data_1P1V
# 
_entry.id   1P1V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   1P1V         pdb_00001p1v 10.2210/pdb1p1v/pdb 
RCSB  RCSB018909   ?            ?                   
WWPDB D_1000018909 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1AZV 'Crystal Structure of FALS-associated Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant G37R'           unspecified 
PDB 1OZU 'Crystal Structure of FALS-associated Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant S134N'          unspecified 
PDB 1OZT 'Crystal Structure of FALS-associated Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant apo-H46R'       unspecified 
PDB 1OEZ 'Crystal Structure of FALS-associated Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant Zn-loaded H46R' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1P1V 
_pdbx_database_status.recvd_initial_deposition_date   2003-04-14 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Elam, J.S.'      1 
'Malek, K.'       2 
'Rodriguez, J.A.' 3 
'Doucette, P.A.'  4 
'Taylor, A.B.'    5 
'Hayward, L.J.'   6 
'Cabelli, D.E.'   7 
'Valentine, J.S.' 8 
'Hart, P.J.'      9 
# 
_citation.id                        primary 
_citation.title                     
;An Alternative Mechanism of Bicarbonate-mediated Peroxidation by Copper-Zinc Superoxide Dismutase: RATES ENHANCED VIA PROPOSED ENZYME-ASSOCIATED PEROXYCARBONATE INTERMEDIATE
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            278 
_citation.page_first                21032 
_citation.page_last                 21039 
_citation.year                      2003 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12649272 
_citation.pdbx_database_id_DOI      10.1074/jbc.M300484200 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Elam, J.S.'      1 ? 
primary 'Malek, K.'       2 ? 
primary 'Rodriguez, J.A.' 3 ? 
primary 'Doucette, P.A.'  4 ? 
primary 'Taylor, A.B.'    5 ? 
primary 'Hayward, L.J.'   6 ? 
primary 'Cabelli, D.E.'   7 ? 
primary 'Valentine, J.S.' 8 ? 
primary 'Hart, P.J.'      9 ? 
# 
_cell.entry_id           1P1V 
_cell.length_a           70.449 
_cell.length_b           101.140 
_cell.length_c           143.080 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              24 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1P1V 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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]' 15866.621 3   1.15.1.1 D125H ? ? 
2 non-polymer syn 'SULFATE ION'                  96.063    3   ?        ?     ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    6   ?        ?     ? ? 
4 water       nat water                          18.015    736 ?        ?     ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDH(CSX)IIGRTLVVHEKADHLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADHLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C 
_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  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CSX 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 HIS n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               
;baker's yeast
;
_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                     Saccharomyces 
_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           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1P1V A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 1P1V B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
3 1 1P1V C 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1P1V CSX A 111 ? UNP P00441 CYS 111 'modified residue'    111 1 
1 1P1V HIS A 125 ? UNP P00441 ASP 125 'engineered mutation' 125 2 
2 1P1V CSX B 111 ? UNP P00441 CYS 111 'modified residue'    111 3 
2 1P1V HIS B 125 ? UNP P00441 ASP 125 'engineered mutation' 125 4 
3 1P1V CSX C 111 ? UNP P00441 CYS 111 'modified residue'    111 5 
3 1P1V HIS C 125 ? UNP P00441 ASP 125 'engineered mutation' 125 6 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE          ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE         ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE       ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'  ? 'C4 H7 N O4'     133.103 
CSX 'L-peptide linking' n 'S-OXY CYSTEINE' ? 'C3 H7 N O3 S'   137.158 
CYS 'L-peptide linking' y CYSTEINE         ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE        ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'  ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE          ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE        ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER            ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE       ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE          ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE           ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE    ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE          ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE           ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'    ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE        ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN       ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE           ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'       ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1P1V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.42 
_exptl_crystal.density_percent_sol   49.2 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            278 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    'zinc sulfate, PEG MME 550, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
loop_
_diffrn.id 
_diffrn.ambient_temp 
_diffrn.ambient_temp_details 
_diffrn.crystal_id 
1 100 ? 1 
2 100 ? 1 
# 
loop_
_diffrn_detector.diffrn_id 
_diffrn_detector.detector 
_diffrn_detector.type 
_diffrn_detector.pdbx_collection_date 
_diffrn_detector.details 
1 CCD 'ADSC QUANTUM 4' 2001-06-07 mirrors 
2 CCD 'ADSC QUANTUM 4' 2001-06-07 mirrors 
# 
loop_
_diffrn_radiation.diffrn_id 
_diffrn_radiation.wavelength_id 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l 
_diffrn_radiation.monochromator 
_diffrn_radiation.pdbx_diffrn_protocol 
_diffrn_radiation.pdbx_scattering_type 
1 1 M mirrors 'SINGLE WAVELENGTH' x-ray 
2 1 M mirrors 'SINGLE WAVELENGTH' x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 1.0000 1.0 
2 1.2811 1.0 
# 
loop_
_diffrn_source.diffrn_id 
_diffrn_source.source 
_diffrn_source.type 
_diffrn_source.pdbx_synchrotron_site 
_diffrn_source.pdbx_synchrotron_beamline 
_diffrn_source.pdbx_wavelength 
_diffrn_source.pdbx_wavelength_list 
1 SYNCHROTRON 'NSLS BEAMLINE X12B' NSLS X12B ? 1.0000 
2 SYNCHROTRON 'NSLS BEAMLINE X8C'  NSLS X8C  ? 1.2811 
# 
_reflns.entry_id                     1P1V 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50.0 
_reflns.d_resolution_high            1.40 
_reflns.number_obs                   95234 
_reflns.number_all                   95234 
_reflns.percent_possible_obs         94.7 
_reflns.pdbx_Rmerge_I_obs            0.048 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        30.16 
_reflns.B_iso_Wilson_estimate        13.05 
_reflns.pdbx_redundancy              6.91 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1,2 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.40 
_reflns_shell.d_res_low              1.45 
_reflns_shell.percent_possible_all   85.1 
_reflns_shell.Rmerge_I_obs           0.426 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.62 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      8434 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1P1V 
_refine.ls_number_reflns_obs                     91976 
_refine.ls_number_reflns_all                     94875 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             10.00 
_refine.ls_d_res_high                            1.40 
_refine.ls_percent_reflns_obs                    93.9 
_refine.ls_R_factor_obs                          0.1463 
_refine.ls_R_factor_all                          0.1474 
_refine.ls_R_factor_R_work                       0.1463 
_refine.ls_R_factor_R_free                       0.2121 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  2899 
_refine.ls_number_parameters                     35428 
_refine.ls_number_restraints                     41292 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R' 
_refine.details                                  'ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 4.1%' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          SAD 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'ENGH AND HUBER' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1P1V 
_refine_analyze.Luzzati_coordinate_error_obs    0.176 
_refine_analyze.Luzzati_sigma_a_obs             0.1268 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.198 
_refine_analyze.Luzzati_sigma_a_free            0.1073 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      0 
_refine_analyze.occupancy_sum_hydrogen          0.00 
_refine_analyze.occupancy_sum_non_hydrogen      3936.00 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3180 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.number_atoms_solvent             736 
_refine_hist.number_atoms_total               3937 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        10.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.011  ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              0.028  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    0.0303 ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.055  ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.071  ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.015  ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.004  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.053  ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.083  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1P1V 
_pdbx_refine.R_factor_all_no_cutoff                      0.1474 
_pdbx_refine.R_factor_obs_no_cutoff                      ? 
_pdbx_refine.free_R_factor_no_cutoff                     ? 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     ? 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            ? 
_pdbx_refine.R_factor_all_4sig_cutoff                    0.1328 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               78424 
_pdbx_refine.number_reflns_obs_no_cutoff                 ? 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  1P1V 
_struct.title                     
'Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1P1V 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'beta-barrel, bound anion at copper site, CuZnSOD peroxidation mechanism, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 
;The biological assembly is a homodimer. In the asymmetric unit we have one homodimer and one monomer. The monomer's dimeric partner is generated through a crystallographic two fold axis at the dimer interface.
;
? 
2 ? ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 CYS A 57  ? GLY A 61  ? CYS A 57  GLY A 61  5 ? 5 
HELX_P HELX_P2 2 SER A 107 ? CSX A 111 ? SER A 107 CSX A 111 5 ? 5 
HELX_P HELX_P3 3 ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4 4 CYS C 57  ? GLY C 61  ? CYS C 57  GLY C 61  5 ? 5 
HELX_P HELX_P5 5 SER C 107 ? CSX C 111 ? SER C 107 CSX C 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 ? ? ? ? ? ? ? 2.097 ? ? 
disulf2  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
disulf3  disulf ?    ? C CYS 57  SG  ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
covale1  covale both ? A HIS 110 C   ? ? ? 1_555 A CSX 111 N  ? ? A HIS 110 A CSX 111 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale2  covale both ? A CSX 111 C   ? ? ? 1_555 A ILE 112 N  ? ? A CSX 111 A ILE 112 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale3  covale both ? B HIS 110 C   ? ? ? 1_555 B CSX 111 N  ? ? B HIS 110 B CSX 111 1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale4  covale both ? B CSX 111 C   ? ? ? 1_555 B ILE 112 N  ? ? B CSX 111 B ILE 112 1_555 ? ? ? ? ? ? ? 1.352 ? ? 
covale5  covale both ? C HIS 110 C   ? ? ? 1_555 C CSX 111 N  ? ? C HIS 110 C CSX 111 1_555 ? ? ? ? ? ? ? 1.330 ? ? 
covale6  covale both ? C CSX 111 C   ? ? ? 1_555 C ILE 112 N  ? ? C CSX 111 C ILE 112 1_555 ? ? ? ? ? ? ? 1.348 ? ? 
metalc1  metalc ?    ? A HIS 46  ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 46  A ZN  201 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc2  metalc ?    ? A HIS 48  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 48  A ZN  201 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc3  metalc ?    ? A HIS 63  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 63  A ZN  202 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc4  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 71  A ZN  202 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc5  metalc ?    ? A HIS 80  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 80  A ZN  202 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc6  metalc ?    ? A ASP 83  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
metalc7  metalc ?    ? A ASP 83  OD2 ? ? ? 1_555 F ZN  .   ZN ? ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 2.746 ? ? 
metalc8  metalc ?    ? A HIS 120 NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 120 A ZN  201 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc9  metalc ?    ? E ZN  .   ZN  ? ? ? 1_555 D SO4 .   O1 ? ? A ZN  201 A SO4 801 1_555 ? ? ? ? ? ? ? 1.950 ? ? 
metalc10 metalc ?    ? B HIS 46  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 46  B ZN  203 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc11 metalc ?    ? B HIS 48  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 48  B ZN  203 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc12 metalc ?    ? B HIS 63  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? B HIS 63  B ZN  204 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc13 metalc ?    ? B HIS 71  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? B HIS 71  B ZN  204 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc14 metalc ?    ? B HIS 80  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? B HIS 80  B ZN  204 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc15 metalc ?    ? B ASP 83  OD1 ? ? ? 1_555 I ZN  .   ZN ? ? B ASP 83  B ZN  204 1_555 ? ? ? ? ? ? ? 1.758 ? ? 
metalc16 metalc ?    ? B ASP 83  OD2 ? ? ? 1_555 I ZN  .   ZN ? ? B ASP 83  B ZN  204 1_555 ? ? ? ? ? ? ? 2.645 ? ? 
metalc17 metalc ?    ? B HIS 120 NE2 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 120 B ZN  203 1_555 ? ? ? ? ? ? ? 1.924 ? ? 
metalc18 metalc ?    ? H ZN  .   ZN  ? ? ? 1_555 G SO4 .   O2 ? ? B ZN  203 B SO4 802 1_555 ? ? ? ? ? ? ? 1.918 ? ? 
metalc19 metalc ?    ? C HIS 46  ND1 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 46  C ZN  205 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc20 metalc ?    ? C HIS 48  NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 48  C ZN  205 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc21 metalc ?    ? C HIS 63  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 63  C ZN  206 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc22 metalc ?    ? C HIS 71  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 71  C ZN  206 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc23 metalc ?    ? C HIS 80  ND1 ? ? ? 1_555 L ZN  .   ZN ? ? C HIS 80  C ZN  206 1_555 ? ? ? ? ? ? ? 1.983 ? ? 
metalc24 metalc ?    ? C ASP 83  OD1 ? ? ? 1_555 L ZN  .   ZN ? ? C ASP 83  C ZN  206 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc25 metalc ?    ? C HIS 120 NE2 ? ? ? 1_555 K ZN  .   ZN ? ? C HIS 120 C ZN  205 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc26 metalc ?    ? K ZN  .   ZN  ? ? ? 1_555 J SO4 .   O1 ? ? C ZN  205 C SO4 803 1_555 ? ? ? ? ? ? ? 1.953 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
A 4 LYS A 3   ? LEU A 8   ? LYS A 3   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 THR B 2   ? LEU B 8   ? THR B 2   LEU B 8   
C 5 GLY B 150 ? ALA B 152 ? GLY B 150 ALA B 152 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
E 1 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
E 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
E 3 GLN C 15  ? GLU C 21  ? GLN C 15  GLU C 21  
E 4 LYS C 3   ? LEU C 8   ? LYS C 3   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 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 ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N VAL A 119 ? N VAL A 119 O ALA A 145 ? O ALA A 145 
C 1 2 O ALA B 95  ? O ALA B 95  N ILE B 35  ? N ILE B 35  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O GLN B 22  ? O GLN B 22  N THR B 2   ? N THR B 2   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
D 3 4 N VAL B 119 ? N VAL B 119 O ALA B 145 ? O ALA B 145 
E 1 2 O ALA C 95  ? O ALA C 95  N ILE C 35  ? N ILE C 35  
E 2 3 O LYS C 30  ? O LYS C 30  N GLU C 21  ? N GLU C 21  
E 3 4 O GLY C 16  ? O GLY C 16  N LEU C 8   ? N LEU C 8   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
F 3 4 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A SO4 801 ? 12 'BINDING SITE FOR RESIDUE SO4 A 801' 
AC2 Software B SO4 802 ? 10 'BINDING SITE FOR RESIDUE SO4 B 802' 
AC3 Software C SO4 803 ? 12 'BINDING SITE FOR RESIDUE SO4 C 803' 
AC4 Software A ZN  201 ? 5  'BINDING SITE FOR RESIDUE ZN A 201'  
AC5 Software A ZN  202 ? 4  'BINDING SITE FOR RESIDUE ZN A 202'  
AC6 Software B ZN  203 ? 5  'BINDING SITE FOR RESIDUE ZN B 203'  
AC7 Software B ZN  204 ? 4  'BINDING SITE FOR RESIDUE ZN B 204'  
AC8 Software C ZN  205 ? 5  'BINDING SITE FOR RESIDUE ZN C 205'  
AC9 Software C ZN  206 ? 4  'BINDING SITE FOR RESIDUE ZN C 206'  
# 
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 12 HIS A 46  ? HIS A 46  . ? 1_555 ? 
2  AC1 12 HIS A 48  ? HIS A 48  . ? 1_555 ? 
3  AC1 12 HIS A 63  ? HIS A 63  . ? 1_555 ? 
4  AC1 12 HIS A 120 ? HIS A 120 . ? 1_555 ? 
5  AC1 12 THR A 137 ? THR A 137 . ? 1_555 ? 
6  AC1 12 ARG A 143 ? ARG A 143 . ? 1_555 ? 
7  AC1 12 ZN  E .   ? ZN  A 201 . ? 1_555 ? 
8  AC1 12 HOH M .   ? HOH A 823 . ? 1_555 ? 
9  AC1 12 HOH M .   ? HOH A 852 . ? 1_555 ? 
10 AC1 12 HOH M .   ? HOH A 868 . ? 1_555 ? 
11 AC1 12 HOH M .   ? HOH A 877 . ? 1_555 ? 
12 AC1 12 ASN C 26  ? ASN C 26  . ? 5_545 ? 
13 AC2 10 HIS B 46  ? HIS B 46  . ? 1_555 ? 
14 AC2 10 HIS B 48  ? HIS B 48  . ? 1_555 ? 
15 AC2 10 HIS B 63  ? HIS B 63  . ? 1_555 ? 
16 AC2 10 HIS B 120 ? HIS B 120 . ? 1_555 ? 
17 AC2 10 THR B 137 ? THR B 137 . ? 1_555 ? 
18 AC2 10 ARG B 143 ? ARG B 143 . ? 1_555 ? 
19 AC2 10 ZN  H .   ? ZN  B 203 . ? 1_555 ? 
20 AC2 10 HOH N .   ? HOH B 881 . ? 1_555 ? 
21 AC2 10 HOH N .   ? HOH B 897 . ? 1_555 ? 
22 AC2 10 HOH N .   ? HOH B 899 . ? 1_555 ? 
23 AC3 12 ASN A 26  ? ASN A 26  . ? 1_455 ? 
24 AC3 12 HIS C 46  ? HIS C 46  . ? 1_555 ? 
25 AC3 12 HIS C 48  ? HIS C 48  . ? 1_555 ? 
26 AC3 12 HIS C 63  ? HIS C 63  . ? 1_555 ? 
27 AC3 12 HIS C 120 ? HIS C 120 . ? 1_555 ? 
28 AC3 12 THR C 137 ? THR C 137 . ? 1_555 ? 
29 AC3 12 ARG C 143 ? ARG C 143 . ? 1_555 ? 
30 AC3 12 ZN  K .   ? ZN  C 205 . ? 1_555 ? 
31 AC3 12 HOH O .   ? HOH C 819 . ? 1_555 ? 
32 AC3 12 HOH O .   ? HOH C 826 . ? 1_555 ? 
33 AC3 12 HOH O .   ? HOH C 838 . ? 1_555 ? 
34 AC3 12 HOH O .   ? HOH C 862 . ? 1_555 ? 
35 AC4 5  HIS A 46  ? HIS A 46  . ? 1_555 ? 
36 AC4 5  HIS A 48  ? HIS A 48  . ? 1_555 ? 
37 AC4 5  HIS A 63  ? HIS A 63  . ? 1_555 ? 
38 AC4 5  HIS A 120 ? HIS A 120 . ? 1_555 ? 
39 AC4 5  SO4 D .   ? SO4 A 801 . ? 1_555 ? 
40 AC5 4  HIS A 63  ? HIS A 63  . ? 1_555 ? 
41 AC5 4  HIS A 71  ? HIS A 71  . ? 1_555 ? 
42 AC5 4  HIS A 80  ? HIS A 80  . ? 1_555 ? 
43 AC5 4  ASP A 83  ? ASP A 83  . ? 1_555 ? 
44 AC6 5  HIS B 46  ? HIS B 46  . ? 1_555 ? 
45 AC6 5  HIS B 48  ? HIS B 48  . ? 1_555 ? 
46 AC6 5  HIS B 63  ? HIS B 63  . ? 1_555 ? 
47 AC6 5  HIS B 120 ? HIS B 120 . ? 1_555 ? 
48 AC6 5  SO4 G .   ? SO4 B 802 . ? 1_555 ? 
49 AC7 4  HIS B 63  ? HIS B 63  . ? 1_555 ? 
50 AC7 4  HIS B 71  ? HIS B 71  . ? 1_555 ? 
51 AC7 4  HIS B 80  ? HIS B 80  . ? 1_555 ? 
52 AC7 4  ASP B 83  ? ASP B 83  . ? 1_555 ? 
53 AC8 5  HIS C 46  ? HIS C 46  . ? 1_555 ? 
54 AC8 5  HIS C 48  ? HIS C 48  . ? 1_555 ? 
55 AC8 5  HIS C 63  ? HIS C 63  . ? 1_555 ? 
56 AC8 5  HIS C 120 ? HIS C 120 . ? 1_555 ? 
57 AC8 5  SO4 J .   ? SO4 C 803 . ? 1_555 ? 
58 AC9 4  HIS C 63  ? HIS C 63  . ? 1_555 ? 
59 AC9 4  HIS C 71  ? HIS C 71  . ? 1_555 ? 
60 AC9 4  HIS C 80  ? HIS C 80  . ? 1_555 ? 
61 AC9 4  ASP C 83  ? ASP C 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1P1V 
_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]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    1P1V 
_atom_sites.fract_transf_matrix[1][1]   0.014195 
_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]   0.009887 
_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]   0.006989 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 24.824  40.457 9.393   1.00 42.61 ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 23.353  40.535 9.303   1.00 31.78 ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 22.792  41.726 10.061  1.00 30.88 ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 23.225  42.018 11.169  1.00 37.44 ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 22.736  39.233 9.801   1.00 43.33 ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 21.826  42.454 9.485   1.00 26.89 ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 21.230  43.580 10.159  1.00 21.36 ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 19.752  43.380 10.491  1.00 17.60 ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 19.286  44.136 11.352  1.00 16.72 ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 21.334  44.957 9.464   1.00 21.15 ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 20.551  44.905 8.237   1.00 32.43 ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 22.749  45.254 9.020   1.00 36.13 ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 19.092  42.398 9.896   1.00 18.05 ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 17.699  42.146 10.258  1.00 14.78 ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 17.425  40.658 10.337  1.00 13.29 ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 17.966  39.863 9.576   1.00 15.60 ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 16.751  42.716 9.195   1.00 19.23 ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 16.830  44.240 9.121   1.00 23.24 ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 16.035  44.675 7.885   1.00 38.26 ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 14.704  45.314 8.253   1.00 47.69 ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 14.155  46.182 7.168   1.00 50.25 ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 16.549  40.312 11.268  1.00 14.06 ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 16.139  38.895 11.398  1.00 13.76 ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 14.670  38.871 11.781  1.00 13.24 ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 14.093  39.899 12.155  1.00 15.34 ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 17.013  38.167 12.418  1.00 13.96 ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 14.085  37.688 11.687  1.00 13.79 ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 12.655  37.544 11.932  1.00 13.79 ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 12.411  36.139 12.451  1.00 15.40 ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 13.193  35.215 12.173  1.00 14.84 ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 11.851  37.849 10.652  1.00 15.34 ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 12.051  36.792 9.570   1.00 17.89 ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 10.350  38.009 10.890  1.00 18.46 ? 5    VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 11.335  35.972 13.208  1.00 14.17 ? 6    CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 11.022  34.629 13.735  1.00 13.70 ? 6    CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 9.503   34.511 13.830  1.00 13.10 ? 6    CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 8.802   35.399 14.401  1.00 14.70 ? 6    CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 11.690  34.476 15.114  1.00 15.34 ? 6    CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 11.244  32.934 15.946  1.00 14.72 ? 6    CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 8.978   33.443 13.270  1.00 12.87 ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 7.539   33.122 13.364  1.00 14.12 ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 7.382   32.123 14.509  1.00 14.66 ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 7.956   31.026 14.492  1.00 15.94 ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 7.002   32.598 12.042  1.00 15.49 ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 5.526   32.247 12.182  1.00 18.82 ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 7.193   33.643 10.930  1.00 17.81 ? 7    VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 6.624   32.504 15.531  1.00 15.81 ? 8    LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 6.443   31.667 16.716  1.00 15.23 ? 8    LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 5.160   30.848 16.551  1.00 13.44 ? 8    LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 4.098   31.444 16.326  1.00 16.37 ? 8    LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 6.312   32.502 17.991  1.00 16.50 ? 8    LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 7.498   33.333 18.487  1.00 18.49 ? 8    LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 8.608   32.405 18.956  1.00 28.69 ? 8    LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 7.955   34.344 17.487  1.00 23.18 ? 8    LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 5.229   29.526 16.690  1.00 14.45 ? 9    LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 4.040   28.685 16.640  1.00 18.04 ? 9    LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 4.223   27.527 17.606  1.00 13.97 ? 9    LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 5.355   27.210 17.978  1.00 15.07 ? 9    LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 3.771   28.079 15.245  1.00 25.52 ? 9    LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 3.416   29.104 14.190  1.00 31.45 ? 9    LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 3.349   28.542 12.781  1.00 41.45 ? 9    LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 2.580   29.506 11.886  1.00 44.69 ? 9    LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 2.986   29.355 10.461  1.00 54.51 ? 9    LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 3.102   26.901 17.935  1.00 14.37 ? 10   GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 3.141   25.754 18.798  1.00 16.82 ? 10   GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 1.908   24.892 18.491  1.00 15.98 ? 10   GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 1.264   25.006 17.448  1.00 20.37 ? 10   GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 1.599   24.067 19.464  1.00 17.00 ? 11   ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 0.488   23.128 19.395  1.00 17.53 ? 11   ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? -0.806  23.756 19.894  1.00 17.65 ? 11   ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? -1.872  23.182 19.636  1.00 23.12 ? 11   ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 0.828   21.885 20.211  1.00 20.20 ? 11   ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 1.985   21.130 19.563  1.00 15.67 ? 11   ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 1.825   20.736 18.375  1.00 20.79 ? 11   ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 2.989   20.959 20.267  1.00 17.00 ? 11   ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? -0.723  24.891 20.569  1.00 18.84 ? 12   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? -1.903  25.584 21.081  1.00 18.74 ? 12   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? -2.156  26.866 20.317  1.00 18.35 ? 12   GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? -1.756  27.033 19.166  1.00 20.57 ? 12   GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? -2.836  27.815 20.956  1.00 18.49 ? 13   PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? -3.239  29.048 20.296  1.00 18.76 ? 13   PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? -2.163  30.116 20.303  1.00 17.05 ? 13   PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? -2.417  31.206 19.768  1.00 20.50 ? 13   PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -4.403  29.521 21.187  1.00 18.90 ? 13   PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -3.934  29.094 22.563  1.00 18.92 ? 13   PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? -3.279  27.749 22.364  1.00 19.02 ? 13   PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? -1.004  29.878 20.880  1.00 16.12 ? 14   VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? -0.042  31.000 20.949  1.00 16.73 ? 14   VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 0.719   31.110 19.634  1.00 16.55 ? 14   VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 1.307   30.155 19.103  1.00 18.04 ? 14   VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 0.916   30.792 22.125  1.00 16.53 ? 14   VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 1.931   31.946 22.211  1.00 17.79 ? 14   VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 0.157   30.686 23.443  1.00 18.16 ? 14   VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 0.729   32.333 19.066  1.00 17.13 ? 15   GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 1.426   32.513 17.813  1.00 17.89 ? 15   GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 1.889   33.955 17.711  1.00 17.07 ? 15   GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 1.245   34.837 18.285  1.00 19.68 ? 15   GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 0.559   32.187 16.588  1.00 25.93 ? 15   GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? -0.718  32.996 16.536  1.00 30.65 ? 15   GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? -1.549  32.700 15.309  1.00 35.58 ? 15   GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? -1.221  33.150 14.204  1.00 54.37 ? 15   GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? -2.628  31.969 15.469  1.00 38.88 ? 15   GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 2.960   34.220 16.975  1.00 16.51 ? 16   GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 3.285   35.629 16.792  1.00 19.54 ? 16   GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 4.449   35.745 15.823  1.00 14.71 ? 16   GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 4.971   34.759 15.333  1.00 16.85 ? 16   GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 4.852   36.967 15.605  1.00 15.21 ? 17   ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 5.988   37.297 14.781  1.00 15.43 ? 17   ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 6.859   38.313 15.512  1.00 14.76 ? 17   ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 6.368   39.354 16.006  1.00 17.82 ? 17   ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 5.557   37.890 13.426  1.00 18.66 ? 17   ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 4.623   36.920 12.713  1.00 20.44 ? 17   ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 6.804   38.306 12.640  1.00 19.34 ? 17   ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 3.986   37.474 11.464  1.00 26.36 ? 17   ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 8.143   37.979 15.616  1.00 14.75 ? 18   ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 9.069   38.886 16.288  1.00 12.91 ? 18   ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 10.154  39.241 15.307  1.00 12.56 ? 18   ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 10.702  38.367 14.622  1.00 14.10 ? 18   ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 9.643   38.235 17.567  1.00 13.30 ? 18   ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 8.531   37.968 18.588  1.00 14.34 ? 18   ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 10.747  39.114 18.112  1.00 14.03 ? 18   ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 7.975   39.218 19.252  1.00 15.89 ? 18   ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 10.457  40.523 15.241  1.00 13.24 ? 19   ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 11.437  41.082 14.339  1.00 12.95 ? 19   ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 12.677  41.548 15.112  1.00 12.02 ? 19   ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 12.560  41.962 16.275  1.00 14.28 ? 19   ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 10.890  42.326 13.619  1.00 14.70 ? 19   ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 9.570   42.017 12.913  1.00 14.76 ? 19   ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 9.588   41.420 11.857  1.00 20.10 ? 19   ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 8.431   42.413 13.471  1.00 19.13 ? 19   ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 13.835  41.490 14.453  1.00 13.38 ? 20   PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 15.078  41.936 15.080  1.00 13.25 ? 20   PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 15.773  42.902 14.144  1.00 13.09 ? 20   PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 15.751  42.652 12.916  1.00 16.13 ? 20   PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 16.041  40.770 15.351  1.00 12.62 ? 20   PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 15.465  39.670 16.245  1.00 12.39 ? 20   PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 14.625  38.701 15.730  1.00 14.07 ? 20   PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 15.791  39.612 17.577  1.00 15.00 ? 20   PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 14.117  37.696 16.521  1.00 14.64 ? 20   PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 15.280  38.613 18.401  1.00 15.18 ? 20   PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 14.429  37.639 17.857  1.00 16.41 ? 20   PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 16.380  43.963 14.673  1.00 12.88 ? 21   GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 17.141  44.847 13.791  1.00 13.92 ? 21   GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 18.370  45.320 14.561  1.00 14.00 ? 21   GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 18.270  45.727 15.710  1.00 16.01 ? 21   GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 16.328  46.041 13.312  1.00 17.15 ? 21   GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 17.143  46.984 12.410  1.00 21.12 ? 21   GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 16.182  48.091 11.979  1.00 32.45 ? 21   GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 15.470  47.869 10.989  1.00 45.14 ? 21   GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 16.167  49.140 12.659  1.00 46.79 ? 21   GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 19.516  45.253 13.893  1.00 13.65 ? 22   GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 20.765  45.661 14.506  1.00 14.55 ? 22   GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 21.532  46.510 13.484  1.00 19.34 ? 22   GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 22.177  45.963 12.598  1.00 20.95 ? 22   GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 21.544  44.417 14.938  1.00 15.32 ? 22   GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 22.802  44.801 15.734  1.00 14.39 ? 22   GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 23.584  43.573 16.107  1.00 12.39 ? 22   GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 23.527  42.551 15.389  1.00 13.93 ? 22   GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 24.340  43.655 17.192  1.00 12.96 ? 22   GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 21.404  47.821 13.693  1.00 22.62 ? 23   LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 21.989  48.860 12.868  1.00 26.06 ? 23   LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 23.514  48.790 12.781  1.00 22.28 ? 23   LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 24.125  48.999 11.712  1.00 24.86 ? 23   LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 21.538  50.240 13.379  1.00 34.27 ? 23   LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 22.281  51.429 12.873  1.00 38.79 ? 23   LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 21.472  52.586 12.349  1.00 47.88 ? 23   LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 22.204  53.370 11.268  1.00 56.18 ? 23   LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 23.481  52.742 10.808  1.00 68.09 ? 23   LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 24.146  48.503 13.902  1.00 18.59 ? 24   GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 25.596  48.431 14.021  1.00 17.88 ? 24   GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 26.013  47.085 14.601  1.00 14.78 ? 24   GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 25.423  46.623 15.598  1.00 15.14 ? 24   GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 26.143  49.552 14.914  1.00 25.15 ? 24   GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 26.073  50.913 14.245  1.00 35.97 ? 24   GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 26.013  52.106 15.187  1.00 48.47 ? 24   GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 26.060  51.955 16.429  1.00 66.35 ? 24   GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 25.904  53.265 14.702  1.00 59.38 ? 24   GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 27.012  46.451 14.024  1.00 16.80 ? 25   SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 27.345  45.080 14.440  1.00 17.98 ? 25   SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 27.813  45.051 15.885  1.00 17.07 ? 25   SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 27.639  43.985 16.516  1.00 17.18 ? 25   SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 28.368  44.410 13.502  1.00 21.89 ? 25   SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 29.532  45.213 13.435  1.00 27.27 ? 25   SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 28.328  46.145 16.438  1.00 13.80 ? 26   ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 28.727  46.154 17.847  1.00 12.21 ? 26   ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 27.689  46.880 18.692  1.00 12.52 ? 26   ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 27.983  47.256 19.847  1.00 13.04 ? 26   ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 30.107  46.810 18.009  1.00 13.91 ? 26   ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 31.215  45.979 17.394  1.00 13.46 ? 26   ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 31.069  44.750 17.252  1.00 16.45 ? 26   ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 32.307  46.660 17.064  1.00 14.07 ? 26   ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 26.468  47.092 18.202  1.00 12.28 ? 27   GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 25.430  47.851 18.863  1.00 12.26 ? 27   GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 24.306  46.940 19.376  1.00 12.39 ? 27   GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 24.330  45.711 19.222  1.00 13.41 ? 27   GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 23.297  47.559 19.980  1.00 12.80 ? 28   PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 22.143  46.822 20.480  1.00 13.91 ? 28   PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 21.268  46.313 19.317  1.00 12.69 ? 28   PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 21.301  46.759 18.166  1.00 14.38 ? 28   PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 21.380  47.901 21.249  1.00 15.77 ? 28   PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 22.239  49.118 21.320  1.00 17.61 ? 28   PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 23.280  49.014 20.274  1.00 14.09 ? 28   PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 20.425  45.360 19.665  1.00 13.20 ? 29   VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 19.408  44.782 18.803  1.00 13.02 ? 29   VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 18.036  45.259 19.249  1.00 12.31 ? 29   VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 17.710  45.075 20.417  1.00 14.25 ? 29   VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 19.451  43.232 18.840  1.00 11.87 ? 29   VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 18.415  42.606 17.925  1.00 13.87 ? 29   VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 20.878  42.831 18.442  1.00 13.43 ? 29   VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 17.267  45.824 18.336  1.00 13.26 ? 30   LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 15.856  46.113 18.604  1.00 12.75 ? 30   LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 15.030  44.847 18.339  1.00 15.22 ? 30   LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 15.254  44.206 17.313  1.00 13.71 ? 30   LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 15.305  47.246 17.730  1.00 15.07 ? 30   LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 16.102  48.533 17.922  1.00 20.63 ? 30   LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 15.514  49.686 17.110  1.00 29.02 ? 30   LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 16.261  50.974 17.439  1.00 39.98 ? 30   LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 15.706  52.175 16.753  1.00 53.19 ? 30   LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 14.144  44.505 19.250  1.00 12.63 ? 31   VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 13.279  43.342 19.183  1.00 13.94 ? 31   VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 11.835  43.806 19.266  1.00 14.51 ? 31   VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 11.472  44.456 20.264  1.00 15.91 ? 31   VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 13.614  42.392 20.341  1.00 14.90 ? 31   VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 12.791  41.102 20.231  1.00 15.27 ? 31   VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 15.096  42.017 20.420  1.00 15.07 ? 31   VAL A CG2 1 
ATOM   226  N  N   . TRP A 1 32  ? 11.000  43.502 18.267  1.00 13.40 ? 32   TRP A N   1 
ATOM   227  C  CA  . TRP A 1 32  ? 9.627   44.048 18.325  1.00 14.59 ? 32   TRP A CA  1 
ATOM   228  C  C   . TRP A 1 32  ? 8.684   43.166 17.533  1.00 13.19 ? 32   TRP A C   1 
ATOM   229  O  O   . TRP A 1 32  ? 9.116   42.523 16.580  1.00 15.90 ? 32   TRP A O   1 
ATOM   230  C  CB  . TRP A 1 32  ? 9.567   45.484 17.825  1.00 18.24 ? 32   TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 32  ? 9.572   45.601 16.337  1.00 19.81 ? 32   TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 32  ? 8.485   45.748 15.505  1.00 22.03 ? 32   TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 32  ? 10.741  45.565 15.521  1.00 20.47 ? 32   TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 32  ? 8.956   45.807 14.215  1.00 25.04 ? 32   TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 32  ? 10.324  45.702 14.188  1.00 23.13 ? 32   TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 32  ? 12.103  45.440 15.792  1.00 22.67 ? 32   TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 32  ? 11.189  45.720 13.087  1.00 24.98 ? 32   TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 32  ? 12.949  45.456 14.684  1.00 23.48 ? 32   TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 32  ? 12.519  45.592 13.353  1.00 23.63 ? 32   TRP A CH2 1 
ATOM   240  N  N   . GLY A 1 33  ? 7.431   43.153 17.949  1.00 14.29 ? 33   GLY A N   1 
ATOM   241  C  CA  . GLY A 1 33  ? 6.418   42.358 17.260  1.00 13.18 ? 33   GLY A CA  1 
ATOM   242  C  C   . GLY A 1 33  ? 5.284   42.146 18.251  1.00 14.29 ? 33   GLY A C   1 
ATOM   243  O  O   . GLY A 1 33  ? 5.102   42.959 19.157  1.00 18.61 ? 33   GLY A O   1 
ATOM   244  N  N   . SER A 1 34  ? 4.542   41.062 18.031  1.00 17.99 ? 34   SER A N   1 
ATOM   245  C  CA  . SER A 1 34  ? 3.334   40.787 18.792  1.00 17.75 ? 34   SER A CA  1 
ATOM   246  C  C   . SER A 1 34  ? 3.147   39.279 18.862  1.00 16.55 ? 34   SER A C   1 
ATOM   247  O  O   . SER A 1 34  ? 3.367   38.589 17.866  1.00 20.75 ? 34   SER A O   1 
ATOM   248  C  CB  . SER A 1 34  ? 2.106   41.449 18.146  1.00 20.31 ? 34   SER A CB  1 
ATOM   249  O  OG  . SER A 1 34  ? 1.017   41.384 19.071  1.00 25.71 ? 34   SER A OG  1 
ATOM   250  N  N   . ILE A 1 35  ? 2.761   38.851 20.047  1.00 16.13 ? 35   ILE A N   1 
ATOM   251  C  CA  . ILE A 1 35  ? 2.384   37.465 20.285  1.00 16.54 ? 35   ILE A CA  1 
ATOM   252  C  C   . ILE A 1 35  ? 0.969   37.446 20.851  1.00 16.40 ? 35   ILE A C   1 
ATOM   253  O  O   . ILE A 1 35  ? 0.671   38.206 21.759  1.00 17.47 ? 35   ILE A O   1 
ATOM   254  C  CB  . ILE A 1 35  ? 3.325   36.766 21.271  1.00 16.70 ? 35   ILE A CB  1 
ATOM   255  C  CG1 . ILE A 1 35  ? 4.780   36.996 20.865  1.00 16.72 ? 35   ILE A CG1 1 
ATOM   256  C  CG2 . ILE A 1 35  ? 2.930   35.306 21.415  1.00 16.48 ? 35   ILE A CG2 1 
ATOM   257  C  CD1 . ILE A 1 35  ? 5.782   36.569 21.900  1.00 19.03 ? 35   ILE A CD1 1 
ATOM   258  N  N   . LYS A 1 36  ? 0.124   36.601 20.288  1.00 15.46 ? 36   LYS A N   1 
ATOM   259  C  CA  . LYS A 1 36  ? -1.247  36.499 20.711  1.00 15.47 ? 36   LYS A CA  1 
ATOM   260  C  C   . LYS A 1 36  ? -1.583  35.083 21.183  1.00 15.63 ? 36   LYS A C   1 
ATOM   261  O  O   . LYS A 1 36  ? -0.807  34.101 21.048  1.00 16.97 ? 36   LYS A O   1 
ATOM   262  C  CB  . LYS A 1 36  ? -2.199  36.947 19.600  1.00 20.21 ? 36   LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 36  ? -2.205  36.018 18.401  1.00 23.10 ? 36   LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 36  ? -3.171  36.554 17.348  1.00 31.22 ? 36   LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 36  ? -3.110  35.586 16.166  1.00 39.99 ? 36   LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 36  ? -4.214  34.600 16.232  1.00 52.02 ? 36   LYS A NZ  1 
ATOM   267  N  N   . GLY A 1 37  ? -2.753  35.008 21.817  1.00 17.08 ? 37   GLY A N   1 
ATOM   268  C  CA  . GLY A 1 37  ? -3.239  33.737 22.332  1.00 17.63 ? 37   GLY A CA  1 
ATOM   269  C  C   . GLY A 1 37  ? -2.676  33.368 23.679  1.00 17.99 ? 37   GLY A C   1 
ATOM   270  O  O   . GLY A 1 37  ? -2.817  32.198 24.081  1.00 19.41 ? 37   GLY A O   1 
ATOM   271  N  N   . LEU A 1 38  ? -2.069  34.318 24.365  1.00 16.30 ? 38   LEU A N   1 
ATOM   272  C  CA  . LEU A 1 38  ? -1.452  34.099 25.670  1.00 16.13 ? 38   LEU A CA  1 
ATOM   273  C  C   . LEU A 1 38  ? -2.415  34.324 26.808  1.00 14.16 ? 38   LEU A C   1 
ATOM   274  O  O   . LEU A 1 38  ? -3.387  35.094 26.672  1.00 20.48 ? 38   LEU A O   1 
ATOM   275  C  CB  . LEU A 1 38  ? -0.294  35.088 25.831  1.00 14.96 ? 38   LEU A CB  1 
ATOM   276  C  CG  . LEU A 1 38  ? 0.930   34.762 24.966  1.00 14.41 ? 38   LEU A CG  1 
ATOM   277  C  CD1 . LEU A 1 38  ? 1.907   35.933 24.891  1.00 16.61 ? 38   LEU A CD1 1 
ATOM   278  C  CD2 . LEU A 1 38  ? 1.652   33.551 25.546  1.00 15.32 ? 38   LEU A CD2 1 
ATOM   279  N  N   . THR A 1 39  ? -2.151  33.683 27.949  1.00 15.77 ? 39   THR A N   1 
ATOM   280  C  CA  . THR A 1 39  ? -2.889  34.101 29.132  1.00 16.36 ? 39   THR A CA  1 
ATOM   281  C  C   . THR A 1 39  ? -2.415  35.477 29.615  1.00 15.81 ? 39   THR A C   1 
ATOM   282  O  O   . THR A 1 39  ? -1.239  35.820 29.499  1.00 17.62 ? 39   THR A O   1 
ATOM   283  C  CB  . THR A 1 39  ? -2.713  33.099 30.290  1.00 16.06 ? 39   THR A CB  1 
ATOM   284  O  OG1 . THR A 1 39  ? -1.302  32.982 30.559  1.00 18.59 ? 39   THR A OG1 1 
ATOM   285  C  CG2 . THR A 1 39  ? -3.293  31.738 29.918  1.00 21.48 ? 39   THR A CG2 1 
ATOM   286  N  N   . GLU A 1 40  ? -3.285  36.296 30.172  1.00 16.04 ? 40   GLU A N   1 
ATOM   287  C  CA  . GLU A 1 40  ? -2.951  37.603 30.719  1.00 16.78 ? 40   GLU A CA  1 
ATOM   288  C  C   . GLU A 1 40  ? -1.821  37.513 31.719  1.00 18.35 ? 40   GLU A C   1 
ATOM   289  O  O   . GLU A 1 40  ? -1.942  36.603 32.566  1.00 18.13 ? 40   GLU A O   1 
ATOM   290  C  CB  . GLU A 1 40  ? -4.221  38.193 31.383  1.00 19.86 ? 40   GLU A CB  1 
ATOM   291  C  CG  . GLU A 1 40  ? -3.991  39.632 31.861  1.00 16.91 ? 40   GLU A CG  1 
ATOM   292  C  CD  . GLU A 1 40  ? -5.239  40.236 32.487  1.00 18.59 ? 40   GLU A CD  1 
ATOM   293  O  OE1 . GLU A 1 40  ? -6.339  39.612 32.455  1.00 21.68 ? 40   GLU A OE1 1 
ATOM   294  O  OE2 . GLU A 1 40  ? -5.082  41.337 33.022  1.00 23.55 ? 40   GLU A OE2 1 
ATOM   295  N  N   . GLY A 1 41  ? -0.797  38.364 31.623  1.00 14.89 ? 41   GLY A N   1 
ATOM   296  C  CA  . GLY A 1 41  ? 0.287   38.347 32.627  1.00 18.55 ? 41   GLY A CA  1 
ATOM   297  C  C   . GLY A 1 41  ? 1.638   38.055 31.956  1.00 15.65 ? 41   GLY A C   1 
ATOM   298  O  O   . GLY A 1 41  ? 1.789   38.206 30.729  1.00 15.26 ? 41   GLY A O   1 
ATOM   299  N  N   . LEU A 1 42  ? 2.625   37.675 32.750  1.00 14.79 ? 42   LEU A N   1 
ATOM   300  C  CA  . LEU A 1 42  ? 4.012   37.567 32.297  1.00 12.63 ? 42   LEU A CA  1 
ATOM   301  C  C   . LEU A 1 42  ? 4.315   36.205 31.676  1.00 12.45 ? 42   LEU A C   1 
ATOM   302  O  O   . LEU A 1 42  ? 3.827   35.181 32.182  1.00 15.73 ? 42   LEU A O   1 
ATOM   303  C  CB  . LEU A 1 42  ? 4.967   37.770 33.472  1.00 15.49 ? 42   LEU A CB  1 
ATOM   304  C  CG  . LEU A 1 42  ? 4.859   39.153 34.146  1.00 17.75 ? 42   LEU A CG  1 
ATOM   305  C  CD1 . LEU A 1 42  ? 5.534   39.135 35.508  1.00 21.85 ? 42   LEU A CD1 1 
ATOM   306  C  CD2 . LEU A 1 42  ? 5.530   40.183 33.275  1.00 21.00 ? 42   LEU A CD2 1 
ATOM   307  N  N   . HIS A 1 43  ? 5.129   36.211 30.629  1.00 14.12 ? 43   HIS A N   1 
ATOM   308  C  CA  . HIS A 1 43  ? 5.531   34.984 29.955  1.00 12.57 ? 43   HIS A CA  1 
ATOM   309  C  C   . HIS A 1 43  ? 7.008   34.994 29.631  1.00 11.82 ? 43   HIS A C   1 
ATOM   310  O  O   . HIS A 1 43  ? 7.471   35.908 28.957  1.00 13.35 ? 43   HIS A O   1 
ATOM   311  C  CB  . HIS A 1 43  ? 4.764   34.736 28.639  1.00 11.99 ? 43   HIS A CB  1 
ATOM   312  C  CG  . HIS A 1 43  ? 3.313   34.546 28.950  1.00 13.43 ? 43   HIS A CG  1 
ATOM   313  N  ND1 . HIS A 1 43  ? 2.766   33.295 29.201  1.00 15.40 ? 43   HIS A ND1 1 
ATOM   314  C  CD2 . HIS A 1 43  ? 2.297   35.425 29.087  1.00 13.79 ? 43   HIS A CD2 1 
ATOM   315  C  CE1 . HIS A 1 43  ? 1.473   33.400 29.463  1.00 15.81 ? 43   HIS A CE1 1 
ATOM   316  N  NE2 . HIS A 1 43  ? 1.145   34.694 29.392  1.00 14.68 ? 43   HIS A NE2 1 
ATOM   317  N  N   . GLY A 1 44  ? 7.740   33.997 30.137  1.00 11.77 ? 44   GLY A N   1 
ATOM   318  C  CA  . GLY A 1 44  ? 9.177   33.906 29.871  1.00 11.51 ? 44   GLY A CA  1 
ATOM   319  C  C   . GLY A 1 44  ? 9.507   33.972 28.402  1.00 12.18 ? 44   GLY A C   1 
ATOM   320  O  O   . GLY A 1 44  ? 8.767   33.442 27.548  1.00 11.96 ? 44   GLY A O   1 
ATOM   321  N  N   . PHE A 1 45  ? 10.619  34.650 28.076  1.00 11.21 ? 45   PHE A N   1 
ATOM   322  C  CA  . PHE A 1 45  ? 10.933  34.953 26.673  1.00 11.68 ? 45   PHE A CA  1 
ATOM   323  C  C   . PHE A 1 45  ? 12.413  34.713 26.480  1.00 12.10 ? 45   PHE A C   1 
ATOM   324  O  O   . PHE A 1 45  ? 13.215  35.463 27.043  1.00 12.26 ? 45   PHE A O   1 
ATOM   325  C  CB  . PHE A 1 45  ? 10.530  36.408 26.400  1.00 12.67 ? 45   PHE A CB  1 
ATOM   326  C  CG  . PHE A 1 45  ? 10.525  36.874 24.962  1.00 12.12 ? 45   PHE A CG  1 
ATOM   327  C  CD1 . PHE A 1 45  ? 9.882   36.200 23.949  1.00 13.96 ? 45   PHE A CD1 1 
ATOM   328  C  CD2 . PHE A 1 45  ? 11.183  38.058 24.634  1.00 13.67 ? 45   PHE A CD2 1 
ATOM   329  C  CE1 . PHE A 1 45  ? 9.858   36.658 22.647  1.00 14.88 ? 45   PHE A CE1 1 
ATOM   330  C  CE2 . PHE A 1 45  ? 11.157  38.530 23.340  1.00 16.55 ? 45   PHE A CE2 1 
ATOM   331  C  CZ  . PHE A 1 45  ? 10.503  37.850 22.318  1.00 16.25 ? 45   PHE A CZ  1 
ATOM   332  N  N   . HIS A 1 46  ? 12.779  33.655 25.754  1.00 10.71 ? 46   HIS A N   1 
ATOM   333  C  CA  . HIS A 1 46  ? 14.143  33.193 25.716  1.00 10.05 ? 46   HIS A CA  1 
ATOM   334  C  C   . HIS A 1 46  ? 14.640  32.872 24.323  1.00 10.52 ? 46   HIS A C   1 
ATOM   335  O  O   . HIS A 1 46  ? 13.852  32.405 23.492  1.00 12.09 ? 46   HIS A O   1 
ATOM   336  C  CB  . HIS A 1 46  ? 14.292  31.872 26.494  1.00 10.98 ? 46   HIS A CB  1 
ATOM   337  C  CG  . HIS A 1 46  ? 13.931  31.939 27.943  1.00 11.61 ? 46   HIS A CG  1 
ATOM   338  N  ND1 . HIS A 1 46  ? 13.437  30.830 28.601  1.00 10.85 ? 46   HIS A ND1 1 
ATOM   339  C  CD2 . HIS A 1 46  ? 13.955  32.934 28.852  1.00 12.50 ? 46   HIS A CD2 1 
ATOM   340  C  CE1 . HIS A 1 46  ? 13.197  31.141 29.879  1.00 11.40 ? 46   HIS A CE1 1 
ATOM   341  N  NE2 . HIS A 1 46  ? 13.497  32.427 30.053  1.00 11.71 ? 46   HIS A NE2 1 
ATOM   342  N  N   . VAL A 1 47  ? 15.914  33.038 24.095  1.00 10.25 ? 47   VAL A N   1 
ATOM   343  C  CA  . VAL A 1 47  ? 16.577  32.363 22.976  1.00 9.65  ? 47   VAL A CA  1 
ATOM   344  C  C   . VAL A 1 47  ? 17.225  31.102 23.520  1.00 9.16  ? 47   VAL A C   1 
ATOM   345  O  O   . VAL A 1 47  ? 18.069  31.159 24.413  1.00 11.12 ? 47   VAL A O   1 
ATOM   346  C  CB  . VAL A 1 47  ? 17.648  33.226 22.267  1.00 10.01 ? 47   VAL A CB  1 
ATOM   347  C  CG1 . VAL A 1 47  ? 18.272  32.471 21.088  1.00 11.08 ? 47   VAL A CG1 1 
ATOM   348  C  CG2 . VAL A 1 47  ? 17.086  34.564 21.820  1.00 14.50 ? 47   VAL A CG2 1 
ATOM   349  N  N   . HIS A 1 48  ? 16.732  29.977 23.005  1.00 9.68  ? 48   HIS A N   1 
ATOM   350  C  CA  . HIS A 1 48  ? 17.307  28.664 23.294  1.00 10.20 ? 48   HIS A CA  1 
ATOM   351  C  C   . HIS A 1 48  ? 18.347  28.303 22.249  1.00 10.73 ? 48   HIS A C   1 
ATOM   352  O  O   . HIS A 1 48  ? 18.349  28.807 21.120  1.00 12.86 ? 48   HIS A O   1 
ATOM   353  C  CB  . HIS A 1 48  ? 16.185  27.581 23.339  1.00 10.98 ? 48   HIS A CB  1 
ATOM   354  C  CG  . HIS A 1 48  ? 15.426  27.679 24.647  1.00 10.37 ? 48   HIS A CG  1 
ATOM   355  N  ND1 . HIS A 1 48  ? 15.511  26.688 25.601  1.00 10.55 ? 48   HIS A ND1 1 
ATOM   356  C  CD2 . HIS A 1 48  ? 14.598  28.611 25.178  1.00 10.93 ? 48   HIS A CD2 1 
ATOM   357  C  CE1 . HIS A 1 48  ? 14.751  27.025 26.647  1.00 11.00 ? 48   HIS A CE1 1 
ATOM   358  N  NE2 . HIS A 1 48  ? 14.166  28.202 26.433  1.00 10.36 ? 48   HIS A NE2 1 
ATOM   359  N  N   . GLU A 1 49  ? 19.291  27.436 22.623  1.00 11.61 ? 49   GLU A N   1 
ATOM   360  C  CA  . GLU A 1 49  ? 20.534  27.212 21.910  1.00 11.61 ? 49   GLU A CA  1 
ATOM   361  C  C   . GLU A 1 49  ? 20.373  26.707 20.490  1.00 12.08 ? 49   GLU A C   1 
ATOM   362  O  O   . GLU A 1 49  ? 21.039  27.188 19.554  1.00 12.32 ? 49   GLU A O   1 
ATOM   363  C  CB  . GLU A 1 49  ? 21.412  26.218 22.721  1.00 13.13 ? 49   GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 49  ? 22.794  26.080 22.067  1.00 14.49 ? 49   GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 49  ? 23.717  25.192 22.877  1.00 15.88 ? 49   GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 49  ? 23.304  24.682 23.959  1.00 18.84 ? 49   GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 49  ? 24.866  24.993 22.400  1.00 18.29 ? 49   GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 50  ? 19.491  25.714 20.285  1.00 11.14 ? 50   PHE A N   1 
ATOM   369  C  CA  . PHE A 1 50  ? 19.468  25.053 18.971  1.00 11.93 ? 50   PHE A CA  1 
ATOM   370  C  C   . PHE A 1 50  ? 18.246  25.469 18.176  1.00 10.90 ? 50   PHE A C   1 
ATOM   371  O  O   . PHE A 1 50  ? 17.135  25.546 18.731  1.00 13.09 ? 50   PHE A O   1 
ATOM   372  C  CB  . PHE A 1 50  ? 19.441  23.514 19.170  1.00 12.94 ? 50   PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 50  ? 20.731  23.097 19.875  1.00 14.07 ? 50   PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 50  ? 21.956  23.256 19.243  1.00 16.44 ? 50   PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 50  ? 20.665  22.534 21.136  1.00 16.75 ? 50   PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 50  ? 23.148  22.884 19.865  1.00 16.88 ? 50   PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 50  ? 21.856  22.187 21.779  1.00 16.79 ? 50   PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 50  ? 23.070  22.355 21.142  1.00 18.25 ? 50   PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 51  ? 18.454  25.725 16.900  1.00 12.81 ? 51   GLY A N   1 
ATOM   380  C  CA  . GLY A 1 51  ? 17.335  25.994 15.985  1.00 12.56 ? 51   GLY A CA  1 
ATOM   381  C  C   . GLY A 1 51  ? 16.815  24.664 15.423  1.00 13.00 ? 51   GLY A C   1 
ATOM   382  O  O   . GLY A 1 51  ? 16.705  24.495 14.215  1.00 13.57 ? 51   GLY A O   1 
ATOM   383  N  N   . ASP A 1 52  ? 16.504  23.733 16.321  1.00 13.78 ? 52   ASP A N   1 
ATOM   384  C  CA  . ASP A 1 52  ? 16.039  22.396 15.993  1.00 12.54 ? 52   ASP A CA  1 
ATOM   385  C  C   . ASP A 1 52  ? 14.613  22.276 16.470  1.00 12.57 ? 52   ASP A C   1 
ATOM   386  O  O   . ASP A 1 52  ? 14.401  22.169 17.688  1.00 12.61 ? 52   ASP A O   1 
ATOM   387  C  CB  . ASP A 1 52  ? 16.990  21.380 16.674  1.00 13.48 ? 52   ASP A CB  1 
ATOM   388  C  CG  . ASP A 1 52  ? 16.587  19.929 16.425  1.00 14.30 ? 52   ASP A CG  1 
ATOM   389  O  OD1 . ASP A 1 52  ? 15.456  19.688 15.976  1.00 14.24 ? 52   ASP A OD1 1 
ATOM   390  O  OD2 . ASP A 1 52  ? 17.424  19.012 16.641  1.00 18.63 ? 52   ASP A OD2 1 
ATOM   391  N  N   . ASN A 1 53  ? 13.668  22.308 15.528  1.00 12.37 ? 53   ASN A N   1 
ATOM   392  C  CA  . ASN A 1 53  ? 12.277  22.135 15.933  1.00 13.85 ? 53   ASN A CA  1 
ATOM   393  C  C   . ASN A 1 53  ? 11.719  20.808 15.436  1.00 11.93 ? 53   ASN A C   1 
ATOM   394  O  O   . ASN A 1 53  ? 10.513  20.657 15.221  1.00 14.18 ? 53   ASN A O   1 
ATOM   395  C  CB  . ASN A 1 53  ? 11.481  23.344 15.456  1.00 15.86 ? 53   ASN A CB  1 
ATOM   396  C  CG  . ASN A 1 53  ? 11.906  24.646 16.133  1.00 18.13 ? 53   ASN A CG  1 
ATOM   397  O  OD1 . ASN A 1 53  ? 11.433  25.758 15.797  1.00 21.23 ? 53   ASN A OD1 1 
ATOM   398  N  ND2 . ASN A 1 53  ? 12.795  24.677 17.161  1.00 19.20 ? 53   ASN A ND2 1 
ATOM   399  N  N   . THR A 1 54  ? 12.631  19.849 15.257  1.00 11.12 ? 54   THR A N   1 
ATOM   400  C  CA  . THR A 1 54  ? 12.176  18.504 14.856  1.00 11.63 ? 54   THR A CA  1 
ATOM   401  C  C   . THR A 1 54  ? 11.251  17.878 15.882  1.00 12.02 ? 54   THR A C   1 
ATOM   402  O  O   . THR A 1 54  ? 10.374  17.090 15.471  1.00 14.01 ? 54   THR A O   1 
ATOM   403  C  CB  . THR A 1 54  ? 13.337  17.538 14.609  1.00 12.77 ? 54   THR A CB  1 
ATOM   404  O  OG1 . THR A 1 54  ? 14.146  17.435 15.787  1.00 13.90 ? 54   THR A OG1 1 
ATOM   405  C  CG2 . THR A 1 54  ? 14.216  18.021 13.468  1.00 13.67 ? 54   THR A CG2 1 
ATOM   406  N  N   . ALA A 1 55  ? 11.430  18.183 17.152  1.00 11.50 ? 55   ALA A N   1 
ATOM   407  C  CA  . ALA A 1 55  ? 10.584  17.768 18.242  1.00 13.19 ? 55   ALA A CA  1 
ATOM   408  C  C   . ALA A 1 55  ? 9.928   19.022 18.811  1.00 14.08 ? 55   ALA A C   1 
ATOM   409  O  O   . ALA A 1 55  ? 9.891   19.214 20.033  1.00 18.54 ? 55   ALA A O   1 
ATOM   410  C  CB  . ALA A 1 55  ? 11.342  17.016 19.316  1.00 14.06 ? 55   ALA A CB  1 
ATOM   411  N  N   . GLY A 1 56  ? 9.390   19.858 17.945  1.00 13.38 ? 56   GLY A N   1 
ATOM   412  C  CA  . GLY A 1 56  ? 8.771   21.107 18.374  1.00 14.66 ? 56   GLY A CA  1 
ATOM   413  C  C   . GLY A 1 56  ? 9.730   21.932 19.194  1.00 14.60 ? 56   GLY A C   1 
ATOM   414  O  O   . GLY A 1 56  ? 10.920  22.018 18.888  1.00 16.32 ? 56   GLY A O   1 
ATOM   415  N  N   . CYS A 1 57  ? 9.219   22.548 20.279  1.00 12.48 ? 57   CYS A N   1 
ATOM   416  C  CA  . CYS A 1 57  ? 10.109  23.412 21.044  1.00 12.77 ? 57   CYS A CA  1 
ATOM   417  C  C   . CYS A 1 57  ? 11.070  22.656 21.927  1.00 11.34 ? 57   CYS A C   1 
ATOM   418  O  O   . CYS A 1 57  ? 12.008  23.278 22.416  1.00 13.24 ? 57   CYS A O   1 
ATOM   419  C  CB  . CYS A 1 57  ? 9.249   24.368 21.887  1.00 13.41 ? 57   CYS A CB  1 
ATOM   420  S  SG  . CYS A 1 57  ? 8.103   25.353 20.886  1.00 16.85 ? 57   CYS A SG  1 
ATOM   421  N  N   . THR A 1 58  ? 10.850  21.379 22.214  1.00 12.74 ? 58   THR A N   1 
ATOM   422  C  CA  . THR A 1 58  ? 11.738  20.680 23.146  1.00 11.67 ? 58   THR A CA  1 
ATOM   423  C  C   . THR A 1 58  ? 13.135  20.557 22.603  1.00 12.11 ? 58   THR A C   1 
ATOM   424  O  O   . THR A 1 58  ? 14.124  20.653 23.351  1.00 12.95 ? 58   THR A O   1 
ATOM   425  C  CB  . THR A 1 58  ? 11.092  19.323 23.459  1.00 12.23 ? 58   THR A CB  1 
ATOM   426  O  OG1 . THR A 1 58  ? 9.824   19.597 24.067  1.00 14.40 ? 58   THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 58  ? 11.979  18.540 24.432  1.00 13.64 ? 58   THR A CG2 1 
ATOM   428  N  N   . SER A 1 59  ? 13.268  20.308 21.302  1.00 12.50 ? 59   SER A N   1 
ATOM   429  C  CA  . SER A 1 59  ? 14.603  20.057 20.709  1.00 13.41 ? 59   SER A CA  1 
ATOM   430  C  C   . SER A 1 59  ? 15.444  21.328 20.594  1.00 11.66 ? 59   SER A C   1 
ATOM   431  O  O   . SER A 1 59  ? 16.594  21.302 20.128  1.00 13.29 ? 59   SER A O   1 
ATOM   432  C  CB  . SER A 1 59  ? 14.451  19.332 19.375  1.00 13.15 ? 59   SER A CB  1 
ATOM   433  O  OG  . SER A 1 59  ? 13.367  19.882 18.602  1.00 13.29 ? 59   SER A OG  1 
ATOM   434  N  N   . ALA A 1 60  ? 14.922  22.456 21.047  1.00 11.89 ? 60   ALA A N   1 
ATOM   435  C  CA  . ALA A 1 60  ? 15.704  23.684 21.076  1.00 10.80 ? 60   ALA A CA  1 
ATOM   436  C  C   . ALA A 1 60  ? 16.744  23.665 22.174  1.00 11.27 ? 60   ALA A C   1 
ATOM   437  O  O   . ALA A 1 60  ? 17.639  24.524 22.194  1.00 12.34 ? 60   ALA A O   1 
ATOM   438  C  CB  . ALA A 1 60  ? 14.796  24.909 21.286  1.00 12.64 ? 60   ALA A CB  1 
ATOM   439  N  N   . GLY A 1 61  ? 16.710  22.702 23.104  1.00 11.12 ? 61   GLY A N   1 
ATOM   440  C  CA  . GLY A 1 61  ? 17.748  22.646 24.096  1.00 12.98 ? 61   GLY A CA  1 
ATOM   441  C  C   . GLY A 1 61  ? 17.649  23.745 25.144  1.00 10.63 ? 61   GLY A C   1 
ATOM   442  O  O   . GLY A 1 61  ? 16.573  24.296 25.370  1.00 11.59 ? 61   GLY A O   1 
ATOM   443  N  N   . PRO A 1 62  ? 18.771  24.027 25.793  1.00 11.47 ? 62   PRO A N   1 
ATOM   444  C  CA  . PRO A 1 62  ? 18.789  24.944 26.944  1.00 11.58 ? 62   PRO A CA  1 
ATOM   445  C  C   . PRO A 1 62  ? 18.877  26.405 26.522  1.00 11.22 ? 62   PRO A C   1 
ATOM   446  O  O   . PRO A 1 62  ? 18.899  26.709 25.339  1.00 12.83 ? 62   PRO A O   1 
ATOM   447  C  CB  . PRO A 1 62  ? 20.049  24.492 27.654  1.00 14.00 ? 62   PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 62  ? 20.968  24.102 26.532  1.00 15.72 ? 62   PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 62  ? 20.082  23.406 25.522  1.00 14.08 ? 62   PRO A CD  1 
ATOM   450  N  N   . HIS A 1 63  ? 18.945  27.327 27.493  1.00 13.52 ? 63   HIS A N   1 
ATOM   451  C  CA  . HIS A 1 63  ? 19.149  28.732 27.144  1.00 12.59 ? 63   HIS A CA  1 
ATOM   452  C  C   . HIS A 1 63  ? 20.464  28.895 26.384  1.00 12.73 ? 63   HIS A C   1 
ATOM   453  O  O   . HIS A 1 63  ? 21.491  28.252 26.729  1.00 14.38 ? 63   HIS A O   1 
ATOM   454  C  CB  . HIS A 1 63  ? 19.204  29.622 28.385  1.00 11.85 ? 63   HIS A CB  1 
ATOM   455  C  CG  . HIS A 1 63  ? 17.945  29.594 29.206  1.00 12.44 ? 63   HIS A CG  1 
ATOM   456  N  ND1 . HIS A 1 63  ? 17.704  30.361 30.317  1.00 11.14 ? 63   HIS A ND1 1 
ATOM   457  C  CD2 . HIS A 1 63  ? 16.827  28.824 29.019  1.00 13.65 ? 63   HIS A CD2 1 
ATOM   458  C  CE1 . HIS A 1 63  ? 16.518  30.082 30.801  1.00 12.61 ? 63   HIS A CE1 1 
ATOM   459  N  NE2 . HIS A 1 63  ? 15.954  29.158 30.030  1.00 12.07 ? 63   HIS A NE2 1 
ATOM   460  N  N   . PHE A 1 64  ? 20.419  29.783 25.384  1.00 11.01 ? 64   PHE A N   1 
ATOM   461  C  CA  . PHE A 1 64  ? 21.682  30.086 24.695  1.00 12.21 ? 64   PHE A CA  1 
ATOM   462  C  C   . PHE A 1 64  ? 22.653  30.776 25.661  1.00 11.86 ? 64   PHE A C   1 
ATOM   463  O  O   . PHE A 1 64  ? 22.335  31.835 26.221  1.00 12.75 ? 64   PHE A O   1 
ATOM   464  C  CB  . PHE A 1 64  ? 21.366  30.922 23.462  1.00 12.64 ? 64   PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 64  ? 22.552  31.270 22.614  1.00 12.70 ? 64   PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 64  ? 23.509  30.301 22.306  1.00 13.17 ? 64   PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 64  ? 22.705  32.574 22.177  1.00 13.59 ? 64   PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 64  ? 24.625  30.716 21.578  1.00 13.35 ? 64   PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 64  ? 23.777  32.953 21.384  1.00 13.31 ? 64   PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 64  ? 24.723  31.997 21.073  1.00 13.93 ? 64   PHE A CZ  1 
ATOM   471  N  N   . ASN A 1 65  ? 23.820  30.197 25.829  1.00 12.07 ? 65   ASN A N   1 
ATOM   472  C  CA  . ASN A 1 65  ? 24.736  30.648 26.883  1.00 13.39 ? 65   ASN A CA  1 
ATOM   473  C  C   . ASN A 1 65  ? 26.178  30.470 26.444  1.00 13.59 ? 65   ASN A C   1 
ATOM   474  O  O   . ASN A 1 65  ? 26.917  29.732 27.109  1.00 14.58 ? 65   ASN A O   1 
ATOM   475  C  CB  . ASN A 1 65  ? 24.464  29.867 28.174  1.00 14.68 ? 65   ASN A CB  1 
ATOM   476  C  CG  . ASN A 1 65  ? 25.283  30.374 29.329  1.00 13.72 ? 65   ASN A CG  1 
ATOM   477  O  OD1 . ASN A 1 65  ? 25.679  31.538 29.424  1.00 14.49 ? 65   ASN A OD1 1 
ATOM   478  N  ND2 . ASN A 1 65  ? 25.473  29.556 30.374  1.00 15.47 ? 65   ASN A ND2 1 
ATOM   479  N  N   . PRO A 1 66  ? 26.595  31.111 25.353  1.00 13.61 ? 66   PRO A N   1 
ATOM   480  C  CA  . PRO A 1 66  ? 27.946  30.900 24.827  1.00 13.93 ? 66   PRO A CA  1 
ATOM   481  C  C   . PRO A 1 66  ? 28.984  31.498 25.760  1.00 15.57 ? 66   PRO A C   1 
ATOM   482  O  O   . PRO A 1 66  ? 30.178  31.114 25.642  1.00 18.19 ? 66   PRO A O   1 
ATOM   483  C  CB  . PRO A 1 66  ? 27.926  31.638 23.480  1.00 13.59 ? 66   PRO A CB  1 
ATOM   484  C  CG  . PRO A 1 66  ? 26.928  32.716 23.699  1.00 13.26 ? 66   PRO A CG  1 
ATOM   485  C  CD  . PRO A 1 66  ? 25.847  32.110 24.550  1.00 12.57 ? 66   PRO A CD  1 
ATOM   486  N  N   . LEU A 1 67  ? 28.601  32.412 26.642  1.00 14.84 ? 67   LEU A N   1 
ATOM   487  C  CA  . LEU A 1 67  ? 29.571  33.104 27.491  1.00 15.50 ? 67   LEU A CA  1 
ATOM   488  C  C   . LEU A 1 67  ? 29.642  32.468 28.873  1.00 15.87 ? 67   LEU A C   1 
ATOM   489  O  O   . LEU A 1 67  ? 30.287  32.997 29.799  1.00 17.07 ? 67   LEU A O   1 
ATOM   490  C  CB  . LEU A 1 67  ? 29.235  34.605 27.599  1.00 14.54 ? 67   LEU A CB  1 
ATOM   491  C  CG  . LEU A 1 67  ? 28.952  35.258 26.233  1.00 14.96 ? 67   LEU A CG  1 
ATOM   492  C  CD1 . LEU A 1 67  ? 28.660  36.733 26.431  1.00 14.29 ? 67   LEU A CD1 1 
ATOM   493  C  CD2 . LEU A 1 67  ? 30.131  35.076 25.284  1.00 16.77 ? 67   LEU A CD2 1 
ATOM   494  N  N   . SER A 1 68  ? 28.987  31.336 29.090  1.00 16.41 ? 68   SER A N   1 
ATOM   495  C  CA  . SER A 1 68  ? 29.117  30.573 30.341  1.00 16.93 ? 68   SER A CA  1 
ATOM   496  C  C   . SER A 1 68  ? 28.750  31.359 31.595  1.00 17.29 ? 68   SER A C   1 
ATOM   497  O  O   . SER A 1 68  ? 29.473  31.349 32.596  1.00 18.81 ? 68   SER A O   1 
ATOM   498  C  CB  . SER A 1 68  ? 30.569  30.064 30.469  1.00 19.57 ? 68   SER A CB  1 
ATOM   499  O  OG  . SER A 1 68  ? 30.847  29.200 29.378  1.00 23.60 ? 68   SER A OG  1 
ATOM   500  N  N   . ARG A 1 69  ? 27.610  32.061 31.564  1.00 14.78 ? 69   ARG A N   1 
ATOM   501  C  CA  . ARG A 1 69  ? 27.099  32.837 32.702  1.00 15.62 ? 69   ARG A CA  1 
ATOM   502  C  C   . ARG A 1 69  ? 25.950  32.090 33.358  1.00 13.57 ? 69   ARG A C   1 
ATOM   503  O  O   . ARG A 1 69  ? 25.511  31.004 32.924  1.00 15.98 ? 69   ARG A O   1 
ATOM   504  C  CB  . ARG A 1 69  ? 26.672  34.233 32.243  1.00 14.93 ? 69   ARG A CB  1 
ATOM   505  C  CG  . ARG A 1 69  ? 27.760  35.028 31.508  1.00 14.56 ? 69   ARG A CG  1 
ATOM   506  C  CD  . ARG A 1 69  ? 29.024  35.258 32.325  1.00 14.55 ? 69   ARG A CD  1 
ATOM   507  N  NE  . ARG A 1 69  ? 28.714  36.002 33.553  1.00 16.42 ? 69   ARG A NE  1 
ATOM   508  C  CZ  . ARG A 1 69  ? 28.741  37.317 33.708  1.00 16.40 ? 69   ARG A CZ  1 
ATOM   509  N  NH1 . ARG A 1 69  ? 29.086  38.116 32.680  1.00 15.54 ? 69   ARG A NH1 1 
ATOM   510  N  NH2 . ARG A 1 69  ? 28.445  37.890 34.886  1.00 16.53 ? 69   ARG A NH2 1 
ATOM   511  N  N   . LYS A 1 70  ? 25.448  32.658 34.451  1.00 15.67 ? 70   LYS A N   1 
ATOM   512  C  CA  . LYS A 1 70  ? 24.260  32.109 35.104  1.00 15.77 ? 70   LYS A CA  1 
ATOM   513  C  C   . LYS A 1 70  ? 22.998  32.796 34.630  1.00 13.50 ? 70   LYS A C   1 
ATOM   514  O  O   . LYS A 1 70  ? 23.070  33.906 34.084  1.00 15.01 ? 70   LYS A O   1 
ATOM   515  C  CB  . LYS A 1 70  ? 24.403  32.270 36.625  1.00 18.65 ? 70   LYS A CB  1 
ATOM   516  C  CG  . LYS A 1 70  ? 25.510  31.351 37.169  1.00 24.05 ? 70   LYS A CG  1 
ATOM   517  C  CD  . LYS A 1 70  ? 25.939  31.813 38.545  1.00 28.12 ? 70   LYS A CD  1 
ATOM   518  C  CE  . LYS A 1 70  ? 27.102  31.009 39.082  1.00 40.07 ? 70   LYS A CE  1 
ATOM   519  N  NZ  . LYS A 1 70  ? 27.790  31.824 40.125  1.00 63.52 ? 70   LYS A NZ  1 
ATOM   520  N  N   . HIS A 1 71  ? 21.850  32.159 34.842  1.00 13.47 ? 71   HIS A N   1 
ATOM   521  C  CA  . HIS A 1 71  ? 20.582  32.743 34.400  1.00 14.35 ? 71   HIS A CA  1 
ATOM   522  C  C   . HIS A 1 71  ? 20.253  34.025 35.127  1.00 13.12 ? 71   HIS A C   1 
ATOM   523  O  O   . HIS A 1 71  ? 20.456  34.132 36.357  1.00 16.44 ? 71   HIS A O   1 
ATOM   524  C  CB  . HIS A 1 71  ? 19.458  31.709 34.655  1.00 12.68 ? 71   HIS A CB  1 
ATOM   525  C  CG  . HIS A 1 71  ? 18.148  32.228 34.157  1.00 12.00 ? 71   HIS A CG  1 
ATOM   526  N  ND1 . HIS A 1 71  ? 17.849  32.300 32.807  1.00 11.97 ? 71   HIS A ND1 1 
ATOM   527  C  CD2 . HIS A 1 71  ? 17.065  32.693 34.821  1.00 13.71 ? 71   HIS A CD2 1 
ATOM   528  C  CE1 . HIS A 1 71  ? 16.621  32.819 32.688  1.00 11.88 ? 71   HIS A CE1 1 
ATOM   529  N  NE2 . HIS A 1 71  ? 16.127  33.067 33.916  1.00 12.92 ? 71   HIS A NE2 1 
ATOM   530  N  N   . GLY A 1 72  ? 19.728  35.006 34.384  1.00 13.15 ? 72   GLY A N   1 
ATOM   531  C  CA  . GLY A 1 72  ? 19.289  36.261 34.987  1.00 15.36 ? 72   GLY A CA  1 
ATOM   532  C  C   . GLY A 1 72  ? 18.197  36.879 34.124  1.00 13.46 ? 72   GLY A C   1 
ATOM   533  O  O   . GLY A 1 72  ? 17.675  36.247 33.180  1.00 14.36 ? 72   GLY A O   1 
ATOM   534  N  N   . GLY A 1 73  ? 17.843  38.125 34.442  1.00 14.12 ? 73   GLY A N   1 
ATOM   535  C  CA  . GLY A 1 73  ? 16.961  38.908 33.579  1.00 14.06 ? 73   GLY A CA  1 
ATOM   536  C  C   . GLY A 1 73  ? 17.805  39.727 32.598  1.00 13.26 ? 73   GLY A C   1 
ATOM   537  O  O   . GLY A 1 73  ? 19.032  39.824 32.724  1.00 13.79 ? 73   GLY A O   1 
ATOM   538  N  N   . PRO A 1 74  ? 17.148  40.332 31.609  1.00 13.41 ? 74   PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 17.835  40.986 30.517  1.00 13.80 ? 74   PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 18.635  42.194 30.989  1.00 13.23 ? 74   PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 19.612  42.491 30.292  1.00 15.11 ? 74   PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 16.704  41.397 29.559  1.00 14.55 ? 74   PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 15.460  41.420 30.408  1.00 14.39 ? 74   PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 15.684  40.326 31.413  1.00 14.72 ? 74   PRO A CD  1 
ATOM   545  N  N   . LYS A 1 75  ? 18.252  42.856 32.085  1.00 14.15 ? 75   LYS A N   1 
ATOM   546  C  CA  . LYS A 1 75  ? 19.034  44.024 32.527  1.00 16.12 ? 75   LYS A CA  1 
ATOM   547  C  C   . LYS A 1 75  ? 19.990  43.671 33.651  1.00 17.21 ? 75   LYS A C   1 
ATOM   548  O  O   . LYS A 1 75  ? 20.604  44.559 34.256  1.00 21.35 ? 75   LYS A O   1 
ATOM   549  C  CB  . LYS A 1 75  ? 18.056  45.164 32.891  1.00 19.00 ? 75   LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 75  ? 17.226  45.615 31.675  1.00 22.31 ? 75   LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 75  ? 18.065  45.930 30.443  1.00 25.01 ? 75   LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 75  ? 17.219  46.374 29.257  1.00 31.36 ? 75   LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 75  ? 18.082  46.711 28.074  1.00 35.68 ? 75   LYS A NZ  1 
ATOM   554  N  N   . ASP A 1 76  ? 20.149  42.355 33.908  1.00 16.02 ? 76   ASP A N   1 
ATOM   555  C  CA  . ASP A 1 76  ? 21.198  41.918 34.828  1.00 14.87 ? 76   ASP A CA  1 
ATOM   556  C  C   . ASP A 1 76  ? 22.517  41.762 34.076  1.00 15.71 ? 76   ASP A C   1 
ATOM   557  O  O   . ASP A 1 76  ? 22.436  41.432 32.868  1.00 15.75 ? 76   ASP A O   1 
ATOM   558  C  CB  . ASP A 1 76  ? 20.828  40.589 35.496  1.00 15.87 ? 76   ASP A CB  1 
ATOM   559  C  CG  . ASP A 1 76  ? 19.675  40.689 36.464  1.00 16.64 ? 76   ASP A CG  1 
ATOM   560  O  OD1 . ASP A 1 76  ? 19.550  41.767 37.111  1.00 21.62 ? 76   ASP A OD1 1 
ATOM   561  O  OD2 . ASP A 1 76  ? 18.950  39.678 36.539  1.00 19.86 ? 76   ASP A OD2 1 
ATOM   562  N  N   . GLU A 1 77  ? 23.658  41.964 34.701  1.00 15.48 ? 77   GLU A N   1 
ATOM   563  C  CA  . GLU A 1 77  ? 24.946  41.727 34.038  1.00 14.72 ? 77   GLU A CA  1 
ATOM   564  C  C   . GLU A 1 77  ? 25.211  40.225 34.053  1.00 14.13 ? 77   GLU A C   1 
ATOM   565  O  O   . GLU A 1 77  ? 25.761  39.656 33.100  1.00 14.50 ? 77   GLU A O   1 
ATOM   566  C  CB  . GLU A 1 77  ? 26.066  42.551 34.724  1.00 14.93 ? 77   GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 77  ? 27.327  42.473 33.863  1.00 16.50 ? 77   GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 77  ? 28.273  41.309 34.141  1.00 16.54 ? 77   GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 77  ? 28.047  40.592 35.155  1.00 17.19 ? 77   GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 77  ? 29.185  41.087 33.310  1.00 17.37 ? 77   GLU A OE2 1 
ATOM   571  N  N   . GLU A 1 78  ? 24.840  39.553 35.123  1.00 16.40 ? 78   GLU A N   1 
ATOM   572  C  CA  . GLU A 1 78  ? 24.896  38.093 35.187  1.00 13.37 ? 78   GLU A CA  1 
ATOM   573  C  C   . GLU A 1 78  ? 23.666  37.525 34.531  1.00 13.99 ? 78   GLU A C   1 
ATOM   574  O  O   . GLU A 1 78  ? 22.584  37.423 35.133  1.00 15.45 ? 78   GLU A O   1 
ATOM   575  C  CB  . GLU A 1 78  ? 24.979  37.653 36.643  1.00 16.39 ? 78   GLU A CB  1 
ATOM   576  C  CG  . GLU A 1 78  ? 25.187  36.143 36.759  1.00 18.84 ? 78   GLU A CG  1 
ATOM   577  C  CD  . GLU A 1 78  ? 26.633  35.760 36.460  1.00 19.40 ? 78   GLU A CD  1 
ATOM   578  O  OE1 . GLU A 1 78  ? 27.559  36.299 37.125  1.00 21.44 ? 78   GLU A OE1 1 
ATOM   579  O  OE2 . GLU A 1 78  ? 26.829  34.910 35.548  1.00 23.80 ? 78   GLU A OE2 1 
ATOM   580  N  N   . ARG A 1 79  ? 23.797  37.125 33.261  1.00 14.33 ? 79   ARG A N   1 
ATOM   581  C  CA  . ARG A 1 79  ? 22.702  36.559 32.494  1.00 11.27 ? 79   ARG A CA  1 
ATOM   582  C  C   . ARG A 1 79  ? 23.285  35.713 31.355  1.00 10.40 ? 79   ARG A C   1 
ATOM   583  O  O   . ARG A 1 79  ? 24.433  35.916 30.972  1.00 12.81 ? 79   ARG A O   1 
ATOM   584  C  CB  . ARG A 1 79  ? 21.771  37.632 31.893  1.00 11.85 ? 79   ARG A CB  1 
ATOM   585  C  CG  . ARG A 1 79  ? 22.526  38.608 30.968  1.00 11.07 ? 79   ARG A CG  1 
ATOM   586  C  CD  . ARG A 1 79  ? 21.540  39.512 30.229  1.00 10.72 ? 79   ARG A CD  1 
ATOM   587  N  NE  . ARG A 1 79  ? 21.149  38.866 28.962  1.00 11.71 ? 79   ARG A NE  1 
ATOM   588  C  CZ  . ARG A 1 79  ? 20.534  39.522 27.979  1.00 11.10 ? 79   ARG A CZ  1 
ATOM   589  N  NH1 . ARG A 1 79  ? 20.234  40.818 28.144  1.00 12.45 ? 79   ARG A NH1 1 
ATOM   590  N  NH2 . ARG A 1 79  ? 20.222  38.907 26.839  1.00 11.58 ? 79   ARG A NH2 1 
ATOM   591  N  N   . HIS A 1 80  ? 22.432  34.819 30.844  1.00 11.27 ? 80   HIS A N   1 
ATOM   592  C  CA  . HIS A 1 80  ? 22.707  34.147 29.574  1.00 11.02 ? 80   HIS A CA  1 
ATOM   593  C  C   . HIS A 1 80  ? 22.461  35.041 28.368  1.00 10.70 ? 80   HIS A C   1 
ATOM   594  O  O   . HIS A 1 80  ? 21.615  35.962 28.458  1.00 11.15 ? 80   HIS A O   1 
ATOM   595  C  CB  . HIS A 1 80  ? 21.750  32.934 29.436  1.00 12.01 ? 80   HIS A CB  1 
ATOM   596  C  CG  . HIS A 1 80  ? 21.842  31.940 30.546  1.00 12.93 ? 80   HIS A CG  1 
ATOM   597  N  ND1 . HIS A 1 80  ? 20.781  31.203 31.063  1.00 13.30 ? 80   HIS A ND1 1 
ATOM   598  C  CD2 . HIS A 1 80  ? 22.933  31.514 31.221  1.00 13.17 ? 80   HIS A CD2 1 
ATOM   599  C  CE1 . HIS A 1 80  ? 21.225  30.393 31.983  1.00 14.35 ? 80   HIS A CE1 1 
ATOM   600  N  NE2 . HIS A 1 80  ? 22.529  30.556 32.093  1.00 14.77 ? 80   HIS A NE2 1 
ATOM   601  N  N   . VAL A 1 81  ? 23.121  34.837 27.238  1.00 10.67 ? 81   VAL A N   1 
ATOM   602  C  CA  . VAL A 1 81  ? 22.804  35.649 26.061  1.00 11.65 ? 81   VAL A CA  1 
ATOM   603  C  C   . VAL A 1 81  ? 21.312  35.506 25.754  1.00 10.11 ? 81   VAL A C   1 
ATOM   604  O  O   . VAL A 1 81  ? 20.657  36.505 25.417  1.00 11.52 ? 81   VAL A O   1 
ATOM   605  C  CB  . VAL A 1 81  ? 23.640  35.210 24.839  1.00 10.69 ? 81   VAL A CB  1 
ATOM   606  C  CG1 . VAL A 1 81  ? 23.141  35.856 23.553  1.00 13.39 ? 81   VAL A CG1 1 
ATOM   607  C  CG2 . VAL A 1 81  ? 25.114  35.559 25.082  1.00 12.94 ? 81   VAL A CG2 1 
ATOM   608  N  N   . GLY A 1 82  ? 20.732  34.308 25.916  1.00 10.46 ? 82   GLY A N   1 
ATOM   609  C  CA  . GLY A 1 82  ? 19.327  34.116 25.595  1.00 10.01 ? 82   GLY A CA  1 
ATOM   610  C  C   . GLY A 1 82  ? 18.309  34.622 26.582  1.00 10.82 ? 82   GLY A C   1 
ATOM   611  O  O   . GLY A 1 82  ? 17.103  34.364 26.360  1.00 11.43 ? 82   GLY A O   1 
ATOM   612  N  N   . ASP A 1 83  ? 18.716  35.331 27.642  1.00 10.06 ? 83   ASP A N   1 
ATOM   613  C  CA  . ASP A 1 83  ? 17.765  35.736 28.698  1.00 10.22 ? 83   ASP A CA  1 
ATOM   614  C  C   . ASP A 1 83  ? 17.081  37.077 28.392  1.00 11.12 ? 83   ASP A C   1 
ATOM   615  O  O   . ASP A 1 83  ? 17.559  38.146 28.795  1.00 13.06 ? 83   ASP A O   1 
ATOM   616  C  CB  . ASP A 1 83  ? 18.532  35.823 30.011  1.00 11.51 ? 83   ASP A CB  1 
ATOM   617  C  CG  . ASP A 1 83  ? 18.927  34.462 30.542  1.00 10.94 ? 83   ASP A CG  1 
ATOM   618  O  OD1 . ASP A 1 83  ? 18.392  33.431 30.062  1.00 11.97 ? 83   ASP A OD1 1 
ATOM   619  O  OD2 . ASP A 1 83  ? 19.738  34.401 31.489  1.00 12.03 ? 83   ASP A OD2 1 
ATOM   620  N  N   . LEU A 1 84  ? 15.957  36.995 27.687  1.00 11.67 ? 84   LEU A N   1 
ATOM   621  C  CA  . LEU A 1 84  ? 15.217  38.193 27.314  1.00 11.73 ? 84   LEU A CA  1 
ATOM   622  C  C   . LEU A 1 84  ? 14.062  38.479 28.259  1.00 12.21 ? 84   LEU A C   1 
ATOM   623  O  O   . LEU A 1 84  ? 13.177  39.293 27.938  1.00 14.56 ? 84   LEU A O   1 
ATOM   624  C  CB  . LEU A 1 84  ? 14.765  38.080 25.864  1.00 11.69 ? 84   LEU A CB  1 
ATOM   625  C  CG  . LEU A 1 84  ? 15.927  38.082 24.843  1.00 12.02 ? 84   LEU A CG  1 
ATOM   626  C  CD1 . LEU A 1 84  ? 15.346  37.928 23.450  1.00 12.97 ? 84   LEU A CD1 1 
ATOM   627  C  CD2 . LEU A 1 84  ? 16.783  39.347 25.007  1.00 14.22 ? 84   LEU A CD2 1 
ATOM   628  N  N   . GLY A 1 85  ? 14.037  37.864 29.447  1.00 11.19 ? 85   GLY A N   1 
ATOM   629  C  CA  . GLY A 1 85  ? 13.071  38.271 30.462  1.00 12.72 ? 85   GLY A CA  1 
ATOM   630  C  C   . GLY A 1 85  ? 11.659  37.743 30.196  1.00 11.92 ? 85   GLY A C   1 
ATOM   631  O  O   . GLY A 1 85  ? 11.478  36.546 29.954  1.00 14.05 ? 85   GLY A O   1 
ATOM   632  N  N   . ASN A 1 86  ? 10.686  38.665 30.297  1.00 12.57 ? 86   ASN A N   1 
ATOM   633  C  CA  . ASN A 1 86  ? 9.295   38.324 30.153  1.00 14.13 ? 86   ASN A CA  1 
ATOM   634  C  C   . ASN A 1 86  ? 8.636   39.241 29.148  1.00 12.69 ? 86   ASN A C   1 
ATOM   635  O  O   . ASN A 1 86  ? 9.009   40.433 29.071  1.00 17.31 ? 86   ASN A O   1 
ATOM   636  C  CB  . ASN A 1 86  ? 8.524   38.495 31.480  1.00 13.07 ? 86   ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 86  ? 8.934   37.397 32.453  1.00 13.02 ? 86   ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 86  ? 8.699   36.214 32.177  1.00 13.82 ? 86   ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 86  ? 9.520   37.750 33.598  1.00 16.05 ? 86   ASN A ND2 1 
ATOM   640  N  N   . VAL A 1 87  ? 7.682   38.694 28.424  1.00 14.05 ? 87   VAL A N   1 
ATOM   641  C  CA  . VAL A 1 87  ? 6.744   39.558 27.691  1.00 14.05 ? 87   VAL A CA  1 
ATOM   642  C  C   . VAL A 1 87  ? 5.475   39.628 28.531  1.00 14.41 ? 87   VAL A C   1 
ATOM   643  O  O   . VAL A 1 87  ? 5.233   38.759 29.376  1.00 16.53 ? 87   VAL A O   1 
ATOM   644  C  CB  . VAL A 1 87  ? 6.448   39.113 26.243  1.00 14.07 ? 87   VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 87  ? 7.774   39.155 25.464  1.00 19.04 ? 87   VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 87  ? 5.755   37.755 26.187  1.00 15.74 ? 87   VAL A CG2 1 
ATOM   647  N  N   . THR A 1 88  ? 4.665   40.660 28.368  1.00 14.55 ? 88   THR A N   1 
ATOM   648  C  CA  . THR A 1 88  ? 3.449   40.853 29.115  1.00 14.49 ? 88   THR A CA  1 
ATOM   649  C  C   . THR A 1 88  ? 2.234   40.834 28.188  1.00 13.59 ? 88   THR A C   1 
ATOM   650  O  O   . THR A 1 88  ? 2.106   41.663 27.262  1.00 17.96 ? 88   THR A O   1 
ATOM   651  C  CB  . THR A 1 88  ? 3.439   42.194 29.862  1.00 17.77 ? 88   THR A CB  1 
ATOM   652  O  OG1 . THR A 1 88  ? 4.536   42.213 30.785  1.00 22.74 ? 88   THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 88  ? 2.117   42.367 30.644  1.00 20.13 ? 88   THR A CG2 1 
ATOM   654  N  N   . ALA A 1 89  ? 1.316   39.900 28.435  1.00 15.07 ? 89   ALA A N   1 
ATOM   655  C  CA  . ALA A 1 89  ? 0.112   39.810 27.640  1.00 14.05 ? 89   ALA A CA  1 
ATOM   656  C  C   . ALA A 1 89  ? -0.981  40.582 28.374  1.00 17.67 ? 89   ALA A C   1 
ATOM   657  O  O   . ALA A 1 89  ? -1.066  40.453 29.612  1.00 17.58 ? 89   ALA A O   1 
ATOM   658  C  CB  . ALA A 1 89  ? -0.373  38.359 27.427  1.00 15.97 ? 89   ALA A CB  1 
ATOM   659  N  N   . ASP A 1 90  ? -1.769  41.301 27.601  1.00 15.87 ? 90   ASP A N   1 
ATOM   660  C  CA  . ASP A 1 90  ? -2.874  42.114 28.141  1.00 19.73 ? 90   ASP A CA  1 
ATOM   661  C  C   . ASP A 1 90  ? -4.097  41.238 28.386  1.00 19.34 ? 90   ASP A C   1 
ATOM   662  O  O   . ASP A 1 90  ? -3.993  40.028 28.233  1.00 19.15 ? 90   ASP A O   1 
ATOM   663  C  CB  . ASP A 1 90  ? -3.198  43.267 27.203  1.00 20.87 ? 90   ASP A CB  1 
ATOM   664  C  CG  . ASP A 1 90  ? -3.684  42.931 25.820  1.00 20.46 ? 90   ASP A CG  1 
ATOM   665  O  OD1 . ASP A 1 90  ? -4.178  41.801 25.575  1.00 21.24 ? 90   ASP A OD1 1 
ATOM   666  O  OD2 . ASP A 1 90  ? -3.638  43.807 24.935  1.00 25.46 ? 90   ASP A OD2 1 
ATOM   667  N  N   . LYS A 1 91  ? -5.232  41.844 28.738  1.00 20.63 ? 91   LYS A N   1 
ATOM   668  C  CA  . LYS A 1 91  ? -6.397  41.036 29.103  1.00 22.25 ? 91   LYS A CA  1 
ATOM   669  C  C   . LYS A 1 91  ? -6.938  40.355 27.861  1.00 20.58 ? 91   LYS A C   1 
ATOM   670  O  O   . LYS A 1 91  ? -7.745  39.418 28.024  1.00 25.09 ? 91   LYS A O   1 
ATOM   671  C  CB  . LYS A 1 91  ? -7.434  41.865 29.853  1.00 24.23 ? 91   LYS A CB  1 
ATOM   672  C  CG  . LYS A 1 91  ? -8.031  42.995 29.037  1.00 27.89 ? 91   LYS A CG  1 
ATOM   673  C  CD  . LYS A 1 91  ? -9.177  43.650 29.800  1.00 34.47 ? 91   LYS A CD  1 
ATOM   674  C  CE  . LYS A 1 91  ? -9.715  44.859 29.054  1.00 42.02 ? 91   LYS A CE  1 
ATOM   675  N  NZ  . LYS A 1 91  ? -9.710  44.674 27.569  1.00 56.12 ? 91   LYS A NZ  1 
ATOM   676  N  N   . ASP A 1 92  ? -6.536  40.729 26.657  1.00 20.66 ? 92   ASP A N   1 
ATOM   677  C  CA  . ASP A 1 92  ? -7.017  40.051 25.455  1.00 22.18 ? 92   ASP A CA  1 
ATOM   678  C  C   . ASP A 1 92  ? -6.024  38.990 24.987  1.00 19.56 ? 92   ASP A C   1 
ATOM   679  O  O   . ASP A 1 92  ? -6.209  38.454 23.888  1.00 20.38 ? 92   ASP A O   1 
ATOM   680  C  CB  . ASP A 1 92  ? -7.228  41.028 24.299  1.00 25.20 ? 92   ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 92  ? -8.315  42.050 24.551  1.00 31.99 ? 92   ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 92  ? -9.291  41.693 25.257  1.00 35.88 ? 92   ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 92  ? -8.222  43.190 24.058  1.00 43.57 ? 92   ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 93  ? -4.995  38.725 25.769  1.00 18.32 ? 93   GLY A N   1 
ATOM   685  C  CA  . GLY A 1 93  ? -4.018  37.675 25.474  1.00 18.63 ? 93   GLY A CA  1 
ATOM   686  C  C   . GLY A 1 93  ? -2.932  38.160 24.524  1.00 17.30 ? 93   GLY A C   1 
ATOM   687  O  O   . GLY A 1 93  ? -2.219  37.360 23.929  1.00 16.41 ? 93   GLY A O   1 
ATOM   688  N  N   . VAL A 1 94  ? -2.789  39.483 24.342  1.00 16.96 ? 94   VAL A N   1 
ATOM   689  C  CA  . VAL A 1 94  ? -1.863  39.999 23.343  1.00 14.97 ? 94   VAL A CA  1 
ATOM   690  C  C   . VAL A 1 94  ? -0.670  40.642 24.047  1.00 15.48 ? 94   VAL A C   1 
ATOM   691  O  O   . VAL A 1 94  ? -0.811  41.499 24.900  1.00 16.15 ? 94   VAL A O   1 
ATOM   692  C  CB  . VAL A 1 94  ? -2.504  41.036 22.412  1.00 17.06 ? 94   VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 94  ? -1.466  41.722 21.514  1.00 18.89 ? 94   VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 94  ? -3.587  40.375 21.562  1.00 19.38 ? 94   VAL A CG2 1 
ATOM   695  N  N   . ALA A 1 95  ? 0.504   40.197 23.678  1.00 16.26 ? 95   ALA A N   1 
ATOM   696  C  CA  . ALA A 1 95  ? 1.777   40.721 24.155  1.00 16.60 ? 95   ALA A CA  1 
ATOM   697  C  C   . ALA A 1 95  ? 2.440   41.488 23.026  1.00 16.64 ? 95   ALA A C   1 
ATOM   698  O  O   . ALA A 1 95  ? 3.006   40.904 22.109  1.00 19.99 ? 95   ALA A O   1 
ATOM   699  C  CB  . ALA A 1 95  ? 2.709   39.618 24.632  1.00 18.32 ? 95   ALA A CB  1 
ATOM   700  N  N   . ASP A 1 96  ? 2.356   42.821 23.124  1.00 18.30 ? 96   ASP A N   1 
ATOM   701  C  CA  . ASP A 1 96  ? 3.075   43.658 22.162  1.00 17.67 ? 96   ASP A CA  1 
ATOM   702  C  C   . ASP A 1 96  ? 4.495   43.793 22.687  1.00 16.83 ? 96   ASP A C   1 
ATOM   703  O  O   . ASP A 1 96  ? 4.719   44.083 23.872  1.00 22.75 ? 96   ASP A O   1 
ATOM   704  C  CB  . ASP A 1 96  ? 2.350   44.982 21.990  1.00 24.57 ? 96   ASP A CB  1 
ATOM   705  C  CG  . ASP A 1 96  ? 1.060   44.814 21.203  1.00 31.03 ? 96   ASP A CG  1 
ATOM   706  O  OD1 . ASP A 1 96  ? 1.017   44.077 20.189  1.00 25.84 ? 96   ASP A OD1 1 
ATOM   707  O  OD2 . ASP A 1 96  ? 0.054   45.431 21.631  1.00 45.87 ? 96   ASP A OD2 1 
ATOM   708  N  N   . VAL A 1 97  ? 5.474   43.537 21.842  1.00 16.93 ? 97   VAL A N   1 
ATOM   709  C  CA  . VAL A 1 97  ? 6.860   43.561 22.308  1.00 17.36 ? 97   VAL A CA  1 
ATOM   710  C  C   . VAL A 1 97  ? 7.633   44.678 21.640  1.00 17.40 ? 97   VAL A C   1 
ATOM   711  O  O   . VAL A 1 97  ? 7.571   44.827 20.424  1.00 17.90 ? 97   VAL A O   1 
ATOM   712  C  CB  . VAL A 1 97  ? 7.512   42.223 21.949  1.00 16.86 ? 97   VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 97  ? 8.985   42.224 22.300  1.00 20.11 ? 97   VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 97  ? 6.742   41.116 22.670  1.00 21.81 ? 97   VAL A CG2 1 
ATOM   715  N  N   . SER A 1 98  ? 8.345   45.480 22.409  1.00 21.62 ? 98   SER A N   1 
ATOM   716  C  CA  . SER A 1 98  ? 9.248   46.449 21.796  1.00 19.27 ? 98   SER A CA  1 
ATOM   717  C  C   . SER A 1 98  ? 10.335  46.812 22.791  1.00 19.72 ? 98   SER A C   1 
ATOM   718  O  O   . SER A 1 98  ? 10.117  47.690 23.634  1.00 22.79 ? 98   SER A O   1 
ATOM   719  C  CB  . SER A 1 98  ? 8.504   47.711 21.372  1.00 30.05 ? 98   SER A CB  1 
ATOM   720  O  OG  . SER A 1 98  ? 9.413   48.615 20.750  1.00 35.84 ? 98   SER A OG  1 
ATOM   721  N  N   . ILE A 1 99  ? 11.453  46.128 22.649  1.00 19.00 ? 99   ILE A N   1 
ATOM   722  C  CA  . ILE A 1 99  ? 12.586  46.319 23.533  1.00 16.66 ? 99   ILE A CA  1 
ATOM   723  C  C   . ILE A 1 99  ? 13.900  46.421 22.759  1.00 15.62 ? 99   ILE A C   1 
ATOM   724  O  O   . ILE A 1 99  ? 13.893  46.217 21.544  1.00 16.75 ? 99   ILE A O   1 
ATOM   725  C  CB  . ILE A 1 99  ? 12.660  45.117 24.474  1.00 17.91 ? 99   ILE A CB  1 
ATOM   726  C  CG1 . ILE A 1 99  ? 13.020  43.851 23.651  1.00 18.00 ? 99   ILE A CG1 1 
ATOM   727  C  CG2 . ILE A 1 99  ? 11.414  44.974 25.321  1.00 21.31 ? 99   ILE A CG2 1 
ATOM   728  C  CD1 . ILE A 1 99  ? 13.629  42.778 24.525  1.00 35.02 ? 99   ILE A CD1 1 
ATOM   729  N  N   . GLU A 1 100 ? 14.925  46.810 23.499  1.00 14.66 ? 100  GLU A N   1 
ATOM   730  C  CA  . GLU A 1 100 ? 16.290  46.797 22.949  1.00 14.15 ? 100  GLU A CA  1 
ATOM   731  C  C   . GLU A 1 100 ? 17.151  45.920 23.842  1.00 12.99 ? 100  GLU A C   1 
ATOM   732  O  O   . GLU A 1 100 ? 16.981  45.966 25.063  1.00 16.39 ? 100  GLU A O   1 
ATOM   733  C  CB  . GLU A 1 100 ? 16.914  48.188 22.794  1.00 17.42 ? 100  GLU A CB  1 
ATOM   734  C  CG  . GLU A 1 100 ? 16.210  48.996 21.706  1.00 23.40 ? 100  GLU A CG  1 
ATOM   735  C  CD  . GLU A 1 100 ? 16.880  50.312 21.349  1.00 28.05 ? 100  GLU A CD  1 
ATOM   736  O  OE1 . GLU A 1 100 ? 18.110  50.497 21.515  1.00 34.45 ? 100  GLU A OE1 1 
ATOM   737  O  OE2 . GLU A 1 100 ? 16.136  51.205 20.851  1.00 40.34 ? 100  GLU A OE2 1 
ATOM   738  N  N   . ASP A 1 101 ? 18.050  45.133 23.258  1.00 11.94 ? 101  ASP A N   1 
ATOM   739  C  CA  . ASP A 1 101 ? 18.912  44.304 24.088  1.00 11.69 ? 101  ASP A CA  1 
ATOM   740  C  C   . ASP A 1 101 ? 20.342  44.471 23.586  1.00 11.32 ? 101  ASP A C   1 
ATOM   741  O  O   . ASP A 1 101 ? 20.556  44.532 22.347  1.00 12.21 ? 101  ASP A O   1 
ATOM   742  C  CB  . ASP A 1 101 ? 18.460  42.831 23.961  1.00 12.50 ? 101  ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 101 ? 19.194  42.053 25.048  1.00 12.13 ? 101  ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 101 ? 18.848  42.278 26.240  1.00 14.03 ? 101  ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 101 ? 20.097  41.254 24.724  1.00 11.51 ? 101  ASP A OD2 1 
ATOM   746  N  N   . SER A 1 102 ? 21.279  44.504 24.498  1.00 11.27 ? 102  SER A N   1 
ATOM   747  C  CA  . SER A 1 102 ? 22.704  44.718 24.180  1.00 12.15 ? 102  SER A CA  1 
ATOM   748  C  C   . SER A 1 102 ? 23.581  43.495 24.422  1.00 10.40 ? 102  SER A C   1 
ATOM   749  O  O   . SER A 1 102 ? 24.819  43.627 24.441  1.00 12.64 ? 102  SER A O   1 
ATOM   750  C  CB  . SER A 1 102 ? 23.241  45.938 24.955  1.00 12.52 ? 102  SER A CB  1 
ATOM   751  O  OG  . SER A 1 102 ? 22.695  47.082 24.339  1.00 15.44 ? 102  SER A OG  1 
ATOM   752  N  N   . VAL A 1 103 ? 22.927  42.345 24.597  1.00 11.27 ? 103  VAL A N   1 
ATOM   753  C  CA  . VAL A 1 103 ? 23.716  41.088 24.750  1.00 11.61 ? 103  VAL A CA  1 
ATOM   754  C  C   . VAL A 1 103 ? 23.468  40.190 23.569  1.00 12.12 ? 103  VAL A C   1 
ATOM   755  O  O   . VAL A 1 103 ? 24.403  39.618 22.997  1.00 13.44 ? 103  VAL A O   1 
ATOM   756  C  CB  . VAL A 1 103 ? 23.407  40.421 26.111  1.00 10.83 ? 103  VAL A CB  1 
ATOM   757  C  CG1 . VAL A 1 103 ? 24.189  39.124 26.254  1.00 13.11 ? 103  VAL A CG1 1 
ATOM   758  C  CG2 . VAL A 1 103 ? 23.821  41.332 27.270  1.00 13.16 ? 103  VAL A CG2 1 
ATOM   759  N  N   . ILE A 1 104 ? 22.232  40.021 23.108  1.00 12.06 ? 104  ILE A N   1 
ATOM   760  C  CA  . ILE A 1 104 ? 22.055  39.286 21.870  1.00 10.81 ? 104  ILE A CA  1 
ATOM   761  C  C   . ILE A 1 104 ? 22.682  40.039 20.706  1.00 11.51 ? 104  ILE A C   1 
ATOM   762  O  O   . ILE A 1 104 ? 22.827  41.272 20.803  1.00 11.83 ? 104  ILE A O   1 
ATOM   763  C  CB  . ILE A 1 104 ? 20.561  39.061 21.560  1.00 11.00 ? 104  ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 104 ? 19.790  40.380 21.394  1.00 12.62 ? 104  ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 104 ? 19.941  38.134 22.606  1.00 12.60 ? 104  ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 104 ? 18.377  40.159 20.865  1.00 12.74 ? 104  ILE A CD1 1 
ATOM   767  N  N   . SER A 1 105 ? 23.007  39.293 19.632  1.00 11.08 ? 105  SER A N   1 
ATOM   768  C  CA  . SER A 1 105 ? 23.489  39.965 18.426  1.00 11.36 ? 105  SER A CA  1 
ATOM   769  C  C   . SER A 1 105 ? 23.011  39.193 17.209  1.00 11.67 ? 105  SER A C   1 
ATOM   770  O  O   . SER A 1 105 ? 22.549  38.039 17.346  1.00 12.94 ? 105  SER A O   1 
ATOM   771  C  CB  . SER A 1 105 ? 25.019  40.072 18.437  1.00 12.18 ? 105  SER A CB  1 
ATOM   772  O  OG  . SER A 1 105 ? 25.432  40.876 17.345  1.00 13.14 ? 105  SER A OG  1 
ATOM   773  N  N   . LEU A 1 106 ? 23.108  39.842 16.051  1.00 12.05 ? 106  LEU A N   1 
ATOM   774  C  CA  . LEU A 1 106 ? 22.724  39.184 14.802  1.00 14.18 ? 106  LEU A CA  1 
ATOM   775  C  C   . LEU A 1 106 ? 23.963  38.712 14.015  1.00 14.29 ? 106  LEU A C   1 
ATOM   776  O  O   . LEU A 1 106 ? 23.870  38.276 12.857  1.00 18.63 ? 106  LEU A O   1 
ATOM   777  C  CB  . LEU A 1 106 ? 21.827  40.086 13.954  1.00 13.43 ? 106  LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 106 ? 20.513  40.496 14.620  1.00 12.13 ? 106  LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 106 ? 19.681  41.244 13.573  1.00 14.09 ? 106  LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 106 ? 19.758  39.304 15.217  1.00 13.65 ? 106  LEU A CD2 1 
ATOM   781  N  N   . SER A 1 107 ? 25.111  38.801 14.675  1.00 15.77 ? 107  SER A N   1 
ATOM   782  C  CA  . SER A 1 107 ? 26.384  38.324 14.102  1.00 14.77 ? 107  SER A CA  1 
ATOM   783  C  C   . SER A 1 107 ? 27.370  38.056 15.238  1.00 14.40 ? 107  SER A C   1 
ATOM   784  O  O   . SER A 1 107 ? 27.124  38.413 16.419  1.00 16.21 ? 107  SER A O   1 
ATOM   785  C  CB  . SER A 1 107 ? 26.901  39.337 13.086  1.00 16.41 ? 107  SER A CB  1 
ATOM   786  O  OG  . SER A 1 107 ? 27.367  40.543 13.687  1.00 19.20 ? 107  SER A OG  1 
ATOM   787  N  N   . GLY A 1 108 ? 28.490  37.431 14.959  1.00 16.66 ? 108  GLY A N   1 
ATOM   788  C  CA  . GLY A 1 108 ? 29.536  37.184 15.946  1.00 14.89 ? 108  GLY A CA  1 
ATOM   789  C  C   . GLY A 1 108 ? 29.145  36.103 16.930  1.00 14.61 ? 108  GLY A C   1 
ATOM   790  O  O   . GLY A 1 108 ? 28.273  35.264 16.712  1.00 16.93 ? 108  GLY A O   1 
ATOM   791  N  N   . ASP A 1 109 ? 29.839  36.075 18.076  1.00 15.32 ? 109  ASP A N   1 
ATOM   792  C  CA  . ASP A 1 109 ? 29.654  34.873 18.890  1.00 18.21 ? 109  ASP A CA  1 
ATOM   793  C  C   . ASP A 1 109 ? 28.472  35.035 19.821  1.00 15.58 ? 109  ASP A C   1 
ATOM   794  O  O   . ASP A 1 109 ? 28.136  34.051 20.474  1.00 17.95 ? 109  ASP A O   1 
ATOM   795  C  CB  . ASP A 1 109 ? 30.936  34.475 19.613  1.00 24.17 ? 109  ASP A CB  1 
ATOM   796  C  CG  . ASP A 1 109 ? 31.572  35.556 20.447  1.00 29.23 ? 109  ASP A CG  1 
ATOM   797  O  OD1 . ASP A 1 109 ? 30.955  36.636 20.515  1.00 28.04 ? 109  ASP A OD1 1 
ATOM   798  O  OD2 . ASP A 1 109 ? 32.669  35.326 21.011  1.00 39.35 ? 109  ASP A OD2 1 
ATOM   799  N  N   . HIS A 1 110 ? 27.823  36.194 19.848  1.00 13.32 ? 110  HIS A N   1 
ATOM   800  C  CA  . HIS A 1 110 ? 26.545  36.255 20.542  1.00 13.51 ? 110  HIS A CA  1 
ATOM   801  C  C   . HIS A 1 110 ? 25.388  36.055 19.554  1.00 12.69 ? 110  HIS A C   1 
ATOM   802  O  O   . HIS A 1 110 ? 24.214  36.291 19.894  1.00 13.31 ? 110  HIS A O   1 
ATOM   803  C  CB  . HIS A 1 110 ? 26.299  37.591 21.248  1.00 14.00 ? 110  HIS A CB  1 
ATOM   804  C  CG  . HIS A 1 110 ? 27.359  38.085 22.162  1.00 14.59 ? 110  HIS A CG  1 
ATOM   805  N  ND1 . HIS A 1 110 ? 27.080  39.120 23.028  1.00 14.90 ? 110  HIS A ND1 1 
ATOM   806  C  CD2 . HIS A 1 110 ? 28.675  37.809 22.335  1.00 14.50 ? 110  HIS A CD2 1 
ATOM   807  C  CE1 . HIS A 1 110 ? 28.187  39.416 23.727  1.00 14.64 ? 110  HIS A CE1 1 
ATOM   808  N  NE2 . HIS A 1 110 ? 29.152  38.632 23.311  1.00 14.23 ? 110  HIS A NE2 1 
HETATM 809  N  N   . CSX A 1 111 ? 25.687  35.599 18.345  1.00 13.42 ? 111  CSX A N   1 
HETATM 810  C  CA  . CSX A 1 111 ? 24.656  35.568 17.316  1.00 12.02 ? 111  CSX A CA  1 
HETATM 811  C  CB  . CSX A 1 111 ? 25.304  35.139 15.981  1.00 13.21 ? 111  CSX A CB  1 
HETATM 812  S  SG  . CSX A 1 111 ? 24.192  35.322 14.570  1.00 17.97 ? 111  CSX A SG  1 
HETATM 813  C  C   . CSX A 1 111 ? 23.529  34.566 17.603  1.00 12.01 ? 111  CSX A C   1 
HETATM 814  O  O   . CSX A 1 111 ? 23.789  33.401 17.939  1.00 14.08 ? 111  CSX A O   1 
HETATM 815  O  OD  . CSX A 1 111 ? 25.001  34.863 13.330  1.00 42.00 ? 111  CSX A OD  1 
ATOM   816  N  N   . ILE A 1 112 ? 22.304  35.046 17.436  1.00 11.56 ? 112  ILE A N   1 
ATOM   817  C  CA  . ILE A 1 112 ? 21.115  34.239 17.720  1.00 10.42 ? 112  ILE A CA  1 
ATOM   818  C  C   . ILE A 1 112 ? 20.445  33.771 16.428  1.00 11.68 ? 112  ILE A C   1 
ATOM   819  O  O   . ILE A 1 112 ? 19.467  33.018 16.499  1.00 13.17 ? 112  ILE A O   1 
ATOM   820  C  CB  . ILE A 1 112 ? 20.108  35.035 18.563  1.00 10.62 ? 112  ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 112 ? 19.581  36.291 17.859  1.00 12.52 ? 112  ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 112 ? 20.731  35.322 19.921  1.00 12.96 ? 112  ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 112 ? 18.462  36.975 18.665  1.00 13.43 ? 112  ILE A CD1 1 
ATOM   824  N  N   . ILE A 1 113 ? 20.952  34.180 15.245  1.00 12.91 ? 113  ILE A N   1 
ATOM   825  C  CA  . ILE A 1 113 ? 20.380  33.611 14.030  1.00 14.23 ? 113  ILE A CA  1 
ATOM   826  C  C   . ILE A 1 113 ? 20.612  32.116 13.976  1.00 13.94 ? 113  ILE A C   1 
ATOM   827  O  O   . ILE A 1 113 ? 21.697  31.615 14.293  1.00 15.36 ? 113  ILE A O   1 
ATOM   828  C  CB  . ILE A 1 113 ? 20.984  34.354 12.790  1.00 17.19 ? 113  ILE A CB  1 
ATOM   829  C  CG1 . ILE A 1 113 ? 20.514  35.795 12.763  1.00 19.25 ? 113  ILE A CG1 1 
ATOM   830  C  CG2 . ILE A 1 113 ? 20.675  33.563 11.514  1.00 19.70 ? 113  ILE A CG2 1 
ATOM   831  C  CD1 . ILE A 1 113 ? 21.018  36.671 11.668  1.00 23.87 ? 113  ILE A CD1 1 
ATOM   832  N  N   . GLY A 1 114 ? 19.528  31.402 13.564  1.00 13.51 ? 114  GLY A N   1 
ATOM   833  C  CA  . GLY A 1 114 ? 19.586  29.956 13.487  1.00 15.35 ? 114  GLY A CA  1 
ATOM   834  C  C   . GLY A 1 114 ? 19.375  29.275 14.824  1.00 12.22 ? 114  GLY A C   1 
ATOM   835  O  O   . GLY A 1 114 ? 19.505  28.046 14.914  1.00 13.15 ? 114  GLY A O   1 
ATOM   836  N  N   . ARG A 1 115 ? 19.027  30.072 15.857  1.00 11.64 ? 115  ARG A N   1 
ATOM   837  C  CA  . ARG A 1 115 ? 18.630  29.525 17.158  1.00 11.31 ? 115  ARG A CA  1 
ATOM   838  C  C   . ARG A 1 115 ? 17.125  29.700 17.338  1.00 10.91 ? 115  ARG A C   1 
ATOM   839  O  O   . ARG A 1 115 ? 16.419  30.165 16.444  1.00 12.91 ? 115  ARG A O   1 
ATOM   840  C  CB  . ARG A 1 115 ? 19.477  30.181 18.250  1.00 12.82 ? 115  ARG A CB  1 
ATOM   841  C  CG  . ARG A 1 115 ? 20.962  29.951 17.908  1.00 13.11 ? 115  ARG A CG  1 
ATOM   842  C  CD  . ARG A 1 115 ? 21.907  30.366 18.991  1.00 12.74 ? 115  ARG A CD  1 
ATOM   843  N  NE  . ARG A 1 115 ? 23.313  30.396 18.605  1.00 13.31 ? 115  ARG A NE  1 
ATOM   844  C  CZ  . ARG A 1 115 ? 24.125  29.334 18.663  1.00 14.91 ? 115  ARG A CZ  1 
ATOM   845  N  NH1 . ARG A 1 115 ? 23.663  28.168 19.119  1.00 14.56 ? 115  ARG A NH1 1 
ATOM   846  N  NH2 . ARG A 1 115 ? 25.404  29.434 18.301  1.00 14.89 ? 115  ARG A NH2 1 
ATOM   847  N  N   . THR A 1 116 ? 16.559  29.259 18.462  1.00 11.62 ? 116  THR A N   1 
ATOM   848  C  CA  . THR A 1 116 ? 15.128  29.221 18.633  1.00 10.69 ? 116  THR A CA  1 
ATOM   849  C  C   . THR A 1 116 ? 14.655  30.260 19.663  1.00 10.53 ? 116  THR A C   1 
ATOM   850  O  O   . THR A 1 116 ? 15.126  30.291 20.804  1.00 12.76 ? 116  THR A O   1 
ATOM   851  C  CB  . THR A 1 116 ? 14.667  27.833 19.108  1.00 11.22 ? 116  THR A CB  1 
ATOM   852  O  OG1 . THR A 1 116 ? 14.976  26.869 18.085  1.00 13.03 ? 116  THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 116 ? 13.164  27.820 19.341  1.00 12.54 ? 116  THR A CG2 1 
ATOM   854  N  N   . LEU A 1 117 ? 13.713  31.099 19.275  1.00 10.12 ? 117  LEU A N   1 
ATOM   855  C  CA  . LEU A 1 117 ? 13.023  32.003 20.192  1.00 10.13 ? 117  LEU A CA  1 
ATOM   856  C  C   . LEU A 1 117 ? 11.851  31.244 20.793  1.00 9.81  ? 117  LEU A C   1 
ATOM   857  O  O   . LEU A 1 117 ? 11.101  30.625 20.021  1.00 11.76 ? 117  LEU A O   1 
ATOM   858  C  CB  . LEU A 1 117 ? 12.550  33.250 19.445  1.00 11.57 ? 117  LEU A CB  1 
ATOM   859  C  CG  . LEU A 1 117 ? 11.992  34.395 20.301  1.00 13.66 ? 117  LEU A CG  1 
ATOM   860  C  CD1 . LEU A 1 117 ? 13.051  34.969 21.229  1.00 14.63 ? 117  LEU A CD1 1 
ATOM   861  C  CD2 . LEU A 1 117 ? 11.404  35.495 19.398  1.00 13.64 ? 117  LEU A CD2 1 
ATOM   862  N  N   . VAL A 1 118 ? 11.682  31.352 22.116  1.00 10.40 ? 118  VAL A N   1 
ATOM   863  C  CA  . VAL A 1 118 ? 10.643  30.614 22.807  1.00 9.35  ? 118  VAL A CA  1 
ATOM   864  C  C   . VAL A 1 118 ? 9.837   31.526 23.718  1.00 10.15 ? 118  VAL A C   1 
ATOM   865  O  O   . VAL A 1 118 ? 10.436  32.325 24.470  1.00 11.18 ? 118  VAL A O   1 
ATOM   866  C  CB  . VAL A 1 118 ? 11.261  29.497 23.671  1.00 9.41  ? 118  VAL A CB  1 
ATOM   867  C  CG1 . VAL A 1 118 ? 10.192  28.709 24.428  1.00 12.14 ? 118  VAL A CG1 1 
ATOM   868  C  CG2 . VAL A 1 118 ? 12.080  28.508 22.806  1.00 11.62 ? 118  VAL A CG2 1 
ATOM   869  N  N   . VAL A 1 119 ? 8.527   31.382 23.718  1.00 10.95 ? 119  VAL A N   1 
ATOM   870  C  CA  . VAL A 1 119 ? 7.674   32.012 24.717  1.00 10.97 ? 119  VAL A CA  1 
ATOM   871  C  C   . VAL A 1 119 ? 7.055   30.968 25.624  1.00 10.69 ? 119  VAL A C   1 
ATOM   872  O  O   . VAL A 1 119 ? 6.586   29.888 25.167  1.00 11.71 ? 119  VAL A O   1 
ATOM   873  C  CB  . VAL A 1 119 ? 6.627   32.947 24.063  1.00 12.61 ? 119  VAL A CB  1 
ATOM   874  C  CG1 . VAL A 1 119 ? 5.653   32.199 23.196  1.00 15.59 ? 119  VAL A CG1 1 
ATOM   875  C  CG2 . VAL A 1 119 ? 5.904   33.720 25.180  1.00 12.77 ? 119  VAL A CG2 1 
ATOM   876  N  N   . HIS A 1 120 ? 7.062   31.268 26.926  1.00 11.46 ? 120  HIS A N   1 
ATOM   877  C  CA  . HIS A 1 120 ? 6.720   30.289 27.940  1.00 11.72 ? 120  HIS A CA  1 
ATOM   878  C  C   . HIS A 1 120 ? 5.367   30.467 28.590  1.00 12.06 ? 120  HIS A C   1 
ATOM   879  O  O   . HIS A 1 120 ? 4.734   31.516 28.506  1.00 13.67 ? 120  HIS A O   1 
ATOM   880  C  CB  . HIS A 1 120 ? 7.800   30.383 29.067  1.00 11.41 ? 120  HIS A CB  1 
ATOM   881  C  CG  . HIS A 1 120 ? 9.061   29.608 28.735  1.00 11.88 ? 120  HIS A CG  1 
ATOM   882  N  ND1 . HIS A 1 120 ? 9.259   28.278 29.070  1.00 11.61 ? 120  HIS A ND1 1 
ATOM   883  C  CD2 . HIS A 1 120 ? 10.204  29.996 28.094  1.00 11.10 ? 120  HIS A CD2 1 
ATOM   884  C  CE1 . HIS A 1 120 ? 10.443  27.881 28.667  1.00 11.67 ? 120  HIS A CE1 1 
ATOM   885  N  NE2 . HIS A 1 120 ? 11.045  28.903 28.072  1.00 11.94 ? 120  HIS A NE2 1 
ATOM   886  N  N   . GLU A 1 121 ? 4.952   29.385 29.252  1.00 11.90 ? 121  GLU A N   1 
ATOM   887  C  CA  . GLU A 1 121 ? 3.689   29.287 29.975  1.00 12.62 ? 121  GLU A CA  1 
ATOM   888  C  C   . GLU A 1 121 ? 3.498   30.343 31.047  1.00 13.52 ? 121  GLU A C   1 
ATOM   889  O  O   . GLU A 1 121 ? 2.390   30.934 31.187  1.00 14.81 ? 121  GLU A O   1 
ATOM   890  C  CB  . GLU A 1 121 ? 3.657   27.880 30.611  1.00 14.82 ? 121  GLU A CB  1 
ATOM   891  C  CG  . GLU A 1 121 ? 2.392   27.593 31.427  1.00 19.19 ? 121  GLU A CG  1 
ATOM   892  C  CD  . GLU A 1 121 ? 2.565   26.428 32.385  1.00 21.54 ? 121  GLU A CD  1 
ATOM   893  O  OE1 . GLU A 1 121 ? 3.618   25.762 32.295  1.00 17.81 ? 121  GLU A OE1 1 
ATOM   894  O  OE2 . GLU A 1 121 ? 1.699   26.177 33.236  1.00 26.28 ? 121  GLU A OE2 1 
ATOM   895  N  N   . LYS A 1 122 ? 4.574   30.562 31.825  1.00 13.53 ? 122  LYS A N   1 
ATOM   896  C  CA  . LYS A 1 122 ? 4.442   31.524 32.945  1.00 16.63 ? 122  LYS A CA  1 
ATOM   897  C  C   . LYS A 1 122 ? 5.688   32.397 33.071  1.00 12.66 ? 122  LYS A C   1 
ATOM   898  O  O   . LYS A 1 122 ? 6.529   32.387 32.146  1.00 13.56 ? 122  LYS A O   1 
ATOM   899  C  CB  . LYS A 1 122 ? 4.103   30.830 34.256  1.00 19.62 ? 122  LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 122 ? 4.959   29.668 34.648  1.00 25.23 ? 122  LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 122 ? 4.304   28.797 35.718  1.00 23.75 ? 122  LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 122 ? 5.384   27.850 36.278  1.00 29.63 ? 122  LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 122 ? 4.837   27.040 37.412  1.00 33.84 ? 122  LYS A NZ  1 
ATOM   904  N  N   . ALA A 1 123 ? 5.861   33.145 34.130  1.00 12.86 ? 123  ALA A N   1 
ATOM   905  C  CA  . ALA A 1 123 ? 6.948   34.096 34.241  1.00 13.32 ? 123  ALA A CA  1 
ATOM   906  C  C   . ALA A 1 123 ? 8.291   33.435 34.467  1.00 13.89 ? 123  ALA A C   1 
ATOM   907  O  O   . ALA A 1 123 ? 8.388   32.451 35.207  1.00 14.56 ? 123  ALA A O   1 
ATOM   908  C  CB  . ALA A 1 123 ? 6.699   35.034 35.440  1.00 13.23 ? 123  ALA A CB  1 
ATOM   909  N  N   . ASP A 1 124 ? 9.299   34.043 33.853  1.00 13.97 ? 124  ASP A N   1 
ATOM   910  C  CA  . ASP A 1 124 ? 10.698  33.786 34.215  1.00 12.61 ? 124  ASP A CA  1 
ATOM   911  C  C   . ASP A 1 124 ? 10.944  34.526 35.520  1.00 14.57 ? 124  ASP A C   1 
ATOM   912  O  O   . ASP A 1 124 ? 10.655  35.742 35.627  1.00 15.95 ? 124  ASP A O   1 
ATOM   913  C  CB  . ASP A 1 124 ? 11.568  34.274 33.061  1.00 13.52 ? 124  ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 124 ? 13.056  34.044 33.234  1.00 11.89 ? 124  ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 124 ? 13.572  33.969 34.383  1.00 15.39 ? 124  ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 124 ? 13.742  33.997 32.193  1.00 13.87 ? 124  ASP A OD2 1 
ATOM   917  N  N   . HIS A 1 125 ? 11.471  33.847 36.516  1.00 15.61 ? 125  HIS A N   1 
ATOM   918  C  CA  . HIS A 1 125 ? 11.813  34.434 37.808  1.00 17.69 ? 125  HIS A CA  1 
ATOM   919  C  C   . HIS A 1 125 ? 13.093  35.256 37.798  1.00 16.80 ? 125  HIS A C   1 
ATOM   920  O  O   . HIS A 1 125 ? 13.492  35.863 38.823  1.00 21.53 ? 125  HIS A O   1 
ATOM   921  C  CB  . HIS A 1 125 ? 11.851  33.276 38.834  1.00 25.03 ? 125  HIS A CB  1 
ATOM   922  C  CG  . HIS A 1 125 ? 10.490  32.616 38.932  1.00 34.10 ? 125  HIS A CG  1 
ATOM   923  N  ND1 . HIS A 1 125 ? 9.462   33.128 39.700  1.00 41.70 ? 125  HIS A ND1 1 
ATOM   924  C  CD2 . HIS A 1 125 ? 10.000  31.481 38.366  1.00 37.22 ? 125  HIS A CD2 1 
ATOM   925  C  CE1 . HIS A 1 125 ? 8.408   32.333 39.589  1.00 44.93 ? 125  HIS A CE1 1 
ATOM   926  N  NE2 . HIS A 1 125 ? 8.717   31.323 38.786  1.00 44.14 ? 125  HIS A NE2 1 
ATOM   927  N  N   . LEU A 1 126 ? 13.775  35.380 36.659  1.00 18.08 ? 126  LEU A N   1 
ATOM   928  C  CA  . LEU A 1 126 ? 14.906  36.245 36.435  1.00 17.41 ? 126  LEU A CA  1 
ATOM   929  C  C   . LEU A 1 126 ? 16.061  35.984 37.366  1.00 22.69 ? 126  LEU A C   1 
ATOM   930  O  O   . LEU A 1 126 ? 16.840  36.900 37.696  1.00 26.49 ? 126  LEU A O   1 
ATOM   931  C  CB  . LEU A 1 126 ? 14.447  37.711 36.630  1.00 19.00 ? 126  LEU A CB  1 
ATOM   932  C  CG  . LEU A 1 126 ? 13.199  38.108 35.846  1.00 18.09 ? 126  LEU A CG  1 
ATOM   933  C  CD1 . LEU A 1 126 ? 12.835  39.567 36.110  1.00 24.76 ? 126  LEU A CD1 1 
ATOM   934  C  CD2 . LEU A 1 126 ? 13.415  37.876 34.354  1.00 16.02 ? 126  LEU A CD2 1 
ATOM   935  N  N   . GLY A 1 127 ? 16.247  34.760 37.827  1.00 26.38 ? 127  GLY A N   1 
ATOM   936  C  CA  . GLY A 1 127 ? 17.483  34.601 38.642  1.00 26.55 ? 127  GLY A CA  1 
ATOM   937  C  C   . GLY A 1 127 ? 17.175  34.616 40.114  1.00 27.12 ? 127  GLY A C   1 
ATOM   938  O  O   . GLY A 1 127 ? 17.963  34.113 40.928  1.00 44.10 ? 127  GLY A O   1 
ATOM   939  N  N   . LYS A 1 128 ? 16.030  35.154 40.509  1.00 30.17 ? 128  LYS A N   1 
ATOM   940  C  CA  . LYS A 1 128 ? 15.655  35.105 41.926  1.00 36.49 ? 128  LYS A CA  1 
ATOM   941  C  C   . LYS A 1 128 ? 15.389  33.686 42.416  1.00 46.20 ? 128  LYS A C   1 
ATOM   942  O  O   . LYS A 1 128 ? 14.713  32.944 41.664  1.00 57.02 ? 128  LYS A O   1 
ATOM   943  C  CB  . LYS A 1 128 ? 14.431  36.012 42.120  1.00 36.40 ? 128  LYS A CB  1 
ATOM   944  C  CG  . LYS A 1 128 ? 14.740  37.394 41.554  1.00 38.03 ? 128  LYS A CG  1 
ATOM   945  C  CD  . LYS A 1 128 ? 13.929  38.475 42.251  1.00 40.49 ? 128  LYS A CD  1 
ATOM   946  C  CE  . LYS A 1 128 ? 14.671  39.806 42.213  1.00 33.40 ? 128  LYS A CE  1 
ATOM   947  N  NZ  . LYS A 1 128 ? 15.656  39.924 43.325  1.00 30.48 ? 128  LYS A NZ  1 
ATOM   948  N  N   . LYS A 1 136 ? 18.353  27.846 37.164  1.00 33.42 ? 136  LYS A N   1 
ATOM   949  C  CA  . LYS A 1 136 ? 19.195  27.946 35.961  1.00 31.94 ? 136  LYS A CA  1 
ATOM   950  C  C   . LYS A 1 136 ? 18.348  28.239 34.731  1.00 29.36 ? 136  LYS A C   1 
ATOM   951  O  O   . LYS A 1 136 ? 18.883  28.620 33.663  1.00 29.63 ? 136  LYS A O   1 
ATOM   952  C  CB  . LYS A 1 136 ? 20.017  26.671 35.758  1.00 44.50 ? 136  LYS A CB  1 
ATOM   953  C  CG  . LYS A 1 136 ? 20.273  26.280 34.316  1.00 53.08 ? 136  LYS A CG  1 
ATOM   954  C  CD  . LYS A 1 136 ? 21.735  25.979 34.057  1.00 55.32 ? 136  LYS A CD  1 
ATOM   955  C  CE  . LYS A 1 136 ? 22.188  26.334 32.648  1.00 54.20 ? 136  LYS A CE  1 
ATOM   956  N  NZ  . LYS A 1 136 ? 23.689  26.320 32.563  1.00 39.11 ? 136  LYS A NZ  1 
ATOM   957  N  N   . THR A 1 137 ? 17.017  28.028 34.931  1.00 25.01 ? 137  THR A N   1 
ATOM   958  C  CA  . THR A 1 137 ? 16.135  28.218 33.780  1.00 22.33 ? 137  THR A CA  1 
ATOM   959  C  C   . THR A 1 137 ? 15.173  29.357 34.034  1.00 20.89 ? 137  THR A C   1 
ATOM   960  O  O   . THR A 1 137 ? 14.570  29.872 33.099  1.00 21.54 ? 137  THR A O   1 
ATOM   961  C  CB  . THR A 1 137 ? 15.304  26.972 33.429  1.00 21.56 ? 137  THR A CB  1 
ATOM   962  O  OG1 . THR A 1 137 ? 14.406  26.785 34.548  1.00 23.23 ? 137  THR A OG1 1 
ATOM   963  C  CG2 . THR A 1 137 ? 16.137  25.726 33.316  1.00 26.43 ? 137  THR A CG2 1 
ATOM   964  N  N   . GLY A 1 138 ? 14.949  29.790 35.259  1.00 20.22 ? 138  GLY A N   1 
ATOM   965  C  CA  . GLY A 1 138 ? 13.923  30.794 35.526  1.00 19.60 ? 138  GLY A CA  1 
ATOM   966  C  C   . GLY A 1 138 ? 12.550  30.232 35.819  1.00 18.50 ? 138  GLY A C   1 
ATOM   967  O  O   . GLY A 1 138 ? 11.645  31.014 36.135  1.00 18.96 ? 138  GLY A O   1 
ATOM   968  N  N   . ASN A 1 139 ? 12.293  28.941 35.741  1.00 18.19 ? 139  ASN A N   1 
ATOM   969  C  CA  . ASN A 1 139 ? 11.038  28.251 36.089  1.00 19.27 ? 139  ASN A CA  1 
ATOM   970  C  C   . ASN A 1 139 ? 9.821   28.850 35.371  1.00 18.21 ? 139  ASN A C   1 
ATOM   971  O  O   . ASN A 1 139 ? 8.783   29.096 36.016  1.00 19.94 ? 139  ASN A O   1 
ATOM   972  C  CB  . ASN A 1 139 ? 10.746  28.247 37.598  1.00 25.73 ? 139  ASN A CB  1 
ATOM   973  C  CG  . ASN A 1 139 ? 9.613   27.311 37.995  1.00 39.71 ? 139  ASN A CG  1 
ATOM   974  O  OD1 . ASN A 1 139 ? 9.339   26.275 37.361  1.00 53.26 ? 139  ASN A OD1 1 
ATOM   975  N  ND2 . ASN A 1 139 ? 8.882   27.655 39.064  1.00 59.80 ? 139  ASN A ND2 1 
ATOM   976  N  N   . ALA A 1 140 ? 9.959   29.061 34.072  1.00 14.26 ? 140  ALA A N   1 
ATOM   977  C  CA  . ALA A 1 140 ? 8.830   29.676 33.374  1.00 13.95 ? 140  ALA A CA  1 
ATOM   978  C  C   . ALA A 1 140 ? 7.871   28.654 32.803  1.00 13.25 ? 140  ALA A C   1 
ATOM   979  O  O   . ALA A 1 140 ? 7.034   29.002 31.946  1.00 13.71 ? 140  ALA A O   1 
ATOM   980  C  CB  . ALA A 1 140 ? 9.376   30.565 32.265  1.00 13.61 ? 140  ALA A CB  1 
ATOM   981  N  N   . GLY A 1 141 ? 7.954   27.389 33.203  1.00 13.58 ? 141  GLY A N   1 
ATOM   982  C  CA  . GLY A 1 141 ? 6.939   26.464 32.721  1.00 13.65 ? 141  GLY A CA  1 
ATOM   983  C  C   . GLY A 1 141 ? 7.175   26.039 31.292  1.00 12.28 ? 141  GLY A C   1 
ATOM   984  O  O   . GLY A 1 141 ? 8.246   26.179 30.693  1.00 13.70 ? 141  GLY A O   1 
ATOM   985  N  N   . SER A 1 142 ? 6.106   25.442 30.720  1.00 11.93 ? 142  SER A N   1 
ATOM   986  C  CA  . SER A 1 142 ? 6.270   24.832 29.387  1.00 12.50 ? 142  SER A CA  1 
ATOM   987  C  C   . SER A 1 142 ? 6.584   25.850 28.288  1.00 13.28 ? 142  SER A C   1 
ATOM   988  O  O   . SER A 1 142 ? 6.374   27.058 28.403  1.00 11.73 ? 142  SER A O   1 
ATOM   989  C  CB  . SER A 1 142 ? 5.008   24.072 29.014  1.00 13.87 ? 142  SER A CB  1 
ATOM   990  O  OG  . SER A 1 142 ? 3.883   24.884 28.775  1.00 17.70 ? 142  SER A OG  1 
ATOM   991  N  N   . ARG A 1 143 ? 7.117   25.330 27.193  1.00 10.95 ? 143  ARG A N   1 
ATOM   992  C  CA  . ARG A 1 143 ? 7.347   26.092 25.989  1.00 11.73 ? 143  ARG A CA  1 
ATOM   993  C  C   . ARG A 1 143 ? 6.095   26.125 25.143  1.00 11.54 ? 143  ARG A C   1 
ATOM   994  O  O   . ARG A 1 143 ? 5.710   25.072 24.606  1.00 15.47 ? 143  ARG A O   1 
ATOM   995  C  CB  . ARG A 1 143 ? 8.531   25.460 25.219  1.00 11.81 ? 143  ARG A CB  1 
ATOM   996  C  CG  . ARG A 1 143 ? 9.778   25.406 26.124  1.00 11.65 ? 143  ARG A CG  1 
ATOM   997  C  CD  . ARG A 1 143 ? 11.001  24.858 25.379  1.00 11.70 ? 143  ARG A CD  1 
ATOM   998  N  NE  . ARG A 1 143 ? 12.102  24.699 26.371  1.00 10.61 ? 143  ARG A NE  1 
ATOM   999  C  CZ  . ARG A 1 143 ? 13.221  24.006 26.131  1.00 10.85 ? 143  ARG A CZ  1 
ATOM   1000 N  NH1 . ARG A 1 143 ? 13.438  23.411 24.926  1.00 11.70 ? 143  ARG A NH1 1 
ATOM   1001 N  NH2 . ARG A 1 143 ? 14.170  23.890 27.080  1.00 12.40 ? 143  ARG A NH2 1 
ATOM   1002 N  N   . LEU A 1 144 ? 5.434   27.283 25.085  1.00 11.72 ? 144  LEU A N   1 
ATOM   1003 C  CA  . LEU A 1 144 ? 4.148   27.341 24.383  1.00 11.00 ? 144  LEU A CA  1 
ATOM   1004 C  C   . LEU A 1 144 ? 4.250   27.540 22.879  1.00 10.47 ? 144  LEU A C   1 
ATOM   1005 O  O   . LEU A 1 144 ? 3.417   27.056 22.110  1.00 12.17 ? 144  LEU A O   1 
ATOM   1006 C  CB  . LEU A 1 144 ? 3.295   28.513 24.926  1.00 12.59 ? 144  LEU A CB  1 
ATOM   1007 C  CG  . LEU A 1 144 ? 2.940   28.411 26.401  1.00 14.49 ? 144  LEU A CG  1 
ATOM   1008 C  CD1 . LEU A 1 144 ? 2.058   29.611 26.755  1.00 20.07 ? 144  LEU A CD1 1 
ATOM   1009 C  CD2 . LEU A 1 144 ? 2.244   27.092 26.706  1.00 18.83 ? 144  LEU A CD2 1 
ATOM   1010 N  N   . ALA A 1 145 ? 5.254   28.328 22.444  1.00 11.22 ? 145  ALA A N   1 
ATOM   1011 C  CA  . ALA A 1 145 ? 5.456   28.562 21.017  1.00 11.25 ? 145  ALA A CA  1 
ATOM   1012 C  C   . ALA A 1 145 ? 6.911   28.912 20.772  1.00 10.31 ? 145  ALA A C   1 
ATOM   1013 O  O   . ALA A 1 145 ? 7.558   29.448 21.680  1.00 12.74 ? 145  ALA A O   1 
ATOM   1014 C  CB  . ALA A 1 145 ? 4.538   29.654 20.487  1.00 12.49 ? 145  ALA A CB  1 
ATOM   1015 N  N   . CYS A 1 146 ? 7.374   28.633 19.548  1.00 11.18 ? 146  CYS A N   1 
ATOM   1016 C  CA  . CYS A 1 146 ? 8.787   28.864 19.252  1.00 11.27 ? 146  CYS A CA  1 
ATOM   1017 C  C   . CYS A 1 146 ? 8.945   28.914 17.733  1.00 10.91 ? 146  CYS A C   1 
ATOM   1018 O  O   . CYS A 1 146 ? 8.021   28.577 16.980  1.00 11.95 ? 146  CYS A O   1 
ATOM   1019 C  CB  . CYS A 1 146 ? 9.647   27.767 19.858  1.00 13.02 ? 146  CYS A CB  1 
ATOM   1020 S  SG  . CYS A 1 146 ? 9.252   26.080 19.290  1.00 15.75 ? 146  CYS A SG  1 
ATOM   1021 N  N   . GLY A 1 147 ? 10.114  29.394 17.306  1.00 12.04 ? 147  GLY A N   1 
ATOM   1022 C  CA  . GLY A 1 147 ? 10.449  29.330 15.897  1.00 12.43 ? 147  GLY A CA  1 
ATOM   1023 C  C   . GLY A 1 147 ? 11.949  29.538 15.753  1.00 10.73 ? 147  GLY A C   1 
ATOM   1024 O  O   . GLY A 1 147 ? 12.574  30.022 16.717  1.00 12.15 ? 147  GLY A O   1 
ATOM   1025 N  N   . VAL A 1 148 ? 12.469  29.194 14.596  1.00 11.07 ? 148  VAL A N   1 
ATOM   1026 C  CA  . VAL A 1 148 ? 13.882  29.431 14.315  1.00 11.42 ? 148  VAL A CA  1 
ATOM   1027 C  C   . VAL A 1 148 ? 14.050  30.876 13.836  1.00 12.13 ? 148  VAL A C   1 
ATOM   1028 O  O   . VAL A 1 148 ? 13.252  31.382 13.036  1.00 15.24 ? 148  VAL A O   1 
ATOM   1029 C  CB  . VAL A 1 148 ? 14.391  28.410 13.272  1.00 13.40 ? 148  VAL A CB  1 
ATOM   1030 C  CG1 . VAL A 1 148 ? 15.882  28.604 13.074  1.00 14.39 ? 148  VAL A CG1 1 
ATOM   1031 C  CG2 . VAL A 1 148 ? 14.051  27.008 13.756  1.00 13.97 ? 148  VAL A CG2 1 
ATOM   1032 N  N   . ILE A 1 149 ? 15.088  31.547 14.356  1.00 12.02 ? 149  ILE A N   1 
ATOM   1033 C  CA  . ILE A 1 149 ? 15.345  32.932 13.995  1.00 11.92 ? 149  ILE A CA  1 
ATOM   1034 C  C   . ILE A 1 149 ? 16.074  32.982 12.665  1.00 12.76 ? 149  ILE A C   1 
ATOM   1035 O  O   . ILE A 1 149 ? 17.157  32.402 12.517  1.00 16.82 ? 149  ILE A O   1 
ATOM   1036 C  CB  . ILE A 1 149 ? 16.147  33.622 15.114  1.00 11.02 ? 149  ILE A CB  1 
ATOM   1037 C  CG1 . ILE A 1 149 ? 15.370  33.603 16.444  1.00 11.64 ? 149  ILE A CG1 1 
ATOM   1038 C  CG2 . ILE A 1 149 ? 16.568  35.037 14.698  1.00 14.34 ? 149  ILE A CG2 1 
ATOM   1039 C  CD1 . ILE A 1 149 ? 16.212  33.974 17.645  1.00 12.59 ? 149  ILE A CD1 1 
ATOM   1040 N  N   . GLY A 1 150 ? 15.458  33.635 11.676  1.00 13.44 ? 150  GLY A N   1 
ATOM   1041 C  CA  . GLY A 1 150 ? 16.037  33.621 10.339  1.00 14.00 ? 150  GLY A CA  1 
ATOM   1042 C  C   . GLY A 1 150 ? 16.493  34.990 9.870   1.00 14.03 ? 150  GLY A C   1 
ATOM   1043 O  O   . GLY A 1 150 ? 16.060  36.029 10.366  1.00 15.19 ? 150  GLY A O   1 
ATOM   1044 N  N   . ILE A 1 151 ? 17.395  35.032 8.891   1.00 15.90 ? 151  ILE A N   1 
ATOM   1045 C  CA  . ILE A 1 151 ? 17.863  36.267 8.279   1.00 17.58 ? 151  ILE A CA  1 
ATOM   1046 C  C   . ILE A 1 151 ? 16.729  36.865 7.461   1.00 17.92 ? 151  ILE A C   1 
ATOM   1047 O  O   . ILE A 1 151 ? 16.109  36.133 6.663   1.00 20.96 ? 151  ILE A O   1 
ATOM   1048 C  CB  . ILE A 1 151 ? 19.057  35.990 7.358   1.00 20.98 ? 151  ILE A CB  1 
ATOM   1049 C  CG1 . ILE A 1 151 ? 20.273  35.500 8.128   1.00 21.28 ? 151  ILE A CG1 1 
ATOM   1050 C  CG2 . ILE A 1 151 ? 19.371  37.230 6.534   1.00 20.58 ? 151  ILE A CG2 1 
ATOM   1051 C  CD1 . ILE A 1 151 ? 21.362  34.865 7.270   1.00 24.23 ? 151  ILE A CD1 1 
ATOM   1052 N  N   . ALA A 1 152 ? 16.475  38.159 7.678   1.00 17.84 ? 152  ALA A N   1 
ATOM   1053 C  CA  . ALA A 1 152 ? 15.428  38.877 6.955   1.00 19.08 ? 152  ALA A CA  1 
ATOM   1054 C  C   . ALA A 1 152 ? 16.060  39.900 6.017   1.00 21.33 ? 152  ALA A C   1 
ATOM   1055 O  O   . ALA A 1 152 ? 17.200  40.351 6.204   1.00 23.54 ? 152  ALA A O   1 
ATOM   1056 C  CB  . ALA A 1 152 ? 14.425  39.520 7.905   1.00 19.15 ? 152  ALA A CB  1 
ATOM   1057 N  N   . GLN A 1 153 ? 15.289  40.252 4.995   1.00 27.64 ? 153  GLN A N   1 
ATOM   1058 C  CA  . GLN A 1 153 ? 15.657  41.284 4.054   1.00 30.21 ? 153  GLN A CA  1 
ATOM   1059 C  C   . GLN A 1 153 ? 15.631  42.670 4.684   1.00 34.94 ? 153  GLN A C   1 
ATOM   1060 O  O   . GLN A 1 153 ? 16.582  43.424 4.394   1.00 37.57 ? 153  GLN A O   1 
ATOM   1061 C  CB  . GLN A 1 153 ? 14.715  41.284 2.843   1.00 33.38 ? 153  GLN A CB  1 
ATOM   1062 C  CG  . GLN A 1 153 ? 15.393  42.081 1.695   1.00 35.65 ? 153  GLN A CG  1 
ATOM   1063 C  CD  . GLN A 1 153 ? 14.459  42.095 0.513   1.00 37.04 ? 153  GLN A CD  1 
ATOM   1064 O  OE1 . GLN A 1 153 ? 13.254  42.174 0.741   1.00 44.47 ? 153  GLN A OE1 1 
ATOM   1065 N  NE2 . GLN A 1 153 ? 15.024  42.009 -0.675  1.00 42.47 ? 153  GLN A NE2 1 
ATOM   1066 O  OXT . GLN A 1 153 ? 14.677  42.985 5.419   1.00 33.77 ? 153  GLN A OXT 1 
ATOM   1067 N  N   . ALA B 1 1   ? 33.291  20.125 13.658  1.00 51.03 ? 1    ALA B N   1 
ATOM   1068 C  CA  . ALA B 1 1   ? 32.059  19.572 13.103  1.00 54.73 ? 1    ALA B CA  1 
ATOM   1069 C  C   . ALA B 1 1   ? 30.836  20.359 13.538  1.00 57.78 ? 1    ALA B C   1 
ATOM   1070 O  O   . ALA B 1 1   ? 30.342  20.334 14.664  1.00 65.04 ? 1    ALA B O   1 
ATOM   1071 C  CB  . ALA B 1 1   ? 31.896  18.111 13.498  1.00 63.42 ? 1    ALA B CB  1 
ATOM   1072 N  N   . THR B 1 2   ? 30.284  21.115 12.588  1.00 45.62 ? 2    THR B N   1 
ATOM   1073 C  CA  . THR B 1 2   ? 29.068  21.826 12.943  1.00 42.68 ? 2    THR B CA  1 
ATOM   1074 C  C   . THR B 1 2   ? 27.917  21.046 12.296  1.00 35.61 ? 2    THR B C   1 
ATOM   1075 O  O   . THR B 1 2   ? 28.137  20.356 11.299  1.00 37.20 ? 2    THR B O   1 
ATOM   1076 C  CB  . THR B 1 2   ? 29.027  23.293 12.504  1.00 46.36 ? 2    THR B CB  1 
ATOM   1077 O  OG1 . THR B 1 2   ? 30.327  23.726 12.060  1.00 63.44 ? 2    THR B OG1 1 
ATOM   1078 C  CG2 . THR B 1 2   ? 28.687  24.177 13.697  1.00 51.73 ? 2    THR B CG2 1 
ATOM   1079 N  N   . LYS B 1 3   ? 26.753  21.220 12.924  1.00 29.20 ? 3    LYS B N   1 
ATOM   1080 C  CA  . LYS B 1 3   ? 25.551  20.583 12.457  1.00 22.61 ? 3    LYS B CA  1 
ATOM   1081 C  C   . LYS B 1 3   ? 24.423  21.606 12.365  1.00 20.85 ? 3    LYS B C   1 
ATOM   1082 O  O   . LYS B 1 3   ? 24.377  22.553 13.159  1.00 21.30 ? 3    LYS B O   1 
ATOM   1083 C  CB  . LYS B 1 3   ? 25.144  19.419 13.360  1.00 26.59 ? 3    LYS B CB  1 
ATOM   1084 C  CG  . LYS B 1 3   ? 26.097  18.226 13.312  1.00 32.46 ? 3    LYS B CG  1 
ATOM   1085 C  CD  . LYS B 1 3   ? 25.585  17.105 14.217  1.00 38.61 ? 3    LYS B CD  1 
ATOM   1086 C  CE  . LYS B 1 3   ? 26.381  15.837 14.028  1.00 44.44 ? 3    LYS B CE  1 
ATOM   1087 N  NZ  . LYS B 1 3   ? 25.931  14.684 14.862  1.00 59.48 ? 3    LYS B NZ  1 
ATOM   1088 N  N   . ALA B 1 4   ? 23.534  21.341 11.412  1.00 19.19 ? 4    ALA B N   1 
ATOM   1089 C  CA  . ALA B 1 4   ? 22.305  22.122 11.245  1.00 16.83 ? 4    ALA B CA  1 
ATOM   1090 C  C   . ALA B 1 4   ? 21.153  21.191 10.868  1.00 16.07 ? 4    ALA B C   1 
ATOM   1091 O  O   . ALA B 1 4   ? 21.381  20.029 10.544  1.00 17.94 ? 4    ALA B O   1 
ATOM   1092 C  CB  . ALA B 1 4   ? 22.440  23.221 10.225  1.00 16.60 ? 4    ALA B CB  1 
ATOM   1093 N  N   . VAL B 1 5   ? 19.935  21.728 10.950  1.00 14.96 ? 5    VAL B N   1 
ATOM   1094 C  CA  . VAL B 1 5   ? 18.750  20.928 10.664  1.00 15.31 ? 5    VAL B CA  1 
ATOM   1095 C  C   . VAL B 1 5   ? 17.670  21.862 10.159  1.00 15.02 ? 5    VAL B C   1 
ATOM   1096 O  O   . VAL B 1 5   ? 17.640  23.059 10.461  1.00 17.08 ? 5    VAL B O   1 
ATOM   1097 C  CB  . VAL B 1 5   ? 18.307  20.152 11.924  1.00 14.66 ? 5    VAL B CB  1 
ATOM   1098 C  CG1 . VAL B 1 5   ? 17.797  21.057 13.059  1.00 15.69 ? 5    VAL B CG1 1 
ATOM   1099 C  CG2 . VAL B 1 5   ? 17.239  19.087 11.592  1.00 16.40 ? 5    VAL B CG2 1 
ATOM   1100 N  N   . CYS B 1 6   ? 16.752  21.291 9.365   1.00 13.86 ? 6    CYS B N   1 
ATOM   1101 C  CA  . CYS B 1 6   ? 15.665  22.053 8.810   1.00 13.29 ? 6    CYS B CA  1 
ATOM   1102 C  C   . CYS B 1 6   ? 14.407  21.214 8.783   1.00 13.24 ? 6    CYS B C   1 
ATOM   1103 O  O   . CYS B 1 6   ? 14.432  20.060 8.260   1.00 15.15 ? 6    CYS B O   1 
ATOM   1104 C  CB  . CYS B 1 6   ? 16.046  22.447 7.354   1.00 15.04 ? 6    CYS B CB  1 
ATOM   1105 S  SG  . CYS B 1 6   ? 14.763  23.472 6.617   1.00 16.88 ? 6    CYS B SG  1 
ATOM   1106 N  N   . VAL B 1 7   ? 13.310  21.736 9.342   1.00 12.67 ? 7    VAL B N   1 
ATOM   1107 C  CA  . VAL B 1 7   ? 12.011  21.077 9.227   1.00 12.48 ? 7    VAL B CA  1 
ATOM   1108 C  C   . VAL B 1 7   ? 11.260  21.687 8.059   1.00 13.15 ? 7    VAL B C   1 
ATOM   1109 O  O   . VAL B 1 7   ? 10.937  22.871 8.152   1.00 14.08 ? 7    VAL B O   1 
ATOM   1110 C  CB  . VAL B 1 7   ? 11.200  21.237 10.527  1.00 13.54 ? 7    VAL B CB  1 
ATOM   1111 C  CG1 . VAL B 1 7   ? 9.820   20.636 10.338  1.00 16.58 ? 7    VAL B CG1 1 
ATOM   1112 C  CG2 . VAL B 1 7   ? 11.955  20.609 11.695  1.00 16.02 ? 7    VAL B CG2 1 
ATOM   1113 N  N   . LEU B 1 8   ? 10.975  20.911 7.015   1.00 12.69 ? 8    LEU B N   1 
ATOM   1114 C  CA  . LEU B 1 8   ? 10.288  21.498 5.860   1.00 14.72 ? 8    LEU B CA  1 
ATOM   1115 C  C   . LEU B 1 8   ? 8.795   21.283 6.005   1.00 13.56 ? 8    LEU B C   1 
ATOM   1116 O  O   . LEU B 1 8   ? 8.384   20.108 6.209   1.00 15.79 ? 8    LEU B O   1 
ATOM   1117 C  CB  . LEU B 1 8   ? 10.795  20.863 4.563   1.00 17.95 ? 8    LEU B CB  1 
ATOM   1118 C  CG  . LEU B 1 8   ? 12.237  21.198 4.196   1.00 20.01 ? 8    LEU B CG  1 
ATOM   1119 C  CD1 . LEU B 1 8   ? 13.220  20.230 4.865   1.00 20.60 ? 8    LEU B CD1 1 
ATOM   1120 C  CD2 . LEU B 1 8   ? 12.443  21.169 2.697   1.00 31.49 ? 8    LEU B CD2 1 
ATOM   1121 N  N   . LYS B 1 9   ? 8.024   22.356 5.899   1.00 15.36 ? 9    LYS B N   1 
ATOM   1122 C  CA  . LYS B 1 9   ? 6.571   22.288 5.969   1.00 18.09 ? 9    LYS B CA  1 
ATOM   1123 C  C   . LYS B 1 9   ? 5.955   23.252 4.948   1.00 18.98 ? 9    LYS B C   1 
ATOM   1124 O  O   . LYS B 1 9   ? 6.686   24.191 4.564   1.00 18.47 ? 9    LYS B O   1 
ATOM   1125 C  CB  . LYS B 1 9   ? 6.036   22.753 7.315   1.00 22.86 ? 9    LYS B CB  1 
ATOM   1126 C  CG  . LYS B 1 9   ? 6.528   21.929 8.481   1.00 25.46 ? 9    LYS B CG  1 
ATOM   1127 C  CD  . LYS B 1 9   ? 5.902   22.494 9.759   1.00 30.35 ? 9    LYS B CD  1 
ATOM   1128 C  CE  . LYS B 1 9   ? 5.351   21.357 10.578  1.00 36.32 ? 9    LYS B CE  1 
ATOM   1129 N  NZ  . LYS B 1 9   ? 4.986   21.719 11.980  1.00 25.35 ? 9    LYS B NZ  1 
ATOM   1130 N  N   . GLY B 1 10  ? 4.697   23.017 4.601   1.00 19.96 ? 10   GLY B N   1 
ATOM   1131 C  CA  . GLY B 1 10  ? 4.032   23.940 3.674   1.00 24.09 ? 10   GLY B CA  1 
ATOM   1132 C  C   . GLY B 1 10  ? 2.519   23.774 3.786   1.00 28.17 ? 10   GLY B C   1 
ATOM   1133 O  O   . GLY B 1 10  ? 2.079   23.264 4.823   1.00 29.27 ? 10   GLY B O   1 
ATOM   1134 N  N   . ASP B 1 11  ? 1.744   24.161 2.778   1.00 29.26 ? 11   ASP B N   1 
ATOM   1135 C  CA  . ASP B 1 11  ? 0.296   24.162 2.881   1.00 33.47 ? 11   ASP B CA  1 
ATOM   1136 C  C   . ASP B 1 11  ? -0.330  22.871 2.346   1.00 36.95 ? 11   ASP B C   1 
ATOM   1137 O  O   . ASP B 1 11  ? -1.565  22.749 2.355   1.00 42.96 ? 11   ASP B O   1 
ATOM   1138 C  CB  . ASP B 1 11  ? -0.331  25.337 2.108   1.00 39.89 ? 11   ASP B CB  1 
ATOM   1139 C  CG  . ASP B 1 11  ? -0.061  26.644 2.816   1.00 39.91 ? 11   ASP B CG  1 
ATOM   1140 O  OD1 . ASP B 1 11  ? -0.471  26.728 3.987   1.00 45.71 ? 11   ASP B OD1 1 
ATOM   1141 O  OD2 . ASP B 1 11  ? 0.551   27.556 2.221   1.00 42.08 ? 11   ASP B OD2 1 
ATOM   1142 N  N   . GLY B 1 12  ? 0.513   21.963 1.893   1.00 36.25 ? 12   GLY B N   1 
ATOM   1143 C  CA  . GLY B 1 12  ? 0.062   20.707 1.345   1.00 30.94 ? 12   GLY B CA  1 
ATOM   1144 C  C   . GLY B 1 12  ? 0.671   19.530 2.085   1.00 29.55 ? 12   GLY B C   1 
ATOM   1145 O  O   . GLY B 1 12  ? 1.049   19.631 3.251   1.00 28.25 ? 12   GLY B O   1 
ATOM   1146 N  N   . PRO B 1 13  ? 0.729   18.411 1.386   1.00 27.78 ? 13   PRO B N   1 
ATOM   1147 C  CA  . PRO B 1 13  ? 1.188   17.202 2.061   1.00 26.57 ? 13   PRO B CA  1 
ATOM   1148 C  C   . PRO B 1 13  ? 2.694   17.084 2.131   1.00 21.21 ? 13   PRO B C   1 
ATOM   1149 O  O   . PRO B 1 13  ? 3.153   16.111 2.766   1.00 25.11 ? 13   PRO B O   1 
ATOM   1150 C  CB  . PRO B 1 13  ? 0.612   16.100 1.139   1.00 29.35 ? 13   PRO B CB  1 
ATOM   1151 C  CG  . PRO B 1 13  ? 0.814   16.730 -0.205  1.00 30.08 ? 13   PRO B CG  1 
ATOM   1152 C  CD  . PRO B 1 13  ? 0.366   18.157 -0.030  1.00 30.41 ? 13   PRO B CD  1 
ATOM   1153 N  N   . VAL B 1 14  ? 3.478   17.974 1.539   1.00 20.41 ? 14   VAL B N   1 
ATOM   1154 C  CA  . VAL B 1 14  ? 4.928   17.752 1.534   1.00 17.86 ? 14   VAL B CA  1 
ATOM   1155 C  C   . VAL B 1 14  ? 5.513   18.188 2.864   1.00 18.36 ? 14   VAL B C   1 
ATOM   1156 O  O   . VAL B 1 14  ? 5.223   19.273 3.386   1.00 20.29 ? 14   VAL B O   1 
ATOM   1157 C  CB  . VAL B 1 14  ? 5.612   18.512 0.372   1.00 19.24 ? 14   VAL B CB  1 
ATOM   1158 C  CG1 . VAL B 1 14  ? 7.132   18.326 0.406   1.00 18.36 ? 14   VAL B CG1 1 
ATOM   1159 C  CG2 . VAL B 1 14  ? 5.005   18.065 -0.936  1.00 20.71 ? 14   VAL B CG2 1 
ATOM   1160 N  N   . GLN B 1 15  ? 6.353   17.322 3.430   1.00 17.53 ? 15   GLN B N   1 
ATOM   1161 C  CA  . GLN B 1 15  ? 6.987   17.635 4.704   1.00 18.81 ? 15   GLN B CA  1 
ATOM   1162 C  C   . GLN B 1 15  ? 8.197   16.759 4.874   1.00 16.96 ? 15   GLN B C   1 
ATOM   1163 O  O   . GLN B 1 15  ? 8.232   15.631 4.358   1.00 20.66 ? 15   GLN B O   1 
ATOM   1164 C  CB  . GLN B 1 15  ? 5.955   17.427 5.813   1.00 21.75 ? 15   GLN B CB  1 
ATOM   1165 C  CG  . GLN B 1 15  ? 5.474   15.996 5.911   1.00 30.92 ? 15   GLN B CG  1 
ATOM   1166 C  CD  . GLN B 1 15  ? 4.489   15.572 6.956   1.00 41.50 ? 15   GLN B CD  1 
ATOM   1167 O  OE1 . GLN B 1 15  ? 4.082   14.397 6.982   1.00 49.68 ? 15   GLN B OE1 1 
ATOM   1168 N  NE2 . GLN B 1 15  ? 4.030   16.418 7.877   1.00 55.66 ? 15   GLN B NE2 1 
ATOM   1169 N  N   . GLY B 1 16  ? 9.173   17.275 5.621   1.00 16.09 ? 16   GLY B N   1 
ATOM   1170 C  CA  . GLY B 1 16  ? 10.322  16.397 5.875   1.00 18.09 ? 16   GLY B CA  1 
ATOM   1171 C  C   . GLY B 1 16  ? 11.341  17.098 6.768   1.00 15.03 ? 16   GLY B C   1 
ATOM   1172 O  O   . GLY B 1 16  ? 11.089  18.210 7.255   1.00 17.12 ? 16   GLY B O   1 
ATOM   1173 N  N   . ILE B 1 17  ? 12.450  16.392 6.990   1.00 14.87 ? 17   ILE B N   1 
ATOM   1174 C  CA  . ILE B 1 17  ? 13.536  16.909 7.845   1.00 14.48 ? 17   ILE B CA  1 
ATOM   1175 C  C   . ILE B 1 17  ? 14.825  16.684 7.087   1.00 16.68 ? 17   ILE B C   1 
ATOM   1176 O  O   . ILE B 1 17  ? 15.014  15.596 6.557   1.00 18.41 ? 17   ILE B O   1 
ATOM   1177 C  CB  . ILE B 1 17  ? 13.564  16.225 9.214   1.00 14.83 ? 17   ILE B CB  1 
ATOM   1178 C  CG1 . ILE B 1 17  ? 12.347  16.612 10.079  1.00 15.96 ? 17   ILE B CG1 1 
ATOM   1179 C  CG2 . ILE B 1 17  ? 14.873  16.513 9.923   1.00 16.32 ? 17   ILE B CG2 1 
ATOM   1180 C  CD1 . ILE B 1 17  ? 12.209  15.700 11.304  1.00 20.21 ? 17   ILE B CD1 1 
ATOM   1181 N  N   . ILE B 1 18  ? 15.667  17.712 7.016   1.00 16.45 ? 18   ILE B N   1 
ATOM   1182 C  CA  . ILE B 1 18  ? 16.969  17.583 6.360   1.00 15.47 ? 18   ILE B CA  1 
ATOM   1183 C  C   . ILE B 1 18  ? 18.035  18.016 7.373   1.00 16.50 ? 18   ILE B C   1 
ATOM   1184 O  O   . ILE B 1 18  ? 17.886  19.056 8.017   1.00 16.64 ? 18   ILE B O   1 
ATOM   1185 C  CB  . ILE B 1 18  ? 17.027  18.388 5.072   1.00 16.90 ? 18   ILE B CB  1 
ATOM   1186 C  CG1 . ILE B 1 18  ? 16.038  17.866 4.017   1.00 17.52 ? 18   ILE B CG1 1 
ATOM   1187 C  CG2 . ILE B 1 18  ? 18.456  18.487 4.553   1.00 17.24 ? 18   ILE B CG2 1 
ATOM   1188 C  CD1 . ILE B 1 18  ? 16.389  16.549 3.403   1.00 18.57 ? 18   ILE B CD1 1 
ATOM   1189 N  N   . ASN B 1 19  ? 19.052  17.201 7.539   1.00 19.76 ? 19   ASN B N   1 
ATOM   1190 C  CA  . ASN B 1 19  ? 20.163  17.376 8.435   1.00 20.46 ? 19   ASN B CA  1 
ATOM   1191 C  C   . ASN B 1 19  ? 21.391  17.791 7.638   1.00 23.21 ? 19   ASN B C   1 
ATOM   1192 O  O   . ASN B 1 19  ? 21.579  17.337 6.508   1.00 22.94 ? 19   ASN B O   1 
ATOM   1193 C  CB  . ASN B 1 19  ? 20.516  16.074 9.173   1.00 21.75 ? 19   ASN B CB  1 
ATOM   1194 C  CG  . ASN B 1 19  ? 19.277  15.470 9.833   1.00 24.54 ? 19   ASN B CG  1 
ATOM   1195 O  OD1 . ASN B 1 19  ? 18.963  15.921 10.916  1.00 23.03 ? 19   ASN B OD1 1 
ATOM   1196 N  ND2 . ASN B 1 19  ? 18.588  14.517 9.188   1.00 22.49 ? 19   ASN B ND2 1 
ATOM   1197 N  N   . PHE B 1 20  ? 22.214  18.612 8.259   1.00 23.72 ? 20   PHE B N   1 
ATOM   1198 C  CA  . PHE B 1 20  ? 23.454  19.082 7.680   1.00 25.76 ? 20   PHE B CA  1 
ATOM   1199 C  C   . PHE B 1 20  ? 24.600  18.806 8.673   1.00 28.90 ? 20   PHE B C   1 
ATOM   1200 O  O   . PHE B 1 20  ? 24.421  19.061 9.864   1.00 26.65 ? 20   PHE B O   1 
ATOM   1201 C  CB  . PHE B 1 20  ? 23.391  20.568 7.380   1.00 23.43 ? 20   PHE B CB  1 
ATOM   1202 C  CG  . PHE B 1 20  ? 22.297  21.058 6.464   1.00 21.92 ? 20   PHE B CG  1 
ATOM   1203 C  CD1 . PHE B 1 20  ? 21.026  21.333 6.947   1.00 22.00 ? 20   PHE B CD1 1 
ATOM   1204 C  CD2 . PHE B 1 20  ? 22.560  21.226 5.097   1.00 22.72 ? 20   PHE B CD2 1 
ATOM   1205 C  CE1 . PHE B 1 20  ? 20.000  21.769 6.120   1.00 20.30 ? 20   PHE B CE1 1 
ATOM   1206 C  CE2 . PHE B 1 20  ? 21.556  21.675 4.262   1.00 22.16 ? 20   PHE B CE2 1 
ATOM   1207 C  CZ  . PHE B 1 20  ? 20.289  21.952 4.776   1.00 22.31 ? 20   PHE B CZ  1 
ATOM   1208 N  N   . GLU B 1 21  ? 25.743  18.302 8.223   1.00 30.09 ? 21   GLU B N   1 
ATOM   1209 C  CA  . GLU B 1 21  ? 26.907  18.076 9.065   1.00 30.08 ? 21   GLU B CA  1 
ATOM   1210 C  C   . GLU B 1 21  ? 28.192  18.463 8.327   1.00 32.70 ? 21   GLU B C   1 
ATOM   1211 O  O   . GLU B 1 21  ? 28.488  18.025 7.224   1.00 38.20 ? 21   GLU B O   1 
ATOM   1212 C  CB  . GLU B 1 21  ? 27.083  16.616 9.507   1.00 33.54 ? 21   GLU B CB  1 
ATOM   1213 C  CG  . GLU B 1 21  ? 28.076  16.452 10.644  1.00 41.82 ? 21   GLU B CG  1 
ATOM   1214 C  CD  . GLU B 1 21  ? 28.643  15.052 10.717  1.00 50.69 ? 21   GLU B CD  1 
ATOM   1215 O  OE1 . GLU B 1 21  ? 28.025  14.127 10.143  1.00 60.85 ? 21   GLU B OE1 1 
ATOM   1216 O  OE2 . GLU B 1 21  ? 29.717  14.899 11.356  1.00 67.02 ? 21   GLU B OE2 1 
ATOM   1217 N  N   . GLN B 1 22  ? 28.946  19.333 8.969   1.00 36.97 ? 22   GLN B N   1 
ATOM   1218 C  CA  . GLN B 1 22  ? 30.202  19.830 8.441   1.00 41.24 ? 22   GLN B CA  1 
ATOM   1219 C  C   . GLN B 1 22  ? 31.304  19.519 9.460   1.00 49.13 ? 22   GLN B C   1 
ATOM   1220 O  O   . GLN B 1 22  ? 31.439  20.221 10.455  1.00 51.42 ? 22   GLN B O   1 
ATOM   1221 C  CB  . GLN B 1 22  ? 30.061  21.319 8.162   1.00 41.82 ? 22   GLN B CB  1 
ATOM   1222 C  CG  . GLN B 1 22  ? 31.298  21.913 7.488   1.00 44.90 ? 22   GLN B CG  1 
ATOM   1223 C  CD  . GLN B 1 22  ? 30.951  23.328 7.040   1.00 43.09 ? 22   GLN B CD  1 
ATOM   1224 O  OE1 . GLN B 1 22  ? 30.397  24.074 7.842   1.00 40.21 ? 22   GLN B OE1 1 
ATOM   1225 N  NE2 . GLN B 1 22  ? 31.271  23.633 5.793   1.00 38.80 ? 22   GLN B NE2 1 
ATOM   1226 N  N   . LYS B 1 23  ? 32.032  18.439 9.196   1.00 57.90 ? 23   LYS B N   1 
ATOM   1227 C  CA  . LYS B 1 23  ? 32.992  17.935 10.161  1.00 61.55 ? 23   LYS B CA  1 
ATOM   1228 C  C   . LYS B 1 23  ? 34.174  18.882 10.355  1.00 61.51 ? 23   LYS B C   1 
ATOM   1229 O  O   . LYS B 1 23  ? 34.826  18.883 11.402  1.00 64.27 ? 23   LYS B O   1 
ATOM   1230 C  CB  . LYS B 1 23  ? 33.520  16.574 9.690   1.00 66.21 ? 23   LYS B CB  1 
ATOM   1231 C  CG  . LYS B 1 23  ? 34.893  16.726 9.042   1.00 73.24 ? 23   LYS B CG  1 
ATOM   1232 C  CD  . LYS B 1 23  ? 34.785  16.779 7.528   1.00 76.62 ? 23   LYS B CD  1 
ATOM   1233 C  CE  . LYS B 1 23  ? 36.114  17.116 6.869   1.00 76.23 ? 23   LYS B CE  1 
ATOM   1234 N  NZ  . LYS B 1 23  ? 37.217  17.087 7.871   1.00 65.96 ? 23   LYS B NZ  1 
ATOM   1235 N  N   . GLU B 1 24  ? 34.424  19.674 9.314   1.00 61.57 ? 24   GLU B N   1 
ATOM   1236 C  CA  . GLU B 1 24  ? 35.562  20.573 9.284   1.00 60.28 ? 24   GLU B CA  1 
ATOM   1237 C  C   . GLU B 1 24  ? 35.239  21.954 8.727   1.00 60.74 ? 24   GLU B C   1 
ATOM   1238 O  O   . GLU B 1 24  ? 34.426  22.138 7.829   1.00 58.04 ? 24   GLU B O   1 
ATOM   1239 C  CB  . GLU B 1 24  ? 36.685  19.985 8.420   1.00 59.79 ? 24   GLU B CB  1 
ATOM   1240 C  CG  . GLU B 1 24  ? 37.366  20.985 7.501   1.00 63.38 ? 24   GLU B CG  1 
ATOM   1241 C  CD  . GLU B 1 24  ? 38.772  20.578 7.088   1.00 69.03 ? 24   GLU B CD  1 
ATOM   1242 O  OE1 . GLU B 1 24  ? 38.899  19.646 6.262   1.00 78.72 ? 24   GLU B OE1 1 
ATOM   1243 O  OE2 . GLU B 1 24  ? 39.745  21.183 7.581   1.00 68.78 ? 24   GLU B OE2 1 
ATOM   1244 N  N   . SER B 1 25  ? 35.951  22.919 9.294   1.00 63.89 ? 25   SER B N   1 
ATOM   1245 C  CA  . SER B 1 25  ? 35.906  24.297 8.838   1.00 65.69 ? 25   SER B CA  1 
ATOM   1246 C  C   . SER B 1 25  ? 36.060  24.351 7.318   1.00 60.25 ? 25   SER B C   1 
ATOM   1247 O  O   . SER B 1 25  ? 37.097  23.958 6.779   1.00 56.90 ? 25   SER B O   1 
ATOM   1248 C  CB  . SER B 1 25  ? 36.994  25.127 9.531   1.00 67.44 ? 25   SER B CB  1 
ATOM   1249 O  OG  . SER B 1 25  ? 36.399  26.218 10.228  1.00 63.76 ? 25   SER B OG  1 
ATOM   1250 N  N   . ASN B 1 26  ? 34.996  24.822 6.686   1.00 59.44 ? 26   ASN B N   1 
ATOM   1251 C  CA  . ASN B 1 26  ? 34.948  25.084 5.256   1.00 57.90 ? 26   ASN B CA  1 
ATOM   1252 C  C   . ASN B 1 26  ? 34.973  23.773 4.473   1.00 54.31 ? 26   ASN B C   1 
ATOM   1253 O  O   . ASN B 1 26  ? 35.179  23.752 3.262   1.00 61.82 ? 26   ASN B O   1 
ATOM   1254 C  CB  . ASN B 1 26  ? 36.095  26.030 4.878   1.00 62.19 ? 26   ASN B CB  1 
ATOM   1255 C  CG  . ASN B 1 26  ? 35.870  27.419 5.460   1.00 65.97 ? 26   ASN B CG  1 
ATOM   1256 O  OD1 . ASN B 1 26  ? 36.440  27.818 6.490   1.00 75.35 ? 26   ASN B OD1 1 
ATOM   1257 N  ND2 . ASN B 1 26  ? 35.017  28.206 4.801   1.00 76.69 ? 26   ASN B ND2 1 
ATOM   1258 N  N   . GLY B 1 27  ? 34.738  22.685 5.205   1.00 50.35 ? 27   GLY B N   1 
ATOM   1259 C  CA  . GLY B 1 27  ? 34.747  21.332 4.720   1.00 50.76 ? 27   GLY B CA  1 
ATOM   1260 C  C   . GLY B 1 27  ? 33.471  20.986 3.993   1.00 47.13 ? 27   GLY B C   1 
ATOM   1261 O  O   . GLY B 1 27  ? 32.505  21.742 3.889   1.00 49.05 ? 27   GLY B O   1 
ATOM   1262 N  N   . PRO B 1 28  ? 33.432  19.784 3.433   1.00 47.55 ? 28   PRO B N   1 
ATOM   1263 C  CA  . PRO B 1 28  ? 32.218  19.355 2.733   1.00 45.14 ? 28   PRO B CA  1 
ATOM   1264 C  C   . PRO B 1 28  ? 31.090  19.244 3.750   1.00 43.52 ? 28   PRO B C   1 
ATOM   1265 O  O   . PRO B 1 28  ? 31.344  18.837 4.884   1.00 43.59 ? 28   PRO B O   1 
ATOM   1266 C  CB  . PRO B 1 28  ? 32.605  17.990 2.176   1.00 48.38 ? 28   PRO B CB  1 
ATOM   1267 C  CG  . PRO B 1 28  ? 34.105  18.007 2.162   1.00 50.43 ? 28   PRO B CG  1 
ATOM   1268 C  CD  . PRO B 1 28  ? 34.491  18.765 3.418   1.00 49.07 ? 28   PRO B CD  1 
ATOM   1269 N  N   . VAL B 1 29  ? 29.914  19.622 3.286   1.00 38.02 ? 29   VAL B N   1 
ATOM   1270 C  CA  . VAL B 1 29  ? 28.662  19.571 4.023   1.00 36.13 ? 29   VAL B CA  1 
ATOM   1271 C  C   . VAL B 1 29  ? 27.842  18.366 3.565   1.00 36.70 ? 29   VAL B C   1 
ATOM   1272 O  O   . VAL B 1 29  ? 27.388  18.315 2.423   1.00 37.46 ? 29   VAL B O   1 
ATOM   1273 C  CB  . VAL B 1 29  ? 27.815  20.838 3.848   1.00 32.50 ? 29   VAL B CB  1 
ATOM   1274 C  CG1 . VAL B 1 29  ? 26.623  20.796 4.803   1.00 33.54 ? 29   VAL B CG1 1 
ATOM   1275 C  CG2 . VAL B 1 29  ? 28.663  22.081 4.088   1.00 33.85 ? 29   VAL B CG2 1 
ATOM   1276 N  N   . LYS B 1 30  ? 27.680  17.422 4.472   1.00 32.31 ? 30   LYS B N   1 
ATOM   1277 C  CA  . LYS B 1 30  ? 26.773  16.296 4.244   1.00 29.78 ? 30   LYS B CA  1 
ATOM   1278 C  C   . LYS B 1 30  ? 25.367  16.849 4.405   1.00 34.41 ? 30   LYS B C   1 
ATOM   1279 O  O   . LYS B 1 30  ? 25.120  17.683 5.289   1.00 35.48 ? 30   LYS B O   1 
ATOM   1280 C  CB  . LYS B 1 30  ? 27.070  15.161 5.214   1.00 35.49 ? 30   LYS B CB  1 
ATOM   1281 C  CG  . LYS B 1 30  ? 28.131  14.210 4.685   1.00 38.07 ? 30   LYS B CG  1 
ATOM   1282 C  CD  . LYS B 1 30  ? 29.237  13.910 5.659   1.00 46.32 ? 30   LYS B CD  1 
ATOM   1283 C  CE  . LYS B 1 30  ? 29.175  12.491 6.211   1.00 54.06 ? 30   LYS B CE  1 
ATOM   1284 N  NZ  . LYS B 1 30  ? 30.293  12.256 7.174   1.00 59.61 ? 30   LYS B NZ  1 
ATOM   1285 N  N   . VAL B 1 31  ? 24.484  16.422 3.532   1.00 32.11 ? 31   VAL B N   1 
ATOM   1286 C  CA  . VAL B 1 31  ? 23.074  16.799 3.620   1.00 29.42 ? 31   VAL B CA  1 
ATOM   1287 C  C   . VAL B 1 31  ? 22.244  15.536 3.521   1.00 26.38 ? 31   VAL B C   1 
ATOM   1288 O  O   . VAL B 1 31  ? 22.358  14.804 2.534   1.00 30.82 ? 31   VAL B O   1 
ATOM   1289 C  CB  . VAL B 1 31  ? 22.733  17.757 2.473   1.00 29.77 ? 31   VAL B CB  1 
ATOM   1290 C  CG1 . VAL B 1 31  ? 21.294  18.210 2.599   1.00 26.71 ? 31   VAL B CG1 1 
ATOM   1291 C  CG2 . VAL B 1 31  ? 23.722  18.918 2.441   1.00 29.47 ? 31   VAL B CG2 1 
ATOM   1292 N  N   . TRP B 1 32  ? 21.399  15.224 4.493   1.00 23.84 ? 32   TRP B N   1 
ATOM   1293 C  CA  . TRP B 1 32  ? 20.674  13.958 4.409   1.00 23.22 ? 32   TRP B CA  1 
ATOM   1294 C  C   . TRP B 1 32  ? 19.387  14.050 5.206   1.00 23.06 ? 32   TRP B C   1 
ATOM   1295 O  O   . TRP B 1 32  ? 19.264  14.872 6.110   1.00 22.42 ? 32   TRP B O   1 
ATOM   1296 C  CB  . TRP B 1 32  ? 21.574  12.830 4.897   1.00 28.41 ? 32   TRP B CB  1 
ATOM   1297 C  CG  . TRP B 1 32  ? 21.663  12.781 6.391   1.00 29.57 ? 32   TRP B CG  1 
ATOM   1298 C  CD1 . TRP B 1 32  ? 20.940  12.005 7.250   1.00 30.64 ? 32   TRP B CD1 1 
ATOM   1299 C  CD2 . TRP B 1 32  ? 22.545  13.555 7.202   1.00 30.15 ? 32   TRP B CD2 1 
ATOM   1300 N  NE1 . TRP B 1 32  ? 21.321  12.258 8.532   1.00 32.29 ? 32   TRP B NE1 1 
ATOM   1301 C  CE2 . TRP B 1 32  ? 22.307  13.204 8.533   1.00 29.63 ? 32   TRP B CE2 1 
ATOM   1302 C  CE3 . TRP B 1 32  ? 23.517  14.517 6.941   1.00 34.77 ? 32   TRP B CE3 1 
ATOM   1303 C  CZ2 . TRP B 1 32  ? 22.981  13.753 9.620   1.00 28.54 ? 32   TRP B CZ2 1 
ATOM   1304 C  CZ3 . TRP B 1 32  ? 24.179  15.055 8.016   1.00 34.68 ? 32   TRP B CZ3 1 
ATOM   1305 C  CH2 . TRP B 1 32  ? 23.929  14.692 9.338   1.00 31.91 ? 32   TRP B CH2 1 
ATOM   1306 N  N   . GLY B 1 33  ? 18.410  13.222 4.861   1.00 22.86 ? 33   GLY B N   1 
ATOM   1307 C  CA  . GLY B 1 33  ? 17.124  13.181 5.536   1.00 19.84 ? 33   GLY B CA  1 
ATOM   1308 C  C   . GLY B 1 33  ? 16.079  12.595 4.614   1.00 19.64 ? 33   GLY B C   1 
ATOM   1309 O  O   . GLY B 1 33  ? 16.378  11.852 3.685   1.00 23.41 ? 33   GLY B O   1 
ATOM   1310 N  N   . SER B 1 34  ? 14.825  12.933 4.873   1.00 20.21 ? 34   SER B N   1 
ATOM   1311 C  CA  . SER B 1 34  ? 13.728  12.375 4.083   1.00 19.37 ? 34   SER B CA  1 
ATOM   1312 C  C   . SER B 1 34  ? 12.646  13.415 3.892   1.00 17.97 ? 34   SER B C   1 
ATOM   1313 O  O   . SER B 1 34  ? 12.327  14.169 4.847   1.00 19.32 ? 34   SER B O   1 
ATOM   1314 C  CB  . SER B 1 34  ? 13.178  11.137 4.803   1.00 22.31 ? 34   SER B CB  1 
ATOM   1315 O  OG  . SER B 1 34  ? 12.410  10.372 3.888   1.00 26.58 ? 34   SER B OG  1 
ATOM   1316 N  N   . ILE B 1 35  ? 12.075  13.474 2.706   1.00 19.43 ? 35   ILE B N   1 
ATOM   1317 C  CA  . ILE B 1 35  ? 10.932  14.372 2.471   1.00 18.62 ? 35   ILE B CA  1 
ATOM   1318 C  C   . ILE B 1 35  ? 9.783   13.520 1.939   1.00 17.83 ? 35   ILE B C   1 
ATOM   1319 O  O   . ILE B 1 35  ? 10.039  12.730 1.025   1.00 22.16 ? 35   ILE B O   1 
ATOM   1320 C  CB  . ILE B 1 35  ? 11.269  15.510 1.505   1.00 19.52 ? 35   ILE B CB  1 
ATOM   1321 C  CG1 . ILE B 1 35  ? 12.475  16.342 1.985   1.00 22.81 ? 35   ILE B CG1 1 
ATOM   1322 C  CG2 . ILE B 1 35  ? 10.072  16.408 1.215   1.00 18.74 ? 35   ILE B CG2 1 
ATOM   1323 C  CD1 . ILE B 1 35  ? 12.973  17.292 0.914   1.00 21.04 ? 35   ILE B CD1 1 
ATOM   1324 N  N   . LYS B 1 36  ? 8.564   13.632 2.457   1.00 19.64 ? 36   LYS B N   1 
ATOM   1325 C  CA  . LYS B 1 36  ? 7.512   12.737 1.960   1.00 19.61 ? 36   LYS B CA  1 
ATOM   1326 C  C   . LYS B 1 36  ? 6.362   13.589 1.417   1.00 19.81 ? 36   LYS B C   1 
ATOM   1327 O  O   . LYS B 1 36  ? 6.403   14.797 1.538   1.00 18.30 ? 36   LYS B O   1 
ATOM   1328 C  CB  . LYS B 1 36  ? 6.968   11.789 3.023   1.00 23.69 ? 36   LYS B CB  1 
ATOM   1329 C  CG  . LYS B 1 36  ? 6.162   12.543 4.082   1.00 30.47 ? 36   LYS B CG  1 
ATOM   1330 C  CD  . LYS B 1 36  ? 6.055   11.648 5.326   1.00 37.31 ? 36   LYS B CD  1 
ATOM   1331 C  CE  . LYS B 1 36  ? 4.629   11.201 5.574   1.00 43.13 ? 36   LYS B CE  1 
ATOM   1332 N  NZ  . LYS B 1 36  ? 4.274   11.163 7.031   1.00 57.31 ? 36   LYS B NZ  1 
ATOM   1333 N  N   . GLY B 1 37  ? 5.398   12.883 0.831   1.00 18.72 ? 37   GLY B N   1 
ATOM   1334 C  CA  . GLY B 1 37  ? 4.244   13.496 0.215   1.00 18.23 ? 37   GLY B CA  1 
ATOM   1335 C  C   . GLY B 1 37  ? 4.484   14.145 -1.123  1.00 19.09 ? 37   GLY B C   1 
ATOM   1336 O  O   . GLY B 1 37  ? 3.582   14.889 -1.562  1.00 22.10 ? 37   GLY B O   1 
ATOM   1337 N  N   . LEU B 1 38  ? 5.628   13.857 -1.744  1.00 17.71 ? 38   LEU B N   1 
ATOM   1338 C  CA  . LEU B 1 38  ? 5.957   14.409 -3.055  1.00 19.27 ? 38   LEU B CA  1 
ATOM   1339 C  C   . LEU B 1 38  ? 5.401   13.562 -4.201  1.00 20.78 ? 38   LEU B C   1 
ATOM   1340 O  O   . LEU B 1 38  ? 5.194   12.366 -4.047  1.00 26.71 ? 38   LEU B O   1 
ATOM   1341 C  CB  . LEU B 1 38  ? 7.471   14.485 -3.229  1.00 19.43 ? 38   LEU B CB  1 
ATOM   1342 C  CG  . LEU B 1 38  ? 8.215   15.476 -2.328  1.00 16.51 ? 38   LEU B CG  1 
ATOM   1343 C  CD1 . LEU B 1 38  ? 9.674   15.069 -2.216  1.00 19.88 ? 38   LEU B CD1 1 
ATOM   1344 C  CD2 . LEU B 1 38  ? 8.070   16.891 -2.881  1.00 19.21 ? 38   LEU B CD2 1 
ATOM   1345 N  N   . THR B 1 39  ? 5.195   14.215 -5.338  1.00 18.98 ? 39   THR B N   1 
ATOM   1346 C  CA  . THR B 1 39  ? 4.855   13.410 -6.518  1.00 19.58 ? 39   THR B CA  1 
ATOM   1347 C  C   . THR B 1 39  ? 6.097   12.644 -6.930  1.00 19.63 ? 39   THR B C   1 
ATOM   1348 O  O   . THR B 1 39  ? 7.224   13.142 -6.768  1.00 21.21 ? 39   THR B O   1 
ATOM   1349 C  CB  . THR B 1 39  ? 4.374   14.253 -7.712  1.00 20.64 ? 39   THR B CB  1 
ATOM   1350 O  OG1 . THR B 1 39  ? 5.331   15.297 -7.989  1.00 21.73 ? 39   THR B OG1 1 
ATOM   1351 C  CG2 . THR B 1 39  ? 3.023   14.866 -7.363  1.00 21.56 ? 39   THR B CG2 1 
ATOM   1352 N  N   . GLU B 1 40  ? 5.912   11.446 -7.453  1.00 20.27 ? 40   GLU B N   1 
ATOM   1353 C  CA  . GLU B 1 40  ? 7.069   10.681 -7.907  1.00 20.54 ? 40   GLU B CA  1 
ATOM   1354 C  C   . GLU B 1 40  ? 7.909   11.464 -8.900  1.00 19.54 ? 40   GLU B C   1 
ATOM   1355 O  O   . GLU B 1 40  ? 7.327   12.133 -9.759  1.00 22.56 ? 40   GLU B O   1 
ATOM   1356 C  CB  . GLU B 1 40  ? 6.537   9.403  -8.562  1.00 21.53 ? 40   GLU B CB  1 
ATOM   1357 C  CG  . GLU B 1 40  ? 7.617   8.509  -9.131  1.00 21.56 ? 40   GLU B CG  1 
ATOM   1358 C  CD  . GLU B 1 40  ? 7.036   7.257  -9.770  1.00 21.45 ? 40   GLU B CD  1 
ATOM   1359 O  OE1 . GLU B 1 40  ? 5.914   6.866  -9.393  1.00 21.63 ? 40   GLU B OE1 1 
ATOM   1360 O  OE2 . GLU B 1 40  ? 7.713   6.682  -10.652 1.00 22.26 ? 40   GLU B OE2 1 
ATOM   1361 N  N   . GLY B 1 41  ? 9.234   11.372 -8.828  1.00 19.73 ? 41   GLY B N   1 
ATOM   1362 C  CA  . GLY B 1 41  ? 10.080  12.086 -9.760  1.00 18.61 ? 41   GLY B CA  1 
ATOM   1363 C  C   . GLY B 1 41  ? 10.951  13.136 -9.112  1.00 21.33 ? 41   GLY B C   1 
ATOM   1364 O  O   . GLY B 1 41  ? 11.124  13.189 -7.883  1.00 21.24 ? 41   GLY B O   1 
ATOM   1365 N  N   . LEU B 1 42  ? 11.548  13.994 -9.947  1.00 22.38 ? 42   LEU B N   1 
ATOM   1366 C  CA  . LEU B 1 42  ? 12.523  14.970 -9.469  1.00 22.89 ? 42   LEU B CA  1 
ATOM   1367 C  C   . LEU B 1 42  ? 11.902  16.249 -8.942  1.00 24.82 ? 42   LEU B C   1 
ATOM   1368 O  O   . LEU B 1 42  ? 10.928  16.753 -9.503  1.00 26.87 ? 42   LEU B O   1 
ATOM   1369 C  CB  . LEU B 1 42  ? 13.435  15.335 -10.647 1.00 29.39 ? 42   LEU B CB  1 
ATOM   1370 C  CG  . LEU B 1 42  ? 14.709  14.498 -10.802 1.00 31.84 ? 42   LEU B CG  1 
ATOM   1371 C  CD1 . LEU B 1 42  ? 14.420  13.012 -10.933 1.00 34.17 ? 42   LEU B CD1 1 
ATOM   1372 C  CD2 . LEU B 1 42  ? 15.494  14.989 -12.004 1.00 32.91 ? 42   LEU B CD2 1 
ATOM   1373 N  N   . HIS B 1 43  ? 12.468  16.801 -7.870  1.00 21.59 ? 43   HIS B N   1 
ATOM   1374 C  CA  . HIS B 1 43  ? 11.991  18.052 -7.287  1.00 19.91 ? 43   HIS B CA  1 
ATOM   1375 C  C   . HIS B 1 43  ? 13.144  18.998 -6.997  1.00 21.06 ? 43   HIS B C   1 
ATOM   1376 O  O   . HIS B 1 43  ? 14.066  18.557 -6.302  1.00 22.09 ? 43   HIS B O   1 
ATOM   1377 C  CB  . HIS B 1 43  ? 11.233  17.772 -5.970  1.00 18.33 ? 43   HIS B CB  1 
ATOM   1378 C  CG  . HIS B 1 43  ? 9.969   17.007 -6.277  1.00 18.08 ? 43   HIS B CG  1 
ATOM   1379 N  ND1 . HIS B 1 43  ? 8.774   17.619 -6.542  1.00 19.97 ? 43   HIS B ND1 1 
ATOM   1380 C  CD2 . HIS B 1 43  ? 9.736   15.664 -6.388  1.00 18.86 ? 43   HIS B CD2 1 
ATOM   1381 C  CE1 . HIS B 1 43  ? 7.845   16.704 -6.797  1.00 20.22 ? 43   HIS B CE1 1 
ATOM   1382 N  NE2 . HIS B 1 43  ? 8.399   15.504 -6.698  1.00 20.19 ? 43   HIS B NE2 1 
ATOM   1383 N  N   . GLY B 1 44  ? 13.087  20.225 -7.515  1.00 21.26 ? 44   GLY B N   1 
ATOM   1384 C  CA  . GLY B 1 44  ? 14.137  21.212 -7.265  1.00 22.02 ? 44   GLY B CA  1 
ATOM   1385 C  C   . GLY B 1 44  ? 14.377  21.411 -5.772  1.00 23.52 ? 44   GLY B C   1 
ATOM   1386 O  O   . GLY B 1 44  ? 13.452  21.393 -4.959  1.00 22.30 ? 44   GLY B O   1 
ATOM   1387 N  N   . PHE B 1 45  ? 15.634  21.601 -5.385  1.00 23.33 ? 45   PHE B N   1 
ATOM   1388 C  CA  . PHE B 1 45  ? 16.068  21.619 -3.980  1.00 19.96 ? 45   PHE B CA  1 
ATOM   1389 C  C   . PHE B 1 45  ? 17.016  22.795 -3.797  1.00 22.74 ? 45   PHE B C   1 
ATOM   1390 O  O   . PHE B 1 45  ? 18.131  22.704 -4.366  1.00 22.53 ? 45   PHE B O   1 
ATOM   1391 C  CB  . PHE B 1 45  ? 16.728  20.284 -3.668  1.00 24.80 ? 45   PHE B CB  1 
ATOM   1392 C  CG  . PHE B 1 45  ? 17.030  19.924 -2.234  1.00 23.31 ? 45   PHE B CG  1 
ATOM   1393 C  CD1 . PHE B 1 45  ? 16.051  20.041 -1.261  1.00 21.28 ? 45   PHE B CD1 1 
ATOM   1394 C  CD2 . PHE B 1 45  ? 18.265  19.434 -1.850  1.00 22.98 ? 45   PHE B CD2 1 
ATOM   1395 C  CE1 . PHE B 1 45  ? 16.322  19.670 0.034   1.00 21.67 ? 45   PHE B CE1 1 
ATOM   1396 C  CE2 . PHE B 1 45  ? 18.571  19.075 -0.553  1.00 22.32 ? 45   PHE B CE2 1 
ATOM   1397 C  CZ  . PHE B 1 45  ? 17.567  19.203 0.382   1.00 23.44 ? 45   PHE B CZ  1 
ATOM   1398 N  N   . HIS B 1 46  ? 16.575  23.828 -3.076  1.00 20.50 ? 46   HIS B N   1 
ATOM   1399 C  CA  . HIS B 1 46  ? 17.316  25.084 -3.104  1.00 21.64 ? 46   HIS B CA  1 
ATOM   1400 C  C   . HIS B 1 46  ? 17.464  25.693 -1.711  1.00 21.48 ? 46   HIS B C   1 
ATOM   1401 O  O   . HIS B 1 46  ? 16.531  25.620 -0.919  1.00 21.33 ? 46   HIS B O   1 
ATOM   1402 C  CB  . HIS B 1 46  ? 16.559  26.135 -3.910  1.00 22.64 ? 46   HIS B CB  1 
ATOM   1403 C  CG  . HIS B 1 46  ? 16.348  25.864 -5.365  1.00 23.05 ? 46   HIS B CG  1 
ATOM   1404 N  ND1 . HIS B 1 46  ? 15.315  26.486 -6.012  1.00 22.36 ? 46   HIS B ND1 1 
ATOM   1405 C  CD2 . HIS B 1 46  ? 16.994  25.083 -6.276  1.00 22.98 ? 46   HIS B CD2 1 
ATOM   1406 C  CE1 . HIS B 1 46  ? 15.328  26.097 -7.280  1.00 25.55 ? 46   HIS B CE1 1 
ATOM   1407 N  NE2 . HIS B 1 46  ? 16.329  25.238 -7.475  1.00 24.02 ? 46   HIS B NE2 1 
ATOM   1408 N  N   . VAL B 1 47  ? 18.574  26.344 -1.435  1.00 22.33 ? 47   VAL B N   1 
ATOM   1409 C  CA  . VAL B 1 47  ? 18.637  27.289 -0.320  1.00 23.36 ? 47   VAL B CA  1 
ATOM   1410 C  C   . VAL B 1 47  ? 18.227  28.664 -0.850  1.00 21.05 ? 47   VAL B C   1 
ATOM   1411 O  O   . VAL B 1 47  ? 18.845  29.204 -1.802  1.00 26.33 ? 47   VAL B O   1 
ATOM   1412 C  CB  . VAL B 1 47  ? 20.043  27.336 0.284   1.00 24.79 ? 47   VAL B CB  1 
ATOM   1413 C  CG1 . VAL B 1 47  ? 20.074  28.248 1.501   1.00 24.92 ? 47   VAL B CG1 1 
ATOM   1414 C  CG2 . VAL B 1 47  ? 20.533  25.943 0.667   1.00 27.66 ? 47   VAL B CG2 1 
ATOM   1415 N  N   . HIS B 1 48  ? 17.193  29.250 -0.298  1.00 22.21 ? 48   HIS B N   1 
ATOM   1416 C  CA  . HIS B 1 48  ? 16.745  30.590 -0.639  1.00 21.34 ? 48   HIS B CA  1 
ATOM   1417 C  C   . HIS B 1 48  ? 17.334  31.546 0.382   1.00 21.14 ? 48   HIS B C   1 
ATOM   1418 O  O   . HIS B 1 48  ? 17.689  31.118 1.490   1.00 21.56 ? 48   HIS B O   1 
ATOM   1419 C  CB  . HIS B 1 48  ? 15.223  30.648 -0.722  1.00 21.08 ? 48   HIS B CB  1 
ATOM   1420 C  CG  . HIS B 1 48  ? 14.741  30.075 -2.032  1.00 23.28 ? 48   HIS B CG  1 
ATOM   1421 N  ND1 . HIS B 1 48  ? 14.145  30.856 -2.993  1.00 27.51 ? 48   HIS B ND1 1 
ATOM   1422 C  CD2 . HIS B 1 48  ? 14.796  28.845 -2.582  1.00 22.95 ? 48   HIS B CD2 1 
ATOM   1423 C  CE1 . HIS B 1 48  ? 13.830  30.113 -4.052  1.00 27.09 ? 48   HIS B CE1 1 
ATOM   1424 N  NE2 . HIS B 1 48  ? 14.217  28.851 -3.823  1.00 23.40 ? 48   HIS B NE2 1 
ATOM   1425 N  N   . GLU B 1 49  ? 17.438  32.807 0.015   1.00 23.05 ? 49   GLU B N   1 
ATOM   1426 C  CA  . GLU B 1 49  ? 18.227  33.761 0.770   1.00 23.80 ? 49   GLU B CA  1 
ATOM   1427 C  C   . GLU B 1 49  ? 17.694  34.097 2.165   1.00 22.74 ? 49   GLU B C   1 
ATOM   1428 O  O   . GLU B 1 49  ? 18.543  34.231 3.068   1.00 21.57 ? 49   GLU B O   1 
ATOM   1429 C  CB  . GLU B 1 49  ? 18.364  35.054 -0.072  1.00 24.57 ? 49   GLU B CB  1 
ATOM   1430 C  CG  . GLU B 1 49  ? 19.285  36.073 0.600   1.00 25.91 ? 49   GLU B CG  1 
ATOM   1431 C  CD  . GLU B 1 49  ? 19.404  37.370 -0.149  1.00 31.28 ? 49   GLU B CD  1 
ATOM   1432 O  OE1 . GLU B 1 49  ? 18.793  37.537 -1.233  1.00 34.73 ? 49   GLU B OE1 1 
ATOM   1433 O  OE2 . GLU B 1 49  ? 20.150  38.254 0.361   1.00 32.65 ? 49   GLU B OE2 1 
ATOM   1434 N  N   . PHE B 1 50  ? 16.391  34.280 2.368   1.00 21.86 ? 50   PHE B N   1 
ATOM   1435 C  CA  . PHE B 1 50  ? 15.895  34.747 3.664   1.00 19.98 ? 50   PHE B CA  1 
ATOM   1436 C  C   . PHE B 1 50  ? 15.229  33.624 4.472   1.00 18.50 ? 50   PHE B C   1 
ATOM   1437 O  O   . PHE B 1 50  ? 14.455  32.836 3.923   1.00 18.50 ? 50   PHE B O   1 
ATOM   1438 C  CB  . PHE B 1 50  ? 14.869  35.883 3.502   1.00 21.78 ? 50   PHE B CB  1 
ATOM   1439 C  CG  . PHE B 1 50  ? 15.489  37.007 2.673   1.00 25.12 ? 50   PHE B CG  1 
ATOM   1440 C  CD1 . PHE B 1 50  ? 16.594  37.669 3.157   1.00 27.74 ? 50   PHE B CD1 1 
ATOM   1441 C  CD2 . PHE B 1 50  ? 14.978  37.387 1.442   1.00 24.99 ? 50   PHE B CD2 1 
ATOM   1442 C  CE1 . PHE B 1 50  ? 17.225  38.691 2.449   1.00 30.41 ? 50   PHE B CE1 1 
ATOM   1443 C  CE2 . PHE B 1 50  ? 15.605  38.387 0.729   1.00 29.58 ? 50   PHE B CE2 1 
ATOM   1444 C  CZ  . PHE B 1 50  ? 16.724  39.052 1.221   1.00 31.78 ? 50   PHE B CZ  1 
ATOM   1445 N  N   . GLY B 1 51  ? 15.540  33.614 5.760   1.00 16.67 ? 51   GLY B N   1 
ATOM   1446 C  CA  . GLY B 1 51  ? 14.917  32.701 6.721   1.00 17.06 ? 51   GLY B CA  1 
ATOM   1447 C  C   . GLY B 1 51  ? 13.633  33.347 7.236   1.00 17.40 ? 51   GLY B C   1 
ATOM   1448 O  O   . GLY B 1 51  ? 13.387  33.392 8.431   1.00 19.31 ? 51   GLY B O   1 
ATOM   1449 N  N   . ASP B 1 52  ? 12.821  33.863 6.322   1.00 18.46 ? 52   ASP B N   1 
ATOM   1450 C  CA  . ASP B 1 52  ? 11.599  34.608 6.633   1.00 16.50 ? 52   ASP B CA  1 
ATOM   1451 C  C   . ASP B 1 52  ? 10.449  33.735 6.184   1.00 18.88 ? 52   ASP B C   1 
ATOM   1452 O  O   . ASP B 1 52  ? 10.261  33.605 4.974   1.00 21.66 ? 52   ASP B O   1 
ATOM   1453 C  CB  . ASP B 1 52  ? 11.653  35.955 5.940   1.00 19.53 ? 52   ASP B CB  1 
ATOM   1454 C  CG  . ASP B 1 52  ? 10.471  36.855 6.199   1.00 19.26 ? 52   ASP B CG  1 
ATOM   1455 O  OD1 . ASP B 1 52  ? 9.424   36.307 6.624   1.00 22.25 ? 52   ASP B OD1 1 
ATOM   1456 O  OD2 . ASP B 1 52  ? 10.572  38.090 5.986   1.00 22.04 ? 52   ASP B OD2 1 
ATOM   1457 N  N   . ASN B 1 53  ? 9.723   33.192 7.159   1.00 18.67 ? 53   ASN B N   1 
ATOM   1458 C  CA  . ASN B 1 53  ? 8.531   32.404 6.877   1.00 21.07 ? 53   ASN B CA  1 
ATOM   1459 C  C   . ASN B 1 53  ? 7.263   33.175 7.182   1.00 20.82 ? 53   ASN B C   1 
ATOM   1460 O  O   . ASN B 1 53  ? 6.202   32.560 7.338   1.00 22.03 ? 53   ASN B O   1 
ATOM   1461 C  CB  . ASN B 1 53  ? 8.572   31.149 7.757   1.00 22.44 ? 53   ASN B CB  1 
ATOM   1462 C  CG  . ASN B 1 53  ? 7.560   30.094 7.334   1.00 24.68 ? 53   ASN B CG  1 
ATOM   1463 O  OD1 . ASN B 1 53  ? 6.759   29.554 8.100   1.00 37.16 ? 53   ASN B OD1 1 
ATOM   1464 N  ND2 . ASN B 1 53  ? 7.559   29.805 6.049   1.00 32.13 ? 53   ASN B ND2 1 
ATOM   1465 N  N   . THR B 1 54  ? 7.346   34.505 7.281   1.00 20.32 ? 54   THR B N   1 
ATOM   1466 C  CA  . THR B 1 54  ? 6.141   35.243 7.626   1.00 21.65 ? 54   THR B CA  1 
ATOM   1467 C  C   . THR B 1 54  ? 5.022   35.103 6.592   1.00 26.99 ? 54   THR B C   1 
ATOM   1468 O  O   . THR B 1 54  ? 3.853   35.159 6.983   1.00 32.69 ? 54   THR B O   1 
ATOM   1469 C  CB  . THR B 1 54  ? 6.414   36.754 7.839   1.00 22.42 ? 54   THR B CB  1 
ATOM   1470 O  OG1 . THR B 1 54  ? 6.984   37.362 6.667   1.00 23.42 ? 54   THR B OG1 1 
ATOM   1471 C  CG2 . THR B 1 54  ? 7.388   36.895 8.996   1.00 22.50 ? 54   THR B CG2 1 
ATOM   1472 N  N   . ALA B 1 55  ? 5.319   34.947 5.317   1.00 28.11 ? 55   ALA B N   1 
ATOM   1473 C  CA  . ALA B 1 55  ? 4.404   34.719 4.212   1.00 25.67 ? 55   ALA B CA  1 
ATOM   1474 C  C   . ALA B 1 55  ? 4.663   33.338 3.617   1.00 29.33 ? 55   ALA B C   1 
ATOM   1475 O  O   . ALA B 1 55  ? 4.692   33.109 2.404   1.00 34.98 ? 55   ALA B O   1 
ATOM   1476 C  CB  . ALA B 1 55  ? 4.551   35.837 3.190   1.00 31.26 ? 55   ALA B CB  1 
ATOM   1477 N  N   . GLY B 1 56  ? 4.838   32.375 4.525   1.00 27.83 ? 56   GLY B N   1 
ATOM   1478 C  CA  . GLY B 1 56  ? 5.182   31.026 4.081   1.00 27.85 ? 56   GLY B CA  1 
ATOM   1479 C  C   . GLY B 1 56  ? 6.459   31.023 3.260   1.00 26.10 ? 56   GLY B C   1 
ATOM   1480 O  O   . GLY B 1 56  ? 7.361   31.864 3.430   1.00 31.83 ? 56   GLY B O   1 
ATOM   1481 N  N   . CYS B 1 57  ? 6.584   30.071 2.333   1.00 22.17 ? 57   CYS B N   1 
ATOM   1482 C  CA  . CYS B 1 57  ? 7.808   29.971 1.545   1.00 21.32 ? 57   CYS B CA  1 
ATOM   1483 C  C   . CYS B 1 57  ? 7.985   31.151 0.614   1.00 21.82 ? 57   CYS B C   1 
ATOM   1484 O  O   . CYS B 1 57  ? 9.050   31.379 0.043   1.00 22.92 ? 57   CYS B O   1 
ATOM   1485 C  CB  . CYS B 1 57  ? 7.748   28.693 0.716   1.00 22.13 ? 57   CYS B CB  1 
ATOM   1486 S  SG  . CYS B 1 57  ? 7.592   27.202 1.743   1.00 24.04 ? 57   CYS B SG  1 
ATOM   1487 N  N   . THR B 1 58  ? 6.919   31.919 0.417   1.00 23.41 ? 58   THR B N   1 
ATOM   1488 C  CA  . THR B 1 58  ? 7.045   33.037 -0.517  1.00 26.23 ? 58   THR B CA  1 
ATOM   1489 C  C   . THR B 1 58  ? 7.983   34.123 -0.023  1.00 25.67 ? 58   THR B C   1 
ATOM   1490 O  O   . THR B 1 58  ? 8.595   34.843 -0.786  1.00 26.98 ? 58   THR B O   1 
ATOM   1491 C  CB  . THR B 1 58  ? 5.665   33.662 -0.775  1.00 27.49 ? 58   THR B CB  1 
ATOM   1492 O  OG1 . THR B 1 58  ? 4.819   32.642 -1.320  1.00 32.16 ? 58   THR B OG1 1 
ATOM   1493 C  CG2 . THR B 1 58  ? 5.786   34.779 -1.812  1.00 31.03 ? 58   THR B CG2 1 
ATOM   1494 N  N   . SER B 1 59  ? 8.071   34.248 1.301   1.00 22.47 ? 59   SER B N   1 
ATOM   1495 C  CA  . SER B 1 59  ? 8.921   35.334 1.814   1.00 22.69 ? 59   SER B CA  1 
ATOM   1496 C  C   . SER B 1 59  ? 10.374  34.912 1.880   1.00 22.04 ? 59   SER B C   1 
ATOM   1497 O  O   . SER B 1 59  ? 11.236  35.664 2.404   1.00 23.16 ? 59   SER B O   1 
ATOM   1498 C  CB  . SER B 1 59  ? 8.317   35.800 3.142   1.00 23.95 ? 59   SER B CB  1 
ATOM   1499 O  OG  . SER B 1 59  ? 7.860   34.737 3.948   1.00 26.90 ? 59   SER B OG  1 
ATOM   1500 N  N   . ALA B 1 60  ? 10.747  33.735 1.361   1.00 21.53 ? 60   ALA B N   1 
ATOM   1501 C  CA  . ALA B 1 60  ? 12.138  33.329 1.439   1.00 20.75 ? 60   ALA B CA  1 
ATOM   1502 C  C   . ALA B 1 60  ? 13.047  34.013 0.419   1.00 21.75 ? 60   ALA B C   1 
ATOM   1503 O  O   . ALA B 1 60  ? 14.274  33.776 0.463   1.00 24.08 ? 60   ALA B O   1 
ATOM   1504 C  CB  . ALA B 1 60  ? 12.273  31.808 1.282   1.00 23.22 ? 60   ALA B CB  1 
ATOM   1505 N  N   . GLY B 1 61  ? 12.532  34.842 -0.478  1.00 23.28 ? 61   GLY B N   1 
ATOM   1506 C  CA  . GLY B 1 61  ? 13.359  35.532 -1.471  1.00 25.75 ? 61   GLY B CA  1 
ATOM   1507 C  C   . GLY B 1 61  ? 13.921  34.602 -2.525  1.00 26.83 ? 61   GLY B C   1 
ATOM   1508 O  O   . GLY B 1 61  ? 13.430  33.474 -2.715  1.00 26.02 ? 61   GLY B O   1 
ATOM   1509 N  N   . PRO B 1 62  ? 14.963  35.069 -3.185  1.00 29.41 ? 62   PRO B N   1 
ATOM   1510 C  CA  . PRO B 1 62  ? 15.528  34.372 -4.353  1.00 28.65 ? 62   PRO B CA  1 
ATOM   1511 C  C   . PRO B 1 62  ? 16.512  33.304 -3.917  1.00 28.59 ? 62   PRO B C   1 
ATOM   1512 O  O   . PRO B 1 62  ? 16.699  33.102 -2.702  1.00 26.62 ? 62   PRO B O   1 
ATOM   1513 C  CB  . PRO B 1 62  ? 16.222  35.513 -5.123  1.00 28.11 ? 62   PRO B CB  1 
ATOM   1514 C  CG  . PRO B 1 62  ? 16.726  36.372 -4.005  1.00 31.65 ? 62   PRO B CG  1 
ATOM   1515 C  CD  . PRO B 1 62  ? 15.699  36.312 -2.904  1.00 33.19 ? 62   PRO B CD  1 
ATOM   1516 N  N   . HIS B 1 63  ? 17.133  32.606 -4.853  1.00 27.26 ? 63   HIS B N   1 
ATOM   1517 C  CA  . HIS B 1 63  ? 18.168  31.650 -4.528  1.00 28.15 ? 63   HIS B CA  1 
ATOM   1518 C  C   . HIS B 1 63  ? 19.336  32.286 -3.794  1.00 27.54 ? 63   HIS B C   1 
ATOM   1519 O  O   . HIS B 1 63  ? 19.775  33.353 -4.187  1.00 33.50 ? 63   HIS B O   1 
ATOM   1520 C  CB  . HIS B 1 63  ? 18.742  31.040 -5.809  1.00 28.99 ? 63   HIS B CB  1 
ATOM   1521 C  CG  . HIS B 1 63  ? 17.747  30.270 -6.609  1.00 29.87 ? 63   HIS B CG  1 
ATOM   1522 N  ND1 . HIS B 1 63  ? 18.073  29.531 -7.730  1.00 34.44 ? 63   HIS B ND1 1 
ATOM   1523 C  CD2 . HIS B 1 63  ? 16.411  30.123 -6.417  1.00 29.79 ? 63   HIS B CD2 1 
ATOM   1524 C  CE1 . HIS B 1 63  ? 16.976  28.978 -8.191  1.00 31.81 ? 63   HIS B CE1 1 
ATOM   1525 N  NE2 . HIS B 1 63  ? 15.936  29.316 -7.412  1.00 29.33 ? 63   HIS B NE2 1 
ATOM   1526 N  N   . PHE B 1 64  ? 19.839  31.623 -2.760  1.00 28.21 ? 64   PHE B N   1 
ATOM   1527 C  CA  . PHE B 1 64  ? 21.001  32.222 -2.056  1.00 28.71 ? 64   PHE B CA  1 
ATOM   1528 C  C   . PHE B 1 64  ? 22.135  32.341 -3.076  1.00 32.08 ? 64   PHE B C   1 
ATOM   1529 O  O   . PHE B 1 64  ? 22.665  31.346 -3.582  1.00 36.12 ? 64   PHE B O   1 
ATOM   1530 C  CB  . PHE B 1 64  ? 21.293  31.400 -0.809  1.00 29.03 ? 64   PHE B CB  1 
ATOM   1531 C  CG  . PHE B 1 64  ? 22.467  31.924 0.006   1.00 31.83 ? 64   PHE B CG  1 
ATOM   1532 C  CD1 . PHE B 1 64  ? 22.582  33.268 0.299   1.00 31.80 ? 64   PHE B CD1 1 
ATOM   1533 C  CD2 . PHE B 1 64  ? 23.447  31.064 0.459   1.00 32.02 ? 64   PHE B CD2 1 
ATOM   1534 C  CE1 . PHE B 1 64  ? 23.656  33.765 1.036   1.00 29.20 ? 64   PHE B CE1 1 
ATOM   1535 C  CE2 . PHE B 1 64  ? 24.509  31.524 1.194   1.00 31.66 ? 64   PHE B CE2 1 
ATOM   1536 C  CZ  . PHE B 1 64  ? 24.617  32.878 1.485   1.00 29.41 ? 64   PHE B CZ  1 
ATOM   1537 N  N   . ASN B 1 65  ? 22.461  33.584 -3.407  1.00 33.72 ? 65   ASN B N   1 
ATOM   1538 C  CA  . ASN B 1 65  ? 23.334  33.989 -4.495  1.00 34.28 ? 65   ASN B CA  1 
ATOM   1539 C  C   . ASN B 1 65  ? 24.312  35.083 -4.066  1.00 38.25 ? 65   ASN B C   1 
ATOM   1540 O  O   . ASN B 1 65  ? 24.331  36.115 -4.748  1.00 40.76 ? 65   ASN B O   1 
ATOM   1541 C  CB  . ASN B 1 65  ? 22.516  34.553 -5.664  1.00 35.79 ? 65   ASN B CB  1 
ATOM   1542 C  CG  . ASN B 1 65  ? 23.318  34.706 -6.940  1.00 37.29 ? 65   ASN B CG  1 
ATOM   1543 O  OD1 . ASN B 1 65  ? 24.437  34.185 -7.037  1.00 33.71 ? 65   ASN B OD1 1 
ATOM   1544 N  ND2 . ASN B 1 65  ? 22.740  35.385 -7.936  1.00 38.49 ? 65   ASN B ND2 1 
ATOM   1545 N  N   . PRO B 1 66  ? 25.110  34.868 -3.030  1.00 39.00 ? 66   PRO B N   1 
ATOM   1546 C  CA  . PRO B 1 66  ? 26.047  35.885 -2.538  1.00 39.37 ? 66   PRO B CA  1 
ATOM   1547 C  C   . PRO B 1 66  ? 27.092  36.258 -3.582  1.00 43.18 ? 66   PRO B C   1 
ATOM   1548 O  O   . PRO B 1 66  ? 27.811  37.251 -3.445  1.00 44.49 ? 66   PRO B O   1 
ATOM   1549 C  CB  . PRO B 1 66  ? 26.740  35.206 -1.341  1.00 39.48 ? 66   PRO B CB  1 
ATOM   1550 C  CG  . PRO B 1 66  ? 26.604  33.745 -1.658  1.00 40.59 ? 66   PRO B CG  1 
ATOM   1551 C  CD  . PRO B 1 66  ? 25.222  33.629 -2.238  1.00 38.48 ? 66   PRO B CD  1 
ATOM   1552 N  N   . LEU B 1 67  ? 27.234  35.464 -4.655  1.00 39.38 ? 67   LEU B N   1 
ATOM   1553 C  CA  . LEU B 1 67  ? 28.316  35.763 -5.592  1.00 35.67 ? 67   LEU B CA  1 
ATOM   1554 C  C   . LEU B 1 67  ? 27.797  36.304 -6.918  1.00 41.51 ? 67   LEU B C   1 
ATOM   1555 O  O   . LEU B 1 67  ? 28.589  36.492 -7.849  1.00 45.19 ? 67   LEU B O   1 
ATOM   1556 C  CB  . LEU B 1 67  ? 29.140  34.495 -5.748  1.00 35.99 ? 67   LEU B CB  1 
ATOM   1557 C  CG  . LEU B 1 67  ? 30.123  34.127 -4.643  1.00 40.25 ? 67   LEU B CG  1 
ATOM   1558 C  CD1 . LEU B 1 67  ? 29.478  34.016 -3.286  1.00 48.95 ? 67   LEU B CD1 1 
ATOM   1559 C  CD2 . LEU B 1 67  ? 30.810  32.809 -4.983  1.00 49.98 ? 67   LEU B CD2 1 
ATOM   1560 N  N   . SER B 1 68  ? 26.503  36.560 -6.987  1.00 39.25 ? 68   SER B N   1 
ATOM   1561 C  CA  . SER B 1 68  ? 25.828  37.071 -8.167  1.00 38.68 ? 68   SER B CA  1 
ATOM   1562 C  C   . SER B 1 68  ? 26.287  36.300 -9.404  1.00 39.88 ? 68   SER B C   1 
ATOM   1563 O  O   . SER B 1 68  ? 26.776  36.897 -10.361 1.00 46.17 ? 68   SER B O   1 
ATOM   1564 C  CB  . SER B 1 68  ? 26.092  38.564 -8.354  1.00 43.32 ? 68   SER B CB  1 
ATOM   1565 O  OG  . SER B 1 68  ? 25.920  39.275 -7.145  1.00 48.19 ? 68   SER B OG  1 
ATOM   1566 N  N   . ARG B 1 69  ? 26.164  34.986 -9.341  1.00 40.80 ? 69   ARG B N   1 
ATOM   1567 C  CA  . ARG B 1 69  ? 26.431  34.029 -10.397 1.00 41.79 ? 69   ARG B CA  1 
ATOM   1568 C  C   . ARG B 1 69  ? 25.115  33.609 -11.036 1.00 47.69 ? 69   ARG B C   1 
ATOM   1569 O  O   . ARG B 1 69  ? 24.055  33.981 -10.511 1.00 46.54 ? 69   ARG B O   1 
ATOM   1570 C  CB  . ARG B 1 69  ? 27.176  32.817 -9.846  1.00 45.16 ? 69   ARG B CB  1 
ATOM   1571 C  CG  . ARG B 1 69  ? 28.649  33.064 -9.601  1.00 51.29 ? 69   ARG B CG  1 
ATOM   1572 C  CD  . ARG B 1 69  ? 29.403  31.776 -9.293  1.00 61.70 ? 69   ARG B CD  1 
ATOM   1573 N  NE  . ARG B 1 69  ? 30.822  32.018 -9.061  1.00 68.43 ? 69   ARG B NE  1 
ATOM   1574 C  CZ  . ARG B 1 69  ? 31.671  31.303 -8.341  1.00 74.10 ? 69   ARG B CZ  1 
ATOM   1575 N  NH1 . ARG B 1 69  ? 31.279  30.202 -7.706  1.00 87.35 ? 69   ARG B NH1 1 
ATOM   1576 N  NH2 . ARG B 1 69  ? 32.948  31.674 -8.239  1.00 75.82 ? 69   ARG B NH2 1 
ATOM   1577 N  N   . LYS B 1 70  ? 25.209  32.854 -12.140 1.00 46.25 ? 70   LYS B N   1 
ATOM   1578 C  CA  . LYS B 1 70  ? 23.961  32.416 -12.766 1.00 47.93 ? 70   LYS B CA  1 
ATOM   1579 C  C   . LYS B 1 70  ? 23.495  31.102 -12.172 1.00 42.11 ? 70   LYS B C   1 
ATOM   1580 O  O   . LYS B 1 70  ? 24.298  30.374 -11.564 1.00 43.43 ? 70   LYS B O   1 
ATOM   1581 C  CB  . LYS B 1 70  ? 24.174  32.311 -14.281 1.00 52.72 ? 70   LYS B CB  1 
ATOM   1582 C  CG  . LYS B 1 70  ? 24.788  33.553 -14.918 1.00 58.11 ? 70   LYS B CG  1 
ATOM   1583 C  CD  . LYS B 1 70  ? 24.690  33.519 -16.433 1.00 62.14 ? 70   LYS B CD  1 
ATOM   1584 C  CE  . LYS B 1 70  ? 26.021  33.635 -17.156 1.00 62.43 ? 70   LYS B CE  1 
ATOM   1585 N  NZ  . LYS B 1 70  ? 26.592  35.004 -17.118 1.00 63.69 ? 70   LYS B NZ  1 
ATOM   1586 N  N   . HIS B 1 71  ? 22.205  30.790 -12.342 1.00 40.85 ? 71   HIS B N   1 
ATOM   1587 C  CA  . HIS B 1 71  ? 21.682  29.527 -11.849 1.00 42.05 ? 71   HIS B CA  1 
ATOM   1588 C  C   . HIS B 1 71  ? 22.312  28.301 -12.491 1.00 41.28 ? 71   HIS B C   1 
ATOM   1589 O  O   . HIS B 1 71  ? 22.706  28.272 -13.643 1.00 47.01 ? 71   HIS B O   1 
ATOM   1590 C  CB  . HIS B 1 71  ? 20.161  29.460 -12.093 1.00 39.85 ? 71   HIS B CB  1 
ATOM   1591 C  CG  . HIS B 1 71  ? 19.619  28.177 -11.520 1.00 37.40 ? 71   HIS B CG  1 
ATOM   1592 N  ND1 . HIS B 1 71  ? 19.483  27.930 -10.180 1.00 34.33 ? 71   HIS B ND1 1 
ATOM   1593 C  CD2 . HIS B 1 71  ? 19.188  27.066 -12.172 1.00 37.42 ? 71   HIS B CD2 1 
ATOM   1594 C  CE1 . HIS B 1 71  ? 18.989  26.710 -10.031 1.00 33.08 ? 71   HIS B CE1 1 
ATOM   1595 N  NE2 . HIS B 1 71  ? 18.790  26.160 -11.205 1.00 32.97 ? 71   HIS B NE2 1 
ATOM   1596 N  N   . GLY B 1 72  ? 22.439  27.193 -11.760 1.00 43.34 ? 72   GLY B N   1 
ATOM   1597 C  CA  . GLY B 1 72  ? 22.942  25.974 -12.404 1.00 45.45 ? 72   GLY B CA  1 
ATOM   1598 C  C   . GLY B 1 72  ? 22.679  24.793 -11.478 1.00 41.18 ? 72   GLY B C   1 
ATOM   1599 O  O   . GLY B 1 72  ? 21.846  24.974 -10.594 1.00 40.04 ? 72   GLY B O   1 
ATOM   1600 N  N   . GLY B 1 73  ? 23.359  23.680 -11.678 1.00 40.55 ? 73   GLY B N   1 
ATOM   1601 C  CA  . GLY B 1 73  ? 23.267  22.505 -10.835 1.00 39.89 ? 73   GLY B CA  1 
ATOM   1602 C  C   . GLY B 1 73  ? 24.428  22.369 -9.876  1.00 39.52 ? 73   GLY B C   1 
ATOM   1603 O  O   . GLY B 1 73  ? 25.445  23.058 -10.063 1.00 41.91 ? 73   GLY B O   1 
ATOM   1604 N  N   . PRO B 1 74  ? 24.320  21.532 -8.857  1.00 37.31 ? 74   PRO B N   1 
ATOM   1605 C  CA  . PRO B 1 74  ? 25.342  21.493 -7.800  1.00 38.85 ? 74   PRO B CA  1 
ATOM   1606 C  C   . PRO B 1 74  ? 26.736  21.206 -8.337  1.00 44.49 ? 74   PRO B C   1 
ATOM   1607 O  O   . PRO B 1 74  ? 27.713  21.564 -7.666  1.00 52.05 ? 74   PRO B O   1 
ATOM   1608 C  CB  . PRO B 1 74  ? 24.856  20.394 -6.850  1.00 39.62 ? 74   PRO B CB  1 
ATOM   1609 C  CG  . PRO B 1 74  ? 23.848  19.617 -7.621  1.00 38.20 ? 74   PRO B CG  1 
ATOM   1610 C  CD  . PRO B 1 74  ? 23.201  20.615 -8.542  1.00 37.39 ? 74   PRO B CD  1 
ATOM   1611 N  N   . LYS B 1 75  ? 26.805  20.594 -9.513  1.00 48.32 ? 75   LYS B N   1 
ATOM   1612 C  CA  . LYS B 1 75  ? 28.040  20.332 -10.227 1.00 48.20 ? 75   LYS B CA  1 
ATOM   1613 C  C   . LYS B 1 75  ? 28.455  21.498 -11.108 1.00 49.40 ? 75   LYS B C   1 
ATOM   1614 O  O   . LYS B 1 75  ? 29.578  21.486 -11.630 1.00 58.27 ? 75   LYS B O   1 
ATOM   1615 C  CB  . LYS B 1 75  ? 27.883  19.056 -11.076 1.00 47.12 ? 75   LYS B CB  1 
ATOM   1616 C  CG  . LYS B 1 75  ? 26.923  18.032 -10.507 1.00 49.53 ? 75   LYS B CG  1 
ATOM   1617 C  CD  . LYS B 1 75  ? 27.669  16.788 -10.040 1.00 56.39 ? 75   LYS B CD  1 
ATOM   1618 C  CE  . LYS B 1 75  ? 27.785  15.766 -11.161 1.00 54.94 ? 75   LYS B CE  1 
ATOM   1619 N  NZ  . LYS B 1 75  ? 29.157  15.202 -11.309 1.00 60.82 ? 75   LYS B NZ  1 
ATOM   1620 N  N   . ASP B 1 76  ? 27.614  22.514 -11.310 1.00 51.56 ? 76   ASP B N   1 
ATOM   1621 C  CA  . ASP B 1 76  ? 28.028  23.604 -12.205 1.00 48.79 ? 76   ASP B CA  1 
ATOM   1622 C  C   . ASP B 1 76  ? 28.962  24.593 -11.530 1.00 49.02 ? 76   ASP B C   1 
ATOM   1623 O  O   . ASP B 1 76  ? 28.819  24.909 -10.356 1.00 50.35 ? 76   ASP B O   1 
ATOM   1624 C  CB  . ASP B 1 76  ? 26.804  24.371 -12.710 1.00 53.94 ? 76   ASP B CB  1 
ATOM   1625 C  CG  . ASP B 1 76  ? 26.109  23.672 -13.860 1.00 56.20 ? 76   ASP B CG  1 
ATOM   1626 O  OD1 . ASP B 1 76  ? 26.747  22.789 -14.465 1.00 63.10 ? 76   ASP B OD1 1 
ATOM   1627 O  OD2 . ASP B 1 76  ? 24.945  24.014 -14.159 1.00 53.29 ? 76   ASP B OD2 1 
ATOM   1628 N  N   . GLU B 1 77  ? 29.946  25.103 -12.274 1.00 51.86 ? 77   GLU B N   1 
ATOM   1629 C  CA  . GLU B 1 77  ? 30.807  26.161 -11.761 1.00 56.26 ? 77   GLU B CA  1 
ATOM   1630 C  C   . GLU B 1 77  ? 29.980  27.433 -11.580 1.00 53.20 ? 77   GLU B C   1 
ATOM   1631 O  O   . GLU B 1 77  ? 29.994  28.110 -10.562 1.00 61.62 ? 77   GLU B O   1 
ATOM   1632 C  CB  . GLU B 1 77  ? 31.957  26.501 -12.718 1.00 62.39 ? 77   GLU B CB  1 
ATOM   1633 C  CG  . GLU B 1 77  ? 32.862  27.604 -12.144 1.00 67.18 ? 77   GLU B CG  1 
ATOM   1634 C  CD  . GLU B 1 77  ? 33.480  27.060 -10.854 1.00 72.74 ? 77   GLU B CD  1 
ATOM   1635 O  OE1 . GLU B 1 77  ? 33.453  25.814 -10.702 1.00 74.15 ? 77   GLU B OE1 1 
ATOM   1636 O  OE2 . GLU B 1 77  ? 33.968  27.859 -10.030 1.00 70.23 ? 77   GLU B OE2 1 
ATOM   1637 N  N   . GLU B 1 78  ? 29.277  27.701 -12.688 1.00 52.19 ? 78   GLU B N   1 
ATOM   1638 C  CA  . GLU B 1 78  ? 28.366  28.841 -12.702 1.00 51.13 ? 78   GLU B CA  1 
ATOM   1639 C  C   . GLU B 1 78  ? 27.034  28.417 -12.107 1.00 46.98 ? 78   GLU B C   1 
ATOM   1640 O  O   . GLU B 1 78  ? 26.099  27.919 -12.727 1.00 50.15 ? 78   GLU B O   1 
ATOM   1641 C  CB  . GLU B 1 78  ? 28.270  29.390 -14.125 1.00 54.79 ? 78   GLU B CB  1 
ATOM   1642 C  CG  . GLU B 1 78  ? 27.089  30.337 -14.294 1.00 54.49 ? 78   GLU B CG  1 
ATOM   1643 C  CD  . GLU B 1 78  ? 27.497  31.798 -14.250 1.00 52.90 ? 78   GLU B CD  1 
ATOM   1644 O  OE1 . GLU B 1 78  ? 27.588  32.387 -13.157 1.00 55.32 ? 78   GLU B OE1 1 
ATOM   1645 O  OE2 . GLU B 1 78  ? 27.715  32.313 -15.367 1.00 56.17 ? 78   GLU B OE2 1 
ATOM   1646 N  N   . ARG B 1 79  ? 26.917  28.610 -10.786 1.00 44.84 ? 79   ARG B N   1 
ATOM   1647 C  CA  . ARG B 1 79  ? 25.779  28.279 -9.971  1.00 41.77 ? 79   ARG B CA  1 
ATOM   1648 C  C   . ARG B 1 79  ? 25.604  29.270 -8.827  1.00 41.23 ? 79   ARG B C   1 
ATOM   1649 O  O   . ARG B 1 79  ? 26.493  30.046 -8.463  1.00 36.99 ? 79   ARG B O   1 
ATOM   1650 C  CB  . ARG B 1 79  ? 25.913  26.874 -9.357  1.00 39.89 ? 79   ARG B CB  1 
ATOM   1651 C  CG  . ARG B 1 79  ? 27.101  26.746 -8.412  1.00 39.59 ? 79   ARG B CG  1 
ATOM   1652 C  CD  . ARG B 1 79  ? 27.024  25.421 -7.666  1.00 40.44 ? 79   ARG B CD  1 
ATOM   1653 N  NE  . ARG B 1 79  ? 26.177  25.617 -6.456  1.00 38.36 ? 79   ARG B NE  1 
ATOM   1654 C  CZ  . ARG B 1 79  ? 26.152  24.700 -5.497  1.00 37.03 ? 79   ARG B CZ  1 
ATOM   1655 N  NH1 . ARG B 1 79  ? 26.901  23.615 -5.673  1.00 35.79 ? 79   ARG B NH1 1 
ATOM   1656 N  NH2 . ARG B 1 79  ? 25.420  24.827 -4.396  1.00 38.02 ? 79   ARG B NH2 1 
ATOM   1657 N  N   . HIS B 1 80  ? 24.406  29.192 -8.252  1.00 37.50 ? 80   HIS B N   1 
ATOM   1658 C  CA  . HIS B 1 80  ? 24.136  29.923 -7.029  1.00 37.35 ? 80   HIS B CA  1 
ATOM   1659 C  C   . HIS B 1 80  ? 24.649  29.083 -5.869  1.00 36.97 ? 80   HIS B C   1 
ATOM   1660 O  O   . HIS B 1 80  ? 24.627  27.851 -5.978  1.00 37.17 ? 80   HIS B O   1 
ATOM   1661 C  CB  . HIS B 1 80  ? 22.641  30.161 -6.884  1.00 37.22 ? 80   HIS B CB  1 
ATOM   1662 C  CG  . HIS B 1 80  ? 22.074  30.995 -7.989  1.00 36.23 ? 80   HIS B CG  1 
ATOM   1663 N  ND1 . HIS B 1 80  ? 20.803  30.784 -8.461  1.00 37.27 ? 80   HIS B ND1 1 
ATOM   1664 C  CD2 . HIS B 1 80  ? 22.601  32.021 -8.704  1.00 36.64 ? 80   HIS B CD2 1 
ATOM   1665 C  CE1 . HIS B 1 80  ? 20.548  31.653 -9.421  1.00 37.63 ? 80   HIS B CE1 1 
ATOM   1666 N  NE2 . HIS B 1 80  ? 21.621  32.416 -9.590  1.00 39.04 ? 80   HIS B NE2 1 
ATOM   1667 N  N   . VAL B 1 81  ? 25.082  29.706 -4.782  1.00 36.81 ? 81   VAL B N   1 
ATOM   1668 C  CA  . VAL B 1 81  ? 25.427  28.875 -3.625  1.00 34.84 ? 81   VAL B CA  1 
ATOM   1669 C  C   . VAL B 1 81  ? 24.277  27.957 -3.213  1.00 31.90 ? 81   VAL B C   1 
ATOM   1670 O  O   . VAL B 1 81  ? 24.485  26.822 -2.779  1.00 29.44 ? 81   VAL B O   1 
ATOM   1671 C  CB  . VAL B 1 81  ? 25.822  29.748 -2.429  1.00 36.20 ? 81   VAL B CB  1 
ATOM   1672 C  CG1 . VAL B 1 81  ? 25.986  28.872 -1.202  1.00 37.39 ? 81   VAL B CG1 1 
ATOM   1673 C  CG2 . VAL B 1 81  ? 27.109  30.498 -2.765  1.00 35.05 ? 81   VAL B CG2 1 
ATOM   1674 N  N   . GLY B 1 82  ? 23.045  28.441 -3.370  1.00 29.12 ? 82   GLY B N   1 
ATOM   1675 C  CA  . GLY B 1 82  ? 21.877  27.691 -2.908  1.00 29.77 ? 82   GLY B CA  1 
ATOM   1676 C  C   . GLY B 1 82  ? 21.421  26.623 -3.885  1.00 31.52 ? 82   GLY B C   1 
ATOM   1677 O  O   . GLY B 1 82  ? 20.385  25.996 -3.645  1.00 30.56 ? 82   GLY B O   1 
ATOM   1678 N  N   . ASP B 1 83  ? 22.131  26.379 -4.970  1.00 32.04 ? 83   ASP B N   1 
ATOM   1679 C  CA  . ASP B 1 83  ? 21.702  25.425 -6.012  1.00 26.99 ? 83   ASP B CA  1 
ATOM   1680 C  C   . ASP B 1 83  ? 22.059  23.995 -5.680  1.00 29.56 ? 83   ASP B C   1 
ATOM   1681 O  O   . ASP B 1 83  ? 23.125  23.446 -6.022  1.00 31.09 ? 83   ASP B O   1 
ATOM   1682 C  CB  . ASP B 1 83  ? 22.307  25.926 -7.336  1.00 28.12 ? 83   ASP B CB  1 
ATOM   1683 C  CG  . ASP B 1 83  ? 21.618  27.146 -7.893  1.00 30.06 ? 83   ASP B CG  1 
ATOM   1684 O  OD1 . ASP B 1 83  ? 20.538  27.635 -7.508  1.00 31.77 ? 83   ASP B OD1 1 
ATOM   1685 O  OD2 . ASP B 1 83  ? 22.191  27.707 -8.860  1.00 33.48 ? 83   ASP B OD2 1 
ATOM   1686 N  N   . LEU B 1 84  ? 21.164  23.269 -4.995  1.00 27.45 ? 84   LEU B N   1 
ATOM   1687 C  CA  . LEU B 1 84  ? 21.469  21.878 -4.645  1.00 29.34 ? 84   LEU B CA  1 
ATOM   1688 C  C   . LEU B 1 84  ? 20.767  20.916 -5.587  1.00 30.17 ? 84   LEU B C   1 
ATOM   1689 O  O   . LEU B 1 84  ? 20.617  19.719 -5.279  1.00 32.23 ? 84   LEU B O   1 
ATOM   1690 C  CB  . LEU B 1 84  ? 21.099  21.588 -3.177  1.00 29.19 ? 84   LEU B CB  1 
ATOM   1691 C  CG  . LEU B 1 84  ? 21.897  22.412 -2.144  1.00 29.09 ? 84   LEU B CG  1 
ATOM   1692 C  CD1 . LEU B 1 84  ? 21.294  22.212 -0.757  1.00 28.25 ? 84   LEU B CD1 1 
ATOM   1693 C  CD2 . LEU B 1 84  ? 23.370  22.064 -2.158  1.00 28.19 ? 84   LEU B CD2 1 
ATOM   1694 N  N   . GLY B 1 85  ? 20.321  21.379 -6.750  1.00 29.36 ? 85   GLY B N   1 
ATOM   1695 C  CA  . GLY B 1 85  ? 19.850  20.397 -7.729  1.00 29.36 ? 85   GLY B CA  1 
ATOM   1696 C  C   . GLY B 1 85  ? 18.459  19.889 -7.483  1.00 29.27 ? 85   GLY B C   1 
ATOM   1697 O  O   . GLY B 1 85  ? 17.550  20.692 -7.230  1.00 28.01 ? 85   GLY B O   1 
ATOM   1698 N  N   . ASN B 1 86  ? 18.283  18.575 -7.574  1.00 27.70 ? 86   ASN B N   1 
ATOM   1699 C  CA  . ASN B 1 86  ? 17.041  17.881 -7.355  1.00 23.89 ? 86   ASN B CA  1 
ATOM   1700 C  C   . ASN B 1 86  ? 17.184  16.748 -6.341  1.00 24.94 ? 86   ASN B C   1 
ATOM   1701 O  O   . ASN B 1 86  ? 18.215  16.098 -6.149  1.00 29.80 ? 86   ASN B O   1 
ATOM   1702 C  CB  . ASN B 1 86  ? 16.507  17.273 -8.674  1.00 26.83 ? 86   ASN B CB  1 
ATOM   1703 C  CG  . ASN B 1 86  ? 16.210  18.345 -9.716  1.00 27.19 ? 86   ASN B CG  1 
ATOM   1704 O  OD1 . ASN B 1 86  ? 15.232  19.081 -9.575  1.00 27.23 ? 86   ASN B OD1 1 
ATOM   1705 N  ND2 . ASN B 1 86  ? 17.071  18.402 -10.730 1.00 29.37 ? 86   ASN B ND2 1 
ATOM   1706 N  N   . VAL B 1 87  ? 16.082  16.510 -5.666  1.00 24.51 ? 87   VAL B N   1 
ATOM   1707 C  CA  . VAL B 1 87  ? 15.829  15.297 -4.903  1.00 22.07 ? 87   VAL B CA  1 
ATOM   1708 C  C   . VAL B 1 87  ? 14.871  14.463 -5.730  1.00 21.33 ? 87   VAL B C   1 
ATOM   1709 O  O   . VAL B 1 87  ? 14.075  14.969 -6.533  1.00 23.24 ? 87   VAL B O   1 
ATOM   1710 C  CB  . VAL B 1 87  ? 15.295  15.619 -3.502  1.00 19.90 ? 87   VAL B CB  1 
ATOM   1711 C  CG1 . VAL B 1 87  ? 16.345  16.468 -2.792  1.00 24.57 ? 87   VAL B CG1 1 
ATOM   1712 C  CG2 . VAL B 1 87  ? 13.967  16.357 -3.543  1.00 21.08 ? 87   VAL B CG2 1 
ATOM   1713 N  N   . THR B 1 88  ? 14.952  13.162 -5.534  1.00 23.66 ? 88   THR B N   1 
ATOM   1714 C  CA  . THR B 1 88  ? 14.135  12.230 -6.303  1.00 23.67 ? 88   THR B CA  1 
ATOM   1715 C  C   . THR B 1 88  ? 13.161  11.522 -5.376  1.00 22.21 ? 88   THR B C   1 
ATOM   1716 O  O   . THR B 1 88  ? 13.613  10.800 -4.483  1.00 22.88 ? 88   THR B O   1 
ATOM   1717 C  CB  . THR B 1 88  ? 15.024  11.191 -7.009  1.00 27.18 ? 88   THR B CB  1 
ATOM   1718 O  OG1 . THR B 1 88  ? 15.759  11.828 -8.063  1.00 33.67 ? 88   THR B OG1 1 
ATOM   1719 C  CG2 . THR B 1 88  ? 14.186  10.090 -7.649  1.00 25.27 ? 88   THR B CG2 1 
ATOM   1720 N  N   . ALA B 1 89  ? 11.872  11.745 -5.593  1.00 18.68 ? 89   ALA B N   1 
ATOM   1721 C  CA  . ALA B 1 89  ? 10.880  10.984 -4.840  1.00 20.58 ? 89   ALA B CA  1 
ATOM   1722 C  C   . ALA B 1 89  ? 10.593  9.628  -5.487  1.00 20.46 ? 89   ALA B C   1 
ATOM   1723 O  O   . ALA B 1 89  ? 10.492  9.544  -6.729  1.00 22.56 ? 89   ALA B O   1 
ATOM   1724 C  CB  . ALA B 1 89  ? 9.619   11.811 -4.731  1.00 20.84 ? 89   ALA B CB  1 
ATOM   1725 N  N   . ASP B 1 90  ? 10.440  8.589  -4.663  1.00 22.06 ? 90   ASP B N   1 
ATOM   1726 C  CA  . ASP B 1 90  ? 10.193  7.233  -5.146  1.00 24.52 ? 90   ASP B CA  1 
ATOM   1727 C  C   . ASP B 1 90  ? 8.724   7.061  -5.475  1.00 27.28 ? 90   ASP B C   1 
ATOM   1728 O  O   . ASP B 1 90  ? 8.003   8.061  -5.421  1.00 25.02 ? 90   ASP B O   1 
ATOM   1729 C  CB  . ASP B 1 90  ? 10.685  6.221  -4.122  1.00 26.92 ? 90   ASP B CB  1 
ATOM   1730 C  CG  . ASP B 1 90  ? 9.920   6.188  -2.816  1.00 26.05 ? 90   ASP B CG  1 
ATOM   1731 O  OD1 . ASP B 1 90  ? 8.811   6.757  -2.690  1.00 26.11 ? 90   ASP B OD1 1 
ATOM   1732 O  OD2 . ASP B 1 90  ? 10.479  5.565  -1.878  1.00 26.92 ? 90   ASP B OD2 1 
ATOM   1733 N  N   . LYS B 1 91  ? 8.249   5.864  -5.841  1.00 31.14 ? 91   LYS B N   1 
ATOM   1734 C  CA  . LYS B 1 91  ? 6.864   5.689  -6.276  1.00 30.93 ? 91   LYS B CA  1 
ATOM   1735 C  C   . LYS B 1 91  ? 5.880   5.904  -5.132  1.00 29.49 ? 91   LYS B C   1 
ATOM   1736 O  O   . LYS B 1 91  ? 4.684   6.102  -5.374  1.00 37.48 ? 91   LYS B O   1 
ATOM   1737 C  CB  . LYS B 1 91  ? 6.710   4.314  -6.922  1.00 34.23 ? 91   LYS B CB  1 
ATOM   1738 C  CG  . LYS B 1 91  ? 7.569   3.232  -6.278  1.00 40.98 ? 91   LYS B CG  1 
ATOM   1739 C  CD  . LYS B 1 91  ? 7.285   1.836  -6.829  1.00 50.96 ? 91   LYS B CD  1 
ATOM   1740 C  CE  . LYS B 1 91  ? 7.342   0.801  -5.715  1.00 56.75 ? 91   LYS B CE  1 
ATOM   1741 N  NZ  . LYS B 1 91  ? 6.039   0.084  -5.536  1.00 78.12 ? 91   LYS B NZ  1 
ATOM   1742 N  N   . ASP B 1 92  ? 6.388   5.908  -3.896  1.00 27.21 ? 92   ASP B N   1 
ATOM   1743 C  CA  . ASP B 1 92  ? 5.619   6.210  -2.706  1.00 28.02 ? 92   ASP B CA  1 
ATOM   1744 C  C   . ASP B 1 92  ? 5.700   7.672  -2.294  1.00 25.71 ? 92   ASP B C   1 
ATOM   1745 O  O   . ASP B 1 92  ? 5.127   8.010  -1.258  1.00 28.45 ? 92   ASP B O   1 
ATOM   1746 C  CB  . ASP B 1 92  ? 6.103   5.330  -1.537  1.00 31.23 ? 92   ASP B CB  1 
ATOM   1747 C  CG  . ASP B 1 92  ? 5.998   3.875  -1.975  1.00 38.92 ? 92   ASP B CG  1 
ATOM   1748 O  OD1 . ASP B 1 92  ? 4.882   3.513  -2.422  1.00 49.07 ? 92   ASP B OD1 1 
ATOM   1749 O  OD2 . ASP B 1 92  ? 6.972   3.096  -1.895  1.00 49.96 ? 92   ASP B OD2 1 
ATOM   1750 N  N   . GLY B 1 93  ? 6.347   8.538  -3.068  1.00 23.57 ? 93   GLY B N   1 
ATOM   1751 C  CA  . GLY B 1 93  ? 6.308   9.967  -2.757  1.00 21.61 ? 93   GLY B CA  1 
ATOM   1752 C  C   . GLY B 1 93  ? 7.385   10.359 -1.769  1.00 19.01 ? 93   GLY B C   1 
ATOM   1753 O  O   . GLY B 1 93  ? 7.327   11.492 -1.284  1.00 20.57 ? 93   GLY B O   1 
ATOM   1754 N  N   . VAL B 1 94  ? 8.328   9.464  -1.487  1.00 20.00 ? 94   VAL B N   1 
ATOM   1755 C  CA  . VAL B 1 94  ? 9.387   9.725  -0.511  1.00 22.80 ? 94   VAL B CA  1 
ATOM   1756 C  C   . VAL B 1 94  ? 10.711  9.993  -1.203  1.00 20.06 ? 94   VAL B C   1 
ATOM   1757 O  O   . VAL B 1 94  ? 11.169  9.193  -2.033  1.00 24.50 ? 94   VAL B O   1 
ATOM   1758 C  CB  . VAL B 1 94  ? 9.561   8.539  0.463   1.00 23.51 ? 94   VAL B CB  1 
ATOM   1759 C  CG1 . VAL B 1 94  ? 10.649  8.812  1.504   1.00 24.54 ? 94   VAL B CG1 1 
ATOM   1760 C  CG2 . VAL B 1 94  ? 8.232   8.258  1.164   1.00 22.82 ? 94   VAL B CG2 1 
ATOM   1761 N  N   . ALA B 1 95  ? 11.337  11.111 -0.872  1.00 20.68 ? 95   ALA B N   1 
ATOM   1762 C  CA  . ALA B 1 95  ? 12.682  11.443 -1.327  1.00 21.56 ? 95   ALA B CA  1 
ATOM   1763 C  C   . ALA B 1 95  ? 13.640  11.290 -0.155  1.00 19.76 ? 95   ALA B C   1 
ATOM   1764 O  O   . ALA B 1 95  ? 13.738  12.083 0.802   1.00 22.90 ? 95   ALA B O   1 
ATOM   1765 C  CB  . ALA B 1 95  ? 12.750  12.836 -1.928  1.00 19.41 ? 95   ALA B CB  1 
ATOM   1766 N  N   . ASP B 1 96  ? 14.374  10.191 -0.187  1.00 23.61 ? 96   ASP B N   1 
ATOM   1767 C  CA  . ASP B 1 96  ? 15.434  9.977  0.783   1.00 22.65 ? 96   ASP B CA  1 
ATOM   1768 C  C   . ASP B 1 96  ? 16.631  10.731 0.210   1.00 23.02 ? 96   ASP B C   1 
ATOM   1769 O  O   . ASP B 1 96  ? 17.048  10.545 -0.927  1.00 28.01 ? 96   ASP B O   1 
ATOM   1770 C  CB  . ASP B 1 96  ? 15.680  8.493  0.994   1.00 27.43 ? 96   ASP B CB  1 
ATOM   1771 C  CG  . ASP B 1 96  ? 14.743  7.848  1.992   1.00 34.51 ? 96   ASP B CG  1 
ATOM   1772 O  OD1 . ASP B 1 96  ? 13.991  8.482  2.754   1.00 31.21 ? 96   ASP B OD1 1 
ATOM   1773 O  OD2 . ASP B 1 96  ? 14.743  6.603  2.059   1.00 49.39 ? 96   ASP B OD2 1 
ATOM   1774 N  N   . VAL B 1 97  ? 17.187  11.648 0.985   1.00 25.22 ? 97   VAL B N   1 
ATOM   1775 C  CA  . VAL B 1 97  ? 18.231  12.536 0.471   1.00 25.48 ? 97   VAL B CA  1 
ATOM   1776 C  C   . VAL B 1 97  ? 19.565  12.194 1.098   1.00 28.19 ? 97   VAL B C   1 
ATOM   1777 O  O   . VAL B 1 97  ? 19.676  11.992 2.297   1.00 28.14 ? 97   VAL B O   1 
ATOM   1778 C  CB  . VAL B 1 97  ? 17.882  13.996 0.790   1.00 25.37 ? 97   VAL B CB  1 
ATOM   1779 C  CG1 . VAL B 1 97  ? 18.994  14.939 0.341   1.00 30.59 ? 97   VAL B CG1 1 
ATOM   1780 C  CG2 . VAL B 1 97  ? 16.557  14.394 0.141   1.00 28.09 ? 97   VAL B CG2 1 
ATOM   1781 N  N   . SER B 1 98  ? 20.597  12.112 0.262   1.00 30.98 ? 98   SER B N   1 
ATOM   1782 C  CA  . SER B 1 98  ? 21.927  11.949 0.807   1.00 32.40 ? 98   SER B CA  1 
ATOM   1783 C  C   . SER B 1 98  ? 22.907  12.517 -0.211  1.00 36.02 ? 98   SER B C   1 
ATOM   1784 O  O   . SER B 1 98  ? 23.260  11.892 -1.213  1.00 47.09 ? 98   SER B O   1 
ATOM   1785 C  CB  . SER B 1 98  ? 22.341  10.523 1.156   1.00 37.25 ? 98   SER B CB  1 
ATOM   1786 O  OG  . SER B 1 98  ? 23.606  10.547 1.815   1.00 51.25 ? 98   SER B OG  1 
ATOM   1787 N  N   . ILE B 1 99  ? 23.345  13.740 0.097   1.00 35.88 ? 99   ILE B N   1 
ATOM   1788 C  CA  . ILE B 1 99  ? 24.388  14.245 -0.794  1.00 35.68 ? 99   ILE B CA  1 
ATOM   1789 C  C   . ILE B 1 99  ? 25.494  14.870 0.057   1.00 35.84 ? 99   ILE B C   1 
ATOM   1790 O  O   . ILE B 1 99  ? 25.393  14.890 1.284   1.00 33.62 ? 99   ILE B O   1 
ATOM   1791 C  CB  . ILE B 1 99  ? 23.868  15.281 -1.798  1.00 36.45 ? 99   ILE B CB  1 
ATOM   1792 C  CG1 . ILE B 1 99  ? 23.215  16.485 -1.114  1.00 36.26 ? 99   ILE B CG1 1 
ATOM   1793 C  CG2 . ILE B 1 99  ? 22.968  14.601 -2.821  1.00 46.68 ? 99   ILE B CG2 1 
ATOM   1794 C  CD1 . ILE B 1 99  ? 22.171  17.180 -1.941  1.00 41.55 ? 99   ILE B CD1 1 
ATOM   1795 N  N   . GLU B 1 100 ? 26.457  15.345 -0.709  1.00 37.42 ? 100  GLU B N   1 
ATOM   1796 C  CA  . GLU B 1 100 ? 27.597  16.140 -0.284  1.00 37.86 ? 100  GLU B CA  1 
ATOM   1797 C  C   . GLU B 1 100 ? 27.739  17.363 -1.192  1.00 39.65 ? 100  GLU B C   1 
ATOM   1798 O  O   . GLU B 1 100 ? 27.614  17.265 -2.418  1.00 39.60 ? 100  GLU B O   1 
ATOM   1799 C  CB  . GLU B 1 100 ? 28.883  15.312 -0.284  1.00 44.38 ? 100  GLU B CB  1 
ATOM   1800 C  CG  . GLU B 1 100 ? 29.989  15.907 0.587   1.00 46.49 ? 100  GLU B CG  1 
ATOM   1801 C  CD  . GLU B 1 100 ? 30.949  14.802 1.008   1.00 52.35 ? 100  GLU B CD  1 
ATOM   1802 O  OE1 . GLU B 1 100 ? 30.452  13.680 1.258   1.00 60.37 ? 100  GLU B OE1 1 
ATOM   1803 O  OE2 . GLU B 1 100 ? 32.162  15.066 1.074   1.00 65.80 ? 100  GLU B OE2 1 
ATOM   1804 N  N   . ASP B 1 101 ? 27.993  18.503 -0.557  1.00 38.44 ? 101  ASP B N   1 
ATOM   1805 C  CA  . ASP B 1 101 ? 28.142  19.741 -1.297  1.00 37.89 ? 101  ASP B CA  1 
ATOM   1806 C  C   . ASP B 1 101 ? 29.265  20.586 -0.716  1.00 39.82 ? 101  ASP B C   1 
ATOM   1807 O  O   . ASP B 1 101 ? 29.369  20.659 0.503   1.00 38.90 ? 101  ASP B O   1 
ATOM   1808 C  CB  . ASP B 1 101 ? 26.860  20.585 -1.258  1.00 40.24 ? 101  ASP B CB  1 
ATOM   1809 C  CG  . ASP B 1 101 ? 26.946  21.612 -2.375  1.00 40.65 ? 101  ASP B CG  1 
ATOM   1810 O  OD1 . ASP B 1 101 ? 26.893  21.163 -3.543  1.00 47.85 ? 101  ASP B OD1 1 
ATOM   1811 O  OD2 . ASP B 1 101 ? 27.080  22.818 -2.115  1.00 44.92 ? 101  ASP B OD2 1 
ATOM   1812 N  N   . SER B 1 102 ? 30.065  21.190 -1.581  1.00 40.43 ? 102  SER B N   1 
ATOM   1813 C  CA  . SER B 1 102 ? 31.207  21.975 -1.100  1.00 41.30 ? 102  SER B CA  1 
ATOM   1814 C  C   . SER B 1 102 ? 31.020  23.472 -1.256  1.00 40.84 ? 102  SER B C   1 
ATOM   1815 O  O   . SER B 1 102 ? 31.909  24.228 -0.851  1.00 48.24 ? 102  SER B O   1 
ATOM   1816 C  CB  . SER B 1 102 ? 32.473  21.533 -1.854  1.00 46.14 ? 102  SER B CB  1 
ATOM   1817 O  OG  . SER B 1 102 ? 33.173  20.624 -1.011  1.00 57.85 ? 102  SER B OG  1 
ATOM   1818 N  N   . VAL B 1 103 ? 29.904  23.872 -1.851  1.00 38.25 ? 103  VAL B N   1 
ATOM   1819 C  CA  . VAL B 1 103 ? 29.671  25.303 -2.062  1.00 36.51 ? 103  VAL B CA  1 
ATOM   1820 C  C   . VAL B 1 103 ? 28.912  25.814 -0.861  1.00 34.93 ? 103  VAL B C   1 
ATOM   1821 O  O   . VAL B 1 103 ? 29.288  26.832 -0.251  1.00 38.80 ? 103  VAL B O   1 
ATOM   1822 C  CB  . VAL B 1 103 ? 28.989  25.598 -3.403  1.00 40.20 ? 103  VAL B CB  1 
ATOM   1823 C  CG1 . VAL B 1 103 ? 28.733  27.095 -3.523  1.00 41.16 ? 103  VAL B CG1 1 
ATOM   1824 C  CG2 . VAL B 1 103 ? 29.849  25.109 -4.567  1.00 42.17 ? 103  VAL B CG2 1 
ATOM   1825 N  N   . ILE B 1 104 ? 27.850  25.149 -0.406  1.00 35.58 ? 104  ILE B N   1 
ATOM   1826 C  CA  . ILE B 1 104 ? 27.306  25.615 0.867   1.00 34.53 ? 104  ILE B CA  1 
ATOM   1827 C  C   . ILE B 1 104 ? 28.240  25.412 2.046   1.00 31.81 ? 104  ILE B C   1 
ATOM   1828 O  O   . ILE B 1 104 ? 29.147  24.590 1.990   1.00 36.39 ? 104  ILE B O   1 
ATOM   1829 C  CB  . ILE B 1 104 ? 26.008  24.833 1.177   1.00 33.94 ? 104  ILE B CB  1 
ATOM   1830 C  CG1 . ILE B 1 104 ? 26.247  23.335 1.383   1.00 33.51 ? 104  ILE B CG1 1 
ATOM   1831 C  CG2 . ILE B 1 104 ? 24.970  25.133 0.111   1.00 36.47 ? 104  ILE B CG2 1 
ATOM   1832 C  CD1 . ILE B 1 104 ? 25.008  22.525 1.751   1.00 30.93 ? 104  ILE B CD1 1 
ATOM   1833 N  N   . SER B 1 105 ? 27.983  26.148 3.148   1.00 27.95 ? 105  SER B N   1 
ATOM   1834 C  CA  . SER B 1 105 ? 28.790  25.994 4.338   1.00 30.45 ? 105  SER B CA  1 
ATOM   1835 C  C   . SER B 1 105 ? 27.922  26.243 5.559   1.00 28.47 ? 105  SER B C   1 
ATOM   1836 O  O   . SER B 1 105 ? 26.888  26.897 5.424   1.00 31.10 ? 105  SER B O   1 
ATOM   1837 C  CB  . SER B 1 105 ? 29.962  26.985 4.360   1.00 32.91 ? 105  SER B CB  1 
ATOM   1838 O  OG  . SER B 1 105 ? 30.870  26.719 5.411   1.00 36.41 ? 105  SER B OG  1 
ATOM   1839 N  N   . LEU B 1 106 ? 28.359  25.764 6.707   1.00 30.63 ? 106  LEU B N   1 
ATOM   1840 C  CA  . LEU B 1 106 ? 27.654  26.147 7.922   1.00 31.94 ? 106  LEU B CA  1 
ATOM   1841 C  C   . LEU B 1 106 ? 28.408  27.324 8.570   1.00 38.51 ? 106  LEU B C   1 
ATOM   1842 O  O   . LEU B 1 106 ? 27.967  27.712 9.662   1.00 35.92 ? 106  LEU B O   1 
ATOM   1843 C  CB  . LEU B 1 106 ? 27.457  24.929 8.828   1.00 29.04 ? 106  LEU B CB  1 
ATOM   1844 C  CG  . LEU B 1 106 ? 26.762  23.716 8.213   1.00 27.85 ? 106  LEU B CG  1 
ATOM   1845 C  CD1 . LEU B 1 106 ? 26.466  22.617 9.221   1.00 32.05 ? 106  LEU B CD1 1 
ATOM   1846 C  CD2 . LEU B 1 106 ? 25.460  24.135 7.518   1.00 26.33 ? 106  LEU B CD2 1 
ATOM   1847 N  N   . SER B 1 107 ? 29.459  27.897 7.989   1.00 38.57 ? 107  SER B N   1 
ATOM   1848 C  CA  . SER B 1 107 ? 30.198  29.094 8.381   1.00 40.85 ? 107  SER B CA  1 
ATOM   1849 C  C   . SER B 1 107 ? 30.440  30.076 7.227   1.00 40.09 ? 107  SER B C   1 
ATOM   1850 O  O   . SER B 1 107 ? 30.274  29.813 6.043   1.00 42.46 ? 107  SER B O   1 
ATOM   1851 C  CB  . SER B 1 107 ? 31.621  28.865 8.899   1.00 46.98 ? 107  SER B CB  1 
ATOM   1852 O  OG  . SER B 1 107 ? 31.829  27.678 9.614   1.00 64.05 ? 107  SER B OG  1 
ATOM   1853 N  N   . GLY B 1 108 ? 30.905  31.267 7.581   1.00 40.53 ? 108  GLY B N   1 
ATOM   1854 C  CA  . GLY B 1 108 ? 31.334  32.310 6.705   1.00 42.73 ? 108  GLY B CA  1 
ATOM   1855 C  C   . GLY B 1 108 ? 30.456  32.807 5.600   1.00 44.10 ? 108  GLY B C   1 
ATOM   1856 O  O   . GLY B 1 108 ? 29.232  32.850 5.670   1.00 45.77 ? 108  GLY B O   1 
ATOM   1857 N  N   . ASP B 1 109 ? 31.066  33.241 4.489   1.00 48.92 ? 109  ASP B N   1 
ATOM   1858 C  CA  . ASP B 1 109 ? 30.266  33.955 3.494   1.00 50.09 ? 109  ASP B CA  1 
ATOM   1859 C  C   . ASP B 1 109 ? 29.255  33.028 2.829   1.00 49.32 ? 109  ASP B C   1 
ATOM   1860 O  O   . ASP B 1 109 ? 28.205  33.541 2.430   1.00 49.56 ? 109  ASP B O   1 
ATOM   1861 C  CB  . ASP B 1 109 ? 31.122  34.650 2.435   1.00 57.14 ? 109  ASP B CB  1 
ATOM   1862 C  CG  . ASP B 1 109 ? 32.142  33.761 1.765   1.00 67.05 ? 109  ASP B CG  1 
ATOM   1863 O  OD1 . ASP B 1 109 ? 32.575  32.757 2.369   1.00 81.75 ? 109  ASP B OD1 1 
ATOM   1864 O  OD2 . ASP B 1 109 ? 32.532  34.073 0.613   1.00 81.05 ? 109  ASP B OD2 1 
ATOM   1865 N  N   . HIS B 1 110 ? 29.588  31.738 2.740   1.00 41.41 ? 110  HIS B N   1 
ATOM   1866 C  CA  . HIS B 1 110 ? 28.631  30.819 2.119   1.00 39.92 ? 110  HIS B CA  1 
ATOM   1867 C  C   . HIS B 1 110 ? 27.622  30.274 3.112   1.00 36.58 ? 110  HIS B C   1 
ATOM   1868 O  O   . HIS B 1 110 ? 26.867  29.352 2.769   1.00 33.15 ? 110  HIS B O   1 
ATOM   1869 C  CB  . HIS B 1 110 ? 29.323  29.607 1.463   1.00 40.80 ? 110  HIS B CB  1 
ATOM   1870 C  CG  . HIS B 1 110 ? 30.160  30.048 0.301   1.00 41.86 ? 110  HIS B CG  1 
ATOM   1871 N  ND1 . HIS B 1 110 ? 30.817  29.187 -0.525  1.00 44.22 ? 110  HIS B ND1 1 
ATOM   1872 C  CD2 . HIS B 1 110 ? 30.426  31.295 -0.147  1.00 42.30 ? 110  HIS B CD2 1 
ATOM   1873 C  CE1 . HIS B 1 110 ? 31.469  29.877 -1.452  1.00 43.07 ? 110  HIS B CE1 1 
ATOM   1874 N  NE2 . HIS B 1 110 ? 31.244  31.168 -1.243  1.00 42.79 ? 110  HIS B NE2 1 
HETATM 1875 N  N   . CSX B 1 111 ? 27.623  30.827 4.311   1.00 36.53 ? 111  CSX B N   1 
HETATM 1876 C  CA  . CSX B 1 111 ? 26.789  30.266 5.376   1.00 32.24 ? 111  CSX B CA  1 
HETATM 1877 C  CB  . CSX B 1 111 ? 27.048  31.101 6.651   1.00 35.88 ? 111  CSX B CB  1 
HETATM 1878 S  SG  . CSX B 1 111 ? 26.165  30.308 8.044   1.00 29.69 ? 111  CSX B SG  1 
HETATM 1879 C  C   . CSX B 1 111 ? 25.301  30.241 5.096   1.00 29.07 ? 111  CSX B C   1 
HETATM 1880 O  O   . CSX B 1 111 ? 24.696  31.220 4.655   1.00 29.14 ? 111  CSX B O   1 
HETATM 1881 O  OD  . CSX B 1 111 ? 26.358  31.269 9.168   1.00 47.60 ? 111  CSX B OD  1 
ATOM   1882 N  N   . ILE B 1 112 ? 24.694  29.068 5.385   1.00 26.46 ? 112  ILE B N   1 
ATOM   1883 C  CA  . ILE B 1 112 ? 23.264  28.918 5.091   1.00 22.79 ? 112  ILE B CA  1 
ATOM   1884 C  C   . ILE B 1 112 ? 22.398  28.886 6.333   1.00 21.35 ? 112  ILE B C   1 
ATOM   1885 O  O   . ILE B 1 112 ? 21.165  28.793 6.222   1.00 20.73 ? 112  ILE B O   1 
ATOM   1886 C  CB  . ILE B 1 112 ? 23.056  27.639 4.239   1.00 23.95 ? 112  ILE B CB  1 
ATOM   1887 C  CG1 . ILE B 1 112 ? 23.482  26.340 4.898   1.00 26.28 ? 112  ILE B CG1 1 
ATOM   1888 C  CG2 . ILE B 1 112 ? 23.743  27.870 2.897   1.00 26.95 ? 112  ILE B CG2 1 
ATOM   1889 C  CD1 . ILE B 1 112 ? 23.060  25.068 4.149   1.00 26.17 ? 112  ILE B CD1 1 
ATOM   1890 N  N   . ILE B 1 113 ? 23.060  28.994 7.493   1.00 20.85 ? 113  ILE B N   1 
ATOM   1891 C  CA  . ILE B 1 113 ? 22.322  28.986 8.747   1.00 20.28 ? 113  ILE B CA  1 
ATOM   1892 C  C   . ILE B 1 113 ? 21.400  30.188 8.747   1.00 17.89 ? 113  ILE B C   1 
ATOM   1893 O  O   . ILE B 1 113 ? 21.823  31.282 8.401   1.00 20.56 ? 113  ILE B O   1 
ATOM   1894 C  CB  . ILE B 1 113 ? 23.244  29.073 9.981   1.00 20.60 ? 113  ILE B CB  1 
ATOM   1895 C  CG1 . ILE B 1 113 ? 24.275  27.968 10.109  1.00 24.25 ? 113  ILE B CG1 1 
ATOM   1896 C  CG2 . ILE B 1 113 ? 22.399  29.160 11.242  1.00 22.47 ? 113  ILE B CG2 1 
ATOM   1897 C  CD1 . ILE B 1 113 ? 23.819  26.612 10.539  1.00 37.57 ? 113  ILE B CD1 1 
ATOM   1898 N  N   . GLY B 1 114 ? 20.136  30.043 9.132   1.00 16.44 ? 114  GLY B N   1 
ATOM   1899 C  CA  . GLY B 1 114 ? 19.277  31.210 9.149   1.00 16.65 ? 114  GLY B CA  1 
ATOM   1900 C  C   . GLY B 1 114 ? 18.647  31.498 7.799   1.00 17.85 ? 114  GLY B C   1 
ATOM   1901 O  O   . GLY B 1 114 ? 17.876  32.453 7.702   1.00 17.17 ? 114  GLY B O   1 
ATOM   1902 N  N   . ARG B 1 115 ? 18.933  30.685 6.775   1.00 17.70 ? 115  ARG B N   1 
ATOM   1903 C  CA  . ARG B 1 115 ? 18.267  30.889 5.464   1.00 18.08 ? 115  ARG B CA  1 
ATOM   1904 C  C   . ARG B 1 115 ? 17.202  29.822 5.319   1.00 15.73 ? 115  ARG B C   1 
ATOM   1905 O  O   . ARG B 1 115 ? 16.917  29.093 6.273   1.00 16.57 ? 115  ARG B O   1 
ATOM   1906 C  CB  . ARG B 1 115 ? 19.337  30.926 4.366   1.00 18.61 ? 115  ARG B CB  1 
ATOM   1907 C  CG  . ARG B 1 115 ? 20.339  32.036 4.746   1.00 20.84 ? 115  ARG B CG  1 
ATOM   1908 C  CD  . ARG B 1 115 ? 21.341  32.253 3.606   1.00 23.47 ? 115  ARG B CD  1 
ATOM   1909 N  NE  . ARG B 1 115 ? 22.397  33.180 4.017   1.00 24.54 ? 115  ARG B NE  1 
ATOM   1910 C  CZ  . ARG B 1 115 ? 22.334  34.508 3.957   1.00 24.53 ? 115  ARG B CZ  1 
ATOM   1911 N  NH1 . ARG B 1 115 ? 21.238  35.104 3.482   1.00 25.12 ? 115  ARG B NH1 1 
ATOM   1912 N  NH2 . ARG B 1 115 ? 23.315  35.316 4.342   1.00 25.47 ? 115  ARG B NH2 1 
ATOM   1913 N  N   . THR B 1 116 ? 16.555  29.728 4.158   1.00 16.72 ? 116  THR B N   1 
ATOM   1914 C  CA  . THR B 1 116 ? 15.441  28.775 4.011   1.00 16.85 ? 116  THR B CA  1 
ATOM   1915 C  C   . THR B 1 116 ? 15.747  27.670 3.014   1.00 16.34 ? 116  THR B C   1 
ATOM   1916 O  O   . THR B 1 116 ? 16.131  27.927 1.858   1.00 19.57 ? 116  THR B O   1 
ATOM   1917 C  CB  . THR B 1 116 ? 14.198  29.568 3.560   1.00 16.16 ? 116  THR B CB  1 
ATOM   1918 O  OG1 . THR B 1 116 ? 13.763  30.443 4.608   1.00 17.17 ? 116  THR B OG1 1 
ATOM   1919 C  CG2 . THR B 1 116 ? 13.048  28.633 3.218   1.00 16.20 ? 116  THR B CG2 1 
ATOM   1920 N  N   . LEU B 1 117 ? 15.547  26.413 3.417   1.00 17.17 ? 117  LEU B N   1 
ATOM   1921 C  CA  . LEU B 1 117 ? 15.642  25.320 2.482   1.00 16.35 ? 117  LEU B CA  1 
ATOM   1922 C  C   . LEU B 1 117 ? 14.268  25.091 1.869   1.00 16.28 ? 117  LEU B C   1 
ATOM   1923 O  O   . LEU B 1 117 ? 13.278  25.076 2.615   1.00 16.04 ? 117  LEU B O   1 
ATOM   1924 C  CB  . LEU B 1 117 ? 16.169  24.077 3.208   1.00 15.89 ? 117  LEU B CB  1 
ATOM   1925 C  CG  . LEU B 1 117 ? 16.442  22.853 2.340   1.00 16.91 ? 117  LEU B CG  1 
ATOM   1926 C  CD1 . LEU B 1 117 ? 17.641  23.081 1.413   1.00 20.03 ? 117  LEU B CD1 1 
ATOM   1927 C  CD2 . LEU B 1 117 ? 16.623  21.623 3.246   1.00 18.02 ? 117  LEU B CD2 1 
ATOM   1928 N  N   . VAL B 1 118 ? 14.228  24.917 0.543   1.00 16.18 ? 118  VAL B N   1 
ATOM   1929 C  CA  . VAL B 1 118 ? 12.969  24.801 -0.196  1.00 16.46 ? 118  VAL B CA  1 
ATOM   1930 C  C   . VAL B 1 118 ? 12.980  23.565 -1.083  1.00 16.70 ? 118  VAL B C   1 
ATOM   1931 O  O   . VAL B 1 118 ? 13.948  23.279 -1.778  1.00 19.52 ? 118  VAL B O   1 
ATOM   1932 C  CB  . VAL B 1 118 ? 12.673  26.034 -1.077  1.00 18.04 ? 118  VAL B CB  1 
ATOM   1933 C  CG1 . VAL B 1 118 ? 11.331  25.855 -1.818  1.00 19.20 ? 118  VAL B CG1 1 
ATOM   1934 C  CG2 . VAL B 1 118 ? 12.712  27.344 -0.286  1.00 20.98 ? 118  VAL B CG2 1 
ATOM   1935 N  N   . VAL B 1 119 ? 11.869  22.825 -1.079  1.00 17.41 ? 119  VAL B N   1 
ATOM   1936 C  CA  . VAL B 1 119 ? 11.687  21.739 -2.047  1.00 17.88 ? 119  VAL B CA  1 
ATOM   1937 C  C   . VAL B 1 119 ? 10.548  22.145 -2.977  1.00 17.50 ? 119  VAL B C   1 
ATOM   1938 O  O   . VAL B 1 119 ? 9.532   22.692 -2.547  1.00 17.70 ? 119  VAL B O   1 
ATOM   1939 C  CB  . VAL B 1 119 ? 11.407  20.377 -1.381  1.00 16.28 ? 119  VAL B CB  1 
ATOM   1940 C  CG1 . VAL B 1 119 ? 10.151  20.384 -0.508  1.00 17.58 ? 119  VAL B CG1 1 
ATOM   1941 C  CG2 . VAL B 1 119 ? 11.332  19.321 -2.477  1.00 17.98 ? 119  VAL B CG2 1 
ATOM   1942 N  N   . HIS B 1 120 ? 10.764  21.916 -4.274  1.00 18.72 ? 120  HIS B N   1 
ATOM   1943 C  CA  . HIS B 1 120 ? 9.922   22.446 -5.333  1.00 18.59 ? 120  HIS B CA  1 
ATOM   1944 C  C   . HIS B 1 120 ? 9.023   21.420 -5.993  1.00 19.90 ? 120  HIS B C   1 
ATOM   1945 O  O   . HIS B 1 120 ? 9.177   20.187 -5.901  1.00 21.50 ? 120  HIS B O   1 
ATOM   1946 C  CB  . HIS B 1 120 ? 10.847  23.084 -6.402  1.00 20.08 ? 120  HIS B CB  1 
ATOM   1947 C  CG  . HIS B 1 120 ? 11.330  24.449 -6.040  1.00 20.23 ? 120  HIS B CG  1 
ATOM   1948 N  ND1 . HIS B 1 120 ? 10.589  25.573 -6.287  1.00 20.93 ? 120  HIS B ND1 1 
ATOM   1949 C  CD2 . HIS B 1 120 ? 12.469  24.893 -5.426  1.00 20.34 ? 120  HIS B CD2 1 
ATOM   1950 C  CE1 . HIS B 1 120 ? 11.227  26.660 -5.860  1.00 19.73 ? 120  HIS B CE1 1 
ATOM   1951 N  NE2 . HIS B 1 120 ? 12.383  26.272 -5.345  1.00 20.98 ? 120  HIS B NE2 1 
ATOM   1952 N  N   . GLU B 1 121 ? 8.030   21.974 -6.678  1.00 22.51 ? 121  GLU B N   1 
ATOM   1953 C  CA  . GLU B 1 121 ? 6.990   21.296 -7.425  1.00 23.77 ? 121  GLU B CA  1 
ATOM   1954 C  C   . GLU B 1 121 ? 7.543   20.409 -8.535  1.00 24.33 ? 121  GLU B C   1 
ATOM   1955 O  O   . GLU B 1 121 ? 7.037   19.288 -8.687  1.00 26.80 ? 121  GLU B O   1 
ATOM   1956 C  CB  . GLU B 1 121 ? 6.065   22.356 -8.030  1.00 29.73 ? 121  GLU B CB  1 
ATOM   1957 C  CG  . GLU B 1 121 ? 4.874   21.819 -8.804  1.00 34.01 ? 121  GLU B CG  1 
ATOM   1958 C  CD  . GLU B 1 121 ? 4.296   22.879 -9.734  1.00 36.78 ? 121  GLU B CD  1 
ATOM   1959 O  OE1 . GLU B 1 121 ? 4.765   24.045 -9.692  1.00 32.11 ? 121  GLU B OE1 1 
ATOM   1960 O  OE2 . GLU B 1 121 ? 3.378   22.513 -10.513 1.00 35.53 ? 121  GLU B OE2 1 
ATOM   1961 N  N   . LYS B 1 122 ? 8.536   20.916 -9.261  1.00 24.88 ? 122  LYS B N   1 
ATOM   1962 C  CA  . LYS B 1 122 ? 9.038   20.273 -10.476 1.00 27.90 ? 122  LYS B CA  1 
ATOM   1963 C  C   . LYS B 1 122 ? 10.560  20.172 -10.422 1.00 27.50 ? 122  LYS B C   1 
ATOM   1964 O  O   . LYS B 1 122 ? 11.224  20.677 -9.521  1.00 25.75 ? 122  LYS B O   1 
ATOM   1965 C  CB  . LYS B 1 122 ? 8.618   21.010 -11.748 1.00 33.45 ? 122  LYS B CB  1 
ATOM   1966 C  CG  . LYS B 1 122 ? 7.281   21.708 -11.785 1.00 40.04 ? 122  LYS B CG  1 
ATOM   1967 C  CD  . LYS B 1 122 ? 6.950   22.319 -13.147 1.00 42.01 ? 122  LYS B CD  1 
ATOM   1968 C  CE  . LYS B 1 122 ? 7.247   23.802 -13.211 1.00 46.50 ? 122  LYS B CE  1 
ATOM   1969 N  NZ  . LYS B 1 122 ? 6.589   24.562 -14.309 1.00 48.33 ? 122  LYS B NZ  1 
ATOM   1970 N  N   . ALA B 1 123 ? 11.101  19.503 -11.426 1.00 27.02 ? 123  ALA B N   1 
ATOM   1971 C  CA  . ALA B 1 123 ? 12.538  19.404 -11.557 1.00 28.99 ? 123  ALA B CA  1 
ATOM   1972 C  C   . ALA B 1 123 ? 13.157  20.760 -11.806 1.00 29.66 ? 123  ALA B C   1 
ATOM   1973 O  O   . ALA B 1 123 ? 12.625  21.616 -12.510 1.00 33.47 ? 123  ALA B O   1 
ATOM   1974 C  CB  . ALA B 1 123 ? 12.859  18.475 -12.735 1.00 30.06 ? 123  ALA B CB  1 
ATOM   1975 N  N   . ASP B 1 124 ? 14.319  20.946 -11.207 1.00 30.14 ? 124  ASP B N   1 
ATOM   1976 C  CA  . ASP B 1 124 ? 15.188  22.067 -11.544 1.00 31.63 ? 124  ASP B CA  1 
ATOM   1977 C  C   . ASP B 1 124 ? 15.841  21.738 -12.872 1.00 33.68 ? 124  ASP B C   1 
ATOM   1978 O  O   . ASP B 1 124 ? 16.388  20.623 -12.922 1.00 37.29 ? 124  ASP B O   1 
ATOM   1979 C  CB  . ASP B 1 124 ? 16.180  22.265 -10.399 1.00 28.37 ? 124  ASP B CB  1 
ATOM   1980 C  CG  . ASP B 1 124 ? 17.137  23.435 -10.536 1.00 30.43 ? 124  ASP B CG  1 
ATOM   1981 O  OD1 . ASP B 1 124 ? 17.509  23.837 -11.665 1.00 35.36 ? 124  ASP B OD1 1 
ATOM   1982 O  OD2 . ASP B 1 124 ? 17.563  23.977 -9.492  1.00 31.82 ? 124  ASP B OD2 1 
ATOM   1983 N  N   . HIS B 1 125 ? 15.817  22.588 -13.894 1.00 40.48 ? 125  HIS B N   1 
ATOM   1984 C  CA  . HIS B 1 125 ? 16.413  22.183 -15.174 1.00 45.53 ? 125  HIS B CA  1 
ATOM   1985 C  C   . HIS B 1 125 ? 17.906  22.507 -15.222 1.00 43.89 ? 125  HIS B C   1 
ATOM   1986 O  O   . HIS B 1 125 ? 18.571  22.317 -16.253 1.00 46.14 ? 125  HIS B O   1 
ATOM   1987 C  CB  . HIS B 1 125 ? 15.682  22.827 -16.358 1.00 57.41 ? 125  HIS B CB  1 
ATOM   1988 C  CG  . HIS B 1 125 ? 14.345  22.177 -16.584 1.00 66.74 ? 125  HIS B CG  1 
ATOM   1989 N  ND1 . HIS B 1 125 ? 13.319  22.758 -17.300 1.00 71.09 ? 125  HIS B ND1 1 
ATOM   1990 C  CD2 . HIS B 1 125 ? 13.877  20.973 -16.169 1.00 68.75 ? 125  HIS B CD2 1 
ATOM   1991 C  CE1 . HIS B 1 125 ? 12.279  21.942 -17.316 1.00 72.49 ? 125  HIS B CE1 1 
ATOM   1992 N  NE2 . HIS B 1 125 ? 12.591  20.844 -16.635 1.00 70.76 ? 125  HIS B NE2 1 
ATOM   1993 N  N   . LEU B 1 126 ? 18.349  22.994 -14.080 1.00 43.06 ? 126  LEU B N   1 
ATOM   1994 C  CA  . LEU B 1 126 ? 19.728  23.199 -13.725 1.00 41.34 ? 126  LEU B CA  1 
ATOM   1995 C  C   . LEU B 1 126 ? 20.481  24.150 -14.634 1.00 41.64 ? 126  LEU B C   1 
ATOM   1996 O  O   . LEU B 1 126 ? 21.691  23.912 -14.756 1.00 44.86 ? 126  LEU B O   1 
ATOM   1997 C  CB  . LEU B 1 126 ? 20.511  21.880 -13.774 1.00 40.64 ? 126  LEU B CB  1 
ATOM   1998 C  CG  . LEU B 1 126 ? 19.941  20.674 -13.029 1.00 41.22 ? 126  LEU B CG  1 
ATOM   1999 C  CD1 . LEU B 1 126 ? 20.802  19.451 -13.339 1.00 41.30 ? 126  LEU B CD1 1 
ATOM   2000 C  CD2 . LEU B 1 126 ? 19.846  20.946 -11.535 1.00 37.85 ? 126  LEU B CD2 1 
ATOM   2001 N  N   . GLY B 1 127 ? 19.820  25.130 -15.223 1.00 39.21 ? 127  GLY B N   1 
ATOM   2002 C  CA  . GLY B 1 127 ? 20.550  25.997 -16.155 1.00 45.42 ? 127  GLY B CA  1 
ATOM   2003 C  C   . GLY B 1 127 ? 20.825  25.266 -17.478 1.00 47.24 ? 127  GLY B C   1 
ATOM   2004 O  O   . GLY B 1 127 ? 21.415  26.027 -18.339 1.00 49.15 ? 127  GLY B O   1 
ATOM   2005 N  N   . THR B 1 137 ? 14.087  30.375 -11.154 1.00 70.29 ? 137  THR B N   1 
ATOM   2006 C  CA  . THR B 1 137 ? 15.231  29.913 -11.939 1.00 71.01 ? 137  THR B CA  1 
ATOM   2007 C  C   . THR B 1 137 ? 15.372  28.391 -11.911 1.00 66.10 ? 137  THR B C   1 
ATOM   2008 O  O   . THR B 1 137 ? 15.236  27.786 -10.846 1.00 60.81 ? 137  THR B O   1 
ATOM   2009 C  CB  . THR B 1 137 ? 16.538  30.556 -11.439 1.00 72.53 ? 137  THR B CB  1 
ATOM   2010 O  OG1 . THR B 1 137 ? 16.217  31.643 -10.562 1.00 77.92 ? 137  THR B OG1 1 
ATOM   2011 C  CG2 . THR B 1 137 ? 17.331  31.145 -12.596 1.00 75.99 ? 137  THR B CG2 1 
ATOM   2012 N  N   . GLY B 1 138 ? 15.643  27.804 -13.074 1.00 59.25 ? 138  GLY B N   1 
ATOM   2013 C  CA  . GLY B 1 138 ? 15.754  26.365 -13.268 1.00 57.22 ? 138  GLY B CA  1 
ATOM   2014 C  C   . GLY B 1 138 ? 14.365  25.746 -13.469 1.00 52.85 ? 138  GLY B C   1 
ATOM   2015 O  O   . GLY B 1 138 ? 14.216  24.534 -13.634 1.00 48.55 ? 138  GLY B O   1 
ATOM   2016 N  N   . ASN B 1 139 ? 13.410  26.669 -13.430 1.00 47.78 ? 139  ASN B N   1 
ATOM   2017 C  CA  . ASN B 1 139 ? 11.990  26.486 -13.636 1.00 48.14 ? 139  ASN B CA  1 
ATOM   2018 C  C   . ASN B 1 139 ? 11.397  25.356 -12.812 1.00 40.50 ? 139  ASN B C   1 
ATOM   2019 O  O   . ASN B 1 139 ? 10.702  24.501 -13.368 1.00 40.97 ? 139  ASN B O   1 
ATOM   2020 C  CB  . ASN B 1 139 ? 11.717  26.213 -15.122 1.00 52.69 ? 139  ASN B CB  1 
ATOM   2021 C  CG  . ASN B 1 139 ? 10.649  27.154 -15.654 1.00 61.75 ? 139  ASN B CG  1 
ATOM   2022 O  OD1 . ASN B 1 139 ? 10.954  28.063 -16.441 1.00 76.36 ? 139  ASN B OD1 1 
ATOM   2023 N  ND2 . ASN B 1 139 ? 9.417   26.916 -15.213 1.00 65.74 ? 139  ASN B ND2 1 
ATOM   2024 N  N   . ALA B 1 140 ? 11.674  25.390 -11.502 1.00 33.01 ? 140  ALA B N   1 
ATOM   2025 C  CA  . ALA B 1 140 ? 11.238  24.275 -10.649 1.00 29.30 ? 140  ALA B CA  1 
ATOM   2026 C  C   . ALA B 1 140 ? 9.823   24.446 -10.114 1.00 31.02 ? 140  ALA B C   1 
ATOM   2027 O  O   . ALA B 1 140 ? 9.347   23.603 -9.331  1.00 25.88 ? 140  ALA B O   1 
ATOM   2028 C  CB  . ALA B 1 140 ? 12.251  24.109 -9.535  1.00 30.00 ? 140  ALA B CB  1 
ATOM   2029 N  N   . GLY B 1 141 ? 9.121   25.514 -10.507 1.00 29.43 ? 141  GLY B N   1 
ATOM   2030 C  CA  . GLY B 1 141 ? 7.716   25.632 -10.146 1.00 29.93 ? 141  GLY B CA  1 
ATOM   2031 C  C   . GLY B 1 141 ? 7.491   25.978 -8.704  1.00 26.70 ? 141  GLY B C   1 
ATOM   2032 O  O   . GLY B 1 141 ? 8.370   26.561 -8.068  1.00 28.57 ? 141  GLY B O   1 
ATOM   2033 N  N   . SER B 1 142 ? 6.328   25.679 -8.115  1.00 27.95 ? 142  SER B N   1 
ATOM   2034 C  CA  . SER B 1 142 ? 6.083   26.308 -6.824  1.00 27.15 ? 142  SER B CA  1 
ATOM   2035 C  C   . SER B 1 142 ? 6.951   25.740 -5.701  1.00 24.30 ? 142  SER B C   1 
ATOM   2036 O  O   . SER B 1 142 ? 7.587   24.703 -5.811  1.00 22.03 ? 142  SER B O   1 
ATOM   2037 C  CB  . SER B 1 142 ? 4.617   26.204 -6.408  1.00 33.10 ? 142  SER B CB  1 
ATOM   2038 O  OG  . SER B 1 142 ? 4.178   24.871 -6.373  1.00 41.67 ? 142  SER B OG  1 
ATOM   2039 N  N   . ARG B 1 143 ? 6.973   26.494 -4.607  1.00 23.53 ? 143  ARG B N   1 
ATOM   2040 C  CA  . ARG B 1 143 ? 7.699   26.132 -3.392  1.00 22.51 ? 143  ARG B CA  1 
ATOM   2041 C  C   . ARG B 1 143 ? 6.769   25.321 -2.500  1.00 20.19 ? 143  ARG B C   1 
ATOM   2042 O  O   . ARG B 1 143 ? 5.862   25.892 -1.886  1.00 28.04 ? 143  ARG B O   1 
ATOM   2043 C  CB  . ARG B 1 143 ? 8.160   27.411 -2.682  1.00 24.02 ? 143  ARG B CB  1 
ATOM   2044 C  CG  . ARG B 1 143 ? 9.209   28.198 -3.484  1.00 25.67 ? 143  ARG B CG  1 
ATOM   2045 C  CD  . ARG B 1 143 ? 9.501   29.551 -2.850  1.00 24.47 ? 143  ARG B CD  1 
ATOM   2046 N  NE  . ARG B 1 143 ? 10.241  30.379 -3.798  1.00 25.81 ? 143  ARG B NE  1 
ATOM   2047 C  CZ  . ARG B 1 143 ? 10.621  31.624 -3.584  1.00 30.35 ? 143  ARG B CZ  1 
ATOM   2048 N  NH1 . ARG B 1 143 ? 10.337  32.180 -2.408  1.00 41.19 ? 143  ARG B NH1 1 
ATOM   2049 N  NH2 . ARG B 1 143 ? 11.289  32.346 -4.496  1.00 28.54 ? 143  ARG B NH2 1 
ATOM   2050 N  N   . LEU B 1 144 ? 6.934   24.005 -2.486  1.00 18.52 ? 144  LEU B N   1 
ATOM   2051 C  CA  . LEU B 1 144 ? 5.956   23.119 -1.831  1.00 17.65 ? 144  LEU B CA  1 
ATOM   2052 C  C   . LEU B 1 144 ? 6.120   23.100 -0.311  1.00 18.74 ? 144  LEU B C   1 
ATOM   2053 O  O   . LEU B 1 144 ? 5.150   23.089 0.428   1.00 20.42 ? 144  LEU B O   1 
ATOM   2054 C  CB  . LEU B 1 144 ? 6.002   21.682 -2.347  1.00 18.21 ? 144  LEU B CB  1 
ATOM   2055 C  CG  . LEU B 1 144 ? 5.627   21.513 -3.836  1.00 23.73 ? 144  LEU B CG  1 
ATOM   2056 C  CD1 . LEU B 1 144 ? 5.689   20.042 -4.192  1.00 29.04 ? 144  LEU B CD1 1 
ATOM   2057 C  CD2 . LEU B 1 144 ? 4.270   22.125 -4.138  1.00 30.33 ? 144  LEU B CD2 1 
ATOM   2058 N  N   . ALA B 1 145 ? 7.361   23.064 0.165   1.00 17.02 ? 145  ALA B N   1 
ATOM   2059 C  CA  . ALA B 1 145 ? 7.609   23.108 1.595   1.00 15.32 ? 145  ALA B CA  1 
ATOM   2060 C  C   . ALA B 1 145 ? 8.941   23.768 1.815   1.00 15.59 ? 145  ALA B C   1 
ATOM   2061 O  O   . ALA B 1 145 ? 9.831   23.739 0.939   1.00 15.35 ? 145  ALA B O   1 
ATOM   2062 C  CB  . ALA B 1 145 ? 7.582   21.669 2.145   1.00 17.19 ? 145  ALA B CB  1 
ATOM   2063 N  N   . CYS B 1 146 ? 9.077   24.342 3.020   1.00 15.43 ? 146  CYS B N   1 
ATOM   2064 C  CA  . CYS B 1 146 ? 10.313  25.012 3.332   1.00 15.80 ? 146  CYS B CA  1 
ATOM   2065 C  C   . CYS B 1 146 ? 10.471  25.118 4.841   1.00 12.73 ? 146  CYS B C   1 
ATOM   2066 O  O   . CYS B 1 146 ? 9.524   24.901 5.594   1.00 15.27 ? 146  CYS B O   1 
ATOM   2067 C  CB  . CYS B 1 146 ? 10.375  26.423 2.721   1.00 17.17 ? 146  CYS B CB  1 
ATOM   2068 S  SG  . CYS B 1 146 ? 8.980   27.424 3.254   1.00 20.24 ? 146  CYS B SG  1 
ATOM   2069 N  N   . GLY B 1 147 ? 11.666  25.487 5.250   1.00 14.53 ? 147  GLY B N   1 
ATOM   2070 C  CA  . GLY B 1 147 ? 11.890  25.743 6.685   1.00 14.44 ? 147  GLY B CA  1 
ATOM   2071 C  C   . GLY B 1 147 ? 13.177  26.512 6.829   1.00 14.66 ? 147  GLY B C   1 
ATOM   2072 O  O   . GLY B 1 147 ? 14.011  26.585 5.920   1.00 15.32 ? 147  GLY B O   1 
ATOM   2073 N  N   . VAL B 1 148 ? 13.363  27.133 7.985   1.00 15.09 ? 148  VAL B N   1 
ATOM   2074 C  CA  . VAL B 1 148 ? 14.562  27.884 8.335   1.00 13.45 ? 148  VAL B CA  1 
ATOM   2075 C  C   . VAL B 1 148 ? 15.640  26.897 8.762   1.00 13.84 ? 148  VAL B C   1 
ATOM   2076 O  O   . VAL B 1 148 ? 15.370  25.995 9.550   1.00 15.28 ? 148  VAL B O   1 
ATOM   2077 C  CB  . VAL B 1 148 ? 14.310  28.934 9.431   1.00 13.00 ? 148  VAL B CB  1 
ATOM   2078 C  CG1 . VAL B 1 148 ? 15.562  29.752 9.711   1.00 15.74 ? 148  VAL B CG1 1 
ATOM   2079 C  CG2 . VAL B 1 148 ? 13.166  29.864 8.996   1.00 18.10 ? 148  VAL B CG2 1 
ATOM   2080 N  N   . ILE B 1 149 ? 16.849  27.039 8.254   1.00 15.17 ? 149  ILE B N   1 
ATOM   2081 C  CA  . ILE B 1 149 ? 17.950  26.167 8.626   1.00 15.19 ? 149  ILE B CA  1 
ATOM   2082 C  C   . ILE B 1 149 ? 18.520  26.634 9.963   1.00 15.88 ? 149  ILE B C   1 
ATOM   2083 O  O   . ILE B 1 149 ? 19.002  27.772 10.111  1.00 18.18 ? 149  ILE B O   1 
ATOM   2084 C  CB  . ILE B 1 149 ? 19.013  26.168 7.536   1.00 16.40 ? 149  ILE B CB  1 
ATOM   2085 C  CG1 . ILE B 1 149 ? 18.435  25.641 6.198   1.00 17.94 ? 149  ILE B CG1 1 
ATOM   2086 C  CG2 . ILE B 1 149 ? 20.248  25.383 7.950   1.00 19.06 ? 149  ILE B CG2 1 
ATOM   2087 C  CD1 . ILE B 1 149 ? 19.412  25.912 5.045   1.00 20.65 ? 149  ILE B CD1 1 
ATOM   2088 N  N   . GLY B 1 150 ? 18.424  25.750 10.953  1.00 15.21 ? 150  GLY B N   1 
ATOM   2089 C  CA  . GLY B 1 150 ? 18.815  26.028 12.323  1.00 14.43 ? 150  GLY B CA  1 
ATOM   2090 C  C   . GLY B 1 150 ? 20.060  25.278 12.745  1.00 17.03 ? 150  GLY B C   1 
ATOM   2091 O  O   . GLY B 1 150 ? 20.379  24.202 12.236  1.00 16.66 ? 150  GLY B O   1 
ATOM   2092 N  N   . ILE B 1 151 ? 20.794  25.851 13.707  1.00 15.13 ? 151  ILE B N   1 
ATOM   2093 C  CA  . ILE B 1 151 ? 21.881  25.161 14.371  1.00 15.37 ? 151  ILE B CA  1 
ATOM   2094 C  C   . ILE B 1 151 ? 21.381  23.978 15.192  1.00 15.99 ? 151  ILE B C   1 
ATOM   2095 O  O   . ILE B 1 151 ? 20.395  24.087 15.924  1.00 16.76 ? 151  ILE B O   1 
ATOM   2096 C  CB  . ILE B 1 151 ? 22.650  26.181 15.225  1.00 15.41 ? 151  ILE B CB  1 
ATOM   2097 C  CG1 . ILE B 1 151 ? 23.163  27.332 14.361  1.00 18.35 ? 151  ILE B CG1 1 
ATOM   2098 C  CG2 . ILE B 1 151 ? 23.781  25.463 15.941  1.00 16.94 ? 151  ILE B CG2 1 
ATOM   2099 C  CD1 . ILE B 1 151 ? 23.659  28.525 15.162  1.00 20.33 ? 151  ILE B CD1 1 
ATOM   2100 N  N   . ALA B 1 152 ? 22.085  22.847 15.062  1.00 16.40 ? 152  ALA B N   1 
ATOM   2101 C  CA  . ALA B 1 152 ? 21.728  21.590 15.679  1.00 17.68 ? 152  ALA B CA  1 
ATOM   2102 C  C   . ALA B 1 152 ? 22.870  21.058 16.537  1.00 15.84 ? 152  ALA B C   1 
ATOM   2103 O  O   . ALA B 1 152 ? 24.047  21.388 16.344  1.00 22.70 ? 152  ALA B O   1 
ATOM   2104 C  CB  . ALA B 1 152 ? 21.370  20.551 14.619  1.00 21.11 ? 152  ALA B CB  1 
ATOM   2105 N  N   . GLN B 1 153 ? 22.483  20.243 17.496  1.00 19.05 ? 153  GLN B N   1 
ATOM   2106 C  CA  . GLN B 1 153 ? 23.477  19.731 18.445  1.00 23.82 ? 153  GLN B CA  1 
ATOM   2107 C  C   . GLN B 1 153 ? 24.330  18.624 17.832  1.00 30.35 ? 153  GLN B C   1 
ATOM   2108 O  O   . GLN B 1 153 ? 25.563  18.654 18.034  1.00 38.14 ? 153  GLN B O   1 
ATOM   2109 C  CB  . GLN B 1 153 ? 22.783  19.205 19.695  1.00 22.43 ? 153  GLN B CB  1 
ATOM   2110 C  CG  . GLN B 1 153 ? 23.760  18.690 20.748  1.00 30.31 ? 153  GLN B CG  1 
ATOM   2111 C  CD  . GLN B 1 153 ? 23.051  18.128 21.967  1.00 35.78 ? 153  GLN B CD  1 
ATOM   2112 O  OE1 . GLN B 1 153 ? 23.579  18.239 23.064  1.00 47.81 ? 153  GLN B OE1 1 
ATOM   2113 N  NE2 . GLN B 1 153 ? 21.889  17.531 21.847  1.00 36.99 ? 153  GLN B NE2 1 
ATOM   2114 O  OXT . GLN B 1 153 ? 23.757  17.734 17.166  1.00 28.37 ? 153  GLN B OXT 1 
ATOM   2115 N  N   . ALA C 1 1   ? -27.717 65.315 38.337  1.00 50.28 ? 1    ALA C N   1 
ATOM   2116 C  CA  . ALA C 1 1   ? -27.184 63.966 38.119  1.00 30.05 ? 1    ALA C CA  1 
ATOM   2117 C  C   . ALA C 1 1   ? -25.984 63.939 37.191  1.00 29.11 ? 1    ALA C C   1 
ATOM   2118 O  O   . ALA C 1 1   ? -25.988 64.322 36.041  1.00 34.75 ? 1    ALA C O   1 
ATOM   2119 C  CB  . ALA C 1 1   ? -28.265 63.040 37.560  1.00 50.01 ? 1    ALA C CB  1 
ATOM   2120 N  N   . THR C 1 2   ? -24.870 63.410 37.708  1.00 23.92 ? 2    THR C N   1 
ATOM   2121 C  CA  . THR C 1 2   ? -23.681 63.353 36.884  1.00 18.93 ? 2    THR C CA  1 
ATOM   2122 C  C   . THR C 1 2   ? -23.362 61.908 36.496  1.00 14.12 ? 2    THR C C   1 
ATOM   2123 O  O   . THR C 1 2   ? -22.529 61.794 35.599  1.00 14.27 ? 2    THR C O   1 
ATOM   2124 C  CB  . THR C 1 2   ? -22.425 63.991 37.474  1.00 20.06 ? 2    THR C CB  1 
ATOM   2125 O  OG1 . THR C 1 2   ? -22.118 63.393 38.754  1.00 29.54 ? 2    THR C OG1 1 
ATOM   2126 C  CG2 . THR C 1 2   ? -22.667 65.458 37.770  1.00 36.35 ? 2    THR C CG2 1 
ATOM   2127 N  N   . LYS C 1 3   ? -23.983 60.901 37.070  1.00 11.82 ? 3    LYS C N   1 
ATOM   2128 C  CA  . LYS C 1 3   ? -23.747 59.507 36.688  1.00 10.61 ? 3    LYS C CA  1 
ATOM   2129 C  C   . LYS C 1 3   ? -25.074 58.772 36.608  1.00 9.21  ? 3    LYS C C   1 
ATOM   2130 O  O   . LYS C 1 3   ? -26.032 59.061 37.320  1.00 10.87 ? 3    LYS C O   1 
ATOM   2131 C  CB  . LYS C 1 3   ? -22.821 58.793 37.665  1.00 14.18 ? 3    LYS C CB  1 
ATOM   2132 C  CG  . LYS C 1 3   ? -21.388 59.385 37.753  1.00 21.42 ? 3    LYS C CG  1 
ATOM   2133 C  CD  . LYS C 1 3   ? -20.492 58.518 38.655  1.00 31.00 ? 3    LYS C CD  1 
ATOM   2134 C  CE  . LYS C 1 3   ? -19.151 59.168 38.910  1.00 38.23 ? 3    LYS C CE  1 
ATOM   2135 N  NZ  . LYS C 1 3   ? -17.918 58.360 38.811  1.00 49.56 ? 3    LYS C NZ  1 
ATOM   2136 N  N   . ALA C 1 4   ? -25.130 57.840 35.681  1.00 10.50 ? 4    ALA C N   1 
ATOM   2137 C  CA  . ALA C 1 4   ? -26.292 56.956 35.525  1.00 10.05 ? 4    ALA C CA  1 
ATOM   2138 C  C   . ALA C 1 4   ? -25.826 55.551 35.142  1.00 8.98  ? 4    ALA C C   1 
ATOM   2139 O  O   . ALA C 1 4   ? -24.653 55.357 34.779  1.00 10.88 ? 4    ALA C O   1 
ATOM   2140 C  CB  . ALA C 1 4   ? -27.293 57.499 34.526  1.00 10.67 ? 4    ALA C CB  1 
ATOM   2141 N  N   . VAL C 1 5   ? -26.732 54.590 35.246  1.00 9.26  ? 5    VAL C N   1 
ATOM   2142 C  CA  . VAL C 1 5   ? -26.342 53.197 34.944  1.00 8.26  ? 5    VAL C CA  1 
ATOM   2143 C  C   . VAL C 1 5   ? -27.579 52.468 34.456  1.00 8.95  ? 5    VAL C C   1 
ATOM   2144 O  O   . VAL C 1 5   ? -28.741 52.868 34.751  1.00 10.51 ? 5    VAL C O   1 
ATOM   2145 C  CB  . VAL C 1 5   ? -25.738 52.519 36.190  1.00 9.86  ? 5    VAL C CB  1 
ATOM   2146 C  CG1 . VAL C 1 5   ? -26.777 52.324 37.289  1.00 12.54 ? 5    VAL C CG1 1 
ATOM   2147 C  CG2 . VAL C 1 5   ? -25.064 51.197 35.850  1.00 11.66 ? 5    VAL C CG2 1 
ATOM   2148 N  N   . CYS C 1 6   ? -27.375 51.430 33.661  1.00 10.56 ? 6    CYS C N   1 
ATOM   2149 C  CA  . CYS C 1 6   ? -28.504 50.631 33.184  1.00 8.98  ? 6    CYS C CA  1 
ATOM   2150 C  C   . CYS C 1 6   ? -28.121 49.171 33.127  1.00 9.10  ? 6    CYS C C   1 
ATOM   2151 O  O   . CYS C 1 6   ? -27.054 48.875 32.547  1.00 9.58  ? 6    CYS C O   1 
ATOM   2152 C  CB  . CYS C 1 6   ? -28.873 51.140 31.786  1.00 10.37 ? 6    CYS C CB  1 
ATOM   2153 S  SG  . CYS C 1 6   ? -30.265 50.275 31.042  1.00 12.28 ? 6    CYS C SG  1 
ATOM   2154 N  N   . VAL C 1 7   ? -28.959 48.302 33.670  1.00 8.42  ? 7    VAL C N   1 
ATOM   2155 C  CA  . VAL C 1 7   ? -28.753 46.864 33.540  1.00 9.06  ? 7    VAL C CA  1 
ATOM   2156 C  C   . VAL C 1 7   ? -29.670 46.381 32.429  1.00 9.29  ? 7    VAL C C   1 
ATOM   2157 O  O   . VAL C 1 7   ? -30.906 46.489 32.530  1.00 11.59 ? 7    VAL C O   1 
ATOM   2158 C  CB  . VAL C 1 7   ? -29.084 46.144 34.858  1.00 10.79 ? 7    VAL C CB  1 
ATOM   2159 C  CG1 . VAL C 1 7   ? -28.859 44.634 34.646  1.00 13.12 ? 7    VAL C CG1 1 
ATOM   2160 C  CG2 . VAL C 1 7   ? -28.200 46.671 35.985  1.00 11.80 ? 7    VAL C CG2 1 
ATOM   2161 N  N   . LEU C 1 8   ? -29.085 45.902 31.338  1.00 10.44 ? 8    LEU C N   1 
ATOM   2162 C  CA  . LEU C 1 8   ? -29.883 45.409 30.212  1.00 10.63 ? 8    LEU C CA  1 
ATOM   2163 C  C   . LEU C 1 8   ? -30.143 43.915 30.385  1.00 9.66  ? 8    LEU C C   1 
ATOM   2164 O  O   . LEU C 1 8   ? -29.170 43.136 30.529  1.00 12.17 ? 8    LEU C O   1 
ATOM   2165 C  CB  . LEU C 1 8   ? -29.151 45.634 28.878  1.00 13.43 ? 8    LEU C CB  1 
ATOM   2166 C  CG  . LEU C 1 8   ? -29.019 47.145 28.503  1.00 15.21 ? 8    LEU C CG  1 
ATOM   2167 C  CD1 . LEU C 1 8   ? -27.838 47.801 29.157  1.00 17.83 ? 8    LEU C CD1 1 
ATOM   2168 C  CD2 . LEU C 1 8   ? -28.969 47.308 26.995  1.00 28.32 ? 8    LEU C CD2 1 
ATOM   2169 N  N   . LYS C 1 9   ? -31.389 43.499 30.322  1.00 10.58 ? 9    LYS C N   1 
ATOM   2170 C  CA  . LYS C 1 9   ? -31.794 42.107 30.428  1.00 11.86 ? 9    LYS C CA  1 
ATOM   2171 C  C   . LYS C 1 9   ? -32.899 41.821 29.416  1.00 12.44 ? 9    LYS C C   1 
ATOM   2172 O  O   . LYS C 1 9   ? -33.564 42.772 28.991  1.00 12.28 ? 9    LYS C O   1 
ATOM   2173 C  CB  . LYS C 1 9   ? -32.353 41.728 31.819  1.00 16.84 ? 9    LYS C CB  1 
ATOM   2174 C  CG  . LYS C 1 9   ? -31.408 41.951 32.972  1.00 19.76 ? 9    LYS C CG  1 
ATOM   2175 C  CD  . LYS C 1 9   ? -32.018 41.282 34.205  1.00 23.40 ? 9    LYS C CD  1 
ATOM   2176 C  CE  . LYS C 1 9   ? -31.099 41.508 35.387  1.00 30.54 ? 9    LYS C CE  1 
ATOM   2177 N  NZ  . LYS C 1 9   ? -31.414 40.571 36.517  1.00 20.69 ? 9    LYS C NZ  1 
ATOM   2178 N  N   . GLY C 1 10  ? -33.114 40.572 29.079  1.00 12.34 ? 10   GLY C N   1 
ATOM   2179 C  CA  . GLY C 1 10  ? -34.273 40.227 28.245  1.00 14.95 ? 10   GLY C CA  1 
ATOM   2180 C  C   . GLY C 1 10  ? -34.659 38.764 28.515  1.00 13.59 ? 10   GLY C C   1 
ATOM   2181 O  O   . GLY C 1 10  ? -34.348 38.210 29.562  1.00 16.11 ? 10   GLY C O   1 
ATOM   2182 N  N   . ASP C 1 11  ? -35.278 38.168 27.525  1.00 14.27 ? 11   ASP C N   1 
ATOM   2183 C  CA  . ASP C 1 11  ? -35.739 36.799 27.686  1.00 14.16 ? 11   ASP C CA  1 
ATOM   2184 C  C   . ASP C 1 11  ? -34.704 35.794 27.179  1.00 14.40 ? 11   ASP C C   1 
ATOM   2185 O  O   . ASP C 1 11  ? -34.929 34.594 27.314  1.00 18.37 ? 11   ASP C O   1 
ATOM   2186 C  CB  . ASP C 1 11  ? -37.062 36.629 26.940  1.00 15.74 ? 11   ASP C CB  1 
ATOM   2187 C  CG  . ASP C 1 11  ? -38.132 37.455 27.629  1.00 13.81 ? 11   ASP C CG  1 
ATOM   2188 O  OD1 . ASP C 1 11  ? -38.431 37.214 28.839  1.00 17.98 ? 11   ASP C OD1 1 
ATOM   2189 O  OD2 . ASP C 1 11  ? -38.654 38.350 26.930  1.00 16.59 ? 11   ASP C OD2 1 
ATOM   2190 N  N   . GLY C 1 12  ? -33.631 36.250 26.581  1.00 16.34 ? 12   GLY C N   1 
ATOM   2191 C  CA  . GLY C 1 12  ? -32.606 35.428 25.994  1.00 15.54 ? 12   GLY C CA  1 
ATOM   2192 C  C   . GLY C 1 12  ? -31.252 35.616 26.687  1.00 14.38 ? 12   GLY C C   1 
ATOM   2193 O  O   . GLY C 1 12  ? -31.238 36.003 27.846  1.00 16.70 ? 12   GLY C O   1 
ATOM   2194 N  N   . PRO C 1 13  ? -30.156 35.313 25.979  1.00 14.78 ? 13   PRO C N   1 
ATOM   2195 C  CA  . PRO C 1 13  ? -28.825 35.374 26.568  1.00 15.11 ? 13   PRO C CA  1 
ATOM   2196 C  C   . PRO C 1 13  ? -28.177 36.754 26.568  1.00 14.72 ? 13   PRO C C   1 
ATOM   2197 O  O   . PRO C 1 13  ? -27.056 36.884 27.032  1.00 16.03 ? 13   PRO C O   1 
ATOM   2198 C  CB  . PRO C 1 13  ? -28.020 34.443 25.649  1.00 18.36 ? 13   PRO C CB  1 
ATOM   2199 C  CG  . PRO C 1 13  ? -28.674 34.629 24.291  1.00 15.90 ? 13   PRO C CG  1 
ATOM   2200 C  CD  . PRO C 1 13  ? -30.153 34.815 24.579  1.00 16.88 ? 13   PRO C CD  1 
ATOM   2201 N  N   . VAL C 1 14  ? -28.879 37.760 26.050  1.00 12.15 ? 14   VAL C N   1 
ATOM   2202 C  CA  . VAL C 1 14  ? -28.206 39.077 25.894  1.00 12.51 ? 14   VAL C CA  1 
ATOM   2203 C  C   . VAL C 1 14  ? -28.374 39.854 27.190  1.00 12.19 ? 14   VAL C C   1 
ATOM   2204 O  O   . VAL C 1 14  ? -29.513 40.042 27.674  1.00 14.22 ? 14   VAL C O   1 
ATOM   2205 C  CB  . VAL C 1 14  ? -28.785 39.829 24.708  1.00 11.62 ? 14   VAL C CB  1 
ATOM   2206 C  CG1 . VAL C 1 14  ? -28.143 41.241 24.623  1.00 12.14 ? 14   VAL C CG1 1 
ATOM   2207 C  CG2 . VAL C 1 14  ? -28.523 39.047 23.421  1.00 14.93 ? 14   VAL C CG2 1 
ATOM   2208 N  N   . GLN C 1 15  ? -27.244 40.295 27.742  1.00 12.50 ? 15   GLN C N   1 
ATOM   2209 C  CA  . GLN C 1 15  ? -27.312 41.101 28.963  1.00 12.81 ? 15   GLN C CA  1 
ATOM   2210 C  C   . GLN C 1 15  ? -26.022 41.885 29.144  1.00 13.80 ? 15   GLN C C   1 
ATOM   2211 O  O   . GLN C 1 15  ? -24.952 41.517 28.642  1.00 13.82 ? 15   GLN C O   1 
ATOM   2212 C  CB  . GLN C 1 15  ? -27.601 40.219 30.182  1.00 16.85 ? 15   GLN C CB  1 
ATOM   2213 C  CG  . GLN C 1 15  ? -26.570 39.144 30.372  1.00 22.75 ? 15   GLN C CG  1 
ATOM   2214 C  CD  . GLN C 1 15  ? -25.441 39.462 31.294  1.00 28.07 ? 15   GLN C CD  1 
ATOM   2215 O  OE1 . GLN C 1 15  ? -24.459 38.729 31.319  1.00 41.47 ? 15   GLN C OE1 1 
ATOM   2216 N  NE2 . GLN C 1 15  ? -25.582 40.545 32.061  1.00 24.34 ? 15   GLN C NE2 1 
ATOM   2217 N  N   . GLY C 1 16  ? -26.121 42.986 29.899  1.00 12.29 ? 16   GLY C N   1 
ATOM   2218 C  CA  . GLY C 1 16  ? -24.906 43.697 30.238  1.00 14.01 ? 16   GLY C CA  1 
ATOM   2219 C  C   . GLY C 1 16  ? -25.249 44.920 31.092  1.00 11.56 ? 16   GLY C C   1 
ATOM   2220 O  O   . GLY C 1 16  ? -26.385 45.139 31.511  1.00 13.16 ? 16   GLY C O   1 
ATOM   2221 N  N   . ILE C 1 17  ? -24.234 45.721 31.303  1.00 11.40 ? 17   ILE C N   1 
ATOM   2222 C  CA  . ILE C 1 17  ? -24.330 46.959 32.063  1.00 10.21 ? 17   ILE C CA  1 
ATOM   2223 C  C   . ILE C 1 17  ? -23.748 48.087 31.226  1.00 10.08 ? 17   ILE C C   1 
ATOM   2224 O  O   . ILE C 1 17  ? -22.654 47.951 30.651  1.00 12.17 ? 17   ILE C O   1 
ATOM   2225 C  CB  . ILE C 1 17  ? -23.559 46.826 33.375  1.00 11.29 ? 17   ILE C CB  1 
ATOM   2226 C  CG1 . ILE C 1 17  ? -24.208 45.762 34.271  1.00 12.81 ? 17   ILE C CG1 1 
ATOM   2227 C  CG2 . ILE C 1 17  ? -23.451 48.192 34.094  1.00 12.35 ? 17   ILE C CG2 1 
ATOM   2228 C  CD1 . ILE C 1 17  ? -23.367 45.435 35.470  1.00 15.59 ? 17   ILE C CD1 1 
ATOM   2229 N  N   . ILE C 1 18  ? -24.478 49.193 31.158  1.00 9.65  ? 18   ILE C N   1 
ATOM   2230 C  CA  . ILE C 1 18  ? -23.954 50.398 30.513  1.00 10.15 ? 18   ILE C CA  1 
ATOM   2231 C  C   . ILE C 1 18  ? -23.984 51.523 31.540  1.00 8.93  ? 18   ILE C C   1 
ATOM   2232 O  O   . ILE C 1 18  ? -24.997 51.765 32.218  1.00 10.49 ? 18   ILE C O   1 
ATOM   2233 C  CB  . ILE C 1 18  ? -24.758 50.742 29.242  1.00 10.71 ? 18   ILE C CB  1 
ATOM   2234 C  CG1 . ILE C 1 18  ? -24.683 49.645 28.164  1.00 10.68 ? 18   ILE C CG1 1 
ATOM   2235 C  CG2 . ILE C 1 18  ? -24.345 52.118 28.669  1.00 11.01 ? 18   ILE C CG2 1 
ATOM   2236 C  CD1 . ILE C 1 18  ? -23.313 49.487 27.543  1.00 12.61 ? 18   ILE C CD1 1 
ATOM   2237 N  N   . ASN C 1 19  ? -22.872 52.200 31.649  1.00 10.64 ? 19   ASN C N   1 
ATOM   2238 C  CA  . ASN C 1 19  ? -22.650 53.327 32.516  1.00 10.93 ? 19   ASN C CA  1 
ATOM   2239 C  C   . ASN C 1 19  ? -22.660 54.626 31.739  1.00 9.21  ? 19   ASN C C   1 
ATOM   2240 O  O   . ASN C 1 19  ? -22.252 54.681 30.589  1.00 11.06 ? 19   ASN C O   1 
ATOM   2241 C  CB  . ASN C 1 19  ? -21.291 53.200 33.224  1.00 13.10 ? 19   ASN C CB  1 
ATOM   2242 C  CG  . ASN C 1 19  ? -21.110 51.839 33.842  1.00 14.21 ? 19   ASN C CG  1 
ATOM   2243 O  OD1 . ASN C 1 19  ? -21.621 51.673 34.956  1.00 15.51 ? 19   ASN C OD1 1 
ATOM   2244 N  ND2 . ASN C 1 19  ? -20.407 50.913 33.195  1.00 17.08 ? 19   ASN C ND2 1 
ATOM   2245 N  N   . PHE C 1 20  ? -23.102 55.700 32.387  1.00 10.76 ? 20   PHE C N   1 
ATOM   2246 C  CA  . PHE C 1 20  ? -23.113 57.044 31.798  1.00 10.65 ? 20   PHE C CA  1 
ATOM   2247 C  C   . PHE C 1 20  ? -22.434 58.002 32.776  1.00 10.65 ? 20   PHE C C   1 
ATOM   2248 O  O   . PHE C 1 20  ? -22.666 57.912 34.008  1.00 11.55 ? 20   PHE C O   1 
ATOM   2249 C  CB  . PHE C 1 20  ? -24.541 57.576 31.587  1.00 10.59 ? 20   PHE C CB  1 
ATOM   2250 C  CG  . PHE C 1 20  ? -25.386 56.662 30.690  1.00 10.53 ? 20   PHE C CG  1 
ATOM   2251 C  CD1 . PHE C 1 20  ? -26.007 55.545 31.221  1.00 11.29 ? 20   PHE C CD1 1 
ATOM   2252 C  CD2 . PHE C 1 20  ? -25.505 56.947 29.345  1.00 11.00 ? 20   PHE C CD2 1 
ATOM   2253 C  CE1 . PHE C 1 20  ? -26.759 54.690 30.420  1.00 11.43 ? 20   PHE C CE1 1 
ATOM   2254 C  CE2 . PHE C 1 20  ? -26.287 56.104 28.527  1.00 12.46 ? 20   PHE C CE2 1 
ATOM   2255 C  CZ  . PHE C 1 20  ? -26.924 54.990 29.056  1.00 12.13 ? 20   PHE C CZ  1 
ATOM   2256 N  N   . GLU C 1 21  ? -21.681 58.969 32.252  1.00 11.27 ? 21   GLU C N   1 
ATOM   2257 C  CA  . GLU C 1 21  ? -21.088 59.970 33.131  1.00 11.60 ? 21   GLU C CA  1 
ATOM   2258 C  C   . GLU C 1 21  ? -21.091 61.281 32.371  1.00 11.47 ? 21   GLU C C   1 
ATOM   2259 O  O   . GLU C 1 21  ? -20.650 61.334 31.209  1.00 14.00 ? 21   GLU C O   1 
ATOM   2260 C  CB  . GLU C 1 21  ? -19.660 59.614 33.555  1.00 13.95 ? 21   GLU C CB  1 
ATOM   2261 C  CG  . GLU C 1 21  ? -19.081 60.627 34.560  1.00 22.05 ? 21   GLU C CG  1 
ATOM   2262 C  CD  . GLU C 1 21  ? -17.824 59.961 35.139  1.00 32.59 ? 21   GLU C CD  1 
ATOM   2263 O  OE1 . GLU C 1 21  ? -17.940 58.885 35.789  1.00 37.91 ? 21   GLU C OE1 1 
ATOM   2264 O  OE2 . GLU C 1 21  ? -16.750 60.510 34.901  1.00 44.96 ? 21   GLU C OE2 1 
ATOM   2265 N  N   . GLN C 1 22  ? -21.549 62.330 33.053  1.00 11.36 ? 22   GLN C N   1 
ATOM   2266 C  CA  . GLN C 1 22  ? -21.594 63.651 32.437  1.00 12.86 ? 22   GLN C CA  1 
ATOM   2267 C  C   . GLN C 1 22  ? -21.055 64.691 33.421  1.00 16.33 ? 22   GLN C C   1 
ATOM   2268 O  O   . GLN C 1 22  ? -21.771 65.056 34.351  1.00 17.50 ? 22   GLN C O   1 
ATOM   2269 C  CB  . GLN C 1 22  ? -23.041 63.994 32.066  1.00 13.12 ? 22   GLN C CB  1 
ATOM   2270 C  CG  . GLN C 1 22  ? -23.181 65.340 31.317  1.00 13.22 ? 22   GLN C CG  1 
ATOM   2271 C  CD  . GLN C 1 22  ? -24.629 65.616 30.943  1.00 10.81 ? 22   GLN C CD  1 
ATOM   2272 O  OE1 . GLN C 1 22  ? -25.562 65.206 31.661  1.00 13.20 ? 22   GLN C OE1 1 
ATOM   2273 N  NE2 . GLN C 1 22  ? -24.831 66.348 29.870  1.00 12.41 ? 22   GLN C NE2 1 
ATOM   2274 N  N   . LYS C 1 23  ? -19.829 65.133 33.171  1.00 19.68 ? 23   LYS C N   1 
ATOM   2275 C  CA  . LYS C 1 23  ? -19.092 66.028 34.052  1.00 23.01 ? 23   LYS C CA  1 
ATOM   2276 C  C   . LYS C 1 23  ? -19.783 67.369 34.226  1.00 19.47 ? 23   LYS C C   1 
ATOM   2277 O  O   . LYS C 1 23  ? -19.844 67.991 35.294  1.00 22.76 ? 23   LYS C O   1 
ATOM   2278 C  CB  . LYS C 1 23  ? -17.687 66.158 33.456  1.00 32.48 ? 23   LYS C CB  1 
ATOM   2279 C  CG  . LYS C 1 23  ? -16.638 67.123 33.955  1.00 40.55 ? 23   LYS C CG  1 
ATOM   2280 C  CD  . LYS C 1 23  ? -15.459 67.226 32.980  1.00 51.70 ? 23   LYS C CD  1 
ATOM   2281 C  CE  . LYS C 1 23  ? -14.190 67.756 33.603  1.00 54.91 ? 23   LYS C CE  1 
ATOM   2282 N  NZ  . LYS C 1 23  ? -13.107 68.161 32.659  1.00 63.99 ? 23   LYS C NZ  1 
ATOM   2283 N  N   . GLU C 1 24  ? -20.317 67.856 33.126  1.00 17.21 ? 24   GLU C N   1 
ATOM   2284 C  CA  . GLU C 1 24  ? -20.824 69.194 32.921  1.00 17.84 ? 24   GLU C CA  1 
ATOM   2285 C  C   . GLU C 1 24  ? -22.247 69.119 32.405  1.00 16.98 ? 24   GLU C C   1 
ATOM   2286 O  O   . GLU C 1 24  ? -22.456 68.400 31.432  1.00 17.11 ? 24   GLU C O   1 
ATOM   2287 C  CB  . GLU C 1 24  ? -20.008 69.933 31.851  1.00 23.79 ? 24   GLU C CB  1 
ATOM   2288 C  CG  . GLU C 1 24  ? -18.533 69.917 32.207  1.00 31.20 ? 24   GLU C CG  1 
ATOM   2289 C  CD  . GLU C 1 24  ? -18.239 71.326 32.702  1.00 41.24 ? 24   GLU C CD  1 
ATOM   2290 O  OE1 . GLU C 1 24  ? -17.818 72.121 31.836  1.00 62.27 ? 24   GLU C OE1 1 
ATOM   2291 O  OE2 . GLU C 1 24  ? -18.471 71.568 33.904  1.00 60.85 ? 24   GLU C OE2 1 
ATOM   2292 N  N   . SER C 1 25  ? -23.190 69.837 32.977  1.00 18.22 ? 25   SER C N   1 
ATOM   2293 C  CA  . SER C 1 25  ? -24.565 69.705 32.504  1.00 17.39 ? 25   SER C CA  1 
ATOM   2294 C  C   . SER C 1 25  ? -24.733 70.102 31.061  1.00 16.13 ? 25   SER C C   1 
ATOM   2295 O  O   . SER C 1 25  ? -25.649 69.601 30.421  1.00 17.23 ? 25   SER C O   1 
ATOM   2296 C  CB  . SER C 1 25  ? -25.521 70.502 33.420  1.00 21.98 ? 25   SER C CB  1 
ATOM   2297 O  OG  . SER C 1 25  ? -25.104 71.845 33.601  1.00 33.49 ? 25   SER C OG  1 
ATOM   2298 N  N   . ASN C 1 26  ? -23.907 71.005 30.550  1.00 14.06 ? 26   ASN C N   1 
ATOM   2299 C  CA  . ASN C 1 26  ? -24.014 71.384 29.136  1.00 13.87 ? 26   ASN C CA  1 
ATOM   2300 C  C   . ASN C 1 26  ? -22.962 70.676 28.309  1.00 12.99 ? 26   ASN C C   1 
ATOM   2301 O  O   . ASN C 1 26  ? -22.675 71.141 27.186  1.00 14.71 ? 26   ASN C O   1 
ATOM   2302 C  CB  . ASN C 1 26  ? -23.853 72.893 29.010  1.00 14.17 ? 26   ASN C CB  1 
ATOM   2303 C  CG  . ASN C 1 26  ? -25.030 73.629 29.642  1.00 11.17 ? 26   ASN C CG  1 
ATOM   2304 O  OD1 . ASN C 1 26  ? -26.138 73.075 29.754  1.00 16.61 ? 26   ASN C OD1 1 
ATOM   2305 N  ND2 . ASN C 1 26  ? -24.819 74.872 29.994  1.00 14.21 ? 26   ASN C ND2 1 
ATOM   2306 N  N   . GLY C 1 27  ? -22.364 69.599 28.800  1.00 13.28 ? 27   GLY C N   1 
ATOM   2307 C  CA  . GLY C 1 27  ? -21.311 68.903 28.072  1.00 13.44 ? 27   GLY C CA  1 
ATOM   2308 C  C   . GLY C 1 27  ? -21.686 67.485 27.658  1.00 12.18 ? 27   GLY C C   1 
ATOM   2309 O  O   . GLY C 1 27  ? -22.841 67.077 27.857  1.00 13.12 ? 27   GLY C O   1 
ATOM   2310 N  N   . PRO C 1 28  ? -20.757 66.759 27.040  1.00 12.05 ? 28   PRO C N   1 
ATOM   2311 C  CA  . PRO C 1 28  ? -20.993 65.427 26.547  1.00 12.09 ? 28   PRO C CA  1 
ATOM   2312 C  C   . PRO C 1 28  ? -21.170 64.418 27.679  1.00 12.04 ? 28   PRO C C   1 
ATOM   2313 O  O   . PRO C 1 28  ? -20.797 64.613 28.844  1.00 12.91 ? 28   PRO C O   1 
ATOM   2314 C  CB  . PRO C 1 28  ? -19.730 65.062 25.784  1.00 13.81 ? 28   PRO C CB  1 
ATOM   2315 C  CG  . PRO C 1 28  ? -18.760 66.165 25.958  1.00 17.34 ? 28   PRO C CG  1 
ATOM   2316 C  CD  . PRO C 1 28  ? -19.392 67.264 26.729  1.00 14.80 ? 28   PRO C CD  1 
ATOM   2317 N  N   . VAL C 1 29  ? -21.763 63.293 27.279  1.00 11.91 ? 29   VAL C N   1 
ATOM   2318 C  CA  . VAL C 1 29  ? -21.981 62.158 28.186  1.00 10.39 ? 29   VAL C CA  1 
ATOM   2319 C  C   . VAL C 1 29  ? -21.055 61.042 27.738  1.00 10.80 ? 29   VAL C C   1 
ATOM   2320 O  O   . VAL C 1 29  ? -21.101 60.670 26.563  1.00 13.07 ? 29   VAL C O   1 
ATOM   2321 C  CB  . VAL C 1 29  ? -23.452 61.697 28.179  1.00 10.87 ? 29   VAL C CB  1 
ATOM   2322 C  CG1 . VAL C 1 29  ? -23.698 60.519 29.137  1.00 11.07 ? 29   VAL C CG1 1 
ATOM   2323 C  CG2 . VAL C 1 29  ? -24.389 62.843 28.577  1.00 12.01 ? 29   VAL C CG2 1 
ATOM   2324 N  N   . LYS C 1 30  ? -20.269 60.502 28.653  1.00 11.01 ? 30   LYS C N   1 
ATOM   2325 C  CA  . LYS C 1 30  ? -19.472 59.291 28.353  1.00 11.22 ? 30   LYS C CA  1 
ATOM   2326 C  C   . LYS C 1 30  ? -20.372 58.077 28.549  1.00 11.01 ? 30   LYS C C   1 
ATOM   2327 O  O   . LYS C 1 30  ? -21.098 57.994 29.541  1.00 12.38 ? 30   LYS C O   1 
ATOM   2328 C  CB  . LYS C 1 30  ? -18.265 59.256 29.301  1.00 13.38 ? 30   LYS C CB  1 
ATOM   2329 C  CG  . LYS C 1 30  ? -17.253 60.361 29.055  1.00 18.51 ? 30   LYS C CG  1 
ATOM   2330 C  CD  . LYS C 1 30  ? -16.073 60.310 30.008  1.00 23.14 ? 30   LYS C CD  1 
ATOM   2331 C  CE  . LYS C 1 30  ? -15.127 61.475 29.729  1.00 30.18 ? 30   LYS C CE  1 
ATOM   2332 N  NZ  . LYS C 1 30  ? -14.553 62.060 30.963  1.00 47.37 ? 30   LYS C NZ  1 
ATOM   2333 N  N   . VAL C 1 31  ? -20.376 57.109 27.657  1.00 10.71 ? 31   VAL C N   1 
ATOM   2334 C  CA  . VAL C 1 31  ? -21.194 55.917 27.724  1.00 11.06 ? 31   VAL C CA  1 
ATOM   2335 C  C   . VAL C 1 31  ? -20.280 54.709 27.633  1.00 10.83 ? 31   VAL C C   1 
ATOM   2336 O  O   . VAL C 1 31  ? -19.567 54.589 26.608  1.00 13.99 ? 31   VAL C O   1 
ATOM   2337 C  CB  . VAL C 1 31  ? -22.232 55.901 26.596  1.00 11.25 ? 31   VAL C CB  1 
ATOM   2338 C  CG1 . VAL C 1 31  ? -23.149 54.695 26.655  1.00 12.65 ? 31   VAL C CG1 1 
ATOM   2339 C  CG2 . VAL C 1 31  ? -23.043 57.226 26.581  1.00 11.88 ? 31   VAL C CG2 1 
ATOM   2340 N  N   . TRP C 1 32  ? -20.275 53.854 28.618  1.00 10.40 ? 32   TRP C N   1 
ATOM   2341 C  CA  . TRP C 1 32  ? -19.305 52.734 28.502  1.00 11.11 ? 32   TRP C CA  1 
ATOM   2342 C  C   . TRP C 1 32  ? -19.801 51.503 29.236  1.00 12.51 ? 32   TRP C C   1 
ATOM   2343 O  O   . TRP C 1 32  ? -20.583 51.612 30.198  1.00 12.37 ? 32   TRP C O   1 
ATOM   2344 C  CB  . TRP C 1 32  ? -17.928 53.123 29.008  1.00 14.18 ? 32   TRP C CB  1 
ATOM   2345 C  CG  . TRP C 1 32  ? -17.806 53.221 30.504  1.00 14.11 ? 32   TRP C CG  1 
ATOM   2346 C  CD1 . TRP C 1 32  ? -17.264 52.275 31.338  1.00 15.79 ? 32   TRP C CD1 1 
ATOM   2347 C  CD2 . TRP C 1 32  ? -18.234 54.298 31.346  1.00 15.44 ? 32   TRP C CD2 1 
ATOM   2348 N  NE1 . TRP C 1 32  ? -17.316 52.709 32.637  1.00 18.13 ? 32   TRP C NE1 1 
ATOM   2349 C  CE2 . TRP C 1 32  ? -17.912 53.948 32.670  1.00 16.41 ? 32   TRP C CE2 1 
ATOM   2350 C  CE3 . TRP C 1 32  ? -18.846 55.529 31.123  1.00 15.60 ? 32   TRP C CE3 1 
ATOM   2351 C  CZ2 . TRP C 1 32  ? -18.182 54.763 33.763  1.00 18.55 ? 32   TRP C CZ2 1 
ATOM   2352 C  CZ3 . TRP C 1 32  ? -19.119 56.356 32.214  1.00 15.46 ? 32   TRP C CZ3 1 
ATOM   2353 C  CH2 . TRP C 1 32  ? -18.785 55.971 33.518  1.00 18.41 ? 32   TRP C CH2 1 
ATOM   2354 N  N   . GLY C 1 33  ? -19.353 50.337 28.822  1.00 11.22 ? 33   GLY C N   1 
ATOM   2355 C  CA  . GLY C 1 33  ? -19.744 49.096 29.512  1.00 10.92 ? 33   GLY C CA  1 
ATOM   2356 C  C   . GLY C 1 33  ? -19.599 47.957 28.527  1.00 11.41 ? 33   GLY C C   1 
ATOM   2357 O  O   . GLY C 1 33  ? -18.780 48.023 27.616  1.00 12.58 ? 33   GLY C O   1 
ATOM   2358 N  N   . SER C 1 34  ? -20.424 46.913 28.713  1.00 12.08 ? 34   SER C N   1 
ATOM   2359 C  CA  . SER C 1 34  ? -20.264 45.730 27.908  1.00 12.85 ? 34   SER C CA  1 
ATOM   2360 C  C   . SER C 1 34  ? -21.586 44.986 27.885  1.00 11.93 ? 34   SER C C   1 
ATOM   2361 O  O   . SER C 1 34  ? -22.244 44.930 28.928  1.00 14.38 ? 34   SER C O   1 
ATOM   2362 C  CB  . SER C 1 34  ? -19.171 44.821 28.502  1.00 14.81 ? 34   SER C CB  1 
ATOM   2363 O  OG  . SER C 1 34  ? -18.932 43.755 27.603  1.00 22.69 ? 34   SER C OG  1 
ATOM   2364 N  N   . ILE C 1 35  ? -21.915 44.448 26.716  1.00 11.86 ? 35   ILE C N   1 
ATOM   2365 C  CA  . ILE C 1 35  ? -23.094 43.623 26.516  1.00 12.29 ? 35   ILE C CA  1 
ATOM   2366 C  C   . ILE C 1 35  ? -22.650 42.273 25.984  1.00 12.45 ? 35   ILE C C   1 
ATOM   2367 O  O   . ILE C 1 35  ? -21.865 42.310 25.036  1.00 15.85 ? 35   ILE C O   1 
ATOM   2368 C  CB  . ILE C 1 35  ? -24.115 44.279 25.562  1.00 12.20 ? 35   ILE C CB  1 
ATOM   2369 C  CG1 . ILE C 1 35  ? -24.433 45.718 26.026  1.00 15.91 ? 35   ILE C CG1 1 
ATOM   2370 C  CG2 . ILE C 1 35  ? -25.332 43.376 25.442  1.00 13.83 ? 35   ILE C CG2 1 
ATOM   2371 C  CD1 . ILE C 1 35  ? -25.205 46.527 24.997  1.00 17.86 ? 35   ILE C CD1 1 
ATOM   2372 N  N   . LYS C 1 36  ? -23.115 41.180 26.555  1.00 13.26 ? 36   LYS C N   1 
ATOM   2373 C  CA  . LYS C 1 36  ? -22.656 39.890 26.024  1.00 12.97 ? 36   LYS C CA  1 
ATOM   2374 C  C   . LYS C 1 36  ? -23.837 39.103 25.522  1.00 13.75 ? 36   LYS C C   1 
ATOM   2375 O  O   . LYS C 1 36  ? -25.002 39.485 25.668  1.00 13.73 ? 36   LYS C O   1 
ATOM   2376 C  CB  . LYS C 1 36  ? -21.898 39.111 27.090  1.00 17.11 ? 36   LYS C CB  1 
ATOM   2377 C  CG  . LYS C 1 36  ? -22.802 38.652 28.217  1.00 23.83 ? 36   LYS C CG  1 
ATOM   2378 C  CD  . LYS C 1 36  ? -22.198 37.356 28.743  1.00 35.90 ? 36   LYS C CD  1 
ATOM   2379 C  CE  . LYS C 1 36  ? -21.644 37.344 30.138  1.00 42.95 ? 36   LYS C CE  1 
ATOM   2380 N  NZ  . LYS C 1 36  ? -20.841 36.089 30.346  1.00 38.67 ? 36   LYS C NZ  1 
ATOM   2381 N  N   . GLY C 1 37  ? -23.533 37.959 24.923  1.00 13.69 ? 37   GLY C N   1 
ATOM   2382 C  CA  . GLY C 1 37  ? -24.601 37.098 24.465  1.00 13.76 ? 37   GLY C CA  1 
ATOM   2383 C  C   . GLY C 1 37  ? -25.085 37.458 23.082  1.00 12.85 ? 37   GLY C C   1 
ATOM   2384 O  O   . GLY C 1 37  ? -26.073 36.874 22.636  1.00 16.01 ? 37   GLY C O   1 
ATOM   2385 N  N   . LEU C 1 38  ? -24.450 38.401 22.379  1.00 13.41 ? 38   LEU C N   1 
ATOM   2386 C  CA  . LEU C 1 38  ? -24.940 38.849 21.078  1.00 13.82 ? 38   LEU C CA  1 
ATOM   2387 C  C   . LEU C 1 38  ? -24.347 38.012 19.973  1.00 13.26 ? 38   LEU C C   1 
ATOM   2388 O  O   . LEU C 1 38  ? -23.252 37.442 20.108  1.00 18.63 ? 38   LEU C O   1 
ATOM   2389 C  CB  . LEU C 1 38  ? -24.438 40.294 20.898  1.00 12.89 ? 38   LEU C CB  1 
ATOM   2390 C  CG  . LEU C 1 38  ? -25.133 41.337 21.804  1.00 12.90 ? 38   LEU C CG  1 
ATOM   2391 C  CD1 . LEU C 1 38  ? -24.293 42.587 21.919  1.00 14.62 ? 38   LEU C CD1 1 
ATOM   2392 C  CD2 . LEU C 1 38  ? -26.524 41.620 21.243  1.00 13.82 ? 38   LEU C CD2 1 
ATOM   2393 N  N   . THR C 1 39  ? -25.023 38.001 18.825  1.00 13.63 ? 39   THR C N   1 
ATOM   2394 C  CA  . THR C 1 39  ? -24.370 37.493 17.621  1.00 15.59 ? 39   THR C CA  1 
ATOM   2395 C  C   . THR C 1 39  ? -23.274 38.456 17.173  1.00 15.78 ? 39   THR C C   1 
ATOM   2396 O  O   . THR C 1 39  ? -23.304 39.689 17.342  1.00 15.44 ? 39   THR C O   1 
ATOM   2397 C  CB  . THR C 1 39  ? -25.361 37.353 16.450  1.00 15.40 ? 39   THR C CB  1 
ATOM   2398 O  OG1 . THR C 1 39  ? -26.019 38.603 16.252  1.00 17.45 ? 39   THR C OG1 1 
ATOM   2399 C  CG2 . THR C 1 39  ? -26.483 36.356 16.702  1.00 19.36 ? 39   THR C CG2 1 
ATOM   2400 N  N   . GLU C 1 40  ? -22.233 37.913 16.528  1.00 16.29 ? 40   GLU C N   1 
ATOM   2401 C  CA  . GLU C 1 40  ? -21.140 38.729 16.047  1.00 15.96 ? 40   GLU C CA  1 
ATOM   2402 C  C   . GLU C 1 40  ? -21.667 39.750 15.049  1.00 16.71 ? 40   GLU C C   1 
ATOM   2403 O  O   . GLU C 1 40  ? -22.470 39.389 14.160  1.00 18.88 ? 40   GLU C O   1 
ATOM   2404 C  CB  . GLU C 1 40  ? -20.062 37.832 15.420  1.00 17.36 ? 40   GLU C CB  1 
ATOM   2405 C  CG  . GLU C 1 40  ? -18.857 38.556 14.894  1.00 20.06 ? 40   GLU C CG  1 
ATOM   2406 C  CD  . GLU C 1 40  ? -17.759 37.650 14.363  1.00 20.77 ? 40   GLU C CD  1 
ATOM   2407 O  OE1 . GLU C 1 40  ? -17.784 36.423 14.623  1.00 20.00 ? 40   GLU C OE1 1 
ATOM   2408 O  OE2 . GLU C 1 40  ? -16.869 38.218 13.671  1.00 27.47 ? 40   GLU C OE2 1 
ATOM   2409 N  N   . GLY C 1 41  ? -21.195 40.979 15.166  1.00 15.86 ? 41   GLY C N   1 
ATOM   2410 C  CA  . GLY C 1 41  ? -21.576 42.036 14.228  1.00 16.85 ? 41   GLY C CA  1 
ATOM   2411 C  C   . GLY C 1 41  ? -22.315 43.186 14.886  1.00 14.41 ? 41   GLY C C   1 
ATOM   2412 O  O   . GLY C 1 41  ? -22.278 43.375 16.104  1.00 14.42 ? 41   GLY C O   1 
ATOM   2413 N  N   . LEU C 1 42  ? -23.003 43.986 14.092  1.00 15.10 ? 42   LEU C N   1 
ATOM   2414 C  CA  . LEU C 1 42  ? -23.637 45.211 14.557  1.00 15.08 ? 42   LEU C CA  1 
ATOM   2415 C  C   . LEU C 1 42  ? -25.015 45.020 15.153  1.00 13.68 ? 42   LEU C C   1 
ATOM   2416 O  O   . LEU C 1 42  ? -25.826 44.229 14.642  1.00 13.83 ? 42   LEU C O   1 
ATOM   2417 C  CB  . LEU C 1 42  ? -23.774 46.166 13.358  1.00 17.28 ? 42   LEU C CB  1 
ATOM   2418 C  CG  . LEU C 1 42  ? -22.484 46.763 12.790  1.00 21.23 ? 42   LEU C CG  1 
ATOM   2419 C  CD1 . LEU C 1 42  ? -22.797 47.565 11.531  1.00 24.63 ? 42   LEU C CD1 1 
ATOM   2420 C  CD2 . LEU C 1 42  ? -21.772 47.607 13.826  1.00 26.64 ? 42   LEU C CD2 1 
ATOM   2421 N  N   . HIS C 1 43  ? -25.308 45.788 16.202  1.00 11.77 ? 43   HIS C N   1 
ATOM   2422 C  CA  . HIS C 1 43  ? -26.582 45.713 16.872  1.00 11.26 ? 43   HIS C CA  1 
ATOM   2423 C  C   . HIS C 1 43  ? -27.054 47.117 17.212  1.00 11.23 ? 43   HIS C C   1 
ATOM   2424 O  O   . HIS C 1 43  ? -26.325 47.874 17.878  1.00 11.72 ? 43   HIS C O   1 
ATOM   2425 C  CB  . HIS C 1 43  ? -26.458 44.932 18.197  1.00 12.69 ? 43   HIS C CB  1 
ATOM   2426 C  CG  . HIS C 1 43  ? -26.192 43.473 17.895  1.00 11.26 ? 43   HIS C CG  1 
ATOM   2427 N  ND1 . HIS C 1 43  ? -27.220 42.570 17.665  1.00 11.95 ? 43   HIS C ND1 1 
ATOM   2428 C  CD2 . HIS C 1 43  ? -25.040 42.769 17.742  1.00 12.09 ? 43   HIS C CD2 1 
ATOM   2429 C  CE1 . HIS C 1 43  ? -26.695 41.356 17.398  1.00 12.94 ? 43   HIS C CE1 1 
ATOM   2430 N  NE2 . HIS C 1 43  ? -25.373 41.454 17.431  1.00 13.48 ? 43   HIS C NE2 1 
ATOM   2431 N  N   . GLY C 1 44  ? -28.258 47.488 16.806  1.00 10.69 ? 44   GLY C N   1 
ATOM   2432 C  CA  . GLY C 1 44  ? -28.779 48.812 17.085  1.00 9.80  ? 44   GLY C CA  1 
ATOM   2433 C  C   . GLY C 1 44  ? -28.831 49.110 18.587  1.00 10.44 ? 44   GLY C C   1 
ATOM   2434 O  O   . GLY C 1 44  ? -29.099 48.215 19.393  1.00 11.09 ? 44   GLY C O   1 
ATOM   2435 N  N   . PHE C 1 45  ? -28.604 50.373 18.934  1.00 9.64  ? 45   PHE C N   1 
ATOM   2436 C  CA  . PHE C 1 45  ? -28.412 50.801 20.319  1.00 8.40  ? 45   PHE C CA  1 
ATOM   2437 C  C   . PHE C 1 45  ? -29.161 52.105 20.536  1.00 9.29  ? 45   PHE C C   1 
ATOM   2438 O  O   . PHE C 1 45  ? -28.721 53.123 19.958  1.00 9.95  ? 45   PHE C O   1 
ATOM   2439 C  CB  . PHE C 1 45  ? -26.910 50.949 20.534  1.00 10.04 ? 45   PHE C CB  1 
ATOM   2440 C  CG  . PHE C 1 45  ? -26.450 51.130 21.957  1.00 9.70  ? 45   PHE C CG  1 
ATOM   2441 C  CD1 . PHE C 1 45  ? -26.896 50.329 22.995  1.00 12.83 ? 45   PHE C CD1 1 
ATOM   2442 C  CD2 . PHE C 1 45  ? -25.519 52.110 22.260  1.00 11.82 ? 45   PHE C CD2 1 
ATOM   2443 C  CE1 . PHE C 1 45  ? -26.409 50.513 24.296  1.00 13.21 ? 45   PHE C CE1 1 
ATOM   2444 C  CE2 . PHE C 1 45  ? -25.028 52.297 23.538  1.00 12.00 ? 45   PHE C CE2 1 
ATOM   2445 C  CZ  . PHE C 1 45  ? -25.449 51.472 24.561  1.00 12.91 ? 45   PHE C CZ  1 
ATOM   2446 N  N   . HIS C 1 46  ? -30.256 52.068 21.274  1.00 8.59  ? 46   HIS C N   1 
ATOM   2447 C  CA  . HIS C 1 46  ? -31.161 53.215 21.320  1.00 8.93  ? 46   HIS C CA  1 
ATOM   2448 C  C   . HIS C 1 46  ? -31.623 53.545 22.735  1.00 8.00  ? 46   HIS C C   1 
ATOM   2449 O  O   . HIS C 1 46  ? -31.802 52.610 23.517  1.00 10.72 ? 46   HIS C O   1 
ATOM   2450 C  CB  . HIS C 1 46  ? -32.494 52.892 20.588  1.00 10.51 ? 46   HIS C CB  1 
ATOM   2451 C  CG  . HIS C 1 46  ? -32.288 52.578 19.145  1.00 10.00 ? 46   HIS C CG  1 
ATOM   2452 N  ND1 . HIS C 1 46  ? -33.160 51.742 18.488  1.00 9.05  ? 46   HIS C ND1 1 
ATOM   2453 C  CD2 . HIS C 1 46  ? -31.362 52.979 18.237  1.00 9.17  ? 46   HIS C CD2 1 
ATOM   2454 C  CE1 . HIS C 1 46  ? -32.770 51.624 17.209  1.00 10.12 ? 46   HIS C CE1 1 
ATOM   2455 N  NE2 . HIS C 1 46  ? -31.678 52.364 17.022  1.00 10.32 ? 46   HIS C NE2 1 
ATOM   2456 N  N   . VAL C 1 47  ? -31.900 54.821 22.957  1.00 8.14  ? 47   VAL C N   1 
ATOM   2457 C  CA  . VAL C 1 47  ? -32.732 55.178 24.116  1.00 8.53  ? 47   VAL C CA  1 
ATOM   2458 C  C   . VAL C 1 47  ? -34.165 55.325 23.609  1.00 8.12  ? 47   VAL C C   1 
ATOM   2459 O  O   . VAL C 1 47  ? -34.415 56.132 22.691  1.00 9.72  ? 47   VAL C O   1 
ATOM   2460 C  CB  . VAL C 1 47  ? -32.305 56.467 24.814  1.00 8.37  ? 47   VAL C CB  1 
ATOM   2461 C  CG1 . VAL C 1 47  ? -33.206 56.734 26.019  1.00 9.63  ? 47   VAL C CG1 1 
ATOM   2462 C  CG2 . VAL C 1 47  ? -30.822 56.401 25.192  1.00 11.64 ? 47   VAL C CG2 1 
ATOM   2463 N  N   . HIS C 1 48  ? -35.069 54.522 24.138  1.00 8.89  ? 48   HIS C N   1 
ATOM   2464 C  CA  . HIS C 1 48  ? -36.497 54.559 23.855  1.00 8.34  ? 48   HIS C CA  1 
ATOM   2465 C  C   . HIS C 1 48  ? -37.168 55.433 24.900  1.00 8.29  ? 48   HIS C C   1 
ATOM   2466 O  O   . HIS C 1 48  ? -36.678 55.633 26.033  1.00 10.25 ? 48   HIS C O   1 
ATOM   2467 C  CB  . HIS C 1 48  ? -37.094 53.140 23.776  1.00 10.46 ? 48   HIS C CB  1 
ATOM   2468 C  CG  . HIS C 1 48  ? -36.715 52.479 22.473  1.00 8.85  ? 48   HIS C CG  1 
ATOM   2469 N  ND1 . HIS C 1 48  ? -37.719 52.203 21.553  1.00 8.80  ? 48   HIS C ND1 1 
ATOM   2470 C  CD2 . HIS C 1 48  ? -35.551 52.026 21.942  1.00 9.40  ? 48   HIS C CD2 1 
ATOM   2471 C  CE1 . HIS C 1 48  ? -37.155 51.630 20.496  1.00 9.24  ? 48   HIS C CE1 1 
ATOM   2472 N  NE2 . HIS C 1 48  ? -35.844 51.492 20.696  1.00 9.19  ? 48   HIS C NE2 1 
ATOM   2473 N  N   . GLU C 1 49  ? -38.313 56.006 24.531  1.00 8.48  ? 49   GLU C N   1 
ATOM   2474 C  CA  . GLU C 1 49  ? -38.935 57.091 25.291  1.00 8.55  ? 49   GLU C CA  1 
ATOM   2475 C  C   . GLU C 1 49  ? -39.348 56.729 26.696  1.00 9.70  ? 49   GLU C C   1 
ATOM   2476 O  O   . GLU C 1 49  ? -39.113 57.521 27.623  1.00 10.32 ? 49   GLU C O   1 
ATOM   2477 C  CB  . GLU C 1 49  ? -40.190 57.513 24.484  1.00 9.67  ? 49   GLU C CB  1 
ATOM   2478 C  CG  . GLU C 1 49  ? -40.822 58.774 25.135  1.00 11.41 ? 49   GLU C CG  1 
ATOM   2479 C  CD  . GLU C 1 49  ? -41.976 59.353 24.371  1.00 12.95 ? 49   GLU C CD  1 
ATOM   2480 O  OE1 . GLU C 1 49  ? -42.338 58.792 23.304  1.00 16.50 ? 49   GLU C OE1 1 
ATOM   2481 O  OE2 . GLU C 1 49  ? -42.520 60.378 24.825  1.00 16.11 ? 49   GLU C OE2 1 
ATOM   2482 N  N   . PHE C 1 50  ? -39.993 55.583 26.902  1.00 8.87  ? 50   PHE C N   1 
ATOM   2483 C  CA  . PHE C 1 50  ? -40.545 55.284 28.235  1.00 9.15  ? 50   PHE C CA  1 
ATOM   2484 C  C   . PHE C 1 50  ? -39.722 54.279 29.011  1.00 7.97  ? 50   PHE C C   1 
ATOM   2485 O  O   . PHE C 1 50  ? -39.241 53.293 28.422  1.00 10.27 ? 50   PHE C O   1 
ATOM   2486 C  CB  . PHE C 1 50  ? -41.982 54.728 28.082  1.00 9.70  ? 50   PHE C CB  1 
ATOM   2487 C  CG  . PHE C 1 50  ? -42.836 55.786 27.373  1.00 10.44 ? 50   PHE C CG  1 
ATOM   2488 C  CD1 . PHE C 1 50  ? -43.076 56.997 27.993  1.00 12.30 ? 50   PHE C CD1 1 
ATOM   2489 C  CD2 . PHE C 1 50  ? -43.369 55.525 26.109  1.00 13.55 ? 50   PHE C CD2 1 
ATOM   2490 C  CE1 . PHE C 1 50  ? -43.830 57.978 27.362  1.00 14.54 ? 50   PHE C CE1 1 
ATOM   2491 C  CE2 . PHE C 1 50  ? -44.113 56.511 25.454  1.00 15.68 ? 50   PHE C CE2 1 
ATOM   2492 C  CZ  . PHE C 1 50  ? -44.322 57.735 26.080  1.00 15.93 ? 50   PHE C CZ  1 
ATOM   2493 N  N   . GLY C 1 51  ? -39.604 54.527 30.324  1.00 8.49  ? 51   GLY C N   1 
ATOM   2494 C  CA  . GLY C 1 51  ? -38.944 53.607 31.215  1.00 9.91  ? 51   GLY C CA  1 
ATOM   2495 C  C   . GLY C 1 51  ? -39.997 52.650 31.782  1.00 9.33  ? 51   GLY C C   1 
ATOM   2496 O  O   . GLY C 1 51  ? -40.042 52.436 32.992  1.00 10.15 ? 51   GLY C O   1 
ATOM   2497 N  N   . ASP C 1 52  ? -40.800 52.102 30.875  1.00 9.81  ? 52   ASP C N   1 
ATOM   2498 C  CA  . ASP C 1 52  ? -41.899 51.212 31.214  1.00 9.51  ? 52   ASP C CA  1 
ATOM   2499 C  C   . ASP C 1 52  ? -41.536 49.793 30.722  1.00 10.36 ? 52   ASP C C   1 
ATOM   2500 O  O   . ASP C 1 52  ? -41.600 49.597 29.524  1.00 11.26 ? 52   ASP C O   1 
ATOM   2501 C  CB  . ASP C 1 52  ? -43.186 51.730 30.579  1.00 10.65 ? 52   ASP C CB  1 
ATOM   2502 C  CG  . ASP C 1 52  ? -44.411 50.900 30.877  1.00 11.19 ? 52   ASP C CG  1 
ATOM   2503 O  OD1 . ASP C 1 52  ? -44.241 49.748 31.299  1.00 11.13 ? 52   ASP C OD1 1 
ATOM   2504 O  OD2 . ASP C 1 52  ? -45.556 51.397 30.727  1.00 13.05 ? 52   ASP C OD2 1 
ATOM   2505 N  N   . ASN C 1 53  ? -41.204 48.940 31.693  1.00 10.14 ? 53   ASN C N   1 
ATOM   2506 C  CA  . ASN C 1 53  ? -40.874 47.561 31.271  1.00 12.83 ? 53   ASN C CA  1 
ATOM   2507 C  C   . ASN C 1 53  ? -41.967 46.612 31.779  1.00 9.98  ? 53   ASN C C   1 
ATOM   2508 O  O   . ASN C 1 53  ? -41.692 45.418 31.987  1.00 12.86 ? 53   ASN C O   1 
ATOM   2509 C  CB  . ASN C 1 53  ? -39.453 47.214 31.689  1.00 14.53 ? 53   ASN C CB  1 
ATOM   2510 C  CG  . ASN C 1 53  ? -38.356 48.042 30.998  1.00 14.37 ? 53   ASN C CG  1 
ATOM   2511 O  OD1 . ASN C 1 53  ? -37.163 48.005 31.373  1.00 21.29 ? 53   ASN C OD1 1 
ATOM   2512 N  ND2 . ASN C 1 53  ? -38.587 48.906 29.973  1.00 20.34 ? 53   ASN C ND2 1 
ATOM   2513 N  N   . THR C 1 54  ? -43.194 47.149 31.956  1.00 9.26  ? 54   THR C N   1 
ATOM   2514 C  CA  . THR C 1 54  ? -44.291 46.250 32.366  1.00 10.93 ? 54   THR C CA  1 
ATOM   2515 C  C   . THR C 1 54  ? -44.594 45.209 31.288  1.00 10.85 ? 54   THR C C   1 
ATOM   2516 O  O   . THR C 1 54  ? -45.073 44.107 31.631  1.00 12.99 ? 54   THR C O   1 
ATOM   2517 C  CB  . THR C 1 54  ? -45.597 47.022 32.652  1.00 11.06 ? 54   THR C CB  1 
ATOM   2518 O  OG1 . THR C 1 54  ? -45.990 47.758 31.480  1.00 13.12 ? 54   THR C OG1 1 
ATOM   2519 C  CG2 . THR C 1 54  ? -45.423 47.997 33.825  1.00 11.85 ? 54   THR C CG2 1 
ATOM   2520 N  N   . ALA C 1 55  ? -44.285 45.527 30.036  1.00 11.46 ? 55   ALA C N   1 
ATOM   2521 C  CA  . ALA C 1 55  ? -44.414 44.573 28.907  1.00 11.58 ? 55   ALA C CA  1 
ATOM   2522 C  C   . ALA C 1 55  ? -43.021 44.388 28.313  1.00 11.67 ? 55   ALA C C   1 
ATOM   2523 O  O   . ALA C 1 55  ? -42.791 44.441 27.091  1.00 15.91 ? 55   ALA C O   1 
ATOM   2524 C  CB  . ALA C 1 55  ? -45.429 45.041 27.894  1.00 13.05 ? 55   ALA C CB  1 
ATOM   2525 N  N   . GLY C 1 56  ? -42.061 44.160 29.179  1.00 12.65 ? 56   GLY C N   1 
ATOM   2526 C  CA  . GLY C 1 56  ? -40.697 43.928 28.690  1.00 12.34 ? 56   GLY C CA  1 
ATOM   2527 C  C   . GLY C 1 56  ? -40.203 45.114 27.916  1.00 12.06 ? 56   GLY C C   1 
ATOM   2528 O  O   . GLY C 1 56  ? -40.495 46.266 28.269  1.00 14.86 ? 56   GLY C O   1 
ATOM   2529 N  N   . CYS C 1 57  ? -39.448 44.893 26.816  1.00 11.10 ? 57   CYS C N   1 
ATOM   2530 C  CA  . CYS C 1 57  ? -38.914 46.010 26.101  1.00 10.60 ? 57   CYS C CA  1 
ATOM   2531 C  C   . CYS C 1 57  ? -39.968 46.668 25.209  1.00 10.21 ? 57   CYS C C   1 
ATOM   2532 O  O   . CYS C 1 57  ? -39.712 47.782 24.738  1.00 10.97 ? 57   CYS C O   1 
ATOM   2533 C  CB  . CYS C 1 57  ? -37.721 45.562 25.252  1.00 11.48 ? 57   CYS C CB  1 
ATOM   2534 S  SG  . CYS C 1 57  ? -36.442 44.747 26.257  1.00 15.09 ? 57   CYS C SG  1 
ATOM   2535 N  N   . THR C 1 58  ? -41.097 46.019 24.957  1.00 10.53 ? 58   THR C N   1 
ATOM   2536 C  CA  . THR C 1 58  ? -42.062 46.620 24.038  1.00 10.69 ? 58   THR C CA  1 
ATOM   2537 C  C   . THR C 1 58  ? -42.671 47.883 24.571  1.00 10.49 ? 58   THR C C   1 
ATOM   2538 O  O   . THR C 1 58  ? -42.875 48.852 23.838  1.00 11.06 ? 58   THR C O   1 
ATOM   2539 C  CB  . THR C 1 58  ? -43.145 45.572 23.684  1.00 10.09 ? 58   THR C CB  1 
ATOM   2540 O  OG1 . THR C 1 58  ? -42.439 44.489 23.073  1.00 12.27 ? 58   THR C OG1 1 
ATOM   2541 C  CG2 . THR C 1 58  ? -44.166 46.181 22.704  1.00 11.78 ? 58   THR C CG2 1 
ATOM   2542 N  N   . SER C 1 59  ? -42.967 47.896 25.884  1.00 10.65 ? 59   SER C N   1 
ATOM   2543 C  CA  . SER C 1 59  ? -43.615 49.067 26.459  1.00 9.16  ? 59   SER C CA  1 
ATOM   2544 C  C   . SER C 1 59  ? -42.695 50.278 26.595  1.00 9.53  ? 59   SER C C   1 
ATOM   2545 O  O   . SER C 1 59  ? -43.108 51.350 27.064  1.00 10.85 ? 59   SER C O   1 
ATOM   2546 C  CB  . SER C 1 59  ? -44.204 48.671 27.822  1.00 10.19 ? 59   SER C CB  1 
ATOM   2547 O  OG  . SER C 1 59  ? -43.343 47.835 28.553  1.00 10.89 ? 59   SER C OG  1 
ATOM   2548 N  N   . ALA C 1 60  ? -41.446 50.174 26.166  1.00 9.33  ? 60   ALA C N   1 
ATOM   2549 C  CA  . ALA C 1 60  ? -40.556 51.340 26.099  1.00 10.31 ? 60   ALA C CA  1 
ATOM   2550 C  C   . ALA C 1 60  ? -40.982 52.306 25.002  1.00 11.07 ? 60   ALA C C   1 
ATOM   2551 O  O   . ALA C 1 60  ? -40.480 53.445 24.974  1.00 10.21 ? 60   ALA C O   1 
ATOM   2552 C  CB  . ALA C 1 60  ? -39.112 50.884 25.898  1.00 11.66 ? 60   ALA C CB  1 
ATOM   2553 N  N   . GLY C 1 61  ? -41.875 51.887 24.086  1.00 9.94  ? 61   GLY C N   1 
ATOM   2554 C  CA  . GLY C 1 61  ? -42.337 52.881 23.112  1.00 10.63 ? 61   GLY C CA  1 
ATOM   2555 C  C   . GLY C 1 61  ? -41.260 53.172 22.064  1.00 9.10  ? 61   GLY C C   1 
ATOM   2556 O  O   . GLY C 1 61  ? -40.388 52.334 21.805  1.00 10.33 ? 61   GLY C O   1 
ATOM   2557 N  N   . PRO C 1 62  ? -41.368 54.312 21.397  1.00 10.28 ? 62   PRO C N   1 
ATOM   2558 C  CA  . PRO C 1 62  ? -40.521 54.656 20.246  1.00 10.23 ? 62   PRO C CA  1 
ATOM   2559 C  C   . PRO C 1 62  ? -39.205 55.242 20.678  1.00 10.05 ? 62   PRO C C   1 
ATOM   2560 O  O   . PRO C 1 62  ? -38.875 55.348 21.866  1.00 10.72 ? 62   PRO C O   1 
ATOM   2561 C  CB  . PRO C 1 62  ? -41.427 55.707 19.547  1.00 12.02 ? 62   PRO C CB  1 
ATOM   2562 C  CG  . PRO C 1 62  ? -42.058 56.438 20.692  1.00 13.63 ? 62   PRO C CG  1 
ATOM   2563 C  CD  . PRO C 1 62  ? -42.396 55.359 21.689  1.00 13.70 ? 62   PRO C CD  1 
ATOM   2564 N  N   . HIS C 1 63  ? -38.362 55.625 19.701  1.00 10.81 ? 63   HIS C N   1 
ATOM   2565 C  CA  . HIS C 1 63  ? -37.126 56.304 20.060  1.00 10.16 ? 63   HIS C CA  1 
ATOM   2566 C  C   . HIS C 1 63  ? -37.419 57.593 20.837  1.00 9.18  ? 63   HIS C C   1 
ATOM   2567 O  O   . HIS C 1 63  ? -38.394 58.307 20.529  1.00 11.26 ? 63   HIS C O   1 
ATOM   2568 C  CB  . HIS C 1 63  ? -36.314 56.705 18.830  1.00 11.15 ? 63   HIS C CB  1 
ATOM   2569 C  CG  . HIS C 1 63  ? -35.918 55.513 18.013  1.00 9.58  ? 63   HIS C CG  1 
ATOM   2570 N  ND1 . HIS C 1 63  ? -35.171 55.615 16.884  1.00 10.22 ? 63   HIS C ND1 1 
ATOM   2571 C  CD2 . HIS C 1 63  ? -36.236 54.181 18.156  1.00 9.63  ? 63   HIS C CD2 1 
ATOM   2572 C  CE1 . HIS C 1 63  ? -35.005 54.399 16.362  1.00 11.13 ? 63   HIS C CE1 1 
ATOM   2573 N  NE2 . HIS C 1 63  ? -35.639 53.487 17.114  1.00 10.49 ? 63   HIS C NE2 1 
ATOM   2574 N  N   . PHE C 1 64  ? -36.541 57.844 21.812  1.00 9.11  ? 64   PHE C N   1 
ATOM   2575 C  CA  . PHE C 1 64  ? -36.707 59.132 22.523  1.00 9.17  ? 64   PHE C CA  1 
ATOM   2576 C  C   . PHE C 1 64  ? -36.382 60.301 21.604  1.00 8.62  ? 64   PHE C C   1 
ATOM   2577 O  O   . PHE C 1 64  ? -35.303 60.398 21.003  1.00 10.76 ? 64   PHE C O   1 
ATOM   2578 C  CB  . PHE C 1 64  ? -35.779 59.092 23.746  1.00 10.13 ? 64   PHE C CB  1 
ATOM   2579 C  CG  . PHE C 1 64  ? -35.827 60.361 24.578  1.00 10.55 ? 64   PHE C CG  1 
ATOM   2580 C  CD1 . PHE C 1 64  ? -37.047 60.944 24.921  1.00 11.94 ? 64   PHE C CD1 1 
ATOM   2581 C  CD2 . PHE C 1 64  ? -34.667 60.962 25.015  1.00 12.45 ? 64   PHE C CD2 1 
ATOM   2582 C  CE1 . PHE C 1 64  ? -37.106 62.098 25.652  1.00 12.33 ? 64   PHE C CE1 1 
ATOM   2583 C  CE2 . PHE C 1 64  ? -34.697 62.120 25.794  1.00 12.00 ? 64   PHE C CE2 1 
ATOM   2584 C  CZ  . PHE C 1 64  ? -35.921 62.666 26.152  1.00 12.90 ? 64   PHE C CZ  1 
ATOM   2585 N  N   . ASN C 1 65  ? -37.343 61.200 21.407  1.00 9.96  ? 65   ASN C N   1 
ATOM   2586 C  CA  . ASN C 1 65  ? -37.260 62.237 20.383  1.00 12.20 ? 65   ASN C CA  1 
ATOM   2587 C  C   . ASN C 1 65  ? -37.937 63.524 20.853  1.00 12.67 ? 65   ASN C C   1 
ATOM   2588 O  O   . ASN C 1 65  ? -38.888 63.966 20.185  1.00 14.38 ? 65   ASN C O   1 
ATOM   2589 C  CB  . ASN C 1 65  ? -37.963 61.711 19.115  1.00 11.73 ? 65   ASN C CB  1 
ATOM   2590 C  CG  . ASN C 1 65  ? -37.814 62.685 17.952  1.00 10.62 ? 65   ASN C CG  1 
ATOM   2591 O  OD1 . ASN C 1 65  ? -36.858 63.455 17.842  1.00 13.80 ? 65   ASN C OD1 1 
ATOM   2592 N  ND2 . ASN C 1 65  ? -38.711 62.576 16.986  1.00 15.24 ? 65   ASN C ND2 1 
ATOM   2593 N  N   . PRO C 1 66  ? -37.427 64.102 21.919  1.00 12.08 ? 66   PRO C N   1 
ATOM   2594 C  CA  . PRO C 1 66  ? -38.056 65.326 22.461  1.00 13.57 ? 66   PRO C CA  1 
ATOM   2595 C  C   . PRO C 1 66  ? -37.855 66.555 21.568  1.00 14.95 ? 66   PRO C C   1 
ATOM   2596 O  O   . PRO C 1 66  ? -38.512 67.584 21.747  1.00 17.80 ? 66   PRO C O   1 
ATOM   2597 C  CB  . PRO C 1 66  ? -37.327 65.573 23.778  1.00 12.44 ? 66   PRO C CB  1 
ATOM   2598 C  CG  . PRO C 1 66  ? -35.964 64.979 23.508  1.00 12.30 ? 66   PRO C CG  1 
ATOM   2599 C  CD  . PRO C 1 66  ? -36.213 63.735 22.706  1.00 11.80 ? 66   PRO C CD  1 
ATOM   2600 N  N   . LEU C 1 67  ? -36.939 66.505 20.623  1.00 14.78 ? 67   LEU C N   1 
ATOM   2601 C  CA  . LEU C 1 67  ? -36.637 67.676 19.791  1.00 17.18 ? 67   LEU C CA  1 
ATOM   2602 C  C   . LEU C 1 67  ? -37.309 67.527 18.442  1.00 17.90 ? 67   LEU C C   1 
ATOM   2603 O  O   . LEU C 1 67  ? -37.089 68.346 17.515  1.00 20.67 ? 67   LEU C O   1 
ATOM   2604 C  CB  . LEU C 1 67  ? -35.123 67.851 19.701  1.00 18.88 ? 67   LEU C CB  1 
ATOM   2605 C  CG  . LEU C 1 67  ? -34.360 67.860 21.038  1.00 16.75 ? 67   LEU C CG  1 
ATOM   2606 C  CD1 . LEU C 1 67  ? -32.869 68.104 20.787  1.00 17.75 ? 67   LEU C CD1 1 
ATOM   2607 C  CD2 . LEU C 1 67  ? -34.957 68.884 21.994  1.00 18.74 ? 67   LEU C CD2 1 
ATOM   2608 N  N   . SER C 1 68  ? -38.148 66.500 18.270  1.00 17.69 ? 68   SER C N   1 
ATOM   2609 C  CA  . SER C 1 68  ? -38.925 66.348 17.042  1.00 19.43 ? 68   SER C CA  1 
ATOM   2610 C  C   . SER C 1 68  ? -38.108 66.339 15.737  1.00 16.86 ? 68   SER C C   1 
ATOM   2611 O  O   . SER C 1 68  ? -38.379 67.016 14.720  1.00 21.61 ? 68   SER C O   1 
ATOM   2612 C  CB  . SER C 1 68  ? -39.959 67.489 16.994  1.00 22.86 ? 68   SER C CB  1 
ATOM   2613 O  OG  . SER C 1 68  ? -40.947 67.334 18.026  1.00 26.48 ? 68   SER C OG  1 
ATOM   2614 N  N   . ARG C 1 69  ? -37.098 65.485 15.745  1.00 16.44 ? 69   ARG C N   1 
ATOM   2615 C  CA  . ARG C 1 69  ? -36.233 65.286 14.590  1.00 16.96 ? 69   ARG C CA  1 
ATOM   2616 C  C   . ARG C 1 69  ? -36.537 63.948 13.917  1.00 15.35 ? 69   ARG C C   1 
ATOM   2617 O  O   . ARG C 1 69  ? -37.301 63.153 14.452  1.00 16.24 ? 69   ARG C O   1 
ATOM   2618 C  CB  . ARG C 1 69  ? -34.748 65.334 15.000  1.00 15.99 ? 69   ARG C CB  1 
ATOM   2619 C  CG  . ARG C 1 69  ? -34.358 66.632 15.720  1.00 17.49 ? 69   ARG C CG  1 
ATOM   2620 C  CD  . ARG C 1 69  ? -34.541 67.851 14.864  1.00 17.67 ? 69   ARG C CD  1 
ATOM   2621 N  NE  . ARG C 1 69  ? -33.697 67.946 13.684  1.00 19.64 ? 69   ARG C NE  1 
ATOM   2622 C  CZ  . ARG C 1 69  ? -32.477 68.415 13.482  1.00 18.68 ? 69   ARG C CZ  1 
ATOM   2623 N  NH1 . ARG C 1 69  ? -31.738 68.932 14.478  1.00 21.40 ? 69   ARG C NH1 1 
ATOM   2624 N  NH2 . ARG C 1 69  ? -31.915 68.390 12.269  1.00 20.33 ? 69   ARG C NH2 1 
ATOM   2625 N  N   . LYS C 1 70  ? -35.910 63.739 12.772  1.00 15.52 ? 70   LYS C N   1 
ATOM   2626 C  CA  . LYS C 1 70  ? -35.978 62.436 12.108  1.00 13.87 ? 70   LYS C CA  1 
ATOM   2627 C  C   . LYS C 1 70  ? -34.847 61.535 12.585  1.00 12.86 ? 70   LYS C C   1 
ATOM   2628 O  O   . LYS C 1 70  ? -33.820 61.958 13.106  1.00 15.35 ? 70   LYS C O   1 
ATOM   2629 C  CB  . LYS C 1 70  ? -35.862 62.621 10.585  1.00 15.76 ? 70   LYS C CB  1 
ATOM   2630 C  CG  . LYS C 1 70  ? -37.047 63.424 10.060  1.00 24.12 ? 70   LYS C CG  1 
ATOM   2631 C  CD  . LYS C 1 70  ? -38.388 62.767 10.291  1.00 31.39 ? 70   LYS C CD  1 
ATOM   2632 C  CE  . LYS C 1 70  ? -39.494 63.622 9.649   1.00 40.27 ? 70   LYS C CE  1 
ATOM   2633 N  NZ  . LYS C 1 70  ? -40.827 63.173 10.151  1.00 46.37 ? 70   LYS C NZ  1 
ATOM   2634 N  N   . HIS C 1 71  ? -35.026 60.237 12.343  1.00 13.25 ? 71   HIS C N   1 
ATOM   2635 C  CA  . HIS C 1 71  ? -34.035 59.239 12.754  1.00 12.48 ? 71   HIS C CA  1 
ATOM   2636 C  C   . HIS C 1 71  ? -32.715 59.387 12.034  1.00 12.72 ? 71   HIS C C   1 
ATOM   2637 O  O   . HIS C 1 71  ? -32.688 59.655 10.811  1.00 14.62 ? 71   HIS C O   1 
ATOM   2638 C  CB  . HIS C 1 71  ? -34.630 57.844 12.494  1.00 11.35 ? 71   HIS C CB  1 
ATOM   2639 C  CG  . HIS C 1 71  ? -33.680 56.762 12.920  1.00 11.13 ? 71   HIS C CG  1 
ATOM   2640 N  ND1 . HIS C 1 71  ? -33.486 56.486 14.275  1.00 11.00 ? 71   HIS C ND1 1 
ATOM   2641 C  CD2 . HIS C 1 71  ? -32.860 55.941 12.214  1.00 13.26 ? 71   HIS C CD2 1 
ATOM   2642 C  CE1 . HIS C 1 71  ? -32.580 55.517 14.376  1.00 10.72 ? 71   HIS C CE1 1 
ATOM   2643 N  NE2 . HIS C 1 71  ? -32.201 55.154 13.141  1.00 11.91 ? 71   HIS C NE2 1 
ATOM   2644 N  N   . GLY C 1 72  ? -31.592 59.179 12.718  1.00 11.42 ? 72   GLY C N   1 
ATOM   2645 C  CA  . GLY C 1 72  ? -30.311 59.143 12.053  1.00 13.07 ? 72   GLY C CA  1 
ATOM   2646 C  C   . GLY C 1 72  ? -29.346 58.341 12.941  1.00 12.10 ? 72   GLY C C   1 
ATOM   2647 O  O   . GLY C 1 72  ? -29.724 57.662 13.892  1.00 13.09 ? 72   GLY C O   1 
ATOM   2648 N  N   . GLY C 1 73  ? -28.073 58.487 12.571  1.00 13.81 ? 73   GLY C N   1 
ATOM   2649 C  CA  . GLY C 1 73  ? -26.961 57.968 13.363  1.00 16.60 ? 73   GLY C CA  1 
ATOM   2650 C  C   . GLY C 1 73  ? -26.485 58.981 14.395  1.00 13.87 ? 73   GLY C C   1 
ATOM   2651 O  O   . GLY C 1 73  ? -26.829 60.162 14.283  1.00 14.54 ? 73   GLY C O   1 
ATOM   2652 N  N   . PRO C 1 74  ? -25.721 58.570 15.380  1.00 15.04 ? 74   PRO C N   1 
ATOM   2653 C  CA  . PRO C 1 74  ? -25.298 59.450 16.458  1.00 15.74 ? 74   PRO C CA  1 
ATOM   2654 C  C   . PRO C 1 74  ? -24.473 60.631 15.978  1.00 16.98 ? 74   PRO C C   1 
ATOM   2655 O  O   . PRO C 1 74  ? -24.486 61.683 16.615  1.00 18.81 ? 74   PRO C O   1 
ATOM   2656 C  CB  . PRO C 1 74  ? -24.499 58.529 17.424  1.00 15.74 ? 74   PRO C CB  1 
ATOM   2657 C  CG  . PRO C 1 74  ? -24.136 57.358 16.582  1.00 16.44 ? 74   PRO C CG  1 
ATOM   2658 C  CD  . PRO C 1 74  ? -25.243 57.176 15.587  1.00 16.28 ? 74   PRO C CD  1 
ATOM   2659 N  N   . LYS C 1 75  ? -23.763 60.530 14.847  1.00 17.55 ? 75   LYS C N   1 
ATOM   2660 C  CA  . LYS C 1 75  ? -22.927 61.629 14.424  1.00 21.42 ? 75   LYS C CA  1 
ATOM   2661 C  C   . LYS C 1 75  ? -23.621 62.426 13.325  1.00 17.84 ? 75   LYS C C   1 
ATOM   2662 O  O   . LYS C 1 75  ? -22.955 63.330 12.817  1.00 25.34 ? 75   LYS C O   1 
ATOM   2663 C  CB  . LYS C 1 75  ? -21.558 61.106 13.959  1.00 26.32 ? 75   LYS C CB  1 
ATOM   2664 C  CG  . LYS C 1 75  ? -20.656 60.546 15.064  1.00 31.47 ? 75   LYS C CG  1 
ATOM   2665 C  CD  . LYS C 1 75  ? -20.535 61.466 16.273  1.00 35.30 ? 75   LYS C CD  1 
ATOM   2666 C  CE  . LYS C 1 75  ? -19.782 60.831 17.426  1.00 37.93 ? 75   LYS C CE  1 
ATOM   2667 N  NZ  . LYS C 1 75  ? -20.150 61.396 18.766  1.00 46.12 ? 75   LYS C NZ  1 
ATOM   2668 N  N   . ASP C 1 76  ? -24.871 62.149 12.958  1.00 15.82 ? 76   ASP C N   1 
ATOM   2669 C  CA  . ASP C 1 76  ? -25.693 63.023 12.126  1.00 17.19 ? 76   ASP C CA  1 
ATOM   2670 C  C   . ASP C 1 76  ? -26.250 64.190 12.934  1.00 15.43 ? 76   ASP C C   1 
ATOM   2671 O  O   . ASP C 1 76  ? -26.553 64.007 14.131  1.00 16.43 ? 76   ASP C O   1 
ATOM   2672 C  CB  . ASP C 1 76  ? -26.879 62.252 11.514  1.00 19.13 ? 76   ASP C CB  1 
ATOM   2673 C  CG  . ASP C 1 76  ? -26.402 61.183 10.548  1.00 21.54 ? 76   ASP C CG  1 
ATOM   2674 O  OD1 . ASP C 1 76  ? -25.417 61.455 9.856   1.00 27.15 ? 76   ASP C OD1 1 
ATOM   2675 O  OD2 . ASP C 1 76  ? -26.993 60.082 10.503  1.00 19.42 ? 76   ASP C OD2 1 
ATOM   2676 N  N   . GLU C 1 77  ? -26.417 65.359 12.299  1.00 15.87 ? 77   GLU C N   1 
ATOM   2677 C  CA  . GLU C 1 77  ? -27.094 66.455 13.008  1.00 14.96 ? 77   GLU C CA  1 
ATOM   2678 C  C   . GLU C 1 77  ? -28.577 66.160 13.081  1.00 15.14 ? 77   GLU C C   1 
ATOM   2679 O  O   . GLU C 1 77  ? -29.239 66.496 14.073  1.00 15.56 ? 77   GLU C O   1 
ATOM   2680 C  CB  . GLU C 1 77  ? -26.753 67.781 12.302  1.00 18.00 ? 77   GLU C CB  1 
ATOM   2681 C  CG  . GLU C 1 77  ? -27.166 68.960 13.168  1.00 16.95 ? 77   GLU C CG  1 
ATOM   2682 C  CD  . GLU C 1 77  ? -28.588 69.411 12.949  1.00 17.66 ? 77   GLU C CD  1 
ATOM   2683 O  OE1 . GLU C 1 77  ? -29.213 68.959 11.951  1.00 22.64 ? 77   GLU C OE1 1 
ATOM   2684 O  OE2 . GLU C 1 77  ? -29.117 70.163 13.805  1.00 23.63 ? 77   GLU C OE2 1 
ATOM   2685 N  N   . GLU C 1 78  ? -29.132 65.556 12.025  1.00 15.42 ? 78   GLU C N   1 
ATOM   2686 C  CA  . GLU C 1 78  ? -30.543 65.161 12.081  1.00 15.39 ? 78   GLU C CA  1 
ATOM   2687 C  C   . GLU C 1 78  ? -30.647 63.754 12.670  1.00 14.08 ? 78   GLU C C   1 
ATOM   2688 O  O   . GLU C 1 78  ? -30.355 62.748 12.028  1.00 16.44 ? 78   GLU C O   1 
ATOM   2689 C  CB  . GLU C 1 78  ? -31.188 65.159 10.717  1.00 20.56 ? 78   GLU C CB  1 
ATOM   2690 C  CG  . GLU C 1 78  ? -32.655 64.753 10.694  1.00 24.13 ? 78   GLU C CG  1 
ATOM   2691 C  CD  . GLU C 1 78  ? -33.517 65.997 10.857  1.00 23.55 ? 78   GLU C CD  1 
ATOM   2692 O  OE1 . GLU C 1 78  ? -33.164 67.030 10.231  1.00 29.15 ? 78   GLU C OE1 1 
ATOM   2693 O  OE2 . GLU C 1 78  ? -34.523 65.942 11.574  1.00 30.70 ? 78   GLU C OE2 1 
ATOM   2694 N  N   . ARG C 1 79  ? -31.019 63.724 13.946  1.00 12.28 ? 79   ARG C N   1 
ATOM   2695 C  CA  . ARG C 1 79  ? -31.153 62.464 14.671  1.00 11.06 ? 79   ARG C CA  1 
ATOM   2696 C  C   . ARG C 1 79  ? -32.100 62.677 15.846  1.00 10.42 ? 79   ARG C C   1 
ATOM   2697 O  O   . ARG C 1 79  ? -32.322 63.794 16.303  1.00 12.01 ? 79   ARG C O   1 
ATOM   2698 C  CB  . ARG C 1 79  ? -29.836 61.952 15.253  1.00 11.01 ? 79   ARG C CB  1 
ATOM   2699 C  CG  . ARG C 1 79  ? -29.133 62.991 16.138  1.00 12.25 ? 79   ARG C CG  1 
ATOM   2700 C  CD  . ARG C 1 79  ? -27.932 62.359 16.853  1.00 12.74 ? 79   ARG C CD  1 
ATOM   2701 N  NE  . ARG C 1 79  ? -28.366 61.753 18.123  1.00 11.27 ? 79   ARG C NE  1 
ATOM   2702 C  CZ  . ARG C 1 79  ? -27.496 61.429 19.085  1.00 11.13 ? 79   ARG C CZ  1 
ATOM   2703 N  NH1 . ARG C 1 79  ? -26.202 61.622 18.902  1.00 12.91 ? 79   ARG C NH1 1 
ATOM   2704 N  NH2 . ARG C 1 79  ? -27.953 60.905 20.213  1.00 11.56 ? 79   ARG C NH2 1 
ATOM   2705 N  N   . HIS C 1 80  ? -32.625 61.574 16.325  1.00 10.92 ? 80   HIS C N   1 
ATOM   2706 C  CA  . HIS C 1 80  ? -33.346 61.586 17.581  1.00 12.09 ? 80   HIS C CA  1 
ATOM   2707 C  C   . HIS C 1 80  ? -32.382 61.645 18.768  1.00 10.58 ? 80   HIS C C   1 
ATOM   2708 O  O   . HIS C 1 80  ? -31.247 61.159 18.638  1.00 11.73 ? 80   HIS C O   1 
ATOM   2709 C  CB  . HIS C 1 80  ? -34.108 60.259 17.741  1.00 10.96 ? 80   HIS C CB  1 
ATOM   2710 C  CG  . HIS C 1 80  ? -35.127 59.980 16.676  1.00 11.33 ? 80   HIS C CG  1 
ATOM   2711 N  ND1 . HIS C 1 80  ? -35.428 58.750 16.120  1.00 10.74 ? 80   HIS C ND1 1 
ATOM   2712 C  CD2 . HIS C 1 80  ? -35.929 60.878 16.070  1.00 11.70 ? 80   HIS C CD2 1 
ATOM   2713 C  CE1 . HIS C 1 80  ? -36.400 58.906 15.232  1.00 11.01 ? 80   HIS C CE1 1 
ATOM   2714 N  NE2 . HIS C 1 80  ? -36.749 60.215 15.177  1.00 11.66 ? 80   HIS C NE2 1 
ATOM   2715 N  N   . VAL C 1 81  ? -32.815 62.152 19.912  1.00 11.00 ? 81   VAL C N   1 
ATOM   2716 C  CA  . VAL C 1 81  ? -31.925 62.120 21.084  1.00 10.77 ? 81   VAL C CA  1 
ATOM   2717 C  C   . VAL C 1 81  ? -31.489 60.674 21.354  1.00 9.69  ? 81   VAL C C   1 
ATOM   2718 O  O   . VAL C 1 81  ? -30.318 60.427 21.658  1.00 10.71 ? 81   VAL C O   1 
ATOM   2719 C  CB  . VAL C 1 81  ? -32.575 62.764 22.329  1.00 9.29  ? 81   VAL C CB  1 
ATOM   2720 C  CG1 . VAL C 1 81  ? -31.724 62.512 23.585  1.00 10.91 ? 81   VAL C CG1 1 
ATOM   2721 C  CG2 . VAL C 1 81  ? -32.708 64.276 22.121  1.00 13.02 ? 81   VAL C CG2 1 
ATOM   2722 N  N   . GLY C 1 82  ? -32.418 59.730 21.212  1.00 9.38  ? 82   GLY C N   1 
ATOM   2723 C  CA  . GLY C 1 82  ? -32.095 58.338 21.568  1.00 9.94  ? 82   GLY C CA  1 
ATOM   2724 C  C   . GLY C 1 82  ? -31.314 57.592 20.516  1.00 9.09  ? 82   GLY C C   1 
ATOM   2725 O  O   . GLY C 1 82  ? -31.109 56.378 20.664  1.00 10.14 ? 82   GLY C O   1 
ATOM   2726 N  N   . ASP C 1 83  ? -30.807 58.223 19.452  1.00 10.05 ? 83   ASP C N   1 
ATOM   2727 C  CA  . ASP C 1 83  ? -30.132 57.508 18.356  1.00 9.65  ? 83   ASP C CA  1 
ATOM   2728 C  C   . ASP C 1 83  ? -28.658 57.304 18.623  1.00 10.63 ? 83   ASP C C   1 
ATOM   2729 O  O   . ASP C 1 83  ? -27.806 58.106 18.165  1.00 11.98 ? 83   ASP C O   1 
ATOM   2730 C  CB  . ASP C 1 83  ? -30.353 58.314 17.054  1.00 10.90 ? 83   ASP C CB  1 
ATOM   2731 C  CG  . ASP C 1 83  ? -31.756 58.184 16.540  1.00 10.80 ? 83   ASP C CG  1 
ATOM   2732 O  OD1 . ASP C 1 83  ? -32.542 57.336 17.033  1.00 11.38 ? 83   ASP C OD1 1 
ATOM   2733 O  OD2 . ASP C 1 83  ? -32.121 58.961 15.618  1.00 11.52 ? 83   ASP C OD2 1 
ATOM   2734 N  N   . LEU C 1 84  ? -28.322 56.237 19.359  1.00 10.56 ? 84   LEU C N   1 
ATOM   2735 C  CA  . LEU C 1 84  ? -26.933 55.966 19.695  1.00 11.10 ? 84   LEU C CA  1 
ATOM   2736 C  C   . LEU C 1 84  ? -26.311 54.979 18.718  1.00 13.40 ? 84   LEU C C   1 
ATOM   2737 O  O   . LEU C 1 84  ? -25.229 54.455 19.025  1.00 14.25 ? 84   LEU C O   1 
ATOM   2738 C  CB  . LEU C 1 84  ? -26.795 55.502 21.136  1.00 10.93 ? 84   LEU C CB  1 
ATOM   2739 C  CG  . LEU C 1 84  ? -27.197 56.560 22.176  1.00 11.43 ? 84   LEU C CG  1 
ATOM   2740 C  CD1 . LEU C 1 84  ? -27.144 55.960 23.580  1.00 11.88 ? 84   LEU C CD1 1 
ATOM   2741 C  CD2 . LEU C 1 84  ? -26.305 57.778 22.043  1.00 14.32 ? 84   LEU C CD2 1 
ATOM   2742 N  N   . GLY C 1 85  ? -26.944 54.741 17.553  1.00 11.78 ? 85   GLY C N   1 
ATOM   2743 C  CA  . GLY C 1 85  ? -26.150 54.028 16.540  1.00 12.21 ? 85   GLY C CA  1 
ATOM   2744 C  C   . GLY C 1 85  ? -26.189 52.529 16.725  1.00 11.42 ? 85   GLY C C   1 
ATOM   2745 O  O   . GLY C 1 85  ? -27.221 51.895 16.994  1.00 12.26 ? 85   GLY C O   1 
ATOM   2746 N  N   . ASN C 1 86  ? -25.010 51.956 16.577  1.00 13.29 ? 86   ASN C N   1 
ATOM   2747 C  CA  . ASN C 1 86  ? -24.786 50.522 16.696  1.00 12.48 ? 86   ASN C CA  1 
ATOM   2748 C  C   . ASN C 1 86  ? -23.680 50.196 17.671  1.00 12.32 ? 86   ASN C C   1 
ATOM   2749 O  O   . ASN C 1 86  ? -22.706 50.934 17.708  1.00 16.81 ? 86   ASN C O   1 
ATOM   2750 C  CB  . ASN C 1 86  ? -24.375 49.947 15.317  1.00 14.27 ? 86   ASN C CB  1 
ATOM   2751 C  CG  . ASN C 1 86  ? -25.553 49.909 14.373  1.00 11.86 ? 86   ASN C CG  1 
ATOM   2752 O  OD1 . ASN C 1 86  ? -26.559 49.278 14.659  1.00 12.76 ? 86   ASN C OD1 1 
ATOM   2753 N  ND2 . ASN C 1 86  ? -25.405 50.615 13.252  1.00 13.48 ? 86   ASN C ND2 1 
ATOM   2754 N  N   . VAL C 1 87  ? -23.782 49.114 18.434  1.00 13.66 ? 87   VAL C N   1 
ATOM   2755 C  CA  . VAL C 1 87  ? -22.626 48.507 19.098  1.00 12.90 ? 87   VAL C CA  1 
ATOM   2756 C  C   . VAL C 1 87  ? -22.149 47.341 18.231  1.00 12.71 ? 87   VAL C C   1 
ATOM   2757 O  O   . VAL C 1 87  ? -22.911 46.820 17.407  1.00 14.86 ? 87   VAL C O   1 
ATOM   2758 C  CB  . VAL C 1 87  ? -22.939 48.081 20.537  1.00 13.06 ? 87   VAL C CB  1 
ATOM   2759 C  CG1 . VAL C 1 87  ? -23.341 49.274 21.387  1.00 17.12 ? 87   VAL C CG1 1 
ATOM   2760 C  CG2 . VAL C 1 87  ? -24.030 46.997 20.597  1.00 13.88 ? 87   VAL C CG2 1 
ATOM   2761 N  N   . THR C 1 88  ? -20.911 46.921 18.391  1.00 14.26 ? 88   THR C N   1 
ATOM   2762 C  CA  . THR C 1 88  ? -20.347 45.820 17.645  1.00 14.15 ? 88   THR C CA  1 
ATOM   2763 C  C   . THR C 1 88  ? -19.928 44.685 18.568  1.00 13.06 ? 88   THR C C   1 
ATOM   2764 O  O   . THR C 1 88  ? -19.077 44.897 19.436  1.00 15.45 ? 88   THR C O   1 
ATOM   2765 C  CB  . THR C 1 88  ? -19.125 46.330 16.845  1.00 15.20 ? 88   THR C CB  1 
ATOM   2766 O  OG1 . THR C 1 88  ? -19.562 47.320 15.890  1.00 24.31 ? 88   THR C OG1 1 
ATOM   2767 C  CG2 . THR C 1 88  ? -18.501 45.175 16.076  1.00 20.09 ? 88   THR C CG2 1 
ATOM   2768 N  N   . ALA C 1 89  ? -20.544 43.514 18.346  1.00 14.78 ? 89   ALA C N   1 
ATOM   2769 C  CA  . ALA C 1 89  ? -20.165 42.316 19.103  1.00 15.27 ? 89   ALA C CA  1 
ATOM   2770 C  C   . ALA C 1 89  ? -19.047 41.596 18.379  1.00 15.43 ? 89   ALA C C   1 
ATOM   2771 O  O   . ALA C 1 89  ? -19.074 41.458 17.147  1.00 17.60 ? 89   ALA C O   1 
ATOM   2772 C  CB  . ALA C 1 89  ? -21.358 41.398 19.281  1.00 15.47 ? 89   ALA C CB  1 
ATOM   2773 N  N   . ASP C 1 90  ? -18.073 41.139 19.158  1.00 16.60 ? 90   ASP C N   1 
ATOM   2774 C  CA  . ASP C 1 90  ? -16.950 40.396 18.592  1.00 18.16 ? 90   ASP C CA  1 
ATOM   2775 C  C   . ASP C 1 90  ? -17.316 38.934 18.405  1.00 18.67 ? 90   ASP C C   1 
ATOM   2776 O  O   . ASP C 1 90  ? -18.475 38.577 18.588  1.00 18.29 ? 90   ASP C O   1 
ATOM   2777 C  CB  . ASP C 1 90  ? -15.723 40.529 19.480  1.00 20.55 ? 90   ASP C CB  1 
ATOM   2778 C  CG  . ASP C 1 90  ? -15.821 39.938 20.858  1.00 20.17 ? 90   ASP C CG  1 
ATOM   2779 O  OD1 . ASP C 1 90  ? -16.674 39.086 21.125  1.00 18.70 ? 90   ASP C OD1 1 
ATOM   2780 O  OD2 . ASP C 1 90  ? -14.984 40.364 21.700  1.00 23.90 ? 90   ASP C OD2 1 
ATOM   2781 N  N   . LYS C 1 91  ? -16.311 38.126 18.055  1.00 19.19 ? 91   LYS C N   1 
ATOM   2782 C  CA  . LYS C 1 91  ? -16.552 36.720 17.745  1.00 20.63 ? 91   LYS C CA  1 
ATOM   2783 C  C   . LYS C 1 91  ? -17.021 35.924 18.956  1.00 19.61 ? 91   LYS C C   1 
ATOM   2784 O  O   . LYS C 1 91  ? -17.604 34.855 18.792  1.00 23.98 ? 91   LYS C O   1 
ATOM   2785 C  CB  . LYS C 1 91  ? -15.284 36.099 17.166  1.00 22.67 ? 91   LYS C CB  1 
ATOM   2786 C  CG  . LYS C 1 91  ? -14.136 36.111 18.183  1.00 28.08 ? 91   LYS C CG  1 
ATOM   2787 C  CD  . LYS C 1 91  ? -12.933 35.401 17.615  1.00 33.49 ? 91   LYS C CD  1 
ATOM   2788 C  CE  . LYS C 1 91  ? -11.840 35.195 18.650  1.00 38.09 ? 91   LYS C CE  1 
ATOM   2789 N  NZ  . LYS C 1 91  ? -11.933 33.824 19.233  1.00 51.12 ? 91   LYS C NZ  1 
ATOM   2790 N  N   . ASP C 1 92  ? -16.763 36.429 20.160  1.00 19.89 ? 92   ASP C N   1 
ATOM   2791 C  CA  . ASP C 1 92  ? -17.263 35.781 21.378  1.00 20.12 ? 92   ASP C CA  1 
ATOM   2792 C  C   . ASP C 1 92  ? -18.618 36.336 21.831  1.00 19.24 ? 92   ASP C C   1 
ATOM   2793 O  O   . ASP C 1 92  ? -19.094 36.011 22.923  1.00 21.54 ? 92   ASP C O   1 
ATOM   2794 C  CB  . ASP C 1 92  ? -16.244 35.929 22.511  1.00 21.87 ? 92   ASP C CB  1 
ATOM   2795 C  CG  . ASP C 1 92  ? -14.912 35.319 22.127  1.00 26.39 ? 92   ASP C CG  1 
ATOM   2796 O  OD1 . ASP C 1 92  ? -14.895 34.156 21.646  1.00 35.04 ? 92   ASP C OD1 1 
ATOM   2797 O  OD2 . ASP C 1 92  ? -13.861 35.974 22.295  1.00 34.66 ? 92   ASP C OD2 1 
ATOM   2798 N  N   . GLY C 1 93  ? -19.263 37.156 21.018  1.00 16.35 ? 93   GLY C N   1 
ATOM   2799 C  CA  . GLY C 1 93  ? -20.571 37.735 21.319  1.00 16.37 ? 93   GLY C CA  1 
ATOM   2800 C  C   . GLY C 1 93  ? -20.556 38.916 22.269  1.00 15.66 ? 93   GLY C C   1 
ATOM   2801 O  O   . GLY C 1 93  ? -21.604 39.311 22.818  1.00 14.70 ? 93   GLY C O   1 
ATOM   2802 N  N   . VAL C 1 94  ? -19.383 39.512 22.495  1.00 14.54 ? 94   VAL C N   1 
ATOM   2803 C  CA  . VAL C 1 94  ? -19.217 40.602 23.455  1.00 13.89 ? 94   VAL C CA  1 
ATOM   2804 C  C   . VAL C 1 94  ? -19.087 41.921 22.724  1.00 14.03 ? 94   VAL C C   1 
ATOM   2805 O  O   . VAL C 1 94  ? -18.247 42.124 21.852  1.00 15.30 ? 94   VAL C O   1 
ATOM   2806 C  CB  . VAL C 1 94  ? -17.962 40.401 24.321  1.00 15.11 ? 94   VAL C CB  1 
ATOM   2807 C  CG1 . VAL C 1 94  ? -17.704 41.586 25.248  1.00 17.54 ? 94   VAL C CG1 1 
ATOM   2808 C  CG2 . VAL C 1 94  ? -18.072 39.084 25.076  1.00 15.54 ? 94   VAL C CG2 1 
ATOM   2809 N  N   . ALA C 1 95  ? -19.949 42.852 23.101  1.00 13.80 ? 95   ALA C N   1 
ATOM   2810 C  CA  . ALA C 1 95  ? -19.870 44.230 22.593  1.00 12.81 ? 95   ALA C CA  1 
ATOM   2811 C  C   . ALA C 1 95  ? -19.359 45.103 23.735  1.00 12.68 ? 95   ALA C C   1 
ATOM   2812 O  O   . ALA C 1 95  ? -20.115 45.511 24.633  1.00 14.40 ? 95   ALA C O   1 
ATOM   2813 C  CB  . ALA C 1 95  ? -21.226 44.702 22.147  1.00 13.88 ? 95   ALA C CB  1 
ATOM   2814 N  N   . ASP C 1 96  ? -18.070 45.413 23.744  1.00 14.90 ? 96   ASP C N   1 
ATOM   2815 C  CA  . ASP C 1 96  ? -17.532 46.422 24.636  1.00 14.58 ? 96   ASP C CA  1 
ATOM   2816 C  C   . ASP C 1 96  ? -17.852 47.791 24.052  1.00 15.78 ? 96   ASP C C   1 
ATOM   2817 O  O   . ASP C 1 96  ? -17.738 48.037 22.836  1.00 20.66 ? 96   ASP C O   1 
ATOM   2818 C  CB  . ASP C 1 96  ? -16.032 46.182 24.814  1.00 19.38 ? 96   ASP C CB  1 
ATOM   2819 C  CG  . ASP C 1 96  ? -15.730 44.969 25.669  1.00 20.46 ? 96   ASP C CG  1 
ATOM   2820 O  OD1 . ASP C 1 96  ? -16.461 44.695 26.652  1.00 19.25 ? 96   ASP C OD1 1 
ATOM   2821 O  OD2 . ASP C 1 96  ? -14.752 44.247 25.365  1.00 30.93 ? 96   ASP C OD2 1 
ATOM   2822 N  N   . VAL C 1 97  ? -18.338 48.688 24.890  1.00 12.71 ? 97   VAL C N   1 
ATOM   2823 C  CA  . VAL C 1 97  ? -18.825 49.996 24.483  1.00 12.46 ? 97   VAL C CA  1 
ATOM   2824 C  C   . VAL C 1 97  ? -18.016 51.072 25.190  1.00 13.20 ? 97   VAL C C   1 
ATOM   2825 O  O   . VAL C 1 97  ? -17.870 51.032 26.401  1.00 13.42 ? 97   VAL C O   1 
ATOM   2826 C  CB  . VAL C 1 97  ? -20.303 50.192 24.841  1.00 13.25 ? 97   VAL C CB  1 
ATOM   2827 C  CG1 . VAL C 1 97  ? -20.815 51.585 24.464  1.00 16.69 ? 97   VAL C CG1 1 
ATOM   2828 C  CG2 . VAL C 1 97  ? -21.134 49.142 24.118  1.00 15.86 ? 97   VAL C CG2 1 
ATOM   2829 N  N   . SER C 1 98  ? -17.492 52.012 24.421  1.00 14.85 ? 98   SER C N   1 
ATOM   2830 C  CA  . SER C 1 98  ? -16.860 53.197 25.002  1.00 14.95 ? 98   SER C CA  1 
ATOM   2831 C  C   . SER C 1 98  ? -17.029 54.359 24.032  1.00 16.30 ? 98   SER C C   1 
ATOM   2832 O  O   . SER C 1 98  ? -16.190 54.434 23.112  1.00 19.21 ? 98   SER C O   1 
ATOM   2833 C  CB  . SER C 1 98  ? -15.378 53.058 25.346  1.00 21.31 ? 98   SER C CB  1 
ATOM   2834 O  OG  . SER C 1 98  ? -14.953 54.191 26.075  1.00 25.41 ? 98   SER C OG  1 
ATOM   2835 N  N   . ILE C 1 99  ? -18.064 55.139 24.257  1.00 14.66 ? 99   ILE C N   1 
ATOM   2836 C  CA  . ILE C 1 99  ? -18.287 56.271 23.360  1.00 13.93 ? 99   ILE C CA  1 
ATOM   2837 C  C   . ILE C 1 99  ? -18.574 57.536 24.140  1.00 12.95 ? 99   ILE C C   1 
ATOM   2838 O  O   . ILE C 1 99  ? -18.716 57.506 25.362  1.00 13.43 ? 99   ILE C O   1 
ATOM   2839 C  CB  . ILE C 1 99  ? -19.472 56.003 22.405  1.00 14.37 ? 99   ILE C CB  1 
ATOM   2840 C  CG1 . ILE C 1 99  ? -20.799 55.809 23.166  1.00 14.11 ? 99   ILE C CG1 1 
ATOM   2841 C  CG2 . ILE C 1 99  ? -19.142 54.804 21.518  1.00 17.68 ? 99   ILE C CG2 1 
ATOM   2842 C  CD1 . ILE C 1 99  ? -22.003 55.573 22.274  1.00 22.87 ? 99   ILE C CD1 1 
ATOM   2843 N  N   . GLU C 1 100 ? -18.662 58.657 23.408  1.00 14.02 ? 100  GLU C N   1 
ATOM   2844 C  CA  . GLU C 1 100 ? -19.106 59.921 23.961  1.00 13.18 ? 100  GLU C CA  1 
ATOM   2845 C  C   . GLU C 1 100 ? -20.241 60.410 23.067  1.00 12.89 ? 100  GLU C C   1 
ATOM   2846 O  O   . GLU C 1 100 ? -20.137 60.233 21.847  1.00 16.14 ? 100  GLU C O   1 
ATOM   2847 C  CB  . GLU C 1 100 ? -17.963 60.933 23.974  1.00 18.03 ? 100  GLU C CB  1 
ATOM   2848 C  CG  . GLU C 1 100 ? -16.953 60.536 25.058  1.00 22.19 ? 100  GLU C CG  1 
ATOM   2849 C  CD  . GLU C 1 100 ? -16.072 61.661 25.537  1.00 22.17 ? 100  GLU C CD  1 
ATOM   2850 O  OE1 . GLU C 1 100 ? -16.363 62.864 25.328  1.00 29.68 ? 100  GLU C OE1 1 
ATOM   2851 O  OE2 . GLU C 1 100 ? -15.013 61.334 26.171  1.00 34.65 ? 100  GLU C OE2 1 
ATOM   2852 N  N   . ASP C 1 101 ? -21.243 60.992 23.710  1.00 11.72 ? 101  ASP C N   1 
ATOM   2853 C  CA  . ASP C 1 101 ? -22.357 61.519 22.914  1.00 10.51 ? 101  ASP C CA  1 
ATOM   2854 C  C   . ASP C 1 101 ? -22.755 62.904 23.423  1.00 10.57 ? 101  ASP C C   1 
ATOM   2855 O  O   . ASP C 1 101 ? -22.783 63.081 24.646  1.00 12.49 ? 101  ASP C O   1 
ATOM   2856 C  CB  . ASP C 1 101 ? -23.572 60.578 22.989  1.00 11.26 ? 101  ASP C CB  1 
ATOM   2857 C  CG  . ASP C 1 101 ? -24.592 60.977 21.940  1.00 11.52 ? 101  ASP C CG  1 
ATOM   2858 O  OD1 . ASP C 1 101 ? -24.337 60.641 20.752  1.00 14.06 ? 101  ASP C OD1 1 
ATOM   2859 O  OD2 . ASP C 1 101 ? -25.631 61.603 22.267  1.00 11.83 ? 101  ASP C OD2 1 
ATOM   2860 N  N   . SER C 1 102 ? -23.023 63.818 22.501  1.00 10.71 ? 102  SER C N   1 
ATOM   2861 C  CA  . SER C 1 102 ? -23.313 65.192 22.879  1.00 12.30 ? 102  SER C CA  1 
ATOM   2862 C  C   . SER C 1 102 ? -24.771 65.592 22.648  1.00 11.51 ? 102  SER C C   1 
ATOM   2863 O  O   . SER C 1 102 ? -25.081 66.789 22.703  1.00 14.22 ? 102  SER C O   1 
ATOM   2864 C  CB  . SER C 1 102 ? -22.358 66.170 22.175  1.00 12.96 ? 102  SER C CB  1 
ATOM   2865 O  OG  . SER C 1 102 ? -21.038 66.038 22.709  1.00 16.73 ? 102  SER C OG  1 
ATOM   2866 N  N   . VAL C 1 103 ? -25.640 64.603 22.441  1.00 12.02 ? 103  VAL C N   1 
ATOM   2867 C  CA  . VAL C 1 103 ? -27.085 64.904 22.315  1.00 11.36 ? 103  VAL C CA  1 
ATOM   2868 C  C   . VAL C 1 103 ? -27.859 64.336 23.489  1.00 10.74 ? 103  VAL C C   1 
ATOM   2869 O  O   . VAL C 1 103 ? -28.714 65.031 24.054  1.00 12.97 ? 103  VAL C O   1 
ATOM   2870 C  CB  . VAL C 1 103 ? -27.580 64.388 20.966  1.00 11.21 ? 103  VAL C CB  1 
ATOM   2871 C  CG1 . VAL C 1 103 ? -29.088 64.620 20.855  1.00 15.12 ? 103  VAL C CG1 1 
ATOM   2872 C  CG2 . VAL C 1 103 ? -26.840 65.088 19.816  1.00 11.61 ? 103  VAL C CG2 1 
ATOM   2873 N  N   . ILE C 1 104 ? -27.578 63.103 23.918  1.00 11.57 ? 104  ILE C N   1 
ATOM   2874 C  CA  . ILE C 1 104 ? -28.163 62.655 25.198  1.00 10.51 ? 104  ILE C CA  1 
ATOM   2875 C  C   . ILE C 1 104 ? -27.660 63.513 26.339  1.00 9.80  ? 104  ILE C C   1 
ATOM   2876 O  O   . ILE C 1 104 ? -26.572 64.111 26.241  1.00 13.04 ? 104  ILE C O   1 
ATOM   2877 C  CB  . ILE C 1 104 ? -27.836 61.175 25.503  1.00 9.75  ? 104  ILE C CB  1 
ATOM   2878 C  CG1 . ILE C 1 104 ? -26.342 60.930 25.654  1.00 10.91 ? 104  ILE C CG1 1 
ATOM   2879 C  CG2 . ILE C 1 104 ? -28.449 60.298 24.420  1.00 11.84 ? 104  ILE C CG2 1 
ATOM   2880 C  CD1 . ILE C 1 104 ? -25.951 59.547 26.091  1.00 11.72 ? 104  ILE C CD1 1 
ATOM   2881 N  N   . SER C 1 105 ? -28.435 63.585 27.421  1.00 9.99  ? 105  SER C N   1 
ATOM   2882 C  CA  . SER C 1 105 ? -27.956 64.293 28.609  1.00 9.89  ? 105  SER C CA  1 
ATOM   2883 C  C   . SER C 1 105 ? -28.472 63.564 29.828  1.00 10.25 ? 105  SER C C   1 
ATOM   2884 O  O   . SER C 1 105 ? -29.414 62.773 29.688  1.00 11.48 ? 105  SER C O   1 
ATOM   2885 C  CB  . SER C 1 105 ? -28.472 65.748 28.634  1.00 11.28 ? 105  SER C CB  1 
ATOM   2886 O  OG  . SER C 1 105 ? -27.852 66.430 29.705  1.00 11.11 ? 105  SER C OG  1 
ATOM   2887 N  N   . LEU C 1 106 ? -27.926 63.838 30.988  1.00 10.46 ? 106  LEU C N   1 
ATOM   2888 C  CA  . LEU C 1 106 ? -28.423 63.267 32.240  1.00 10.92 ? 106  LEU C CA  1 
ATOM   2889 C  C   . LEU C 1 106 ? -29.274 64.290 33.017  1.00 11.93 ? 106  LEU C C   1 
ATOM   2890 O  O   . LEU C 1 106 ? -29.603 64.072 34.198  1.00 13.13 ? 106  LEU C O   1 
ATOM   2891 C  CB  . LEU C 1 106 ? -27.288 62.717 33.092  1.00 10.84 ? 106  LEU C CB  1 
ATOM   2892 C  CG  . LEU C 1 106 ? -26.393 61.675 32.397  1.00 9.15  ? 106  LEU C CG  1 
ATOM   2893 C  CD1 . LEU C 1 106 ? -25.370 61.151 33.407  1.00 12.98 ? 106  LEU C CD1 1 
ATOM   2894 C  CD2 . LEU C 1 106 ? -27.217 60.514 31.809  1.00 12.12 ? 106  LEU C CD2 1 
ATOM   2895 N  N   . SER C 1 107 ? -29.616 65.403 32.354  1.00 11.08 ? 107  SER C N   1 
ATOM   2896 C  CA  . SER C 1 107 ? -30.491 66.390 32.963  1.00 12.10 ? 107  SER C CA  1 
ATOM   2897 C  C   . SER C 1 107 ? -31.139 67.228 31.861  1.00 12.20 ? 107  SER C C   1 
ATOM   2898 O  O   . SER C 1 107 ? -30.699 67.117 30.710  1.00 13.66 ? 107  SER C O   1 
ATOM   2899 C  CB  . SER C 1 107 ? -29.765 67.314 33.954  1.00 16.13 ? 107  SER C CB  1 
ATOM   2900 O  OG  . SER C 1 107 ? -28.752 68.063 33.273  1.00 16.52 ? 107  SER C OG  1 
ATOM   2901 N  N   . GLY C 1 108 ? -32.108 68.059 32.169  1.00 12.14 ? 108  GLY C N   1 
ATOM   2902 C  CA  . GLY C 1 108 ? -32.681 68.929 31.143  1.00 13.85 ? 108  GLY C CA  1 
ATOM   2903 C  C   . GLY C 1 108 ? -33.616 68.257 30.170  1.00 13.10 ? 108  GLY C C   1 
ATOM   2904 O  O   . GLY C 1 108 ? -34.059 67.112 30.374  1.00 13.87 ? 108  GLY C O   1 
ATOM   2905 N  N   . ASP C 1 109 ? -33.922 68.981 29.074  1.00 14.59 ? 109  ASP C N   1 
ATOM   2906 C  CA  . ASP C 1 109 ? -34.790 68.591 28.008  1.00 17.60 ? 109  ASP C CA  1 
ATOM   2907 C  C   . ASP C 1 109 ? -34.377 67.320 27.298  1.00 13.79 ? 109  ASP C C   1 
ATOM   2908 O  O   . ASP C 1 109 ? -35.155 66.588 26.691  1.00 15.22 ? 109  ASP C O   1 
ATOM   2909 C  CB  . ASP C 1 109 ? -34.643 69.695 26.879  1.00 27.24 ? 109  ASP C CB  1 
ATOM   2910 C  CG  . ASP C 1 109 ? -35.639 70.783 27.015  1.00 29.48 ? 109  ASP C CG  1 
ATOM   2911 O  OD1 . ASP C 1 109 ? -36.118 71.042 28.131  1.00 41.61 ? 109  ASP C OD1 1 
ATOM   2912 O  OD2 . ASP C 1 109 ? -35.927 71.368 25.962  1.00 35.62 ? 109  ASP C OD2 1 
ATOM   2913 N  N   . HIS C 1 110 ? -33.076 67.005 27.293  1.00 12.47 ? 110  HIS C N   1 
ATOM   2914 C  CA  . HIS C 1 110 ? -32.575 65.797 26.626  1.00 12.26 ? 110  HIS C CA  1 
ATOM   2915 C  C   . HIS C 1 110 ? -32.328 64.651 27.592  1.00 10.61 ? 110  HIS C C   1 
ATOM   2916 O  O   . HIS C 1 110 ? -31.677 63.661 27.221  1.00 10.87 ? 110  HIS C O   1 
ATOM   2917 C  CB  . HIS C 1 110 ? -31.243 66.102 25.912  1.00 12.79 ? 110  HIS C CB  1 
ATOM   2918 C  CG  . HIS C 1 110 ? -31.164 67.287 24.989  1.00 14.27 ? 110  HIS C CG  1 
ATOM   2919 N  ND1 . HIS C 1 110 ? -30.070 67.361 24.129  1.00 18.49 ? 110  HIS C ND1 1 
ATOM   2920 C  CD2 . HIS C 1 110 ? -31.849 68.425 24.776  1.00 14.05 ? 110  HIS C CD2 1 
ATOM   2921 C  CE1 . HIS C 1 110 ? -30.131 68.487 23.401  1.00 17.66 ? 110  HIS C CE1 1 
ATOM   2922 N  NE2 . HIS C 1 110 ? -31.223 69.150 23.788  1.00 15.33 ? 110  HIS C NE2 1 
HETATM 2923 N  N   . CSX C 1 111 ? -32.832 64.801 28.814  1.00 10.21 ? 111  CSX C N   1 
HETATM 2924 C  CA  . CSX C 1 111 ? -32.510 63.810 29.844  1.00 10.48 ? 111  CSX C CA  1 
HETATM 2925 C  CB  . CSX C 1 111 ? -33.155 64.262 31.156  1.00 12.61 ? 111  CSX C CB  1 
HETATM 2926 S  SG  . CSX C 1 111 ? -32.572 63.302 32.551  1.00 14.64 ? 111  CSX C SG  1 
HETATM 2927 C  C   . CSX C 1 111 ? -33.030 62.418 29.494  1.00 8.99  ? 111  CSX C C   1 
HETATM 2928 O  O   . CSX C 1 111 ? -34.201 62.280 29.162  1.00 10.73 ? 111  CSX C O   1 
HETATM 2929 O  OD  . CSX C 1 111 ? -33.214 63.794 33.850  1.00 37.15 ? 111  CSX C OD  1 
ATOM   2930 N  N   . ILE C 1 112 ? -32.115 61.440 29.647  1.00 9.00  ? 112  ILE C N   1 
ATOM   2931 C  CA  . ILE C 1 112 ? -32.470 60.048 29.391  1.00 7.83  ? 112  ILE C CA  1 
ATOM   2932 C  C   . ILE C 1 112 ? -32.696 59.241 30.686  1.00 9.07  ? 112  ILE C C   1 
ATOM   2933 O  O   . ILE C 1 112 ? -33.062 58.062 30.628  1.00 10.18 ? 112  ILE C O   1 
ATOM   2934 C  CB  . ILE C 1 112 ? -31.373 59.381 28.532  1.00 8.27  ? 112  ILE C CB  1 
ATOM   2935 C  CG1 . ILE C 1 112 ? -29.999 59.333 29.205  1.00 11.66 ? 112  ILE C CG1 1 
ATOM   2936 C  CG2 . ILE C 1 112 ? -31.282 60.092 27.194  1.00 11.49 ? 112  ILE C CG2 1 
ATOM   2937 C  CD1 . ILE C 1 112 ? -28.949 58.527 28.454  1.00 12.55 ? 112  ILE C CD1 1 
ATOM   2938 N  N   . ILE C 1 113 ? -32.480 59.826 31.869  1.00 10.94 ? 113  ILE C N   1 
ATOM   2939 C  CA  . ILE C 1 113 ? -32.746 59.130 33.121  1.00 9.88  ? 113  ILE C CA  1 
ATOM   2940 C  C   . ILE C 1 113 ? -34.226 58.807 33.157  1.00 9.22  ? 113  ILE C C   1 
ATOM   2941 O  O   . ILE C 1 113 ? -35.090 59.629 32.819  1.00 10.90 ? 113  ILE C O   1 
ATOM   2942 C  CB  . ILE C 1 113 ? -32.258 59.928 34.334  1.00 12.76 ? 113  ILE C CB  1 
ATOM   2943 C  CG1 . ILE C 1 113 ? -30.703 59.944 34.381  1.00 17.47 ? 113  ILE C CG1 1 
ATOM   2944 C  CG2 . ILE C 1 113 ? -32.876 59.400 35.635  1.00 12.86 ? 113  ILE C CG2 1 
ATOM   2945 C  CD1 . ILE C 1 113 ? -30.023 60.939 35.238  1.00 23.92 ? 113  ILE C CD1 1 
ATOM   2946 N  N   . GLY C 1 114 ? -34.525 57.570 33.539  1.00 8.24  ? 114  GLY C N   1 
ATOM   2947 C  CA  . GLY C 1 114 ? -35.910 57.124 33.612  1.00 9.13  ? 114  GLY C CA  1 
ATOM   2948 C  C   . GLY C 1 114 ? -36.470 56.653 32.284  1.00 7.79  ? 114  GLY C C   1 
ATOM   2949 O  O   . GLY C 1 114 ? -37.680 56.320 32.227  1.00 8.98  ? 114  GLY C O   1 
ATOM   2950 N  N   . ARG C 1 115 ? -35.619 56.567 31.259  1.00 8.35  ? 115  ARG C N   1 
ATOM   2951 C  CA  . ARG C 1 115 ? -36.049 56.053 29.962  1.00 9.34  ? 115  ARG C CA  1 
ATOM   2952 C  C   . ARG C 1 115 ? -35.369 54.694 29.773  1.00 8.87  ? 115  ARG C C   1 
ATOM   2953 O  O   . ARG C 1 115 ? -34.654 54.204 30.655  1.00 11.70 ? 115  ARG C O   1 
ATOM   2954 C  CB  . ARG C 1 115 ? -35.702 57.072 28.853  1.00 8.41  ? 115  ARG C CB  1 
ATOM   2955 C  CG  . ARG C 1 115 ? -36.445 58.364 29.262  1.00 9.93  ? 115  ARG C CG  1 
ATOM   2956 C  CD  . ARG C 1 115 ? -36.344 59.425 28.208  1.00 10.16 ? 115  ARG C CD  1 
ATOM   2957 N  NE  . ARG C 1 115 ? -36.907 60.707 28.621  1.00 11.71 ? 115  ARG C NE  1 
ATOM   2958 C  CZ  . ARG C 1 115 ? -38.187 61.104 28.565  1.00 10.38 ? 115  ARG C CZ  1 
ATOM   2959 N  NH1 . ARG C 1 115 ? -39.140 60.290 28.103  1.00 11.06 ? 115  ARG C NH1 1 
ATOM   2960 N  NH2 . ARG C 1 115 ? -38.521 62.343 28.959  1.00 11.68 ? 115  ARG C NH2 1 
ATOM   2961 N  N   . THR C 1 116 ? -35.617 54.042 28.639  1.00 8.97  ? 116  THR C N   1 
ATOM   2962 C  CA  . THR C 1 116 ? -35.151 52.673 28.451  1.00 8.58  ? 116  THR C CA  1 
ATOM   2963 C  C   . THR C 1 116 ? -34.021 52.597 27.431  1.00 7.90  ? 116  THR C C   1 
ATOM   2964 O  O   . THR C 1 116 ? -34.141 53.037 26.276  1.00 9.71  ? 116  THR C O   1 
ATOM   2965 C  CB  . THR C 1 116 ? -36.308 51.764 28.000  1.00 8.60  ? 116  THR C CB  1 
ATOM   2966 O  OG1 . THR C 1 116 ? -37.273 51.688 29.067  1.00 11.00 ? 116  THR C OG1 1 
ATOM   2967 C  CG2 . THR C 1 116 ? -35.875 50.318 27.760  1.00 11.34 ? 116  THR C CG2 1 
ATOM   2968 N  N   . LEU C 1 117 ? -32.909 51.989 27.821  1.00 9.53  ? 117  LEU C N   1 
ATOM   2969 C  CA  . LEU C 1 117 ? -31.830 51.679 26.870  1.00 8.76  ? 117  LEU C CA  1 
ATOM   2970 C  C   . LEU C 1 117 ? -32.125 50.307 26.266  1.00 8.86  ? 117  LEU C C   1 
ATOM   2971 O  O   . LEU C 1 117 ? -32.466 49.390 27.028  1.00 9.72  ? 117  LEU C O   1 
ATOM   2972 C  CB  . LEU C 1 117 ? -30.475 51.663 27.605  1.00 8.88  ? 117  LEU C CB  1 
ATOM   2973 C  CG  . LEU C 1 117 ? -29.225 51.579 26.734  1.00 9.40  ? 117  LEU C CG  1 
ATOM   2974 C  CD1 . LEU C 1 117 ? -29.019 52.801 25.839  1.00 14.36 ? 117  LEU C CD1 1 
ATOM   2975 C  CD2 . LEU C 1 117 ? -28.026 51.390 27.649  1.00 13.04 ? 117  LEU C CD2 1 
ATOM   2976 N  N   . VAL C 1 118 ? -31.998 50.190 24.956  1.00 8.46  ? 118  VAL C N   1 
ATOM   2977 C  CA  . VAL C 1 118 ? -32.344 48.959 24.231  1.00 9.23  ? 118  VAL C CA  1 
ATOM   2978 C  C   . VAL C 1 118 ? -31.211 48.527 23.301  1.00 9.10  ? 118  VAL C C   1 
ATOM   2979 O  O   . VAL C 1 118 ? -30.672 49.393 22.566  1.00 10.52 ? 118  VAL C O   1 
ATOM   2980 C  CB  . VAL C 1 118 ? -33.608 49.164 23.363  1.00 9.37  ? 118  VAL C CB  1 
ATOM   2981 C  CG1 . VAL C 1 118 ? -34.002 47.902 22.596  1.00 11.10 ? 118  VAL C CG1 1 
ATOM   2982 C  CG2 . VAL C 1 118 ? -34.757 49.661 24.257  1.00 10.45 ? 118  VAL C CG2 1 
ATOM   2983 N  N   . VAL C 1 119 ? -30.863 47.266 23.287  1.00 9.45  ? 119  VAL C N   1 
ATOM   2984 C  CA  . VAL C 1 119 ? -29.974 46.703 22.262  1.00 9.64  ? 119  VAL C CA  1 
ATOM   2985 C  C   . VAL C 1 119 ? -30.781 45.765 21.382  1.00 9.29  ? 119  VAL C C   1 
ATOM   2986 O  O   . VAL C 1 119 ? -31.626 44.992 21.860  1.00 10.48 ? 119  VAL C O   1 
ATOM   2987 C  CB  . VAL C 1 119 ? -28.725 46.047 22.886  1.00 10.47 ? 119  VAL C CB  1 
ATOM   2988 C  CG1 . VAL C 1 119 ? -29.054 44.872 23.789  1.00 11.31 ? 119  VAL C CG1 1 
ATOM   2989 C  CG2 . VAL C 1 119 ? -27.759 45.629 21.783  1.00 12.19 ? 119  VAL C CG2 1 
ATOM   2990 N  N   . HIS C 1 120 ? -30.510 45.855 20.084  1.00 10.15 ? 120  HIS C N   1 
ATOM   2991 C  CA  . HIS C 1 120 ? -31.349 45.247 19.051  1.00 11.16 ? 120  HIS C CA  1 
ATOM   2992 C  C   . HIS C 1 120 ? -30.727 44.040 18.356  1.00 10.21 ? 120  HIS C C   1 
ATOM   2993 O  O   . HIS C 1 120 ? -29.500 43.819 18.376  1.00 12.28 ? 120  HIS C O   1 
ATOM   2994 C  CB  . HIS C 1 120 ? -31.647 46.282 17.951  1.00 10.36 ? 120  HIS C CB  1 
ATOM   2995 C  CG  . HIS C 1 120 ? -32.795 47.183 18.315  1.00 10.11 ? 120  HIS C CG  1 
ATOM   2996 N  ND1 . HIS C 1 120 ? -34.096 46.895 18.044  1.00 10.42 ? 120  HIS C ND1 1 
ATOM   2997 C  CD2 . HIS C 1 120 ? -32.814 48.382 18.924  1.00 9.60  ? 120  HIS C CD2 1 
ATOM   2998 C  CE1 . HIS C 1 120 ? -34.894 47.895 18.467  1.00 9.96  ? 120  HIS C CE1 1 
ATOM   2999 N  NE2 . HIS C 1 120 ? -34.106 48.830 19.013  1.00 10.14 ? 120  HIS C NE2 1 
ATOM   3000 N  N   . GLU C 1 121 ? -31.626 43.289 17.722  1.00 10.96 ? 121  GLU C N   1 
ATOM   3001 C  CA  . GLU C 1 121 ? -31.259 42.096 16.971  1.00 11.90 ? 121  GLU C CA  1 
ATOM   3002 C  C   . GLU C 1 121 ? -30.252 42.301 15.866  1.00 11.40 ? 121  GLU C C   1 
ATOM   3003 O  O   . GLU C 1 121 ? -29.396 41.458 15.653  1.00 13.46 ? 121  GLU C O   1 
ATOM   3004 C  CB  . GLU C 1 121 ? -32.557 41.553 16.347  1.00 13.59 ? 121  GLU C CB  1 
ATOM   3005 C  CG  . GLU C 1 121 ? -32.408 40.357 15.439  1.00 14.41 ? 121  GLU C CG  1 
ATOM   3006 C  CD  . GLU C 1 121 ? -33.669 40.072 14.643  1.00 17.39 ? 121  GLU C CD  1 
ATOM   3007 O  OE1 . GLU C 1 121 ? -34.650 40.812 14.779  1.00 15.25 ? 121  GLU C OE1 1 
ATOM   3008 O  OE2 . GLU C 1 121 ? -33.682 39.095 13.848  1.00 21.61 ? 121  GLU C OE2 1 
ATOM   3009 N  N   . LYS C 1 122 ? -30.372 43.396 15.139  1.00 13.14 ? 122  LYS C N   1 
ATOM   3010 C  CA  . LYS C 1 122 ? -29.480 43.605 13.989  1.00 13.13 ? 122  LYS C CA  1 
ATOM   3011 C  C   . LYS C 1 122 ? -29.153 45.078 13.876  1.00 10.41 ? 122  LYS C C   1 
ATOM   3012 O  O   . LYS C 1 122 ? -29.452 45.845 14.801  1.00 12.74 ? 122  LYS C O   1 
ATOM   3013 C  CB  . LYS C 1 122 ? -30.108 42.983 12.769  1.00 17.68 ? 122  LYS C CB  1 
ATOM   3014 C  CG  . LYS C 1 122 ? -31.464 43.511 12.390  1.00 19.86 ? 122  LYS C CG  1 
ATOM   3015 C  CD  . LYS C 1 122 ? -32.121 42.568 11.362  1.00 21.31 ? 122  LYS C CD  1 
ATOM   3016 C  CE  . LYS C 1 122 ? -33.361 43.210 10.800  1.00 23.55 ? 122  LYS C CE  1 
ATOM   3017 N  NZ  . LYS C 1 122 ? -32.956 44.246 9.800   1.00 30.67 ? 122  LYS C NZ  1 
ATOM   3018 N  N   . ALA C 1 123 ? -28.527 45.497 12.783  1.00 13.31 ? 123  ALA C N   1 
ATOM   3019 C  CA  . ALA C 1 123 ? -28.024 46.865 12.673  1.00 12.89 ? 123  ALA C CA  1 
ATOM   3020 C  C   . ALA C 1 123 ? -29.111 47.926 12.504  1.00 12.50 ? 123  ALA C C   1 
ATOM   3021 O  O   . ALA C 1 123 ? -30.099 47.722 11.818  1.00 14.12 ? 123  ALA C O   1 
ATOM   3022 C  CB  . ALA C 1 123 ? -27.067 46.935 11.469  1.00 13.87 ? 123  ALA C CB  1 
ATOM   3023 N  N   . ASP C 1 124 ? -28.864 49.088 13.130  1.00 12.89 ? 124  ASP C N   1 
ATOM   3024 C  CA  . ASP C 1 124 ? -29.606 50.282 12.746  1.00 12.59 ? 124  ASP C CA  1 
ATOM   3025 C  C   . ASP C 1 124 ? -29.042 50.772 11.419  1.00 14.18 ? 124  ASP C C   1 
ATOM   3026 O  O   . ASP C 1 124 ? -27.804 50.907 11.309  1.00 15.40 ? 124  ASP C O   1 
ATOM   3027 C  CB  . ASP C 1 124 ? -29.396 51.302 13.865  1.00 12.09 ? 124  ASP C CB  1 
ATOM   3028 C  CG  . ASP C 1 124 ? -30.162 52.588 13.746  1.00 10.76 ? 124  ASP C CG  1 
ATOM   3029 O  OD1 . ASP C 1 124 ? -30.512 53.003 12.612  1.00 13.73 ? 124  ASP C OD1 1 
ATOM   3030 O  OD2 . ASP C 1 124 ? -30.433 53.215 14.800  1.00 11.99 ? 124  ASP C OD2 1 
ATOM   3031 N  N   . HIS C 1 125 ? -29.912 51.041 10.456  1.00 14.18 ? 125  HIS C N   1 
ATOM   3032 C  CA  . HIS C 1 125 ? -29.462 51.542 9.160   1.00 16.66 ? 125  HIS C CA  1 
ATOM   3033 C  C   . HIS C 1 125 ? -29.070 53.012 9.192   1.00 15.46 ? 125  HIS C C   1 
ATOM   3034 O  O   . HIS C 1 125 ? -28.544 53.552 8.203   1.00 19.03 ? 125  HIS C O   1 
ATOM   3035 C  CB  . HIS C 1 125 ? -30.527 51.244 8.111   1.00 20.12 ? 125  HIS C CB  1 
ATOM   3036 C  CG  . HIS C 1 125 ? -31.814 51.990 8.201   1.00 29.67 ? 125  HIS C CG  1 
ATOM   3037 N  ND1 . HIS C 1 125 ? -31.985 53.302 8.597   1.00 33.34 ? 125  HIS C ND1 1 
ATOM   3038 C  CD2 . HIS C 1 125 ? -33.072 51.551 7.907   1.00 28.41 ? 125  HIS C CD2 1 
ATOM   3039 C  CE1 . HIS C 1 125 ? -33.249 53.674 8.568   1.00 30.27 ? 125  HIS C CE1 1 
ATOM   3040 N  NE2 . HIS C 1 125 ? -33.929 52.600 8.146   1.00 34.73 ? 125  HIS C NE2 1 
ATOM   3041 N  N   . LEU C 1 126 ? -29.323 53.728 10.284  1.00 15.82 ? 126  LEU C N   1 
ATOM   3042 C  CA  . LEU C 1 126 ? -28.787 55.084 10.501  1.00 16.88 ? 126  LEU C CA  1 
ATOM   3043 C  C   . LEU C 1 126 ? -29.423 56.129 9.593   1.00 19.80 ? 126  LEU C C   1 
ATOM   3044 O  O   . LEU C 1 126 ? -28.866 57.199 9.320   1.00 23.13 ? 126  LEU C O   1 
ATOM   3045 C  CB  . LEU C 1 126 ? -27.254 55.135 10.409  1.00 18.30 ? 126  LEU C CB  1 
ATOM   3046 C  CG  . LEU C 1 126 ? -26.471 54.103 11.219  1.00 17.86 ? 126  LEU C CG  1 
ATOM   3047 C  CD1 . LEU C 1 126 ? -24.967 54.271 10.962  1.00 21.40 ? 126  LEU C CD1 1 
ATOM   3048 C  CD2 . LEU C 1 126 ? -26.711 54.133 12.722  1.00 17.18 ? 126  LEU C CD2 1 
ATOM   3049 N  N   . GLY C 1 127 ? -30.635 55.815 9.142   1.00 20.25 ? 127  GLY C N   1 
ATOM   3050 C  CA  . GLY C 1 127 ? -31.323 56.773 8.275   1.00 25.15 ? 127  GLY C CA  1 
ATOM   3051 C  C   . GLY C 1 127 ? -31.041 56.524 6.823   1.00 29.05 ? 127  GLY C C   1 
ATOM   3052 O  O   . GLY C 1 127 ? -31.646 57.188 5.979   1.00 42.46 ? 127  GLY C O   1 
ATOM   3053 N  N   . LYS C 1 128 ? -30.159 55.586 6.471   1.00 33.39 ? 128  LYS C N   1 
ATOM   3054 C  CA  . LYS C 1 128 ? -29.938 55.358 5.031   1.00 38.27 ? 128  LYS C CA  1 
ATOM   3055 C  C   . LYS C 1 128 ? -30.974 54.450 4.389   1.00 46.30 ? 128  LYS C C   1 
ATOM   3056 O  O   . LYS C 1 128 ? -31.119 53.255 4.742   1.00 46.82 ? 128  LYS C O   1 
ATOM   3057 C  CB  . LYS C 1 128 ? -28.529 54.786 4.864   1.00 39.02 ? 128  LYS C CB  1 
ATOM   3058 C  CG  . LYS C 1 128 ? -27.436 55.721 5.374   1.00 45.39 ? 128  LYS C CG  1 
ATOM   3059 C  CD  . LYS C 1 128 ? -26.192 54.921 5.735   1.00 52.03 ? 128  LYS C CD  1 
ATOM   3060 C  CE  . LYS C 1 128 ? -25.551 55.434 7.016   1.00 55.56 ? 128  LYS C CE  1 
ATOM   3061 N  NZ  . LYS C 1 128 ? -24.234 54.768 7.256   1.00 58.70 ? 128  LYS C NZ  1 
ATOM   3062 N  N   . LYS C 1 136 ? -37.613 55.627 9.889   1.00 34.63 ? 136  LYS C N   1 
ATOM   3063 C  CA  . LYS C 1 136 ? -38.037 56.149 11.205  1.00 32.21 ? 136  LYS C CA  1 
ATOM   3064 C  C   . LYS C 1 136 ? -37.449 55.398 12.394  1.00 27.45 ? 136  LYS C C   1 
ATOM   3065 O  O   . LYS C 1 136 ? -37.073 55.987 13.438  1.00 30.49 ? 136  LYS C O   1 
ATOM   3066 C  CB  . LYS C 1 136 ? -39.559 56.071 11.248  1.00 42.58 ? 136  LYS C CB  1 
ATOM   3067 C  CG  . LYS C 1 136 ? -40.241 56.495 12.530  1.00 48.45 ? 136  LYS C CG  1 
ATOM   3068 C  CD  . LYS C 1 136 ? -41.752 56.563 12.319  1.00 50.74 ? 136  LYS C CD  1 
ATOM   3069 C  CE  . LYS C 1 136 ? -42.185 57.962 11.901  1.00 53.61 ? 136  LYS C CE  1 
ATOM   3070 N  NZ  . LYS C 1 136 ? -41.060 58.745 11.324  1.00 70.77 ? 136  LYS C NZ  1 
ATOM   3071 N  N   . THR C 1 137 ? -37.353 54.059 12.249  1.00 23.16 ? 137  THR C N   1 
ATOM   3072 C  CA  . THR C 1 137 ? -36.858 53.243 13.333  1.00 21.11 ? 137  THR C CA  1 
ATOM   3073 C  C   . THR C 1 137 ? -35.416 52.816 13.085  1.00 19.56 ? 137  THR C C   1 
ATOM   3074 O  O   . THR C 1 137 ? -34.765 52.488 14.068  1.00 21.05 ? 137  THR C O   1 
ATOM   3075 C  CB  . THR C 1 137 ? -37.612 51.918 13.582  1.00 20.57 ? 137  THR C CB  1 
ATOM   3076 O  OG1 . THR C 1 137 ? -37.400 51.072 12.424  1.00 22.79 ? 137  THR C OG1 1 
ATOM   3077 C  CG2 . THR C 1 137 ? -39.089 52.108 13.729  1.00 29.76 ? 137  THR C CG2 1 
ATOM   3078 N  N   . GLY C 1 138 ? -34.940 52.775 11.851  1.00 18.35 ? 138  GLY C N   1 
ATOM   3079 C  CA  . GLY C 1 138 ? -33.624 52.207 11.587  1.00 17.37 ? 138  GLY C CA  1 
ATOM   3080 C  C   . GLY C 1 138 ? -33.680 50.720 11.298  1.00 15.27 ? 138  GLY C C   1 
ATOM   3081 O  O   . GLY C 1 138 ? -32.613 50.174 10.963  1.00 16.66 ? 138  GLY C O   1 
ATOM   3082 N  N   . ASN C 1 139 ? -34.828 50.046 11.416  1.00 16.37 ? 139  ASN C N   1 
ATOM   3083 C  CA  . ASN C 1 139 ? -34.926 48.629 11.017  1.00 16.80 ? 139  ASN C CA  1 
ATOM   3084 C  C   . ASN C 1 139 ? -33.938 47.713 11.708  1.00 13.74 ? 139  ASN C C   1 
ATOM   3085 O  O   . ASN C 1 139 ? -33.349 46.790 11.100  1.00 16.30 ? 139  ASN C O   1 
ATOM   3086 C  CB  . ASN C 1 139 ? -34.749 48.489 9.490   1.00 22.11 ? 139  ASN C CB  1 
ATOM   3087 C  CG  . ASN C 1 139 ? -35.420 47.294 8.859   1.00 31.11 ? 139  ASN C CG  1 
ATOM   3088 O  OD1 . ASN C 1 139 ? -36.223 46.620 9.514   1.00 40.72 ? 139  ASN C OD1 1 
ATOM   3089 N  ND2 . ASN C 1 139 ? -35.164 46.978 7.586   1.00 51.33 ? 139  ASN C ND2 1 
ATOM   3090 N  N   . ALA C 1 140 ? -33.756 47.868 13.028  1.00 11.83 ? 140  ALA C N   1 
ATOM   3091 C  CA  . ALA C 1 140 ? -32.776 47.071 13.753  1.00 12.28 ? 140  ALA C CA  1 
ATOM   3092 C  C   . ALA C 1 140 ? -33.360 45.778 14.321  1.00 11.75 ? 140  ALA C C   1 
ATOM   3093 O  O   . ALA C 1 140 ? -32.688 45.110 15.119  1.00 12.14 ? 140  ALA C O   1 
ATOM   3094 C  CB  . ALA C 1 140 ? -32.141 47.873 14.896  1.00 12.13 ? 140  ALA C CB  1 
ATOM   3095 N  N   . GLY C 1 141 ? -34.586 45.420 13.910  1.00 12.07 ? 141  GLY C N   1 
ATOM   3096 C  CA  . GLY C 1 141 ? -35.111 44.128 14.350  1.00 13.67 ? 141  GLY C CA  1 
ATOM   3097 C  C   . GLY C 1 141 ? -35.528 44.174 15.804  1.00 12.19 ? 141  GLY C C   1 
ATOM   3098 O  O   . GLY C 1 141 ? -35.775 45.274 16.377  1.00 13.49 ? 141  GLY C O   1 
ATOM   3099 N  N   . SER C 1 142 ? -35.654 42.991 16.401  1.00 11.32 ? 142  SER C N   1 
ATOM   3100 C  CA  . SER C 1 142 ? -36.288 42.913 17.711  1.00 12.16 ? 142  SER C CA  1 
ATOM   3101 C  C   . SER C 1 142 ? -35.434 43.548 18.797  1.00 10.69 ? 142  SER C C   1 
ATOM   3102 O  O   . SER C 1 142 ? -34.240 43.798 18.657  1.00 11.79 ? 142  SER C O   1 
ATOM   3103 C  CB  . SER C 1 142 ? -36.571 41.454 18.093  1.00 14.01 ? 142  SER C CB  1 
ATOM   3104 O  OG  . SER C 1 142 ? -35.378 40.745 18.288  1.00 16.88 ? 142  SER C OG  1 
ATOM   3105 N  N   . ARG C 1 143 ? -36.094 43.844 19.910  1.00 10.48 ? 143  ARG C N   1 
ATOM   3106 C  CA  . ARG C 1 143 ? -35.461 44.360 21.103  1.00 9.91  ? 143  ARG C CA  1 
ATOM   3107 C  C   . ARG C 1 143 ? -34.959 43.204 21.947  1.00 10.13 ? 143  ARG C C   1 
ATOM   3108 O  O   . ARG C 1 143 ? -35.780 42.462 22.514  1.00 13.51 ? 143  ARG C O   1 
ATOM   3109 C  CB  . ARG C 1 143 ? -36.466 45.235 21.891  1.00 9.99  ? 143  ARG C CB  1 
ATOM   3110 C  CG  . ARG C 1 143 ? -37.003 46.387 21.034  1.00 10.17 ? 143  ARG C CG  1 
ATOM   3111 C  CD  . ARG C 1 143 ? -37.898 47.318 21.814  1.00 10.63 ? 143  ARG C CD  1 
ATOM   3112 N  NE  . ARG C 1 143 ? -38.470 48.289 20.868  1.00 10.12 ? 143  ARG C NE  1 
ATOM   3113 C  CZ  . ARG C 1 143 ? -39.484 49.107 21.058  1.00 9.01  ? 143  ARG C CZ  1 
ATOM   3114 N  NH1 . ARG C 1 143 ? -40.108 49.119 22.257  1.00 10.38 ? 143  ARG C NH1 1 
ATOM   3115 N  NH2 . ARG C 1 143 ? -39.876 49.903 20.078  1.00 10.37 ? 143  ARG C NH2 1 
ATOM   3116 N  N   . LEU C 1 144 ? -33.628 42.972 21.960  1.00 10.29 ? 144  LEU C N   1 
ATOM   3117 C  CA  . LEU C 1 144 ? -33.114 41.783 22.617  1.00 11.09 ? 144  LEU C CA  1 
ATOM   3118 C  C   . LEU C 1 144 ? -32.952 41.931 24.129  1.00 11.11 ? 144  LEU C C   1 
ATOM   3119 O  O   . LEU C 1 144 ? -33.104 40.935 24.854  1.00 12.19 ? 144  LEU C O   1 
ATOM   3120 C  CB  . LEU C 1 144 ? -31.731 41.411 22.073  1.00 12.48 ? 144  LEU C CB  1 
ATOM   3121 C  CG  . LEU C 1 144 ? -31.621 41.140 20.585  1.00 13.39 ? 144  LEU C CG  1 
ATOM   3122 C  CD1 . LEU C 1 144 ? -30.157 40.842 20.256  1.00 18.77 ? 144  LEU C CD1 1 
ATOM   3123 C  CD2 . LEU C 1 144 ? -32.526 39.976 20.243  1.00 18.41 ? 144  LEU C CD2 1 
ATOM   3124 N  N   . ALA C 1 145 ? -32.606 43.139 24.561  1.00 10.60 ? 145  ALA C N   1 
ATOM   3125 C  CA  . ALA C 1 145 ? -32.449 43.363 25.999  1.00 9.54  ? 145  ALA C CA  1 
ATOM   3126 C  C   . ALA C 1 145 ? -32.622 44.854 26.260  1.00 9.88  ? 145  ALA C C   1 
ATOM   3127 O  O   . ALA C 1 145 ? -32.376 45.673 25.371  1.00 11.25 ? 145  ALA C O   1 
ATOM   3128 C  CB  . ALA C 1 145 ? -31.109 42.904 26.530  1.00 12.42 ? 145  ALA C CB  1 
ATOM   3129 N  N   . CYS C 1 146 ? -33.047 45.199 27.467  1.00 9.55  ? 146  CYS C N   1 
ATOM   3130 C  CA  . CYS C 1 146 ? -33.294 46.592 27.779  1.00 9.53  ? 146  CYS C CA  1 
ATOM   3131 C  C   . CYS C 1 146 ? -33.308 46.746 29.303  1.00 8.59  ? 146  CYS C C   1 
ATOM   3132 O  O   . CYS C 1 146 ? -33.323 45.792 30.070  1.00 10.50 ? 146  CYS C O   1 
ATOM   3133 C  CB  . CYS C 1 146 ? -34.623 47.053 27.170  1.00 10.73 ? 146  CYS C CB  1 
ATOM   3134 S  SG  . CYS C 1 146 ? -36.052 46.128 27.817  1.00 13.29 ? 146  CYS C SG  1 
ATOM   3135 N  N   . GLY C 1 147 ? -33.289 48.024 29.701  1.00 9.25  ? 147  GLY C N   1 
ATOM   3136 C  CA  . GLY C 1 147 ? -33.421 48.301 31.117  1.00 10.16 ? 147  GLY C CA  1 
ATOM   3137 C  C   . GLY C 1 147 ? -33.708 49.776 31.298  1.00 8.62  ? 147  GLY C C   1 
ATOM   3138 O  O   . GLY C 1 147 ? -33.478 50.551 30.353  1.00 9.85  ? 147  GLY C O   1 
ATOM   3139 N  N   . VAL C 1 148 ? -34.174 50.175 32.466  1.00 8.84  ? 148  VAL C N   1 
ATOM   3140 C  CA  . VAL C 1 148 ? -34.442 51.574 32.762  1.00 8.21  ? 148  VAL C CA  1 
ATOM   3141 C  C   . VAL C 1 148 ? -33.132 52.233 33.192  1.00 8.10  ? 148  VAL C C   1 
ATOM   3142 O  O   . VAL C 1 148 ? -32.364 51.658 33.993  1.00 10.65 ? 148  VAL C O   1 
ATOM   3143 C  CB  . VAL C 1 148 ? -35.521 51.708 33.848  1.00 8.84  ? 148  VAL C CB  1 
ATOM   3144 C  CG1 . VAL C 1 148 ? -35.823 53.184 34.139  1.00 11.48 ? 148  VAL C CG1 1 
ATOM   3145 C  CG2 . VAL C 1 148 ? -36.796 50.988 33.399  1.00 11.77 ? 148  VAL C CG2 1 
ATOM   3146 N  N   . ILE C 1 149 ? -32.868 53.421 32.694  1.00 8.91  ? 149  ILE C N   1 
ATOM   3147 C  CA  . ILE C 1 149 ? -31.628 54.151 33.043  1.00 8.62  ? 149  ILE C CA  1 
ATOM   3148 C  C   . ILE C 1 149 ? -31.836 54.825 34.381  1.00 9.23  ? 149  ILE C C   1 
ATOM   3149 O  O   . ILE C 1 149 ? -32.733 55.641 34.551  1.00 9.58  ? 149  ILE C O   1 
ATOM   3150 C  CB  . ILE C 1 149 ? -31.259 55.152 31.935  1.00 8.70  ? 149  ILE C CB  1 
ATOM   3151 C  CG1 . ILE C 1 149 ? -31.026 54.421 30.607  1.00 10.93 ? 149  ILE C CG1 1 
ATOM   3152 C  CG2 . ILE C 1 149 ? -30.066 56.018 32.296  1.00 9.85  ? 149  ILE C CG2 1 
ATOM   3153 C  CD1 . ILE C 1 149 ? -31.080 55.330 29.378  1.00 12.39 ? 149  ILE C CD1 1 
ATOM   3154 N  N   . GLY C 1 150 ? -30.998 54.490 35.342  1.00 9.12  ? 150  GLY C N   1 
ATOM   3155 C  CA  . GLY C 1 150 ? -31.160 54.987 36.713  1.00 10.03 ? 150  GLY C CA  1 
ATOM   3156 C  C   . GLY C 1 150 ? -30.025 55.894 37.132  1.00 8.66  ? 150  GLY C C   1 
ATOM   3157 O  O   . GLY C 1 150 ? -28.907 55.761 36.611  1.00 10.41 ? 150  GLY C O   1 
ATOM   3158 N  N   . ILE C 1 151 ? -30.271 56.771 38.105  1.00 9.17  ? 151  ILE C N   1 
ATOM   3159 C  CA  . ILE C 1 151 ? -29.215 57.589 38.672  1.00 8.79  ? 151  ILE C CA  1 
ATOM   3160 C  C   . ILE C 1 151 ? -28.219 56.749 39.461  1.00 9.14  ? 151  ILE C C   1 
ATOM   3161 O  O   . ILE C 1 151 ? -28.634 55.867 40.218  1.00 11.26 ? 151  ILE C O   1 
ATOM   3162 C  CB  . ILE C 1 151 ? -29.855 58.682 39.576  1.00 10.79 ? 151  ILE C CB  1 
ATOM   3163 C  CG1 . ILE C 1 151 ? -30.772 59.608 38.790  1.00 13.87 ? 151  ILE C CG1 1 
ATOM   3164 C  CG2 . ILE C 1 151 ? -28.762 59.430 40.291  1.00 14.26 ? 151  ILE C CG2 1 
ATOM   3165 C  CD1 . ILE C 1 151 ? -31.721 60.446 39.618  1.00 14.52 ? 151  ILE C CD1 1 
ATOM   3166 N  N   . ALA C 1 152 ? -26.930 57.018 39.306  1.00 9.77  ? 152  ALA C N   1 
ATOM   3167 C  CA  . ALA C 1 152 ? -25.889 56.235 39.966  1.00 10.41 ? 152  ALA C CA  1 
ATOM   3168 C  C   . ALA C 1 152 ? -25.007 57.158 40.799  1.00 11.03 ? 152  ALA C C   1 
ATOM   3169 O  O   . ALA C 1 152 ? -25.010 58.375 40.581  1.00 14.19 ? 152  ALA C O   1 
ATOM   3170 C  CB  . ALA C 1 152 ? -25.032 55.493 38.958  1.00 11.90 ? 152  ALA C CB  1 
ATOM   3171 N  N   . GLN C 1 153 ? -24.320 56.534 41.746  1.00 12.53 ? 153  GLN C N   1 
ATOM   3172 C  CA  . GLN C 1 153 ? -23.494 57.283 42.687  1.00 16.71 ? 153  GLN C CA  1 
ATOM   3173 C  C   . GLN C 1 153 ? -22.228 57.739 41.990  1.00 20.23 ? 153  GLN C C   1 
ATOM   3174 O  O   . GLN C 1 153 ? -21.814 58.892 42.263  1.00 27.80 ? 153  GLN C O   1 
ATOM   3175 C  CB  . GLN C 1 153 ? -23.138 56.430 43.899  1.00 18.11 ? 153  GLN C CB  1 
ATOM   3176 C  CG  . GLN C 1 153 ? -22.481 57.201 45.043  1.00 23.91 ? 153  GLN C CG  1 
ATOM   3177 C  CD  . GLN C 1 153 ? -22.206 56.245 46.198  1.00 29.29 ? 153  GLN C CD  1 
ATOM   3178 O  OE1 . GLN C 1 153 ? -21.651 55.177 46.003  1.00 37.83 ? 153  GLN C OE1 1 
ATOM   3179 N  NE2 . GLN C 1 153 ? -22.624 56.677 47.362  1.00 39.76 ? 153  GLN C NE2 1 
ATOM   3180 O  OXT . GLN C 1 153 ? -21.693 56.937 41.205  1.00 23.81 ? 153  GLN C OXT 1 
HETATM 3181 S  S   . SO4 D 2 .   ? 13.368  26.443 29.942  1.00 13.38 ? 801  SO4 A S   1 
HETATM 3182 O  O1  . SO4 D 2 .   ? 13.673  27.857 29.425  1.00 13.16 ? 801  SO4 A O1  1 
HETATM 3183 O  O2  . SO4 D 2 .   ? 12.690  25.655 28.917  1.00 12.56 ? 801  SO4 A O2  1 
HETATM 3184 O  O3  . SO4 D 2 .   ? 14.612  25.899 30.214  1.00 19.03 ? 801  SO4 A O3  1 
HETATM 3185 O  O4  . SO4 D 2 .   ? 12.613  26.527 31.171  1.00 17.57 ? 801  SO4 A O4  1 
HETATM 3186 ZN ZN  . ZN  E 3 .   ? 13.065  28.972 27.945  1.00 11.03 ? 201  ZN  A ZN  1 
HETATM 3187 ZN ZN  . ZN  F 3 .   ? 18.849  31.834 31.089  1.00 11.64 ? 202  ZN  A ZN  1 
HETATM 3188 S  S   . SO4 G 2 .   ? 12.421  29.552 -7.317  1.00 32.21 ? 802  SO4 B S   1 
HETATM 3189 O  O1  . SO4 G 2 .   ? 13.018  30.986 -7.575  1.00 50.53 ? 802  SO4 B O1  1 
HETATM 3190 O  O2  . SO4 G 2 .   ? 13.559  28.765 -6.887  1.00 30.00 ? 802  SO4 B O2  1 
HETATM 3191 O  O3  . SO4 G 2 .   ? 11.457  29.734 -6.444  1.00 30.63 ? 802  SO4 B O3  1 
HETATM 3192 O  O4  . SO4 G 2 .   ? 11.988  29.163 -8.634  1.00 43.57 ? 802  SO4 B O4  1 
HETATM 3193 ZN ZN  . ZN  H 3 .   ? 13.751  27.625 -5.357  1.00 25.09 ? 203  ZN  B ZN  1 
HETATM 3194 ZN ZN  . ZN  I 3 .   ? 19.911  28.983 -8.447  1.00 33.95 ? 204  ZN  B ZN  1 
HETATM 3195 S  S   . SO4 J 2 .   ? -37.265 50.141 17.194  1.00 11.74 ? 803  SO4 C S   1 
HETATM 3196 O  O1  . SO4 J 2 .   ? -36.026 50.914 17.668  1.00 10.25 ? 803  SO4 C O1  1 
HETATM 3197 O  O2  . SO4 J 2 .   ? -36.942 49.472 15.938  1.00 17.66 ? 803  SO4 C O2  1 
HETATM 3198 O  O3  . SO4 J 2 .   ? -37.753 49.266 18.137  1.00 11.58 ? 803  SO4 C O3  1 
HETATM 3199 O  O4  . SO4 J 2 .   ? -38.291 51.200 16.949  1.00 18.19 ? 803  SO4 C O4  1 
HETATM 3200 ZN ZN  . ZN  K 3 .   ? -34.776 50.735 19.158  1.00 9.85  ? 205  ZN  C ZN  1 
HETATM 3201 ZN ZN  . ZN  L 3 .   ? -34.217 57.182 16.026  1.00 10.27 ? 206  ZN  C ZN  1 
HETATM 3202 O  O   . HOH M 4 .   ? 9.257   14.826 16.415  1.00 15.54 ? 802  HOH A O   1 
HETATM 3203 O  O   . HOH M 4 .   ? 15.439  36.062 31.356  1.00 14.61 ? 803  HOH A O   1 
HETATM 3204 O  O   . HOH M 4 .   ? 25.952  33.566 27.642  1.00 13.16 ? 804  HOH A O   1 
HETATM 3205 O  O   . HOH M 4 .   ? 25.863  36.028 28.623  1.00 14.02 ? 805  HOH A O   1 
HETATM 3206 O  O   . HOH M 4 .   ? 10.786  31.591 11.951  1.00 15.46 ? 806  HOH A O   1 
HETATM 3207 O  O   . HOH M 4 .   ? 28.364  38.834 18.855  1.00 13.98 ? 807  HOH A O   1 
HETATM 3208 O  O   . HOH M 4 .   ? 7.685   22.523 27.161  1.00 16.36 ? 808  HOH A O   1 
HETATM 3209 O  O   . HOH M 4 .   ? 24.297  43.545 20.995  1.00 18.99 ? 809  HOH A O   1 
HETATM 3210 O  O   . HOH M 4 .   ? 14.566  23.088 12.927  1.00 13.91 ? 810  HOH A O   1 
HETATM 3211 O  O   . HOH M 4 .   ? 29.330  37.632 29.942  1.00 16.08 ? 811  HOH A O   1 
HETATM 3212 O  O   . HOH M 4 .   ? 21.816  43.996 29.615  1.00 15.87 ? 812  HOH A O   1 
HETATM 3213 O  O   . HOH M 4 .   ? 20.476  44.462 27.281  1.00 17.17 ? 813  HOH A O   1 
HETATM 3214 O  O   . HOH M 4 .   ? 27.925  41.166 20.327  1.00 17.21 ? 814  HOH A O   1 
HETATM 3215 O  O   . HOH M 4 .   ? 24.659  27.845 24.537  1.00 19.10 ? 815  HOH A O   1 
HETATM 3216 O  O   . HOH M 4 .   ? 27.495  49.910 21.073  1.00 16.64 ? 816  HOH A O   1 
HETATM 3217 O  O   . HOH M 4 .   ? 16.763  43.946 26.913  1.00 17.81 ? 817  HOH A O   1 
HETATM 3218 O  O   . HOH M 4 .   ? 26.013  40.511 30.548  1.00 14.99 ? 818  HOH A O   1 
HETATM 3219 O  O   . HOH M 4 .   ? 2.515   24.531 22.080  1.00 18.93 ? 819  HOH A O   1 
HETATM 3220 O  O   . HOH M 4 .   ? 10.881  28.038 12.417  1.00 17.59 ? 820  HOH A O   1 
HETATM 3221 O  O   . HOH M 4 .   ? 3.119   20.961 22.847  1.00 18.37 ? 821  HOH A O   1 
HETATM 3222 O  O   . HOH M 4 .   ? 5.582   42.666 26.363  1.00 21.56 ? 822  HOH A O   1 
HETATM 3223 O  O   . HOH M 4 .   ? 12.140  29.032 32.283  1.00 19.62 ? 823  HOH A O   1 
HETATM 3224 O  O   . HOH M 4 .   ? -0.535  31.401 27.695  1.00 17.31 ? 824  HOH A O   1 
HETATM 3225 O  O   . HOH M 4 .   ? 25.021  42.144 13.249  1.00 21.86 ? 825  HOH A O   1 
HETATM 3226 O  O   . HOH M 4 .   ? 19.807  19.581 17.893  1.00 21.84 ? 826  HOH A O   1 
HETATM 3227 O  O   . HOH M 4 .   ? 9.726   40.741 34.016  1.00 21.26 ? 827  HOH A O   1 
HETATM 3228 O  O   . HOH M 4 .   ? 27.794  40.558 37.861  1.00 22.33 ? 828  HOH A O   1 
HETATM 3229 O  O   . HOH M 4 .   ? 0.567   27.311 21.475  1.00 21.48 ? 829  HOH A O   1 
HETATM 3230 O  O   . HOH M 4 .   ? 32.218  34.896 30.118  1.00 20.35 ? 830  HOH A O   1 
HETATM 3231 O  O   . HOH M 4 .   ? 24.022  49.362 24.674  1.00 19.19 ? 831  HOH A O   1 
HETATM 3232 O  O   . HOH M 4 .   ? 12.462  41.919 28.102  1.00 21.33 ? 832  HOH A O   1 
HETATM 3233 O  O   . HOH M 4 .   ? 21.690  36.322 37.503  1.00 22.18 ? 833  HOH A O   1 
HETATM 3234 O  O   . HOH M 4 .   ? 15.685  42.868 43.051  1.00 27.35 ? 834  HOH A O   1 
HETATM 3235 O  O   . HOH M 4 .   ? 6.384   22.193 20.775  1.00 27.98 ? 835  HOH A O   1 
HETATM 3236 O  O   . HOH M 4 .   ? 31.666  38.600 24.280  1.00 16.64 ? 836  HOH A O   1 
HETATM 3237 O  O   . HOH M 4 .   ? 16.642  19.353 24.432  1.00 20.68 ? 837  HOH A O   1 
HETATM 3238 O  O   . HOH M 4 .   ? 28.043  41.263 16.332  1.00 20.11 ? 838  HOH A O   1 
HETATM 3239 O  O   . HOH M 4 .   ? 31.564  43.700 14.939  1.00 26.57 ? 839  HOH A O   1 
HETATM 3240 O  O   . HOH M 4 .   ? -3.970  35.888 34.172  1.00 20.50 ? 840  HOH A O   1 
HETATM 3241 O  O   . HOH M 4 .   ? 25.507  26.016 20.061  1.00 23.77 ? 841  HOH A O   1 
HETATM 3242 O  O   . HOH M 4 .   ? 0.052   30.105 30.228  1.00 17.95 ? 842  HOH A O   1 
HETATM 3243 O  O   . HOH M 4 .   ? 15.869  42.401 34.175  1.00 27.87 ? 843  HOH A O   1 
HETATM 3244 O  O   . HOH M 4 .   ? 8.300   17.424 24.484  1.00 23.01 ? 844  HOH A O   1 
HETATM 3245 O  O   . HOH M 4 .   ? 29.581  48.381 14.840  1.00 22.51 ? 845  HOH A O   1 
HETATM 3246 O  O   . HOH M 4 .   ? 26.230  32.110 17.762  1.00 21.84 ? 846  HOH A O   1 
HETATM 3247 O  O   . HOH M 4 .   ? 12.312  48.065 19.837  1.00 28.23 ? 847  HOH A O   1 
HETATM 3248 O  O   . HOH M 4 .   ? -2.430  30.329 26.098  1.00 21.19 ? 848  HOH A O   1 
HETATM 3249 O  O   . HOH M 4 .   ? 0.445   28.123 17.710  1.00 23.12 ? 849  HOH A O   1 
HETATM 3250 O  O   . HOH M 4 .   ? 22.853  48.481 16.601  1.00 18.59 ? 850  HOH A O   1 
HETATM 3251 O  O   . HOH M 4 .   ? -5.100  36.885 21.986  1.00 22.21 ? 851  HOH A O   1 
HETATM 3252 O  O   . HOH M 4 .   ? 17.650  25.860 29.902  1.00 24.95 ? 852  HOH A O   1 
HETATM 3253 O  O   . HOH M 4 .   ? 2.146   37.412 35.614  1.00 28.58 ? 853  HOH A O   1 
HETATM 3254 O  O   . HOH M 4 .   ? -0.671  20.283 17.183  1.00 22.17 ? 854  HOH A O   1 
HETATM 3255 O  O   . HOH M 4 .   ? 26.998  43.484 19.143  1.00 25.14 ? 855  HOH A O   1 
HETATM 3256 O  O   . HOH M 4 .   ? 18.686  19.649 20.506  1.00 20.90 ? 856  HOH A O   1 
HETATM 3257 O  O   . HOH M 4 .   ? 20.099  47.533 24.902  1.00 24.53 ? 857  HOH A O   1 
HETATM 3258 O  O   . HOH M 4 .   ? 5.312   20.160 19.340  1.00 24.15 ? 858  HOH A O   1 
HETATM 3259 O  O   . HOH M 4 .   ? 18.050  38.918 42.882  1.00 25.14 ? 859  HOH A O   1 
HETATM 3260 O  O   . HOH M 4 .   ? 28.707  41.281 30.483  1.00 24.73 ? 860  HOH A O   1 
HETATM 3261 O  O   . HOH M 4 .   ? 10.029  21.659 25.909  1.00 21.32 ? 861  HOH A O   1 
HETATM 3262 O  O   . HOH M 4 .   ? 3.884   33.397 36.303  1.00 26.16 ? 862  HOH A O   1 
HETATM 3263 O  O   . HOH M 4 .   ? -7.054  42.565 34.196  1.00 31.27 ? 863  HOH A O   1 
HETATM 3264 O  O   . HOH M 4 .   ? 8.155   17.905 21.710  1.00 23.00 ? 864  HOH A O   1 
HETATM 3265 O  O   . HOH M 4 .   ? -6.598  36.805 33.213  1.00 29.66 ? 865  HOH A O   1 
HETATM 3266 O  O   . HOH M 4 .   ? 22.116  29.535 35.968  1.00 28.91 ? 866  HOH A O   1 
HETATM 3267 O  O   . HOH M 4 .   ? 4.927   23.236 22.645  1.00 24.35 ? 867  HOH A O   1 
HETATM 3268 O  O   . HOH M 4 .   ? 14.959  23.228 30.310  1.00 24.52 ? 868  HOH A O   1 
HETATM 3269 O  O   . HOH M 4 .   ? 23.554  28.510 33.748  1.00 24.86 ? 869  HOH A O   1 
HETATM 3270 O  O   . HOH M 4 .   ? 14.363  47.903 26.163  1.00 26.49 ? 870  HOH A O   1 
HETATM 3271 O  O   . HOH M 4 .   ? 16.624  48.649 26.959  1.00 35.90 ? 871  HOH A O   1 
HETATM 3272 O  O   . HOH M 4 .   ? -0.759  34.093 32.992  1.00 24.14 ? 872  HOH A O   1 
HETATM 3273 O  O   . HOH M 4 .   ? 11.974  41.480 10.314  1.00 27.59 ? 873  HOH A O   1 
HETATM 3274 O  O   . HOH M 4 .   ? 9.225   37.409 37.431  1.00 27.22 ? 874  HOH A O   1 
HETATM 3275 O  O   . HOH M 4 .   ? 3.244   23.923 26.203  1.00 29.69 ? 875  HOH A O   1 
HETATM 3276 O  O   . HOH M 4 .   ? -6.112  35.581 30.320  1.00 28.25 ? 876  HOH A O   1 
HETATM 3277 O  O   . HOH M 4 .   ? 12.029  24.973 33.280  1.00 28.60 ? 877  HOH A O   1 
HETATM 3278 O  O   . HOH M 4 .   ? 7.793   45.798 25.214  1.00 23.84 ? 878  HOH A O   1 
HETATM 3279 O  O   . HOH M 4 .   ? 1.907   34.142 33.723  1.00 25.50 ? 879  HOH A O   1 
HETATM 3280 O  O   . HOH M 4 .   ? 19.558  41.486 7.112   1.00 35.39 ? 880  HOH A O   1 
HETATM 3281 O  O   . HOH M 4 .   ? 14.034  14.815 16.702  1.00 25.06 ? 881  HOH A O   1 
HETATM 3282 O  O   . HOH M 4 .   ? 5.742   42.129 12.423  1.00 30.08 ? 882  HOH A O   1 
HETATM 3283 O  O   . HOH M 4 .   ? 15.369  32.364 38.230  1.00 31.84 ? 883  HOH A O   1 
HETATM 3284 O  O   . HOH M 4 .   ? 11.609  41.495 30.707  1.00 24.79 ? 884  HOH A O   1 
HETATM 3285 O  O   . HOH M 4 .   ? 32.269  31.430 33.102  1.00 39.01 ? 885  HOH A O   1 
HETATM 3286 O  O   . HOH M 4 .   ? 24.541  25.597 26.144  1.00 26.08 ? 886  HOH A O   1 
HETATM 3287 O  O   . HOH M 4 .   ? 17.802  16.683 15.154  1.00 33.06 ? 887  HOH A O   1 
HETATM 3288 O  O   . HOH M 4 .   ? 24.766  44.896 12.202  1.00 29.21 ? 888  HOH A O   1 
HETATM 3289 O  O   . HOH M 4 .   ? 9.522   25.973 13.938  1.00 25.06 ? 889  HOH A O   1 
HETATM 3290 O  O   . HOH M 4 .   ? 28.339  31.571 19.587  1.00 24.48 ? 890  HOH A O   1 
HETATM 3291 O  O   . HOH M 4 .   ? 24.395  26.916 30.219  1.00 25.22 ? 891  HOH A O   1 
HETATM 3292 O  O   . HOH M 4 .   ? 19.463  48.641 16.842  1.00 28.05 ? 892  HOH A O   1 
HETATM 3293 O  O   . HOH M 4 .   ? 4.146   43.521 33.273  1.00 30.55 ? 893  HOH A O   1 
HETATM 3294 O  O   . HOH M 4 .   ? 31.675  38.458 18.147  1.00 30.67 ? 894  HOH A O   1 
HETATM 3295 O  O   . HOH M 4 .   ? 23.703  22.181 25.024  1.00 28.01 ? 895  HOH A O   1 
HETATM 3296 O  O   . HOH M 4 .   ? 9.956   42.302 27.368  1.00 28.08 ? 896  HOH A O   1 
HETATM 3297 O  O   . HOH M 4 .   ? 9.415   25.503 34.688  1.00 32.79 ? 897  HOH A O   1 
HETATM 3298 O  O   . HOH M 4 .   ? 8.281   21.814 14.066  1.00 27.14 ? 898  HOH A O   1 
HETATM 3299 O  O   . HOH M 4 .   ? 7.180   42.366 30.320  1.00 27.53 ? 899  HOH A O   1 
HETATM 3300 O  O   . HOH M 4 .   ? 16.903  22.056 27.951  1.00 36.88 ? 900  HOH A O   1 
HETATM 3301 O  O   . HOH M 4 .   ? 28.865  36.091 12.368  1.00 36.38 ? 901  HOH A O   1 
HETATM 3302 O  O   . HOH M 4 .   ? 7.972   40.572 9.745   1.00 30.64 ? 902  HOH A O   1 
HETATM 3303 O  O   . HOH M 4 .   ? 33.164  36.385 22.991  1.00 28.63 ? 903  HOH A O   1 
HETATM 3304 O  O   . HOH M 4 .   ? 19.506  27.526 31.167  1.00 32.17 ? 904  HOH A O   1 
HETATM 3305 O  O   . HOH M 4 .   ? 30.700  28.925 23.465  1.00 50.72 ? 905  HOH A O   1 
HETATM 3306 O  O   . HOH M 4 .   ? 1.156   38.261 15.914  1.00 53.12 ? 906  HOH A O   1 
HETATM 3307 O  O   . HOH M 4 .   ? 26.574  23.075 22.521  1.00 43.39 ? 907  HOH A O   1 
HETATM 3308 O  O   . HOH M 4 .   ? -5.073  44.588 29.788  1.00 29.11 ? 908  HOH A O   1 
HETATM 3309 O  O   . HOH M 4 .   ? 29.862  41.043 12.623  1.00 34.36 ? 909  HOH A O   1 
HETATM 3310 O  O   . HOH M 4 .   ? -5.628  26.626 19.502  1.00 47.22 ? 910  HOH A O   1 
HETATM 3311 O  O   . HOH M 4 .   ? 32.247  30.605 27.476  1.00 31.98 ? 911  HOH A O   1 
HETATM 3312 O  O   . HOH M 4 .   ? 20.547  47.391 34.560  1.00 39.94 ? 912  HOH A O   1 
HETATM 3313 O  O   . HOH M 4 .   ? -8.836  39.504 33.260  1.00 29.51 ? 913  HOH A O   1 
HETATM 3314 O  O   . HOH M 4 .   ? 18.910  37.517 40.525  1.00 43.56 ? 914  HOH A O   1 
HETATM 3315 O  O   . HOH M 4 .   ? 12.316  42.047 5.536   1.00 34.86 ? 915  HOH A O   1 
HETATM 3316 O  O   . HOH M 4 .   ? 11.118  49.394 16.521  1.00 44.25 ? 916  HOH A O   1 
HETATM 3317 O  O   . HOH M 4 .   ? 5.444   46.460 18.962  1.00 40.35 ? 917  HOH A O   1 
HETATM 3318 O  O   . HOH M 4 .   ? 11.264  37.422 39.859  1.00 45.40 ? 918  HOH A O   1 
HETATM 3319 O  O   . HOH M 4 .   ? 4.365   28.897 39.394  1.00 34.54 ? 919  HOH A O   1 
HETATM 3320 O  O   . HOH M 4 .   ? 26.936  38.565 28.807  1.00 15.06 ? 920  HOH A O   1 
HETATM 3321 O  O   . HOH M 4 .   ? 27.774  40.162 26.739  1.00 16.28 ? 921  HOH A O   1 
HETATM 3322 O  O   . HOH M 4 .   ? 6.004   20.774 25.759  1.00 22.31 ? 922  HOH A O   1 
HETATM 3323 O  O   . HOH M 4 .   ? 30.500  41.338 21.467  1.00 19.08 ? 923  HOH A O   1 
HETATM 3324 O  O   . HOH M 4 .   ? 14.322  44.029 28.190  1.00 20.68 ? 924  HOH A O   1 
HETATM 3325 O  O   . HOH M 4 .   ? 5.931   17.872 20.412  1.00 23.03 ? 925  HOH A O   1 
HETATM 3326 O  O   . HOH M 4 .   ? 8.811   23.983 12.238  1.00 24.48 ? 926  HOH A O   1 
HETATM 3327 O  O   . HOH M 4 .   ? 3.400   21.274 26.299  1.00 23.82 ? 927  HOH A O   1 
HETATM 3328 O  O   . HOH M 4 .   ? -0.224  26.535 24.030  1.00 28.90 ? 928  HOH A O   1 
HETATM 3329 O  O   . HOH M 4 .   ? -1.741  27.819 25.930  1.00 24.71 ? 929  HOH A O   1 
HETATM 3330 O  O   . HOH M 4 .   ? 9.317   29.366 10.941  1.00 27.82 ? 930  HOH A O   1 
HETATM 3331 O  O   . HOH M 4 .   ? 18.894  36.646 44.559  1.00 27.49 ? 931  HOH A O   1 
HETATM 3332 O  O   . HOH M 4 .   ? 0.994   24.269 24.433  1.00 31.97 ? 932  HOH A O   1 
HETATM 3333 O  O   . HOH M 4 .   ? 35.502  37.653 22.626  1.00 33.47 ? 933  HOH A O   1 
HETATM 3334 O  O   . HOH M 4 .   ? 20.559  32.407 38.362  1.00 30.84 ? 934  HOH A O   1 
HETATM 3335 O  O   . HOH M 4 .   ? 8.356   42.644 32.323  1.00 44.65 ? 935  HOH A O   1 
HETATM 3336 O  O   . HOH M 4 .   ? 19.582  19.969 23.135  1.00 27.98 ? 936  HOH A O   1 
HETATM 3337 O  O   . HOH M 4 .   ? 1.974   31.934 37.540  1.00 29.88 ? 937  HOH A O   1 
HETATM 3338 O  O   . HOH M 4 .   ? -5.823  38.384 19.533  1.00 37.01 ? 938  HOH A O   1 
HETATM 3339 O  O   . HOH M 4 .   ? 27.800  51.814 19.386  1.00 34.75 ? 939  HOH A O   1 
HETATM 3340 O  O   . HOH M 4 .   ? -0.885  27.630 28.980  1.00 35.67 ? 940  HOH A O   1 
HETATM 3341 O  O   . HOH M 4 .   ? 1.312   39.972 35.959  1.00 31.93 ? 941  HOH A O   1 
HETATM 3342 O  O   . HOH M 4 .   ? 32.776  34.436 32.635  1.00 48.96 ? 942  HOH A O   1 
HETATM 3343 O  O   . HOH M 4 .   ? 0.337   43.982 25.013  1.00 29.16 ? 943  HOH A O   1 
HETATM 3344 O  O   . HOH M 4 .   ? 30.471  41.016 17.153  1.00 41.13 ? 944  HOH A O   1 
HETATM 3345 O  O   . HOH M 4 .   ? 5.210   47.019 24.638  1.00 50.88 ? 945  HOH A O   1 
HETATM 3346 O  O   . HOH M 4 .   ? -5.000  30.096 27.266  1.00 33.71 ? 946  HOH A O   1 
HETATM 3347 O  O   . HOH M 4 .   ? 7.446   26.624 15.150  1.00 35.80 ? 947  HOH A O   1 
HETATM 3348 O  O   . HOH M 4 .   ? -2.691  20.611 19.439  1.00 38.93 ? 948  HOH A O   1 
HETATM 3349 O  O   . HOH M 4 .   ? 26.962  27.149 17.730  1.00 46.45 ? 949  HOH A O   1 
HETATM 3350 O  O   . HOH M 4 .   ? 24.160  32.203 13.433  1.00 40.36 ? 950  HOH A O   1 
HETATM 3351 O  O   . HOH M 4 .   ? -6.276  43.512 36.509  1.00 43.36 ? 951  HOH A O   1 
HETATM 3352 O  O   . HOH M 4 .   ? 9.515   41.560 36.428  1.00 36.99 ? 952  HOH A O   1 
HETATM 3353 O  O   . HOH M 4 .   ? 20.315  38.278 38.528  1.00 32.31 ? 953  HOH A O   1 
HETATM 3354 O  O   . HOH M 4 .   ? 21.612  51.571 24.071  1.00 37.03 ? 954  HOH A O   1 
HETATM 3355 O  O   . HOH M 4 .   ? 28.302  29.366 20.399  1.00 44.32 ? 955  HOH A O   1 
HETATM 3356 O  O   . HOH M 4 .   ? 29.796  38.676 38.767  1.00 42.25 ? 956  HOH A O   1 
HETATM 3357 O  O   . HOH M 4 .   ? -0.895  40.000 17.848  1.00 38.31 ? 957  HOH A O   1 
HETATM 3358 O  O   . HOH M 4 .   ? 18.747  18.538 26.326  1.00 38.59 ? 958  HOH A O   1 
HETATM 3359 O  O   . HOH M 4 .   ? -0.774  44.860 30.204  1.00 41.10 ? 959  HOH A O   1 
HETATM 3360 O  O   . HOH M 4 .   ? -8.481  38.491 22.193  1.00 51.26 ? 960  HOH A O   1 
HETATM 3361 O  O   . HOH M 4 .   ? -0.396  31.069 12.885  1.00 62.67 ? 961  HOH A O   1 
HETATM 3362 O  O   . HOH M 4 .   ? 4.380   40.974 14.659  1.00 32.79 ? 962  HOH A O   1 
HETATM 3363 O  O   . HOH M 4 .   ? 2.147   26.066 36.513  1.00 46.13 ? 963  HOH A O   1 
HETATM 3364 O  O   . HOH M 4 .   ? 5.234   31.653 38.578  1.00 36.32 ? 964  HOH A O   1 
HETATM 3365 O  O   . HOH M 4 .   ? 4.444   23.816 34.160  1.00 34.23 ? 965  HOH A O   1 
HETATM 3366 O  O   . HOH M 4 .   ? 29.607  31.022 17.298  1.00 49.93 ? 966  HOH A O   1 
HETATM 3367 O  O   . HOH M 4 .   ? -3.633  43.391 32.151  1.00 41.01 ? 967  HOH A O   1 
HETATM 3368 O  O   . HOH M 4 .   ? 26.920  31.557 15.059  1.00 38.90 ? 968  HOH A O   1 
HETATM 3369 O  O   . HOH M 4 .   ? 17.084  39.365 38.382  1.00 35.80 ? 969  HOH A O   1 
HETATM 3370 O  O   . HOH M 4 .   ? 1.303   29.739 38.831  1.00 43.87 ? 970  HOH A O   1 
HETATM 3371 O  O   . HOH M 4 .   ? -11.000 39.919 31.281  1.00 32.91 ? 971  HOH A O   1 
HETATM 3372 O  O   . HOH M 4 .   ? 28.494  49.059 12.410  1.00 43.00 ? 972  HOH A O   1 
HETATM 3373 O  O   . HOH M 4 .   ? 4.145   28.021 41.923  1.00 41.15 ? 973  HOH A O   1 
HETATM 3374 O  O   . HOH M 4 .   ? 2.355   33.617 13.841  1.00 39.57 ? 974  HOH A O   1 
HETATM 3375 O  O   . HOH M 4 .   ? 26.466  27.927 34.583  1.00 62.88 ? 975  HOH A O   1 
HETATM 3376 O  O   . HOH M 4 .   ? 13.567  50.575 20.534  1.00 37.33 ? 976  HOH A O   1 
HETATM 3377 O  O   . HOH M 4 .   ? -0.545  43.970 18.075  1.00 34.79 ? 977  HOH A O   1 
HETATM 3378 O  O   . HOH M 4 .   ? 4.424   22.264 15.873  1.00 61.49 ? 978  HOH A O   1 
HETATM 3379 O  O   . HOH M 4 .   ? 7.324   21.131 23.101  1.00 41.89 ? 979  HOH A O   1 
HETATM 3380 O  O   . HOH M 4 .   ? 28.296  26.952 27.725  1.00 39.58 ? 980  HOH A O   1 
HETATM 3381 O  O   . HOH M 4 .   ? 7.346   28.741 13.151  1.00 33.92 ? 981  HOH A O   1 
HETATM 3382 O  O   . HOH M 4 .   ? 24.999  36.836 10.839  1.00 36.17 ? 982  HOH A O   1 
HETATM 3383 O  O   . HOH M 4 .   ? 24.389  21.996 27.645  1.00 44.91 ? 983  HOH A O   1 
HETATM 3384 O  O   . HOH M 4 .   ? 18.371  23.563 31.077  1.00 37.84 ? 984  HOH A O   1 
HETATM 3385 O  O   . HOH M 4 .   ? -12.309 43.050 27.603  1.00 56.64 ? 985  HOH A O   1 
HETATM 3386 O  O   . HOH M 4 .   ? -13.067 41.643 31.894  1.00 41.53 ? 986  HOH A O   1 
HETATM 3387 O  O   . HOH M 4 .   ? -3.628  40.237 17.918  1.00 38.33 ? 987  HOH A O   1 
HETATM 3388 O  O   . HOH M 4 .   ? -0.109  28.763 15.165  1.00 53.14 ? 988  HOH A O   1 
HETATM 3389 O  O   . HOH M 4 .   ? 31.584  41.134 14.724  1.00 38.49 ? 989  HOH A O   1 
HETATM 3390 O  O   . HOH M 4 .   ? 22.968  35.337 39.646  1.00 32.34 ? 990  HOH A O   1 
HETATM 3391 O  O   . HOH M 4 .   ? -3.987  25.685 25.853  1.00 59.64 ? 991  HOH A O   1 
HETATM 3392 O  O   . HOH M 4 .   ? 19.921  16.402 25.490  1.00 34.33 ? 992  HOH A O   1 
HETATM 3393 O  O   . HOH M 4 .   ? 28.651  30.560 35.251  1.00 37.66 ? 993  HOH A O   1 
HETATM 3394 O  O   . HOH M 4 .   ? -6.588  32.070 28.223  1.00 53.48 ? 994  HOH A O   1 
HETATM 3395 O  O   . HOH M 4 .   ? 12.457  41.345 32.863  1.00 44.02 ? 995  HOH A O   1 
HETATM 3396 O  O   . HOH M 4 .   ? 13.906  44.805 30.730  1.00 51.83 ? 996  HOH A O   1 
HETATM 3397 O  O   . HOH M 4 .   ? -0.118  27.934 33.966  1.00 40.54 ? 997  HOH A O   1 
HETATM 3398 O  O   . HOH M 4 .   ? 21.387  53.019 22.177  1.00 47.61 ? 998  HOH A O   1 
HETATM 3399 O  O   . HOH M 4 .   ? 23.787  52.432 20.631  1.00 46.65 ? 999  HOH A O   1 
HETATM 3400 O  O   . HOH M 4 .   ? -7.684  38.262 30.545  1.00 34.91 ? 1000 HOH A O   1 
HETATM 3401 O  O   . HOH M 4 .   ? 26.697  27.825 23.054  1.00 39.84 ? 1001 HOH A O   1 
HETATM 3402 O  O   . HOH M 4 .   ? 27.492  25.551 29.608  1.00 88.42 ? 1002 HOH A O   1 
HETATM 3403 O  O   . HOH M 4 .   ? 3.696   43.927 15.643  1.00 44.50 ? 1003 HOH A O   1 
HETATM 3404 O  O   . HOH M 4 .   ? 28.135  33.661 14.376  1.00 38.35 ? 1004 HOH A O   1 
HETATM 3405 O  O   . HOH M 4 .   ? 13.471  46.685 28.043  1.00 36.10 ? 1005 HOH A O   1 
HETATM 3406 O  O   . HOH M 4 .   ? 26.212  45.713 10.325  1.00 48.77 ? 1006 HOH A O   1 
HETATM 3407 O  O   . HOH M 4 .   ? 7.634   45.769 11.957  1.00 49.70 ? 1007 HOH A O   1 
HETATM 3408 O  O   . HOH M 4 .   ? 30.377  46.210 11.164  1.00 37.39 ? 1008 HOH A O   1 
HETATM 3409 O  O   . HOH M 4 .   ? -1.729  25.320 16.466  1.00 48.27 ? 1009 HOH A O   1 
HETATM 3410 O  O   . HOH M 4 .   ? 22.953  26.483 28.170  1.00 33.46 ? 1010 HOH A O   1 
HETATM 3411 O  O   . HOH M 4 .   ? 22.875  51.245 17.200  1.00 33.71 ? 1011 HOH A O   1 
HETATM 3412 O  O   . HOH M 4 .   ? 11.400  42.169 7.851   1.00 49.14 ? 1012 HOH A O   1 
HETATM 3413 O  O   . HOH M 4 .   ? 13.182  43.279 41.822  1.00 34.64 ? 1013 HOH A O   1 
HETATM 3414 O  O   . HOH M 4 .   ? 12.177  42.767 37.162  1.00 43.30 ? 1014 HOH A O   1 
HETATM 3415 O  O   . HOH M 4 .   ? 1.638   25.394 12.714  1.00 54.94 ? 1015 HOH A O   1 
HETATM 3416 O  O   . HOH M 4 .   ? -7.203  35.696 17.883  1.00 50.02 ? 1016 HOH A O   1 
HETATM 3417 O  O   . HOH M 4 .   ? 19.483  51.946 20.095  1.00 52.21 ? 1017 HOH A O   1 
HETATM 3418 O  O   . HOH M 4 .   ? 16.226  41.945 -4.502  1.00 56.97 ? 1018 HOH A O   1 
HETATM 3419 O  O   . HOH M 4 .   ? -5.318  43.889 23.057  1.00 40.82 ? 1019 HOH A O   1 
HETATM 3420 O  O   . HOH M 4 .   ? 2.249   42.558 34.463  1.00 35.49 ? 1020 HOH A O   1 
HETATM 3421 O  O   . HOH M 4 .   ? -10.559 39.848 28.450  1.00 36.59 ? 1021 HOH A O   1 
HETATM 3422 O  O   . HOH M 4 .   ? 12.263  52.427 18.712  1.00 65.82 ? 1022 HOH A O   1 
HETATM 3423 O  O   . HOH M 4 .   ? -4.944  32.872 13.474  1.00 46.42 ? 1023 HOH A O   1 
HETATM 3424 O  O   . HOH M 4 .   ? -3.207  42.987 18.009  1.00 45.53 ? 1024 HOH A O   1 
HETATM 3425 O  O   . HOH M 4 .   ? 19.320  50.076 24.081  1.00 26.86 ? 1025 HOH A O   1 
HETATM 3426 O  O   . HOH M 4 .   ? 14.927  44.424 33.621  1.00 58.81 ? 1026 HOH A O   1 
HETATM 3427 O  O   . HOH M 4 .   ? -6.540  42.399 20.783  1.00 41.41 ? 1027 HOH A O   1 
HETATM 3428 O  O   . HOH M 4 .   ? 22.945  50.832 26.708  1.00 30.47 ? 1028 HOH A O   1 
HETATM 3429 O  O   . HOH M 4 .   ? -3.001  23.932 23.786  1.00 48.80 ? 1029 HOH A O   1 
HETATM 3430 O  O   . HOH M 4 .   ? 8.182   48.097 27.201  1.00 50.98 ? 1030 HOH A O   1 
HETATM 3431 O  O   . HOH M 4 .   ? 1.354   45.917 31.977  1.00 53.41 ? 1031 HOH A O   1 
HETATM 3432 O  O   . HOH M 4 .   ? 6.930   31.212 37.058  1.00 28.83 ? 1032 HOH A O   1 
HETATM 3433 O  O   . HOH M 4 .   ? 5.522   40.574 9.727   1.00 39.35 ? 1033 HOH A O   1 
HETATM 3434 O  O   . HOH M 4 .   ? 33.488  32.399 23.750  1.00 58.43 ? 1034 HOH A O   1 
HETATM 3435 O  O   . HOH M 4 .   ? 3.867   39.886 8.245   1.00 50.09 ? 1035 HOH A O   1 
HETATM 3436 O  O   . HOH M 4 .   ? 16.382  41.509 37.961  1.00 52.83 ? 1036 HOH A O   1 
HETATM 3437 O  O   . HOH M 4 .   ? 26.841  22.058 19.831  1.00 53.36 ? 1037 HOH A O   1 
HETATM 3438 O  O   . HOH M 4 .   ? 26.697  24.459 18.180  1.00 42.14 ? 1038 HOH A O   1 
HETATM 3439 O  O   . HOH M 4 .   ? 13.738  42.972 11.001  1.00 32.14 ? 1039 HOH A O   1 
HETATM 3440 O  O   . HOH M 4 .   ? 27.598  47.317 11.211  1.00 45.29 ? 1040 HOH A O   1 
HETATM 3441 O  O   . HOH M 4 .   ? 23.856  47.911 8.742   1.00 52.10 ? 1041 HOH A O   1 
HETATM 3442 O  O   . HOH M 4 .   ? 12.484  49.518 14.678  1.00 47.36 ? 1042 HOH A O   1 
HETATM 3443 O  O   . HOH M 4 .   ? 17.760  53.448 24.094  1.00 49.23 ? 1043 HOH A O   1 
HETATM 3444 O  O   . HOH M 4 .   ? 12.477  49.676 25.070  1.00 49.19 ? 1044 HOH A O   1 
HETATM 3445 O  O   . HOH M 4 .   ? 8.068   43.449 25.984  1.00 30.79 ? 1045 HOH A O   1 
HETATM 3446 O  O   . HOH M 4 .   ? -6.261  34.604 26.007  1.00 49.35 ? 1046 HOH A O   1 
HETATM 3447 O  O   . HOH M 4 .   ? 2.520   22.292 14.586  1.00 55.12 ? 1047 HOH A O   1 
HETATM 3448 O  O   . HOH M 4 .   ? 18.435  42.314 1.991   1.00 58.70 ? 1048 HOH A O   1 
HETATM 3449 O  O   . HOH M 4 .   ? 17.796  50.650 26.216  1.00 45.55 ? 1049 HOH A O   1 
HETATM 3450 O  O   . HOH M 4 .   ? 24.587  36.338 8.636   1.00 49.41 ? 1050 HOH A O   1 
HETATM 3451 O  O   . HOH M 4 .   ? 31.800  39.032 20.946  1.00 20.33 ? 1051 HOH A O   1 
HETATM 3452 O  O   . HOH M 4 .   ? 26.743  42.525 38.523  1.00 30.63 ? 1052 HOH A O   1 
HETATM 3453 O  O   . HOH M 4 .   ? -1.179  42.501 31.475  1.00 34.38 ? 1053 HOH A O   1 
HETATM 3454 O  O   . HOH M 4 .   ? -2.276  46.084 20.117  1.00 66.07 ? 1054 HOH A O   1 
HETATM 3455 O  O   . HOH M 4 .   ? -6.849  34.589 21.986  1.00 48.78 ? 1055 HOH A O   1 
HETATM 3456 O  O   . HOH M 4 .   ? -0.157  30.835 37.431  1.00 50.14 ? 1056 HOH A O   1 
HETATM 3457 O  O   . HOH M 4 .   ? 0.000   35.866 35.770  0.50 34.52 ? 1057 HOH A O   1 
HETATM 3458 O  O   . HOH M 4 .   ? 18.979  21.014 28.153  1.00 45.12 ? 1058 HOH A O   1 
HETATM 3459 O  O   . HOH M 4 .   ? 2.518   41.740 36.996  1.00 40.10 ? 1059 HOH A O   1 
HETATM 3460 O  O   . HOH M 4 .   ? 28.767  26.981 25.329  1.00 66.61 ? 1060 HOH A O   1 
HETATM 3461 O  O   . HOH M 4 .   ? -6.059  32.139 24.773  1.00 46.40 ? 1061 HOH A O   1 
HETATM 3462 O  O   . HOH M 4 .   ? 6.149   30.418 40.290  1.00 45.25 ? 1062 HOH A O   1 
HETATM 3463 O  O   . HOH M 4 .   ? 1.032   44.604 27.461  1.00 45.68 ? 1063 HOH A O   1 
HETATM 3464 O  O   . HOH M 4 .   ? -4.368  32.218 18.369  1.00 40.44 ? 1064 HOH A O   1 
HETATM 3465 O  O   . HOH M 4 .   ? 31.123  30.875 21.373  1.00 45.07 ? 1065 HOH A O   1 
HETATM 3466 O  O   . HOH M 4 .   ? -2.073  22.203 16.175  1.00 54.80 ? 1066 HOH A O   1 
HETATM 3467 O  O   . HOH M 4 .   ? 28.076  27.535 32.199  1.00 43.76 ? 1067 HOH A O   1 
HETATM 3468 O  O   . HOH M 4 .   ? -0.265  42.563 15.392  1.00 62.86 ? 1068 HOH A O   1 
HETATM 3469 O  O   . HOH M 4 .   ? 10.611  47.102 28.700  1.00 41.24 ? 1069 HOH A O   1 
HETATM 3470 O  O   . HOH M 4 .   ? 16.233  40.180 -2.459  1.00 47.64 ? 1070 HOH A O   1 
HETATM 3471 O  O   . HOH M 4 .   ? 28.239  28.293 15.447  1.00 65.57 ? 1071 HOH A O   1 
HETATM 3472 O  O   . HOH M 4 .   ? 35.464  36.285 19.465  1.00 44.05 ? 1072 HOH A O   1 
HETATM 3473 O  O   . HOH M 4 .   ? -8.376  36.446 25.557  1.00 45.35 ? 1073 HOH A O   1 
HETATM 3474 O  O   . HOH M 4 .   ? -6.159  46.554 22.562  1.00 58.04 ? 1074 HOH A O   1 
HETATM 3475 O  O   . HOH M 4 .   ? 17.230  42.580 40.250  1.00 48.03 ? 1075 HOH A O   1 
HETATM 3476 O  O   . HOH M 4 .   ? 26.080  53.593 19.423  1.00 47.71 ? 1076 HOH A O   1 
HETATM 3477 O  O   . HOH M 4 .   ? 0.557   35.334 14.606  1.00 49.71 ? 1077 HOH A O   1 
HETATM 3478 O  O   . HOH M 4 .   ? 19.736  40.079 4.438   1.00 49.56 ? 1078 HOH A O   1 
HETATM 3479 O  O   . HOH M 4 .   ? 28.376  33.192 35.864  1.00 55.88 ? 1079 HOH A O   1 
HETATM 3480 O  O   . HOH M 4 .   ? 9.907   44.819 29.144  1.00 41.87 ? 1080 HOH A O   1 
HETATM 3481 O  O   . HOH M 4 .   ? -0.097  23.739 27.112  1.00 47.62 ? 1081 HOH A O   1 
HETATM 3482 O  O   . HOH M 4 .   ? -7.714  36.703 28.860  1.00 60.08 ? 1082 HOH A O   1 
HETATM 3483 O  O   . HOH M 4 .   ? 30.865  39.726 10.748  1.00 69.80 ? 1083 HOH A O   1 
HETATM 3484 O  O   . HOH M 4 .   ? -6.826  31.805 21.394  1.00 43.55 ? 1084 HOH A O   1 
HETATM 3485 O  O   . HOH M 4 .   ? 6.261   24.004 16.170  1.00 61.81 ? 1085 HOH A O   1 
HETATM 3486 O  O   . HOH M 4 .   ? 21.736  23.331 30.717  1.00 52.01 ? 1086 HOH A O   1 
HETATM 3487 O  O   . HOH M 4 .   ? 18.946  44.643 36.565  1.00 72.59 ? 1087 HOH A O   1 
HETATM 3488 O  O   . HOH M 4 .   ? -10.407 44.237 23.571  1.00 65.40 ? 1088 HOH A O   1 
HETATM 3489 O  O   . HOH M 4 .   ? 2.865   45.419 18.554  1.00 59.28 ? 1089 HOH A O   1 
HETATM 3490 O  O   . HOH M 4 .   ? 19.272  49.222 14.637  1.00 46.03 ? 1090 HOH A O   1 
HETATM 3491 O  O   . HOH M 4 .   ? 24.265  23.963 33.829  1.00 57.07 ? 1091 HOH A O   1 
HETATM 3492 O  O   . HOH M 4 .   ? 20.756  20.689 29.572  1.00 58.29 ? 1092 HOH A O   1 
HETATM 3493 O  O   . HOH M 4 .   ? 15.082  51.888 10.666  1.00 55.13 ? 1093 HOH A O   1 
HETATM 3494 O  O   . HOH M 4 .   ? 15.115  15.151 19.119  1.00 48.78 ? 1094 HOH A O   1 
HETATM 3495 O  O   . HOH M 4 .   ? -5.578  30.659 14.741  1.00 70.76 ? 1095 HOH A O   1 
HETATM 3496 O  O   . HOH M 4 .   ? -8.658  36.355 19.826  1.00 58.75 ? 1096 HOH A O   1 
HETATM 3497 O  O   . HOH M 4 .   ? -4.909  23.089 17.175  1.00 72.35 ? 1097 HOH A O   1 
HETATM 3498 O  O   . HOH N 4 .   ? 13.509  24.292 10.688  1.00 14.26 ? 803  HOH B O   1 
HETATM 3499 O  O   . HOH N 4 .   ? 4.597   4.637  -9.842  1.00 19.04 ? 804  HOH B O   1 
HETATM 3500 O  O   . HOH N 4 .   ? 11.539  26.433 10.281  1.00 19.80 ? 805  HOH B O   1 
HETATM 3501 O  O   . HOH N 4 .   ? 10.894  33.285 9.716   1.00 18.45 ? 806  HOH B O   1 
HETATM 3502 O  O   . HOH N 4 .   ? 9.468   24.623 9.640   1.00 22.02 ? 807  HOH B O   1 
HETATM 3503 O  O   . HOH N 4 .   ? 4.824   9.994  0.709   1.00 27.25 ? 808  HOH B O   1 
HETATM 3504 O  O   . HOH N 4 .   ? 5.110   16.992 -5.189  1.00 21.21 ? 809  HOH B O   1 
HETATM 3505 O  O   . HOH N 4 .   ? 11.482  7.528  -8.527  1.00 26.33 ? 810  HOH B O   1 
HETATM 3506 O  O   . HOH N 4 .   ? 3.988   11.053 9.751   1.00 25.37 ? 811  HOH B O   1 
HETATM 3507 O  O   . HOH N 4 .   ? 4.783   18.304 -7.635  1.00 24.69 ? 812  HOH B O   1 
HETATM 3508 O  O   . HOH N 4 .   ? 3.943   7.349  -7.771  1.00 26.10 ? 813  HOH B O   1 
HETATM 3509 O  O   . HOH N 4 .   ? 6.777   14.665 -10.195 1.00 29.15 ? 814  HOH B O   1 
HETATM 3510 O  O   . HOH N 4 .   ? 17.000  33.350 -7.786  1.00 42.92 ? 815  HOH B O   1 
HETATM 3511 O  O   . HOH N 4 .   ? 5.687   28.953 -4.660  1.00 38.63 ? 816  HOH B O   1 
HETATM 3512 O  O   . HOH N 4 .   ? 12.703  39.152 4.682   1.00 25.23 ? 817  HOH B O   1 
HETATM 3513 O  O   . HOH N 4 .   ? 6.507   10.599 8.158   1.00 41.89 ? 818  HOH B O   1 
HETATM 3514 O  O   . HOH N 4 .   ? 8.512   17.829 8.699   1.00 25.89 ? 819  HOH B O   1 
HETATM 3515 O  O   . HOH N 4 .   ? 13.931  8.049  -2.266  1.00 41.94 ? 820  HOH B O   1 
HETATM 3516 O  O   . HOH N 4 .   ? 11.621  38.446 2.247   1.00 27.80 ? 821  HOH B O   1 
HETATM 3517 O  O   . HOH N 4 .   ? 2.717   16.695 -3.472  1.00 24.36 ? 822  HOH B O   1 
HETATM 3518 O  O   . HOH N 4 .   ? 5.437   11.075 -11.433 1.00 28.42 ? 823  HOH B O   1 
HETATM 3519 O  O   . HOH N 4 .   ? 20.896  38.047 2.756   1.00 34.10 ? 824  HOH B O   1 
HETATM 3520 O  O   . HOH N 4 .   ? 19.140  16.371 -11.145 1.00 33.45 ? 825  HOH B O   1 
HETATM 3521 O  O   . HOH N 4 .   ? 2.070   13.740 4.057   1.00 49.51 ? 826  HOH B O   1 
HETATM 3522 O  O   . HOH N 4 .   ? 17.090  15.455 13.000  1.00 34.43 ? 827  HOH B O   1 
HETATM 3523 O  O   . HOH N 4 .   ? 19.959  23.737 -8.758  1.00 34.43 ? 828  HOH B O   1 
HETATM 3524 O  O   . HOH N 4 .   ? 3.739   20.292 4.968   1.00 32.55 ? 829  HOH B O   1 
HETATM 3525 O  O   . HOH N 4 .   ? 8.737   16.231 -11.238 1.00 32.11 ? 830  HOH B O   1 
HETATM 3526 O  O   . HOH N 4 .   ? 3.425   10.265 -7.598  1.00 30.53 ? 831  HOH B O   1 
HETATM 3527 O  O   . HOH N 4 .   ? 10.298  3.846  -6.329  1.00 46.79 ? 832  HOH B O   1 
HETATM 3528 O  O   . HOH N 4 .   ? 4.247   27.909 2.542   1.00 38.73 ? 833  HOH B O   1 
HETATM 3529 O  O   . HOH N 4 .   ? 20.841  17.696 12.203  1.00 31.00 ? 834  HOH B O   1 
HETATM 3530 O  O   . HOH N 4 .   ? 0.358   15.684 -4.869  1.00 37.56 ? 835  HOH B O   1 
HETATM 3531 O  O   . HOH N 4 .   ? 33.818  19.107 6.317   1.00 42.88 ? 836  HOH B O   1 
HETATM 3532 O  O   . HOH N 4 .   ? 10.162  2.896  -8.430  1.00 30.19 ? 837  HOH B O   1 
HETATM 3533 O  O   . HOH N 4 .   ? 10.065  30.944 4.078   1.00 27.70 ? 838  HOH B O   1 
HETATM 3534 O  O   . HOH N 4 .   ? 1.929   19.190 -3.436  1.00 33.13 ? 839  HOH B O   1 
HETATM 3535 O  O   . HOH N 4 .   ? 26.371  22.117 16.115  1.00 38.64 ? 840  HOH B O   1 
HETATM 3536 O  O   . HOH N 4 .   ? 9.615   10.590 5.009   1.00 40.27 ? 841  HOH B O   1 
HETATM 3537 O  O   . HOH N 4 .   ? 9.720   40.004 7.662   1.00 32.16 ? 842  HOH B O   1 
HETATM 3538 O  O   . HOH N 4 .   ? 11.186  29.591 5.945   1.00 30.49 ? 843  HOH B O   1 
HETATM 3539 O  O   . HOH N 4 .   ? 2.881   10.601 -4.178  1.00 46.76 ? 844  HOH B O   1 
HETATM 3540 O  O   . HOH N 4 .   ? 20.055  7.843  1.569   1.00 38.80 ? 845  HOH B O   1 
HETATM 3541 O  O   . HOH N 4 .   ? 16.811  12.244 -3.475  1.00 38.01 ? 846  HOH B O   1 
HETATM 3542 O  O   . HOH N 4 .   ? 9.950   28.371 8.034   1.00 33.37 ? 847  HOH B O   1 
HETATM 3543 O  O   . HOH N 4 .   ? 26.095  13.998 -3.769  1.00 47.06 ? 848  HOH B O   1 
HETATM 3544 O  O   . HOH N 4 .   ? 5.347   8.281  3.019   1.00 40.81 ? 849  HOH B O   1 
HETATM 3545 O  O   . HOH N 4 .   ? 5.900   29.961 -1.975  1.00 36.42 ? 850  HOH B O   1 
HETATM 3546 O  O   . HOH N 4 .   ? 32.882  26.513 0.582   1.00 39.91 ? 851  HOH B O   1 
HETATM 3547 O  O   . HOH N 4 .   ? 21.219  17.284 16.897  1.00 38.02 ? 852  HOH B O   1 
HETATM 3548 O  O   . HOH N 4 .   ? 22.271  35.514 -1.832  1.00 37.52 ? 853  HOH B O   1 
HETATM 3549 O  O   . HOH N 4 .   ? 5.333   24.357 12.960  1.00 43.03 ? 854  HOH B O   1 
HETATM 3550 O  O   . HOH N 4 .   ? 14.900  12.936 8.133   1.00 34.03 ? 855  HOH B O   1 
HETATM 3551 O  O   . HOH N 4 .   ? 3.477   32.331 9.156   1.00 39.65 ? 856  HOH B O   1 
HETATM 3552 O  O   . HOH N 4 .   ? 7.335   26.113 8.766   1.00 37.21 ? 857  HOH B O   1 
HETATM 3553 O  O   . HOH N 4 .   ? 9.656   17.767 -13.341 1.00 38.19 ? 858  HOH B O   1 
HETATM 3554 O  O   . HOH N 4 .   ? 1.115   13.342 -1.385  1.00 41.99 ? 859  HOH B O   1 
HETATM 3555 O  O   . HOH N 4 .   ? 22.879  17.844 25.571  1.00 40.98 ? 860  HOH B O   1 
HETATM 3556 O  O   . HOH N 4 .   ? 20.148  14.975 -4.764  1.00 42.65 ? 861  HOH B O   1 
HETATM 3557 O  O   . HOH N 4 .   ? 10.986  21.554 -14.653 1.00 40.87 ? 862  HOH B O   1 
HETATM 3558 O  O   . HOH N 4 .   ? 21.738  20.095 25.303  1.00 37.39 ? 863  HOH B O   1 
HETATM 3559 O  O   . HOH N 4 .   ? 27.084  16.621 18.221  1.00 54.12 ? 864  HOH B O   1 
HETATM 3560 O  O   . HOH N 4 .   ? 2.782   24.367 0.335   1.00 42.48 ? 865  HOH B O   1 
HETATM 3561 O  O   . HOH N 4 .   ? 34.068  22.728 13.439  1.00 54.72 ? 866  HOH B O   1 
HETATM 3562 O  O   . HOH N 4 .   ? 23.086  37.276 -0.605  1.00 44.19 ? 867  HOH B O   1 
HETATM 3563 O  O   . HOH N 4 .   ? 27.817  35.041 -13.842 1.00 43.73 ? 868  HOH B O   1 
HETATM 3564 O  O   . HOH N 4 .   ? 25.795  33.747 4.858   1.00 35.76 ? 869  HOH B O   1 
HETATM 3565 O  O   . HOH N 4 .   ? 19.371  13.233 -2.905  1.00 40.59 ? 870  HOH B O   1 
HETATM 3566 O  O   . HOH N 4 .   ? 32.327  26.017 8.107   1.00 39.04 ? 871  HOH B O   1 
HETATM 3567 O  O   . HOH N 4 .   ? -1.681  14.267 -1.058  1.00 47.98 ? 872  HOH B O   1 
HETATM 3568 O  O   . HOH N 4 .   ? 17.641  13.603 -7.760  1.00 51.74 ? 873  HOH B O   1 
HETATM 3569 O  O   . HOH N 4 .   ? 33.960  16.293 4.904   1.00 67.13 ? 874  HOH B O   1 
HETATM 3570 O  O   . HOH N 4 .   ? 15.441  10.626 6.963   1.00 48.59 ? 875  HOH B O   1 
HETATM 3571 O  O   . HOH N 4 .   ? 3.457   28.668 6.921   1.00 48.70 ? 876  HOH B O   1 
HETATM 3572 O  O   . HOH N 4 .   ? 26.401  36.309 -12.551 1.00 52.24 ? 877  HOH B O   1 
HETATM 3573 O  O   . HOH N 4 .   ? 33.331  13.727 3.720   1.00 50.19 ? 878  HOH B O   1 
HETATM 3574 O  O   . HOH N 4 .   ? 27.772  30.895 -6.284  1.00 36.21 ? 879  HOH B O   1 
HETATM 3575 O  O   . HOH N 4 .   ? 25.313  12.077 2.988   1.00 43.13 ? 880  HOH B O   1 
HETATM 3576 O  O   . HOH N 4 .   ? 13.154  26.815 -9.867  1.00 33.65 ? 881  HOH B O   1 
HETATM 3577 O  O   . HOH N 4 .   ? 29.630  29.605 -5.928  1.00 41.84 ? 882  HOH B O   1 
HETATM 3578 O  O   . HOH N 4 .   ? 30.398  24.873 -14.718 1.00 53.03 ? 883  HOH B O   1 
HETATM 3579 O  O   . HOH N 4 .   ? 5.250   5.629  1.827   1.00 43.72 ? 884  HOH B O   1 
HETATM 3580 O  O   . HOH N 4 .   ? 10.136  5.789  -9.559  1.00 31.38 ? 885  HOH B O   1 
HETATM 3581 O  O   . HOH N 4 .   ? 7.460   26.781 6.576   1.00 40.65 ? 886  HOH B O   1 
HETATM 3582 O  O   . HOH N 4 .   ? 2.572   34.066 10.393  1.00 44.58 ? 887  HOH B O   1 
HETATM 3583 O  O   . HOH N 4 .   ? 32.306  22.490 -13.227 1.00 52.78 ? 888  HOH B O   1 
HETATM 3584 O  O   . HOH N 4 .   ? 18.383  39.381 -2.542  1.00 52.14 ? 889  HOH B O   1 
HETATM 3585 O  O   . HOH N 4 .   ? 12.793  7.450  4.426   1.00 40.52 ? 890  HOH B O   1 
HETATM 3586 O  O   . HOH N 4 .   ? 26.282  32.635 -5.501  1.00 37.46 ? 891  HOH B O   1 
HETATM 3587 O  O   . HOH N 4 .   ? 20.574  36.826 -2.631  1.00 48.52 ? 892  HOH B O   1 
HETATM 3588 O  O   . HOH N 4 .   ? 24.533  19.663 -11.384 1.00 42.95 ? 893  HOH B O   1 
HETATM 3589 O  O   . HOH N 4 .   ? 2.506   29.309 4.737   1.00 59.09 ? 894  HOH B O   1 
HETATM 3590 O  O   . HOH N 4 .   ? 19.074  41.328 -0.282  1.00 41.56 ? 895  HOH B O   1 
HETATM 3591 O  O   . HOH N 4 .   ? 33.128  33.076 -2.106  1.00 44.79 ? 896  HOH B O   1 
HETATM 3592 O  O   . HOH N 4 .   ? 8.868   29.669 -7.150  1.00 68.27 ? 897  HOH B O   1 
HETATM 3593 O  O   . HOH N 4 .   ? 3.118   21.349 1.420   1.00 45.85 ? 898  HOH B O   1 
HETATM 3594 O  O   . HOH N 4 .   ? 14.604  32.575 -7.116  1.00 36.82 ? 899  HOH B O   1 
HETATM 3595 O  O   . HOH N 4 .   ? 27.604  20.489 17.465  1.00 46.29 ? 900  HOH B O   1 
HETATM 3596 O  O   . HOH N 4 .   ? 24.583  16.670 -5.170  1.00 44.99 ? 901  HOH B O   1 
HETATM 3597 O  O   . HOH N 4 .   ? 25.583  36.613 2.184   1.00 56.88 ? 902  HOH B O   1 
HETATM 3598 O  O   . HOH N 4 .   ? 12.203  38.986 -0.582  1.00 47.16 ? 903  HOH B O   1 
HETATM 3599 O  O   . HOH N 4 .   ? 6.692   28.780 10.695  1.00 42.46 ? 904  HOH B O   1 
HETATM 3600 O  O   . HOH N 4 .   ? 4.220   25.948 9.799   1.00 60.26 ? 905  HOH B O   1 
HETATM 3601 O  O   . HOH N 4 .   ? 7.863   8.216  5.007   1.00 48.69 ? 906  HOH B O   1 
HETATM 3602 O  O   . HOH N 4 .   ? 26.562  18.538 -4.021  1.00 44.18 ? 907  HOH B O   1 
HETATM 3603 O  O   . HOH N 4 .   ? 23.046  17.076 12.069  1.00 47.81 ? 908  HOH B O   1 
HETATM 3604 O  O   . HOH N 4 .   ? 10.499  35.991 -1.361  1.00 64.69 ? 909  HOH B O   1 
HETATM 3605 O  O   . HOH N 4 .   ? 4.221   26.193 0.570   1.00 38.30 ? 910  HOH B O   1 
HETATM 3606 O  O   . HOH N 4 .   ? 23.126  22.216 -15.978 1.00 53.35 ? 911  HOH B O   1 
HETATM 3607 O  O   . HOH N 4 .   ? 37.343  30.195 6.218   1.00 45.63 ? 912  HOH B O   1 
HETATM 3608 O  O   . HOH N 4 .   ? 31.587  24.951 2.400   1.00 39.23 ? 913  HOH B O   1 
HETATM 3609 O  O   . HOH N 4 .   ? 5.538   26.895 5.321   1.00 99.56 ? 914  HOH B O   1 
HETATM 3610 O  O   . HOH N 4 .   ? 18.996  9.932  3.055   1.00 40.50 ? 915  HOH B O   1 
HETATM 3611 O  O   . HOH N 4 .   ? 6.652   33.051 -3.992  1.00 64.32 ? 916  HOH B O   1 
HETATM 3612 O  O   . HOH N 4 .   ? 13.012  39.145 -2.722  1.00 50.87 ? 917  HOH B O   1 
HETATM 3613 O  O   . HOH N 4 .   ? 1.765   21.333 -1.696  1.00 50.32 ? 918  HOH B O   1 
HETATM 3614 O  O   . HOH N 4 .   ? 20.722  17.522 -9.275  1.00 48.05 ? 919  HOH B O   1 
HETATM 3615 O  O   . HOH N 4 .   ? 2.829   24.932 7.252   1.00 54.00 ? 920  HOH B O   1 
HETATM 3616 O  O   . HOH N 4 .   ? 32.720  22.782 11.058  1.00 43.31 ? 921  HOH B O   1 
HETATM 3617 O  O   . HOH N 4 .   ? 25.580  21.015 23.155  1.00 61.30 ? 922  HOH B O   1 
HETATM 3618 O  O   . HOH N 4 .   ? 8.224   34.864 -3.184  1.00 61.95 ? 923  HOH B O   1 
HETATM 3619 O  O   . HOH N 4 .   ? 6.019   8.527  7.253   1.00 47.04 ? 924  HOH B O   1 
HETATM 3620 O  O   . HOH N 4 .   ? 2.827   9.228  6.406   1.00 55.38 ? 925  HOH B O   1 
HETATM 3621 O  O   . HOH N 4 .   ? 23.534  14.408 12.873  1.00 52.69 ? 926  HOH B O   1 
HETATM 3622 O  O   . HOH N 4 .   ? 26.954  34.621 7.440   1.00 54.21 ? 927  HOH B O   1 
HETATM 3623 O  O   . HOH N 4 .   ? -0.260  16.104 -7.632  1.00 60.46 ? 928  HOH B O   1 
HETATM 3624 O  O   . HOH N 4 .   ? 28.673  21.542 -4.948  1.00 56.60 ? 929  HOH B O   1 
HETATM 3625 O  O   . HOH N 4 .   ? 6.871   40.041 5.885   1.00 60.43 ? 930  HOH B O   1 
HETATM 3626 O  O   . HOH N 4 .   ? 31.615  30.053 3.673   1.00 41.77 ? 931  HOH B O   1 
HETATM 3627 O  O   . HOH N 4 .   ? 21.653  15.803 19.336  1.00 51.92 ? 932  HOH B O   1 
HETATM 3628 O  O   . HOH N 4 .   ? 22.048  17.427 -5.295  1.00 42.71 ? 933  HOH B O   1 
HETATM 3629 O  O   . HOH N 4 .   ? 2.749   6.702  -0.597  1.00 48.92 ? 934  HOH B O   1 
HETATM 3630 O  O   . HOH N 4 .   ? 19.103  13.562 13.298  1.00 55.69 ? 935  HOH B O   1 
HETATM 3631 O  O   . HOH N 4 .   ? 8.993   39.710 2.984   1.00 59.28 ? 936  HOH B O   1 
HETATM 3632 O  O   . HOH N 4 .   ? 4.504   31.288 0.506   1.00 72.35 ? 937  HOH B O   1 
HETATM 3633 O  O   . HOH N 4 .   ? 34.187  29.938 8.608   1.00 64.36 ? 938  HOH B O   1 
HETATM 3634 O  O   . HOH N 4 .   ? 13.581  5.995  -7.223  1.00 49.97 ? 939  HOH B O   1 
HETATM 3635 O  O   . HOH N 4 .   ? 30.900  16.331 7.108   1.00 51.89 ? 940  HOH B O   1 
HETATM 3636 O  O   . HOH N 4 .   ? 37.713  23.319 3.369   1.00 62.26 ? 941  HOH B O   1 
HETATM 3637 O  O   . HOH N 4 .   ? 30.005  14.443 -3.358  1.00 57.06 ? 942  HOH B O   1 
HETATM 3638 O  O   . HOH N 4 .   ? 21.849  13.630 -5.522  1.00 51.70 ? 943  HOH B O   1 
HETATM 3639 O  O   . HOH N 4 .   ? 16.481  12.922 10.354  1.00 36.87 ? 944  HOH B O   1 
HETATM 3640 O  O   . HOH N 4 .   ? 6.263   17.920 -10.812 1.00 58.14 ? 945  HOH B O   1 
HETATM 3641 O  O   . HOH N 4 .   ? 17.412  25.966 -16.090 1.00 50.10 ? 946  HOH B O   1 
HETATM 3642 O  O   . HOH N 4 .   ? 24.016  11.858 -5.361  1.00 56.20 ? 947  HOH B O   1 
HETATM 3643 O  O   . HOH N 4 .   ? 26.870  38.983 0.252   1.00 56.40 ? 948  HOH B O   1 
HETATM 3644 O  O   . HOH N 4 .   ? 9.196   19.102 -16.017 1.00 67.04 ? 949  HOH B O   1 
HETATM 3645 O  O   . HOH N 4 .   ? 34.940  30.815 10.975  1.00 77.65 ? 950  HOH B O   1 
HETATM 3646 O  O   . HOH O 4 .   ? -31.301 49.340 35.048  1.00 10.66 ? 804  HOH C O   1 
HETATM 3647 O  O   . HOH O 4 .   ? -35.039 64.396 19.603  1.00 12.34 ? 805  HOH C O   1 
HETATM 3648 O  O   . HOH O 4 .   ? -27.745 38.794 19.171  1.00 14.89 ? 806  HOH C O   1 
HETATM 3649 O  O   . HOH O 4 .   ? -38.988 43.449 19.974  1.00 13.94 ? 807  HOH C O   1 
HETATM 3650 O  O   . HOH O 4 .   ? -40.786 50.019 34.272  1.00 11.44 ? 808  HOH C O   1 
HETATM 3651 O  O   . HOH O 4 .   ? -29.104 55.518 15.730  1.00 13.64 ? 809  HOH C O   1 
HETATM 3652 O  O   . HOH O 4 .   ? -45.900 53.739 29.448  1.00 15.14 ? 810  HOH C O   1 
HETATM 3653 O  O   . HOH O 4 .   ? -26.092 42.443 12.645  1.00 19.16 ? 811  HOH C O   1 
HETATM 3654 O  O   . HOH O 4 .   ? -27.947 36.527 20.736  1.00 18.11 ? 812  HOH C O   1 
HETATM 3655 O  O   . HOH O 4 .   ? -35.327 39.278 25.016  1.00 14.91 ? 813  HOH C O   1 
HETATM 3656 O  O   . HOH O 4 .   ? -37.155 41.072 24.435  1.00 18.92 ? 814  HOH C O   1 
HETATM 3657 O  O   . HOH O 4 .   ? -28.328 68.983 30.606  1.00 18.66 ? 815  HOH C O   1 
HETATM 3658 O  O   . HOH O 4 .   ? -46.707 42.326 30.590  1.00 14.25 ? 816  HOH C O   1 
HETATM 3659 O  O   . HOH O 4 .   ? -32.638 65.152 18.587  1.00 13.97 ? 817  HOH C O   1 
HETATM 3660 O  O   . HOH O 4 .   ? -34.590 48.173 34.592  1.00 18.74 ? 818  HOH C O   1 
HETATM 3661 O  O   . HOH O 4 .   ? -34.575 49.882 14.806  1.00 18.53 ? 819  HOH C O   1 
HETATM 3662 O  O   . HOH O 4 .   ? -22.564 54.745 18.757  1.00 17.69 ? 820  HOH C O   1 
HETATM 3663 O  O   . HOH O 4 .   ? -39.007 42.244 26.178  1.00 19.17 ? 821  HOH C O   1 
HETATM 3664 O  O   . HOH O 4 .   ? -20.047 71.647 26.135  1.00 15.13 ? 822  HOH C O   1 
HETATM 3665 O  O   . HOH O 4 .   ? -45.524 52.690 26.911  1.00 17.87 ? 823  HOH C O   1 
HETATM 3666 O  O   . HOH O 4 .   ? -26.560 66.627 33.808  1.00 22.64 ? 824  HOH C O   1 
HETATM 3667 O  O   . HOH O 4 .   ? -28.432 66.890 16.649  1.00 16.46 ? 825  HOH C O   1 
HETATM 3668 O  O   . HOH O 4 .   ? -38.256 48.404 13.948  1.00 21.29 ? 826  HOH C O   1 
HETATM 3669 O  O   . HOH O 4 .   ? -39.815 61.218 22.709  1.00 16.99 ? 827  HOH C O   1 
HETATM 3670 O  O   . HOH O 4 .   ? -29.422 38.973 16.851  1.00 16.56 ? 828  HOH C O   1 
HETATM 3671 O  O   . HOH O 4 .   ? -24.952 66.316 26.191  1.00 18.52 ? 829  HOH C O   1 
HETATM 3672 O  O   . HOH O 4 .   ? -43.321 42.389 25.353  1.00 17.64 ? 830  HOH C O   1 
HETATM 3673 O  O   . HOH O 4 .   ? -22.796 63.139 19.682  1.00 18.32 ? 831  HOH C O   1 
HETATM 3674 O  O   . HOH O 4 .   ? -28.506 68.885 26.706  1.00 18.08 ? 832  HOH C O   1 
HETATM 3675 O  O   . HOH O 4 .   ? -19.853 66.755 30.405  1.00 18.23 ? 833  HOH C O   1 
HETATM 3676 O  O   . HOH O 4 .   ? -40.117 40.372 27.842  1.00 18.25 ? 834  HOH C O   1 
HETATM 3677 O  O   . HOH O 4 .   ? -43.955 42.327 22.390  1.00 19.17 ? 835  HOH C O   1 
HETATM 3678 O  O   . HOH O 4 .   ? -31.856 38.390 25.619  1.00 19.46 ? 836  HOH C O   1 
HETATM 3679 O  O   . HOH O 4 .   ? -21.979 59.434 19.966  1.00 17.89 ? 837  HOH C O   1 
HETATM 3680 O  O   . HOH O 4 .   ? -39.278 53.918 17.346  1.00 21.77 ? 838  HOH C O   1 
HETATM 3681 O  O   . HOH O 4 .   ? -40.589 45.410 21.177  1.00 19.11 ? 839  HOH C O   1 
HETATM 3682 O  O   . HOH O 4 .   ? -31.034 38.552 29.236  1.00 20.04 ? 840  HOH C O   1 
HETATM 3683 O  O   . HOH O 4 .   ? -22.758 51.697 12.591  1.00 22.88 ? 841  HOH C O   1 
HETATM 3684 O  O   . HOH O 4 .   ? -17.414 58.428 20.784  1.00 22.03 ? 842  HOH C O   1 
HETATM 3685 O  O   . HOH O 4 .   ? -22.679 53.835 15.898  1.00 21.84 ? 843  HOH C O   1 
HETATM 3686 O  O   . HOH O 4 .   ? -23.878 41.701 34.062  1.00 21.70 ? 844  HOH C O   1 
HETATM 3687 O  O   . HOH O 4 .   ? -39.816 43.672 32.936  1.00 25.01 ? 845  HOH C O   1 
HETATM 3688 O  O   . HOH O 4 .   ? -45.044 50.710 22.678  1.00 21.98 ? 846  HOH C O   1 
HETATM 3689 O  O   . HOH O 4 .   ? -36.066 39.919 21.041  1.00 23.48 ? 847  HOH C O   1 
HETATM 3690 O  O   . HOH O 4 .   ? -32.209 68.961 17.274  1.00 19.62 ? 848  HOH C O   1 
HETATM 3691 O  O   . HOH O 4 .   ? -23.824 64.184 17.417  1.00 20.47 ? 849  HOH C O   1 
HETATM 3692 O  O   . HOH O 4 .   ? -21.118 52.401 19.395  1.00 24.11 ? 850  HOH C O   1 
HETATM 3693 O  O   . HOH O 4 .   ? -41.768 61.295 27.262  1.00 22.65 ? 851  HOH C O   1 
HETATM 3694 O  O   . HOH O 4 .   ? -48.258 46.614 30.303  1.00 20.86 ? 852  HOH C O   1 
HETATM 3695 O  O   . HOH O 4 .   ? -21.295 44.540 31.548  1.00 24.96 ? 853  HOH C O   1 
HETATM 3696 O  O   . HOH O 4 .   ? -36.301 64.137 29.403  1.00 20.74 ? 854  HOH C O   1 
HETATM 3697 O  O   . HOH O 4 .   ? -25.280 61.104 39.751  1.00 24.14 ? 855  HOH C O   1 
HETATM 3698 O  O   . HOH O 4 .   ? -19.764 63.804 22.035  1.00 23.81 ? 856  HOH C O   1 
HETATM 3699 O  O   . HOH O 4 .   ? -39.090 60.497 13.597  1.00 20.83 ? 857  HOH C O   1 
HETATM 3700 O  O   . HOH O 4 .   ? -21.584 55.907 35.929  1.00 26.04 ? 858  HOH C O   1 
HETATM 3701 O  O   . HOH O 4 .   ? -20.948 36.494 24.876  1.00 21.65 ? 859  HOH C O   1 
HETATM 3702 O  O   . HOH O 4 .   ? -17.073 51.662 21.603  1.00 19.98 ? 860  HOH C O   1 
HETATM 3703 O  O   . HOH O 4 .   ? -44.797 58.405 22.085  1.00 25.80 ? 861  HOH C O   1 
HETATM 3704 O  O   . HOH O 4 .   ? -40.888 50.407 16.665  1.00 21.96 ? 862  HOH C O   1 
HETATM 3705 O  O   . HOH O 4 .   ? -23.716 58.282 12.905  1.00 25.36 ? 863  HOH C O   1 
HETATM 3706 O  O   . HOH O 4 .   ? -38.629 56.218 16.120  1.00 24.51 ? 864  HOH C O   1 
HETATM 3707 O  O   . HOH O 4 .   ? -21.856 54.384 41.329  1.00 26.04 ? 865  HOH C O   1 
HETATM 3708 O  O   . HOH O 4 .   ? -40.355 42.587 23.950  1.00 29.83 ? 866  HOH C O   1 
HETATM 3709 O  O   . HOH O 4 .   ? -22.263 72.915 32.131  1.00 26.15 ? 867  HOH C O   1 
HETATM 3710 O  O   . HOH O 4 .   ? -19.394 68.027 22.559  1.00 20.12 ? 868  HOH C O   1 
HETATM 3711 O  O   . HOH O 4 .   ? -19.416 48.463 20.319  1.00 19.96 ? 869  HOH C O   1 
HETATM 3712 O  O   . HOH O 4 .   ? -28.734 69.895 16.615  1.00 27.52 ? 870  HOH C O   1 
HETATM 3713 O  O   . HOH O 4 .   ? -37.571 66.001 27.495  1.00 22.79 ? 871  HOH C O   1 
HETATM 3714 O  O   . HOH O 4 .   ? -27.841 40.567 13.447  1.00 23.12 ? 872  HOH C O   1 
HETATM 3715 O  O   . HOH O 4 .   ? -25.106 35.364 28.004  1.00 28.21 ? 873  HOH C O   1 
HETATM 3716 O  O   . HOH O 4 .   ? -41.949 60.331 21.066  1.00 28.45 ? 874  HOH C O   1 
HETATM 3717 O  O   . HOH O 4 .   ? -24.415 36.100 30.177  1.00 44.65 ? 875  HOH C O   1 
HETATM 3718 O  O   . HOH O 4 .   ? -19.534 41.210 28.856  1.00 30.08 ? 876  HOH C O   1 
HETATM 3719 O  O   . HOH O 4 .   ? -36.979 46.128 12.579  1.00 29.14 ? 877  HOH C O   1 
HETATM 3720 O  O   . HOH O 4 .   ? -26.141 65.811 9.389   1.00 26.68 ? 878  HOH C O   1 
HETATM 3721 O  O   . HOH O 4 .   ? -26.096 68.819 27.837  1.00 22.71 ? 879  HOH C O   1 
HETATM 3722 O  O   . HOH O 4 .   ? -25.674 50.507 9.430   1.00 33.46 ? 880  HOH C O   1 
HETATM 3723 O  O   . HOH O 4 .   ? -23.776 67.187 34.835  1.00 30.60 ? 881  HOH C O   1 
HETATM 3724 O  O   . HOH O 4 .   ? -13.835 39.358 16.830  1.00 28.48 ? 882  HOH C O   1 
HETATM 3725 O  O   . HOH O 4 .   ? -29.029 70.491 34.528  1.00 31.19 ? 883  HOH C O   1 
HETATM 3726 O  O   . HOH O 4 .   ? -19.586 48.354 34.243  1.00 32.69 ? 884  HOH C O   1 
HETATM 3727 O  O   . HOH O 4 .   ? -24.989 53.719 47.513  1.00 26.17 ? 885  HOH C O   1 
HETATM 3728 O  O   . HOH O 4 .   ? -16.108 34.518 13.827  1.00 29.41 ? 886  HOH C O   1 
HETATM 3729 O  O   . HOH O 4 .   ? -37.008 33.033 28.154  1.00 34.67 ? 887  HOH C O   1 
HETATM 3730 O  O   . HOH O 4 .   ? -25.606 33.834 22.948  1.00 30.48 ? 888  HOH C O   1 
HETATM 3731 O  O   . HOH O 4 .   ? -29.143 68.446 9.323   1.00 28.91 ? 889  HOH C O   1 
HETATM 3732 O  O   . HOH O 4 .   ? -32.268 71.452 28.947  1.00 28.91 ? 890  HOH C O   1 
HETATM 3733 O  O   . HOH O 4 .   ? -15.771 49.394 27.512  1.00 27.87 ? 891  HOH C O   1 
HETATM 3734 O  O   . HOH O 4 .   ? -33.341 68.326 34.636  1.00 31.88 ? 892  HOH C O   1 
HETATM 3735 O  O   . HOH O 4 .   ? -17.992 50.083 17.793  1.00 43.74 ? 893  HOH C O   1 
HETATM 3736 O  O   . HOH O 4 .   ? -31.404 38.004 12.961  1.00 35.24 ? 894  HOH C O   1 
HETATM 3737 O  O   . HOH O 4 .   ? -19.381 34.478 15.579  1.00 31.80 ? 895  HOH C O   1 
HETATM 3738 O  O   . HOH O 4 .   ? -17.805 63.662 32.230  1.00 43.35 ? 896  HOH C O   1 
HETATM 3739 O  O   . HOH O 4 .   ? -40.490 59.055 18.867  1.00 29.01 ? 897  HOH C O   1 
HETATM 3740 O  O   . HOH O 4 .   ? -21.775 49.643 37.105  1.00 26.43 ? 898  HOH C O   1 
HETATM 3741 O  O   . HOH O 4 .   ? -13.339 46.207 28.589  1.00 83.32 ? 899  HOH C O   1 
HETATM 3742 O  O   . HOH O 4 .   ? -26.967 38.028 13.560  1.00 27.67 ? 900  HOH C O   1 
HETATM 3743 O  O   . HOH O 4 .   ? -47.900 50.859 32.242  1.00 30.61 ? 901  HOH C O   1 
HETATM 3744 O  O   . HOH O 4 .   ? -32.807 45.302 33.980  1.00 28.70 ? 902  HOH C O   1 
HETATM 3745 O  O   . HOH O 4 .   ? -17.248 42.113 15.114  1.00 36.64 ? 903  HOH C O   1 
HETATM 3746 O  O   . HOH O 4 .   ? -41.170 63.636 28.968  1.00 35.29 ? 904  HOH C O   1 
HETATM 3747 O  O   . HOH O 4 .   ? -22.404 34.998 19.558  1.00 32.19 ? 905  HOH C O   1 
HETATM 3748 O  O   . HOH O 4 .   ? -16.518 56.559 27.067  1.00 25.69 ? 906  HOH C O   1 
HETATM 3749 O  O   . HOH O 4 .   ? -24.443 63.785 8.107   1.00 35.55 ? 907  HOH C O   1 
HETATM 3750 O  O   . HOH O 4 .   ? -24.195 40.613 12.139  1.00 30.74 ? 908  HOH C O   1 
HETATM 3751 O  O   . HOH O 4 .   ? -23.451 59.387 47.883  1.00 37.89 ? 909  HOH C O   1 
HETATM 3752 O  O   . HOH O 4 .   ? -35.017 44.541 32.423  1.00 36.75 ? 910  HOH C O   1 
HETATM 3753 O  O   . HOH O 4 .   ? -40.599 63.227 24.433  1.00 29.29 ? 911  HOH C O   1 
HETATM 3754 O  O   . HOH O 4 .   ? -32.478 39.330 39.898  1.00 46.81 ? 912  HOH C O   1 
HETATM 3755 O  O   . HOH O 4 .   ? -47.445 50.295 29.135  1.00 32.50 ? 913  HOH C O   1 
HETATM 3756 O  O   . HOH O 4 .   ? -22.059 35.072 16.026  1.00 32.48 ? 914  HOH C O   1 
HETATM 3757 O  O   . HOH O 4 .   ? -17.483 60.987 19.907  1.00 34.21 ? 915  HOH C O   1 
HETATM 3758 O  O   . HOH O 4 .   ? -22.447 71.263 35.499  1.00 36.57 ? 916  HOH C O   1 
HETATM 3759 O  O   . HOH O 4 .   ? -35.636 66.461 33.094  1.00 42.77 ? 917  HOH C O   1 
HETATM 3760 O  O   . HOH O 4 .   ? -37.247 39.514 14.681  1.00 46.05 ? 918  HOH C O   1 
HETATM 3761 O  O   . HOH O 4 .   ? -20.448 64.530 13.600  1.00 37.91 ? 919  HOH C O   1 
HETATM 3762 O  O   . HOH O 4 .   ? -23.338 37.270 13.121  1.00 40.16 ? 920  HOH C O   1 
HETATM 3763 O  O   . HOH O 4 .   ? -24.357 58.447 9.879   1.00 54.38 ? 921  HOH C O   1 
HETATM 3764 O  O   . HOH O 4 .   ? -30.773 68.451 28.247  1.00 14.42 ? 922  HOH C O   1 
HETATM 3765 O  O   . HOH O 4 .   ? -30.561 67.084 18.433  1.00 16.52 ? 923  HOH C O   1 
HETATM 3766 O  O   . HOH O 4 .   ? -21.174 57.132 18.631  1.00 19.97 ? 924  HOH C O   1 
HETATM 3767 O  O   . HOH O 4 .   ? -14.955 64.818 26.984  1.00 50.66 ? 925  HOH C O   1 
HETATM 3768 O  O   . HOH O 4 .   ? -19.676 51.027 20.991  1.00 23.03 ? 926  HOH C O   1 
HETATM 3769 O  O   . HOH O 4 .   ? -32.390 37.516 23.088  1.00 28.45 ? 927  HOH C O   1 
HETATM 3770 O  O   . HOH O 4 .   ? -30.732 36.292 21.228  1.00 21.73 ? 928  HOH C O   1 
HETATM 3771 O  O   . HOH O 4 .   ? -37.598 59.437 11.375  1.00 21.94 ? 929  HOH C O   1 
HETATM 3772 O  O   . HOH O 4 .   ? -34.759 72.181 23.915  1.00 22.74 ? 930  HOH C O   1 
HETATM 3773 O  O   . HOH O 4 .   ? -39.910 65.052 26.322  1.00 29.32 ? 931  HOH C O   1 
HETATM 3774 O  O   . HOH O 4 .   ? -22.347 55.857 13.919  1.00 30.58 ? 932  HOH C O   1 
HETATM 3775 O  O   . HOH O 4 .   ? -31.269 37.315 18.310  1.00 33.48 ? 933  HOH C O   1 
HETATM 3776 O  O   . HOH O 4 .   ? -27.389 34.215 19.371  1.00 31.62 ? 934  HOH C O   1 
HETATM 3777 O  O   . HOH O 4 .   ? -27.221 73.373 32.258  1.00 28.07 ? 935  HOH C O   1 
HETATM 3778 O  O   . HOH O 4 .   ? -32.330 45.038 36.719  1.00 28.18 ? 936  HOH C O   1 
HETATM 3779 O  O   . HOH O 4 .   ? -16.317 44.173 21.723  1.00 32.24 ? 937  HOH C O   1 
HETATM 3780 O  O   . HOH O 4 .   ? -35.533 62.513 33.286  1.00 40.79 ? 938  HOH C O   1 
HETATM 3781 O  O   . HOH O 4 .   ? -21.945 41.716 30.058  1.00 31.26 ? 939  HOH C O   1 
HETATM 3782 O  O   . HOH O 4 .   ? -14.668 58.431 26.561  1.00 43.70 ? 940  HOH C O   1 
HETATM 3783 O  O   . HOH O 4 .   ? -13.459 35.624 13.788  1.00 40.36 ? 941  HOH C O   1 
HETATM 3784 O  O   . HOH O 4 .   ? -18.398 57.006 18.622  1.00 26.86 ? 942  HOH C O   1 
HETATM 3785 O  O   . HOH O 4 .   ? -40.553 60.479 17.035  1.00 29.21 ? 943  HOH C O   1 
HETATM 3786 O  O   . HOH O 4 .   ? -22.215 39.812 32.273  1.00 31.28 ? 944  HOH C O   1 
HETATM 3787 O  O   . HOH O 4 .   ? -16.494 66.606 23.018  1.00 36.05 ? 945  HOH C O   1 
HETATM 3788 O  O   . HOH O 4 .   ? -16.113 53.461 19.814  1.00 33.51 ? 946  HOH C O   1 
HETATM 3789 O  O   . HOH O 4 .   ? -18.509 43.546 12.886  1.00 31.61 ? 947  HOH C O   1 
HETATM 3790 O  O   . HOH O 4 .   ? -16.689 64.791 29.222  1.00 48.96 ? 948  HOH C O   1 
HETATM 3791 O  O   . HOH O 4 .   ? -17.751 67.667 20.409  1.00 36.44 ? 949  HOH C O   1 
HETATM 3792 O  O   . HOH O 4 .   ? -33.501 73.310 30.750  1.00 55.94 ? 950  HOH C O   1 
HETATM 3793 O  O   . HOH O 4 .   ? -41.749 53.833 16.246  1.00 36.28 ? 951  HOH C O   1 
HETATM 3794 O  O   . HOH O 4 .   ? -20.521 50.937 13.712  1.00 29.88 ? 952  HOH C O   1 
HETATM 3795 O  O   . HOH O 4 .   ? -14.546 39.236 24.043  1.00 43.14 ? 953  HOH C O   1 
HETATM 3796 O  O   . HOH O 4 .   ? -23.704 32.963 16.323  1.00 41.68 ? 954  HOH C O   1 
HETATM 3797 O  O   . HOH O 4 .   ? -41.704 63.901 19.292  1.00 41.88 ? 955  HOH C O   1 
HETATM 3798 O  O   . HOH O 4 .   ? -25.637 63.324 6.079   1.00 38.01 ? 956  HOH C O   1 
HETATM 3799 O  O   . HOH O 4 .   ? -30.846 47.986 8.562   1.00 36.44 ? 957  HOH C O   1 
HETATM 3800 O  O   . HOH O 4 .   ? -37.018 64.168 32.052  1.00 33.34 ? 958  HOH C O   1 
HETATM 3801 O  O   . HOH O 4 .   ? -38.048 67.308 29.714  1.00 43.48 ? 959  HOH C O   1 
HETATM 3802 O  O   . HOH O 4 .   ? -18.297 32.269 14.707  1.00 36.33 ? 960  HOH C O   1 
HETATM 3803 O  O   . HOH O 4 .   ? -21.595 54.083 12.066  1.00 38.94 ? 961  HOH C O   1 
HETATM 3804 O  O   . HOH O 4 .   ? -34.539 41.689 39.340  1.00 47.24 ? 962  HOH C O   1 
HETATM 3805 O  O   . HOH O 4 .   ? -17.429 67.860 29.833  1.00 30.33 ? 963  HOH C O   1 
HETATM 3806 O  O   . HOH O 4 .   ? -23.453 59.412 7.233   1.00 49.93 ? 964  HOH C O   1 
HETATM 3807 O  O   . HOH O 4 .   ? -22.634 43.485 11.268  1.00 34.69 ? 965  HOH C O   1 
HETATM 3808 O  O   . HOH O 4 .   ? -27.704 67.651 37.467  1.00 49.65 ? 966  HOH C O   1 
HETATM 3809 O  O   . HOH O 4 .   ? -14.003 51.120 28.337  1.00 48.59 ? 967  HOH C O   1 
HETATM 3810 O  O   . HOH O 4 .   ? -29.757 72.214 32.206  1.00 40.78 ? 968  HOH C O   1 
HETATM 3811 O  O   . HOH O 4 .   ? -16.486 45.221 19.611  1.00 48.45 ? 969  HOH C O   1 
HETATM 3812 O  O   . HOH O 4 .   ? -28.320 65.007 9.393   1.00 33.34 ? 970  HOH C O   1 
HETATM 3813 O  O   . HOH O 4 .   ? -38.577 69.524 14.118  1.00 42.47 ? 971  HOH C O   1 
HETATM 3814 O  O   . HOH O 4 .   ? -29.725 71.159 29.958  1.00 36.06 ? 972  HOH C O   1 
HETATM 3815 O  O   . HOH O 4 .   ? -14.303 59.997 34.184  1.00 55.17 ? 973  HOH C O   1 
HETATM 3816 O  O   . HOH O 4 .   ? -18.937 52.651 17.948  1.00 47.20 ? 974  HOH C O   1 
HETATM 3817 O  O   . HOH O 4 .   ? -24.515 55.555 49.512  1.00 36.00 ? 975  HOH C O   1 
HETATM 3818 O  O   . HOH O 4 .   ? -19.946 34.357 18.187  1.00 42.44 ? 976  HOH C O   1 
HETATM 3819 O  O   . HOH O 4 .   ? -31.946 37.613 35.908  1.00 47.98 ? 977  HOH C O   1 
HETATM 3820 O  O   . HOH O 4 .   ? -18.577 56.955 36.853  1.00 49.64 ? 978  HOH C O   1 
HETATM 3821 O  O   . HOH O 4 .   ? -40.030 69.280 19.737  1.00 39.30 ? 979  HOH C O   1 
HETATM 3822 O  O   . HOH O 4 .   ? -22.183 39.957 11.299  1.00 41.45 ? 980  HOH C O   1 
HETATM 3823 O  O   . HOH O 4 .   ? -30.254 65.690 37.419  1.00 55.58 ? 981  HOH C O   1 
HETATM 3824 O  O   . HOH O 4 .   ? -48.787 48.086 28.087  1.00 43.38 ? 982  HOH C O   1 
HETATM 3825 O  O   . HOH O 4 .   ? -34.459 59.284 8.688   1.00 26.52 ? 983  HOH C O   1 
HETATM 3826 O  O   . HOH O 4 .   ? -20.240 49.831 16.532  1.00 31.44 ? 984  HOH C O   1 
HETATM 3827 O  O   . HOH O 4 .   ? -20.306 56.896 15.688  1.00 28.96 ? 985  HOH C O   1 
HETATM 3828 O  O   . HOH O 4 .   ? -29.735 37.107 14.751  1.00 28.43 ? 986  HOH C O   1 
HETATM 3829 O  O   . HOH O 4 .   ? -33.170 42.213 41.108  1.00 51.15 ? 987  HOH C O   1 
HETATM 3830 O  O   . HOH O 4 .   ? -38.540 49.234 11.668  1.00 49.33 ? 988  HOH C O   1 
HETATM 3831 O  O   . HOH O 4 .   ? -13.855 42.027 25.627  1.00 42.88 ? 989  HOH C O   1 
HETATM 3832 O  O   . HOH O 4 .   ? -39.246 65.888 12.126  1.00 50.51 ? 990  HOH C O   1 
HETATM 3833 O  O   . HOH O 4 .   ? -26.211 52.425 7.312   1.00 37.29 ? 991  HOH C O   1 
HETATM 3834 O  O   . HOH O 4 .   ? -18.068 47.215 13.474  1.00 39.71 ? 992  HOH C O   1 
HETATM 3835 O  O   . HOH O 4 .   ? -22.585 34.143 25.134  1.00 52.94 ? 993  HOH C O   1 
HETATM 3836 O  O   . HOH O 4 .   ? -23.803 55.896 3.234   1.00 53.64 ? 994  HOH C O   1 
HETATM 3837 O  O   . HOH O 4 .   ? -42.295 64.666 23.043  1.00 37.22 ? 995  HOH C O   1 
HETATM 3838 O  O   . HOH O 4 .   ? -15.440 49.794 21.322  1.00 47.40 ? 996  HOH C O   1 
HETATM 3839 O  O   . HOH O 4 .   ? -43.168 62.495 20.609  1.00 46.43 ? 997  HOH C O   1 
HETATM 3840 O  O   . HOH O 4 .   ? -31.415 69.763 8.602   1.00 56.30 ? 998  HOH C O   1 
HETATM 3841 O  O   . HOH O 4 .   ? -16.752 51.430 35.230  1.00 48.63 ? 999  HOH C O   1 
HETATM 3842 O  O   . HOH O 4 .   ? -19.975 46.756 32.259  1.00 37.91 ? 1000 HOH C O   1 
HETATM 3843 O  O   . HOH O 4 .   ? -21.499 55.939 4.666   1.00 59.67 ? 1001 HOH C O   1 
HETATM 3844 O  O   . HOH O 4 .   ? -23.030 51.389 9.997   1.00 39.48 ? 1002 HOH C O   1 
HETATM 3845 O  O   . HOH O 4 .   ? -23.394 52.552 8.048   1.00 52.54 ? 1003 HOH C O   1 
HETATM 3846 O  O   . HOH O 4 .   ? -34.521 70.616 34.258  1.00 43.09 ? 1004 HOH C O   1 
HETATM 3847 O  O   . HOH O 4 .   ? -13.838 49.660 25.417  1.00 36.53 ? 1005 HOH C O   1 
HETATM 3848 O  O   . HOH O 4 .   ? -40.303 62.951 13.775  1.00 49.27 ? 1006 HOH C O   1 
HETATM 3849 O  O   . HOH O 4 .   ? -20.504 68.331 38.492  1.00 69.92 ? 1007 HOH C O   1 
HETATM 3850 O  O   . HOH O 4 .   ? -24.665 57.525 4.604   1.00 73.63 ? 1008 HOH C O   1 
HETATM 3851 O  O   . HOH O 4 .   ? -17.371 46.682 31.208  1.00 40.13 ? 1009 HOH C O   1 
HETATM 3852 O  O   . HOH O 4 .   ? -26.791 58.386 8.748   1.00 42.77 ? 1010 HOH C O   1 
HETATM 3853 O  O   . HOH O 4 .   ? -45.212 65.007 21.298  1.00 61.46 ? 1011 HOH C O   1 
HETATM 3854 O  O   . HOH O 4 .   ? -34.896 39.537 11.398  1.00 43.00 ? 1012 HOH C O   1 
HETATM 3855 O  O   . HOH O 4 .   ? -19.473 41.577 11.054  1.00 39.86 ? 1013 HOH C O   1 
HETATM 3856 O  O   . HOH O 4 .   ? -36.509 67.300 11.127  1.00 42.28 ? 1014 HOH C O   1 
HETATM 3857 O  O   . HOH O 4 .   ? -44.982 61.732 24.641  1.00 55.13 ? 1015 HOH C O   1 
HETATM 3858 O  O   . HOH O 4 .   ? -34.619 37.126 9.586   1.00 58.10 ? 1016 HOH C O   1 
HETATM 3859 O  O   . HOH O 4 .   ? -45.252 64.268 30.817  1.00 53.77 ? 1017 HOH C O   1 
HETATM 3860 O  O   . HOH O 4 .   ? -48.787 53.591 32.801  1.00 36.58 ? 1018 HOH C O   1 
HETATM 3861 O  O   . HOH O 4 .   ? -14.492 46.166 33.066  1.00 53.88 ? 1019 HOH C O   1 
HETATM 3862 O  O   . HOH O 4 .   ? -29.390 34.443 14.745  1.00 40.66 ? 1020 HOH C O   1 
HETATM 3863 O  O   . HOH O 4 .   ? -15.160 44.441 17.908  1.00 46.06 ? 1021 HOH C O   1 
HETATM 3864 O  O   . HOH O 4 .   ? -19.055 50.860 37.212  1.00 52.50 ? 1022 HOH C O   1 
HETATM 3865 O  O   . HOH O 4 .   ? -15.144 56.963 32.214  1.00 44.23 ? 1023 HOH C O   1 
HETATM 3866 O  O   . HOH O 4 .   ? -22.391 53.815 36.361  1.00 23.61 ? 1024 HOH C O   1 
HETATM 3867 O  O   . HOH O 4 .   ? -36.426 46.338 33.082  1.00 29.71 ? 1025 HOH C O   1 
HETATM 3868 O  O   . HOH O 4 .   ? -25.467 36.569 12.624  1.00 48.01 ? 1026 HOH C O   1 
HETATM 3869 O  O   . HOH O 4 .   ? -15.215 40.289 14.740  1.00 41.30 ? 1027 HOH C O   1 
HETATM 3870 O  O   . HOH O 4 .   ? -20.555 52.523 15.374  1.00 47.69 ? 1028 HOH C O   1 
HETATM 3871 O  O   . HOH O 4 .   ? -16.263 62.325 33.272  1.00 49.08 ? 1029 HOH C O   1 
HETATM 3872 O  O   . HOH O 4 .   ? -42.921 57.284 16.633  1.00 50.84 ? 1030 HOH C O   1 
HETATM 3873 O  O   . HOH O 4 .   ? -16.660 63.058 20.975  1.00 52.86 ? 1031 HOH C O   1 
HETATM 3874 O  O   . HOH O 4 .   ? -21.659 42.943 33.160  1.00 35.38 ? 1032 HOH C O   1 
HETATM 3875 O  O   . HOH O 4 .   ? -17.188 49.249 34.041  1.00 56.27 ? 1033 HOH C O   1 
HETATM 3876 O  O   . HOH O 4 .   ? -15.830 46.806 28.528  1.00 38.16 ? 1034 HOH C O   1 
HETATM 3877 O  O   . HOH O 4 .   ? -34.379 37.733 17.786  1.00 69.77 ? 1035 HOH C O   1 
HETATM 3878 O  O   . HOH O 4 .   ? -17.115 63.979 23.030  1.00 23.16 ? 1036 HOH C O   1 
HETATM 3879 O  O   . HOH O 4 .   ? -40.318 58.461 14.977  1.00 46.96 ? 1037 HOH C O   1 
HETATM 3880 O  O   . HOH O 4 .   ? -24.292 33.437 18.493  1.00 38.52 ? 1038 HOH C O   1 
HETATM 3881 O  O   . HOH O 4 .   ? -31.601 34.155 20.691  1.00 66.58 ? 1039 HOH C O   1 
HETATM 3882 O  O   . HOH O 4 .   ? -16.580 47.373 36.132  1.00 55.95 ? 1040 HOH C O   1 
HETATM 3883 O  O   . HOH O 4 .   ? -40.370 67.953 24.160  1.00 59.15 ? 1041 HOH C O   1 
HETATM 3884 O  O   . HOH O 4 .   ? -39.043 59.032 9.272   1.00 50.78 ? 1042 HOH C O   1 
HETATM 3885 O  O   . HOH O 4 .   ? -17.148 54.810 18.265  1.00 38.05 ? 1043 HOH C O   1 
HETATM 3886 O  O   . HOH O 4 .   ? -22.199 55.173 9.009   1.00 53.62 ? 1044 HOH C O   1 
HETATM 3887 O  O   . HOH O 4 .   ? -43.087 62.592 30.499  1.00 51.71 ? 1045 HOH C O   1 
HETATM 3888 O  O   . HOH O 4 .   ? -34.111 42.222 36.857  1.00 41.31 ? 1046 HOH C O   1 
HETATM 3889 O  O   . HOH O 4 .   ? -32.215 48.285 6.750   1.00 55.95 ? 1047 HOH C O   1 
HETATM 3890 O  O   . HOH O 4 .   ? -18.615 54.224 12.459  1.00 52.80 ? 1048 HOH C O   1 
HETATM 3891 O  O   . HOH O 4 .   ? -32.583 47.096 35.381  1.00 37.72 ? 1049 HOH C O   1 
HETATM 3892 O  O   . HOH O 4 .   ? -15.481 48.973 18.385  1.00 55.50 ? 1050 HOH C O   1 
HETATM 3893 O  O   . HOH O 4 .   ? -18.471 63.611 30.055  1.00 23.69 ? 1051 HOH C O   1 
HETATM 3894 O  O   . HOH O 4 .   ? -18.112 67.408 17.997  1.00 40.03 ? 1052 HOH C O   1 
HETATM 3895 O  O   . HOH O 4 .   ? -36.571 37.988 16.973  1.00 49.42 ? 1053 HOH C O   1 
HETATM 3896 O  O   . HOH O 4 .   ? -24.213 34.754 13.928  1.00 50.70 ? 1054 HOH C O   1 
HETATM 3897 O  O   . HOH O 4 .   ? -34.956 56.440 9.031   1.00 48.80 ? 1055 HOH C O   1 
HETATM 3898 O  O   . HOH O 4 .   ? -13.655 53.270 22.202  1.00 43.67 ? 1056 HOH C O   1 
HETATM 3899 O  O   . HOH O 4 .   ? -41.071 60.656 9.279   1.00 51.89 ? 1057 HOH C O   1 
HETATM 3900 O  O   . HOH O 4 .   ? -26.397 60.434 42.504  1.00 45.07 ? 1058 HOH C O   1 
HETATM 3901 O  O   . HOH O 4 .   ? -14.116 38.065 14.170  1.00 54.36 ? 1059 HOH C O   1 
HETATM 3902 O  O   . HOH O 4 .   ? -13.453 32.118 20.252  1.00 52.74 ? 1060 HOH C O   1 
HETATM 3903 O  O   . HOH O 4 .   ? -31.590 64.421 36.050  1.00 36.57 ? 1061 HOH C O   1 
HETATM 3904 O  O   . HOH O 4 .   ? -22.084 34.004 22.221  1.00 50.99 ? 1062 HOH C O   1 
HETATM 3905 O  O   . HOH O 4 .   ? -36.818 43.124 11.375  1.00 43.35 ? 1063 HOH C O   1 
HETATM 3906 O  O   . HOH O 4 .   ? -27.333 71.642 36.043  1.00 41.08 ? 1064 HOH C O   1 
HETATM 3907 O  O   . HOH O 4 .   ? -41.900 63.685 15.821  1.00 53.78 ? 1065 HOH C O   1 
HETATM 3908 O  O   . HOH O 4 .   ? -20.427 53.938 44.125  1.00 42.67 ? 1066 HOH C O   1 
HETATM 3909 O  O   . HOH O 4 .   ? -45.239 58.568 19.299  1.00 44.71 ? 1067 HOH C O   1 
HETATM 3910 O  O   . HOH O 4 .   ? -34.471 38.186 32.726  1.00 48.60 ? 1068 HOH C O   1 
HETATM 3911 O  O   . HOH O 4 .   ? -22.209 49.137 8.319   1.00 51.03 ? 1069 HOH C O   1 
HETATM 3912 O  O   . HOH O 4 .   ? -18.693 49.051 39.117  1.00 46.14 ? 1070 HOH C O   1 
HETATM 3913 O  O   . HOH O 4 .   ? -32.796 39.153 9.580   1.00 46.33 ? 1071 HOH C O   1 
HETATM 3914 O  O   . HOH O 4 .   ? -23.220 68.071 36.933  1.00 59.74 ? 1072 HOH C O   1 
HETATM 3915 O  O   . HOH O 4 .   ? -31.028 64.427 39.219  1.00 42.87 ? 1073 HOH C O   1 
HETATM 3916 O  O   . HOH O 4 .   ? -18.776 49.760 12.055  1.00 45.19 ? 1074 HOH C O   1 
HETATM 3917 O  O   . HOH O 4 .   ? -13.873 64.422 30.513  1.00 51.26 ? 1075 HOH C O   1 
HETATM 3918 O  O   . HOH O 4 .   ? -49.438 48.733 31.678  1.00 58.96 ? 1076 HOH C O   1 
HETATM 3919 O  O   . HOH O 4 .   ? -22.833 62.697 9.325   1.00 53.42 ? 1077 HOH C O   1 
HETATM 3920 O  O   . HOH O 4 .   ? -14.686 55.582 30.318  1.00 48.75 ? 1078 HOH C O   1 
HETATM 3921 O  O   . HOH O 4 .   ? -23.606 60.795 44.236  1.00 50.03 ? 1079 HOH C O   1 
HETATM 3922 O  O   . HOH O 4 .   ? -26.540 55.051 1.994   1.00 53.56 ? 1080 HOH C O   1 
HETATM 3923 O  O   . HOH O 4 .   ? -12.859 58.357 29.139  1.00 59.82 ? 1081 HOH C O   1 
HETATM 3924 O  O   . HOH O 4 .   ? -51.666 54.170 33.418  1.00 72.14 ? 1082 HOH C O   1 
HETATM 3925 O  O   . HOH O 4 .   ? -16.116 60.143 38.840  1.00 58.53 ? 1083 HOH C O   1 
HETATM 3926 O  O   . HOH O 4 .   ? -29.770 34.987 17.589  1.00 66.25 ? 1084 HOH C O   1 
HETATM 3927 O  O   . HOH O 4 .   ? -33.929 33.668 22.821  1.00 51.46 ? 1085 HOH C O   1 
HETATM 3928 O  O   . HOH O 4 .   ? -35.225 63.149 35.770  0.50 51.57 ? 1086 HOH C O   1 
HETATM 3929 O  O   . HOH O 4 .   ? -38.762 70.560 24.537  1.00 73.43 ? 1087 HOH C O   1 
HETATM 3930 O  O   . HOH O 4 .   ? -33.578 65.618 35.201  1.00 44.69 ? 1088 HOH C O   1 
HETATM 3931 O  O   . HOH O 4 .   ? -18.492 33.445 24.759  1.00 95.09 ? 1089 HOH C O   1 
HETATM 3932 O  O   . HOH O 4 .   ? -22.287 55.597 50.071  1.00 56.92 ? 1090 HOH C O   1 
HETATM 3933 O  O   . HOH O 4 .   ? -30.290 31.575 13.398  1.00 55.74 ? 1091 HOH C O   1 
HETATM 3934 O  O   . HOH O 4 .   ? -18.335 55.851 44.889  1.00 64.48 ? 1092 HOH C O   1 
HETATM 3935 O  O   . HOH O 4 .   ? -37.628 72.735 26.678  1.00 49.17 ? 1093 HOH C O   1 
HETATM 3936 O  O   . HOH O 4 .   ? -16.999 64.804 17.251  1.00 63.03 ? 1094 HOH C O   1 
HETATM 3937 O  O   . HOH O 4 .   ? -18.151 57.675 15.663  1.00 67.64 ? 1095 HOH C 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  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CSX 111 111 111 CSX CSX 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 HIS 125 125 125 HIS HIS 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 ?   ?   ?   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 ?   ?   ?   A . n 
A 1 134 SER 134 134 ?   ?   ?   A . n 
A 1 135 THR 135 135 ?   ?   ?   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  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CSX 111 111 111 CSX CSX 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 HIS 125 125 125 HIS HIS B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 ?   ?   ?   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 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CSX 111 111 111 CSX CSX C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 HIS 125 125 125 HIS HIS C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 ?   ?   ?   C . n 
C 1 130 GLY 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 ?   ?   ?   C . n 
C 1 132 GLU 132 132 ?   ?   ?   C . n 
C 1 133 GLU 133 133 ?   ?   ?   C . n 
C 1 134 SER 134 134 ?   ?   ?   C . n 
C 1 135 THR 135 135 ?   ?   ?   C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . 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 
D 2 SO4 1   801  1   SO4 SO4 A . 
E 3 ZN  1   201  1   ZN  ZN2 A . 
F 3 ZN  1   202  2   ZN  ZN2 A . 
G 2 SO4 1   802  2   SO4 SO4 B . 
H 3 ZN  1   203  3   ZN  ZN2 B . 
I 3 ZN  1   204  4   ZN  ZN2 B . 
J 2 SO4 1   803  3   SO4 SO4 C . 
K 3 ZN  1   205  5   ZN  ZN2 C . 
L 3 ZN  1   206  6   ZN  ZN2 C . 
M 4 HOH 1   802  2   HOH HOH A . 
M 4 HOH 2   803  7   HOH HOH A . 
M 4 HOH 3   804  9   HOH HOH A . 
M 4 HOH 4   805  11  HOH HOH A . 
M 4 HOH 5   806  13  HOH HOH A . 
M 4 HOH 6   807  17  HOH HOH A . 
M 4 HOH 7   808  18  HOH HOH A . 
M 4 HOH 8   809  21  HOH HOH A . 
M 4 HOH 9   810  24  HOH HOH A . 
M 4 HOH 10  811  27  HOH HOH A . 
M 4 HOH 11  812  28  HOH HOH A . 
M 4 HOH 12  813  34  HOH HOH A . 
M 4 HOH 13  814  35  HOH HOH A . 
M 4 HOH 14  815  38  HOH HOH A . 
M 4 HOH 15  816  39  HOH HOH A . 
M 4 HOH 16  817  40  HOH HOH A . 
M 4 HOH 17  818  41  HOH HOH A . 
M 4 HOH 18  819  43  HOH HOH A . 
M 4 HOH 19  820  49  HOH HOH A . 
M 4 HOH 20  821  50  HOH HOH A . 
M 4 HOH 21  822  52  HOH HOH A . 
M 4 HOH 22  823  53  HOH HOH A . 
M 4 HOH 23  824  54  HOH HOH A . 
M 4 HOH 24  825  57  HOH HOH A . 
M 4 HOH 25  826  60  HOH HOH A . 
M 4 HOH 26  827  61  HOH HOH A . 
M 4 HOH 27  828  63  HOH HOH A . 
M 4 HOH 28  829  64  HOH HOH A . 
M 4 HOH 29  830  66  HOH HOH A . 
M 4 HOH 30  831  67  HOH HOH A . 
M 4 HOH 31  832  68  HOH HOH A . 
M 4 HOH 32  833  69  HOH HOH A . 
M 4 HOH 33  834  70  HOH HOH A . 
M 4 HOH 34  835  73  HOH HOH A . 
M 4 HOH 35  836  74  HOH HOH A . 
M 4 HOH 36  837  75  HOH HOH A . 
M 4 HOH 37  838  76  HOH HOH A . 
M 4 HOH 38  839  78  HOH HOH A . 
M 4 HOH 39  840  80  HOH HOH A . 
M 4 HOH 40  841  82  HOH HOH A . 
M 4 HOH 41  842  86  HOH HOH A . 
M 4 HOH 42  843  87  HOH HOH A . 
M 4 HOH 43  844  90  HOH HOH A . 
M 4 HOH 44  845  95  HOH HOH A . 
M 4 HOH 45  846  97  HOH HOH A . 
M 4 HOH 46  847  99  HOH HOH A . 
M 4 HOH 47  848  101 HOH HOH A . 
M 4 HOH 48  849  107 HOH HOH A . 
M 4 HOH 49  850  109 HOH HOH A . 
M 4 HOH 50  851  110 HOH HOH A . 
M 4 HOH 51  852  114 HOH HOH A . 
M 4 HOH 52  853  118 HOH HOH A . 
M 4 HOH 53  854  120 HOH HOH A . 
M 4 HOH 54  855  121 HOH HOH A . 
M 4 HOH 55  856  122 HOH HOH A . 
M 4 HOH 56  857  128 HOH HOH A . 
M 4 HOH 57  858  129 HOH HOH A . 
M 4 HOH 58  859  130 HOH HOH A . 
M 4 HOH 59  860  131 HOH HOH A . 
M 4 HOH 60  861  134 HOH HOH A . 
M 4 HOH 61  862  137 HOH HOH A . 
M 4 HOH 62  863  138 HOH HOH A . 
M 4 HOH 63  864  141 HOH HOH A . 
M 4 HOH 64  865  142 HOH HOH A . 
M 4 HOH 65  866  144 HOH HOH A . 
M 4 HOH 66  867  145 HOH HOH A . 
M 4 HOH 67  868  147 HOH HOH A . 
M 4 HOH 68  869  148 HOH HOH A . 
M 4 HOH 69  870  159 HOH HOH A . 
M 4 HOH 70  871  160 HOH HOH A . 
M 4 HOH 71  872  162 HOH HOH A . 
M 4 HOH 72  873  163 HOH HOH A . 
M 4 HOH 73  874  168 HOH HOH A . 
M 4 HOH 74  875  169 HOH HOH A . 
M 4 HOH 75  876  171 HOH HOH A . 
M 4 HOH 76  877  172 HOH HOH A . 
M 4 HOH 77  878  173 HOH HOH A . 
M 4 HOH 78  879  175 HOH HOH A . 
M 4 HOH 79  880  177 HOH HOH A . 
M 4 HOH 80  881  178 HOH HOH A . 
M 4 HOH 81  882  182 HOH HOH A . 
M 4 HOH 82  883  183 HOH HOH A . 
M 4 HOH 83  884  185 HOH HOH A . 
M 4 HOH 84  885  186 HOH HOH A . 
M 4 HOH 85  886  187 HOH HOH A . 
M 4 HOH 86  887  190 HOH HOH A . 
M 4 HOH 87  888  197 HOH HOH A . 
M 4 HOH 88  889  198 HOH HOH A . 
M 4 HOH 89  890  199 HOH HOH A . 
M 4 HOH 90  891  203 HOH HOH A . 
M 4 HOH 91  892  204 HOH HOH A . 
M 4 HOH 92  893  206 HOH HOH A . 
M 4 HOH 93  894  208 HOH HOH A . 
M 4 HOH 94  895  209 HOH HOH A . 
M 4 HOH 95  896  210 HOH HOH A . 
M 4 HOH 96  897  216 HOH HOH A . 
M 4 HOH 97  898  218 HOH HOH A . 
M 4 HOH 98  899  224 HOH HOH A . 
M 4 HOH 99  900  225 HOH HOH A . 
M 4 HOH 100 901  230 HOH HOH A . 
M 4 HOH 101 902  234 HOH HOH A . 
M 4 HOH 102 903  235 HOH HOH A . 
M 4 HOH 103 904  236 HOH HOH A . 
M 4 HOH 104 905  237 HOH HOH A . 
M 4 HOH 105 906  239 HOH HOH A . 
M 4 HOH 106 907  243 HOH HOH A . 
M 4 HOH 107 908  248 HOH HOH A . 
M 4 HOH 108 909  249 HOH HOH A . 
M 4 HOH 109 910  250 HOH HOH A . 
M 4 HOH 110 911  251 HOH HOH A . 
M 4 HOH 111 912  252 HOH HOH A . 
M 4 HOH 112 913  253 HOH HOH A . 
M 4 HOH 113 914  255 HOH HOH A . 
M 4 HOH 114 915  257 HOH HOH A . 
M 4 HOH 115 916  261 HOH HOH A . 
M 4 HOH 116 917  262 HOH HOH A . 
M 4 HOH 117 918  266 HOH HOH A . 
M 4 HOH 118 919  268 HOH HOH A . 
M 4 HOH 119 920  270 HOH HOH A . 
M 4 HOH 120 921  272 HOH HOH A . 
M 4 HOH 121 922  273 HOH HOH A . 
M 4 HOH 122 923  275 HOH HOH A . 
M 4 HOH 123 924  276 HOH HOH A . 
M 4 HOH 124 925  277 HOH HOH A . 
M 4 HOH 125 926  280 HOH HOH A . 
M 4 HOH 126 927  284 HOH HOH A . 
M 4 HOH 127 928  285 HOH HOH A . 
M 4 HOH 128 929  287 HOH HOH A . 
M 4 HOH 129 930  292 HOH HOH A . 
M 4 HOH 130 931  294 HOH HOH A . 
M 4 HOH 131 932  295 HOH HOH A . 
M 4 HOH 132 933  296 HOH HOH A . 
M 4 HOH 133 934  297 HOH HOH A . 
M 4 HOH 134 935  298 HOH HOH A . 
M 4 HOH 135 936  299 HOH HOH A . 
M 4 HOH 136 937  301 HOH HOH A . 
M 4 HOH 137 938  304 HOH HOH A . 
M 4 HOH 138 939  306 HOH HOH A . 
M 4 HOH 139 940  307 HOH HOH A . 
M 4 HOH 140 941  310 HOH HOH A . 
M 4 HOH 141 942  314 HOH HOH A . 
M 4 HOH 142 943  315 HOH HOH A . 
M 4 HOH 143 944  316 HOH HOH A . 
M 4 HOH 144 945  327 HOH HOH A . 
M 4 HOH 145 946  331 HOH HOH A . 
M 4 HOH 146 947  332 HOH HOH A . 
M 4 HOH 147 948  333 HOH HOH A . 
M 4 HOH 148 949  334 HOH HOH A . 
M 4 HOH 149 950  338 HOH HOH A . 
M 4 HOH 150 951  339 HOH HOH A . 
M 4 HOH 151 952  341 HOH HOH A . 
M 4 HOH 152 953  342 HOH HOH A . 
M 4 HOH 153 954  343 HOH HOH A . 
M 4 HOH 154 955  346 HOH HOH A . 
M 4 HOH 155 956  352 HOH HOH A . 
M 4 HOH 156 957  354 HOH HOH A . 
M 4 HOH 157 958  357 HOH HOH A . 
M 4 HOH 158 959  358 HOH HOH A . 
M 4 HOH 159 960  360 HOH HOH A . 
M 4 HOH 160 961  362 HOH HOH A . 
M 4 HOH 161 962  364 HOH HOH A . 
M 4 HOH 162 963  366 HOH HOH A . 
M 4 HOH 163 964  367 HOH HOH A . 
M 4 HOH 164 965  370 HOH HOH A . 
M 4 HOH 165 966  375 HOH HOH A . 
M 4 HOH 166 967  378 HOH HOH A . 
M 4 HOH 167 968  385 HOH HOH A . 
M 4 HOH 168 969  387 HOH HOH A . 
M 4 HOH 169 970  388 HOH HOH A . 
M 4 HOH 170 971  389 HOH HOH A . 
M 4 HOH 171 972  395 HOH HOH A . 
M 4 HOH 172 973  401 HOH HOH A . 
M 4 HOH 173 974  402 HOH HOH A . 
M 4 HOH 174 975  403 HOH HOH A . 
M 4 HOH 175 976  408 HOH HOH A . 
M 4 HOH 176 977  410 HOH HOH A . 
M 4 HOH 177 978  413 HOH HOH A . 
M 4 HOH 178 979  415 HOH HOH A . 
M 4 HOH 179 980  416 HOH HOH A . 
M 4 HOH 180 981  418 HOH HOH A . 
M 4 HOH 181 982  422 HOH HOH A . 
M 4 HOH 182 983  423 HOH HOH A . 
M 4 HOH 183 984  425 HOH HOH A . 
M 4 HOH 184 985  435 HOH HOH A . 
M 4 HOH 185 986  437 HOH HOH A . 
M 4 HOH 186 987  438 HOH HOH A . 
M 4 HOH 187 988  442 HOH HOH A . 
M 4 HOH 188 989  443 HOH HOH A . 
M 4 HOH 189 990  446 HOH HOH A . 
M 4 HOH 190 991  447 HOH HOH A . 
M 4 HOH 191 992  448 HOH HOH A . 
M 4 HOH 192 993  452 HOH HOH A . 
M 4 HOH 193 994  453 HOH HOH A . 
M 4 HOH 194 995  454 HOH HOH A . 
M 4 HOH 195 996  455 HOH HOH A . 
M 4 HOH 196 997  456 HOH HOH A . 
M 4 HOH 197 998  461 HOH HOH A . 
M 4 HOH 198 999  462 HOH HOH A . 
M 4 HOH 199 1000 464 HOH HOH A . 
M 4 HOH 200 1001 465 HOH HOH A . 
M 4 HOH 201 1002 471 HOH HOH A . 
M 4 HOH 202 1003 473 HOH HOH A . 
M 4 HOH 203 1004 474 HOH HOH A . 
M 4 HOH 204 1005 477 HOH HOH A . 
M 4 HOH 205 1006 480 HOH HOH A . 
M 4 HOH 206 1007 481 HOH HOH A . 
M 4 HOH 207 1008 482 HOH HOH A . 
M 4 HOH 208 1009 484 HOH HOH A . 
M 4 HOH 209 1010 487 HOH HOH A . 
M 4 HOH 210 1011 489 HOH HOH A . 
M 4 HOH 211 1012 492 HOH HOH A . 
M 4 HOH 212 1013 495 HOH HOH A . 
M 4 HOH 213 1014 498 HOH HOH A . 
M 4 HOH 214 1015 505 HOH HOH A . 
M 4 HOH 215 1016 506 HOH HOH A . 
M 4 HOH 216 1017 507 HOH HOH A . 
M 4 HOH 217 1018 509 HOH HOH A . 
M 4 HOH 218 1019 511 HOH HOH A . 
M 4 HOH 219 1020 512 HOH HOH A . 
M 4 HOH 220 1021 513 HOH HOH A . 
M 4 HOH 221 1022 514 HOH HOH A . 
M 4 HOH 222 1023 520 HOH HOH A . 
M 4 HOH 223 1024 522 HOH HOH A . 
M 4 HOH 224 1025 523 HOH HOH A . 
M 4 HOH 225 1026 528 HOH HOH A . 
M 4 HOH 226 1027 529 HOH HOH A . 
M 4 HOH 227 1028 530 HOH HOH A . 
M 4 HOH 228 1029 532 HOH HOH A . 
M 4 HOH 229 1030 536 HOH HOH A . 
M 4 HOH 230 1031 538 HOH HOH A . 
M 4 HOH 231 1032 539 HOH HOH A . 
M 4 HOH 232 1033 543 HOH HOH A . 
M 4 HOH 233 1034 544 HOH HOH A . 
M 4 HOH 234 1035 546 HOH HOH A . 
M 4 HOH 235 1036 548 HOH HOH A . 
M 4 HOH 236 1037 549 HOH HOH A . 
M 4 HOH 237 1038 551 HOH HOH A . 
M 4 HOH 238 1039 555 HOH HOH A . 
M 4 HOH 239 1040 556 HOH HOH A . 
M 4 HOH 240 1041 557 HOH HOH A . 
M 4 HOH 241 1042 558 HOH HOH A . 
M 4 HOH 242 1043 559 HOH HOH A . 
M 4 HOH 243 1044 560 HOH HOH A . 
M 4 HOH 244 1045 561 HOH HOH A . 
M 4 HOH 245 1046 563 HOH HOH A . 
M 4 HOH 246 1047 566 HOH HOH A . 
M 4 HOH 247 1048 567 HOH HOH A . 
M 4 HOH 248 1049 570 HOH HOH A . 
M 4 HOH 249 1050 571 HOH HOH A . 
M 4 HOH 250 1051 574 HOH HOH A . 
M 4 HOH 251 1052 577 HOH HOH A . 
M 4 HOH 252 1053 587 HOH HOH A . 
M 4 HOH 253 1054 591 HOH HOH A . 
M 4 HOH 254 1055 596 HOH HOH A . 
M 4 HOH 255 1056 599 HOH HOH A . 
M 4 HOH 256 1057 602 HOH HOH A . 
M 4 HOH 257 1058 605 HOH HOH A . 
M 4 HOH 258 1059 606 HOH HOH A . 
M 4 HOH 259 1060 617 HOH HOH A . 
M 4 HOH 260 1061 618 HOH HOH A . 
M 4 HOH 261 1062 622 HOH HOH A . 
M 4 HOH 262 1063 629 HOH HOH A . 
M 4 HOH 263 1064 631 HOH HOH A . 
M 4 HOH 264 1065 633 HOH HOH A . 
M 4 HOH 265 1066 634 HOH HOH A . 
M 4 HOH 266 1067 635 HOH HOH A . 
M 4 HOH 267 1068 642 HOH HOH A . 
M 4 HOH 268 1069 646 HOH HOH A . 
M 4 HOH 269 1070 647 HOH HOH A . 
M 4 HOH 270 1071 649 HOH HOH A . 
M 4 HOH 271 1072 650 HOH HOH A . 
M 4 HOH 272 1073 656 HOH HOH A . 
M 4 HOH 273 1074 660 HOH HOH A . 
M 4 HOH 274 1075 662 HOH HOH A . 
M 4 HOH 275 1076 666 HOH HOH A . 
M 4 HOH 276 1077 670 HOH HOH A . 
M 4 HOH 277 1078 671 HOH HOH A . 
M 4 HOH 278 1079 677 HOH HOH A . 
M 4 HOH 279 1080 680 HOH HOH A . 
M 4 HOH 280 1081 684 HOH HOH A . 
M 4 HOH 281 1082 689 HOH HOH A . 
M 4 HOH 282 1083 692 HOH HOH A . 
M 4 HOH 283 1084 696 HOH HOH A . 
M 4 HOH 284 1085 697 HOH HOH A . 
M 4 HOH 285 1086 699 HOH HOH A . 
M 4 HOH 286 1087 700 HOH HOH A . 
M 4 HOH 287 1088 702 HOH HOH A . 
M 4 HOH 288 1089 703 HOH HOH A . 
M 4 HOH 289 1090 705 HOH HOH A . 
M 4 HOH 290 1091 706 HOH HOH A . 
M 4 HOH 291 1092 710 HOH HOH A . 
M 4 HOH 292 1093 718 HOH HOH A . 
M 4 HOH 293 1094 722 HOH HOH A . 
M 4 HOH 294 1095 730 HOH HOH A . 
M 4 HOH 295 1096 731 HOH HOH A . 
M 4 HOH 296 1097 734 HOH HOH A . 
N 4 HOH 1   803  10  HOH HOH B . 
N 4 HOH 2   804  30  HOH HOH B . 
N 4 HOH 3   805  83  HOH HOH B . 
N 4 HOH 4   806  88  HOH HOH B . 
N 4 HOH 5   807  89  HOH HOH B . 
N 4 HOH 6   808  92  HOH HOH B . 
N 4 HOH 7   809  116 HOH HOH B . 
N 4 HOH 8   810  124 HOH HOH B . 
N 4 HOH 9   811  139 HOH HOH B . 
N 4 HOH 10  812  156 HOH HOH B . 
N 4 HOH 11  813  157 HOH HOH B . 
N 4 HOH 12  814  158 HOH HOH B . 
N 4 HOH 13  815  174 HOH HOH B . 
N 4 HOH 14  816  176 HOH HOH B . 
N 4 HOH 15  817  179 HOH HOH B . 
N 4 HOH 16  818  181 HOH HOH B . 
N 4 HOH 17  819  184 HOH HOH B . 
N 4 HOH 18  820  191 HOH HOH B . 
N 4 HOH 19  821  193 HOH HOH B . 
N 4 HOH 20  822  194 HOH HOH B . 
N 4 HOH 21  823  207 HOH HOH B . 
N 4 HOH 22  824  214 HOH HOH B . 
N 4 HOH 23  825  220 HOH HOH B . 
N 4 HOH 24  826  223 HOH HOH B . 
N 4 HOH 25  827  227 HOH HOH B . 
N 4 HOH 26  828  229 HOH HOH B . 
N 4 HOH 27  829  231 HOH HOH B . 
N 4 HOH 28  830  240 HOH HOH B . 
N 4 HOH 29  831  247 HOH HOH B . 
N 4 HOH 30  832  260 HOH HOH B . 
N 4 HOH 31  833  263 HOH HOH B . 
N 4 HOH 32  834  267 HOH HOH B . 
N 4 HOH 33  835  300 HOH HOH B . 
N 4 HOH 34  836  302 HOH HOH B . 
N 4 HOH 35  837  308 HOH HOH B . 
N 4 HOH 36  838  309 HOH HOH B . 
N 4 HOH 37  839  323 HOH HOH B . 
N 4 HOH 38  840  324 HOH HOH B . 
N 4 HOH 39  841  326 HOH HOH B . 
N 4 HOH 40  842  329 HOH HOH B . 
N 4 HOH 41  843  337 HOH HOH B . 
N 4 HOH 42  844  347 HOH HOH B . 
N 4 HOH 43  845  349 HOH HOH B . 
N 4 HOH 44  846  353 HOH HOH B . 
N 4 HOH 45  847  355 HOH HOH B . 
N 4 HOH 46  848  356 HOH HOH B . 
N 4 HOH 47  849  361 HOH HOH B . 
N 4 HOH 48  850  363 HOH HOH B . 
N 4 HOH 49  851  365 HOH HOH B . 
N 4 HOH 50  852  369 HOH HOH B . 
N 4 HOH 51  853  372 HOH HOH B . 
N 4 HOH 52  854  377 HOH HOH B . 
N 4 HOH 53  855  380 HOH HOH B . 
N 4 HOH 54  856  381 HOH HOH B . 
N 4 HOH 55  857  386 HOH HOH B . 
N 4 HOH 56  858  394 HOH HOH B . 
N 4 HOH 57  859  397 HOH HOH B . 
N 4 HOH 58  860  405 HOH HOH B . 
N 4 HOH 59  861  406 HOH HOH B . 
N 4 HOH 60  862  411 HOH HOH B . 
N 4 HOH 61  863  412 HOH HOH B . 
N 4 HOH 62  864  414 HOH HOH B . 
N 4 HOH 63  865  420 HOH HOH B . 
N 4 HOH 64  866  424 HOH HOH B . 
N 4 HOH 65  867  427 HOH HOH B . 
N 4 HOH 66  868  428 HOH HOH B . 
N 4 HOH 67  869  434 HOH HOH B . 
N 4 HOH 68  870  436 HOH HOH B . 
N 4 HOH 69  871  440 HOH HOH B . 
N 4 HOH 70  872  441 HOH HOH B . 
N 4 HOH 71  873  444 HOH HOH B . 
N 4 HOH 72  874  450 HOH HOH B . 
N 4 HOH 73  875  451 HOH HOH B . 
N 4 HOH 74  876  459 HOH HOH B . 
N 4 HOH 75  877  463 HOH HOH B . 
N 4 HOH 76  878  466 HOH HOH B . 
N 4 HOH 77  879  468 HOH HOH B . 
N 4 HOH 78  880  470 HOH HOH B . 
N 4 HOH 79  881  472 HOH HOH B . 
N 4 HOH 80  882  475 HOH HOH B . 
N 4 HOH 81  883  478 HOH HOH B . 
N 4 HOH 82  884  485 HOH HOH B . 
N 4 HOH 83  885  488 HOH HOH B . 
N 4 HOH 84  886  490 HOH HOH B . 
N 4 HOH 85  887  493 HOH HOH B . 
N 4 HOH 86  888  494 HOH HOH B . 
N 4 HOH 87  889  499 HOH HOH B . 
N 4 HOH 88  890  500 HOH HOH B . 
N 4 HOH 89  891  503 HOH HOH B . 
N 4 HOH 90  892  508 HOH HOH B . 
N 4 HOH 91  893  516 HOH HOH B . 
N 4 HOH 92  894  517 HOH HOH B . 
N 4 HOH 93  895  519 HOH HOH B . 
N 4 HOH 94  896  521 HOH HOH B . 
N 4 HOH 95  897  526 HOH HOH B . 
N 4 HOH 96  898  527 HOH HOH B . 
N 4 HOH 97  899  531 HOH HOH B . 
N 4 HOH 98  900  540 HOH HOH B . 
N 4 HOH 99  901  542 HOH HOH B . 
N 4 HOH 100 902  550 HOH HOH B . 
N 4 HOH 101 903  554 HOH HOH B . 
N 4 HOH 102 904  564 HOH HOH B . 
N 4 HOH 103 905  565 HOH HOH B . 
N 4 HOH 104 906  568 HOH HOH B . 
N 4 HOH 105 907  579 HOH HOH B . 
N 4 HOH 106 908  582 HOH HOH B . 
N 4 HOH 107 909  595 HOH HOH B . 
N 4 HOH 108 910  607 HOH HOH B . 
N 4 HOH 109 911  608 HOH HOH B . 
N 4 HOH 110 912  615 HOH HOH B . 
N 4 HOH 111 913  623 HOH HOH B . 
N 4 HOH 112 914  624 HOH HOH B . 
N 4 HOH 113 915  626 HOH HOH B . 
N 4 HOH 114 916  630 HOH HOH B . 
N 4 HOH 115 917  636 HOH HOH B . 
N 4 HOH 116 918  637 HOH HOH B . 
N 4 HOH 117 919  638 HOH HOH B . 
N 4 HOH 118 920  641 HOH HOH B . 
N 4 HOH 119 921  645 HOH HOH B . 
N 4 HOH 120 922  648 HOH HOH B . 
N 4 HOH 121 923  651 HOH HOH B . 
N 4 HOH 122 924  652 HOH HOH B . 
N 4 HOH 123 925  653 HOH HOH B . 
N 4 HOH 124 926  657 HOH HOH B . 
N 4 HOH 125 927  667 HOH HOH B . 
N 4 HOH 126 928  668 HOH HOH B . 
N 4 HOH 127 929  673 HOH HOH B . 
N 4 HOH 128 930  675 HOH HOH B . 
N 4 HOH 129 931  678 HOH HOH B . 
N 4 HOH 130 932  679 HOH HOH B . 
N 4 HOH 131 933  681 HOH HOH B . 
N 4 HOH 132 934  682 HOH HOH B . 
N 4 HOH 133 935  683 HOH HOH B . 
N 4 HOH 134 936  685 HOH HOH B . 
N 4 HOH 135 937  687 HOH HOH B . 
N 4 HOH 136 938  690 HOH HOH B . 
N 4 HOH 137 939  694 HOH HOH B . 
N 4 HOH 138 940  695 HOH HOH B . 
N 4 HOH 139 941  698 HOH HOH B . 
N 4 HOH 140 942  708 HOH HOH B . 
N 4 HOH 141 943  709 HOH HOH B . 
N 4 HOH 142 944  711 HOH HOH B . 
N 4 HOH 143 945  716 HOH HOH B . 
N 4 HOH 144 946  717 HOH HOH B . 
N 4 HOH 145 947  724 HOH HOH B . 
N 4 HOH 146 948  727 HOH HOH B . 
N 4 HOH 147 949  729 HOH HOH B . 
N 4 HOH 148 950  732 HOH HOH B . 
O 4 HOH 1   804  1   HOH HOH C . 
O 4 HOH 2   805  3   HOH HOH C . 
O 4 HOH 3   806  4   HOH HOH C . 
O 4 HOH 4   807  5   HOH HOH C . 
O 4 HOH 5   808  6   HOH HOH C . 
O 4 HOH 6   809  8   HOH HOH C . 
O 4 HOH 7   810  12  HOH HOH C . 
O 4 HOH 8   811  14  HOH HOH C . 
O 4 HOH 9   812  15  HOH HOH C . 
O 4 HOH 10  813  16  HOH HOH C . 
O 4 HOH 11  814  19  HOH HOH C . 
O 4 HOH 12  815  20  HOH HOH C . 
O 4 HOH 13  816  22  HOH HOH C . 
O 4 HOH 14  817  23  HOH HOH C . 
O 4 HOH 15  818  25  HOH HOH C . 
O 4 HOH 16  819  26  HOH HOH C . 
O 4 HOH 17  820  29  HOH HOH C . 
O 4 HOH 18  821  31  HOH HOH C . 
O 4 HOH 19  822  32  HOH HOH C . 
O 4 HOH 20  823  33  HOH HOH C . 
O 4 HOH 21  824  36  HOH HOH C . 
O 4 HOH 22  825  37  HOH HOH C . 
O 4 HOH 23  826  42  HOH HOH C . 
O 4 HOH 24  827  44  HOH HOH C . 
O 4 HOH 25  828  45  HOH HOH C . 
O 4 HOH 26  829  46  HOH HOH C . 
O 4 HOH 27  830  47  HOH HOH C . 
O 4 HOH 28  831  48  HOH HOH C . 
O 4 HOH 29  832  51  HOH HOH C . 
O 4 HOH 30  833  55  HOH HOH C . 
O 4 HOH 31  834  56  HOH HOH C . 
O 4 HOH 32  835  58  HOH HOH C . 
O 4 HOH 33  836  59  HOH HOH C . 
O 4 HOH 34  837  62  HOH HOH C . 
O 4 HOH 35  838  65  HOH HOH C . 
O 4 HOH 36  839  71  HOH HOH C . 
O 4 HOH 37  840  72  HOH HOH C . 
O 4 HOH 38  841  77  HOH HOH C . 
O 4 HOH 39  842  79  HOH HOH C . 
O 4 HOH 40  843  81  HOH HOH C . 
O 4 HOH 41  844  84  HOH HOH C . 
O 4 HOH 42  845  85  HOH HOH C . 
O 4 HOH 43  846  91  HOH HOH C . 
O 4 HOH 44  847  93  HOH HOH C . 
O 4 HOH 45  848  94  HOH HOH C . 
O 4 HOH 46  849  96  HOH HOH C . 
O 4 HOH 47  850  98  HOH HOH C . 
O 4 HOH 48  851  100 HOH HOH C . 
O 4 HOH 49  852  102 HOH HOH C . 
O 4 HOH 50  853  103 HOH HOH C . 
O 4 HOH 51  854  104 HOH HOH C . 
O 4 HOH 52  855  105 HOH HOH C . 
O 4 HOH 53  856  106 HOH HOH C . 
O 4 HOH 54  857  108 HOH HOH C . 
O 4 HOH 55  858  111 HOH HOH C . 
O 4 HOH 56  859  112 HOH HOH C . 
O 4 HOH 57  860  113 HOH HOH C . 
O 4 HOH 58  861  115 HOH HOH C . 
O 4 HOH 59  862  117 HOH HOH C . 
O 4 HOH 60  863  119 HOH HOH C . 
O 4 HOH 61  864  123 HOH HOH C . 
O 4 HOH 62  865  125 HOH HOH C . 
O 4 HOH 63  866  126 HOH HOH C . 
O 4 HOH 64  867  127 HOH HOH C . 
O 4 HOH 65  868  132 HOH HOH C . 
O 4 HOH 66  869  133 HOH HOH C . 
O 4 HOH 67  870  135 HOH HOH C . 
O 4 HOH 68  871  136 HOH HOH C . 
O 4 HOH 69  872  140 HOH HOH C . 
O 4 HOH 70  873  143 HOH HOH C . 
O 4 HOH 71  874  146 HOH HOH C . 
O 4 HOH 72  875  149 HOH HOH C . 
O 4 HOH 73  876  150 HOH HOH C . 
O 4 HOH 74  877  151 HOH HOH C . 
O 4 HOH 75  878  152 HOH HOH C . 
O 4 HOH 76  879  153 HOH HOH C . 
O 4 HOH 77  880  154 HOH HOH C . 
O 4 HOH 78  881  155 HOH HOH C . 
O 4 HOH 79  882  161 HOH HOH C . 
O 4 HOH 80  883  164 HOH HOH C . 
O 4 HOH 81  884  165 HOH HOH C . 
O 4 HOH 82  885  166 HOH HOH C . 
O 4 HOH 83  886  167 HOH HOH C . 
O 4 HOH 84  887  170 HOH HOH C . 
O 4 HOH 85  888  180 HOH HOH C . 
O 4 HOH 86  889  188 HOH HOH C . 
O 4 HOH 87  890  189 HOH HOH C . 
O 4 HOH 88  891  192 HOH HOH C . 
O 4 HOH 89  892  195 HOH HOH C . 
O 4 HOH 90  893  196 HOH HOH C . 
O 4 HOH 91  894  200 HOH HOH C . 
O 4 HOH 92  895  201 HOH HOH C . 
O 4 HOH 93  896  202 HOH HOH C . 
O 4 HOH 94  897  205 HOH HOH C . 
O 4 HOH 95  898  211 HOH HOH C . 
O 4 HOH 96  899  212 HOH HOH C . 
O 4 HOH 97  900  213 HOH HOH C . 
O 4 HOH 98  901  215 HOH HOH C . 
O 4 HOH 99  902  217 HOH HOH C . 
O 4 HOH 100 903  219 HOH HOH C . 
O 4 HOH 101 904  221 HOH HOH C . 
O 4 HOH 102 905  222 HOH HOH C . 
O 4 HOH 103 906  226 HOH HOH C . 
O 4 HOH 104 907  228 HOH HOH C . 
O 4 HOH 105 908  232 HOH HOH C . 
O 4 HOH 106 909  233 HOH HOH C . 
O 4 HOH 107 910  238 HOH HOH C . 
O 4 HOH 108 911  241 HOH HOH C . 
O 4 HOH 109 912  242 HOH HOH C . 
O 4 HOH 110 913  244 HOH HOH C . 
O 4 HOH 111 914  245 HOH HOH C . 
O 4 HOH 112 915  246 HOH HOH C . 
O 4 HOH 113 916  254 HOH HOH C . 
O 4 HOH 114 917  256 HOH HOH C . 
O 4 HOH 115 918  258 HOH HOH C . 
O 4 HOH 116 919  259 HOH HOH C . 
O 4 HOH 117 920  264 HOH HOH C . 
O 4 HOH 118 921  265 HOH HOH C . 
O 4 HOH 119 922  269 HOH HOH C . 
O 4 HOH 120 923  271 HOH HOH C . 
O 4 HOH 121 924  274 HOH HOH C . 
O 4 HOH 122 925  278 HOH HOH C . 
O 4 HOH 123 926  279 HOH HOH C . 
O 4 HOH 124 927  281 HOH HOH C . 
O 4 HOH 125 928  282 HOH HOH C . 
O 4 HOH 126 929  283 HOH HOH C . 
O 4 HOH 127 930  286 HOH HOH C . 
O 4 HOH 128 931  288 HOH HOH C . 
O 4 HOH 129 932  289 HOH HOH C . 
O 4 HOH 130 933  290 HOH HOH C . 
O 4 HOH 131 934  291 HOH HOH C . 
O 4 HOH 132 935  293 HOH HOH C . 
O 4 HOH 133 936  303 HOH HOH C . 
O 4 HOH 134 937  305 HOH HOH C . 
O 4 HOH 135 938  311 HOH HOH C . 
O 4 HOH 136 939  312 HOH HOH C . 
O 4 HOH 137 940  313 HOH HOH C . 
O 4 HOH 138 941  317 HOH HOH C . 
O 4 HOH 139 942  318 HOH HOH C . 
O 4 HOH 140 943  319 HOH HOH C . 
O 4 HOH 141 944  320 HOH HOH C . 
O 4 HOH 142 945  321 HOH HOH C . 
O 4 HOH 143 946  322 HOH HOH C . 
O 4 HOH 144 947  325 HOH HOH C . 
O 4 HOH 145 948  328 HOH HOH C . 
O 4 HOH 146 949  330 HOH HOH C . 
O 4 HOH 147 950  335 HOH HOH C . 
O 4 HOH 148 951  336 HOH HOH C . 
O 4 HOH 149 952  340 HOH HOH C . 
O 4 HOH 150 953  344 HOH HOH C . 
O 4 HOH 151 954  345 HOH HOH C . 
O 4 HOH 152 955  348 HOH HOH C . 
O 4 HOH 153 956  350 HOH HOH C . 
O 4 HOH 154 957  351 HOH HOH C . 
O 4 HOH 155 958  359 HOH HOH C . 
O 4 HOH 156 959  368 HOH HOH C . 
O 4 HOH 157 960  371 HOH HOH C . 
O 4 HOH 158 961  373 HOH HOH C . 
O 4 HOH 159 962  374 HOH HOH C . 
O 4 HOH 160 963  376 HOH HOH C . 
O 4 HOH 161 964  379 HOH HOH C . 
O 4 HOH 162 965  382 HOH HOH C . 
O 4 HOH 163 966  383 HOH HOH C . 
O 4 HOH 164 967  384 HOH HOH C . 
O 4 HOH 165 968  390 HOH HOH C . 
O 4 HOH 166 969  391 HOH HOH C . 
O 4 HOH 167 970  392 HOH HOH C . 
O 4 HOH 168 971  393 HOH HOH C . 
O 4 HOH 169 972  396 HOH HOH C . 
O 4 HOH 170 973  398 HOH HOH C . 
O 4 HOH 171 974  399 HOH HOH C . 
O 4 HOH 172 975  400 HOH HOH C . 
O 4 HOH 173 976  404 HOH HOH C . 
O 4 HOH 174 977  407 HOH HOH C . 
O 4 HOH 175 978  409 HOH HOH C . 
O 4 HOH 176 979  417 HOH HOH C . 
O 4 HOH 177 980  419 HOH HOH C . 
O 4 HOH 178 981  421 HOH HOH C . 
O 4 HOH 179 982  426 HOH HOH C . 
O 4 HOH 180 983  429 HOH HOH C . 
O 4 HOH 181 984  430 HOH HOH C . 
O 4 HOH 182 985  431 HOH HOH C . 
O 4 HOH 183 986  432 HOH HOH C . 
O 4 HOH 184 987  433 HOH HOH C . 
O 4 HOH 185 988  439 HOH HOH C . 
O 4 HOH 186 989  445 HOH HOH C . 
O 4 HOH 187 990  449 HOH HOH C . 
O 4 HOH 188 991  457 HOH HOH C . 
O 4 HOH 189 992  458 HOH HOH C . 
O 4 HOH 190 993  460 HOH HOH C . 
O 4 HOH 191 994  467 HOH HOH C . 
O 4 HOH 192 995  469 HOH HOH C . 
O 4 HOH 193 996  476 HOH HOH C . 
O 4 HOH 194 997  479 HOH HOH C . 
O 4 HOH 195 998  483 HOH HOH C . 
O 4 HOH 196 999  486 HOH HOH C . 
O 4 HOH 197 1000 491 HOH HOH C . 
O 4 HOH 198 1001 496 HOH HOH C . 
O 4 HOH 199 1002 497 HOH HOH C . 
O 4 HOH 200 1003 501 HOH HOH C . 
O 4 HOH 201 1004 502 HOH HOH C . 
O 4 HOH 202 1005 504 HOH HOH C . 
O 4 HOH 203 1006 510 HOH HOH C . 
O 4 HOH 204 1007 515 HOH HOH C . 
O 4 HOH 205 1008 518 HOH HOH C . 
O 4 HOH 206 1009 524 HOH HOH C . 
O 4 HOH 207 1010 525 HOH HOH C . 
O 4 HOH 208 1011 533 HOH HOH C . 
O 4 HOH 209 1012 534 HOH HOH C . 
O 4 HOH 210 1013 535 HOH HOH C . 
O 4 HOH 211 1014 537 HOH HOH C . 
O 4 HOH 212 1015 541 HOH HOH C . 
O 4 HOH 213 1016 545 HOH HOH C . 
O 4 HOH 214 1017 547 HOH HOH C . 
O 4 HOH 215 1018 552 HOH HOH C . 
O 4 HOH 216 1019 553 HOH HOH C . 
O 4 HOH 217 1020 562 HOH HOH C . 
O 4 HOH 218 1021 569 HOH HOH C . 
O 4 HOH 219 1022 572 HOH HOH C . 
O 4 HOH 220 1023 573 HOH HOH C . 
O 4 HOH 221 1024 575 HOH HOH C . 
O 4 HOH 222 1025 576 HOH HOH C . 
O 4 HOH 223 1026 578 HOH HOH C . 
O 4 HOH 224 1027 580 HOH HOH C . 
O 4 HOH 225 1028 581 HOH HOH C . 
O 4 HOH 226 1029 583 HOH HOH C . 
O 4 HOH 227 1030 584 HOH HOH C . 
O 4 HOH 228 1031 585 HOH HOH C . 
O 4 HOH 229 1032 586 HOH HOH C . 
O 4 HOH 230 1033 588 HOH HOH C . 
O 4 HOH 231 1034 589 HOH HOH C . 
O 4 HOH 232 1035 590 HOH HOH C . 
O 4 HOH 233 1036 592 HOH HOH C . 
O 4 HOH 234 1037 593 HOH HOH C . 
O 4 HOH 235 1038 594 HOH HOH C . 
O 4 HOH 236 1039 597 HOH HOH C . 
O 4 HOH 237 1040 598 HOH HOH C . 
O 4 HOH 238 1041 600 HOH HOH C . 
O 4 HOH 239 1042 601 HOH HOH C . 
O 4 HOH 240 1043 603 HOH HOH C . 
O 4 HOH 241 1044 604 HOH HOH C . 
O 4 HOH 242 1045 609 HOH HOH C . 
O 4 HOH 243 1046 610 HOH HOH C . 
O 4 HOH 244 1047 611 HOH HOH C . 
O 4 HOH 245 1048 612 HOH HOH C . 
O 4 HOH 246 1049 613 HOH HOH C . 
O 4 HOH 247 1050 614 HOH HOH C . 
O 4 HOH 248 1051 616 HOH HOH C . 
O 4 HOH 249 1052 619 HOH HOH C . 
O 4 HOH 250 1053 620 HOH HOH C . 
O 4 HOH 251 1054 621 HOH HOH C . 
O 4 HOH 252 1055 625 HOH HOH C . 
O 4 HOH 253 1056 627 HOH HOH C . 
O 4 HOH 254 1057 628 HOH HOH C . 
O 4 HOH 255 1058 632 HOH HOH C . 
O 4 HOH 256 1059 639 HOH HOH C . 
O 4 HOH 257 1060 640 HOH HOH C . 
O 4 HOH 258 1061 643 HOH HOH C . 
O 4 HOH 259 1062 644 HOH HOH C . 
O 4 HOH 260 1063 654 HOH HOH C . 
O 4 HOH 261 1064 655 HOH HOH C . 
O 4 HOH 262 1065 658 HOH HOH C . 
O 4 HOH 263 1066 659 HOH HOH C . 
O 4 HOH 264 1067 661 HOH HOH C . 
O 4 HOH 265 1068 663 HOH HOH C . 
O 4 HOH 266 1069 664 HOH HOH C . 
O 4 HOH 267 1070 665 HOH HOH C . 
O 4 HOH 268 1071 669 HOH HOH C . 
O 4 HOH 269 1072 672 HOH HOH C . 
O 4 HOH 270 1073 674 HOH HOH C . 
O 4 HOH 271 1074 676 HOH HOH C . 
O 4 HOH 272 1075 686 HOH HOH C . 
O 4 HOH 273 1076 688 HOH HOH C . 
O 4 HOH 274 1077 691 HOH HOH C . 
O 4 HOH 275 1078 693 HOH HOH C . 
O 4 HOH 276 1079 701 HOH HOH C . 
O 4 HOH 277 1080 704 HOH HOH C . 
O 4 HOH 278 1081 707 HOH HOH C . 
O 4 HOH 279 1082 712 HOH HOH C . 
O 4 HOH 280 1083 713 HOH HOH C . 
O 4 HOH 281 1084 714 HOH HOH C . 
O 4 HOH 282 1085 715 HOH HOH C . 
O 4 HOH 283 1086 719 HOH HOH C . 
O 4 HOH 284 1087 720 HOH HOH C . 
O 4 HOH 285 1088 721 HOH HOH C . 
O 4 HOH 286 1089 723 HOH HOH C . 
O 4 HOH 287 1090 725 HOH HOH C . 
O 4 HOH 288 1091 726 HOH HOH C . 
O 4 HOH 289 1092 728 HOH HOH C . 
O 4 HOH 290 1093 733 HOH HOH C . 
O 4 HOH 291 1094 735 HOH HOH C . 
O 4 HOH 292 1095 736 HOH HOH C . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSX 111 A CSX 111 ? CYS 'S-OXY CYSTEINE' 
2 B CSX 111 B CSX 111 ? CYS 'S-OXY CYSTEINE' 
3 C CSX 111 C CSX 111 ? CYS 'S-OXY CYSTEINE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_defined_assembly              ?    dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,D,E,F,G,H,I,M,N 
2 1,2 C,J,K,L,O           
# 
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)' 2030  ? 
1 MORE         -129  ? 
1 'SSA (A^2)'  13100 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_455 -x-1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 -70.4490000000 0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 71.5400000000 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 1057 ? M HOH . 
2 1 C HOH 1086 ? O HOH . 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 119.8 ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 101.3 ? 
3  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 125.2 ? 
4  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 O1  ? D SO4 .   ? A SO4 801 ? 1_555 102.9 ? 
5  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 O1  ? D SO4 .   ? A SO4 801 ? 1_555 100.4 ? 
6  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? E ZN . ? A ZN 201 ? 1_555 O1  ? D SO4 .   ? A SO4 801 ? 1_555 104.1 ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 102.2 ? 
8  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 107.9 ? 
9  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 123.2 ? 
10 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 105.2 ? 
11 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 98.1  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 118.0 ? 
13 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 157.1 ? 
14 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 79.8  ? 
15 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 89.1  ? 
16 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? F ZN . ? A ZN 202 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 52.3  ? 
17 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 113.9 ? 
18 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 98.9  ? 
19 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 125.9 ? 
20 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 O2  ? G SO4 .   ? B SO4 802 ? 1_555 98.8  ? 
21 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 O2  ? G SO4 .   ? B SO4 802 ? 1_555 105.6 ? 
22 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 ZN ? H ZN . ? B ZN 203 ? 1_555 O2  ? G SO4 .   ? B SO4 802 ? 1_555 110.6 ? 
23 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 104.1 ? 
24 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 99.3  ? 
25 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 122.8 ? 
26 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 109.8 ? 
27 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 97.5  ? 
28 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 122.2 ? 
29 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 163.2 ? 
30 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 78.6  ? 
31 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 92.8  ? 
32 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 ZN ? I ZN . ? B ZN 204 ? 1_555 OD2 ? B ASP 83  ? B ASP 83  ? 1_555 53.6  ? 
33 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 119.3 ? 
34 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 100.4 ? 
35 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 125.6 ? 
36 ND1 ? C HIS 46  ? C HIS 46  ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 O1  ? J SO4 .   ? C SO4 803 ? 1_555 102.3 ? 
37 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 O1  ? J SO4 .   ? C SO4 803 ? 1_555 102.0 ? 
38 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 ZN ? K ZN . ? C ZN 205 ? 1_555 O1  ? J SO4 .   ? C SO4 803 ? 1_555 104.1 ? 
39 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 105.7 ? 
40 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 107.7 ? 
41 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 122.3 ? 
42 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 104.2 ? 
43 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 99.4  ? 
44 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 ZN ? L ZN . ? C ZN 206 ? 1_555 OD1 ? C ASP 83  ? C ASP 83  ? 1_555 115.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2003-08-26 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-10-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Database references'       
4 4 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' database_2             
2 4 'Structure model' pdbx_struct_conn_angle 
3 4 'Structure model' struct_conn            
4 4 'Structure model' struct_conn_type       
5 4 'Structure model' struct_ref_seq_dif     
6 4 'Structure model' struct_site            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_database_2.pdbx_DOI'                        
2  4 'Structure model' '_database_2.pdbx_database_accession'         
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
17 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
18 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
19 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
20 4 'Structure model' '_pdbx_struct_conn_angle.value'               
21 4 'Structure model' '_struct_conn.conn_type_id'                   
22 4 'Structure model' '_struct_conn.id'                             
23 4 'Structure model' '_struct_conn.pdbx_dist_value'                
24 4 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
25 4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
26 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
27 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
28 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
29 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
30 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
31 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
32 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
33 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
34 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
35 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
36 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
37 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
38 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
39 4 'Structure model' '_struct_conn_type.id'                        
40 4 'Structure model' '_struct_ref_seq_dif.details'                 
41 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
42 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
43 4 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
SHELX     'model building' . ? 1 
SHELXL-97 refinement       . ? 2 
HKL-2000  'data reduction' . ? 3 
SCALEPACK 'data scaling'   . ? 4 
CNS       phasing          . ? 5 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 79  ? ? CZ B ARG 79  ? ? NH1 B ARG 79  ? ? 117.22 120.30 -3.08 0.50 N 
2 1 CB B ASP 83  ? ? CG B ASP 83  ? ? OD1 B ASP 83  ? ? 126.82 118.30 8.52  0.90 N 
3 1 CB B ASP 96  ? ? CG B ASP 96  ? ? OD1 B ASP 96  ? ? 124.12 118.30 5.82  0.90 N 
4 1 NE B ARG 115 ? ? CZ B ARG 115 ? ? NH2 B ARG 115 ? ? 123.99 120.30 3.69  0.50 N 
5 1 CD C ARG 69  ? ? NE C ARG 69  ? ? CZ  C ARG 69  ? ? 133.05 123.60 9.45  1.40 N 
# 
_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    A 
_pdbx_validate_torsion.auth_seq_id     65 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -147.63 
_pdbx_validate_torsion.psi             59.98 
# 
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 GLY 129 ? A GLY 129 
2  1 Y 1 A GLY 130 ? A GLY 130 
3  1 Y 1 A ASN 131 ? A ASN 131 
4  1 Y 1 A GLU 132 ? A GLU 132 
5  1 Y 1 A GLU 133 ? A GLU 133 
6  1 Y 1 A SER 134 ? A SER 134 
7  1 Y 1 A THR 135 ? A THR 135 
8  1 Y 1 B LYS 128 ? B LYS 128 
9  1 Y 1 B GLY 129 ? B GLY 129 
10 1 Y 1 B GLY 130 ? B GLY 130 
11 1 Y 1 B ASN 131 ? B ASN 131 
12 1 Y 1 B GLU 132 ? B GLU 132 
13 1 Y 1 B GLU 133 ? B GLU 133 
14 1 Y 1 B SER 134 ? B SER 134 
15 1 Y 1 B THR 135 ? B THR 135 
16 1 Y 1 B LYS 136 ? B LYS 136 
17 1 Y 1 C GLY 129 ? C GLY 129 
18 1 Y 1 C GLY 130 ? C GLY 130 
19 1 Y 1 C ASN 131 ? C ASN 131 
20 1 Y 1 C GLU 132 ? C GLU 132 
21 1 Y 1 C GLU 133 ? C GLU 133 
22 1 Y 1 C SER 134 ? C SER 134 
23 1 Y 1 C THR 135 ? C THR 135 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 'ZINC ION'    ZN  
4 water         HOH 
# 
