1 1 
ATOM   1092 C CG2 . THR B 1 2   ? -5.206  14.240  3.941   1.00 22.89 ? 2   THR B CG2 1 
ATOM   1093 N N   . LYS B 1 3   ? -7.425  13.420  -0.156  1.00 14.75 ? 3   LYS B N   1 
ATOM   1094 C CA  . LYS B 1 3   ? -8.433  12.834  -1.034  1.00 11.88 ? 3   LYS B CA  1 
ATOM   1095 C C   . LYS B 1 3   ? -8.214  13.267  -2.475  1.00 14.78 ? 3   LYS B C   1 
ATOM   1096 O O   . LYS B 1 3   ? -7.786  14.392  -2.731  1.00 13.62 ? 3   LYS B O   1 
ATOM   1097 C CB  . LYS B 1 3   ? -9.840  13.237  -0.592  1.00 17.06 ? 3   LYS B CB  1 
ATOM   1098 C CG  . LYS B 1 3   ? -10.954 12.523  -1.343  1.00 19.78 ? 3   LYS B CG  1 
ATOM   1099 C CD  . LYS B 1 3   ? -12.287 12.707  -0.623  1.00 23.87 ? 3   LYS B CD  1 
ATOM   1100 C CE  . LYS B 1 3   ? -13.382 11.883  -1.283  1.00 31.12 ? 3   LYS B CE  1 
ATOM   1101 N NZ  . LYS B 1 3   ? -14.710 12.132  -0.647  1.00 40.55 ? 3   LYS B NZ  1 
ATOM   1102 N N   . ALA B 1 4   ? -8.516  12.362  -3.403  1.00 12.84 ? 4   ALA B N   1 
ATOM   1103 C CA  . ALA B 1 4   ? -8.460  12.653  -4.832  1.00 10.60 ? 4   ALA B CA  1 
ATOM   1104 C C   . ALA B 1 4   ? -9.724  12.103  -5.488  1.00 12.80 ? 4   ALA B C   1 
ATOM   1105 O O   . ALA B 1 4   ? -10.450 11.300  -4.893  1.00 14.26 ? 4   ALA B O   1 
ATOM   1106 C CB  . ALA B 1 4   ? -7.216  12.043  -5.457  1.00 13.47 ? 4   ALA B CB  1 
ATOM   1107 N N   . VAL B 1 5   ? -9.997  12.542  -6.707  1.00 13.81 ? 5   VAL B N   1 
ATOM   1108 C CA  . VAL B 1 5   ? -11.190 12.092  -7.409  1.00 11.56 ? 5   VAL B CA  1 
ATOM   1109 C C   . VAL B 1 5   ? -10.894 12.110  -8.892  1.00 14.58 ? 5   VAL B C   1 
ATOM   1110 O O   . VAL B 1 5   ? -10.074 12.904  -9.360  1.00 13.01 ? 5   VAL B O   1 
ATOM   1111 C CB  . VAL B 1 5   ? -12.413 12.983  -7.100  1.00 16.65 ? 5   VAL B CB  1 
ATOM   1112 C CG1 . VAL B 1 5   ? -12.222 14.368  -7.705  1.00 16.53 ? 5   VAL B CG1 1 
ATOM   1113 C CG2 . VAL B 1 5   ? -13.708 12.335  -7.607  1.00 15.08 ? 5   VAL B CG2 1 
ATOM   1114 N N   . CYS B 1 6   ? -11.557 11.223  -9.624  1.00 12.57 ? 6   CYS B N   1 
ATOM   1115 C CA  . CYS B 1 6   ? -11.340 11.113  -11.055 1.00 9.82  ? 6   CYS B CA  1 
ATOM   1116 C C   . CYS B 1 6   ? -12.669 10.855  -11.750 1.00 16.75 ? 6   CYS B C   1 
ATOM   1117 O O   . CYS B 1 6   ? -13.444 9.994   -11.326 1.00 14.68 ? 6   CYS B O   1 
ATOM   1118 C CB  . CYS B 1 6   ? -10.360 9.981   -11.355 1.00 13.35 ? 6   CYS B CB  1 
ATOM   1119 S SG  . CYS B 1 6   ? -10.047 9.775   -13.126 1.00 15.54 ? 6   CYS B SG  1 
ATOM   1120 N N   . VAL B 1 7   ? -12.937 11.631  -12.797 1.00 13.42 ? 7   VAL B N   1 
ATOM   1121 C CA  . VAL B 1 7   ? -14.096 11.411  -13.648 1.00 12.02 ? 7   VAL B CA  1 
ATOM   1122 C C   . VAL B 1 7   ? -13.648 10.655  -14.892 1.00 14.33 ? 7   VAL B C   1 
ATOM   1123 O O   . VAL B 1 7   ? -12.848 11.168  -15.680 1.00 15.35 ? 7   VAL B O   1 
ATOM   1124 C CB  . VAL B 1 7   ? -14.740 12.733  -14.097 1.00 17.20 ? 7   VAL B CB  1 
ATOM   1125 C CG1 . VAL B 1 7   ? -15.934 12.453  -15.005 1.00 19.33 ? 7   VAL B CG1 1 
ATOM   1126 C CG2 . VAL B 1 7   ? -15.166 13.559  -12.894 1.00 17.55 ? 7   VAL B CG2 1 
ATOM   1127 N N   . LEU B 1 8   ? -14.138 9.428   -15.048 1.00 12.50 ? 8   LEU B N   1 
ATOM   1128 C CA  . LEU B 1 8   ? -13.821 8.623   -16.221 1.00 14.72 ? 8   LEU B CA  1 
ATOM   1129 C C   . LEU B 1 8   ? -14.796 8.925   -17.346 1.00 18.42 ? 8   LEU B C   1 
ATOM   1130 O O   . LEU B 1 8   ? -16.012 8.936   -17.141 1.00 15.49 ? 8   LEU B O   1 
ATOM   1131 C CB  . LEU B 1 8   ? -13.907 7.136   -15.881 1.00 15.35 ? 8   LEU B CB  1 
ATOM   1132 C CG  . LEU B 1 8   ? -12.979 6.624   -14.782 1.00 17.90 ? 8   LEU B CG  1 
ATOM   1133 C CD1 . LEU B 1 8   ? -13.367 5.206   -14.400 1.00 21.92 ? 8   LEU B CD1 1 
ATOM   1134 C CD2 . LEU B 1 8   ? -11.555 6.683   -15.263 1.00 16.67 ? 8   LEU B CD2 1 
ATOM   1135 N N   . LYS B 1 9   ? -14.254 9.163   -18.535 1.00 14.79 ? 9   LYS B N   1 
ATOM   1136 C CA  . LYS B 1 9   ? -15.069 9.364   -19.729 1.00 18.06 ? 9   LYS B CA  1 
ATOM   1137 C C   . LYS B 1 9   ? -14.312 8.865   -20.958 1.00 18.89 ? 9   LYS B C   1 
ATOM   1138 O O   . LYS B 1 9   ? -13.083 8.833   -20.981 1.00 15.33 ? 9   LYS B O   1 
ATOM   1139 C CB  . LYS B 1 9   ? -15.425 10.844  -19.886 1.00 20.56 ? 9   LYS B CB  1 
ATOM   1140 C CG  . LYS B 1 9   ? -16.197 11.176  -21.152 1.00 36.76 ? 9   LYS B CG  1 
ATOM   1141 C CD  . LYS B 1 9   ? -16.522 12.661  -21.231 1.00 47.65 ? 9   LYS B CD  1 
ATOM   1142 C CE  . LYS B 1 9   ? -17.021 13.047  -22.617 1.00 48.88 ? 9   LYS B CE  1 
ATOM   1143 N NZ  . LYS B 1 9   ? -18.202 12.238  -23.036 1.00 42.33 ? 9   LYS B NZ  1 
ATOM   1144 N N   . GLY B 1 10  ? -15.045 8.467   -21.986 1.00 18.91 ? 10  GLY B N   1 
ATOM   1145 C CA  . GLY B 1 10  ? -14.402 7.988   -23.192 1.00 20.44 ? 10  GLY B CA  1 
ATOM   1146 C C   . GLY B 1 10  ? -15.233 8.288   -24.416 1.00 23.96 ? 10  GLY B C   1 
ATOM   1147 O O   . GLY B 1 10  ? -16.203 9.043   -24.347 1.00 21.36 ? 10  GLY B O   1 
ATOM   1148 N N   . ASP B 1 11  ? -14.846 7.697   -25.540 1.00 20.01 ? 11  ASP B N   1 
ATOM   1149 C CA  . ASP B 1 11  ? -15.595 7.859   -26.785 1.00 27.02 ? 11  ASP B CA  1 
ATOM   1150 C C   . ASP B 1 11  ? -16.897 7.059   -26.783 1.00 28.47 ? 11  ASP B C   1 
ATOM   1151 O O   . ASP B 1 11  ? -17.806 7.337   -27.568 1.00 32.94 ? 11  ASP B O   1 
ATOM   1152 C CB  . ASP B 1 11  ? -14.729 7.459   -27.980 1.00 26.79 ? 11  ASP B CB  1 
ATOM   1153 C CG  . ASP B 1 11  ? -13.610 8.446   -28.239 1.00 38.60 ? 11  ASP B CG  1 
ATOM   1154 O OD1 . ASP B 1 11  ? -13.788 9.638   -27.901 1.00 36.06 ? 11  ASP B OD1 1 
ATOM   1155 O OD2 . ASP B 1 11  ? -12.559 8.035   -28.777 1.00 35.23 ? 11  ASP B OD2 1 
ATOM   1156 N N   . GLY B 1 12  ? -16.975 6.062   -25.907 1.00 24.01 ? 12  GLY B N   1 
ATOM   1157 C CA  . GLY B 1 12  ? -18.156 5.225   -25.794 1.00 23.53 ? 12  GLY B CA  1 
ATOM   1158 C C   . GLY B 1 12  ? -19.000 5.588   -24.588 1.00 23.09 ? 12  GLY B C   1 
ATOM   1159 O O   . GLY B 1 12  ? -18.963 6.731   -24.126 1.00 18.63 ? 12  GLY B O   1 
ATOM   1160 N N   . PRO B 1 13  ? -19.769 4.614   -24.072 1.00 22.61 ? 13  PRO B N   1 
ATOM   1161 C CA  . PRO B 1 13  ? -20.708 4.796   -22.959 1.00 23.05 ? 13  PRO B CA  1 
ATOM   1162 C C   . PRO B 1 13  ? -20.078 4.614   -21.579 1.00 20.50 ? 13  PRO B C   1 
ATOM   1163 O O   . PRO B 1 13  ? -20.774 4.793   -20.583 1.00 20.54 ? 13  PRO B O   1 
ATOM   1164 C CB  . PRO B 1 13  ? -21.725 3.678   -23.186 1.00 21.84 ? 13  PRO B CB  1 
ATOM   1165 C CG  . PRO B 1 13  ? -20.932 2.597   -23.842 1.00 21.20 ? 13  PRO B CG  1 
ATOM   1166 C CD  . PRO B 1 13  ? -19.836 3.252   -24.632 1.00 25.83 ? 13  PRO B CD  1 
ATOM   1167 N N   . VAL B 1 14  ? -18.802 4.249   -21.513 1.00 16.55 ? 14  VAL B N   1 
ATOM   1168 C CA  . VAL B 1 14  ? -18.185 4.000   -20.211 1.00 14.59 ? 14  VAL B CA  1 
ATOM   1169 C C   . VAL B 1 14  ? -17.972 5.304   -19.456 1.00 15.78 ? 14  VAL B C   1 
ATOM   1170 O O   . VAL B 1 14  ? -17.312 6.214   -19.944 1.00 19.56 ? 14  VAL B O   1 
ATOM   1171 C CB  . VAL B 1 14  ? -16.849 3.246   -20.313 1.00 17.84 ? 14  VAL B CB  1 
ATOM   1172 C CG1 . VAL B 1 14  ? -16.265 3.035   -18.909 1.00 19.23 ? 14  VAL B CG1 1 
ATOM   1173 C CG2 . VAL B 1 14  ? -17.045 1.909   -21.033 1.00 19.10 ? 14  VAL B CG2 1 
ATOM   1174 N N   . GLN B 1 15  ? -18.537 5.387   -18.259 1.00 20.02 ? 15  GLN B N   1 
ATOM   1175 C CA  . GLN B 1 15  ? -18.383 6.580   -17.439 1.00 19.62 ? 15  GLN B CA  1 
ATOM   1176 C C   . GLN B 1 15  ? -18.392 6.201   -15.969 1.00 18.81 ? 15  GLN B C   1 
ATOM   1177 O O   . GLN B 1 15  ? -19.065 5.256   -15.568 1.00 20.75 ? 15  GLN B O   1 
ATOM   1178 C CB  . GLN B 1 15  ? -19.493 7.587   -17.743 1.00 26.44 ? 15  GLN B CB  1 
ATOM   1179 C CG  . GLN B 1 15  ? -20.891 7.024   -17.601 1.00 29.69 ? 15  GLN B CG  1 
ATOM   1180 C CD  . GLN B 1 15  ? -21.956 7.935   -18.200 1.00 37.89 ? 15  GLN B CD  1 
ATOM   1181 O OE1 . GLN B 1 15  ? -21.701 9.238   -18.180 1.00 30.74 ? 15  GLN B OE1 1 
ATOM   1182 N NE2 . GLN B 1 15  ? -22.992 7.469   -18.675 1.00 30.05 ? 15  GLN B NE2 1 
ATOM   1183 N N   . GLY B 1 16  ? -17.637 6.935   -15.165 1.00 18.69 ? 16  GLY B N   1 
ATOM   1184 C CA  . GLY B 1 16  ? -17.589 6.644   -13.748 1.00 16.57 ? 16  GLY B CA  1 
ATOM   1185 C C   . GLY B 1 16  ? -16.967 7.753   -12.934 1.00 15.78 ? 16  GLY B C   1 
ATOM   1186 O O   . GLY B 1 16  ? -16.367 8.682   -13.477 1.00 15.50 ? 16  GLY B O   1 
ATOM   1187 N N   . ILE B 1 17  ? -17.158 7.666   -11.622 1.00 15.39 ? 17  ILE B N   1 
ATOM   1188 C CA  . ILE B 1 17  ? -16.473 8.537   -10.686 1.00 20.88 ? 17  ILE B CA  1 
ATOM   1189 C C   . ILE B 1 17  ? -15.771 7.639   -9.685  1.00 13.69 ? 17  ILE B C   1 
ATOM   1190 O O   . ILE B 1 17  ? -16.397 6.760   -9.084  1.00 16.11 ? 17  ILE B O   1 
ATOM   1191 C CB  . ILE B 1 17  ? -17.444 9.456   -9.923  1.00 20.46 ? 17  ILE B CB  1 
ATOM   1192 C CG1 . ILE B 1 17  ? -18.190 10.380  -10.886 1.00 21.55 ? 17  ILE B CG1 1 
ATOM   1193 C CG2 . ILE B 1 17  ? -16.688 10.283  -8.894  1.00 20.37 ? 17  ILE B CG2 1 
ATOM   1194 C CD1 . ILE B 1 17  ? -17.307 11.389  -11.556 1.00 30.35 ? 17  ILE B CD1 1 
ATOM   1195 N N   . ILE B 1 18  ? -14.471 7.851   -9.520  1.00 14.35 ? 18  ILE B N   1 
ATOM   1196 C CA  . ILE B 1 18  ? -13.679 7.075   -8.582  1.00 15.15 ? 18  ILE B CA  1 
ATOM   1197 C C   . ILE B 1 18  ? -13.040 8.024   -7.579  1.00 18.52 ? 18  ILE B C   1 
ATOM   1198 O O   . ILE B 1 18  ? -12.477 9.055   -7.963  1.00 15.52 ? 18  ILE B O   1 
ATOM   1199 C CB  . ILE B 1 18  ? -12.583 6.267   -9.303  1.00 16.31 ? 18  ILE B CB  1 
ATOM   1200 C CG1 . ILE B 1 18  ? -13.210 5.252   -10.262 1.00 17.49 ? 18  ILE B CG1 1 
ATOM   1201 C CG2 . ILE B 1 18  ? -11.684 5.562   -8.289  1.00 16.86 ? 18  ILE B CG2 1 
ATOM   1202 C CD1 . ILE B 1 18  ? -14.100 4.222   -9.567  1.00 17.84 ? 18  ILE B CD1 1 
ATOM   1203 N N   . ASN B 1 19  ? -13.157 7.673   -6.299  1.00 13.20 ? 19  ASN B N   1 
ATOM   1204 C CA  . ASN B 1 19  ? -12.613 8.448   -5.196  1.00 15.15 ? 19  ASN B CA  1 
ATOM   1205 C C   . ASN B 1 19  ? -11.393 7.755   -4.621  1.00 14.47 ? 19  ASN B C   1 
ATOM   1206 O O   . ASN B 1 19  ? -11.307 6.527   -4.638  1.00 15.42 ? 19  ASN B O   1 
ATOM   1207 C CB  . ASN B 1 19  ? -13.663 8.592   -4.086  1.00 14.81 ? 19  ASN B CB  1 
ATOM   1208 C CG  . ASN B 1 19  ? -14.970 9.169   -4.590  1.00 16.89 ? 19  ASN B CG  1 
ATOM   1209 O OD1 . ASN B 1 19  ? -15.942 8.442   -4.809  1.00 22.30 ? 19  ASN B OD1 1 
ATOM   1210 N ND2 . ASN B 1 19  ? -15.002 10.481  -4.780  1.00 17.26 ? 19  ASN B ND2 1 
ATOM   1211 N N   . PHE B 1 20  ? -10.454 8.551   -4.119  1.00 13.11 ? 20  PHE B N   1 
ATOM   1212 C CA  . PHE B 1 20  ? -9.268  8.041   -3.444  1.00 14.02 ? 20  PHE B CA  1 
ATOM   1213 C C   . PHE B 1 20  ? -9.140  8.779   -2.129  1.00 15.62 ? 20  PHE B C   1 
ATOM   1214 O O   . PHE B 1 20  ? -9.236  10.005  -2.090  1.00 15.50 ? 20  PHE B O   1 
ATOM   1215 C CB  . PHE B 1 20  ? -8.001  8.324   -4.256  1.00 13.19 ? 20  PHE B CB  1 
ATOM   1216 C CG  . PHE B 1 20  ? -8.018  7.766   -5.660  1.00 16.02 ? 20  PHE B CG  1 
ATOM   1217 C CD1 . PHE B 1 20  ? -8.674  8.433   -6.681  1.00 17.95 ? 20  PHE B CD1 1 
ATOM   1218 C CD2 . PHE B 1 20  ? -7.343  6.593   -5.957  1.00 15.23 ? 20  PHE B CD2 1 
ATOM   1219 C CE1 . PHE B 1 20  ? -8.677  7.926   -7.974  1.00 17.41 ? 20  PHE B CE1 1 
ATOM   1220 C CE2 . PHE B 1 20  ? -7.341  6.081   -7.237  1.00 16.02 ? 20  PHE B CE2 1 
ATOM   1221 C CZ  . PHE B 1 20  ? -8.017  6.749   -8.253  1.00 16.37 ? 20  PHE B CZ  1 
ATOM   1222 N N   . GLU B 1 21  ? -8.915  8.049   -1.045  1.00 18.52 ? 21  GLU B N   1 
ATOM   1223 C CA  . GLU B 1 21  ? -8.681  8.710   0.232   1.00 14.02 ? 21  GLU B CA  1 
ATOM   1224 C C   . GLU B 1 21  ? -7.503  8.095   0.966   1.00 15.08 ? 21  GLU B C   1 
ATOM   1225 O O   . GLU B 1 21  ? -7.367  6.873   1.037   1.00 15.61 ? 21  GLU B O   1 
ATOM   1226 C CB  . GLU B 1 21  ? -9.932  8.701   1.101   1.00 18.94 ? 21  GLU B CB  1 
ATOM   1227 C CG  . GLU B 1 21  ? -9.821  9.619   2.306   1.00 16.89 ? 21  GLU B CG  1 
ATOM   1228 C CD  . GLU B 1 21  ? -11.172 9.927   2.899   1.00 27.27 ? 21  GLU B CD  1 
ATOM   1229 O OE1 . GLU B 1 21  ? -11.799 8.999   3.444   1.00 24.05 ? 21  GLU B OE1 1 
ATOM   1230 O OE2 . GLU B 1 21  ? -11.606 11.093  2.811   1.00 34.13 ? 21  GLU B OE2 1 
ATOM   1231 N N   . GLN B 1 22  ? -6.642  8.963   1.486   1.00 13.33 ? 22  GLN B N   1 
ATOM   1232 C CA  . GLN B 1 22  ? -5.448  8.553   2.208   1.00 12.30 ? 22  GLN B CA  1 
ATOM   1233 C C   . GLN B 1 22  ? -5.285  9.483   3.400   1.00 16.06 ? 22  GLN B C   1 
ATOM   1234 O O   . GLN B 1 22  ? -4.572  10.482  3.330   1.00 18.38 ? 22  GLN B O   1 
ATOM   1235 C CB  . GLN B 1 22  ? -4.215  8.618   1.297   1.00 14.18 ? 22  GLN B CB  1 
ATOM   1236 C CG  . GLN B 1 22  ? -2.968  8.025   1.941   1.00 13.86 ? 22  GLN B CG  1 
ATOM   1237 C CD  . GLN B 1 22  ? -1.752  8.100   1.046   1.00 16.16 ? 22  GLN B CD  1 
ATOM   1238 O OE1 . GLN B 1 22  ? -1.642  9.184   0.289   1.00 18.16 ? 22  GLN B OE1 1 
ATOM   1239 N NE2 . GLN B 1 22  ? -0.924  7.189   1.029   1.00 11.87 ? 22  GLN B NE2 1 
ATOM   1240 N N   . LYS B 1 23  ? -5.976  9.168   4.490   1.00 15.69 ? 23  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 23  ? -5.967  10.031  5.669   1.00 18.27 ? 23  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 23  ? -4.586  10.130  6.299   1.00 15.97 ? 23  LYS B C   1 
ATOM   1243 O O   . LYS B 1 23  ? -4.280  11.115  6.976   1.00 17.86 ? 23  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 23  ? -6.964  9.535   6.714   1.00 17.75 ? 23  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 23  ? -8.432  9.703   6.325   1.00 26.35 ? 23  LYS B CG  1 
ATOM   1246 C CD  . LYS B 1 23  ? -8.818  11.169  6.226   1.00 29.55 ? 23  LYS B CD  1 
ATOM   1247 C CE  . LYS B 1 23  ? -10.326 11.349  6.316   1.00 32.36 ? 23  LYS B CE  1 
ATOM   1248 N NZ  . LYS B 1 23  ? -10.718 12.787  6.280   1.00 33.74 ? 23  LYS B NZ  1 
ATOM   1249 N N   . GLU B 1 24  ? -3.762  9.108   6.095   1.00 15.81 ? 24  GLU B N   1 
ATOM   1250 C CA  . GLU B 1 24  ? -2.414  9.110   6.674   1.00 16.69 ? 24  GLU B CA  1 
ATOM   1251 C C   . GLU B 1 24  ? -1.310  9.065   5.620   1.00 15.30 ? 24  GLU B C   1 
ATOM   1252 O O   . GLU B 1 24  ? -1.306  8.192   4.766   1.00 17.61 ? 24  GLU B O   1 
ATOM   1253 C CB  . GLU B 1 24  ? -2.235  7.947   7.659   1.00 16.06 ? 24  GLU B CB  1 
ATOM   1254 C CG  . GLU B 1 24  ? -3.213  7.943   8.842   1.00 16.97 ? 24  GLU B CG  1 
ATOM   1255 C CD  . GLU B 1 24  ? -4.465  7.123   8.568   1.00 23.43 ? 24  GLU B CD  1 
ATOM   1256 O OE1 . GLU B 1 24  ? -4.456  6.302   7.625   1.00 21.55 ? 24  GLU B OE1 1 
ATOM   1257 O OE2 . GLU B 1 24  ? -5.459  7.291   9.304   1.00 26.07 ? 24  GLU B OE2 1 
ATOM   1258 N N   . SER B 1 25  ? -0.352  9.987   5.711   1.00 17.17 ? 25  SER B N   1 
ATOM   1259 C CA  . SER B 1 25  ? 0.772   9.990   4.776   1.00 14.59 ? 25  SER B CA  1 
ATOM   1260 C C   . SER B 1 25  ? 1.401   8.603   4.708   1.00 15.48 ? 25  SER B C   1 
ATOM   1261 O O   . SER B 1 25  ? 1.647   7.969   5.739   1.00 18.12 ? 25  SER B O   1 
ATOM   1262 C CB  . SER B 1 25  ? 1.826   11.028  5.175   1.00 17.46 ? 25  SER B CB  1 
ATOM   1263 O OG  . SER B 1 25  ? 1.349   12.348  4.970   1.00 22.08 ? 25  SER B OG  1 
ATOM   1264 N N   . ASN B 1 26  ? 1.642   8.137   3.487   1.00 17.59 ? 26  ASN B N   1 
ATOM   1265 C CA  . ASN B 1 26  ? 2.255   6.834   3.240   1.00 21.75 ? 26  ASN B CA  1 
ATOM   1266 C C   . ASN B 1 26  ? 1.385   5.649   3.658   1.00 18.82 ? 26  ASN B C   1 
ATOM   1267 O O   . ASN B 1 26  ? 1.802   4.496   3.544   1.00 21.46 ? 26  ASN B O   1 
ATOM   1268 C CB  . ASN B 1 26  ? 3.630   6.757   3.910   1.00 20.93 ? 26  ASN B CB  1 
ATOM   1269 C CG  . ASN B 1 26  ? 4.545   7.878   3.477   1.00 20.35 ? 26  ASN B CG  1 
ATOM   1270 O OD1 . ASN B 1 26  ? 4.643   8.191   2.289   1.00 23.07 ? 26  ASN B OD1 1 
ATOM   1271 N ND2 . ASN B 1 26  ? 5.222   8.495   4.437   1.00 18.94 ? 26  ASN B ND2 1 
ATOM   1272 N N   . GLY B 1 27  ? 0.173   5.941   4.118   1.00 18.98 ? 27  GLY B N   1 
ATOM   1273 C CA  . GLY B 1 27  ? -0.752  4.908   4.558   1.00 19.48 ? 27  GLY B CA  1 
ATOM   1274 C C   . GLY B 1 27  ? -1.512  4.300   3.393   1.00 19.78 ? 27  GLY B C   1 
ATOM   1275 O O   . GLY B 1 27  ? -1.328  4.708   2.248   1.00 19.04 ? 27  GLY B O   1 
ATOM   1276 N N   . PRO B 1 28  ? -2.365  3.305   3.676   1.00 20.72 ? 28  PRO B N   1 
ATOM   1277 C CA  . PRO B 1 28  ? -3.168  2.711   2.605   1.00 19.28 ? 28  PRO B CA  1 
ATOM   1278 C C   . PRO B 1 28  ? -4.106  3.736   1.989   1.00 16.51 ? 28  PRO B C   1 
ATOM   1279 O O   . PRO B 1 28  ? -4.554  4.667   2.660   1.00 17.60 ? 28  PRO B O   1 
ATOM   1280 C CB  . PRO B 1 28  ? -3.972  1.630   3.331   1.00 21.46 ? 28  PRO B CB  1 
ATOM   1281 C CG  . PRO B 1 28  ? -3.125  1.278   4.520   1.00 30.15 ? 28  PRO B CG  1 
ATOM   1282 C CD  . PRO B 1 28  ? -2.516  2.581   4.949   1.00 25.18 ? 28  PRO B CD  1 
ATOM   1283 N N   . VAL B 1 29  ? -4.398  3.553   0.709   1.00 18.77 ? 29  VAL B N   1 
ATOM   1284 C CA  . VAL B 1 29  ? -5.325  4.420   0.006   1.00 17.51 ? 29  VAL B CA  1 
ATOM   1285 C C   . VAL B 1 29  ? -6.624  3.662   -0.216  1.00 21.98 ? 29  VAL B C   1 
ATOM   1286 O O   . VAL B 1 29  ? -6.620  2.573   -0.792  1.00 17.58 ? 29  VAL B O   1 
ATOM   1287 C CB  . VAL B 1 29  ? -4.769  4.834   -1.375  1.00 17.52 ? 29  VAL B CB  1 
ATOM   1288 C CG1 . VAL B 1 29  ? -5.746  5.756   -2.091  1.00 18.79 ? 29  VAL B CG1 1 
ATOM   1289 C CG2 . VAL B 1 29  ? -3.400  5.501   -1.236  1.00 17.27 ? 29  VAL B CG2 1 
ATOM   1290 N N   . LYS B 1 30  ? -7.730  4.231   0.253   1.00 15.95 ? 30  LYS B N   1 
ATOM   1291 C CA  . LYS B 1 30  ? -9.043  3.686   -0.064  1.00 15.77 ? 30  LYS B CA  1 
ATOM   1292 C C   . LYS B 1 30  ? -9.475  4.148   -1.459  1.00 16.41 ? 30  LYS B C   1 
ATOM   1293 O O   . LYS B 1 30  ? -9.410  5.338   -1.775  1.00 18.00 ? 30  LYS B O   1 
ATOM   1294 C CB  . LYS B 1 30  ? -10.077 4.126   0.974   1.00 17.59 ? 30  LYS B CB  1 
ATOM   1295 C CG  . LYS B 1 30  ? -9.786  3.676   2.402   1.00 28.17 ? 30  LYS B CG  1 
ATOM   1296 C CD  . LYS B 1 30  ? -9.967  2.173   2.562   1.00 36.26 ? 30  LYS B CD  1 
ATOM   1297 C CE  . LYS B 1 30  ? -10.051 1.776   4.033   1.00 38.40 ? 30  LYS B CE  1 
ATOM   1298 N NZ  . LYS B 1 30  ? -8.839  2.195   4.796   1.00 42.61 ? 30  LYS B NZ  1 
ATOM   1299 N N   . VAL B 1 31  ? -9.915  3.205   -2.286  1.00 13.20 ? 31  VAL B N   1 
ATOM   1300 C CA  . VAL B 1 31  ? -10.413 3.515   -3.626  1.00 17.24 ? 31  VAL B CA  1 
ATOM   1301 C C   . VAL B 1 31  ? -11.848 3.019   -3.778  1.00 18.15 ? 31  VAL B C   1 
ATOM   1302 O O   . VAL B 1 31  ? -12.135 1.833   -3.586  1.00 17.07 ? 31  VAL B O   1 
ATOM   1303 C CB  . VAL B 1 31  ? -9.533  2.874   -4.716  1.00 17.15 ? 31  VAL B CB  1 
ATOM   1304 C CG1 . VAL B 1 31  ? -9.968  3.343   -6.105  1.00 18.34 ? 31  VAL B CG1 1 
ATOM   1305 C CG2 . VAL B 1 31  ? -8.064  3.206   -4.466  1.00 15.48 ? 31  VAL B CG2 1 
ATOM   1306 N N   . TRP B 1 32  ? -12.759 3.922   -4.115  1.00 14.21 ? 32  TRP B N   1 
ATOM   1307 C CA  . TRP B 1 32  ? -14.146 3.506   -4.275  1.00 16.54 ? 32  TRP B CA  1 
ATOM   1308 C C   . TRP B 1 32  ? -14.921 4.362   -5.264  1.00 19.46 ? 32  TRP B C   1 
ATOM   1309 O O   . TRP B 1 32  ? -14.577 5.512   -5.527  1.00 18.31 ? 32  TRP B O   1 
ATOM   1310 C CB  . TRP B 1 32  ? -14.854 3.487   -2.917  1.00 17.03 ? 32  TRP B CB  1 
ATOM   1311 C CG  . TRP B 1 32  ? -15.267 4.837   -2.414  1.00 18.91 ? 32  TRP B CG  1 
ATOM   1312 C CD1 . TRP B 1 32  ? -16.482 5.439   -2.585  1.00 19.13 ? 32  TRP B CD1 1 
ATOM   1313 C CD2 . TRP B 1 32  ? -14.473 5.748   -1.646  1.00 18.46 ? 32  TRP B CD2 1 
ATOM   1314 N NE1 . TRP B 1 32  ? -16.490 6.668   -1.977  1.00 18.93 ? 32  TRP B NE1 1 
ATOM   1315 C CE2 . TRP B 1 32  ? -15.272 6.880   -1.389  1.00 20.01 ? 32  TRP B CE2 1 
ATOM   1316 C CE3 . TRP B 1 32  ? -13.168 5.715   -1.147  1.00 19.46 ? 32  TRP B CE3 1 
ATOM   1317 C CZ2 . TRP B 1 32  ? -14.804 7.971   -0.661  1.00 17.91 ? 32  TRP B CZ2 1 
ATOM   1318 C CZ3 . TRP B 1 32  ? -12.709 6.801   -0.419  1.00 20.55 ? 32  TRP B CZ3 1 
ATOM   1319 C CH2 . TRP B 1 32  ? -13.522 7.913   -0.187  1.00 16.27 ? 32  TRP B CH2 1 
ATOM   1320 N N   . GLY B 1 33  ? -15.984 3.785   -5.804  1.00 17.23 ? 33  GLY B N   1 
ATOM   1321 C CA  . GLY B 1 33  ? -16.868 4.512   -6.688  1.00 19.35 ? 33  GLY B CA  1 
ATOM   1322 C C   . GLY B 1 33  ? -17.638 3.530   -7.537  1.00 21.96 ? 33  GLY B C   1 
ATOM   1323 O O   . GLY B 1 33  ? -17.814 2.375   -7.149  1.00 21.84 ? 33  GLY B O   1 
ATOM   1324 N N   . SER B 1 34  ? -18.091 3.990   -8.696  1.00 21.90 ? 34  SER B N   1 
ATOM   1325 C CA  . SER B 1 34  ? -18.839 3.140   -9.612  1.00 22.73 ? 34  SER B CA  1 
ATOM   1326 C C   . SER B 1 34  ? -18.556 3.520   -11.058 1.00 21.14 ? 34  SER B C   1 
ATOM   1327 O O   . SER B 1 34  ? -18.422 4.700   -11.387 1.00 19.19 ? 34  SER B O   1 
ATOM   1328 C CB  . SER B 1 34  ? -20.340 3.229   -9.330  1.00 20.37 ? 34  SER B CB  1 
ATOM   1329 O OG  . SER B 1 34  ? -21.069 2.442   -10.256 1.00 30.37 ? 34  SER B OG  1 
ATOM   1330 N N   . ILE B 1 35  ? -18.457 2.510   -11.914 1.00 17.74 ? 35  ILE B N   1 
ATOM   1331 C CA  . ILE B 1 35  ? -18.256 2.721   -13.341 1.00 14.63 ? 35  ILE B CA  1 
ATOM   1332 C C   . ILE B 1 35  ? -19.388 2.002   -14.065 1.00 18.26 ? 35  ILE B C   1 
ATOM   1333 O O   . ILE B 1 35  ? -19.684 0.846   -13.765 1.00 20.70 ? 35  ILE B O   1 
ATOM   1334 C CB  . ILE B 1 35  ? -16.908 2.147   -13.804 1.00 20.37 ? 35  ILE B CB  1 
ATOM   1335 C CG1 . ILE B 1 35  ? -15.778 2.662   -12.907 1.00 18.87 ? 35  ILE B CG1 1 
ATOM   1336 C CG2 . ILE B 1 35  ? -16.646 2.474   -15.282 1.00 14.74 ? 35  ILE B CG2 1 
ATOM   1337 C CD1 . ILE B 1 35  ? -14.440 1.986   -13.158 1.00 23.98 ? 35  ILE B CD1 1 
ATOM   1338 N N   . LYS B 1 36  ? -20.028 2.685   -15.003 1.00 21.15 ? 36  LYS B N   1 
ATOM   1339 C CA  . LYS B 1 36  ? -21.113 2.075   -15.767 1.00 17.85 ? 36  LYS B CA  1 
ATOM   1340 C C   . LYS B 1 36  ? -20.831 2.109   -17.263 1.00 19.02 ? 36  LYS B C   1 
ATOM   1341 O O   . LYS B 1 36  ? -19.889 2.765   -17.715 1.00 20.73 ? 36  LYS B O   1 
ATOM   1342 C CB  . LYS B 1 36  ? -22.444 2.760   -15.459 1.00 19.15 ? 36  LYS B CB  1 
ATOM   1343 C CG  . LYS B 1 36  ? -22.486 4.228   -15.827 1.00 20.47 ? 36  LYS B CG  1 
ATOM   1344 C CD  . LYS B 1 36  ? -23.769 4.880   -15.327 1.00 23.58 ? 36  LYS B CD  1 
ATOM   1345 C CE  . LYS B 1 36  ? -23.807 6.355   -15.694 1.00 25.20 ? 36  LYS B CE  1 
ATOM   1346 N NZ  . LYS B 1 36  ? -24.923 7.069   -15.014 1.00 25.37 ? 36  LYS B NZ  1 
ATOM   1347 N N   . GLY B 1 37  ? -21.656 1.394   -18.025 1.00 21.43 ? 37  GLY B N   1 
ATOM   1348 C CA  . GLY B 1 37  ? -21.515 1.329   -19.468 1.00 20.15 ? 37  GLY B CA  1 
ATOM   1349 C C   . GLY B 1 37  ? -20.578 0.238   -19.955 1.00 20.60 ? 37  GLY B C   1 
ATOM   1350 O O   . GLY B 1 37  ? -20.213 0.204   -21.130 1.00 20.30 ? 37  GLY B O   1 
ATOM   1351 N N   . LEU B 1 38  ? -20.194 -0.661  -19.055 1.00 19.28 ? 38  LEU B N   1 
ATOM   1352 C CA  . LEU B 1 38  ? -19.238 -1.721  -19.370 1.00 17.64 ? 38  LEU B CA  1 
ATOM   1353 C C   . LEU B 1 38  ? -19.957 -3.009  -19.752 1.00 27.05 ? 38  LEU B C   1 
ATOM   1354 O O   . LEU B 1 38  ? -21.141 -3.176  -19.464 1.00 24.91 ? 38  LEU B O   1 
ATOM   1355 C CB  . LEU B 1 38  ? -18.353 -2.001  -18.152 1.00 22.93 ? 38  LEU B CB  1 
ATOM   1356 C CG  . LEU B 1 38  ? -17.400 -0.900  -17.689 1.00 17.69 ? 38  LEU B CG  1 
ATOM   1357 C CD1 . LEU B 1 38  ? -17.039 -1.085  -16.225 1.00 21.47 ? 38  LEU B CD1 1 
ATOM   1358 C CD2 . LEU B 1 38  ? -16.148 -0.898  -18.550 1.00 17.47 ? 38  LEU B CD2 1 
ATOM   1359 N N   . THR B 1 39  ? -19.232 -3.922  -20.393 1.00 24.70 ? 39  THR B N   1 
ATOM   1360 C CA  . THR B 1 39  ? -19.736 -5.271  -20.623 1.00 26.26 ? 39  THR B CA  1 
ATOM   1361 C C   . THR B 1 39  ? -19.593 -6.094  -19.342 1.00 26.67 ? 39  THR B C   1 
ATOM   1362 O O   . THR B 1 39  ? -18.628 -5.927  -18.596 1.00 25.38 ? 39  THR B O   1 
ATOM   1363 C CB  . THR B 1 39  ? -18.974 -5.973  -21.756 1.00 28.28 ? 39  THR B CB  1 
ATOM   1364 O OG1 . THR B 1 39  ? -17.568 -5.945  -21.474 1.00 21.26 ? 39  THR B OG1 1 
ATOM   1365 C CG2 . THR B 1 39  ? -19.229 -5.278  -23.086 1.00 25.02 ? 39  THR B CG2 1 
ATOM   1366 N N   . GLU B 1 40  ? -20.554 -6.979  -19.088 1.00 24.34 ? 40  GLU B N   1 
ATOM   1367 C CA  . GLU B 1 40  ? -20.526 -7.821  -17.896 1.00 28.78 ? 40  GLU B CA  1 
ATOM   1368 C C   . GLU B 1 40  ? -19.199 -8.563  -17.776 1.00 28.91 ? 40  GLU B C   1 
ATOM   1369 O O   . GLU B 1 40  ? -18.715 -9.136  -18.749 1.00 27.55 ? 40  GLU B O   1 
ATOM   1370 C CB  . GLU B 1 40  ? -21.680 -8.828  -17.920 1.00 29.29 ? 40  GLU B CB  1 
ATOM   1371 C CG  . GLU B 1 40  ? -21.733 -9.741  -16.695 1.00 32.27 ? 40  GLU B CG  1 
ATOM   1372 C CD  . GLU B 1 40  ? -22.958 -10.642 -16.684 1.00 38.36 ? 40  GLU B CD  1 
ATOM   1373 O OE1 . GLU B 1 40  ? -23.696 -10.658 -17.691 1.00 41.02 ? 40  GLU B OE1 1 
ATOM   1374 O OE2 . GLU B 1 40  ? -23.183 -11.333 -15.668 1.00 33.26 ? 40  GLU B OE2 1 
ATOM   1375 N N   . GLY B 1 41  ? -18.612 -8.550  -16.582 1.00 27.52 ? 41  GLY B N   1 
ATOM   1376 C CA  . GLY B 1 41  ? -17.361 -9.253  -16.359 1.00 31.19 ? 41  GLY B CA  1 
ATOM   1377 C C   . GLY B 1 41  ? -16.199 -8.363  -15.954 1.00 24.92 ? 41  GLY B C   1 
ATOM   1378 O O   . GLY B 1 41  ? -16.392 -7.214  -15.561 1.00 23.38 ? 41  GLY B O   1 
ATOM   1379 N N   . LEU B 1 42  ? -14.987 -8.897  -16.071 1.00 26.95 ? 42  LEU B N   1 
ATOM   1380 C CA  . LEU B 1 42  ? -13.786 -8.220  -15.583 1.00 23.35 ? 42  LEU B CA  1 
ATOM   1381 C C   . LEU B 1 42  ? -13.202 -7.194  -16.557 1.00 23.29 ? 42  LEU B C   1 
ATOM   1382 O O   . LEU B 1 42  ? -13.155 -7.418  -17.767 1.00 26.79 ? 42  LEU B O   1 
ATOM   1383 C CB  . LEU B 1 42  ? -12.710 -9.247  -15.234 1.00 28.75 ? 42  LEU B CB  1 
ATOM   1384 C CG  . LEU B 1 42  ? -13.074 -10.326 -14.217 1.00 36.21 ? 42  LEU B CG  1 
ATOM   1385 C CD1 . LEU B 1 42  ? -11.936 -11.319 -14.091 1.00 38.80 ? 42  LEU B CD1 1 
ATOM   1386 C CD2 . LEU B 1 42  ? -13.395 -9.707  -12.872 1.00 36.95 ? 42  LEU B CD2 1 
ATOM   1387 N N   . HIS B 1 43  ? -12.737 -6.077  -16.004 1.00 21.07 ? 43  HIS B N   1 
ATOM   1388 C CA  . HIS B 1 43  ? -12.085 -5.033  -16.784 1.00 19.49 ? 43  HIS B CA  1 
ATOM   1389 C C   . HIS B 1 43  ? -10.843 -4.499  -16.077 1.00 20.44 ? 43  HIS B C   1 
ATOM   1390 O O   . HIS B 1 43  ? -10.890 -4.137  -14.904 1.00 21.44 ? 43  HIS B O   1 
ATOM   1391 C CB  . HIS B 1 43  ? -13.055 -3.891  -17.066 1.00 18.31 ? 43  HIS B CB  1 
ATOM   1392 C CG  . HIS B 1 43  ? -14.234 -4.298  -17.895 1.00 21.05 ? 43  HIS B CG  1 
ATOM   1393 N ND1 . HIS B 1 43  ? -14.204 -4.314  -19.272 1.00 21.32 ? 43  HIS B ND1 1 
ATOM   1394 C CD2 . HIS B 1 43  ? -15.469 -4.723  -17.540 1.00 24.21 ? 43  HIS B CD2 1 
ATOM   1395 C CE1 . HIS B 1 43  ? -15.374 -4.721  -19.731 1.00 23.60 ? 43  HIS B CE1 1 
ATOM   1396 N NE2 . HIS B 1 43  ? -16.160 -4.974  -18.700 1.00 21.64 ? 43  HIS B NE2 1 
ATOM   1397 N N   . GLY B 1 44  ? -9.732  -4.452  -16.799 1.00 20.10 ? 44  GLY B N   1 
ATOM   1398 C CA  . GLY B 1 44  ? -8.500  -3.928  -16.242 1.00 18.53 ? 44  GLY B CA  1 
ATOM   1399 C C   . GLY B 1 44  ? -8.678  -2.526  -15.697 1.00 17.89 ? 44  GLY B C   1 
ATOM   1400 O O   . GLY B 1 44  ? -9.354  -1.696  -16.293 1.00 16.57 ? 44  GLY B O   1 
ATOM   1401 N N   . PHE B 1 45  ? -8.048  -2.268  -14.559 1.00 19.90 ? 45  PHE B N   1 
ATOM   1402 C CA  . PHE B 1 45  ? -8.181  -1.009  -13.839 1.00 17.22 ? 45  PHE B CA  1 
ATOM   1403 C C   . PHE B 1 45  ? -6.757  -0.561  -13.522 1.00 20.72 ? 45  PHE B C   1 
ATOM   1404 O O   . PHE B 1 45  ? -6.034  -1.256  -12.810 1.00 22.43 ? 45  PHE B O   1 
ATOM   1405 C CB  . PHE B 1 45  ? -8.991  -1.270  -12.566 1.00 19.00 ? 45  PHE B CB  1 
ATOM   1406 C CG  . PHE B 1 45  ? -9.510  -0.033  -11.886 1.00 20.03 ? 45  PHE B CG  1 
ATOM   1407 C CD1 . PHE B 1 45  ? -9.999  1.036   -12.621 1.00 20.51 ? 45  PHE B CD1 1 
ATOM   1408 C CD2 . PHE B 1 45  ? -9.549  0.037   -10.502 1.00 21.82 ? 45  PHE B CD2 1 
ATOM   1409 C CE1 . PHE B 1 45  ? -10.493 2.159   -11.983 1.00 17.08 ? 45  PHE B CE1 1 
ATOM   1410 C CE2 . PHE B 1 45  ? -10.039 1.159   -9.860  1.00 19.46 ? 45  PHE B CE2 1 
ATOM   1411 C CZ  . PHE B 1 45  ? -10.506 2.223   -10.601 1.00 19.40 ? 45  PHE B CZ  1 
ATOM   1412 N N   . ARG B 1 46  ? -6.342  0.581   -14.068 1.00 15.66 ? 46  ARG B N   1 
ATOM   1413 C CA  . ARG B 1 46  ? -4.935  0.973   -14.029 1.00 20.38 ? 46  ARG B CA  1 
ATOM   1414 C C   . ARG B 1 46  ? -4.718  2.477   -13.934 1.00 17.29 ? 46  ARG B C   1 
ATOM   1415 O O   . ARG B 1 46  ? -5.554  3.258   -14.370 1.00 17.91 ? 46  ARG B O   1 
ATOM   1416 C CB  . ARG B 1 46  ? -4.223  0.480   -15.293 1.00 23.64 ? 46  ARG B CB  1 
ATOM   1417 C CG  . ARG B 1 46  ? -4.150  -1.025  -15.435 1.00 29.27 ? 46  ARG B CG  1 
ATOM   1418 C CD  . ARG B 1 46  ? -3.275  -1.403  -16.616 1.00 31.90 ? 46  ARG B CD  1 
ATOM   1419 N NE  . ARG B 1 46  ? -3.323  -2.835  -16.882 1.00 41.69 ? 46  ARG B NE  1 
ATOM   1420 C CZ  . ARG B 1 46  ? -2.856  -3.400  -17.988 1.00 43.61 ? 46  ARG B CZ  1 
ATOM   1421 N NH1 . ARG B 1 46  ? -2.305  -2.649  -18.932 1.00 40.84 ? 46  ARG B NH1 1 
ATOM   1422 N NH2 . ARG B 1 46  ? -2.943  -4.715  -18.151 1.00 52.74 ? 46  ARG B NH2 1 
ATOM   1423 N N   . VAL B 1 47  ? -3.575  2.872   -13.380 1.00 13.82 ? 47  VAL B N   1 
ATOM   1424 C CA  . VAL B 1 47  ? -3.142  4.265   -13.426 1.00 12.97 ? 47  VAL B CA  1 
ATOM   1425 C C   . VAL B 1 47  ? -2.022  4.388   -14.450 1.00 21.48 ? 47  VAL B C   1 
ATOM   1426 O O   . VAL B 1 47  ? -1.041  3.641   -14.394 1.00 17.14 ? 47  VAL B O   1 
ATOM   1427 C CB  . VAL B 1 47  ? -2.612  4.752   -12.067 1.00 17.06 ? 47  VAL B CB  1 
ATOM   1428 C CG1 . VAL B 1 47  ? -2.149  6.201   -12.169 1.00 16.74 ? 47  VAL B CG1 1 
ATOM   1429 C CG2 . VAL B 1 47  ? -3.674  4.609   -10.993 1.00 16.95 ? 47  VAL B CG2 1 
ATOM   1430 N N   . GLN B 1 48  ? -2.173  5.325   -15.381 1.00 14.41 ? 48  GLN B N   1 
ATOM   1431 C CA  . GLN B 1 48  ? -1.155  5.574   -16.399 1.00 15.52 ? 48  GLN B CA  1 
ATOM   1432 C C   . GLN B 1 48  ? -0.223  6.693   -15.960 1.00 17.70 ? 48  GLN B C   1 
ATOM   1433 O O   . GLN B 1 48  ? -0.597  7.534   -15.148 1.00 21.51 ? 48  GLN B O   1 
ATOM   1434 C CB  . GLN B 1 48  ? -1.807  5.933   -17.735 1.00 21.04 ? 48  GLN B CB  1 
ATOM   1435 C CG  . GLN B 1 48  ? -2.771  4.877   -18.232 1.00 16.67 ? 48  GLN B CG  1 
ATOM   1436 C CD  . GLN B 1 48  ? -2.098  3.536   -18.441 1.00 26.03 ? 48  GLN B CD  1 
ATOM   1437 O OE1 . GLN B 1 48  ? -2.553  2.530   -17.708 1.00 27.72 ? 48  GLN B OE1 1 
ATOM   1438 N NE2 . GLN B 1 48  ? -1.182  3.402   -19.259 1.00 25.71 ? 48  GLN B NE2 1 
ATOM   1439 N N   . GLU B 1 49  ? 0.986   6.712   -16.520 1.00 15.00 ? 49  GLU B N   1 
ATOM   1440 C CA  . GLU B 1 49  ? 2.021   7.640   -16.081 1.00 15.22 ? 49  GLU B CA  1 
ATOM   1441 C C   . GLU B 1 49  ? 1.627   9.108   -16.209 1.00 14.47 ? 49  GLU B C   1 
ATOM   1442 O O   . GLU B 1 49  ? 1.915   9.917   -15.323 1.00 18.09 ? 49  GLU B O   1 
ATOM   1443 C CB  . GLU B 1 49  ? 3.308   7.398   -16.875 1.00 14.51 ? 49  GLU B CB  1 
ATOM   1444 C CG  . GLU B 1 49  ? 4.472   8.272   -16.448 1.00 15.01 ? 49  GLU B CG  1 
ATOM   1445 C CD  . GLU B 1 49  ? 5.746   7.874   -17.140 1.00 18.19 ? 49  GLU B CD  1 
ATOM   1446 O OE1 . GLU B 1 49  ? 5.659   7.022   -18.049 1.00 19.77 ? 49  GLU B OE1 1 
ATOM   1447 O OE2 . GLU B 1 49  ? 6.823   8.399   -16.775 1.00 16.83 ? 49  GLU B OE2 1 
ATOM   1448 N N   . PHE B 1 50  ? 0.981   9.462   -17.309 1.00 15.35 ? 50  PHE B N   1 
ATOM   1449 C CA  . PHE B 1 50  ? 0.725   10.872  -17.574 1.00 13.99 ? 50  PHE B CA  1 
ATOM   1450 C C   . PHE B 1 50  ? -0.747  11.267  -17.461 1.00 17.59 ? 50  PHE B C   1 
ATOM   1451 O O   . PHE B 1 50  ? -1.639  10.507  -17.836 1.00 22.78 ? 50  PHE B O   1 
ATOM   1452 C CB  . PHE B 1 50  ? 1.301   11.253  -18.936 1.00 15.93 ? 50  PHE B CB  1 
ATOM   1453 C CG  . PHE B 1 50  ? 2.782   11.020  -19.033 1.00 16.82 ? 50  PHE B CG  1 
ATOM   1454 C CD1 . PHE B 1 50  ? 3.663   11.825  -18.335 1.00 17.18 ? 50  PHE B CD1 1 
ATOM   1455 C CD2 . PHE B 1 50  ? 3.288   9.977   -19.791 1.00 23.39 ? 50  PHE B CD2 1 
ATOM   1456 C CE1 . PHE B 1 50  ? 5.035   11.608  -18.404 1.00 20.52 ? 50  PHE B CE1 1 
ATOM   1457 C CE2 . PHE B 1 50  ? 4.657   9.755   -19.866 1.00 23.43 ? 50  PHE B CE2 1 
ATOM   1458 C CZ  . PHE B 1 50  ? 5.528   10.573  -19.173 1.00 20.76 ? 50  PHE B CZ  1 
ATOM   1459 N N   . GLY B 1 51  ? -0.996  12.465  -16.940 1.00 14.11 ? 51  GLY B N   1 
ATOM   1460 C CA  . GLY B 1 51  ? -2.347  12.999  -16.909 1.00 13.31 ? 51  GLY B CA  1 
ATOM   1461 C C   . GLY B 1 51  ? -2.616  13.814  -18.161 1.00 17.55 ? 51  GLY B C   1 
ATOM   1462 O O   . GLY B 1 51  ? -3.057  14.959  -18.084 1.00 15.08 ? 51  GLY B O   1 
ATOM   1463 N N   . ASP B 1 52  ? -2.319  13.217  -19.315 1.00 15.62 ? 52  ASP B N   1 
ATOM   1464 C CA  . ASP B 1 52  ? -2.400  13.888  -20.614 1.00 15.93 ? 52  ASP B CA  1 
ATOM   1465 C C   . ASP B 1 52  ? -3.540  13.267  -21.389 1.00 18.79 ? 52  ASP B C   1 
ATOM   1466 O O   . ASP B 1 52  ? -3.431  12.148  -21.881 1.00 17.46 ? 52  ASP B O   1 
ATOM   1467 C CB  . ASP B 1 52  ? -1.083  13.708  -21.385 1.00 16.18 ? 52  ASP B CB  1 
ATOM   1468 C CG  . ASP B 1 52  ? -1.082  14.393  -22.745 1.00 17.33 ? 52  ASP B CG  1 
ATOM   1469 O OD1 . ASP B 1 52  ? -2.165  14.619  -23.326 1.00 15.46 ? 52  ASP B OD1 1 
ATOM   1470 O OD2 . ASP B 1 52  ? 0.023   14.687  -23.250 1.00 20.20 ? 52  ASP B OD2 1 
ATOM   1471 N N   . ASN B 1 53  ? -4.655  13.978  -21.461 1.00 18.28 ? 53  ASN B N   1 
ATOM   1472 C CA  . ASN B 1 53  ? -5.797  13.476  -22.202 1.00 19.45 ? 53  ASN B CA  1 
ATOM   1473 C C   . ASN B 1 53  ? -6.066  14.347  -23.430 1.00 16.89 ? 53  ASN B C   1 
ATOM   1474 O O   . ASN B 1 53  ? -7.206  14.501  -23.869 1.00 18.55 ? 53  ASN B O   1 
ATOM   1475 C CB  . ASN B 1 53  ? -7.010  13.352  -21.279 1.00 24.84 ? 53  ASN B CB  1 
ATOM   1476 C CG  . ASN B 1 53  ? -6.796  12.327  -20.159 1.00 30.16 ? 53  ASN B CG  1 
ATOM   1477 O OD1 . ASN B 1 53  ? -5.667  11.621  -20.200 1.00 30.53 ? 53  ASN B OD1 1 
ATOM   1478 N ND2 . ASN B 1 53  ? -7.637  12.176  -19.273 1.00 28.71 ? 53  ASN B ND2 1 
ATOM   1479 N N   . THR B 1 54  ? -4.993  14.906  -23.989 1.00 18.88 ? 54  THR B N   1 
ATOM   1480 C CA  . THR B 1 54  ? -5.099  15.745  -25.182 1.00 21.06 ? 54  THR B CA  1 
ATOM   1481 C C   . THR B 1 54  ? -5.596  14.959  -26.391 1.00 20.87 ? 54  THR B C   1 
ATOM   1482 O O   . THR B 1 54  ? -6.171  15.530  -27.316 1.00 22.95 ? 54  THR B O   1 
ATOM   1483 C CB  . THR B 1 54  ? -3.764  16.434  -25.540 1.00 18.75 ? 54  THR B CB  1 
ATOM   1484 O OG1 . THR B 1 54  ? -2.734  15.451  -25.712 1.00 17.08 ? 54  THR B OG1 1 
ATOM   1485 C CG2 . THR B 1 54  ? -3.358  17.421  -24.449 1.00 17.89 ? 54  THR B CG2 1 
ATOM   1486 N N   . ALA B 1 55  ? -5.362  13.651  -26.382 1.00 17.73 ? 55  ALA B N   1 
ATOM   1487 C CA  . ALA B 1 55  ? -5.886  12.766  -27.417 1.00 21.02 ? 55  ALA B CA  1 
ATOM   1488 C C   . ALA B 1 55  ? -6.732  11.685  -26.760 1.00 22.65 ? 55  ALA B C   1 
ATOM   1489 O O   . ALA B 1 55  ? -6.585  10.496  -27.047 1.00 27.28 ? 55  ALA B O   1 
ATOM   1490 C CB  . ALA B 1 55  ? -4.752  12.148  -28.222 1.00 24.54 ? 55  ALA B CB  1 
ATOM   1491 N N   . GLY B 1 56  ? -7.623  12.109  -25.874 1.00 22.76 ? 56  GLY B N   1 
ATOM   1492 C CA  . GLY B 1 56  ? -8.415  11.173  -25.102 1.00 27.11 ? 56  GLY B CA  1 
ATOM   1493 C C   . GLY B 1 56  ? -7.490  10.253  -24.341 1.00 22.11 ? 56  GLY B C   1 
ATOM   1494 O O   . GLY B 1 56  ? -6.457  10.681  -23.830 1.00 20.11 ? 56  GLY B O   1 
ATOM   1495 N N   . CYS B 1 57  ? -7.836  8.975   -24.286 1.00 19.08 ? 57  CYS B N   1 
ATOM   1496 C CA  . CYS B 1 57  ? -7.078  8.038   -23.466 1.00 24.45 ? 57  CYS B CA  1 
ATOM   1497 C C   . CYS B 1 57  ? -5.802  7.551   -24.146 1.00 18.92 ? 57  CYS B C   1 
ATOM   1498 O O   . CYS B 1 57  ? -4.992  6.852   -23.538 1.00 20.35 ? 57  CYS B O   1 
ATOM   1499 C CB  . CYS B 1 57  ? -7.953  6.845   -23.088 1.00 21.78 ? 57  CYS B CB  1 
ATOM   1500 S SG  . CYS B 1 57  ? -9.507  7.317   -22.325 1.00 24.67 ? 57  CYS B SG  1 
ATOM   1501 N N   . THR B 1 58  ? -5.629  7.910   -25.411 1.00 19.76 ? 58  THR B N   1 
ATOM   1502 C CA  . THR B 1 58  ? -4.484  7.428   -26.176 1.00 22.55 ? 58  THR B CA  1 
ATOM   1503 C C   . THR B 1 58  ? -3.188  8.171   -25.851 1.00 19.70 ? 58  THR B C   1 
ATOM   1504 O O   . THR B 1 58  ? -2.104  7.733   -26.238 1.00 20.57 ? 58  THR B O   1 
ATOM   1505 C CB  . THR B 1 58  ? -4.760  7.502   -27.692 1.00 20.37 ? 58  THR B CB  1 
ATOM   1506 O OG1 . THR B 1 58  ? -4.648  8.858   -28.139 1.00 22.20 ? 58  THR B OG1 1 
ATOM   1507 C CG2 . THR B 1 58  ? -6.162  6.986   -28.000 1.00 22.92 ? 58  THR B CG2 1 
ATOM   1508 N N   . SER B 1 59  ? -3.301  9.295   -25.146 1.00 14.97 ? 59  SER B N   1 
ATOM   1509 C CA  . SER B 1 59  ? -2.137  10.113  -24.814 1.00 15.97 ? 59  SER B CA  1 
ATOM   1510 C C   . SER B 1 59  ? -1.653  9.925   -23.378 1.00 18.15 ? 59  SER B C   1 
ATOM   1511 O O   . SER B 1 59  ? -0.725  10.608  -22.940 1.00 19.10 ? 59  SER B O   1 
ATOM   1512 C CB  . SER B 1 59  ? -2.451  11.590  -25.060 1.00 17.61 ? 59  SER B CB  1 
ATOM   1513 O OG  . SER B 1 59  ? -3.777  11.896  -24.664 1.00 18.75 ? 59  SER B OG  1 
ATOM   1514 N N   . ALA B 1 60  ? -2.262  8.990   -22.655 1.00 18.76 ? 60  ALA B N   1 
ATOM   1515 C CA  . ALA B 1 60  ? -2.001  8.849   -21.218 1.00 19.37 ? 60  ALA B CA  1 
ATOM   1516 C C   . ALA B 1 60  ? -0.660  8.199   -20.875 1.00 17.30 ? 60  ALA B C   1 
ATOM   1517 O O   . ALA B 1 60  ? -0.227  8.235   -19.723 1.00 18.17 ? 60  ALA B O   1 
ATOM   1518 C CB  . ALA B 1 60  ? -3.144  8.108   -20.535 1.00 22.13 ? 60  ALA B CB  1 
ATOM   1519 N N   . GLY B 1 61  ? -0.003  7.610   -21.868 1.00 16.51 ? 61  GLY B N   1 
ATOM   1520 C CA  . GLY B 1 61  ? 1.309   7.028   -21.655 1.00 14.85 ? 61  GLY B CA  1 
ATOM   1521 C C   . GLY B 1 61  ? 1.247   5.604   -21.142 1.00 20.83 ? 61  GLY B C   1 
ATOM   1522 O O   . GLY B 1 61  ? 0.175   5.003   -21.108 1.00 17.97 ? 61  GLY B O   1 
ATOM   1523 N N   . PRO B 1 62  ? 2.405   5.055   -20.735 1.00 18.04 ? 62  PRO B N   1 
ATOM   1524 C CA  . PRO B 1 62  ? 2.488   3.674   -20.253 1.00 18.07 ? 62  PRO B CA  1 
ATOM   1525 C C   . PRO B 1 62  ? 1.917   3.589   -18.842 1.00 16.96 ? 62  PRO B C   1 
ATOM   1526 O O   . PRO B 1 62  ? 1.741   4.620   -18.194 1.00 17.32 ? 62  PRO B O   1 
ATOM   1527 C CB  . PRO B 1 62  ? 3.996   3.402   -20.201 1.00 20.17 ? 62  PRO B CB  1 
ATOM   1528 C CG  . PRO B 1 62  ? 4.678   4.665   -20.651 1.00 23.67 ? 62  PRO B CG  1 
ATOM   1529 C CD  . PRO B 1 62  ? 3.681   5.767   -20.581 1.00 19.30 ? 62  PRO B CD  1 
ATOM   1530 N N   . HIS B 1 63  ? 1.623   2.388   -18.366 1.00 18.46 ? 63  HIS B N   1 
ATOM   1531 C CA  . HIS B 1 63  ? 1.131   2.274   -17.001 1.00 20.36 ? 63  HIS B CA  1 
ATOM   1532 C C   . HIS B 1 63  ? 2.188   2.812   -16.037 1.00 18.55 ? 63  HIS B C   1 
ATOM   1533 O O   . HIS B 1 63  ? 3.388   2.723   -16.295 1.00 19.32 ? 63  HIS B O   1 
ATOM   1534 C CB  . HIS B 1 63  ? 0.714   0.837   -16.662 1.00 27.31 ? 63  HIS B CB  1 
ATOM   1535 C CG  . HIS B 1 63  ? 1.859   -0.112  -16.510 1.00 29.54 ? 63  HIS B CG  1 
ATOM   1536 N ND1 . HIS B 1 63  ? 2.406   -0.797  -17.574 1.00 38.96 ? 63  HIS B ND1 1 
ATOM   1537 C CD2 . HIS B 1 63  ? 2.549   -0.508  -15.414 1.00 34.32 ? 63  HIS B CD2 1 
ATOM   1538 C CE1 . HIS B 1 63  ? 3.391   -1.564  -17.142 1.00 43.30 ? 63  HIS B CE1 1 
ATOM   1539 N NE2 . HIS B 1 63  ? 3.499   -1.408  -15.834 1.00 43.61 ? 63  HIS B NE2 1 
ATOM   1540 N N   . PHE B 1 64  ? 1.727   3.410   -14.945 1.00 16.19 ? 64  PHE B N   1 
ATOM   1541 C CA  . PHE B 1 64  ? 2.614   4.025   -13.960 1.00 17.84 ? 64  PHE B CA  1 
ATOM   1542 C C   . PHE B 1 64  ? 3.460   2.958   -13.275 1.00 21.63 ? 64  PHE B C   1 
ATOM   1543 O O   . PHE B 1 64  ? 2.936   2.005   -12.702 1.00 20.24 ? 64  PHE B O   1 
ATOM   1544 C CB  . PHE B 1 64  ? 1.779   4.823   -12.953 1.00 16.03 ? 64  PHE B CB  1 
ATOM   1545 C CG  . PHE B 1 64  ? 2.592   5.595   -11.946 1.00 17.42 ? 64  PHE B CG  1 
ATOM   1546 C CD1 . PHE B 1 64  ? 3.683   6.345   -12.336 1.00 18.54 ? 64  PHE B CD1 1 
ATOM   1547 C CD2 . PHE B 1 64  ? 2.225   5.601   -10.611 1.00 17.66 ? 64  PHE B CD2 1 
ATOM   1548 C CE1 . PHE B 1 64  ? 4.419   7.065   -11.405 1.00 23.06 ? 64  PHE B CE1 1 
ATOM   1549 C CE2 . PHE B 1 64  ? 2.955   6.313   -9.676  1.00 21.06 ? 64  PHE B CE2 1 
ATOM   1550 C CZ  . PHE B 1 64  ? 4.055   7.048   -10.075 1.00 20.30 ? 64  PHE B CZ  1 
ATOM   1551 N N   . ASN B 1 65  ? 4.778   3.118   -13.352 1.00 20.69 ? 65  ASN B N   1 
ATOM   1552 C CA  . ASN B 1 65  ? 5.705   2.117   -12.843 1.00 25.28 ? 65  ASN B CA  1 
ATOM   1553 C C   . ASN B 1 65  ? 7.091   2.726   -12.711 1.00 21.52 ? 65  ASN B C   1 
ATOM   1554 O O   . ASN B 1 65  ? 7.995   2.383   -13.467 1.00 24.27 ? 65  ASN B O   1 
ATOM   1555 C CB  . ASN B 1 65  ? 5.744   0.917   -13.799 1.00 29.18 ? 65  ASN B CB  1 
ATOM   1556 C CG  . ASN B 1 65  ? 6.673   -0.188  -13.327 1.00 35.55 ? 65  ASN B CG  1 
ATOM   1557 O OD1 . ASN B 1 65  ? 7.146   -0.179  -12.194 1.00 39.09 ? 65  ASN B OD1 1 
ATOM   1558 N ND2 . ASN B 1 65  ? 6.934   -1.151  -14.202 1.00 39.32 ? 65  ASN B ND2 1 
ATOM   1559 N N   . PRO B 1 66  ? 7.261   3.644   -11.748 1.00 24.16 ? 66  PRO B N   1 
ATOM   1560 C CA  . PRO B 1 66  ? 8.535   4.360   -11.629 1.00 32.38 ? 66  PRO B CA  1 
ATOM   1561 C C   . PRO B 1 66  ? 9.688   3.379   -11.469 1.00 36.85 ? 66  PRO B C   1 
ATOM   1562 O O   . PRO B 1 66  ? 9.591   2.464   -10.650 1.00 32.87 ? 66  PRO B O   1 
ATOM   1563 C CB  . PRO B 1 66  ? 8.365   5.184   -10.350 1.00 32.74 ? 66  PRO B CB  1 
ATOM   1564 C CG  . PRO B 1 66  ? 6.904   5.227   -10.092 1.00 29.62 ? 66  PRO B CG  1 
ATOM   1565 C CD  . PRO B 1 66  ? 6.341   3.958   -10.642 1.00 28.55 ? 66  PRO B CD  1 
ATOM   1566 N N   . LEU B 1 67  ? 10.750  3.572   -12.247 1.00 33.57 ? 67  LEU B N   1 
ATOM   1567 C CA  . LEU B 1 67  ? 11.897  2.662   -12.267 1.00 34.40 ? 67  LEU B CA  1 
ATOM   1568 C C   . LEU B 1 67  ? 11.577  1.350   -12.981 1.00 47.20 ? 67  LEU B C   1 
ATOM   1569 O O   . LEU B 1 67  ? 11.915  1.173   -14.155 1.00 28.00 ? 67  LEU B O   1 
ATOM   1570 C CB  . LEU B 1 67  ? 12.420  2.399   -10.852 1.00 42.60 ? 67  LEU B CB  1 
ATOM   1571 C CG  . LEU B 1 67  ? 13.498  3.364   -10.361 1.00 46.96 ? 67  LEU B CG  1 
ATOM   1572 C CD1 . LEU B 1 67  ? 14.883  2.874   -10.755 1.00 52.01 ? 67  LEU B CD1 1 
ATOM   1573 C CD2 . LEU B 1 67  ? 13.249  4.763   -10.897 1.00 31.71 ? 67  LEU B CD2 1 
ATOM   1574 N N   . ARG B 1 79  ? 3.501   -6.240  -7.758  1.00 48.95 ? 79  ARG B N   1 
ATOM   1575 C CA  . ARG B 1 79  ? 2.809   -5.583  -8.860  1.00 46.88 ? 79  ARG B CA  1 
ATOM   1576 C C   . ARG B 1 79  ? 3.457   -4.240  -9.176  1.00 40.24 ? 79  ARG B C   1 
ATOM   1577 O O   . ARG B 1 79  ? 4.186   -3.682  -8.355  1.00 42.11 ? 79  ARG B O   1 
ATOM   1578 C CB  . ARG B 1 79  ? 1.333   -5.367  -8.515  1.00 43.99 ? 79  ARG B CB  1 
ATOM   1579 C CG  . ARG B 1 79  ? 1.083   -4.182  -7.590  1.00 42.40 ? 79  ARG B CG  1 
ATOM   1580 C CD  . ARG B 1 79  ? -0.403  -3.942  -7.364  1.00 41.78 ? 79  ARG B CD  1 
ATOM   1581 N NE  . ARG B 1 79  ? -0.656  -2.699  -6.634  1.00 44.67 ? 79  ARG B NE  1 
ATOM   1582 C CZ  . ARG B 1 79  ? -0.774  -1.509  -7.215  1.00 24.34 ? 79  ARG B CZ  1 
ATOM   1583 N NH1 . ARG B 1 79  ? -0.658  -1.403  -8.527  1.00 43.91 ? 79  ARG B NH1 1 
ATOM   1584 N NH2 . ARG B 1 79  ? -1.005  -0.426  -6.492  1.00 31.70 ? 79  ARG B NH2 1 
ATOM   1585 N N   . HIS B 1 80  ? 3.191   -3.725  -10.370 1.00 37.24 ? 80  HIS B N   1 
ATOM   1586 C CA  . HIS B 1 80  ? 3.601   -2.370  -10.708 1.00 35.72 ? 80  HIS B CA  1 
ATOM   1587 C C   . HIS B 1 80  ? 2.663   -1.399  -10.007 1.00 25.17 ? 80  HIS B C   1 
ATOM   1588 O O   . HIS B 1 80  ? 1.503   -1.726  -9.752  1.00 25.03 ? 80  HIS B O   1 
ATOM   1589 C CB  . HIS B 1 80  ? 3.581   -2.152  -12.222 1.00 34.70 ? 80  HIS B CB  1 
ATOM   1590 C CG  . HIS B 1 80  ? 4.551   -3.016  -12.967 1.00 46.49 ? 80  HIS B CG  1 
ATOM   1591 N ND1 . HIS B 1 80  ? 4.261   -3.576  -14.193 1.00 47.13 ? 80  HIS B ND1 1 
ATOM   1592 C CD2 . HIS B 1 80  ? 5.801   -3.430  -12.651 1.00 47.70 ? 80  HIS B CD2 1 
ATOM   1593 C CE1 . HIS B 1 80  ? 5.296   -4.287  -14.605 1.00 50.93 ? 80  HIS B CE1 1 
ATOM   1594 N NE2 . HIS B 1 80  ? 6.243   -4.216  -13.687 1.00 45.03 ? 80  HIS B NE2 1 
ATOM   1595 N N   . VAL B 1 81  ? 3.167   -0.214  -9.684  1.00 21.67 ? 81  VAL B N   1 
ATOM   1596 C CA  . VAL B 1 81  ? 2.411   0.745   -8.884  1.00 20.69 ? 81  VAL B CA  1 
ATOM   1597 C C   . VAL B 1 81  ? 1.023   1.014   -9.454  1.00 23.50 ? 81  VAL B C   1 
ATOM   1598 O O   . VAL B 1 81  ? 0.041   1.067   -8.717  1.00 25.05 ? 81  VAL B O   1 
ATOM   1599 C CB  . VAL B 1 81  ? 3.158   2.089   -8.746  1.00 24.15 ? 81  VAL B CB  1 
ATOM   1600 C CG1 . VAL B 1 81  ? 2.261   3.123   -8.089  1.00 23.72 ? 81  VAL B CG1 1 
ATOM   1601 C CG2 . VAL B 1 81  ? 4.447   1.911   -7.944  1.00 24.44 ? 81  VAL B CG2 1 
ATOM   1602 N N   . GLY B 1 82  ? 0.942   1.185   -10.767 1.00 18.31 ? 82  GLY B N   1 
ATOM   1603 C CA  . GLY B 1 82  ? -0.311  1.572   -11.400 1.00 19.87 ? 82  GLY B CA  1 
ATOM   1604 C C   . GLY B 1 82  ? -1.322  0.455   -11.566 1.00 22.99 ? 82  GLY B C   1 
ATOM   1605 O O   . GLY B 1 82  ? -2.474  0.706   -11.915 1.00 27.28 ? 82  GLY B O   1 
ATOM   1606 N N   . ASP B 1 83  ? -0.895  -0.780  -11.322 1.00 22.14 ? 83  ASP B N   1 
ATOM   1607 C CA  . ASP B 1 83  ? -1.733  -1.947  -11.585 1.00 24.40 ? 83  ASP B CA  1 
ATOM   1608 C C   . ASP B 1 83  ? -2.763  -2.160  -10.483 1.00 26.23 ? 83  ASP B C   1 
ATOM   1609 O O   . ASP B 1 83  ? -2.470  -2.773  -9.457  1.00 30.09 ? 83  ASP B O   1 
ATOM   1610 C CB  . ASP B 1 83  ? -0.866  -3.197  -11.753 1.00 28.65 ? 83  ASP B CB  1 
ATOM   1611 C CG  . ASP B 1 83  ? -1.685  -4.452  -12.003 1.00 32.89 ? 83  ASP B CG  1 
ATOM   1612 O OD1 . ASP B 1 83  ? -2.926  -4.391  -11.896 1.00 31.83 ? 83  ASP B OD1 1 
ATOM   1613 O OD2 . ASP B 1 83  ? -1.084  -5.504  -12.304 1.00 44.72 ? 83  ASP B OD2 1 
ATOM   1614 N N   . LEU B 1 84  ? -3.974  -1.659  -10.701 1.00 23.43 ? 84  LEU B N   1 
ATOM   1615 C CA  . LEU B 1 84  ? -5.032  -1.766  -9.705  1.00 18.63 ? 84  LEU B CA  1 
ATOM   1616 C C   . LEU B 1 84  ? -5.950  -2.974  -9.909  1.00 27.63 ? 84  LEU B C   1 
ATOM   1617 O O   . LEU B 1 84  ? -7.077  -2.994  -9.408  1.00 30.87 ? 84  LEU B O   1 
ATOM   1618 C CB  . LEU B 1 84  ? -5.873  -0.485  -9.668  1.00 19.69 ? 84  LEU B CB  1 
ATOM   1619 C CG  . LEU B 1 84  ? -5.161  0.814   -9.286  1.00 26.98 ? 84  LEU B CG  1 
ATOM   1620 C CD1 . LEU B 1 84  ? -6.135  1.985   -9.322  1.00 26.21 ? 84  LEU B CD1 1 
ATOM   1621 C CD2 . LEU B 1 84  ? -4.524  0.688   -7.918  1.00 23.36 ? 84  LEU B CD2 1 
ATOM   1622 N N   . GLY B 1 85  ? -5.471  -3.975  -10.639 1.00 24.51 ? 85  GLY B N   1 
ATOM   1623 C CA  . GLY B 1 85  ? -6.226  -5.196  -10.850 1.00 29.40 ? 85  GLY B CA  1 
ATOM   1624 C C   . GLY B 1 85  ? -7.424  -5.023  -11.763 1.00 25.75 ? 85  GLY B C   1 
ATOM   1625 O O   . GLY B 1 85  ? -7.322  -4.405  -12.822 1.00 24.69 ? 85  GLY B O   1 
ATOM   1626 N N   . ASN B 1 86  ? -8.559  -5.584  -11.356 1.00 20.86 ? 86  ASN B N   1 
ATOM   1627 C CA  . ASN B 1 86  ? -9.783  -5.529  -12.153 1.00 24.28 ? 86  ASN B CA  1 
ATOM   1628 C C   . ASN B 1 86  ? -10.941 -4.910  -11.389 1.00 27.27 ? 86  ASN B C   1 
ATOM   1629 O O   . ASN B 1 86  ? -10.987 -4.978  -10.161 1.00 22.71 ? 86  ASN B O   1 
ATOM   1630 C CB  . ASN B 1 86  ? -10.214 -6.940  -12.561 1.00 26.99 ? 86  ASN B CB  1 
ATOM   1631 C CG  . ASN B 1 86  ? -9.288  -7.569  -13.568 1.00 24.14 ? 86  ASN B CG  1 
ATOM   1632 O OD1 . ASN B 1 86  ? -9.120  -7.057  -14.673 1.00 23.41 ? 86  ASN B OD1 1 
ATOM   1633 N ND2 . ASN B 1 86  ? -8.691  -8.699  -13.202 1.00 30.64 ? 86  ASN B ND2 1 
ATOM   1634 N N   . VAL B 1 87  ? -11.877 -4.316  -12.123 1.00 22.66 ? 87  VAL B N   1 
ATOM   1635 C CA  . VAL B 1 87  ? -13.207 -4.034  -11.597 1.00 25.44 ? 87  VAL B CA  1 
ATOM   1636 C C   . VAL B 1 87  ? -14.149 -5.043  -12.247 1.00 25.20 ? 87  VAL B C   1 
ATOM   1637 O O   . VAL B 1 87  ? -13.810 -5.637  -13.266 1.00 18.91 ? 87  VAL B O   1 
ATOM   1638 C CB  . VAL B 1 87  ? -13.673 -2.596  -11.910 1.00 21.92 ? 87  VAL B CB  1 
ATOM   1639 C CG1 . VAL B 1 87  ? -12.696 -1.582  -11.330 1.00 23.62 ? 87  VAL B CG1 1 
ATOM   1640 C CG2 . VAL B 1 87  ? -13.824 -2.395  -13.404 1.00 21.13 ? 87  VAL B CG2 1 
ATOM   1641 N N   . THR B 1 88  ? -15.318 -5.258  -11.654 1.00 19.17 ? 88  THR B N   1 
ATOM   1642 C CA  . THR B 1 88  ? -16.246 -6.256  -12.177 1.00 24.96 ? 88  THR B CA  1 
ATOM   1643 C C   . THR B 1 88  ? -17.610 -5.650  -12.469 1.00 23.37 ? 88  THR B C   1 
ATOM   1644 O O   . THR B 1 88  ? -18.298 -5.172  -11.568 1.00 23.35 ? 88  THR B O   1 
ATOM   1645 C CB  . THR B 1 88  ? -16.411 -7.445  -11.206 1.00 28.99 ? 88  THR B CB  1 
ATOM   1646 O OG1 . THR B 1 88  ? -15.141 -8.072  -11.002 1.00 31.29 ? 88  THR B OG1 1 
ATOM   1647 C CG2 . THR B 1 88  ? -17.390 -8.469  -11.769 1.00 32.56 ? 88  THR B CG2 1 
ATOM   1648 N N   . ALA B 1 89  ? -17.990 -5.661  -13.739 1.00 22.62 ? 89  ALA B N   1 
ATOM   1649 C CA  . ALA B 1 89  ? -19.297 -5.166  -14.145 1.00 23.46 ? 89  ALA B CA  1 
ATOM   1650 C C   . ALA B 1 89  ? -20.335 -6.274  -14.003 1.00 27.93 ? 89  ALA B C   1 
ATOM   1651 O O   . ALA B 1 89  ? -20.050 -7.440  -14.290 1.00 23.81 ? 89  ALA B O   1 
ATOM   1652 C CB  . ALA B 1 89  ? -19.246 -4.658  -15.575 1.00 25.56 ? 89  ALA B CB  1 
ATOM   1653 N N   . ASP B 1 90  ? -21.529 -5.910  -13.543 1.00 26.87 ? 90  ASP B N   1 
ATOM   1654 C CA  . ASP B 1 90  ? -22.632 -6.862  -13.448 1.00 30.66 ? 90  ASP B CA  1 
ATOM   1655 C C   . ASP B 1 90  ? -23.400 -6.926  -14.767 1.00 35.69 ? 90  ASP B C   1 
ATOM   1656 O O   . ASP B 1 90  ? -22.949 -6.391  -15.782 1.00 31.66 ? 90  ASP B O   1 
ATOM   1657 C CB  . ASP B 1 90  ? -23.564 -6.518  -12.274 1.00 33.65 ? 90  ASP B CB  1 
ATOM   1658 C CG  . ASP B 1 90  ? -24.239 -5.161  -12.427 1.00 32.58 ? 90  ASP B CG  1 
ATOM   1659 O OD1 . ASP B 1 90  ? -24.330 -4.651  -13.563 1.00 30.46 ? 90  ASP B OD1 1 
ATOM   1660 O OD2 . ASP B 1 90  ? -24.688 -4.607  -11.400 1.00 34.41 ? 90  ASP B OD2 1 
ATOM   1661 N N   . LYS B 1 91  ? -24.556 -7.583  -14.760 1.00 35.95 ? 91  LYS B N   1 
ATOM   1662 C CA  . LYS B 1 91  ? -25.336 -7.730  -15.985 1.00 32.61 ? 91  LYS B CA  1 
ATOM   1663 C C   . LYS B 1 91  ? -25.869 -6.391  -16.493 1.00 33.06 ? 91  LYS B C   1 
ATOM   1664 O O   . LYS B 1 91  ? -26.138 -6.234  -17.685 1.00 37.79 ? 91  LYS B O   1 
ATOM   1665 C CB  . LYS B 1 91  ? -26.485 -8.723  -15.792 1.00 45.87 ? 91  LYS B CB  1 
ATOM   1666 C CG  . LYS B 1 91  ? -27.182 -9.100  -17.093 1.00 50.99 ? 91  LYS B CG  1 
ATOM   1667 C CD  . LYS B 1 91  ? -28.217 -10.195 -16.887 1.00 65.66 ? 91  LYS B CD  1 
ATOM   1668 C CE  . LYS B 1 91  ? -28.856 -10.600 -18.209 1.00 64.13 ? 91  LYS B CE  1 
ATOM   1669 N NZ  . LYS B 1 91  ? -29.874 -11.673 -18.033 1.00 79.73 ? 91  LYS B NZ  1 
ATOM   1670 N N   . ASP B 1 92  ? -26.016 -5.428  -15.589 1.00 29.38 ? 92  ASP B N   1 
ATOM   1671 C CA  . ASP B 1 92  ? -26.469 -4.087  -15.956 1.00 29.87 ? 92  ASP B CA  1 
ATOM   1672 C C   . ASP B 1 92  ? -25.326 -3.245  -16.528 1.00 32.05 ? 92  ASP B C   1 
ATOM   1673 O O   . ASP B 1 92  ? -25.551 -2.160  -17.071 1.00 32.60 ? 92  ASP B O   1 
ATOM   1674 C CB  . ASP B 1 92  ? -27.087 -3.379  -14.747 1.00 30.95 ? 92  ASP B CB  1 
ATOM   1675 C CG  . ASP B 1 92  ? -28.464 -3.920  -14.390 1.00 41.16 ? 92  ASP B CG  1 
ATOM   1676 O OD1 . ASP B 1 92  ? -29.239 -4.242  -15.315 1.00 42.96 ? 92  ASP B OD1 1 
ATOM   1677 O OD2 . ASP B 1 92  ? -28.773 -4.016  -13.184 1.00 47.25 ? 92  ASP B OD2 1 
ATOM   1678 N N   . GLY B 1 93  ? -24.102 -3.748  -16.398 1.00 27.29 ? 93  GLY B N   1 
ATOM   1679 C CA  . GLY B 1 93  ? -22.936 -3.065  -16.931 1.00 25.43 ? 93  GLY B CA  1 
ATOM   1680 C C   . GLY B 1 93  ? -22.303 -2.111  -15.936 1.00 25.84 ? 93  GLY B C   1 
ATOM   1681 O O   . GLY B 1 93  ? -21.535 -1.226  -16.315 1.00 23.35 ? 93  GLY B O   1 
ATOM   1682 N N   . VAL B 1 94  ? -22.630 -2.303  -14.662 1.00 22.69 ? 94  VAL B N   1 
ATOM   1683 C CA  . VAL B 1 94  ? -22.166 -1.435  -13.588 1.00 18.20 ? 94  VAL B CA  1 
ATOM   1684 C C   . VAL B 1 94  ? -21.119 -2.141  -12.739 1.00 26.09 ? 94  VAL B C   1 
ATOM   1685 O O   . VAL B 1 94  ? -21.317 -3.275  -12.303 1.00 25.41 ? 94  VAL B O   1 
ATOM   1686 C CB  . VAL B 1 94  ? -23.341 -0.986  -12.682 1.00 22.60 ? 94  VAL B CB  1 
ATOM   1687 C CG1 . VAL B 1 94  ? -22.824 -0.252  -11.444 1.00 23.02 ? 94  VAL B CG1 1 
ATOM   1688 C CG2 . VAL B 1 94  ? -24.307 -0.115  -13.462 1.00 21.74 ? 94  VAL B CG2 1 
ATOM   1689 N N   . ALA B 1 95  ? -19.999 -1.467  -12.514 1.00 21.53 ? 95  ALA B N   1 
ATOM   1690 C CA  . ALA B 1 95  ? -18.945 -2.007  -11.674 1.00 20.71 ? 95  ALA B CA  1 
ATOM   1691 C C   . ALA B 1 95  ? -18.783 -1.122  -10.450 1.00 24.17 ? 95  ALA B C   1 
ATOM   1692 O O   . ALA B 1 95  ? -18.379 0.035   -10.558 1.00 22.30 ? 95  ALA B O   1 
ATOM   1693 C CB  . ALA B 1 95  ? -17.643 -2.090  -12.451 1.00 21.55 ? 95  ALA B CB  1 
ATOM   1694 N N   . ASP B 1 96  ? -19.123 -1.661  -9.287  1.00 21.56 ? 96  ASP B N   1 
ATOM   1695 C CA  . ASP B 1 96  ? -18.916 -0.937  -8.043  1.00 23.71 ? 96  ASP B CA  1 
ATOM   1696 C C   . ASP B 1 96  ? -17.512 -1.240  -7.554  1.00 26.03 ? 96  ASP B C   1 
ATOM   1697 O O   . ASP B 1 96  ? -17.077 -2.390  -7.562  1.00 25.83 ? 96  ASP B O   1 
ATOM   1698 C CB  . ASP B 1 96  ? -19.966 -1.327  -6.998  1.00 28.40 ? 96  ASP B CB  1 
ATOM   1699 C CG  . ASP B 1 96  ? -21.360 -0.843  -7.365  1.00 37.93 ? 96  ASP B CG  1 
ATOM   1700 O OD1 . ASP B 1 96  ? -22.336 -1.580  -7.106  1.00 43.60 ? 96  ASP B OD1 1 
ATOM   1701 O OD2 . ASP B 1 96  ? -21.481 0.271   -7.920  1.00 33.09 ? 96  ASP B OD2 1 
ATOM   1702 N N   . VAL B 1 97  ? -16.799 -0.197  -7.150  1.00 20.37 ? 97  VAL B N   1 
ATOM   1703 C CA  . VAL B 1 97  ? -15.412 -0.331  -6.741  1.00 22.04 ? 97  VAL B CA  1 
ATOM   1704 C C   . VAL B 1 97  ? -15.244 -0.035  -5.256  1.00 19.70 ? 97  VAL B C   1 
ATOM   1705 O O   . VAL B 1 97  ? -15.742 0.969   -4.753  1.00 17.12 ? 97  VAL B O   1 
ATOM   1706 C CB  . VAL B 1 97  ? -14.503 0.621   -7.551  1.00 20.15 ? 97  VAL B CB  1 
ATOM   1707 C CG1 . VAL B 1 97  ? -13.063 0.507   -7.087  1.00 22.58 ? 97  VAL B CG1 1 
ATOM   1708 C CG2 . VAL B 1 97  ? -14.624 0.338   -9.043  1.00 27.76 ? 97  VAL B CG2 1 
ATOM   1709 N N   . SER B 1 98  ? -14.549 -0.926  -4.559  1.00 18.77 ? 98  SER B N   1 
ATOM   1710 C CA  . SER B 1 98  ? -14.145 -0.686  -3.180  1.00 21.62 ? 98  SER B CA  1 
ATOM   1711 C C   . SER B 1 98  ? -12.873 -1.473  -2.923  1.00 26.95 ? 98  SER B C   1 
ATOM   1712 O O   . SER B 1 98  ? -12.912 -2.681  -2.697  1.00 30.05 ? 98  SER B O   1 
ATOM   1713 C CB  . SER B 1 98  ? -15.237 -1.091  -2.191  1.00 22.13 ? 98  SER B CB  1 
ATOM   1714 O OG  . SER B 1 98  ? -14.900 -0.675  -0.876  1.00 29.33 ? 98  SER B OG  1 
ATOM   1715 N N   . ILE B 1 99  ? -11.744 -0.778  -2.985  1.00 23.00 ? 99  ILE B N   1 
ATOM   1716 C CA  . ILE B 1 99  ? -10.438 -1.407  -2.852  1.00 22.51 ? 99  ILE B CA  1 
ATOM   1717 C C   . ILE B 1 99  ? -9.581  -0.663  -1.842  1.00 27.01 ? 99  ILE B C   1 
ATOM   1718 O O   . ILE B 1 99  ? -9.742  0.541   -1.647  1.00 22.41 ? 99  ILE B O   1 
ATOM   1719 C CB  . ILE B 1 99  ? -9.681  -1.398  -4.194  1.00 26.63 ? 99  ILE B CB  1 
ATOM   1720 C CG1 . ILE B 1 99  ? -10.550 -1.971  -5.315  1.00 33.62 ? 99  ILE B CG1 1 
ATOM   1721 C CG2 . ILE B 1 99  ? -8.367  -2.161  -4.081  1.00 38.30 ? 99  ILE B CG2 1 
ATOM   1722 C CD1 . ILE B 1 99  ? -9.937  -1.812  -6.687  1.00 36.13 ? 99  ILE B CD1 1 
ATOM   1723 N N   . GLU B 1 100 ? -8.673  -1.389  -1.200  1.00 21.86 ? 100 GLU B N   1 
ATOM   1724 C CA  . GLU B 1 100 ? -7.634  -0.774  -0.392  1.00 24.22 ? 100 GLU B CA  1 
ATOM   1725 C C   . GLU B 1 100 ? -6.313  -1.079  -1.074  1.00 24.54 ? 100 GLU B C   1 
ATOM   1726 O O   . GLU B 1 100 ? -6.050  -2.224  -1.439  1.00 25.50 ? 100 GLU B O   1 
ATOM   1727 C CB  . GLU B 1 100 ? -7.633  -1.335  1.029   1.00 25.80 ? 100 GLU B CB  1 
ATOM   1728 C CG  . GLU B 1 100 ? -6.641  -0.641  1.956   1.00 26.65 ? 100 GLU B CG  1 
ATOM   1729 C CD  . GLU B 1 100 ? -6.715  -1.146  3.383   1.00 40.72 ? 100 GLU B CD  1 
ATOM   1730 O OE1 . GLU B 1 100 ? -7.832  -1.222  3.935   1.00 44.73 ? 100 GLU B OE1 1 
ATOM   1731 O OE2 . GLU B 1 100 ? -5.650  -1.460  3.953   1.00 37.40 ? 100 GLU B OE2 1 
ATOM   1732 N N   . ASP B 1 101 ? -5.488  -0.058  -1.259  1.00 20.14 ? 101 ASP B N   1 
ATOM   1733 C CA  . ASP B 1 101 ? -4.214  -0.239  -1.937  1.00 21.09 ? 101 ASP B CA  1 
ATOM   1734 C C   . ASP B 1 101 ? -3.109  0.450   -1.158  1.00 21.04 ? 101 ASP B C   1 
ATOM   1735 O O   . ASP B 1 101 ? -3.199  1.639   -0.856  1.00 21.10 ? 101 ASP B O   1 
ATOM   1736 C CB  . ASP B 1 101 ? -4.295  0.322   -3.359  1.00 18.31 ? 101 ASP B CB  1 
ATOM   1737 C CG  . ASP B 1 101 ? -3.135  -0.116  -4.228  1.00 25.63 ? 101 ASP B CG  1 
ATOM   1738 O OD1 . ASP B 1 101 ? -3.355  -0.923  -5.153  1.00 37.43 ? 101 ASP B OD1 1 
ATOM   1739 O OD2 . ASP B 1 101 ? -2.001  0.343   -3.992  1.00 20.34 ? 101 ASP B OD2 1 
ATOM   1740 N N   . SER B 1 102 ? -2.065  -0.300  -0.825  1.00 21.52 ? 102 SER B N   1 
ATOM   1741 C CA  A SER B 1 102 ? -0.954  0.220   -0.037  0.47 22.03 ? 102 SER B CA  1 
ATOM   1742 C CA  B SER B 1 102 ? -0.971  0.265   -0.047  0.53 22.01 ? 102 SER B CA  1 
ATOM   1743 C C   . SER B 1 102 ? 0.274   0.514   -0.892  1.00 24.09 ? 102 SER B C   1 
ATOM   1744 O O   . SER B 1 102 ? 1.355   0.753   -0.364  1.00 23.18 ? 102 SER B O   1 
ATOM   1745 C CB  A SER B 1 102 ? -0.574  -0.774  1.063   0.47 27.08 ? 102 SER B CB  1 
ATOM   1746 C CB  B SER B 1 102 ? -0.648  -0.624  1.155   0.53 27.23 ? 102 SER B CB  1 
ATOM   1747 O OG  A SER B 1 102 ? 0.071   -1.912  0.516   0.47 28.96 ? 102 SER B OG  1 
ATOM   1748 O OG  B SER B 1 102 ? -1.733  -0.629  2.068   0.53 23.20 ? 102 SER B OG  1 
ATOM   1749 N N   . VAL B 1 103 ? 0.107   0.476   -2.209  1.00 19.32 ? 103 VAL B N   1 
ATOM   1750 C CA  . VAL B 1 103 ? 1.217   0.757   -3.116  1.00 17.71 ? 103 VAL B CA  1 
ATOM   1751 C C   . VAL B 1 103 ? 1.066   2.144   -3.732  1.00 21.73 ? 103 VAL B C   1 
ATOM   1752 O O   . VAL B 1 103 ? 2.010   2.934   -3.741  1.00 19.35 ? 103 VAL B O   1 
ATOM   1753 C CB  . VAL B 1 103 ? 1.352   -0.308  -4.214  1.00 21.71 ? 103 VAL B CB  1 
ATOM   1754 C CG1 . VAL B 1 103 ? 2.591   -0.046  -5.056  1.00 28.00 ? 103 VAL B CG1 1 
ATOM   1755 C CG2 . VAL B 1 103 ? 1.414   -1.698  -3.597  1.00 28.20 ? 103 VAL B CG2 1 
ATOM   1756 N N   . ILE B 1 104 ? -0.127  2.448   -4.238  1.00 19.91 ? 104 ILE B N   1 
ATOM   1757 C CA  . ILE B 1 104 ? -0.388  3.791   -4.739  1.00 18.58 ? 104 ILE B CA  1 
ATOM   1758 C C   . ILE B 1 104 ? -0.375  4.753   -3.561  1.00 13.39 ? 104 ILE B C   1 
ATOM   1759 O O   . ILE B 1 104 ? -0.448  4.332   -2.404  1.00 17.81 ? 104 ILE B O   1 
ATOM   1760 C CB  . ILE B 1 104 ? -1.736  3.899   -5.491  1.00 15.57 ? 104 ILE B CB  1 
ATOM   1761 C CG1 . ILE B 1 104 ? -2.902  3.543   -4.573  1.00 20.16 ? 104 ILE B CG1 1 
ATOM   1762 C CG2 . ILE B 1 104 ? -1.730  3.031   -6.756  1.00 18.34 ? 104 ILE B CG2 1 
ATOM   1763 C CD1 . ILE B 1 104 ? -4.248  3.773   -5.210  1.00 14.71 ? 104 ILE B CD1 1 
ATOM   1764 N N   . SER B 1 105 ? -0.288  6.047   -3.852  1.00 14.16 ? 105 SER B N   1 
ATOM   1765 C CA  . SER B 1 105 ? -0.242  7.044   -2.795  1.00 11.39 ? 105 SER B CA  1 
ATOM   1766 C C   . SER B 1 105 ? -0.670  8.394   -3.329  1.00 13.72 ? 105 SER B C   1 
ATOM   1767 O O   . SER B 1 105 ? -0.689  8.602   -4.542  1.00 14.70 ? 105 SER B O   1 
ATOM   1768 C CB  . SER B 1 105 ? 1.171   7.141   -2.213  1.00 15.02 ? 105 SER B CB  1 
ATOM   1769 O OG  . SER B 1 105 ? 1.200   8.030   -1.109  1.00 16.15 ? 105 SER B OG  1 
ATOM   1770 N N   . LEU B 1 106 ? -1.020  9.299   -2.421  1.00 12.11 ? 106 LEU B N   1 
ATOM   1771 C CA  . LEU B 1 106 ? -1.372  10.667  -2.785  1.00 12.76 ? 106 LEU B CA  1 
ATOM   1772 C C   . LEU B 1 106 ? -0.228  11.642  -2.538  1.00 17.37 ? 106 LEU B C   1 
ATOM   1773 O O   . LEU B 1 106 ? -0.414  12.862  -2.593  1.00 15.38 ? 106 LEU B O   1 
ATOM   1774 C CB  . LEU B 1 106 ? -2.648  11.118  -2.068  1.00 15.64 ? 106 LEU B CB  1 
ATOM   1775 C CG  . LEU B 1 106 ? -3.913  10.307  -2.368  1.00 13.92 ? 106 LEU B CG  1 
ATOM   1776 C CD1 . LEU B 1 106 ? -5.143  11.030  -1.830  1.00 16.74 ? 106 LEU B CD1 1 
ATOM   1777 C CD2 . LEU B 1 106 ? -4.078  10.017  -3.861  1.00 15.56 ? 106 LEU B CD2 1 
ATOM   1778 N N   . SER B 1 107 ? 0.960   11.092  -2.282  1.00 16.96 ? 107 SER B N   1 
ATOM   1779 C CA  . SER B 1 107 ? 2.183   11.875  -2.202  1.00 18.72 ? 107 SER B CA  1 
ATOM   1780 C C   . SER B 1 107 ? 3.402   10.990  -2.454  1.00 20.42 ? 107 SER B C   1 
ATOM   1781 O O   . SER B 1 107 ? 3.296   9.759   -2.513  1.00 18.44 ? 107 SER B O   1 
ATOM   1782 C CB  . SER B 1 107 ? 2.309   12.548  -0.834  1.00 26.05 ? 107 SER B CB  1 
ATOM   1783 O OG  . SER B 1 107 ? 2.578   11.589  0.176   1.00 23.04 ? 107 SER B OG  1 
ATOM   1784 N N   . GLY B 1 108 ? 4.560   11.622  -2.608  1.00 20.78 ? 108 GLY B N   1 
ATOM   1785 C CA  . GLY B 1 108 ? 5.809   10.897  -2.731  1.00 25.43 ? 108 GLY B CA  1 
ATOM   1786 C C   . GLY B 1 108 ? 6.009   10.200  -4.060  1.00 22.12 ? 108 GLY B C   1 
ATOM   1787 O O   . GLY B 1 108 ? 5.307   10.476  -5.038  1.00 22.39 ? 108 GLY B O   1 
ATOM   1788 N N   . ASP B 1 109 ? 6.973   9.283   -4.091  1.00 23.94 ? 109 ASP B N   1 
ATOM   1789 C CA  . ASP B 1 109 ? 7.375   8.630   -5.333  1.00 26.60 ? 109 ASP B CA  1 
ATOM   1790 C C   . ASP B 1 109 ? 6.232   7.888   -6.016  1.00 19.89 ? 109 ASP B C   1 
ATOM   1791 O O   . ASP B 1 109 ? 6.234   7.726   -7.231  1.00 19.62 ? 109 ASP B O   1 
ATOM   1792 C CB  . ASP B 1 109 ? 8.537   7.668   -5.083  1.00 30.28 ? 109 ASP B CB  1 
ATOM   1793 C CG  . ASP B 1 109 ? 9.835   8.391   -4.800  1.00 37.98 ? 109 ASP B CG  1 
ATOM   1794 O OD1 . ASP B 1 109 ? 9.902   9.613   -5.054  1.00 35.51 ? 109 ASP B OD1 1 
ATOM   1795 O OD2 . ASP B 1 109 ? 10.786  7.738   -4.325  1.00 36.32 ? 109 ASP B OD2 1 
ATOM   1796 N N   . HIS B 1 110 ? 5.258   7.441   -5.232  1.00 20.02 ? 110 HIS B N   1 
ATOM   1797 C CA  . HIS B 1 110 ? 4.152   6.660   -5.774  1.00 15.31 ? 110 HIS B CA  1 
ATOM   1798 C C   . HIS B 1 110 ? 2.881   7.491   -5.942  1.00 19.44 ? 110 HIS B C   1 
ATOM   1799 O O   . HIS B 1 110 ? 1.787   6.948   -6.116  1.00 15.95 ? 110 HIS B O   1 
ATOM   1800 C CB  . HIS B 1 110 ? 3.889   5.437   -4.896  1.00 17.51 ? 110 HIS B CB  1 
ATOM   1801 C CG  . HIS B 1 110 ? 4.940   4.379   -5.013  1.00 21.89 ? 110 HIS B CG  1 
ATOM   1802 N ND1 . HIS B 1 110 ? 4.770   3.102   -4.524  1.00 24.97 ? 110 HIS B ND1 1 
ATOM   1803 C CD2 . HIS B 1 110 ? 6.173   4.406   -5.575  1.00 20.91 ? 110 HIS B CD2 1 
ATOM   1804 C CE1 . HIS B 1 110 ? 5.856   2.390   -4.771  1.00 27.53 ? 110 HIS B CE1 1 
ATOM   1805 N NE2 . HIS B 1 110 ? 6.723   3.158   -5.407  1.00 23.94 ? 110 HIS B NE2 1 
ATOM   1806 N N   . CYS B 1 111 ? 3.037   8.809   -5.902  1.00 16.94 ? 111 CYS B N   1 
ATOM   1807 C CA  . CYS B 1 111 ? 1.906   9.715   -6.034  1.00 14.55 ? 111 CYS B CA  1 
ATOM   1808 C C   . CYS B 1 111 ? 1.207   9.541   -7.374  1.00 15.68 ? 111 CYS B C   1 
ATOM   1809 O O   . CYS B 1 111 ? 1.864   9.499   -8.413  1.00 14.09 ? 111 CYS B O   1 
ATOM   1810 C CB  . CYS B 1 111 ? 2.343   11.171  -5.882  1.00 17.48 ? 111 CYS B CB  1 
ATOM   1811 S SG  . CYS B 1 111 ? 0.910   12.242  -5.694  1.00 19.32 ? 111 CYS B SG  1 
ATOM   1812 N N   . ILE B 1 112 ? -0.121  9.457   -7.337  1.00 12.32 ? 112 ILE B N   1 
ATOM   1813 C CA  . ILE B 1 112 ? -0.931  9.276   -8.542  1.00 14.55 ? 112 ILE B CA  1 
ATOM   1814 C C   . ILE B 1 112 ? -1.728  10.522  -8.925  1.00 13.96 ? 112 ILE B C   1 
ATOM   1815 O O   . ILE B 1 112 ? -2.445  10.526  -9.936  1.00 12.58 ? 112 ILE B O   1 
ATOM   1816 C CB  . ILE B 1 112 ? -1.898  8.086   -8.421  1.00 15.16 ? 112 ILE B CB  1 
ATOM   1817 C CG1 . ILE B 1 112 ? -2.914  8.319   -7.298  1.00 15.47 ? 112 ILE B CG1 1 
ATOM   1818 C CG2 . ILE B 1 112 ? -1.130  6.793   -8.209  1.00 12.30 ? 112 ILE B CG2 1 
ATOM   1819 C CD1 . ILE B 1 112 ? -3.988  7.254   -7.240  1.00 18.77 ? 112 ILE B CD1 1 
ATOM   1820 N N   . ILE B 1 113 ? -1.611  11.570  -8.114  1.00 12.21 ? 113 ILE B N   1 
ATOM   1821 C CA  A ILE B 1 113 ? -2.236  12.854  -8.421  0.57 11.66 ? 113 ILE B CA  1 
ATOM   1822 C CA  B ILE B 1 113 ? -2.251  12.844  -8.424  0.43 11.70 ? 113 ILE B CA  1 
ATOM   1823 C C   . ILE B 1 113 ? -1.684  13.415  -9.723  1.00 17.56 ? 113 ILE B C   1 
ATOM   1824 O O   . ILE B 1 113 ? -0.470  13.449  -9.922  1.00 13.75 ? 113 ILE B O   1 
ATOM   1825 C CB  A ILE B 1 113 ? -1.978  13.890  -7.311  0.57 16.74 ? 113 ILE B CB  1 
ATOM   1826 C CB  B ILE B 1 113 ? -2.077  13.865  -7.279  0.43 16.73 ? 113 ILE B CB  1 
ATOM   1827 C CG1 A ILE B 1 113 ? -2.573  13.407  -5.993  0.57 16.56 ? 113 ILE B CG1 1 
ATOM   1828 C CG1 B ILE B 1 113 ? -2.864  13.415  -6.046  0.43 16.10 ? 113 ILE B CG1 1 
ATOM   1829 C CG2 A ILE B 1 113 ? -2.579  15.237  -7.693  0.57 15.34 ? 113 ILE B CG2 1 
ATOM   1830 C CG2 B ILE B 1 113 ? -2.536  15.248  -7.720  0.43 15.35 ? 113 ILE B CG2 1 
ATOM   1831 C CD1 A ILE B 1 113 ? -4.063  13.267  -6.044  0.57 12.60 ? 113 ILE B CD1 1 
ATOM   1832 C CD1 B ILE B 1 113 ? -2.622  14.266  -4.808  0.43 15.40 ? 113 ILE B CD1 1 
ATOM   1833 N N   . GLY B 1 114 ? -2.573  13.857  -10.609 1.00 12.20 ? 114 GLY B N   1 
ATOM   1834 C CA  . GLY B 1 114 ? -2.154  14.423  -11.880 1.00 13.47 ? 114 GLY B CA  1 
ATOM   1835 C C   . GLY B 1 114 ? -1.866  13.379  -12.944 1.00 15.50 ? 114 GLY B C   1 
ATOM   1836 O O   . GLY B 1 114 ? -1.474  13.711  -14.063 1.00 14.16 ? 114 GLY B O   1 
ATOM   1837 N N   . ARG B 1 115 ? -2.049  12.109  -12.598 1.00 14.32 ? 115 ARG B N   1 
ATOM   1838 C CA  . ARG B 1 115 ? -1.889  11.034  -13.573 1.00 14.28 ? 115 ARG B CA  1 
ATOM   1839 C C   . ARG B 1 115 ? -3.258  10.561  -14.055 1.00 15.02 ? 115 ARG B C   1 
ATOM   1840 O O   . ARG B 1 115 ? -4.270  11.059  -13.590 1.00 15.37 ? 115 ARG B O   1 
ATOM   1841 C CB  . ARG B 1 115 ? -1.067  9.893   -12.973 1.00 14.05 ? 115 ARG B CB  1 
ATOM   1842 C CG  . ARG B 1 115 ? 0.271   10.387  -12.452 1.00 15.51 ? 115 ARG B CG  1 
ATOM   1843 C CD  . ARG B 1 115 ? 1.252   9.277   -12.169 1.00 15.19 ? 115 ARG B CD  1 
ATOM   1844 N NE  . ARG B 1 115 ? 2.370   9.781   -11.376 1.00 15.88 ? 115 ARG B NE  1 
ATOM   1845 C CZ  . ARG B 1 115 ? 3.497   10.256  -11.892 1.00 21.60 ? 115 ARG B CZ  1 
ATOM   1846 N NH1 . ARG B 1 115 ? 3.666   10.294  -13.205 1.00 18.30 ? 115 ARG B NH1 1 
ATOM   1847 N NH2 . ARG B 1 115 ? 4.460   10.691  -11.092 1.00 28.30 ? 115 ARG B NH2 1 
ATOM   1848 N N   . THR B 1 116 ? -3.288  9.607   -14.981 1.00 11.67 ? 116 THR B N   1 
ATOM   1849 C CA  . THR B 1 116 ? -4.554  9.193   -15.586 1.00 11.98 ? 116 THR B CA  1 
ATOM   1850 C C   . THR B 1 116 ? -5.041  7.835   -15.084 1.00 15.07 ? 116 THR B C   1 
ATOM   1851 O O   . THR B 1 116 ? -4.283  6.874   -15.060 1.00 16.44 ? 116 THR B O   1 
ATOM   1852 C CB  . THR B 1 116 ? -4.453  9.147   -17.125 1.00 14.56 ? 116 THR B CB  1 
ATOM   1853 O OG1 . THR B 1 116 ? -4.230  10.467  -17.626 1.00 16.22 ? 116 THR B OG1 1 
ATOM   1854 C CG2 . THR B 1 116 ? -5.736  8.606   -17.714 1.00 13.99 ? 116 THR B CG2 1 
ATOM   1855 N N   . LEU B 1 117 ? -6.314  7.778   -14.705 1.00 14.52 ? 117 LEU B N   1 
ATOM   1856 C CA  . LEU B 1 117 ? -6.964  6.525   -14.349 1.00 11.98 ? 117 LEU B CA  1 
ATOM   1857 C C   . LEU B 1 117 ? -7.679  5.983   -15.585 1.00 14.41 ? 117 LEU B C   1 
ATOM   1858 O O   . LEU B 1 117 ? -8.295  6.727   -16.326 1.00 14.28 ? 117 LEU B O   1 
ATOM   1859 C CB  . LEU B 1 117 ? -7.958  6.733   -13.209 1.00 12.04 ? 117 LEU B CB  1 
ATOM   1860 C CG  . LEU B 1 117 ? -8.638  5.504   -12.609 1.00 13.87 ? 117 LEU B CG  1 
ATOM   1861 C CD1 . LEU B 1 117 ? -7.626  4.580   -11.978 1.00 15.43 ? 117 LEU B CD1 1 
ATOM   1862 C CD2 . LEU B 1 117 ? -9.695  5.890   -11.602 1.00 10.23 ? 117 LEU B CD2 1 
ATOM   1863 N N   . VAL B 1 118 ? -7.591  4.675   -15.789 1.00 13.01 ? 118 VAL B N   1 
ATOM   1864 C CA  . VAL B 1 118 ? -8.122  4.047   -16.984 1.00 11.81 ? 118 VAL B CA  1 
ATOM   1865 C C   . VAL B 1 118 ? -8.850  2.739   -16.675 1.00 19.75 ? 118 VAL B C   1 
ATOM   1866 O O   . VAL B 1 118 ? -8.479  2.031   -15.757 1.00 16.54 ? 118 VAL B O   1 
ATOM   1867 C CB  . VAL B 1 118 ? -6.980  3.745   -17.964 1.00 18.63 ? 118 VAL B CB  1 
ATOM   1868 C CG1 . VAL B 1 118 ? -7.425  2.772   -19.008 1.00 16.50 ? 118 VAL B CG1 1 
ATOM   1869 C CG2 . VAL B 1 118 ? -6.456  5.022   -18.577 1.00 23.89 ? 118 VAL B CG2 1 
ATOM   1870 N N   . VAL B 1 119 ? -9.888  2.444   -17.450 1.00 15.89 ? 119 VAL B N   1 
ATOM   1871 C CA  . VAL B 1 119 ? -10.586 1.165   -17.373 1.00 18.04 ? 119 VAL B CA  1 
ATOM   1872 C C   . VAL B 1 119 ? -10.521 0.504   -18.745 1.00 16.74 ? 119 VAL B C   1 
ATOM   1873 O O   . VAL B 1 119 ? -10.747 1.157   -19.751 1.00 17.00 ? 119 VAL B O   1 
ATOM   1874 C CB  . VAL B 1 119 ? -12.053 1.312   -16.899 1.00 17.38 ? 119 VAL B CB  1 
ATOM   1875 C CG1 . VAL B 1 119 ? -12.799 2.329   -17.731 1.00 20.01 ? 119 VAL B CG1 1 
ATOM   1876 C CG2 . VAL B 1 119 ? -12.756 -0.031  -16.924 1.00 18.48 ? 119 VAL B CG2 1 
ATOM   1877 N N   . HIS B 1 120 ? -10.175 -0.780  -18.775 1.00 15.68 ? 120 HIS B N   1 
ATOM   1878 C CA  . HIS B 1 120 ? -9.914  -1.471  -20.036 1.00 23.27 ? 120 HIS B CA  1 
ATOM   1879 C C   . HIS B 1 120 ? -11.078 -2.318  -20.542 1.00 17.86 ? 120 HIS B C   1 
ATOM   1880 O O   . HIS B 1 120 ? -12.004 -2.655  -19.798 1.00 20.81 ? 120 HIS B O   1 
ATOM   1881 C CB  . HIS B 1 120 ? -8.667  -2.356  -19.923 1.00 18.86 ? 120 HIS B CB  1 
ATOM   1882 C CG  . HIS B 1 120 ? -7.376  -1.600  -19.993 1.00 19.89 ? 120 HIS B CG  1 
ATOM   1883 N ND1 . HIS B 1 120 ? -6.695  -1.405  -21.176 1.00 17.61 ? 120 HIS B ND1 1 
ATOM   1884 C CD2 . HIS B 1 120 ? -6.636  -1.002  -19.031 1.00 23.80 ? 120 HIS B CD2 1 
ATOM   1885 C CE1 . HIS B 1 120 ? -5.595  -0.713  -20.939 1.00 21.23 ? 120 HIS B CE1 1 
ATOM   1886 N NE2 . HIS B 1 120 ? -5.534  -0.458  -19.646 1.00 21.96 ? 120 HIS B NE2 1 
ATOM   1887 N N   . GLU B 1 121 ? -10.982 -2.662  -21.822 1.00 20.86 ? 121 GLU B N   1 
ATOM   1888 C CA  . GLU B 1 121 ? -11.919 -3.513  -22.540 1.00 24.00 ? 121 GLU B CA  1 
ATOM   1889 C C   . GLU B 1 121 ? -12.000 -4.916  -21.941 1.00 22.99 ? 121 GLU B C   1 
ATOM   1890 O O   . GLU B 1 121 ? -13.091 -5.478  -21.785 1.00 20.90 ? 121 GLU B O   1 
ATOM   1891 C CB  . GLU B 1 121 ? -11.453 -3.607  -23.997 1.00 18.13 ? 121 GLU B CB  1 
ATOM   1892 C CG  . GLU B 1 121 ? -12.308 -4.469  -24.905 1.00 33.16 ? 121 GLU B CG  1 
ATOM   1893 C CD  . GLU B 1 121 ? -11.655 -4.710  -26.257 1.00 31.82 ? 121 GLU B CD  1 
ATOM   1894 O OE1 . GLU B 1 121 ? -10.559 -4.158  -26.511 1.00 24.04 ? 121 GLU B OE1 1 
ATOM   1895 O OE2 . GLU B 1 121 ? -12.237 -5.459  -27.067 1.00 38.07 ? 121 GLU B OE2 1 
ATOM   1896 N N   . LYS B 1 122 ? -10.838 -5.479  -21.623 1.00 22.02 ? 122 LYS B N   1 
ATOM   1897 C CA  . LYS B 1 122 ? -10.745 -6.838  -21.094 1.00 21.91 ? 122 LYS B CA  1 
ATOM   1898 C C   . LYS B 1 122 ? -9.996  -6.869  -19.763 1.00 25.59 ? 122 LYS B C   1 
ATOM   1899 O O   . LYS B 1 122 ? -9.505  -5.844  -19.301 1.00 21.64 ? 122 LYS B O   1 
ATOM   1900 C CB  . LYS B 1 122 ? -10.067 -7.755  -22.118 1.00 23.21 ? 122 LYS B CB  1 
ATOM   1901 C CG  . LYS B 1 122 ? -10.729 -7.711  -23.496 1.00 30.95 ? 122 LYS B CG  1 
ATOM   1902 C CD  . LYS B 1 122 ? -10.256 -8.845  -24.389 1.00 37.85 ? 122 LYS B CD  1 
ATOM   1903 C CE  . LYS B 1 122 ? -8.760  -8.771  -24.635 1.00 36.17 ? 122 LYS B CE  1 
ATOM   1904 N NZ  . LYS B 1 122 ? -8.299  -9.835  -25.573 1.00 44.63 ? 122 LYS B NZ  1 
ATOM   1905 N N   . ALA B 1 123 ? -9.907  -8.050  -19.155 1.00 22.49 ? 123 ALA B N   1 
ATOM   1906 C CA  . ALA B 1 123 ? -9.321  -8.196  -17.824 1.00 26.49 ? 123 ALA B CA  1 
ATOM   1907 C C   . ALA B 1 123 ? -7.821  -7.897  -17.768 1.00 25.62 ? 123 ALA B C   1 
ATOM   1908 O O   . ALA B 1 123 ? -7.111  -7.995  -18.770 1.00 29.31 ? 123 ALA B O   1 
ATOM   1909 C CB  . ALA B 1 123 ? -9.604  -9.589  -17.269 1.00 27.70 ? 123 ALA B CB  1 
ATOM   1910 N N   . ASP B 1 124 ? -7.358  -7.527  -16.579 1.00 33.54 ? 124 ASP B N   1 
ATOM   1911 C CA  . ASP B 1 124 ? -5.947  -7.264  -16.325 1.00 31.08 ? 124 ASP B CA  1 
ATOM   1912 C C   . ASP B 1 124 ? -5.092  -8.448  -16.762 1.00 29.75 ? 124 ASP B C   1 
ATOM   1913 O O   . ASP B 1 124 ? -4.021  -8.268  -17.344 1.00 45.52 ? 124 ASP B O   1 
ATOM   1914 C CB  . ASP B 1 124 ? -5.735  -6.988  -14.833 1.00 29.00 ? 124 ASP B CB  1 
ATOM   1915 C CG  . ASP B 1 124 ? -4.364  -6.413  -14.530 1.00 34.86 ? 124 ASP B CG  1 
ATOM   1916 O OD1 . ASP B 1 124 ? -3.715  -5.887  -15.458 1.00 47.48 ? 124 ASP B OD1 1 
ATOM   1917 O OD2 . ASP B 1 124 ? -3.940  -6.482  -13.356 1.00 42.57 ? 124 ASP B OD2 1 
ATOM   1918 N N   . ASN B 1 139 ? -2.812  -7.323  -23.058 1.00 42.54 ? 139 ASN B N   1 
ATOM   1919 C CA  . ASN B 1 139 ? -3.929  -8.248  -23.214 1.00 43.49 ? 139 ASN B CA  1 
ATOM   1920 C C   . ASN B 1 139 ? -5.239  -7.654  -22.709 1.00 38.30 ? 139 ASN B C   1 
ATOM   1921 O O   . ASN B 1 139 ? -6.307  -8.239  -22.895 1.00 34.26 ? 139 ASN B O   1 
ATOM   1922 C CB  . ASN B 1 139 ? -3.649  -9.567  -22.487 1.00 56.12 ? 139 ASN B CB  1 
ATOM   1923 C CG  . ASN B 1 139 ? -2.399  -10.265 -22.995 1.00 63.12 ? 139 ASN B CG  1 
ATOM   1924 O OD1 . ASN B 1 139 ? -2.356  -11.583 -22.839 1.00 70.10 ? 139 ASN B OD1 1 
ATOM   1925 N ND2 . ASN B 1 139 ? -1.483  -9.628  -23.516 1.00 55.63 ? 139 ASN B ND2 1 
ATOM   1926 N N   . ALA B 1 140 ? -5.152  -6.493  -22.068 1.00 25.99 ? 140 ALA B N   1 
ATOM   1927 C CA  . ALA B 1 140 ? -6.331  -5.834  -21.513 1.00 25.65 ? 140 ALA B CA  1 
ATOM   1928 C C   . ALA B 1 140 ? -7.125  -5.097  -22.589 1.00 23.59 ? 140 ALA B C   1 
ATOM   1929 O O   . ALA B 1 140 ? -8.208  -4.575  -22.334 1.00 22.11 ? 140 ALA B O   1 
ATOM   1930 C CB  . ALA B 1 140 ? -5.928  -4.882  -20.394 1.00 30.24 ? 140 ALA B CB  1 
ATOM   1931 N N   . GLY B 1 141 ? -6.584  -5.055  -23.801 1.00 21.72 ? 141 GLY B N   1 
ATOM   1932 C CA  . GLY B 1 141 ? -7.279  -4.423  -24.905 1.00 23.34 ? 141 GLY B CA  1 
ATOM   1933 C C   . GLY B 1 141 ? -7.292  -2.913  -24.783 1.00 21.41 ? 141 GLY B C   1 
ATOM   1934 O O   . GLY B 1 141 ? -6.446  -2.330  -24.103 1.00 21.71 ? 141 GLY B O   1 
ATOM   1935 N N   . SER B 1 142 ? -8.272  -2.282  -25.420 1.00 23.13 ? 142 SER B N   1 
ATOM   1936 C CA  . SER B 1 142 ? -8.294  -0.826  -25.529 1.00 27.63 ? 142 SER B CA  1 
ATOM   1937 C C   . SER B 1 142 ? -8.727  -0.151  -24.230 1.00 19.55 ? 142 SER B C   1 
ATOM   1938 O O   . SER B 1 142 ? -9.321  -0.788  -23.357 1.00 18.15 ? 142 SER B O   1 
ATOM   1939 C CB  . SER B 1 142 ? -9.201  -0.388  -26.682 1.00 32.43 ? 142 SER B CB  1 
ATOM   1940 O OG  . SER B 1 142 ? -10.540 -0.801  -26.464 1.00 34.30 ? 142 SER B OG  1 
ATOM   1941 N N   . ARG B 1 143 ? -8.412  1.138   -24.110 1.00 19.78 ? 143 ARG B N   1 
ATOM   1942 C CA  . ARG B 1 143 ? -8.821  1.937   -22.955 1.00 17.46 ? 143 ARG B CA  1 
ATOM   1943 C C   . ARG B 1 143 ? -10.193 2.529   -23.229 1.00 20.16 ? 143 ARG B C   1 
ATOM   1944 O O   . ARG B 1 143 ? -10.343 3.413   -24.074 1.00 24.37 ? 143 ARG B O   1 
ATOM   1945 C CB  . ARG B 1 143 ? -7.815  3.056   -22.683 1.00 22.35 ? 143 ARG B CB  1 
ATOM   1946 C CG  . ARG B 1 143 ? -6.456  2.550   -22.226 1.00 23.44 ? 143 ARG B CG  1 
ATOM   1947 C CD  . ARG B 1 143 ? -5.387  3.628   -22.323 1.00 22.67 ? 143 ARG B CD  1 
ATOM   1948 N NE  . ARG B 1 143 ? -4.061  3.059   -22.127 1.00 22.23 ? 143 ARG B NE  1 
ATOM   1949 C CZ  . ARG B 1 143 ? -2.954  3.531   -22.686 1.00 20.76 ? 143 ARG B CZ  1 
ATOM   1950 N NH1 . ARG B 1 143 ? -3.011  4.585   -23.492 1.00 25.31 ? 143 ARG B NH1 1 
ATOM   1951 N NH2 . ARG B 1 143 ? -1.791  2.937   -22.450 1.00 20.80 ? 143 ARG B NH2 1 
ATOM   1952 N N   . LEU B 1 144 ? -11.192 2.028   -22.516 1.00 16.55 ? 144 LEU B N   1 
ATOM   1953 C CA  . LEU B 1 144 ? -12.578 2.421   -22.747 1.00 17.33 ? 144 LEU B CA  1 
ATOM   1954 C C   . LEU B 1 144 ? -12.878 3.816   -22.211 1.00 14.63 ? 144 LEU B C   1 
ATOM   1955 O O   . LEU B 1 144 ? -13.654 4.568   -22.799 1.00 15.05 ? 144 LEU B O   1 
ATOM   1956 C CB  . LEU B 1 144 ? -13.520 1.395   -22.120 1.00 18.94 ? 144 LEU B CB  1 
ATOM   1957 C CG  . LEU B 1 144 ? -13.413 -0.011  -22.717 1.00 24.30 ? 144 LEU B CG  1 
ATOM   1958 C CD1 . LEU B 1 144 ? -14.366 -0.982  -22.025 1.00 24.70 ? 144 LEU B CD1 1 
ATOM   1959 C CD2 . LEU B 1 144 ? -13.668 0.030   -24.215 1.00 23.01 ? 144 LEU B CD2 1 
ATOM   1960 N N   . ALA B 1 145 ? -12.267 4.155   -21.084 1.00 16.64 ? 145 ALA B N   1 
ATOM   1961 C CA  . ALA B 1 145 ? -12.500 5.454   -20.473 1.00 13.42 ? 145 ALA B CA  1 
ATOM   1962 C C   . ALA B 1 145 ? -11.337 5.813   -19.566 1.00 16.63 ? 145 ALA B C   1 
ATOM   1963 O O   . ALA B 1 145 ? -10.636 4.938   -19.069 1.00 12.69 ? 145 ALA B O   1 
ATOM   1964 C CB  . ALA B 1 145 ? -13.797 5.438   -19.684 1.00 16.43 ? 145 ALA B CB  1 
ATOM   1965 N N   . CYS B 1 146 ? -11.140 7.107   -19.358 1.00 15.12 ? 146 CYS B N   1 
ATOM   1966 C CA  . CYS B 1 146 ? -10.042 7.586   -18.538 1.00 13.32 ? 146 CYS B CA  1 
ATOM   1967 C C   . CYS B 1 146 ? -10.345 8.989   -18.044 1.00 13.79 ? 146 CYS B C   1 
ATOM   1968 O O   . CYS B 1 146 ? -11.221 9.665   -18.576 1.00 18.65 ? 146 CYS B O   1 
ATOM   1969 C CB  . CYS B 1 146 ? -8.763  7.616   -19.363 1.00 15.53 ? 146 CYS B CB  1 
ATOM   1970 S SG  . CYS B 1 146 ? -8.941  8.612   -20.836 1.00 22.10 ? 146 CYS B SG  1 
ATOM   1971 N N   . GLY B 1 147 ? -9.616  9.423   -17.019 1.00 15.41 ? 147 GLY B N   1 
ATOM   1972 C CA  . GLY B 1 147 ? -9.691  10.799  -16.561 1.00 13.58 ? 147 GLY B CA  1 
ATOM   1973 C C   . GLY B 1 147 ? -8.451  11.152  -15.765 1.00 14.64 ? 147 GLY B C   1 
ATOM   1974 O O   . GLY B 1 147 ? -7.739  10.261  -15.323 1.00 13.03 ? 147 GLY B O   1 
ATOM   1975 N N   . VAL B 1 148 ? -8.187  12.445  -15.587 1.00 9.80  ? 148 VAL B N   1 
ATOM   1976 C CA  . VAL B 1 148 ? -7.046  12.878  -14.796 1.00 11.32 ? 148 VAL B CA  1 
ATOM   1977 C C   . VAL B 1 148 ? -7.436  12.877  -13.317 1.00 12.75 ? 148 VAL B C   1 
ATOM   1978 O O   . VAL B 1 148 ? -8.503  13.367  -12.957 1.00 12.87 ? 148 VAL B O   1 
ATOM   1979 C CB  . VAL B 1 148 ? -6.571  14.285  -15.218 1.00 15.86 ? 148 VAL B CB  1 
ATOM   1980 C CG1 . VAL B 1 148 ? -5.385  14.741  -14.364 1.00 16.30 ? 148 VAL B CG1 1 
ATOM   1981 C CG2 . VAL B 1 148 ? -6.211  14.301  -16.709 1.00 13.36 ? 148 VAL B CG2 1 
ATOM   1982 N N   . ILE B 1 149 ? -6.573  12.310  -12.477 1.00 12.22 ? 149 ILE B N   1 
ATOM   1983 C CA  . ILE B 1 149 ? -6.829  12.214  -11.033 1.00 9.21  ? 149 ILE B CA  1 
ATOM   1984 C C   . ILE B 1 149 ? -6.545  13.563  -10.392 1.00 10.81 ? 149 ILE B C   1 
ATOM   1985 O O   . ILE B 1 149 ? -5.415  14.056  -10.439 1.00 17.51 ? 149 ILE B O   1 
ATOM   1986 C CB  . ILE B 1 149 ? -5.947  11.133  -10.388 1.00 9.67  ? 149 ILE B CB  1 
ATOM   1987 C CG1 . ILE B 1 149 ? -6.317  9.763   -10.947 1.00 9.98  ? 149 ILE B CG1 1 
ATOM   1988 C CG2 . ILE B 1 149 ? -6.084  11.156  -8.849  1.00 12.43 ? 149 ILE B CG2 1 
ATOM   1989 C CD1 . ILE B 1 149 ? -5.265  8.698   -10.747 1.00 12.63 ? 149 ILE B CD1 1 
ATOM   1990 N N   . GLY B 1 150 ? -7.572  14.162  -9.798  1.00 12.16 ? 150 GLY B N   1 
ATOM   1991 C CA  . GLY B 1 150 ? -7.453  15.500  -9.254  1.00 11.41 ? 150 GLY B CA  1 
ATOM   1992 C C   . GLY B 1 150 ? -7.541  15.544  -7.740  1.00 13.30 ? 150 GLY B C   1 
ATOM   1993 O O   . GLY B 1 150 ? -8.069  14.627  -7.113  1.00 12.73 ? 150 GLY B O   1 
ATOM   1994 N N   . ILE B 1 151 ? -7.016  16.617  -7.154  1.00 15.14 ? 151 ILE B N   1 
ATOM   1995 C CA  . ILE B 1 151 ? -7.109  16.830  -5.712  1.00 11.19 ? 151 ILE B CA  1 
ATOM   1996 C C   . ILE B 1 151 ? -8.550  17.145  -5.337  1.00 13.23 ? 151 ILE B C   1 
ATOM   1997 O O   . ILE B 1 151 ? -9.189  17.993  -5.966  1.00 16.65 ? 151 ILE B O   1 
ATOM   1998 C CB  . ILE B 1 151 ? -6.192  17.984  -5.248  1.00 11.53 ? 151 ILE B CB  1 
ATOM   1999 C CG1 . ILE B 1 151 ? -4.732  17.663  -5.575  1.00 16.01 ? 151 ILE B CG1 1 
ATOM   2000 C CG2 . ILE B 1 151 ? -6.343  18.219  -3.737  1.00 12.29 ? 151 ILE B CG2 1 
ATOM   2001 C CD1 . ILE B 1 151 ? -3.768  18.808  -5.317  1.00 19.18 ? 151 ILE B CD1 1 
ATOM   2002 N N   . ALA B 1 152 ? -9.048  16.459  -4.311  1.00 15.20 ? 152 ALA B N   1 
ATOM   2003 C CA  . ALA B 1 152 ? -10.439 16.582  -3.881  1.00 15.76 ? 152 ALA B CA  1 
ATOM   2004 C C   . ALA B 1 152 ? -10.553 17.195  -2.492  1.00 17.87 ? 152 ALA B C   1 
ATOM   2005 O O   . ALA B 1 152 ? -11.560 17.823  -2.167  1.00 17.91 ? 152 ALA B O   1 
ATOM   2006 C CB  . ALA B 1 152 ? -11.120 15.222  -3.908  1.00 17.75 ? 152 ALA B CB  1 
ATOM   2007 N N   . GLN B 1 153 ? -9.521  16.990  -1.678  1.00 18.14 ? 153 GLN B N   1 
ATOM   2008 C CA  . GLN B 1 153 ? -9.449  17.554  -0.333  1.00 20.12 ? 153 GLN B CA  1 
ATOM   2009 C C   . GLN B 1 153 ? -7.995  17.610  0.118   1.00 26.00 ? 153 GLN B C   1 
ATOM   2010 O O   . GLN B 1 153 ? -7.182  16.761  -0.253  1.00 24.91 ? 153 GLN B O   1 
ATOM   2011 C CB  . GLN B 1 153 ? -10.275 16.725  0.661   1.00 22.37 ? 153 GLN B CB  1 
ATOM   2012 C CG  . GLN B 1 153 ? -10.139 17.176  2.120   1.00 25.99 ? 153 GLN B CG  1 
ATOM   2013 C CD  . GLN B 1 153 ? -10.986 16.344  3.067   1.00 33.11 ? 153 GLN B CD  1 
ATOM   2014 O OE1 . GLN B 1 153 ? -11.505 15.296  2.686   1.00 31.30 ? 153 GLN B OE1 1 
ATOM   2015 N NE2 . GLN B 1 153 ? -11.137 16.812  4.307   1.00 31.73 ? 153 GLN B NE2 1 
ATOM   2016 O OXT . GLN B 1 153 ? -7.594  18.502  0.862   1.00 31.69 ? 153 GLN B OXT 1 
HETATM 2017 S S1  . PS5 C 2 .   ? 1.698   14.102  -5.480  0.83 32.71 ? 154 PS5 A S1  1 
HETATM 2018 S S2  . PS5 C 2 .   ? 2.155   15.007  -7.244  0.55 42.75 ? 154 PS5 A S2  1 
HETATM 2019 S S3  . PS5 C 2 .   ? 0.918   16.623  -7.314  0.56 31.80 ? 154 PS5 A S3  1 
HETATM 2020 S S4  . PS5 C 2 .   ? 1.804   17.983  -6.082  0.62 40.17 ? 154 PS5 A S4  1 
HETATM 2021 S S5  . PS5 C 2 .   ? 3.181   18.891  -7.267  0.85 30.17 ? 154 PS5 A S5  1 
HETATM 2022 O O   . HOH D 3 .   ? -6.817  17.748  -18.516 1.00 16.30 ? 155 HOH A O   1 
HETATM 2023 O O   . HOH D 3 .   ? -19.272 22.633  -16.670 1.00 45.02 ? 156 HOH A O   1 
HETATM 2024 O O   . HOH D 3 .   ? -12.101 15.284  -11.219 1.00 14.02 ? 157 HOH A O   1 
HETATM 2025 O O   . HOH D 3 .   ? -20.440 16.874  -7.902  1.00 18.40 ? 158 HOH A O   1 
HETATM 2026 O O   . HOH D 3 .   ? 3.427   29.481  -28.199 1.00 32.73 ? 159 HOH A O   1 
HETATM 2027 O O   . HOH D 3 .   ? -0.005  36.099  -27.727 1.00 18.21 ? 160 HOH A O   1 
HETATM 2028 O O   . HOH D 3 .   ? -18.894 38.919  -29.073 1.00 34.85 ? 161 HOH A O   1 
HETATM 2029 O O   . HOH D 3 .   ? -13.101 29.933  -31.997 1.00 21.02 ? 162 HOH A O   1 
HETATM 2030 O O   . HOH D 3 .   ? 5.788   25.792  -4.526  1.00 23.65 ? 163 HOH A O   1 
HETATM 2031 O O   . HOH D 3 .   ? 2.147   27.492  1.556   1.00 33.93 ? 164 HOH A O   1 
HETATM 2032 O O   . HOH D 3 .   ? 6.412   29.570  -24.082 1.00 31.54 ? 165 HOH A O   1 
HETATM 2033 O O   . HOH D 3 .   ? -4.523  35.984  -27.963 1.00 23.89 ? 166 HOH A O   1 
HETATM 2034 O O   . HOH D 3 .   ? 5.586   30.147  -26.851 1.00 33.80 ? 167 HOH A O   1 
HETATM 2035 O O   . HOH D 3 .   ? -14.906 20.356  -17.822 1.00 29.22 ? 168 HOH A O   1 
HETATM 2036 O O   . HOH D 3 .   ? -12.820 42.673  -23.131 1.00 28.76 ? 169 HOH A O   1 
HETATM 2037 O O   . HOH D 3 .   ? -13.014 29.943  -11.412 1.00 30.77 ? 170 HOH A O   1 
HETATM 2038 O O   . HOH D 3 .   ? -19.612 26.534  -12.835 1.00 40.65 ? 171 HOH A O   1 
HETATM 2039 O O   . HOH D 3 .   ? -11.202 20.216  -25.398 1.00 33.57 ? 172 HOH A O   1 
HETATM 2040 O O   . HOH D 3 .   ? -20.148 28.121  -23.406 1.00 36.04 ? 174 HOH A O   1 
HETATM 2041 O O   . HOH D 3 .   ? -15.651 23.656  -30.388 1.00 38.27 ? 175 HOH A O   1 
HETATM 2042 O O   . HOH D 3 .   ? -18.167 26.175  -23.495 1.00 32.82 ? 176 HOH A O   1 
HETATM 2043 O O   . HOH D 3 .   ? -9.048  40.803  -29.070 1.00 32.66 ? 177 HOH A O   1 
HETATM 2044 O O   . HOH D 3 .   ? -16.730 33.430  -24.269 1.00 21.17 ? 178 HOH A O   1 
HETATM 2045 O O   . HOH D 3 .   ? -13.368 31.890  -9.270  1.00 39.89 ? 179 HOH A O   1 
HETATM 2046 O O   . HOH D 3 .   ? 14.073  28.736  -14.705 1.00 39.08 ? 180 HOH A O   1 
HETATM 2047 O O   . HOH D 3 .   ? 1.191   30.217  -27.056 1.00 22.58 ? 181 HOH A O   1 
HETATM 2048 O O   . HOH D 3 .   ? -9.073  20.523  -27.008 1.00 34.98 ? 182 HOH A O   1 
HETATM 2049 O O   . HOH D 3 .   ? -4.137  39.004  -22.164 1.00 35.56 ? 183 HOH A O   1 
HETATM 2050 O O   . HOH D 3 .   ? 12.515  28.920  -17.240 1.00 41.16 ? 184 HOH A O   1 
HETATM 2051 O O   . HOH D 3 .   ? 10.424  27.229  -17.297 1.00 32.55 ? 185 HOH A O   1 
HETATM 2052 O O   . HOH D 3 .   ? -19.848 12.219  -14.055 1.00 41.22 ? 186 HOH A O   1 
HETATM 2053 O O   . HOH D 3 .   ? -17.764 31.260  -25.314 1.00 25.38 ? 187 HOH A O   1 
HETATM 2054 O O   . HOH D 3 .   ? 5.082   30.928  -22.263 1.00 28.82 ? 188 HOH A O   1 
HETATM 2055 O O   . HOH D 3 .   ? 7.577   29.123  -9.265  1.00 29.53 ? 189 HOH A O   1 
HETATM 2056 O O   . HOH D 3 .   ? -15.181 31.781  -34.574 1.00 23.81 ? 190 HOH A O   1 
HETATM 2057 O O   . HOH D 3 .   ? -5.908  36.273  -30.071 1.00 25.40 ? 191 HOH A O   1 
HETATM 2058 O O   . HOH D 3 .   ? -12.808 17.581  -16.503 1.00 34.03 ? 192 HOH A O   1 
HETATM 2059 O O   . HOH D 3 .   ? -5.583  21.800  -0.992  1.00 32.37 ? 193 HOH A O   1 
HETATM 2060 O O   . HOH D 3 .   ? -15.317 44.275  -14.789 1.00 38.41 ? 194 HOH A O   1 
HETATM 2061 O O   . HOH D 3 .   ? 5.888   31.083  -5.172  1.00 38.22 ? 195 HOH A O   1 
HETATM 2062 O O   . HOH D 3 .   ? -15.967 35.169  -30.840 1.00 21.01 ? 196 HOH A O   1 
HETATM 2063 O O   . HOH D 3 .   ? -9.513  17.196  -17.125 1.00 24.48 ? 197 HOH A O   1 
HETATM 2064 O O   . HOH D 3 .   ? -15.859 31.832  -10.192 1.00 40.65 ? 198 HOH A O   1 
HETATM 2065 O O   . HOH D 3 .   ? 5.260   32.780  -26.632 1.00 25.76 ? 199 HOH A O   1 
HETATM 2066 O O   . HOH D 3 .   ? -8.140  22.374  -28.780 1.00 39.60 ? 200 HOH A O   1 
HETATM 2067 O O   . HOH D 3 .   ? 5.741   15.177  -10.651 1.00 42.17 ? 201 HOH A O   1 
HETATM 2068 O O   . HOH D 3 .   ? 9.675   22.134  -4.802  1.00 26.83 ? 202 HOH A O   1 
HETATM 2069 O O   . HOH D 3 .   ? -2.106  24.020  -27.616 1.00 30.55 ? 203 HOH A O   1 
HETATM 2070 O O   . HOH D 3 .   ? -13.974 17.850  -3.782  1.00 28.94 ? 204 HOH A O   1 
HETATM 2071 O O   . HOH D 3 .   ? -16.992 37.500  -30.335 1.00 25.36 ? 205 HOH A O   1 
HETATM 2072 O O   . HOH D 3 .   ? -14.633 39.997  -22.223 1.00 31.31 ? 206 HOH A O   1 
HETATM 2073 O O   . HOH D 3 .   ? 5.297   33.547  -22.031 1.00 30.29 ? 207 HOH A O   1 
HETATM 2074 O O   . HOH D 3 .   ? -13.490 18.405  -18.742 1.00 36.47 ? 208 HOH A O   1 
HETATM 2075 O O   . HOH D 3 .   ? 7.935   33.345  -22.286 1.00 37.51 ? 209 HOH A O   1 
HETATM 2076 O O   . HOH D 3 .   ? 11.866  27.363  -14.234 1.00 25.61 ? 210 HOH A O   1 
HETATM 2077 O O   . HOH D 3 .   ? 7.340   27.059  -23.727 1.00 30.55 ? 211 HOH A O   1 
HETATM 2078 O O   . HOH D 3 .   ? -15.185 16.199  -19.653 1.00 35.53 ? 212 HOH A O   1 
HETATM 2079 O O   . HOH D 3 .   ? -0.125  21.949  -27.652 1.00 40.03 ? 213 HOH A O   1 
HETATM 2080 O O   . HOH D 3 .   ? -13.769 43.637  -20.397 1.00 37.39 ? 214 HOH A O   1 
HETATM 2081 O O   . HOH D 3 .   ? -1.516  35.006  -22.814 1.00 24.43 ? 215 HOH A O   1 
HETATM 2082 O O   . HOH D 3 .   ? -13.776 14.853  -21.574 1.00 42.92 ? 216 HOH A O   1 
HETATM 2083 O O   . HOH D 3 .   ? -2.221  37.347  -27.233 1.00 29.10 ? 217 HOH A O   1 
HETATM 2084 O O   . HOH D 3 .   ? 1.439   27.989  3.905   1.00 33.86 ? 218 HOH A O   1 
HETATM 2085 O O   . HOH D 3 .   ? -10.948 15.998  -21.121 1.00 34.48 ? 219 HOH A O   1 
HETATM 2086 O O   . HOH D 3 .   ? -16.601 16.204  -15.893 1.00 28.64 ? 220 HOH A O   1 
HETATM 2087 O O   . HOH D 3 .   ? -17.487 20.761  -17.980 1.00 40.26 ? 221 HOH A O   1 
HETATM 2088 O O   . HOH D 3 .   ? -2.536  32.517  -2.471  1.00 34.11 ? 222 HOH A O   1 
HETATM 2089 O O   . HOH D 3 .   ? -7.120  32.806  -35.065 1.00 24.64 ? 223 HOH A O   1 
HETATM 2090 O O   . HOH D 3 .   ? -15.349 41.620  -19.700 1.00 27.67 ? 224 HOH A O   1 
HETATM 2091 O O   . HOH D 3 .   ? -10.938 18.288  -19.533 1.00 26.82 ? 225 HOH A O   1 
HETATM 2092 O O   . HOH D 3 .   ? -1.566  36.802  -17.407 1.00 30.09 ? 226 HOH A O   1 
HETATM 2093 O O   . HOH D 3 .   ? 8.490   24.825  -6.104  1.00 29.52 ? 227 HOH A O   1 
HETATM 2094 O O   . HOH D 3 .   ? -21.980 21.368  -15.175 1.00 40.36 ? 228 HOH A O   1 
HETATM 2095 O O   . HOH D 3 .   ? -2.812  19.747  -1.263  1.00 42.19 ? 229 HOH A O   1 
HETATM 2096 O O   . HOH D 3 .   ? -1.901  21.834  -29.548 1.00 44.87 ? 230 HOH A O   1 
HETATM 2097 O O   . HOH D 3 .   ? 2.613   36.196  -14.484 1.00 28.13 ? 231 HOH A O   1 
HETATM 2098 O O   . HOH D 3 .   ? 8.089   35.097  -14.164 1.00 45.47 ? 232 HOH A O   1 
HETATM 2099 O O   . HOH D 3 .   ? -2.168  36.478  -20.482 1.00 29.07 ? 233 HOH A O   1 
HETATM 2100 O O   . HOH D 3 .   ? -12.772 43.570  -27.326 1.00 45.61 ? 234 HOH A O   1 
HETATM 2101 O O   . HOH D 3 .   ? -16.249 39.400  -32.332 1.00 30.99 ? 235 HOH A O   1 
HETATM 2102 O O   . HOH D 3 .   ? -23.410 22.078  -12.732 1.00 41.87 ? 236 HOH A O   1 
HETATM 2103 O O   . HOH D 3 .   ? 0.338   27.460  -28.434 1.00 30.10 ? 237 HOH A O   1 
HETATM 2104 O O   . HOH D 3 .   ? -16.744 18.314  -17.680 1.00 44.38 ? 238 HOH A O   1 
HETATM 2105 O O   . HOH D 3 .   ? -1.634  29.469  -29.842 1.00 27.03 ? 239 HOH A O   1 
HETATM 2106 O O   . HOH D 3 .   ? 9.495   31.448  -9.076  1.00 39.08 ? 240 HOH A O   1 
HETATM 2107 O O   . HOH D 3 .   ? 6.011   17.512  -9.155  1.00 41.41 ? 241 HOH A O   1 
HETATM 2108 O O   . HOH D 3 .   ? -5.793  37.579  -11.922 1.00 29.42 ? 242 HOH A O   1 
HETATM 2109 O O   . HOH D 3 .   ? -7.877  32.906  -7.799  1.00 34.57 ? 243 HOH A O   1 
HETATM 2110 O O   . HOH D 3 .   ? -7.427  35.174  -12.615 1.00 32.73 ? 244 HOH A O   1 
HETATM 2111 O O   . HOH D 3 .   ? -16.151 39.199  -24.414 1.00 26.80 ? 245 HOH A O   1 
HETATM 2112 O O   . HOH D 3 .   ? 4.812   36.389  -12.238 1.00 35.06 ? 246 HOH A O   1 
HETATM 2113 O O   . HOH D 3 .   ? 8.179   32.369  -1.716  1.00 50.90 ? 247 HOH A O   1 
HETATM 2114 O O   . HOH D 3 .   ? -19.461 14.731  -14.629 1.00 39.64 ? 248 HOH A O   1 
HETATM 2115 O O   . HOH D 3 .   ? -16.778 40.184  -35.207 1.00 47.24 ? 249 HOH A O   1 
HETATM 2116 O O   . HOH D 3 .   ? 8.038   29.973  -0.721  1.00 41.99 ? 250 HOH A O   1 
HETATM 2117 O O   . HOH D 3 .   ? -19.813 29.039  -13.427 1.00 33.41 ? 251 HOH A O   1 
HETATM 2118 O O   . HOH D 3 .   ? -15.495 28.516  -32.172 1.00 22.01 ? 252 HOH A O   1 
HETATM 2119 O O   . HOH D 3 .   ? 9.944   35.403  -16.110 1.00 38.48 ? 253 HOH A O   1 
HETATM 2120 O O   . HOH D 3 .   ? 1.510   20.286  -2.734  1.00 42.51 ? 254 HOH A O   1 
HETATM 2121 O O   . HOH D 3 .   ? -0.633  19.998  -6.149  1.00 32.56 ? 255 HOH A O   1 
HETATM 2122 O O   . HOH D 3 .   ? -17.061 25.135  -6.834  1.00 32.71 ? 256 HOH A O   1 
HETATM 2123 O O   . HOH D 3 .   ? -19.903 26.132  -8.000  1.00 39.27 ? 257 HOH A O   1 
HETATM 2124 O O   . HOH D 3 .   ? -22.535 29.283  -27.012 1.00 29.04 ? 258 HOH A O   1 
HETATM 2125 O O   . HOH D 3 .   ? -19.875 26.026  -15.633 1.00 40.90 ? 259 HOH A O   1 
HETATM 2126 O O   . HOH D 3 .   ? -0.541  23.888  -0.871  1.00 31.35 ? 260 HOH A O   1 
HETATM 2127 O O   . HOH D 3 .   ? 1.184   37.232  -16.826 1.00 37.60 ? 261 HOH A O   1 
HETATM 2128 O O   . HOH D 3 .   ? -9.255  40.053  -33.634 1.00 29.38 ? 262 HOH A O   1 
HETATM 2129 O O   . HOH D 3 .   ? 3.543   36.367  -17.906 1.00 37.32 ? 263 HOH A O   1 
HETATM 2130 O O   . HOH D 3 .   ? -23.566 27.704  -24.935 1.00 36.16 ? 264 HOH A O   1 
HETATM 2131 O O   . HOH D 3 .   ? 7.063   16.056  -15.885 1.00 30.89 ? 265 HOH A O   1 
HETATM 2132 O O   . HOH D 3 .   ? -16.297 22.401  -24.936 1.00 30.68 ? 266 HOH A O   1 
HETATM 2133 O O   . HOH D 3 .   ? -3.697  35.957  -24.383 1.00 24.81 ? 267 HOH A O   1 
HETATM 2134 O O   . HOH D 3 .   ? 6.783   28.216  -1.947  1.00 38.85 ? 268 HOH A O   1 
HETATM 2135 O O   . HOH D 3 .   ? -18.853 24.853  -18.019 1.00 37.22 ? 269 HOH A O   1 
HETATM 2136 O O   . HOH D 3 .   ? -18.290 35.197  -22.375 1.00 26.95 ? 270 HOH A O   1 
HETATM 2137 O O   . HOH D 3 .   ? 2.626   19.816  -22.218 1.00 30.04 ? 271 HOH A O   1 
HETATM 2138 O O   . HOH D 3 .   ? -8.094  35.432  -37.685 1.00 38.54 ? 272 HOH A O   1 
HETATM 2139 O O   . HOH D 3 .   ? 4.716   20.908  -21.084 1.00 32.61 ? 273 HOH A O   1 
HETATM 2140 O O   . HOH D 3 .   ? -20.179 30.164  -24.961 1.00 30.34 ? 274 HOH A O   1 
HETATM 2141 O O   . HOH D 3 .   ? 11.328  21.423  -11.809 1.00 27.65 ? 275 HOH A O   1 
HETATM 2142 O O   . HOH D 3 .   ? -9.119  16.203  -19.362 1.00 36.11 ? 276 HOH A O   1 
HETATM 2143 O O   . HOH D 3 .   ? -22.097 27.526  -8.628  1.00 42.96 ? 277 HOH A O   1 
HETATM 2144 O O   . HOH D 3 .   ? -3.433  39.527  -17.442 1.00 30.59 ? 278 HOH A O   1 
HETATM 2145 O O   . HOH D 3 .   ? -3.414  29.206  -32.279 1.00 40.48 ? 279 HOH A O   1 
HETATM 2146 O O   . HOH D 3 .   ? 7.774   14.965  -18.397 1.00 38.20 ? 280 HOH A O   1 
HETATM 2147 O O   . HOH D 3 .   ? 9.106   21.847  -10.152 1.00 28.43 ? 281 HOH A O   1 
HETATM 2148 O O   . HOH D 3 .   ? 7.573   31.486  -25.972 1.00 29.11 ? 282 HOH A O   1 
HETATM 2149 O O   . HOH D 3 .   ? -5.500  42.027  -18.094 1.00 37.69 ? 283 HOH A O   1 
HETATM 2150 O O   . HOH D 3 .   ? -11.836 35.616  -39.846 1.00 33.73 ? 284 HOH A O   1 
HETATM 2151 O O   . HOH D 3 .   ? -15.167 25.812  -31.615 1.00 34.53 ? 285 HOH A O   1 
HETATM 2152 O O   . HOH D 3 .   ? -15.249 41.815  -15.755 1.00 33.41 ? 286 HOH A O   1 
HETATM 2153 O O   . HOH D 3 .   ? 0.046   37.177  -23.500 1.00 47.64 ? 287 HOH A O   1 
HETATM 2154 O O   . HOH D 3 .   ? -21.678 15.131  -5.646  1.00 35.59 ? 288 HOH A O   1 
HETATM 2155 O O   . HOH D 3 .   ? -6.338  27.396  -1.586  1.00 37.92 ? 289 HOH A O   1 
HETATM 2156 O O   . HOH D 3 .   ? -9.552  41.756  -31.689 1.00 35.65 ? 290 HOH A O   1 
HETATM 2157 O O   . HOH D 3 .   ? -12.261 28.013  -33.889 1.00 33.59 ? 291 HOH A O   1 
HETATM 2158 O O   . HOH D 3 .   ? 5.685   38.016  -17.526 1.00 36.24 ? 292 HOH A O   1 
HETATM 2159 O O   . HOH D 3 .   ? -9.709  42.438  -27.288 1.00 39.26 ? 293 HOH A O   1 
HETATM 2160 O O   . HOH D 3 .   ? 6.566   28.236  -4.905  1.00 39.39 ? 294 HOH A O   1 
HETATM 2161 O O   . HOH E 3 .   ? -24.123 0.122   -17.769 1.00 21.31 ? 154 HOH B O   1 
HETATM 2162 O O   . HOH E 3 .   ? -13.976 10.188  4.298   1.00 33.09 ? 155 HOH B O   1 
HETATM 2163 O O   . HOH E 3 .   ? -11.174 13.814  -13.476 1.00 14.53 ? 156 HOH B O   1 
HETATM 2164 O O   . HOH E 3 .   ? -6.006  17.497  3.322   1.00 37.30 ? 157 HOH B O   1 
HETATM 2165 O O   . HOH E 3 .   ? 4.925   14.747  -2.845  1.00 33.91 ? 158 HOH B O   1 
HETATM 2166 O O   . HOH E 3 .   ? -4.000  6.373   4.734   1.00 19.53 ? 159 HOH B O   1 
HETATM 2167 O O   . HOH E 3 .   ? -19.728 -9.639  -21.549 1.00 35.97 ? 160 HOH B O   1 
HETATM 2168 O O   . HOH E 3 .   ? -4.741  16.465  -19.707 1.00 16.77 ? 161 HOH B O   1 
HETATM 2169 O O   . HOH E 3 .   ? -13.793 -3.717  -5.931  1.00 36.40 ? 162 HOH B O   1 
HETATM 2170 O O   . HOH E 3 .   ? -21.307 -4.611  -5.944  1.00 39.41 ? 163 HOH B O   1 
HETATM 2171 O O   . HOH E 3 .   ? 5.860   5.053   -14.987 1.00 19.58 ? 164 HOH B O   1 
HETATM 2172 O O   . HOH E 3 .   ? -16.309 4.206   -23.650 1.00 21.58 ? 165 HOH B O   1 
HETATM 2173 O O   . HOH E 3 .   ? 5.740   0.103   -10.241 1.00 33.55 ? 166 HOH B O   1 
HETATM 2174 O O   . HOH E 3 .   ? -7.669  6.884   4.350   1.00 20.86 ? 167 HOH B O   1 
HETATM 2175 O O   . HOH E 3 .   ? 9.159   2.939   -15.829 1.00 27.21 ? 168 HOH B O   1 
HETATM 2176 O O   . HOH E 3 .   ? -21.241 -3.888  -9.678  1.00 33.26 ? 169 HOH B O   1 
HETATM 2177 O O   . HOH E 3 .   ? 2.284   13.624  -22.293 1.00 23.21 ? 170 HOH B O   1 
HETATM 2178 O O   . HOH E 3 .   ? -3.754  1.463   -19.598 1.00 28.69 ? 171 HOH B O   1 
HETATM 2179 O O   . HOH E 3 .   ? 0.809   10.117  1.406   1.00 20.63 ? 172 HOH B O   1 
HETATM 2180 O O   . HOH E 3 .   ? 0.138   19.109  -25.560 1.00 36.72 ? 173 HOH B O   1 
HETATM 2181 O O   . HOH E 3 .   ? -3.112  17.504  2.330   1.00 36.06 ? 174 HOH B O   1 
HETATM 2182 O O   . HOH E 3 .   ? 3.534   7.696   -0.015  1.00 24.56 ? 175 HOH B O   1 
HETATM 2183 O O   . HOH E 3 .   ? 4.863   7.366   -2.463  1.00 24.52 ? 176 HOH B O   1 
HETATM 2184 O O   . HOH E 3 .   ? -26.063 -8.993  -12.596 1.00 35.25 ? 177 HOH B O   1 
HETATM 2185 O O   . HOH E 3 .   ? 4.993   14.442  2.838   1.00 41.03 ? 178 HOH B O   1 
HETATM 2186 O O   . HOH E 3 .   ? -16.898 -2.863  -21.955 1.00 25.79 ? 179 HOH B O   1 
HETATM 2187 O O   . HOH E 3 .   ? 5.455   1.711   -17.773 1.00 18.80 ? 180 HOH B O   1 
HETATM 2188 O O   . HOH E 3 .   ? 2.086   12.549  -8.982  1.00 29.13 ? 181 HOH B O   1 
HETATM 2189 O O   . HOH E 3 .   ? -15.321 -4.040  -9.105  1.00 25.55 ? 182 HOH B O   1 
HETATM 2190 O O   . HOH E 3 .   ? -15.468 -4.844  -23.030 1.00 29.87 ? 183 HOH B O   1 
HETATM 2191 O O   . HOH E 3 .   ? -13.071 19.199  -0.490  1.00 26.07 ? 184 HOH B O   1 
HETATM 2192 O O   . HOH E 3 .   ? -1.644  12.017  2.001   1.00 30.88 ? 185 HOH B O   1 
HETATM 2193 O O   . HOH E 3 .   ? -10.034 14.438  -16.654 1.00 25.47 ? 186 HOH B O   1 
HETATM 2194 O O   . HOH E 3 .   ? 5.151   12.299  1.060   1.00 35.97 ? 187 HOH B O   1 
HETATM 2195 O O   . HOH E 3 .   ? -9.942  15.143  -23.772 1.00 29.47 ? 188 HOH B O   1 
HETATM 2196 O O   . HOH E 3 .   ? -24.656 9.727   -15.417 1.00 42.64 ? 189 HOH B O   1 
HETATM 2197 O O   . HOH E 3 .   ? -19.667 9.682   -14.775 1.00 37.39 ? 190 HOH B O   1 
HETATM 2198 O O   . HOH E 3 .   ? -12.365 15.045  -15.708 1.00 25.58 ? 191 HOH B O   1 
HETATM 2199 O O   . HOH E 3 .   ? 0.555   4.408   0.041   1.00 22.48 ? 192 HOH B O   1 
HETATM 2200 O O   . HOH E 3 .   ? -16.968 11.181  -1.904  1.00 33.76 ? 193 HOH B O   1 
HETATM 2201 O O   . HOH E 3 .   ? 4.502   13.431  -8.697  1.00 30.64 ? 194 HOH B O   1 
HETATM 2202 O O   . HOH E 3 .   ? -19.279 6.193   -29.626 1.00 32.88 ? 195 HOH B O   1 
HETATM 2203 O O   . HOH E 3 .   ? -15.222 -7.674  -23.038 1.00 38.37 ? 196 HOH B O   1 
HETATM 2204 O O   . HOH E 3 .   ? -1.982  -3.223  -1.907  1.00 32.67 ? 197 HOH B O   1 
HETATM 2205 O O   . HOH E 3 .   ? -17.867 8.018   -21.775 1.00 22.28 ? 198 HOH B O   1 
HETATM 2206 O O   . HOH E 3 .   ? 7.949   8.992   -9.096  1.00 35.03 ? 199 HOH B O   1 
HETATM 2207 O O   . HOH E 3 .   ? 10.814  8.331   -1.631  1.00 31.24 ? 200 HOH B O   1 
HETATM 2208 O O   . HOH E 3 .   ? -12.928 13.080  -17.588 1.00 28.88 ? 201 HOH B O   1 
HETATM 2209 O O   . HOH E 3 .   ? 7.554   8.416   -12.952 1.00 38.36 ? 202 HOH B O   1 
HETATM 2210 O O   . HOH E 3 .   ? 5.814   12.617  -6.805  1.00 30.63 ? 203 HOH B O   1 
HETATM 2211 O O   . HOH E 3 .   ? -2.366  11.834  4.349   1.00 34.48 ? 204 HOH B O   1 
HETATM 2212 O O   . HOH E 3 .   ? 10.653  3.678   -1.208  1.00 36.66 ? 205 HOH B O   1 
HETATM 2213 O O   . HOH E 3 .   ? 0.560   -4.355  -1.460  1.00 40.05 ? 206 HOH B O   1 
HETATM 2214 O O   . HOH E 3 .   ? -23.284 4.780   -19.430 1.00 25.55 ? 207 HOH B O   1 
HETATM 2215 O O   . HOH E 3 .   ? -10.322 8.050   -25.754 1.00 32.11 ? 208 HOH B O   1 
HETATM 2216 O O   . HOH E 3 .   ? -18.901 6.980   -7.868  1.00 26.62 ? 209 HOH B O   1 
HETATM 2217 O O   . HOH E 3 .   ? 3.271   3.803   -0.286  1.00 37.55 ? 210 HOH B O   1 
HETATM 2218 O O   . HOH E 3 .   ? 1.098   2.240   2.489   1.00 30.93 ? 211 HOH B O   1 
HETATM 2219 O O   . HOH E 3 .   ? 9.443   3.533   -6.516  1.00 39.56 ? 212 HOH B O   1 
HETATM 2220 O O   . HOH E 3 .   ? -16.986 12.288  -5.658  1.00 28.19 ? 213 HOH B O   1 
HETATM 2221 O O   . HOH E 3 .   ? -19.449 11.875  -6.406  1.00 39.22 ? 214 HOH B O   1 
HETATM 2222 O O   . HOH E 3 .   ? -19.518 10.054  -27.623 1.00 32.50 ? 215 HOH B O   1 
HETATM 2223 O O   . HOH E 3 .   ? -14.794 -11.473 -17.777 1.00 34.47 ? 216 HOH B O   1 
HETATM 2224 O O   . HOH E 3 .   ? 10.143  0.103   -17.205 1.00 41.68 ? 217 HOH B O   1 
HETATM 2225 O O   . HOH E 3 .   ? 6.464   10.375  -14.350 1.00 30.33 ? 218 HOH B O   1 
HETATM 2226 O O   . HOH E 3 .   ? -11.226 -10.409 -20.175 1.00 31.96 ? 219 HOH B O   1 
HETATM 2227 O O   . HOH E 3 .   ? -11.795 11.939  -20.053 1.00 30.78 ? 220 HOH B O   1 
HETATM 2228 O O   . HOH E 3 .   ? -8.776  -4.327  -1.518  1.00 31.27 ? 221 HOH B O   1 
HETATM 2229 O O   . HOH E 3 .   ? -8.849  -5.730  -28.048 1.00 39.41 ? 222 HOH B O   1 
HETATM 2230 O O   . HOH E 3 .   ? -18.699 -5.012  -8.968  1.00 38.74 ? 223 HOH B O   1 
HETATM 2231 O O   . HOH E 3 .   ? -24.629 -2.434  -8.801  1.00 40.86 ? 224 HOH B O   1 
HETATM 2232 O O   . HOH E 3 .   ? -16.676 -8.500  -20.804 1.00 37.98 ? 225 HOH B O   1 
HETATM 2233 O O   . HOH E 3 .   ? -5.311  19.371  -0.255  1.00 44.51 ? 226 HOH B O   1 
HETATM 2234 O O   . HOH E 3 .   ? -11.246 11.360  -22.474 1.00 36.00 ? 227 HOH B O   1 
HETATM 2235 O O   . HOH E 3 .   ? -9.767  12.975  3.512   1.00 30.59 ? 228 HOH B O   1 
HETATM 2236 O O   . HOH E 3 .   ? 3.543   14.129  5.354   1.00 25.98 ? 229 HOH B O   1 
HETATM 2237 O O   . HOH E 3 .   ? -14.472 11.512  2.021   1.00 40.82 ? 230 HOH B O   1 
HETATM 2238 O O   . HOH E 3 .   ? -13.626 -7.809  -25.979 1.00 41.36 ? 231 HOH B O   1 
HETATM 2239 O O   . HOH E 3 .   ? -16.395 2.774   -25.790 1.00 32.04 ? 232 HOH B O   1 
HETATM 2240 O O   . HOH E 3 .   ? 2.835   16.261  -1.586  1.00 42.74 ? 233 HOH B O   1 
HETATM 2241 O O   . HOH E 3 .   ? 11.385  4.234   -7.954  1.00 43.08 ? 234 HOH B O   1 
HETATM 2242 O O   . HOH E 3 .   ? 10.606  5.413   -3.070  1.00 44.87 ? 235 HOH B O   1 
HETATM 2243 O O   . HOH E 3 .   ? -13.954 -8.810  -19.946 1.00 33.51 ? 236 HOH B O   1 
HETATM 2244 O O   . HOH E 3 .   ? 8.126   13.740  -6.529  1.00 43.41 ? 237 HOH B O   1 
HETATM 2245 O O   . HOH E 3 .   ? -7.428  -7.617  -27.035 1.00 41.54 ? 238 HOH B O   1 
HETATM 2246 O O   . HOH E 3 .   ? 7.168   12.208  -12.180 1.00 42.65 ? 239 HOH B O   1 
HETATM 2247 O O   . HOH E 3 .   ? -24.663 6.926   -12.095 1.00 40.19 ? 240 HOH B O   1 
HETATM 2248 O O   . HOH E 3 .   ? 8.037   8.286   -1.625  1.00 33.20 ? 241 HOH B O   1 
HETATM 2249 O O   . HOH E 3 .   ? -2.967  -7.319  -10.640 1.00 48.50 ? 242 HOH B O   1 
HETATM 2250 O O   . HOH E 3 .   ? 2.094   11.198  -25.946 1.00 48.50 ? 243 HOH B O   1 
HETATM 2251 O O   . HOH E 3 .   ? -12.128 10.414  -24.708 1.00 35.78 ? 244 HOH B O   1 
HETATM 2252 O O   . HOH E 3 .   ? 13.752  5.659   -7.989  1.00 49.89 ? 245 HOH B O   1 
HETATM 2253 O O   . HOH E 3 .   ? -9.703  13.434  -19.235 1.00 32.04 ? 246 HOH B O   1 
HETATM 2254 O O   . HOH E 3 .   ? -18.150 -0.566  -22.977 1.00 24.07 ? 247 HOH B O   1 
HETATM 2255 O O   . HOH E 3 .   ? 4.121   3.266   2.440   1.00 31.82 ? 248 HOH B O   1 
HETATM 2256 O O   . HOH E 3 .   ? -1.723  14.393  -28.228 1.00 25.94 ? 249 HOH B O   1 
HETATM 2257 O O   . HOH E 3 .   ? -0.291  15.905  -2.148  1.00 34.57 ? 250 HOH B O   1 
HETATM 2258 O O   . HOH E 3 .   ? -19.904 11.016  -18.691 1.00 36.74 ? 251 HOH B O   1 
HETATM 2259 O O   . HOH E 3 .   ? 11.462  1.979   -5.150  1.00 45.80 ? 252 HOH B O   1 
HETATM 2260 O O   . HOH E 3 .   ? 7.258   -0.329  -16.753 1.00 42.22 ? 253 HOH B O   1 
HETATM 2261 O O   . HOH E 3 .   ? -1.127  0.184   -20.208 1.00 30.93 ? 254 HOH B O   1 
HETATM 2262 O O   . HOH E 3 .   ? -18.525 8.720   -1.246  1.00 35.83 ? 255 HOH B O   1 
HETATM 2263 O O   . HOH E 3 .   ? -8.454  17.517  -26.965 1.00 36.23 ? 256 HOH B O   1 
HETATM 2264 O O   . HOH E 3 .   ? -22.988 -6.976  -20.720 1.00 33.70 ? 257 HOH B O   1 
HETATM 2265 O O   . HOH E 3 .   ? 6.731   5.539   -1.406  1.00 34.92 ? 258 HOH B O   1 
HETATM 2266 O O   . HOH E 3 .   ? -8.545  -7.193  -8.706  1.00 32.16 ? 259 HOH B O   1 
HETATM 2267 O O   . HOH E 3 .   ? 4.450   10.634  -8.417  1.00 32.07 ? 260 HOH B O   1 
HETATM 2268 O O   . HOH E 3 .   ? -3.899  -2.972  -23.351 1.00 28.66 ? 261 HOH B O   1 
HETATM 2269 O O   . HOH E 3 .   ? -18.989 9.497   -24.953 1.00 29.68 ? 262 HOH B O   1 
HETATM 2270 O O   . HOH E 3 .   ? 1.599   -5.697  -11.765 1.00 39.37 ? 263 HOH B O   1 
HETATM 2271 O O   . HOH E 3 .   ? -8.808  4.821   -26.349 1.00 33.63 ? 264 HOH B O   1 
HETATM 2272 O O   . HOH E 3 .   ? -19.442 10.333  -21.525 1.00 35.81 ? 265 HOH B O   1 
HETATM 2273 O O   . HOH E 3 .   ? -12.931 5.363   -25.535 1.00 40.06 ? 266 HOH B O   1 
HETATM 2274 O O   . HOH E 3 .   ? -18.617 9.108   -5.806  1.00 29.94 ? 267 HOH B O   1 
HETATM 2275 O O   . HOH E 3 .   ? -2.737  -4.345  -21.092 1.00 35.33 ? 268 HOH B O   1 
HETATM 2276 O O   . HOH E 3 .   ? 2.044   11.107  -23.246 1.00 32.57 ? 269 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  ?   ?   ?   A . n 
A 1 78  GLU 78  78  ?   ?   ?   A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 ?   ?   ?   A . n 
A 1 131 ASN 131 131 ?   ?   ?   A . n 
A 1 132 GLU 132 132 ?   ?   ?   A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  ARG 46  46  46  ARG ARG B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  ?   ?   ?   B . n 
B 1 69  ARG 69  69  ?   ?   ?   B . n 
B 1 70  LYS 70  70  ?   ?   ?   B . n 
B 1 71  HIS 71  71  ?   ?   ?   B . n 
B 1 72  GLY 72  72  ?   ?   ?   B . n 
B 1 73  GLY 73  73  ?   ?   ?   B . n 
B 1 74  PRO 74  74  ?   ?   ?   B . n 
B 1 75  LYS 75  75  ?   ?   ?   B . n 
B 1 76  ASP 76  76  ?   ?   ?   B . n 
B 1 77  GLU 77  77  ?   ?   ?   B . n 
B 1 78  GLU 78  78  ?   ?   ?   B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 ?   ?   ?   B . n 
B 1 126 LEU 126 126 ?   ?   ?   B . n 
B 1 127 GLY 127 127 ?   ?   ?   B . n 
B 1 128 LYS 128 128 ?   ?   ?   B . n 
B 1 129 GLY 129 129 ?   ?   ?   B . n 
B 1 130 GLY 130 130 ?   ?   ?   B . n 
B 1 131 ASN 131 131 ?   ?   ?   B . n 
B 1 132 GLU 132 132 ?   ?   ?   B . n 
B 1 133 GLU 133 133 ?   ?   ?   B . n 
B 1 134 SER 134 134 ?   ?   ?   B . n 
B 1 135 THR 135 135 ?   ?   ?   B . n 
B 1 136 LYS 136 136 ?   ?   ?   B . n 
B 1 137 THR 137 137 ?   ?   ?   B . n 
B 1 138 GLY 138 138 ?   ?   ?   B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PS5 1   154 1   PS5 PS5 A . 
D 3 HOH 1   155 1   HOH HOH A . 
D 3 HOH 2   156 156 HOH HOH A . 
D 3 HOH 3   157 2   HOH HOH A . 
D 3 HOH 4   158 3   HOH HOH A . 
D 3 HOH 5   159 159 HOH HOH A . 
D 3 HOH 6   160 6   HOH HOH A . 
D 3 HOH 7   161 161 HOH HOH A . 
D 3 HOH 8   162 9   HOH HOH A . 
D 3 HOH 9   163 10  HOH HOH A . 
D 3 HOH 10  164 164 HOH HOH A . 
D 3 HOH 11  165 165 HOH HOH A . 
D 3 HOH 12  166 12  HOH HOH A . 
D 3 HOH 13  167 167 HOH HOH A . 
D 3 HOH 14  168 168 HOH HOH A . 
D 3 HOH 15  169 15  HOH HOH A . 
D 3 HOH 16  170 170 HOH HOH A . 
D 3 HOH 17  171 171 HOH HOH A . 
D 3 HOH 18  172 172 HOH HOH A . 
D 3 HOH 19  174 174 HOH HOH A . 
D 3 HOH 20  175 175 HOH HOH A . 
D 3 HOH 21  176 176 HOH HOH A . 
D 3 HOH 22  177 16  HOH HOH A . 
D 3 HOH 23  178 17  HOH HOH A . 
D 3 HOH 24  179 179 HOH HOH A . 
D 3 HOH 25  180 180 HOH HOH A . 
D 3 HOH 26  181 18  HOH HOH A . 
D 3 HOH 27  182 182 HOH HOH A . 
D 3 HOH 28  183 183 HOH HOH A . 
D 3 HOH 29  184 184 HOH HOH A . 
D 3 HOH 30  185 185 HOH HOH A . 
D 3 HOH 31  186 186 HOH HOH A . 
D 3 HOH 32  187 19  HOH HOH A . 
D 3 HOH 33  188 188 HOH HOH A . 
D 3 HOH 34  189 23  HOH HOH A . 
D 3 HOH 35  190 24  HOH HOH A . 
D 3 HOH 36  191 191 HOH HOH A . 
D 3 HOH 37  192 192 HOH HOH A . 
D 3 HOH 38  193 26  HOH HOH A . 
D 3 HOH 39  194 194 HOH HOH A . 
D 3 HOH 40  195 195 HOH HOH A . 
D 3 HOH 41  196 27  HOH HOH A . 
D 3 HOH 42  197 30  HOH HOH A . 
D 3 HOH 43  198 198 HOH HOH A . 
D 3 HOH 44  199 32  HOH HOH A . 
D 3 HOH 45  200 200 HOH HOH A . 
D 3 HOH 46  201 201 HOH HOH A . 
D 3 HOH 47  202 33  HOH HOH A . 
D 3 HOH 48  203 203 HOH HOH A . 
D 3 HOH 49  204 35  HOH HOH A . 
D 3 HOH 50  205 37  HOH HOH A . 
D 3 HOH 51  206 38  HOH HOH A . 
D 3 HOH 52  207 207 HOH HOH A . 
D 3 HOH 53  208 208 HOH HOH A . 
D 3 HOH 54  209 209 HOH HOH A . 
D 3 HOH 55  210 39  HOH HOH A . 
D 3 HOH 56  211 211 HOH HOH A . 
D 3 HOH 57  212 212 HOH HOH A . 
D 3 HOH 58  213 213 HOH HOH A . 
D 3 HOH 59  214 214 HOH HOH A . 
D 3 HOH 60  215 41  HOH HOH A . 
D 3 HOH 61  216 216 HOH HOH A . 
D 3 HOH 62  217 42  HOH HOH A . 
D 3 HOH 63  218 218 HOH HOH A . 
D 3 HOH 64  219 219 HOH HOH A . 
D 3 HOH 65  220 43  HOH HOH A . 
D 3 HOH 66  221 221 HOH HOH A . 
D 3 HOH 67  222 45  HOH HOH A . 
D 3 HOH 68  223 47  HOH HOH A . 
D 3 HOH 69  224 48  HOH HOH A . 
D 3 HOH 70  225 49  HOH HOH A . 
D 3 HOH 71  226 50  HOH HOH A . 
D 3 HOH 72  227 53  HOH HOH A . 
D 3 HOH 73  228 228 HOH HOH A . 
D 3 HOH 74  229 229 HOH HOH A . 
D 3 HOH 75  230 230 HOH HOH A . 
D 3 HOH 76  231 54  HOH HOH A . 
D 3 HOH 77  232 232 HOH HOH A . 
D 3 HOH 78  233 59  HOH HOH A . 
D 3 HOH 79  234 234 HOH HOH A . 
D 3 HOH 80  235 235 HOH HOH A . 
D 3 HOH 81  236 236 HOH HOH A . 
D 3 HOH 82  237 60  HOH HOH A . 
D 3 HOH 83  238 238 HOH HOH A . 
D 3 HOH 84  239 61  HOH HOH A . 
D 3 HOH 85  240 240 HOH HOH A . 
D 3 HOH 86  241 241 HOH HOH A . 
D 3 HOH 87  242 63  HOH HOH A . 
D 3 HOH 88  243 64  HOH HOH A . 
D 3 HOH 89  244 65  HOH HOH A . 
D 3 HOH 90  245 66  HOH HOH A . 
D 3 HOH 91  246 246 HOH HOH A . 
D 3 HOH 92  247 247 HOH HOH A . 
D 3 HOH 93  248 248 HOH HOH A . 
D 3 HOH 94  249 249 HOH HOH A . 
D 3 HOH 95  250 250 HOH HOH A . 
D 3 HOH 96  251 67  HOH HOH A . 
D 3 HOH 97  252 71  HOH HOH A . 
D 3 HOH 98  253 74  HOH HOH A . 
D 3 HOH 99  254 254 HOH HOH A . 
D 3 HOH 100 255 255 HOH HOH A . 
D 3 HOH 101 256 75  HOH HOH A . 
D 3 HOH 102 257 76  HOH HOH A . 
D 3 HOH 103 258 79  HOH HOH A . 
D 3 HOH 104 259 80  HOH HOH A . 
D 3 HOH 105 260 81  HOH HOH A . 
D 3 HOH 106 261 84  HOH HOH A . 
D 3 HOH 107 262 86  HOH HOH A . 
D 3 HOH 108 263 87  HOH HOH A . 
D 3 HOH 109 264 90  HOH HOH A . 
D 3 HOH 110 265 93  HOH HOH A . 
D 3 HOH 111 266 94  HOH HOH A . 
D 3 HOH 112 267 99  HOH HOH A . 
D 3 HOH 113 268 103 HOH HOH A . 
D 3 HOH 114 269 104 HOH HOH A . 
D 3 HOH 115 270 106 HOH HOH A . 
D 3 HOH 116 271 110 HOH HOH A . 
D 3 HOH 117 272 111 HOH HOH A . 
D 3 HOH 118 273 115 HOH HOH A . 
D 3 HOH 119 274 116 HOH HOH A . 
D 3 HOH 120 275 117 HOH HOH A . 
D 3 HOH 121 276 118 HOH HOH A . 
D 3 HOH 122 277 122 HOH HOH A . 
D 3 HOH 123 278 124 HOH HOH A . 
D 3 HOH 124 279 125 HOH HOH A . 
D 3 HOH 125 280 127 HOH HOH A . 
D 3 HOH 126 281 129 HOH HOH A . 
D 3 HOH 127 282 131 HOH HOH A . 
D 3 HOH 128 283 132 HOH HOH A . 
D 3 HOH 129 284 133 HOH HOH A . 
D 3 HOH 130 285 135 HOH HOH A . 
D 3 HOH 131 286 136 HOH HOH A . 
D 3 HOH 132 287 139 HOH HOH A . 
D 3 HOH 133 288 143 HOH HOH A . 
D 3 HOH 134 289 146 HOH HOH A . 
D 3 HOH 135 290 147 HOH HOH A . 
D 3 HOH 136 291 148 HOH HOH A . 
D 3 HOH 137 292 151 HOH HOH A . 
D 3 HOH 138 293 152 HOH HOH A . 
D 3 HOH 139 294 154 HOH HOH A . 
E 3 HOH 1   154 4   HOH HOH B . 
E 3 HOH 2   155 155 HOH HOH B . 
E 3 HOH 3   156 5   HOH HOH B . 
E 3 HOH 4   157 157 HOH HOH B . 
E 3 HOH 5   158 158 HOH HOH B . 
E 3 HOH 6   159 7   HOH HOH B . 
E 3 HOH 7   160 160 HOH HOH B . 
E 3 HOH 8   161 8   HOH HOH B . 
E 3 HOH 9   162 162 HOH HOH B . 
E 3 HOH 10  163 163 HOH HOH B . 
E 3 HOH 11  164 11  HOH HOH B . 
E 3 HOH 12  165 13  HOH HOH B . 
E 3 HOH 13  166 166 HOH HOH B . 
E 3 HOH 14  167 14  HOH HOH B . 
E 3 HOH 15  168 20  HOH HOH B . 
E 3 HOH 16  169 169 HOH HOH B . 
E 3 HOH 17  170 21  HOH HOH B . 
E 3 HOH 18  171 22  HOH HOH B . 
E 3 HOH 19  172 25  HOH HOH B . 
E 3 HOH 20  173 173 HOH HOH B . 
E 3 HOH 21  174 29  HOH HOH B . 
E 3 HOH 22  175 31  HOH HOH B . 
E 3 HOH 23  176 34  HOH HOH B . 
E 3 HOH 24  177 177 HOH HOH B . 
E 3 HOH 25  178 178 HOH HOH B . 
E 3 HOH 26  179 36  HOH HOH B . 
E 3 HOH 27  180 40  HOH HOH B . 
E 3 HOH 28  181 181 HOH HOH B . 
E 3 HOH 29  182 44  HOH HOH B . 
E 3 HOH 30  183 46  HOH HOH B . 
E 3 HOH 31  184 51  HOH HOH B . 
E 3 HOH 32  185 52  HOH HOH B . 
E 3 HOH 33  186 55  HOH HOH B . 
E 3 HOH 34  187 187 HOH HOH B . 
E 3 HOH 35  188 56  HOH HOH B . 
E 3 HOH 36  189 189 HOH HOH B . 
E 3 HOH 37  190 190 HOH HOH B . 
E 3 HOH 38  191 57  HOH HOH B . 
E 3 HOH 39  192 58  HOH HOH B . 
E 3 HOH 40  193 193 HOH HOH B . 
E 3 HOH 41  194 62  HOH HOH B . 
E 3 HOH 42  195 68  HOH HOH B . 
E 3 HOH 43  196 196 HOH HOH B . 
E 3 HOH 44  197 197 HOH HOH B . 
E 3 HOH 45  198 69  HOH HOH B . 
E 3 HOH 46  199 199 HOH HOH B . 
E 3 HOH 47  200 70  HOH HOH B . 
E 3 HOH 48  201 72  HOH HOH B . 
E 3 HOH 49  202 202 HOH HOH B . 
E 3 HOH 50  203 73  HOH HOH B . 
E 3 HOH 51  204 204 HOH HOH B . 
E 3 HOH 52  205 205 HOH HOH B . 
E 3 HOH 53  206 206 HOH HOH B . 
E 3 HOH 54  207 77  HOH HOH B . 
E 3 HOH 55  208 78  HOH HOH B . 
E 3 HOH 56  209 82  HOH HOH B . 
E 3 HOH 57  210 210 HOH HOH B . 
E 3 HOH 58  211 83  HOH HOH B . 
E 3 HOH 59  212 85  HOH HOH B . 
E 3 HOH 60  213 88  HOH HOH B . 
E 3 HOH 61  214 89  HOH HOH B . 
E 3 HOH 62  215 215 HOH HOH B . 
E 3 HOH 63  216 91  HOH HOH B . 
E 3 HOH 64  217 217 HOH HOH B . 
E 3 HOH 65  218 92  HOH HOH B . 
E 3 HOH 66  219 95  HOH HOH B . 
E 3 HOH 67  220 220 HOH HOH B . 
E 3 HOH 68  221 96  HOH HOH B . 
E 3 HOH 69  222 222 HOH HOH B . 
E 3 HOH 70  223 223 HOH HOH B . 
E 3 HOH 71  224 224 HOH HOH B . 
E 3 HOH 72  225 225 HOH HOH B . 
E 3 HOH 73  226 226 HOH HOH B . 
E 3 HOH 74  227 227 HOH HOH B . 
E 3 HOH 75  228 97  HOH HOH B . 
E 3 HOH 76  229 98  HOH HOH B . 
E 3 HOH 77  230 100 HOH HOH B . 
E 3 HOH 78  231 231 HOH HOH B . 
E 3 HOH 79  232 101 HOH HOH B . 
E 3 HOH 80  233 233 HOH HOH B . 
E 3 HOH 81  234 102 HOH HOH B . 
E 3 HOH 82  235 105 HOH HOH B . 
E 3 HOH 83  236 107 HOH HOH B . 
E 3 HOH 84  237 237 HOH HOH B . 
E 3 HOH 85  238 108 HOH HOH B . 
E 3 HOH 86  239 239 HOH HOH B . 
E 3 HOH 87  240 109 HOH HOH B . 
E 3 HOH 88  241 112 HOH HOH B . 
E 3 HOH 89  242 242 HOH HOH B . 
E 3 HOH 90  243 243 HOH HOH B . 
E 3 HOH 91  244 244 HOH HOH B . 
E 3 HOH 92  245 245 HOH HOH B . 
E 3 HOH 93  246 113 HOH HOH B . 
E 3 HOH 94  247 114 HOH HOH B . 
E 3 HOH 95  248 119 HOH HOH B . 
E 3 HOH 96  249 120 HOH HOH B . 
E 3 HOH 97  250 121 HOH HOH B . 
E 3 HOH 98  251 251 HOH HOH B . 
E 3 HOH 99  252 252 HOH HOH B . 
E 3 HOH 100 253 253 HOH HOH B . 
E 3 HOH 101 254 123 HOH HOH B . 
E 3 HOH 102 255 126 HOH HOH B . 
E 3 HOH 103 256 128 HOH HOH B . 
E 3 HOH 104 257 130 HOH HOH B . 
E 3 HOH 105 258 134 HOH HOH B . 
E 3 HOH 106 259 137 HOH HOH B . 
E 3 HOH 107 260 138 HOH HOH B . 
E 3 HOH 108 261 140 HOH HOH B . 
E 3 HOH 109 262 141 HOH HOH B . 
E 3 HOH 110 263 142 HOH HOH B . 
E 3 HOH 111 264 144 HOH HOH B . 
E 3 HOH 112 265 145 HOH HOH B . 
E 3 HOH 113 266 149 HOH HOH B . 
E 3 HOH 114 267 150 HOH HOH B . 
E 3 HOH 115 268 153 HOH HOH B . 
E 3 HOH 116 269 28  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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1680  ? 
1 MORE         -23   ? 
1 'SSA (A^2)'  12510 ? 
# 
_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_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 2010-01-19 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2021-10-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Database references'       
3 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' struct_ref_seq_dif 
3 3 'Structure model' struct_site        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_database_2.pdbx_DOI'                
2 3 'Structure model' '_database_2.pdbx_database_accession' 
3 3 'Structure model' '_struct_ref_seq_dif.details'         
4 3 'Structure model' '_struct_site.pdbx_auth_asym_id'      
5 3 'Structure model' '_struct_site.pdbx_auth_comp_id'      
6 3 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CrystalClear 'data collection' .                        ? 1 
PHENIX       refinement        '(phenix.refine: 1.4_4)' ? 2 
HKL-2000     'data reduction'  .                        ? 3 
HKL-2000     'data scaling'    .                        ? 4 
# 
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 SG A CYS 111 ? ? S5 A PS5 154 ? ? 2.03 
2 1 SG B CYS 111 ? ? S1 A PS5 154 ? ? 2.03 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     65 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -164.23 
_pdbx_validate_torsion.psi             69.77 
# 
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 GLU 77  ? A GLU 77  
2  1 Y 1 A GLU 78  ? A GLU 78  
3  1 Y 1 A GLY 130 ? A GLY 130 
4  1 Y 1 A ASN 131 ? A ASN 131 
5  1 Y 1 A GLU 132 ? A GLU 132 
6  1 Y 1 B SER 68  ? B SER 68  
7  1 Y 1 B ARG 69  ? B ARG 69  
8  1 Y 1 B LYS 70  ? B LYS 70  
9  1 Y 1 B HIS 71  ? B HIS 71  
10 1 Y 1 B GLY 72  ? B GLY 72  
11 1 Y 1 B GLY 73  ? B GLY 73  
12 1 Y 1 B PRO 74  ? B PRO 74  
13 1 Y 1 B LYS 75  ? B LYS 75  
14 1 Y 1 B ASP 76  ? B ASP 76  
15 1 Y 1 B GLU 77  ? B GLU 77  
16 1 Y 1 B GLU 78  ? B GLU 78  
17 1 Y 1 B ASP 125 ? B ASP 125 
18 1 Y 1 B LEU 126 ? B LEU 126 
19 1 Y 1 B GLY 127 ? B GLY 127 
20 1 Y 1 B LYS 128 ? B LYS 128 
21 1 Y 1 B GLY 129 ? B GLY 129 
22 1 Y 1 B GLY 130 ? B GLY 130 
23 1 Y 1 B ASN 131 ? B ASN 131 
24 1 Y 1 B GLU 132 ? B GLU 132 
25 1 Y 1 B GLU 133 ? B GLU 133 
26 1 Y 1 B SER 134 ? B SER 134 
27 1 Y 1 B THR 135 ? B THR 135 
28 1 Y 1 B LYS 136 ? B LYS 136 
29 1 Y 1 B THR 137 ? B THR 137 
30 1 Y 1 B GLY 138 ? B GLY 138 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 PENTASULFIDE-SULFUR PS5 
3 water               HOH 
# 
