data_2V0A
# 
_entry.id   2V0A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2V0A         
PDBE  EBI-32531    
WWPDB D_1290032531 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2V0A 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2007-05-11 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strange, R.W.' 1 
'Antonyuk, S.'  2 
'Yong, C.W.'    3 
'Smith, W.'     4 
'Hasnain, S.S.' 5 
# 
_citation.id                        primary 
_citation.title                     
;Molecular Dynamics Using Atomic-Resolution Structure Reveal Structural Fluctuations that May Lead to Polymerization of Human Cu-Zn Superoxide Dismutase.
;
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            104 
_citation.page_first                10040 
_citation.page_last                 ? 
_citation.year                      2007 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17548825 
_citation.pdbx_database_id_DOI      10.1073/PNAS.0703857104 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strange, R.W.' 1 
primary 'Yong, C.W.'    2 
primary 'Smith, W.'     3 
primary 'Hasnain, S.S.' 4 
# 
_cell.entry_id           2V0A 
_cell.length_a           38.545 
_cell.length_b           68.220 
_cell.length_c           50.306 
_cell.angle_alpha        90.00 
_cell.angle_beta         105.14 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2V0A 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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     nat 'SUPEROXIDE DISMUTASE' 15827.561 2   1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'      63.546    2   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'             65.409    2   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'          96.063    3   ?        ? ? ? 
5 non-polymer syn 'ACETATE ION'          59.044    1   ?        ? ? ? 
6 water       nat water                  18.015    576 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F 
_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 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                HUMAN 
_entity_src_nat.pdbx_organism_scientific   'HOMO SAPIENS' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9606 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    'HUMAN BLOOD' 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 2V0A A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 2V0A F 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
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 
ACT non-polymer         . 'ACETATE ION'     ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ? 'C4 H7 N O4'     133.103 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
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          2V0A 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2 
_exptl_crystal.density_percent_sol   38 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.75 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '3.5 M AMMONIUM SULPHATE, 100MM NACL, 50MM ACETATE BUFFER PH 4.75' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC CCD' 
_diffrn_detector.pdbx_collection_date   2004-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX14.2' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX14.2 
_diffrn_source.pdbx_wavelength             0.98 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2V0A 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             21.500 
_reflns.d_resolution_high            1.150 
_reflns.number_obs                   88555 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.12000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.0000 
_reflns.B_iso_Wilson_estimate        12.00 
_reflns.pdbx_redundancy              3.600 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.15 
_reflns_shell.d_res_low              1.19 
_reflns_shell.percent_possible_all   89.0 
_reflns_shell.Rmerge_I_obs           0.55000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.200 
_reflns_shell.pdbx_redundancy        2.70 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2V0A 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     88555 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             21.50 
_refine.ls_d_res_high                            1.15 
_refine.ls_percent_reflns_obs                    97.5 
_refine.ls_R_factor_obs                          0.157 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.155 
_refine.ls_R_factor_R_free                       0.206 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.000 
_refine.ls_number_reflns_R_free                  3458 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_refine.B_iso_mean                               13.43 
_refine.aniso_B[1][1]                            0.55000 
_refine.aniso_B[2][2]                            -1.43000 
_refine.aniso_B[3][3]                            0.59000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.56000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          OTHER 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.042 
_refine.pdbx_overall_ESU_R_Free                  0.046 
_refine.overall_SU_ML                            0.036 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.746 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2220 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             576 
_refine_hist.number_atoms_total               2819 
_refine_hist.d_res_high                       1.15 
_refine_hist.d_res_low                        21.50 
# 
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 
r_bond_refined_d             0.023  0.021  ? 2436 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 2141 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.209  1.959  ? 3291 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            2.583  3.000  ? 5064 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       10.812 5.000  ? 321  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       40.085 25.872 ? 109  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.210 15.000 ? 415  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       13.232 15.000 ? 9    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.155  0.200  ? 360  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.013  0.020  ? 2775 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.004  0.020  ? 432  'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.369  0.200  ? 632  'X-RAY DIFFRACTION' ? 
r_nbd_other                  0.259  0.200  ? 2388 'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.169  0.200  ? 1157 'X-RAY DIFFRACTION' ? 
r_nbtor_other                0.104  0.200  ? 1473 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.280  0.200  ? 413  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.298  0.200  ? 49   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         0.278  0.200  ? 91   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.287  0.200  ? 83   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.227  2.000  ? 1616 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.114  4.000  ? 2509 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.440  6.000  ? 904  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 6.751  8.000  ? 779  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.15 
_refine_ls_shell.d_res_low                        1.18 
_refine_ls_shell.number_reflns_R_work             5594 
_refine_ls_shell.R_factor_R_work                  0.2790 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.3440 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             259 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  2V0A 
_struct.title                     'Atomic resolution crystal structure of Human Superoxide Dismutase' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2V0A 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;DISEASE MUTATION, MOLECULAR DINAMICS, AMYOTROPHIC LATERAL SCLEROSIS, ZN SUPEROXIDE DISMUTASE, METAL-BINDING, OXIOREDUCTASE, OXIDOREDUCTASE, ZINC, COPPER, HUMAN CU, ACETYLATION, ANTIOXIDANT
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_biol.id   1 
# 
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 GLY A 56  ? GLY A 61  ? GLY A 56  GLY A 61  5 ? 6 
HELX_P HELX_P2 2 SER A 107 ? HIS A 110 ? SER A 107 HIS A 110 5 ? 4 
HELX_P HELX_P3 3 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P4 4 GLY B 56  ? GLY B 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P5 5 SER B 107 ? HIS B 110 ? SER F 107 HIS F 110 5 ? 4 
HELX_P HELX_P6 6 ASN B 131 ? LYS B 136 ? ASN F 131 LYS F 136 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57   A CYS 146 1_555 ? ? ? ? ? ? ? 2.084 ? 
disulf2  disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG  ? ? F CYS 57   F CYS 146 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc1  metalc ? ? C CU  .  CU A ? ? 1_555 A HIS 120 NE2 ? ? A CU  1154 A HIS 120 1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc2  metalc ? ? C CU  .  CU A ? ? 1_555 A HIS 46  ND1 ? ? A CU  1154 A HIS 46  1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc3  metalc ? ? C CU  .  CU A ? ? 1_555 A HIS 48  NE2 ? ? A CU  1154 A HIS 48  1_555 ? ? ? ? ? ? ? 1.962 ? 
metalc4  metalc ? ? C CU  .  CU B ? ? 1_555 A HIS 120 NE2 ? ? A CU  1154 A HIS 120 1_555 ? ? ? ? ? ? ? 2.291 ? 
metalc5  metalc ? ? C CU  .  CU B ? ? 1_555 A HIS 46  ND1 ? ? A CU  1154 A HIS 46  1_555 ? ? ? ? ? ? ? 1.875 ? 
metalc6  metalc ? ? C CU  .  CU B ? ? 1_555 A HIS 63  NE2 ? ? A CU  1154 A HIS 63  1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc7  metalc ? ? C CU  .  CU B ? ? 1_555 A HIS 48  NE2 ? ? A CU  1154 A HIS 48  1_555 ? ? ? ? ? ? ? 2.397 ? 
metalc8  metalc ? ? D ZN  .  ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  1155 A ASP 83  1_555 ? ? ? ? ? ? ? 1.940 ? 
metalc9  metalc ? ? D ZN  .  ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  1155 A HIS 80  1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc10 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  1155 A HIS 71  1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc11 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  1155 A HIS 63  1_555 ? ? ? ? ? ? ? 1.982 ? 
metalc12 metalc ? ? H CU  .  CU B ? ? 1_555 B HIS 63  NE2 ? ? F CU  1156 F HIS 63  1_555 ? ? ? ? ? ? ? 2.442 ? 
metalc13 metalc ? ? H CU  .  CU B ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120 1_555 ? ? ? ? ? ? ? 2.200 ? 
metalc14 metalc ? ? H CU  .  CU B ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46  1_555 ? ? ? ? ? ? ? 1.889 ? 
metalc15 metalc ? ? H CU  .  CU B ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48  1_555 ? ? ? ? ? ? ? 2.413 ? 
metalc16 metalc ? ? H CU  .  CU A ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120 1_555 ? ? ? ? ? ? ? 1.988 ? 
metalc17 metalc ? ? H CU  .  CU A ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46  1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc18 metalc ? ? H CU  .  CU A ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48  1_555 ? ? ? ? ? ? ? 1.939 ? 
metalc19 metalc ? ? I ZN  .  ZN ? ? ? 1_555 B HIS 71  ND1 ? ? F ZN  1157 F HIS 71  1_555 ? ? ? ? ? ? ? 2.062 ? 
metalc20 metalc ? ? I ZN  .  ZN ? ? ? 1_555 B HIS 80  ND1 ? ? F ZN  1157 F HIS 80  1_555 ? ? ? ? ? ? ? 2.013 ? 
metalc21 metalc ? ? I ZN  .  ZN ? ? ? 1_555 B ASP 83  OD1 ? ? F ZN  1157 F ASP 83  1_555 ? ? ? ? ? ? ? 1.954 ? 
metalc22 metalc ? ? I ZN  .  ZN ? ? ? 1_555 B HIS 63  ND1 ? ? F ZN  1157 F HIS 63  1_555 ? ? ? ? ? ? ? 2.029 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           12 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            12 
_struct_mon_prot_cis.auth_asym_id           F 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    13 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     13 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    F 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
FA ? 5 ? 
FB ? 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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
FA 1 2 ? anti-parallel 
FA 2 3 ? anti-parallel 
FA 3 4 ? anti-parallel 
FA 4 5 ? anti-parallel 
FB 1 2 ? anti-parallel 
FB 2 3 ? anti-parallel 
FB 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 
AA 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA 4 LYS A 3   ? LEU A 8   ? LYS A 3   LEU A 8   
AA 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AB 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AB 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AB 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AB 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
FA 1 ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
FA 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
FA 3 VAL B 14  ? GLN B 22  ? VAL F 14  GLN F 22  
FA 4 LYS B 3   ? GLY B 10  ? LYS F 3   GLY F 10  
FA 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
FB 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
FB 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
FB 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
FB 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 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 
AA 1 2 N ASP A 101 ? N ASP A 101 O VAL A 29  ? O VAL A 29  
AA 2 3 N LYS A 36  ? N LYS A 36  O GLN A 15  ? O GLN A 15  
AA 3 4 N PHE A 20  ? N PHE A 20  O ALA A 4   ? O ALA A 4   
AA 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AB 1 2 N ALA A 89  ? N ALA A 89  O GLY A 41  ? O GLY A 41  
AB 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AB 3 4 O VAL A 119 ? O VAL A 119 N LEU A 144 ? N LEU A 144 
FA 1 2 N ASP B 101 ? N ASP F 101 O VAL B 29  ? O VAL F 29  
FA 2 3 N LYS B 36  ? N LYS F 36  O GLN B 15  ? O GLN F 15  
FA 3 4 N PHE B 20  ? N PHE F 20  O ALA B 4   ? O ALA F 4   
FA 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
FB 1 2 N ALA B 89  ? N ALA F 89  O GLY B 41  ? O GLY F 41  
FB 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
FB 3 4 O VAL B 119 ? O VAL F 119 N LEU B 144 ? N LEU F 144 
# 
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 ? ? ? ? 6  'BINDING SITE FOR RESIDUE CU A1154'  
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A1155'  
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A1157' 
AC4 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE SO4 A1158' 
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE ACT F1154' 
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU F1156'  
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F1157'  
AC8 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 F1158' 
# 
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 6  HIS A 46  ? HIS A 46   . ? 1_555 ? 
2  AC1 6  HIS A 48  ? HIS A 48   . ? 1_555 ? 
3  AC1 6  HIS A 63  ? HIS A 63   . ? 1_555 ? 
4  AC1 6  HIS A 120 ? HIS A 120  . ? 1_555 ? 
5  AC1 6  HOH K .   ? HOH A 2114 . ? 1_555 ? 
6  AC1 6  HOH K .   ? HOH A 2231 . ? 1_555 ? 
7  AC2 4  HIS A 63  ? HIS A 63   . ? 1_555 ? 
8  AC2 4  HIS A 71  ? HIS A 71   . ? 1_555 ? 
9  AC2 4  HIS A 80  ? HIS A 80   . ? 1_555 ? 
10 AC2 4  ASP A 83  ? ASP A 83   . ? 1_555 ? 
11 AC3 10 THR A 58  ? THR A 58   . ? 1_555 ? 
12 AC3 10 SER A 142 ? SER A 142  . ? 1_555 ? 
13 AC3 10 ARG A 143 ? ARG A 143  . ? 1_555 ? 
14 AC3 10 HOH K .   ? HOH A 2108 . ? 1_555 ? 
15 AC3 10 HOH K .   ? HOH A 2234 . ? 1_555 ? 
16 AC3 10 HOH K .   ? HOH A 2256 . ? 1_555 ? 
17 AC3 10 HOH K .   ? HOH A 2257 . ? 1_555 ? 
18 AC3 10 HOH K .   ? HOH A 2259 . ? 1_555 ? 
19 AC3 10 HOH K .   ? HOH A 2261 . ? 1_555 ? 
20 AC3 10 HOH K .   ? HOH A 2262 . ? 1_555 ? 
21 AC4 11 GLU A 133 ? GLU A 133  . ? 1_555 ? 
22 AC4 11 THR A 137 ? THR A 137  . ? 1_555 ? 
23 AC4 11 ASN A 139 ? ASN A 139  . ? 1_555 ? 
24 AC4 11 ALA A 140 ? ALA A 140  . ? 1_555 ? 
25 AC4 11 GLY A 141 ? GLY A 141  . ? 1_555 ? 
26 AC4 11 HOH K .   ? HOH A 2204 . ? 1_555 ? 
27 AC4 11 HOH K .   ? HOH A 2226 . ? 1_555 ? 
28 AC4 11 HOH K .   ? HOH A 2263 . ? 1_555 ? 
29 AC4 11 HOH K .   ? HOH A 2265 . ? 1_555 ? 
30 AC4 11 HOH K .   ? HOH A 2266 . ? 1_555 ? 
31 AC4 11 HOH K .   ? HOH A 2267 . ? 1_555 ? 
32 AC5 6  THR B 58  ? THR F 58   . ? 1_555 ? 
33 AC5 6  ARG B 143 ? ARG F 143  . ? 1_555 ? 
34 AC5 6  HOH L .   ? HOH F 2278 . ? 1_555 ? 
35 AC5 6  HOH L .   ? HOH F 2301 . ? 1_555 ? 
36 AC5 6  HOH L .   ? HOH F 2303 . ? 1_555 ? 
37 AC5 6  HOH L .   ? HOH F 2304 . ? 1_555 ? 
38 AC6 5  HIS B 46  ? HIS F 46   . ? 1_555 ? 
39 AC6 5  HIS B 48  ? HIS F 48   . ? 1_555 ? 
40 AC6 5  HIS B 63  ? HIS F 63   . ? 1_555 ? 
41 AC6 5  HIS B 120 ? HIS F 120  . ? 1_555 ? 
42 AC6 5  HOH L .   ? HOH F 2276 . ? 1_555 ? 
43 AC7 4  HIS B 63  ? HIS F 63   . ? 1_555 ? 
44 AC7 4  HIS B 71  ? HIS F 71   . ? 1_555 ? 
45 AC7 4  HIS B 80  ? HIS F 80   . ? 1_555 ? 
46 AC7 4  ASP B 83  ? ASP F 83   . ? 1_555 ? 
47 AC8 10 GLU B 133 ? GLU F 133  . ? 1_555 ? 
48 AC8 10 THR B 137 ? THR F 137  . ? 1_555 ? 
49 AC8 10 ASN B 139 ? ASN F 139  . ? 1_555 ? 
50 AC8 10 ALA B 140 ? ALA F 140  . ? 1_555 ? 
51 AC8 10 GLY B 141 ? GLY F 141  . ? 1_555 ? 
52 AC8 10 HOH L .   ? HOH F 2305 . ? 1_555 ? 
53 AC8 10 HOH L .   ? HOH F 2306 . ? 1_555 ? 
54 AC8 10 HOH L .   ? HOH F 2307 . ? 1_555 ? 
55 AC8 10 HOH L .   ? HOH F 2308 . ? 1_555 ? 
56 AC8 10 HOH L .   ? HOH F 2309 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2V0A 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2V0A 
_atom_sites.fract_transf_matrix[1][1]   0.025944 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007020 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014658 
_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]   0.020593 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A ALA A 1 1   ? 30.311 3.480   23.034  0.40 16.73 ? 1    ALA A N   1 
ATOM   2    N  N   B ALA A 1 1   ? 30.106 5.298   30.258  0.20 15.72 ? 1    ALA A N   1 
ATOM   3    C  CA  A ALA A 1 1   ? 28.888 3.743   23.418  0.40 16.98 ? 1    ALA A CA  1 
ATOM   4    C  CA  B ALA A 1 1   ? 28.791 4.639   30.007  0.20 16.05 ? 1    ALA A CA  1 
ATOM   5    C  C   A ALA A 1 1   ? 28.584 3.119   24.791  0.40 15.12 ? 1    ALA A C   1 
ATOM   6    C  C   B ALA A 1 1   ? 28.466 4.640   28.510  0.20 14.65 ? 1    ALA A C   1 
ATOM   7    O  O   A ALA A 1 1   ? 29.088 2.064   25.111  0.40 14.87 ? 1    ALA A O   1 
ATOM   8    O  O   B ALA A 1 1   ? 28.827 5.588   27.796  0.20 15.72 ? 1    ALA A O   1 
ATOM   9    C  CB  A ALA A 1 1   ? 27.971 3.171   22.373  0.40 16.13 ? 1    ALA A CB  1 
ATOM   10   C  CB  B ALA A 1 1   ? 27.694 5.330   30.791  0.20 16.61 ? 1    ALA A CB  1 
ATOM   11   N  N   A THR A 1 2   ? 27.756 3.789   25.600  0.40 12.58 ? 2    THR A N   1 
ATOM   12   N  N   B THR A 1 2   ? 27.848 3.549   28.046  0.30 13.24 ? 2    THR A N   1 
ATOM   13   C  CA  A THR A 1 2   ? 27.287 3.302   26.893  0.40 14.05 ? 2    THR A CA  1 
ATOM   14   C  CA  B THR A 1 2   ? 27.320 3.397   26.687  0.30 13.90 ? 2    THR A CA  1 
ATOM   15   C  C   A THR A 1 2   ? 25.862 2.931   26.765  0.50 11.48 ? 2    THR A C   1 
ATOM   16   C  C   B THR A 1 2   ? 25.764 3.067   26.919  0.40 12.25 ? 2    THR A C   1 
ATOM   17   O  O   A THR A 1 2   ? 25.506 2.072   27.571  0.50 10.62 ? 2    THR A O   1 
ATOM   18   O  O   B THR A 1 2   ? 25.235 2.579   27.914  0.30 10.27 ? 2    THR A O   1 
ATOM   19   C  CB  A THR A 1 2   ? 27.625 4.280   28.031  0.40 13.76 ? 2    THR A CB  1 
ATOM   20   C  CB  B THR A 1 2   ? 28.053 2.281   25.894  0.30 15.19 ? 2    THR A CB  1 
ATOM   21   O  OG1 A THR A 1 2   ? 26.926 5.519   27.814  0.40 17.26 ? 2    THR A OG1 1 
ATOM   22   O  OG1 B THR A 1 2   ? 29.466 2.480   25.960  0.30 17.93 ? 2    THR A OG1 1 
ATOM   23   C  CG2 A THR A 1 2   ? 29.147 4.530   28.088  0.40 16.81 ? 2    THR A CG2 1 
ATOM   24   C  CG2 B THR A 1 2   ? 27.611 2.238   24.421  0.30 11.32 ? 2    THR A CG2 1 
ATOM   25   N  N   . LYS A 1 3   ? 25.041 3.492   25.873  1.00 12.41 ? 3    LYS A N   1 
ATOM   26   C  CA  . LYS A 1 3   ? 23.638 3.202   25.743  1.00 10.90 ? 3    LYS A CA  1 
ATOM   27   C  C   . LYS A 1 3   ? 23.284 2.836   24.329  1.00 11.49 ? 3    LYS A C   1 
ATOM   28   O  O   . LYS A 1 3   ? 23.837 3.359   23.348  1.00 11.03 ? 3    LYS A O   1 
ATOM   29   C  CB  . LYS A 1 3   ? 22.747 4.353   26.172  1.00 12.92 ? 3    LYS A CB  1 
ATOM   30   C  CG  . LYS A 1 3   ? 22.902 4.684   27.661  1.00 15.90 ? 3    LYS A CG  1 
ATOM   31   C  CD  . LYS A 1 3   ? 22.075 5.857   28.136  1.00 18.40 ? 3    LYS A CD  1 
ATOM   32   C  CE  . LYS A 1 3   ? 22.336 6.106   29.602  1.00 26.24 ? 3    LYS A CE  1 
ATOM   33   N  NZ  . LYS A 1 3   ? 22.087 7.545   29.948  1.00 33.26 ? 3    LYS A NZ  1 
ATOM   34   N  N   . ALA A 1 4   ? 22.301 1.934   24.211  1.00 9.99  ? 4    ALA A N   1 
ATOM   35   C  CA  . ALA A 1 4   ? 21.794 1.544   22.873  1.00 10.43 ? 4    ALA A CA  1 
ATOM   36   C  C   . ALA A 1 4   ? 20.284 1.281   22.989  1.00 9.29  ? 4    ALA A C   1 
ATOM   37   O  O   . ALA A 1 4   ? 19.757 1.202   24.096  1.00 11.04 ? 4    ALA A O   1 
ATOM   38   C  CB  . ALA A 1 4   ? 22.538 0.354   22.303  1.00 12.11 ? 4    ALA A CB  1 
ATOM   39   N  N   . VAL A 1 5   ? 19.621 1.178   21.873  1.00 9.79  ? 5    VAL A N   1 
ATOM   40   C  CA  . VAL A 1 5   ? 18.190 1.046   21.833  1.00 9.76  ? 5    VAL A CA  1 
ATOM   41   C  C   . VAL A 1 5   ? 17.785 0.289   20.582  1.00 9.83  ? 5    VAL A C   1 
ATOM   42   O  O   . VAL A 1 5   ? 18.488 0.287   19.590  1.00 9.92  ? 5    VAL A O   1 
ATOM   43   C  CB  . VAL A 1 5   ? 17.551 2.450   21.909  1.00 10.60 ? 5    VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 5   ? 17.828 3.255   20.615  1.00 12.70 ? 5    VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 5   ? 16.080 2.377   22.141  1.00 12.71 ? 5    VAL A CG2 1 
ATOM   46   N  N   . CYS A 1 6   ? 16.651 -0.383  20.640  1.00 9.49  ? 6    CYS A N   1 
ATOM   47   C  CA  . CYS A 1 6   ? 16.109 -1.094  19.499  1.00 9.56  ? 6    CYS A CA  1 
ATOM   48   C  C   . CYS A 1 6   ? 14.596 -1.061  19.492  1.00 9.11  ? 6    CYS A C   1 
ATOM   49   O  O   . CYS A 1 6   ? 13.953 -1.371  20.524  1.00 10.92 ? 6    CYS A O   1 
ATOM   50   C  CB  . CYS A 1 6   ? 16.558 -2.566  19.583  1.00 9.86  ? 6    CYS A CB  1 
ATOM   51   S  SG  . CYS A 1 6   ? 16.105 -3.550  18.155  1.00 12.19 ? 6    CYS A SG  1 
ATOM   52   N  N   . VAL A 1 7   ? 14.035 -0.716  18.370  1.00 9.73  ? 7    VAL A N   1 
ATOM   53   C  CA  . VAL A 1 7   ? 12.617 -0.712  18.147  1.00 10.00 ? 7    VAL A CA  1 
ATOM   54   C  C   . VAL A 1 7   ? 12.287 -1.939  17.398  1.00 10.36 ? 7    VAL A C   1 
ATOM   55   O  O   . VAL A 1 7   ? 12.791 -2.161  16.276  1.00 11.26 ? 7    VAL A O   1 
ATOM   56   C  CB  . VAL A 1 7   ? 12.204 0.563   17.341  1.00 12.44 ? 7    VAL A CB  1 
ATOM   57   C  CG1 . VAL A 1 7   ? 10.642 0.488   17.089  1.00 15.78 ? 7    VAL A CG1 1 
ATOM   58   C  CG2 . VAL A 1 7   ? 12.542 1.830   18.107  1.00 14.30 ? 7    VAL A CG2 1 
ATOM   59   N  N   . LEU A 1 8   ? 11.511 -2.822  17.973  1.00 11.01 ? 8    LEU A N   1 
ATOM   60   C  CA  . LEU A 1 8   ? 11.119 -4.060  17.369  1.00 10.22 ? 8    LEU A CA  1 
ATOM   61   C  C   . LEU A 1 8   ? 9.769  -3.924  16.630  1.00 11.39 ? 8    LEU A C   1 
ATOM   62   O  O   . LEU A 1 8   ? 8.768  -3.565  17.213  1.00 13.23 ? 8    LEU A O   1 
ATOM   63   C  CB  . LEU A 1 8   ? 10.956 -5.157  18.430  1.00 11.67 ? 8    LEU A CB  1 
ATOM   64   C  CG  . LEU A 1 8   ? 12.190 -5.522  19.245  1.00 13.22 ? 8    LEU A CG  1 
ATOM   65   C  CD1 . LEU A 1 8   ? 11.786 -6.444  20.418  1.00 14.21 ? 8    LEU A CD1 1 
ATOM   66   C  CD2 . LEU A 1 8   ? 13.170 -6.197  18.376  1.00 17.25 ? 8    LEU A CD2 1 
ATOM   67   N  N   . LYS A 1 9   ? 9.747  -4.299  15.352  1.00 13.69 ? 9    LYS A N   1 
ATOM   68   C  CA  . LYS A 1 9   ? 8.532  -4.283  14.511  1.00 15.24 ? 9    LYS A CA  1 
ATOM   69   C  C   . LYS A 1 9   ? 8.618  -5.451  13.553  1.00 13.61 ? 9    LYS A C   1 
ATOM   70   O  O   . LYS A 1 9   ? 9.715  -5.921  13.258  1.00 14.34 ? 9    LYS A O   1 
ATOM   71   C  CB  . LYS A 1 9   ? 8.491  -2.981  13.691  1.00 16.66 ? 9    LYS A CB  1 
ATOM   72   C  CG  . LYS A 1 9   ? 8.310  -1.722  14.429  0.50 15.61 ? 9    LYS A CG  1 
ATOM   73   C  CD  . LYS A 1 9   ? 6.944  -1.643  15.103  0.30 17.11 ? 9    LYS A CD  1 
ATOM   74   C  CE  . LYS A 1 9   ? 6.622  -0.224  15.557  0.30 19.11 ? 9    LYS A CE  1 
ATOM   75   N  NZ  . LYS A 1 9   ? 5.134  -0.044  15.519  0.30 20.77 ? 9    LYS A NZ  1 
ATOM   76   N  N   . GLY A 1 10  ? 7.484  -5.898  13.053  1.00 15.41 ? 10   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 10  ? 7.454  -6.904  12.039  1.00 14.60 ? 10   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 10  ? 6.170  -6.782  11.224  1.00 18.07 ? 10   GLY A C   1 
ATOM   79   O  O   . GLY A 1 10  ? 5.565  -5.689  11.119  1.00 21.56 ? 10   GLY A O   1 
ATOM   80   N  N   . ASP A 1 11  ? 5.767  -7.889  10.647  1.00 17.19 ? 11   ASP A N   1 
ATOM   81   C  CA  . ASP A 1 11  ? 4.588  -7.861  9.742   1.00 20.28 ? 11   ASP A CA  1 
ATOM   82   C  C   . ASP A 1 11  ? 3.269  -8.073  10.442  1.00 20.88 ? 11   ASP A C   1 
ATOM   83   O  O   . ASP A 1 11  ? 2.219  -7.902  9.810   1.00 23.59 ? 11   ASP A O   1 
ATOM   84   C  CB  . ASP A 1 11  ? 4.757  -8.915  8.682   1.00 23.18 ? 11   ASP A CB  1 
ATOM   85   C  CG  . ASP A 1 11  ? 5.832  -8.579  7.719   0.50 19.92 ? 11   ASP A CG  1 
ATOM   86   O  OD1 . ASP A 1 11  ? 6.137  -7.367  7.544   0.50 18.88 ? 11   ASP A OD1 1 
ATOM   87   O  OD2 . ASP A 1 11  ? 6.391  -9.536  7.148   0.50 23.84 ? 11   ASP A OD2 1 
ATOM   88   N  N   . GLY A 1 12  ? 3.268  -8.441  11.724  1.00 19.84 ? 12   GLY A N   1 
ATOM   89   C  CA  . GLY A 1 12  ? 2.099  -8.759  12.471  1.00 18.96 ? 12   GLY A CA  1 
ATOM   90   C  C   . GLY A 1 12  ? 2.005  -7.829  13.618  1.00 17.84 ? 12   GLY A C   1 
ATOM   91   O  O   . GLY A 1 12  ? 2.451  -6.704  13.555  1.00 20.85 ? 12   GLY A O   1 
ATOM   92   N  N   . PRO A 1 13  ? 1.372  -8.290  14.703  1.00 17.90 ? 13   PRO A N   1 
ATOM   93   C  CA  . PRO A 1 13  ? 1.097  -7.433  15.838  1.00 18.46 ? 13   PRO A CA  1 
ATOM   94   C  C   . PRO A 1 13  ? 2.195  -7.230  16.865  1.00 18.00 ? 13   PRO A C   1 
ATOM   95   O  O   . PRO A 1 13  ? 2.053  -6.450  17.823  1.00 21.34 ? 13   PRO A O   1 
ATOM   96   C  CB  . PRO A 1 13  ? -0.082 -8.128  16.508  1.00 21.25 ? 13   PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 13  ? 0.201  -9.602  16.271  1.00 19.99 ? 13   PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 13  ? 0.770  -9.629  14.869  1.00 21.20 ? 13   PRO A CD  1 
ATOM   99   N  N   . VAL A 1 14  ? 3.324  -7.892  16.676  1.00 16.90 ? 14   VAL A N   1 
ATOM   100  C  CA  . VAL A 1 14  ? 4.353  -7.854  17.695  1.00 15.65 ? 14   VAL A CA  1 
ATOM   101  C  C   . VAL A 1 14  ? 5.178  -6.589  17.537  1.00 15.14 ? 14   VAL A C   1 
ATOM   102  O  O   . VAL A 1 14  ? 5.679  -6.295  16.455  1.00 17.59 ? 14   VAL A O   1 
ATOM   103  C  CB  . VAL A 1 14  ? 5.253  -9.104  17.648  1.00 13.42 ? 14   VAL A CB  1 
ATOM   104  C  CG1 . VAL A 1 14  ? 6.313  -9.002  18.676  1.00 14.33 ? 14   VAL A CG1 1 
ATOM   105  C  CG2 . VAL A 1 14  ? 4.405  -10.348 17.859  1.00 17.21 ? 14   VAL A CG2 1 
ATOM   106  N  N   . GLN A 1 15  ? 5.277  -5.832  18.608  1.00 15.51 ? 15   GLN A N   1 
ATOM   107  C  CA  . GLN A 1 15  ? 6.097  -4.617  18.617  1.00 15.53 ? 15   GLN A CA  1 
ATOM   108  C  C   . GLN A 1 15  ? 6.640  -4.385  20.003  1.00 15.62 ? 15   GLN A C   1 
ATOM   109  O  O   . GLN A 1 15  ? 6.047  -4.752  21.030  1.00 18.10 ? 15   GLN A O   1 
ATOM   110  C  CB  . GLN A 1 15  ? 5.296  -3.413  18.160  1.00 20.66 ? 15   GLN A CB  1 
ATOM   111  C  CG  . GLN A 1 15  ? 4.110  -3.089  18.930  1.00 24.11 ? 15   GLN A CG  1 
ATOM   112  C  CD  . GLN A 1 15  ? 3.573  -1.745  18.479  0.50 23.93 ? 15   GLN A CD  1 
ATOM   113  O  OE1 . GLN A 1 15  ? 3.906  -0.698  19.044  0.50 23.51 ? 15   GLN A OE1 1 
ATOM   114  N  NE2 . GLN A 1 15  ? 2.814  -1.763  17.418  0.50 21.47 ? 15   GLN A NE2 1 
ATOM   115  N  N   . GLY A 1 16  ? 7.843  -3.814  20.046  1.00 14.34 ? 16   GLY A N   1 
ATOM   116  C  CA  . GLY A 1 16  ? 8.397  -3.474  21.315  1.00 16.21 ? 16   GLY A CA  1 
ATOM   117  C  C   . GLY A 1 16  ? 9.551  -2.502  21.266  1.00 13.52 ? 16   GLY A C   1 
ATOM   118  O  O   . GLY A 1 16  ? 9.928  -2.035  20.214  1.00 15.15 ? 16   GLY A O   1 
ATOM   119  N  N   . ILE A 1 17  ? 10.008 -2.150  22.444  1.00 12.84 ? 17   ILE A N   1 
ATOM   120  C  CA  . ILE A 1 17  ? 11.152 -1.268  22.599  1.00 13.49 ? 17   ILE A CA  1 
ATOM   121  C  C   . ILE A 1 17  ? 12.071 -1.845  23.644  1.00 11.77 ? 17   ILE A C   1 
ATOM   122  O  O   . ILE A 1 17  ? 11.610 -2.138  24.774  1.00 13.73 ? 17   ILE A O   1 
ATOM   123  C  CB  . ILE A 1 17  ? 10.681 0.180   23.062  1.00 15.97 ? 17   ILE A CB  1 
ATOM   124  C  CG1 A ILE A 1 17  ? 9.449  0.748   22.433  0.50 15.94 ? 17   ILE A CG1 1 
ATOM   125  C  CG1 B ILE A 1 17  ? 11.829 1.100   23.420  0.50 18.36 ? 17   ILE A CG1 1 
ATOM   126  C  CG2 A ILE A 1 17  ? 11.815 1.095   23.254  0.50 16.62 ? 17   ILE A CG2 1 
ATOM   127  C  CG2 B ILE A 1 17  ? 9.462  0.093   23.989  0.50 16.14 ? 17   ILE A CG2 1 
ATOM   128  C  CD1 A ILE A 1 17  ? 9.857  1.101   21.047  0.50 15.39 ? 17   ILE A CD1 1 
ATOM   129  C  CD1 B ILE A 1 17  ? 12.579 1.599   22.150  0.50 21.67 ? 17   ILE A CD1 1 
ATOM   130  N  N   . ILE A 1 18  ? 13.359 -1.908  23.336  1.00 11.13 ? 18   ILE A N   1 
ATOM   131  C  CA  . ILE A 1 18  ? 14.344 -2.483  24.190  1.00 10.91 ? 18   ILE A CA  1 
ATOM   132  C  C   . ILE A 1 18  ? 15.522 -1.566  24.324  1.00 10.76 ? 18   ILE A C   1 
ATOM   133  O  O   . ILE A 1 18  ? 16.066 -1.059  23.317  1.00 11.79 ? 18   ILE A O   1 
ATOM   134  C  CB  . ILE A 1 18  ? 14.822 -3.876  23.681  1.00 10.98 ? 18   ILE A CB  1 
ATOM   135  C  CG1 . ILE A 1 18  ? 13.671 -4.885  23.508  1.00 14.21 ? 18   ILE A CG1 1 
ATOM   136  C  CG2 . ILE A 1 18  ? 15.918 -4.462  24.535  1.00 11.59 ? 18   ILE A CG2 1 
ATOM   137  C  CD1 . ILE A 1 18  ? 12.943 -5.269  24.815  1.00 17.54 ? 18   ILE A CD1 1 
ATOM   138  N  N   . ASN A 1 19  ? 15.927 -1.308  25.552  1.00 10.94 ? 19   ASN A N   1 
ATOM   139  C  CA  . ASN A 1 19  ? 17.012 -0.468  25.846  1.00 10.74 ? 19   ASN A CA  1 
ATOM   140  C  C   . ASN A 1 19  ? 18.204 -1.289  26.383  1.00 10.50 ? 19   ASN A C   1 
ATOM   141  O  O   . ASN A 1 19  ? 17.989 -2.295  27.068  1.00 11.53 ? 19   ASN A O   1 
ATOM   142  C  CB  . ASN A 1 19  ? 16.590 0.556   26.915  1.00 12.91 ? 19   ASN A CB  1 
ATOM   143  C  CG  . ASN A 1 19  ? 15.284 1.245   26.556  1.00 14.73 ? 19   ASN A CG  1 
ATOM   144  O  OD1 . ASN A 1 19  ? 14.167 0.972   27.109  1.00 24.14 ? 19   ASN A OD1 1 
ATOM   145  N  ND2 . ASN A 1 19  ? 15.388 2.183   25.661  1.00 15.38 ? 19   ASN A ND2 1 
ATOM   146  N  N   . PHE A 1 20  ? 19.431 -0.812  26.184  1.00 10.39 ? 20   PHE A N   1 
ATOM   147  C  CA  . PHE A 1 20  ? 20.644 -1.412  26.602  1.00 10.18 ? 20   PHE A CA  1 
ATOM   148  C  C   . PHE A 1 20  ? 21.481 -0.325  27.299  1.00 10.72 ? 20   PHE A C   1 
ATOM   149  O  O   . PHE A 1 20  ? 21.610 0.814   26.837  1.00 11.36 ? 20   PHE A O   1 
ATOM   150  C  CB  . PHE A 1 20  ? 21.493 -1.915  25.409  1.00 11.10 ? 20   PHE A CB  1 
ATOM   151  C  CG  . PHE A 1 20  ? 20.782 -2.966  24.520  1.00 10.81 ? 20   PHE A CG  1 
ATOM   152  C  CD1 . PHE A 1 20  ? 19.865 -2.561  23.566  1.00 12.05 ? 20   PHE A CD1 1 
ATOM   153  C  CD2 . PHE A 1 20  ? 20.978 -4.312  24.696  1.00 11.31 ? 20   PHE A CD2 1 
ATOM   154  C  CE1 . PHE A 1 20  ? 19.254 -3.467  22.770  1.00 11.57 ? 20   PHE A CE1 1 
ATOM   155  C  CE2 . PHE A 1 20  ? 20.352 -5.241  23.910  1.00 11.74 ? 20   PHE A CE2 1 
ATOM   156  C  CZ  . PHE A 1 20  ? 19.481 -4.809  22.945  1.00 12.46 ? 20   PHE A CZ  1 
ATOM   157  N  N   . GLU A 1 21  ? 22.142 -0.726  28.385  1.00 11.50 ? 21   GLU A N   1 
ATOM   158  C  CA  . GLU A 1 21  ? 23.086 0.131   29.050  1.00 13.29 ? 21   GLU A CA  1 
ATOM   159  C  C   . GLU A 1 21  ? 24.295 -0.627  29.516  1.00 11.74 ? 21   GLU A C   1 
ATOM   160  O  O   . GLU A 1 21  ? 24.157 -1.652  30.155  1.00 13.99 ? 21   GLU A O   1 
ATOM   161  C  CB  . GLU A 1 21  ? 22.440 0.898   30.172  1.00 14.43 ? 21   GLU A CB  1 
ATOM   162  C  CG  . GLU A 1 21  ? 23.401 1.904   30.854  1.00 20.54 ? 21   GLU A CG  1 
ATOM   163  C  CD  . GLU A 1 21  ? 22.701 2.907   31.767  0.50 18.84 ? 21   GLU A CD  1 
ATOM   164  O  OE1 . GLU A 1 21  ? 21.605 2.639   32.270  0.50 21.85 ? 21   GLU A OE1 1 
ATOM   165  O  OE2 . GLU A 1 21  ? 23.307 3.969   32.008  0.50 24.85 ? 21   GLU A OE2 1 
ATOM   166  N  N   . GLN A 1 22  ? 25.491 -0.089  29.262  1.00 12.41 ? 22   GLN A N   1 
ATOM   167  C  CA  . GLN A 1 22  ? 26.774 -0.654  29.694  1.00 13.36 ? 22   GLN A CA  1 
ATOM   168  C  C   . GLN A 1 22  ? 27.601 0.449   30.331  1.00 14.40 ? 22   GLN A C   1 
ATOM   169  O  O   . GLN A 1 22  ? 28.147 1.324   29.690  1.00 18.35 ? 22   GLN A O   1 
ATOM   170  C  CB  . GLN A 1 22  ? 27.503 -1.324  28.532  1.00 11.87 ? 22   GLN A CB  1 
ATOM   171  C  CG  . GLN A 1 22  ? 28.708 -2.072  28.913  1.00 13.42 ? 22   GLN A CG  1 
ATOM   172  C  CD  . GLN A 1 22  ? 29.388 -2.695  27.723  1.00 14.51 ? 22   GLN A CD  1 
ATOM   173  O  OE1 . GLN A 1 22  ? 29.322 -2.159  26.596  1.00 15.37 ? 22   GLN A OE1 1 
ATOM   174  N  NE2 . GLN A 1 22  ? 30.077 -3.831  27.934  1.00 14.74 ? 22   GLN A NE2 1 
ATOM   175  N  N   . LYS A 1 23  ? 27.659 0.363   31.631  1.00 17.36 ? 23   LYS A N   1 
ATOM   176  C  CA  . LYS A 1 23  ? 28.356 1.359   32.455  1.00 20.95 ? 23   LYS A CA  1 
ATOM   177  C  C   . LYS A 1 23  ? 29.824 1.414   32.235  1.00 22.68 ? 23   LYS A C   1 
ATOM   178  O  O   . LYS A 1 23  ? 30.424 2.488   32.256  1.00 26.01 ? 23   LYS A O   1 
ATOM   179  C  CB  . LYS A 1 23  ? 28.083 1.078   33.908  1.00 23.18 ? 23   LYS A CB  1 
ATOM   180  C  CG  . LYS A 1 23  ? 26.697 1.509   34.257  1.00 27.79 ? 23   LYS A CG  1 
ATOM   181  C  CD  . LYS A 1 23  ? 26.512 1.604   35.760  0.50 25.93 ? 23   LYS A CD  1 
ATOM   182  C  CE  . LYS A 1 23  ? 26.391 0.204   36.357  0.50 30.01 ? 23   LYS A CE  1 
ATOM   183  N  NZ  . LYS A 1 23  ? 25.805 0.182   37.713  0.50 31.96 ? 23   LYS A NZ  1 
ATOM   184  N  N   . GLU A 1 24  ? 30.392 0.268   32.004  1.00 23.87 ? 24   GLU A N   1 
ATOM   185  C  CA  . GLU A 1 24  ? 31.824 0.222   31.963  1.00 25.13 ? 24   GLU A CA  1 
ATOM   186  C  C   . GLU A 1 24  ? 32.220 -0.547  30.780  1.00 27.32 ? 24   GLU A C   1 
ATOM   187  O  O   . GLU A 1 24  ? 31.587 -1.582  30.404  1.00 26.50 ? 24   GLU A O   1 
ATOM   188  C  CB  . GLU A 1 24  ? 32.392 -0.442  33.225  1.00 27.30 ? 24   GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 24  ? 31.990 0.235   34.512  1.00 28.48 ? 24   GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 24  ? 32.636 -0.415  35.733  0.20 26.90 ? 24   GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 24  ? 33.049 -1.595  35.649  0.20 26.48 ? 24   GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 24  ? 32.726 0.256   36.783  0.20 28.22 ? 24   GLU A OE2 1 
ATOM   193  N  N   . SER A 1 25  ? 33.314 -0.086  30.187  1.00 29.51 ? 25   SER A N   1 
ATOM   194  C  CA  . SER A 1 25  ? 33.937 -0.886  29.206  1.00 30.76 ? 25   SER A CA  1 
ATOM   195  C  C   . SER A 1 25  ? 34.140 -2.276  29.838  1.00 32.29 ? 25   SER A C   1 
ATOM   196  O  O   . SER A 1 25  ? 34.590 -2.404  30.984  1.00 36.53 ? 25   SER A O   1 
ATOM   197  C  CB  . SER A 1 25  ? 35.290 -0.308  28.792  0.50 29.38 ? 25   SER A CB  1 
ATOM   198  O  OG  . SER A 1 25  ? 35.957 -1.247  27.980  0.50 32.29 ? 25   SER A OG  1 
ATOM   199  N  N   . ASN A 1 26  ? 33.816 -3.295  29.066  1.00 31.51 ? 26   ASN A N   1 
ATOM   200  C  CA  . ASN A 1 26  ? 33.873 -4.663  29.510  1.00 28.31 ? 26   ASN A CA  1 
ATOM   201  C  C   . ASN A 1 26  ? 33.094 -5.004  30.789  1.00 26.46 ? 26   ASN A C   1 
ATOM   202  O  O   . ASN A 1 26  ? 33.317 -6.015  31.409  1.00 28.99 ? 26   ASN A O   1 
ATOM   203  C  CB  . ASN A 1 26  ? 35.330 -5.114  29.552  1.00 26.72 ? 26   ASN A CB  1 
ATOM   204  C  CG  . ASN A 1 26  ? 36.018 -5.006  28.171  0.50 25.87 ? 26   ASN A CG  1 
ATOM   205  O  OD1 . ASN A 1 26  ? 35.654 -5.702  27.207  0.50 28.68 ? 26   ASN A OD1 1 
ATOM   206  N  ND2 . ASN A 1 26  ? 36.998 -4.124  28.083  0.50 23.17 ? 26   ASN A ND2 1 
ATOM   207  N  N   . GLY A 1 27  ? 32.082 -4.223  31.100  1.00 22.18 ? 27   GLY A N   1 
ATOM   208  C  CA  . GLY A 1 27  ? 31.169 -4.642  32.165  1.00 19.96 ? 27   GLY A CA  1 
ATOM   209  C  C   . GLY A 1 27  ? 29.861 -5.215  31.601  1.00 16.20 ? 27   GLY A C   1 
ATOM   210  O  O   . GLY A 1 27  ? 29.658 -5.272  30.366  1.00 16.82 ? 27   GLY A O   1 
ATOM   211  N  N   . PRO A 1 28  ? 28.964 -5.638  32.449  1.00 15.36 ? 28   PRO A N   1 
ATOM   212  C  CA  . PRO A 1 28  ? 27.734 -6.240  31.980  1.00 15.33 ? 28   PRO A CA  1 
ATOM   213  C  C   . PRO A 1 28  ? 26.832 -5.210  31.309  1.00 12.91 ? 28   PRO A C   1 
ATOM   214  O  O   . PRO A 1 28  ? 26.930 -4.008  31.587  1.00 13.79 ? 28   PRO A O   1 
ATOM   215  C  CB  . PRO A 1 28  ? 27.087 -6.696  33.273  1.00 17.95 ? 28   PRO A CB  1 
ATOM   216  C  CG  . PRO A 1 28  ? 27.708 -5.782  34.301  1.00 19.71 ? 28   PRO A CG  1 
ATOM   217  C  CD  . PRO A 1 28  ? 29.069 -5.535  33.902  1.00 17.06 ? 28   PRO A CD  1 
ATOM   218  N  N   . VAL A 1 29  ? 25.898 -5.721  30.511  1.00 13.55 ? 29   VAL A N   1 
ATOM   219  C  CA  . VAL A 1 29  ? 24.928 -4.925  29.782  1.00 11.50 ? 29   VAL A CA  1 
ATOM   220  C  C   . VAL A 1 29  ? 23.558 -5.218  30.321  1.00 12.07 ? 29   VAL A C   1 
ATOM   221  O  O   . VAL A 1 29  ? 23.123 -6.336  30.343  1.00 13.19 ? 29   VAL A O   1 
ATOM   222  C  CB  . VAL A 1 29  ? 24.953 -5.204  28.271  1.00 11.92 ? 29   VAL A CB  1 
ATOM   223  C  CG1 . VAL A 1 29  ? 23.984 -4.314  27.569  1.00 12.73 ? 29   VAL A CG1 1 
ATOM   224  C  CG2 . VAL A 1 29  ? 26.379 -5.033  27.683  1.00 13.33 ? 29   VAL A CG2 1 
ATOM   225  N  N   . LYS A 1 30  ? 22.864 -4.160  30.828  1.00 11.47 ? 30   LYS A N   1 
ATOM   226  C  CA  . LYS A 1 30  ? 21.497 -4.210  31.239  1.00 12.07 ? 30   LYS A CA  1 
ATOM   227  C  C   . LYS A 1 30  ? 20.650 -4.101  29.980  1.00 11.54 ? 30   LYS A C   1 
ATOM   228  O  O   . LYS A 1 30  ? 20.865 -3.218  29.172  1.00 12.96 ? 30   LYS A O   1 
ATOM   229  C  CB  . LYS A 1 30  ? 21.236 -3.080  32.224  1.00 13.38 ? 30   LYS A CB  1 
ATOM   230  C  CG  . LYS A 1 30  ? 21.941 -3.197  33.586  1.00 20.59 ? 30   LYS A CG  1 
ATOM   231  C  CD  . LYS A 1 30  ? 21.101 -2.649  34.757  1.00 26.40 ? 30   LYS A CD  1 
ATOM   232  C  CE  . LYS A 1 30  ? 21.945 -2.472  36.005  1.00 30.48 ? 30   LYS A CE  1 
ATOM   233  N  NZ  . LYS A 1 30  ? 21.349 -1.450  36.893  1.00 34.86 ? 30   LYS A NZ  1 
ATOM   234  N  N   . VAL A 1 31  ? 19.601 -4.942  29.914  1.00 12.36 ? 31   VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? 18.727 -5.010  28.754  1.00 12.30 ? 31   VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? 17.316 -4.936  29.369  1.00 14.23 ? 31   VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? 16.950 -5.735  30.259  1.00 16.86 ? 31   VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? 18.875 -6.304  28.012  1.00 13.59 ? 31   VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? 17.963 -6.371  26.761  1.00 13.66 ? 31   VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? 20.346 -6.527  27.638  1.00 13.43 ? 31   VAL A CG2 1 
ATOM   241  N  N   . TRP A 1 32  ? 16.510 -3.936  28.997  1.00 12.94 ? 32   TRP A N   1 
ATOM   242  C  CA  . TRP A 1 32  ? 15.171 -3.774  29.532  1.00 13.96 ? 32   TRP A CA  1 
ATOM   243  C  C   . TRP A 1 32  ? 14.227 -3.070  28.590  1.00 13.43 ? 32   TRP A C   1 
ATOM   244  O  O   . TRP A 1 32  ? 14.581 -2.286  27.745  1.00 12.73 ? 32   TRP A O   1 
ATOM   245  C  CB  . TRP A 1 32  ? 15.230 -3.008  30.868  1.00 17.21 ? 32   TRP A CB  1 
ATOM   246  C  CG  . TRP A 1 32  ? 15.474 -1.578  30.740  1.00 17.42 ? 32   TRP A CG  1 
ATOM   247  C  CD1 . TRP A 1 32  ? 14.542 -0.562  30.757  1.00 20.87 ? 32   TRP A CD1 1 
ATOM   248  C  CD2 . TRP A 1 32  ? 16.761 -0.906  30.571  1.00 14.96 ? 32   TRP A CD2 1 
ATOM   249  N  NE1 . TRP A 1 32  ? 15.129 0.651   30.593  1.00 21.43 ? 32   TRP A NE1 1 
ATOM   250  C  CE2 . TRP A 1 32  ? 16.482 0.484   30.485  1.00 16.12 ? 32   TRP A CE2 1 
ATOM   251  C  CE3 . TRP A 1 32  ? 18.100 -1.337  30.379  1.00 17.75 ? 32   TRP A CE3 1 
ATOM   252  C  CZ2 . TRP A 1 32  ? 17.447 1.412   30.310  1.00 20.89 ? 32   TRP A CZ2 1 
ATOM   253  C  CZ3 . TRP A 1 32  ? 19.069 -0.372  30.247  1.00 19.99 ? 32   TRP A CZ3 1 
ATOM   254  C  CH2 . TRP A 1 32  ? 18.725 0.991   30.222  1.00 21.31 ? 32   TRP A CH2 1 
ATOM   255  N  N   . GLY A 1 33  ? 12.973 -3.429  28.737  1.00 12.79 ? 33   GLY A N   1 
ATOM   256  C  CA  . GLY A 1 33  ? 11.906 -2.819  27.992  1.00 13.09 ? 33   GLY A CA  1 
ATOM   257  C  C   . GLY A 1 33  ? 10.679 -3.690  27.953  1.00 14.64 ? 33   GLY A C   1 
ATOM   258  O  O   . GLY A 1 33  ? 10.435 -4.402  28.938  1.00 16.81 ? 33   GLY A O   1 
ATOM   259  N  N   . SER A 1 34  ? 9.901  -3.609  26.873  1.00 15.55 ? 34   SER A N   1 
ATOM   260  C  CA  . SER A 1 34  ? 8.599  -4.289  26.830  1.00 16.60 ? 34   SER A CA  1 
ATOM   261  C  C   . SER A 1 34  ? 8.353  -4.711  25.368  1.00 15.99 ? 34   SER A C   1 
ATOM   262  O  O   . SER A 1 34  ? 8.692  -4.015  24.450  1.00 17.03 ? 34   SER A O   1 
ATOM   263  C  CB  . SER A 1 34  ? 7.485  -3.352  27.363  1.00 18.39 ? 34   SER A CB  1 
ATOM   264  O  OG  . SER A 1 34  ? 6.295  -4.022  27.370  1.00 23.07 ? 34   SER A OG  1 
ATOM   265  N  N   . ILE A 1 35  ? 7.611  -5.800  25.213  1.00 16.38 ? 35   ILE A N   1 
ATOM   266  C  CA  . ILE A 1 35  ? 7.171  -6.294  23.935  1.00 14.49 ? 35   ILE A CA  1 
ATOM   267  C  C   . ILE A 1 35  ? 5.718  -6.662  24.126  1.00 15.56 ? 35   ILE A C   1 
ATOM   268  O  O   . ILE A 1 35  ? 5.392  -7.326  25.116  1.00 15.89 ? 35   ILE A O   1 
ATOM   269  C  CB  . ILE A 1 35  ? 8.000  -7.463  23.402  1.00 15.31 ? 35   ILE A CB  1 
ATOM   270  C  CG1 . ILE A 1 35  ? 9.511  -7.171  23.472  1.00 14.44 ? 35   ILE A CG1 1 
ATOM   271  C  CG2 . ILE A 1 35  ? 7.579  -7.917  21.979  1.00 14.94 ? 35   ILE A CG2 1 
ATOM   272  C  CD1 . ILE A 1 35  ? 10.405 -8.371  23.181  1.00 14.63 ? 35   ILE A CD1 1 
ATOM   273  N  N   . LYS A 1 36  ? 4.875  -6.290  23.196  1.00 15.54 ? 36   LYS A N   1 
ATOM   274  C  CA  . LYS A 1 36  ? 3.439  -6.592  23.229  1.00 17.61 ? 36   LYS A CA  1 
ATOM   275  C  C   . LYS A 1 36  ? 3.019  -7.339  21.976  1.00 17.03 ? 36   LYS A C   1 
ATOM   276  O  O   . LYS A 1 36  ? 3.764  -7.377  20.991  1.00 15.49 ? 36   LYS A O   1 
ATOM   277  C  CB  . LYS A 1 36  ? 2.630  -5.295  23.412  1.00 18.19 ? 36   LYS A CB  1 
ATOM   278  C  CG  . LYS A 1 36  ? 2.699  -4.291  22.299  1.00 22.37 ? 36   LYS A CG  1 
ATOM   279  C  CD  . LYS A 1 36  ? 1.861  -3.075  22.758  1.00 21.43 ? 36   LYS A CD  1 
ATOM   280  C  CE  . LYS A 1 36  ? 2.039  -1.834  21.869  1.00 25.68 ? 36   LYS A CE  1 
ATOM   281  N  NZ  . LYS A 1 36  ? 1.077  -0.771  22.313  1.00 23.99 ? 36   LYS A NZ  1 
ATOM   282  N  N   . GLY A 1 37  ? 1.804  -7.838  21.935  1.00 18.14 ? 37   GLY A N   1 
ATOM   283  C  CA  . GLY A 1 37  ? 1.245  -8.531  20.775  1.00 18.33 ? 37   GLY A CA  1 
ATOM   284  C  C   . GLY A 1 37  ? 1.647  -9.993  20.669  1.00 16.90 ? 37   GLY A C   1 
ATOM   285  O  O   . GLY A 1 37  ? 1.473  -10.632 19.619  1.00 19.32 ? 37   GLY A O   1 
ATOM   286  N  N   . LEU A 1 38  ? 2.263  -10.528 21.728  1.00 15.78 ? 38   LEU A N   1 
ATOM   287  C  CA  . LEU A 1 38  ? 2.789  -11.887 21.703  1.00 13.46 ? 38   LEU A CA  1 
ATOM   288  C  C   . LEU A 1 38  ? 1.723  -12.886 22.210  1.00 13.65 ? 38   LEU A C   1 
ATOM   289  O  O   . LEU A 1 38  ? 0.889  -12.598 23.044  1.00 20.44 ? 38   LEU A O   1 
ATOM   290  C  CB  . LEU A 1 38  ? 4.014  -11.968 22.626  1.00 15.23 ? 38   LEU A CB  1 
ATOM   291  C  CG  . LEU A 1 38  ? 5.275  -11.215 22.191  1.00 14.60 ? 38   LEU A CG  1 
ATOM   292  C  CD1 . LEU A 1 38  ? 6.182  -11.042 23.409  1.00 15.93 ? 38   LEU A CD1 1 
ATOM   293  C  CD2 . LEU A 1 38  ? 5.941  -12.025 21.050  1.00 13.98 ? 38   LEU A CD2 1 
ATOM   294  N  N   . THR A 1 39  ? 1.914  -14.122 21.759  1.00 13.57 ? 39   THR A N   1 
ATOM   295  C  CA  . THR A 1 39  ? 1.194  -15.243 22.393  1.00 13.78 ? 39   THR A CA  1 
ATOM   296  C  C   . THR A 1 39  ? 1.813  -15.534 23.765  1.00 13.20 ? 39   THR A C   1 
ATOM   297  O  O   . THR A 1 39  ? 2.972  -15.388 24.013  1.00 14.63 ? 39   THR A O   1 
ATOM   298  C  CB  . THR A 1 39  ? 1.211  -16.518 21.568  1.00 14.34 ? 39   THR A CB  1 
ATOM   299  O  OG1 . THR A 1 39  ? 2.558  -16.926 21.333  1.00 15.85 ? 39   THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 39  ? 0.541  -16.273 20.175  1.00 14.96 ? 39   THR A CG2 1 
ATOM   301  N  N   . GLU A 1 40  ? 0.967  -16.035 24.655  1.00 14.52 ? 40   GLU A N   1 
ATOM   302  C  CA  . GLU A 1 40  ? 1.400  -16.349 26.008  1.00 13.58 ? 40   GLU A CA  1 
ATOM   303  C  C   . GLU A 1 40  ? 2.485  -17.394 25.967  1.00 14.63 ? 40   GLU A C   1 
ATOM   304  O  O   . GLU A 1 40  ? 2.417  -18.372 25.231  1.00 15.31 ? 40   GLU A O   1 
ATOM   305  C  CB  . GLU A 1 40  ? 0.167  -16.874 26.802  1.00 15.26 ? 40   GLU A CB  1 
ATOM   306  C  CG  A GLU A 1 40  ? 0.458  -17.458 28.217  0.50 13.61 ? 40   GLU A CG  1 
ATOM   307  C  CG  B GLU A 1 40  ? 0.458  -16.925 28.333  0.50 13.86 ? 40   GLU A CG  1 
ATOM   308  C  CD  A GLU A 1 40  ? -0.732 -18.119 28.825  0.50 16.23 ? 40   GLU A CD  1 
ATOM   309  C  CD  B GLU A 1 40  ? -0.281 -17.961 29.101  0.50 18.23 ? 40   GLU A CD  1 
ATOM   310  O  OE1 A GLU A 1 40  ? -1.559 -18.740 28.082  0.50 19.25 ? 40   GLU A OE1 1 
ATOM   311  O  OE1 B GLU A 1 40  ? -0.971 -18.870 28.531  0.50 20.17 ? 40   GLU A OE1 1 
ATOM   312  O  OE2 A GLU A 1 40  ? -0.827 -18.035 30.058  0.50 15.08 ? 40   GLU A OE2 1 
ATOM   313  O  OE2 B GLU A 1 40  ? -0.194 -17.837 30.326  0.50 17.77 ? 40   GLU A OE2 1 
ATOM   314  N  N   . GLY A 1 41  ? 3.511  -17.196 26.777  1.00 14.00 ? 41   GLY A N   1 
ATOM   315  C  CA  . GLY A 1 41  ? 4.539  -18.156 26.833  1.00 13.12 ? 41   GLY A CA  1 
ATOM   316  C  C   . GLY A 1 41  ? 5.900  -17.622 26.446  1.00 12.59 ? 41   GLY A C   1 
ATOM   317  O  O   . GLY A 1 41  ? 6.125  -16.405 26.313  1.00 12.37 ? 41   GLY A O   1 
ATOM   318  N  N   . LEU A 1 42  ? 6.837  -18.526 26.219  1.00 11.28 ? 42   LEU A N   1 
ATOM   319  C  CA  . LEU A 1 42  ? 8.227  -18.160 25.953  1.00 10.74 ? 42   LEU A CA  1 
ATOM   320  C  C   . LEU A 1 42  ? 8.373  -17.819 24.458  1.00 10.87 ? 42   LEU A C   1 
ATOM   321  O  O   . LEU A 1 42  ? 7.893  -18.521 23.583  1.00 11.79 ? 42   LEU A O   1 
ATOM   322  C  CB  . LEU A 1 42  ? 9.108  -19.354 26.242  1.00 12.14 ? 42   LEU A CB  1 
ATOM   323  C  CG  . LEU A 1 42  ? 9.693  -19.553 27.594  1.00 15.08 ? 42   LEU A CG  1 
ATOM   324  C  CD1 . LEU A 1 42  ? 8.600  -19.783 28.401  1.00 14.78 ? 42   LEU A CD1 1 
ATOM   325  C  CD2 . LEU A 1 42  ? 10.741 -20.692 27.678  1.00 14.84 ? 42   LEU A CD2 1 
ATOM   326  N  N   . HIS A 1 43  ? 9.249  -16.857 24.199  1.00 10.55 ? 43   HIS A N   1 
ATOM   327  C  CA  . HIS A 1 43  ? 9.633  -16.502 22.838  1.00 11.10 ? 43   HIS A CA  1 
ATOM   328  C  C   . HIS A 1 43  ? 11.143 -16.242 22.776  1.00 10.52 ? 43   HIS A C   1 
ATOM   329  O  O   . HIS A 1 43  ? 11.659 -15.423 23.547  1.00 10.99 ? 43   HIS A O   1 
ATOM   330  C  CB  . HIS A 1 43  ? 8.934  -15.220 22.408  1.00 10.79 ? 43   HIS A CB  1 
ATOM   331  C  CG  . HIS A 1 43  ? 7.464  -15.374 22.324  1.00 11.16 ? 43   HIS A CG  1 
ATOM   332  N  ND1 . HIS A 1 43  ? 6.833  -15.745 21.166  1.00 12.44 ? 43   HIS A ND1 1 
ATOM   333  C  CD2 . HIS A 1 43  ? 6.480  -15.293 23.257  1.00 12.52 ? 43   HIS A CD2 1 
ATOM   334  C  CE1 . HIS A 1 43  ? 5.518  -15.942 21.429  1.00 12.70 ? 43   HIS A CE1 1 
ATOM   335  N  NE2 . HIS A 1 43  ? 5.278  -15.586 22.655  1.00 12.66 ? 43   HIS A NE2 1 
ATOM   336  N  N   . GLY A 1 44  ? 11.827 -16.931 21.876  1.00 10.39 ? 44   GLY A N   1 
ATOM   337  C  CA  . GLY A 1 44  ? 13.276 -16.790 21.758  1.00 9.44  ? 44   GLY A CA  1 
ATOM   338  C  C   . GLY A 1 44  ? 13.635 -15.327 21.468  1.00 9.84  ? 44   GLY A C   1 
ATOM   339  O  O   . GLY A 1 44  ? 12.909 -14.613 20.789  1.00 10.31 ? 44   GLY A O   1 
ATOM   340  N  N   . PHE A 1 45  ? 14.809 -14.972 21.939  1.00 9.47  ? 45   PHE A N   1 
ATOM   341  C  CA  . PHE A 1 45  ? 15.207 -13.553 21.985  1.00 9.49  ? 45   PHE A CA  1 
ATOM   342  C  C   . PHE A 1 45  ? 16.721 -13.534 21.754  1.00 10.66 ? 45   PHE A C   1 
ATOM   343  O  O   . PHE A 1 45  ? 17.480 -13.927 22.628  1.00 10.73 ? 45   PHE A O   1 
ATOM   344  C  CB  . PHE A 1 45  ? 14.800 -12.998 23.339  1.00 10.51 ? 45   PHE A CB  1 
ATOM   345  C  CG  . PHE A 1 45  ? 15.007 -11.504 23.512  1.00 11.04 ? 45   PHE A CG  1 
ATOM   346  C  CD1 . PHE A 1 45  ? 14.289 -10.581 22.765  1.00 12.14 ? 45   PHE A CD1 1 
ATOM   347  C  CD2 . PHE A 1 45  ? 15.739 -11.035 24.534  1.00 11.88 ? 45   PHE A CD2 1 
ATOM   348  C  CE1 . PHE A 1 45  ? 14.370 -9.228  23.011  1.00 13.12 ? 45   PHE A CE1 1 
ATOM   349  C  CE2 . PHE A 1 45  ? 15.818 -9.681  24.795  1.00 14.07 ? 45   PHE A CE2 1 
ATOM   350  C  CZ  . PHE A 1 45  ? 15.148 -8.785  24.023  1.00 12.94 ? 45   PHE A CZ  1 
ATOM   351  N  N   . HIS A 1 46  ? 17.205 -13.056 20.560  1.00 9.09  ? 46   HIS A N   1 
ATOM   352  C  CA  . HIS A 1 46  ? 18.606 -13.097 20.254  1.00 8.54  ? 46   HIS A CA  1 
ATOM   353  C  C   . HIS A 1 46  ? 19.022 -11.889 19.466  1.00 8.36  ? 46   HIS A C   1 
ATOM   354  O  O   . HIS A 1 46  ? 18.244 -11.318 18.704  1.00 9.67  ? 46   HIS A O   1 
ATOM   355  C  CB  . HIS A 1 46  ? 18.974 -14.333 19.399  1.00 10.57 ? 46   HIS A CB  1 
ATOM   356  C  CG  . HIS A 1 46  ? 18.195 -15.574 19.730  1.00 10.34 ? 46   HIS A CG  1 
ATOM   357  N  ND1 . HIS A 1 46  ? 17.234 -16.002 18.841  1.00 10.84 ? 46   HIS A ND1 1 
ATOM   358  C  CD2 . HIS A 1 46  ? 18.145 -16.404 20.826  1.00 13.70 ? 46   HIS A CD2 1 
ATOM   359  C  CE1 . HIS A 1 46  ? 16.663 -17.093 19.375  1.00 11.79 ? 46   HIS A CE1 1 
ATOM   360  N  NE2 . HIS A 1 46  ? 17.185 -17.355 20.568  1.00 12.11 ? 46   HIS A NE2 1 
ATOM   361  N  N   . VAL A 1 47  ? 20.341 -11.671 19.507  1.00 8.07  ? 47   VAL A N   1 
ATOM   362  C  CA  . VAL A 1 47  ? 20.986 -10.763 18.572  1.00 8.73  ? 47   VAL A CA  1 
ATOM   363  C  C   . VAL A 1 47  ? 21.485 -11.623 17.354  1.00 8.73  ? 47   VAL A C   1 
ATOM   364  O  O   . VAL A 1 47  ? 22.214 -12.592 17.559  1.00 9.58  ? 47   VAL A O   1 
ATOM   365  C  CB  . VAL A 1 47  ? 22.156 -10.028 19.180  1.00 8.77  ? 47   VAL A CB  1 
ATOM   366  C  CG1 . VAL A 1 47  ? 22.758 -9.048  18.175  1.00 9.88  ? 47   VAL A CG1 1 
ATOM   367  C  CG2 . VAL A 1 47  ? 21.686 -9.223  20.428  1.00 10.97 ? 47   VAL A CG2 1 
ATOM   368  N  N   . HIS A 1 48  ? 21.066 -11.212 16.158  1.00 9.41  ? 48   HIS A N   1 
ATOM   369  C  CA  . HIS A 1 48  ? 21.477 -11.819 14.909  1.00 8.96  ? 48   HIS A CA  1 
ATOM   370  C  C   . HIS A 1 48  ? 22.591 -11.030 14.252  1.00 9.68  ? 48   HIS A C   1 
ATOM   371  O  O   . HIS A 1 48  ? 22.772 -9.847  14.551  1.00 11.38 ? 48   HIS A O   1 
ATOM   372  C  CB  . HIS A 1 48  ? 20.243 -11.974 13.990  1.00 10.20 ? 48   HIS A CB  1 
ATOM   373  C  CG  . HIS A 1 48  ? 19.310 -13.038 14.457  1.00 10.43 ? 48   HIS A CG  1 
ATOM   374  N  ND1 . HIS A 1 48  ? 18.964 -14.119 13.671  1.00 10.50 ? 48   HIS A ND1 1 
ATOM   375  C  CD2 . HIS A 1 48  ? 18.660 -13.178 15.630  1.00 10.60 ? 48   HIS A CD2 1 
ATOM   376  C  CE1 . HIS A 1 48  ? 18.136 -14.892 14.367  1.00 10.44 ? 48   HIS A CE1 1 
ATOM   377  N  NE2 . HIS A 1 48  ? 17.934 -14.337 15.568  1.00 9.14  ? 48   HIS A NE2 1 
ATOM   378  N  N   . GLU A 1 49  ? 23.315 -11.649 13.343  1.00 9.30  ? 49   GLU A N   1 
ATOM   379  C  CA  . GLU A 1 49  ? 24.561 -11.125 12.922  1.00 9.88  ? 49   GLU A CA  1 
ATOM   380  C  C   . GLU A 1 49  ? 24.457 -9.771  12.194  1.00 10.78 ? 49   GLU A C   1 
ATOM   381  O  O   . GLU A 1 49  ? 25.298 -8.873  12.448  1.00 13.10 ? 49   GLU A O   1 
ATOM   382  C  CB  . GLU A 1 49  ? 25.256 -12.164 12.048  1.00 11.15 ? 49   GLU A CB  1 
ATOM   383  C  CG  A GLU A 1 49  ? 26.675 -11.734 11.793  0.70 14.30 ? 49   GLU A CG  1 
ATOM   384  C  CG  B GLU A 1 49  ? 26.566 -11.795 11.414  0.30 10.72 ? 49   GLU A CG  1 
ATOM   385  C  CD  A GLU A 1 49  ? 27.427 -12.730 11.005  0.70 13.43 ? 49   GLU A CD  1 
ATOM   386  C  CD  B GLU A 1 49  ? 27.097 -12.841 10.460  0.30 10.91 ? 49   GLU A CD  1 
ATOM   387  O  OE1 A GLU A 1 49  ? 26.861 -13.740 10.544  0.70 15.84 ? 49   GLU A OE1 1 
ATOM   388  O  OE1 B GLU A 1 49  ? 26.387 -13.809 10.125  0.30 14.33 ? 49   GLU A OE1 1 
ATOM   389  O  OE2 A GLU A 1 49  ? 28.603 -12.460 10.722  0.70 15.38 ? 49   GLU A OE2 1 
ATOM   390  O  OE2 B GLU A 1 49  ? 28.252 -12.657 10.024  0.30 14.13 ? 49   GLU A OE2 1 
ATOM   391  N  N   . PHE A 1 50  ? 23.497 -9.672  11.271  1.00 9.66  ? 50   PHE A N   1 
ATOM   392  C  CA  . PHE A 1 50  ? 23.481 -8.517  10.370  1.00 9.78  ? 50   PHE A CA  1 
ATOM   393  C  C   . PHE A 1 50  ? 22.368 -7.589  10.758  1.00 8.79  ? 50   PHE A C   1 
ATOM   394  O  O   . PHE A 1 50  ? 21.234 -7.997  11.062  1.00 10.05 ? 50   PHE A O   1 
ATOM   395  C  CB  . PHE A 1 50  ? 23.290 -8.978  8.956   1.00 11.16 ? 50   PHE A CB  1 
ATOM   396  C  CG  A PHE A 1 50  ? 24.202 -10.029 8.457   0.80 13.44 ? 50   PHE A CG  1 
ATOM   397  C  CG  B PHE A 1 50  ? 24.626 -9.696  8.555   0.20 12.06 ? 50   PHE A CG  1 
ATOM   398  C  CD1 A PHE A 1 50  ? 25.557 -9.872  8.456   0.80 14.93 ? 50   PHE A CD1 1 
ATOM   399  C  CD1 B PHE A 1 50  ? 25.825 -8.960  8.606   0.20 7.77  ? 50   PHE A CD1 1 
ATOM   400  C  CD2 A PHE A 1 50  ? 23.661 -11.236 8.034   0.80 13.87 ? 50   PHE A CD2 1 
ATOM   401  C  CD2 B PHE A 1 50  ? 24.761 -11.085 8.479   0.20 8.37  ? 50   PHE A CD2 1 
ATOM   402  C  CE1 A PHE A 1 50  ? 26.367 -10.927 8.004   0.80 17.76 ? 50   PHE A CE1 1 
ATOM   403  C  CE1 B PHE A 1 50  ? 27.060 -9.567  8.404   0.20 7.74  ? 50   PHE A CE1 1 
ATOM   404  C  CE2 A PHE A 1 50  ? 24.460 -12.241 7.602   0.80 15.23 ? 50   PHE A CE2 1 
ATOM   405  C  CE2 B PHE A 1 50  ? 26.024 -11.688 8.245   0.20 8.59  ? 50   PHE A CE2 1 
ATOM   406  C  CZ  A PHE A 1 50  ? 25.775 -12.088 7.610   0.80 17.50 ? 50   PHE A CZ  1 
ATOM   407  C  CZ  B PHE A 1 50  ? 27.169 -10.916 8.213   0.20 9.41  ? 50   PHE A CZ  1 
ATOM   408  N  N   . GLY A 1 51  ? 22.629 -6.298  10.753  1.00 9.24  ? 51   GLY A N   1 
ATOM   409  C  CA  . GLY A 1 51  ? 21.667 -5.209  10.842  1.00 9.77  ? 51   GLY A CA  1 
ATOM   410  C  C   . GLY A 1 51  ? 20.991 -4.892  9.568   1.00 10.14 ? 51   GLY A C   1 
ATOM   411  O  O   . GLY A 1 51  ? 20.897 -3.727  9.161   1.00 10.62 ? 51   GLY A O   1 
ATOM   412  N  N   . ASP A 1 52  ? 20.532 -5.943  8.864   1.00 11.36 ? 52   ASP A N   1 
ATOM   413  C  CA  . ASP A 1 52  ? 19.998 -5.864  7.524   1.00 10.54 ? 52   ASP A CA  1 
ATOM   414  C  C   . ASP A 1 52  ? 18.555 -6.298  7.579   1.00 10.51 ? 52   ASP A C   1 
ATOM   415  O  O   . ASP A 1 52  ? 18.271 -7.473  7.898   1.00 12.01 ? 52   ASP A O   1 
ATOM   416  C  CB  . ASP A 1 52  ? 20.782 -6.791  6.595   1.00 12.23 ? 52   ASP A CB  1 
ATOM   417  C  CG  . ASP A 1 52  ? 20.390 -6.611  5.155   1.00 13.29 ? 52   ASP A CG  1 
ATOM   418  O  OD1 . ASP A 1 52  ? 19.301 -6.056  4.895   1.00 14.12 ? 52   ASP A OD1 1 
ATOM   419  O  OD2 . ASP A 1 52  ? 21.172 -7.078  4.278   1.00 16.07 ? 52   ASP A OD2 1 
ATOM   420  N  N   . ASN A 1 53  ? 17.639 -5.373  7.351   1.00 11.10 ? 53   ASN A N   1 
ATOM   421  C  CA  . ASN A 1 53  ? 16.217 -5.662  7.299   1.00 11.55 ? 53   ASN A CA  1 
ATOM   422  C  C   . ASN A 1 53  ? 15.614 -5.434  5.894   1.00 11.12 ? 53   ASN A C   1 
ATOM   423  O  O   . ASN A 1 53  ? 14.419 -5.232  5.755   1.00 12.92 ? 53   ASN A O   1 
ATOM   424  C  CB  . ASN A 1 53  ? 15.502 -4.861  8.419   1.00 14.45 ? 53   ASN A CB  1 
ATOM   425  C  CG  A ASN A 1 53  ? 14.013 -5.223  8.636   0.70 15.97 ? 53   ASN A CG  1 
ATOM   426  C  CG  B ASN A 1 53  ? 15.896 -5.423  9.946   0.30 8.67  ? 53   ASN A CG  1 
ATOM   427  O  OD1 A ASN A 1 53  ? 13.070 -4.382  8.581   0.70 25.80 ? 53   ASN A OD1 1 
ATOM   428  O  OD1 B ASN A 1 53  ? 16.636 -6.431  10.161  0.30 10.92 ? 53   ASN A OD1 1 
ATOM   429  N  ND2 A ASN A 1 53  ? 13.837 -6.442  8.886   0.70 16.20 ? 53   ASN A ND2 1 
ATOM   430  N  ND2 B ASN A 1 53  ? 15.522 -4.681  10.911  0.30 9.12  ? 53   ASN A ND2 1 
ATOM   431  N  N   . THR A 1 54  ? 16.456 -5.599  4.896   1.00 12.56 ? 54   THR A N   1 
ATOM   432  C  CA  . THR A 1 54  ? 16.109 -5.352  3.490   1.00 13.41 ? 54   THR A CA  1 
ATOM   433  C  C   . THR A 1 54  ? 14.814 -6.050  3.142   1.00 14.54 ? 54   THR A C   1 
ATOM   434  O  O   . THR A 1 54  ? 13.860 -5.454  2.571   1.00 15.14 ? 54   THR A O   1 
ATOM   435  C  CB  . THR A 1 54  ? 17.237 -5.834  2.521   1.00 13.79 ? 54   THR A CB  1 
ATOM   436  O  OG1 . THR A 1 54  ? 18.361 -4.979  2.697   1.00 18.36 ? 54   THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 54  ? 16.750 -5.669  1.080   1.00 17.48 ? 54   THR A CG2 1 
ATOM   438  N  N   . ALA A 1 55  ? 14.759 -7.322  3.446   1.00 13.07 ? 55   ALA A N   1 
ATOM   439  C  CA  . ALA A 1 55  ? 13.566 -8.099  3.100   1.00 13.71 ? 55   ALA A CA  1 
ATOM   440  C  C   . ALA A 1 55  ? 12.838 -8.550  4.366   1.00 14.28 ? 55   ALA A C   1 
ATOM   441  O  O   . ALA A 1 55  ? 12.195 -9.580  4.391   1.00 18.70 ? 55   ALA A O   1 
ATOM   442  C  CB  . ALA A 1 55  ? 13.961 -9.291  2.257   1.00 16.28 ? 55   ALA A CB  1 
ATOM   443  N  N   . GLY A 1 56  ? 12.864 -7.750  5.418   1.00 15.05 ? 56   GLY A N   1 
ATOM   444  C  CA  . GLY A 1 56  ? 12.344 -8.098  6.714   1.00 13.55 ? 56   GLY A CA  1 
ATOM   445  C  C   . GLY A 1 56  ? 13.346 -8.812  7.609   1.00 11.98 ? 56   GLY A C   1 
ATOM   446  O  O   . GLY A 1 56  ? 14.557 -8.790  7.341   1.00 12.43 ? 56   GLY A O   1 
ATOM   447  N  N   . CYS A 1 57  ? 12.878 -9.444  8.682   1.00 12.03 ? 57   CYS A N   1 
ATOM   448  C  CA  . CYS A 1 57  ? 13.780 -10.003 9.704   1.00 12.41 ? 57   CYS A CA  1 
ATOM   449  C  C   . CYS A 1 57  ? 14.591 -11.162 9.252   1.00 11.40 ? 57   CYS A C   1 
ATOM   450  O  O   . CYS A 1 57  ? 15.663 -11.426 9.814   1.00 12.14 ? 57   CYS A O   1 
ATOM   451  C  CB  . CYS A 1 57  ? 12.956 -10.420 10.940  1.00 13.93 ? 57   CYS A CB  1 
ATOM   452  S  SG  . CYS A 1 57  ? 11.966 -9.089  11.663  1.00 13.91 ? 57   CYS A SG  1 
ATOM   453  N  N   . THR A 1 58  ? 14.176 -11.784 8.149   1.00 12.25 ? 58   THR A N   1 
ATOM   454  C  CA  . THR A 1 58  ? 14.948 -12.873 7.621   1.00 12.74 ? 58   THR A CA  1 
ATOM   455  C  C   . THR A 1 58  ? 16.349 -12.403 7.179   1.00 11.83 ? 58   THR A C   1 
ATOM   456  O  O   . THR A 1 58  ? 17.350 -13.126 7.197   1.00 13.36 ? 58   THR A O   1 
ATOM   457  C  CB  A THR A 1 58  ? 14.196 -13.490 6.471   0.50 14.25 ? 58   THR A CB  1 
ATOM   458  C  CB  B THR A 1 58  ? 14.255 -13.513 6.401   0.50 16.06 ? 58   THR A CB  1 
ATOM   459  O  OG1 A THR A 1 58  ? 14.994 -14.525 5.899   0.50 24.70 ? 58   THR A OG1 1 
ATOM   460  O  OG1 B THR A 1 58  ? 13.010 -14.115 6.771   0.50 15.88 ? 58   THR A OG1 1 
ATOM   461  C  CG2 A THR A 1 58  ? 13.847 -12.452 5.397   0.50 9.23  ? 58   THR A CG2 1 
ATOM   462  C  CG2 B THR A 1 58  ? 15.078 -14.619 5.866   0.50 18.98 ? 58   THR A CG2 1 
ATOM   463  N  N   . SER A 1 59  ? 16.465 -11.141 6.697   1.00 11.81 ? 59   SER A N   1 
ATOM   464  C  CA  . SER A 1 59  ? 17.719 -10.594 6.185   1.00 11.00 ? 59   SER A CA  1 
ATOM   465  C  C   . SER A 1 59  ? 18.816 -10.465 7.220   1.00 9.97  ? 59   SER A C   1 
ATOM   466  O  O   . SER A 1 59  ? 19.965 -10.302 6.917   1.00 10.74 ? 59   SER A O   1 
ATOM   467  C  CB  . SER A 1 59  ? 17.473 -9.238  5.468   1.00 12.87 ? 59   SER A CB  1 
ATOM   468  O  OG  . SER A 1 59  ? 16.563 -9.348  4.367   1.00 13.69 ? 59   SER A OG  1 
ATOM   469  N  N   . ALA A 1 60  ? 18.473 -10.604 8.512   1.00 10.90 ? 60   ALA A N   1 
ATOM   470  C  CA  . ALA A 1 60  ? 19.420 -10.452 9.595   1.00 10.72 ? 60   ALA A CA  1 
ATOM   471  C  C   . ALA A 1 60  ? 20.341 -11.644 9.750   1.00 11.20 ? 60   ALA A C   1 
ATOM   472  O  O   . ALA A 1 60  ? 21.372 -11.596 10.452  1.00 10.73 ? 60   ALA A O   1 
ATOM   473  C  CB  . ALA A 1 60  ? 18.680 -10.281 10.922  1.00 11.16 ? 60   ALA A CB  1 
ATOM   474  N  N   . GLY A 1 61  ? 20.045 -12.728 9.072   1.00 10.06 ? 61   GLY A N   1 
ATOM   475  C  CA  . GLY A 1 61  ? 21.027 -13.865 9.069   1.00 11.37 ? 61   GLY A CA  1 
ATOM   476  C  C   . GLY A 1 61  ? 20.897 -14.668 10.384  1.00 10.74 ? 61   GLY A C   1 
ATOM   477  O  O   . GLY A 1 61  ? 19.869 -14.599 11.118  1.00 10.10 ? 61   GLY A O   1 
ATOM   478  N  N   . PRO A 1 62  ? 21.941 -15.461 10.684  1.00 10.78 ? 62   PRO A N   1 
ATOM   479  C  CA  . PRO A 1 62  ? 21.938 -16.315 11.830  1.00 10.08 ? 62   PRO A CA  1 
ATOM   480  C  C   . PRO A 1 62  ? 22.263 -15.565 13.128  1.00 10.49 ? 62   PRO A C   1 
ATOM   481  O  O   . PRO A 1 62  ? 22.443 -14.374 13.172  1.00 9.99  ? 62   PRO A O   1 
ATOM   482  C  CB  . PRO A 1 62  ? 23.043 -17.309 11.444  1.00 12.40 ? 62   PRO A CB  1 
ATOM   483  C  CG  . PRO A 1 62  ? 24.001 -16.495 10.747  1.00 12.00 ? 62   PRO A CG  1 
ATOM   484  C  CD  . PRO A 1 62  ? 23.212 -15.502 9.922   1.00 12.10 ? 62   PRO A CD  1 
ATOM   485  N  N   . HIS A 1 63  ? 22.266 -16.296 14.240  1.00 9.72  ? 63   HIS A N   1 
ATOM   486  C  CA  . HIS A 1 63  ? 22.614 -15.711 15.547  1.00 9.46  ? 63   HIS A CA  1 
ATOM   487  C  C   . HIS A 1 63  ? 24.007 -15.120 15.464  1.00 9.59  ? 63   HIS A C   1 
ATOM   488  O  O   . HIS A 1 63  ? 24.904 -15.681 14.853  1.00 10.96 ? 63   HIS A O   1 
ATOM   489  C  CB  . HIS A 1 63  ? 22.524 -16.727 16.658  1.00 10.95 ? 63   HIS A CB  1 
ATOM   490  C  CG  . HIS A 1 63  ? 21.150 -17.241 16.892  1.00 10.93 ? 63   HIS A CG  1 
ATOM   491  N  ND1 . HIS A 1 63  ? 20.884 -18.183 17.876  1.00 10.79 ? 63   HIS A ND1 1 
ATOM   492  C  CD2 . HIS A 1 63  ? 19.977 -17.022 16.239  1.00 13.33 ? 63   HIS A CD2 1 
ATOM   493  C  CE1 . HIS A 1 63  ? 19.579 -18.475 17.817  1.00 11.90 ? 63   HIS A CE1 1 
ATOM   494  N  NE2 . HIS A 1 63  ? 19.016 -17.839 16.800  1.00 13.13 ? 63   HIS A NE2 1 
ATOM   495  N  N   . PHE A 1 64  ? 24.230 -13.993 16.134  1.00 9.84  ? 64   PHE A N   1 
ATOM   496  C  CA  . PHE A 1 64  ? 25.545 -13.402 16.178  1.00 10.14 ? 64   PHE A CA  1 
ATOM   497  C  C   . PHE A 1 64  ? 26.484 -14.310 16.975  1.00 9.85  ? 64   PHE A C   1 
ATOM   498  O  O   . PHE A 1 64  ? 26.283 -14.615 18.146  1.00 10.04 ? 64   PHE A O   1 
ATOM   499  C  CB  . PHE A 1 64  ? 25.426 -12.030 16.888  1.00 10.70 ? 64   PHE A CB  1 
ATOM   500  C  CG  . PHE A 1 64  ? 26.768 -11.298 16.998  1.00 11.01 ? 64   PHE A CG  1 
ATOM   501  C  CD1 . PHE A 1 64  ? 27.687 -11.141 15.981  1.00 12.79 ? 64   PHE A CD1 1 
ATOM   502  C  CD2 . PHE A 1 64  ? 27.001 -10.658 18.222  1.00 12.96 ? 64   PHE A CD2 1 
ATOM   503  C  CE1 . PHE A 1 64  ? 28.919 -10.454 16.186  1.00 14.76 ? 64   PHE A CE1 1 
ATOM   504  C  CE2 . PHE A 1 64  ? 28.191 -9.945  18.385  1.00 13.50 ? 64   PHE A CE2 1 
ATOM   505  C  CZ  . PHE A 1 64  ? 29.119 -9.867  17.411  1.00 15.49 ? 64   PHE A CZ  1 
ATOM   506  N  N   . ASN A 1 65  ? 27.538 -14.770 16.311  1.00 11.59 ? 65   ASN A N   1 
ATOM   507  C  CA  . ASN A 1 65  ? 28.329 -15.898 16.799  1.00 12.26 ? 65   ASN A CA  1 
ATOM   508  C  C   . ASN A 1 65  ? 29.814 -15.717 16.392  1.00 13.96 ? 65   ASN A C   1 
ATOM   509  O  O   . ASN A 1 65  ? 30.421 -16.568 15.689  1.00 14.73 ? 65   ASN A O   1 
ATOM   510  C  CB  . ASN A 1 65  ? 27.784 -17.226 16.255  1.00 12.72 ? 65   ASN A CB  1 
ATOM   511  C  CG  . ASN A 1 65  ? 28.526 -18.470 16.825  1.00 13.03 ? 65   ASN A CG  1 
ATOM   512  O  OD1 . ASN A 1 65  ? 29.089 -18.418 17.927  1.00 13.37 ? 65   ASN A OD1 1 
ATOM   513  N  ND2 . ASN A 1 65  ? 28.421 -19.592 16.107  1.00 14.83 ? 65   ASN A ND2 1 
ATOM   514  N  N   . PRO A 1 66  ? 30.446 -14.612 16.848  1.00 12.34 ? 66   PRO A N   1 
ATOM   515  C  CA  . PRO A 1 66  ? 31.812 -14.328 16.406  1.00 14.41 ? 66   PRO A CA  1 
ATOM   516  C  C   . PRO A 1 66  ? 32.792 -15.404 16.877  1.00 15.72 ? 66   PRO A C   1 
ATOM   517  O  O   . PRO A 1 66  ? 33.860 -15.490 16.303  1.00 19.14 ? 66   PRO A O   1 
ATOM   518  C  CB  . PRO A 1 66  ? 32.109 -12.955 17.000  1.00 15.78 ? 66   PRO A CB  1 
ATOM   519  C  CG  . PRO A 1 66  ? 31.200 -12.914 18.272  1.00 15.68 ? 66   PRO A CG  1 
ATOM   520  C  CD  . PRO A 1 66  ? 29.921 -13.590 17.808  1.00 13.82 ? 66   PRO A CD  1 
ATOM   521  N  N   . LEU A 1 67  ? 32.490 -16.124 17.986  1.00 13.92 ? 67   LEU A N   1 
ATOM   522  C  CA  . LEU A 1 67  ? 33.416 -17.162 18.513  1.00 15.67 ? 67   LEU A CA  1 
ATOM   523  C  C   . LEU A 1 67  ? 33.075 -18.584 18.068  1.00 17.12 ? 67   LEU A C   1 
ATOM   524  O  O   . LEU A 1 67  ? 33.749 -19.563 18.519  1.00 19.49 ? 67   LEU A O   1 
ATOM   525  C  CB  . LEU A 1 67  ? 33.390 -17.098 20.032  1.00 15.62 ? 67   LEU A CB  1 
ATOM   526  C  CG  . LEU A 1 67  ? 33.922 -15.798 20.592  1.00 18.23 ? 67   LEU A CG  1 
ATOM   527  C  CD1 . LEU A 1 67  ? 33.673 -15.699 22.069  1.00 20.21 ? 67   LEU A CD1 1 
ATOM   528  C  CD2 . LEU A 1 67  ? 35.445 -15.829 20.421  1.00 21.09 ? 67   LEU A CD2 1 
ATOM   529  N  N   . SER A 1 68  ? 32.223 -18.747 17.061  1.00 16.63 ? 68   SER A N   1 
ATOM   530  C  CA  . SER A 1 68  ? 31.954 -20.078 16.472  1.00 16.32 ? 68   SER A CA  1 
ATOM   531  C  C   . SER A 1 68  ? 31.627 -21.151 17.529  1.00 14.88 ? 68   SER A C   1 
ATOM   532  O  O   . SER A 1 68  ? 32.151 -22.237 17.450  1.00 20.50 ? 68   SER A O   1 
ATOM   533  C  CB  . SER A 1 68  ? 33.085 -20.522 15.582  1.00 18.12 ? 68   SER A CB  1 
ATOM   534  O  OG  . SER A 1 68  ? 33.374 -19.560 14.572  1.00 20.96 ? 68   SER A OG  1 
ATOM   535  N  N   . ARG A 1 69  ? 30.708 -20.839 18.424  1.00 15.36 ? 69   ARG A N   1 
ATOM   536  C  CA  . ARG A 1 69  ? 30.257 -21.763 19.460  1.00 14.50 ? 69   ARG A CA  1 
ATOM   537  C  C   . ARG A 1 69  ? 28.907 -22.319 18.987  1.00 14.84 ? 69   ARG A C   1 
ATOM   538  O  O   . ARG A 1 69  ? 28.298 -21.849 17.983  1.00 16.52 ? 69   ARG A O   1 
ATOM   539  C  CB  . ARG A 1 69  ? 30.048 -21.034 20.806  1.00 16.04 ? 69   ARG A CB  1 
ATOM   540  C  CG  . ARG A 1 69  ? 31.322 -20.352 21.324  1.00 18.21 ? 69   ARG A CG  1 
ATOM   541  C  CD  . ARG A 1 69  ? 32.497 -21.311 21.568  1.00 26.73 ? 69   ARG A CD  1 
ATOM   542  N  NE  . ARG A 1 69  ? 33.283 -20.860 22.717  0.20 29.17 ? 69   ARG A NE  1 
ATOM   543  C  CZ  . ARG A 1 69  ? 32.922 -21.002 23.993  0.20 34.15 ? 69   ARG A CZ  1 
ATOM   544  N  NH1 . ARG A 1 69  ? 31.780 -21.593 24.318  0.20 38.82 ? 69   ARG A NH1 1 
ATOM   545  N  NH2 . ARG A 1 69  ? 33.708 -20.545 24.956  0.20 33.22 ? 69   ARG A NH2 1 
ATOM   546  N  N   . LYS A 1 70  ? 28.374 -23.297 19.710  1.00 15.22 ? 70   LYS A N   1 
ATOM   547  C  CA  . LYS A 1 70  ? 27.016 -23.784 19.534  1.00 15.51 ? 70   LYS A CA  1 
ATOM   548  C  C   . LYS A 1 70  ? 26.027 -22.940 20.274  1.00 14.60 ? 70   LYS A C   1 
ATOM   549  O  O   . LYS A 1 70  ? 26.357 -22.204 21.211  1.00 14.83 ? 70   LYS A O   1 
ATOM   550  C  CB  . LYS A 1 70  ? 26.878 -25.233 20.025  1.00 16.24 ? 70   LYS A CB  1 
ATOM   551  C  CG  . LYS A 1 70  ? 27.760 -26.258 19.212  1.00 22.09 ? 70   LYS A CG  1 
ATOM   552  C  CD  . LYS A 1 70  ? 27.669 -26.153 17.697  0.50 20.73 ? 70   LYS A CD  1 
ATOM   553  C  CE  . LYS A 1 70  ? 28.705 -26.996 16.956  0.50 23.34 ? 70   LYS A CE  1 
ATOM   554  N  NZ  . LYS A 1 70  ? 29.380 -26.167 15.927  0.50 24.80 ? 70   LYS A NZ  1 
ATOM   555  N  N   . HIS A 1 71  ? 24.780 -23.030 19.819  1.00 13.21 ? 71   HIS A N   1 
ATOM   556  C  CA  . HIS A 1 71  ? 23.704 -22.319 20.482  1.00 11.95 ? 71   HIS A CA  1 
ATOM   557  C  C   . HIS A 1 71  ? 23.548 -22.762 21.932  1.00 12.34 ? 71   HIS A C   1 
ATOM   558  O  O   . HIS A 1 71  ? 23.583 -23.974 22.221  1.00 14.62 ? 71   HIS A O   1 
ATOM   559  C  CB  . HIS A 1 71  ? 22.402 -22.505 19.701  1.00 12.09 ? 71   HIS A CB  1 
ATOM   560  C  CG  . HIS A 1 71  ? 21.243 -21.786 20.267  1.00 11.43 ? 71   HIS A CG  1 
ATOM   561  N  ND1 . HIS A 1 71  ? 21.076 -20.410 20.155  1.00 11.02 ? 71   HIS A ND1 1 
ATOM   562  C  CD2 . HIS A 1 71  ? 20.227 -22.252 21.025  1.00 11.08 ? 71   HIS A CD2 1 
ATOM   563  C  CE1 . HIS A 1 71  ? 19.939 -20.109 20.826  1.00 11.25 ? 71   HIS A CE1 1 
ATOM   564  N  NE2 . HIS A 1 71  ? 19.434 -21.196 21.366  1.00 10.87 ? 71   HIS A NE2 1 
ATOM   565  N  N   . GLY A 1 72  ? 23.219 -21.854 22.849  1.00 11.45 ? 72   GLY A N   1 
ATOM   566  C  CA  . GLY A 1 72  ? 22.884 -22.131 24.260  1.00 11.41 ? 72   GLY A CA  1 
ATOM   567  C  C   . GLY A 1 72  ? 21.970 -21.075 24.838  1.00 11.38 ? 72   GLY A C   1 
ATOM   568  O  O   . GLY A 1 72  ? 21.414 -20.218 24.119  1.00 12.78 ? 72   GLY A O   1 
ATOM   569  N  N   . GLY A 1 73  ? 21.798 -21.133 26.164  1.00 11.57 ? 73   GLY A N   1 
ATOM   570  C  CA  . GLY A 1 73  ? 21.134 -20.071 26.886  1.00 12.42 ? 73   GLY A CA  1 
ATOM   571  C  C   . GLY A 1 73  ? 22.134 -19.044 27.383  1.00 11.20 ? 73   GLY A C   1 
ATOM   572  O  O   . GLY A 1 73  ? 23.355 -19.301 27.428  1.00 11.34 ? 73   GLY A O   1 
ATOM   573  N  N   . PRO A 1 74  ? 21.609 -17.934 27.884  1.00 11.29 ? 74   PRO A N   1 
ATOM   574  C  CA  . PRO A 1 74  ? 22.455 -16.879 28.315  1.00 12.54 ? 74   PRO A CA  1 
ATOM   575  C  C   . PRO A 1 74  ? 23.310 -17.217 29.516  1.00 12.75 ? 74   PRO A C   1 
ATOM   576  O  O   . PRO A 1 74  ? 24.429 -16.672 29.589  1.00 14.34 ? 74   PRO A O   1 
ATOM   577  C  CB  . PRO A 1 74  ? 21.506 -15.717 28.592  1.00 12.56 ? 74   PRO A CB  1 
ATOM   578  C  CG  . PRO A 1 74  ? 20.167 -16.347 28.889  1.00 15.26 ? 74   PRO A CG  1 
ATOM   579  C  CD  . PRO A 1 74  ? 20.205 -17.530 27.925  1.00 11.75 ? 74   PRO A CD  1 
ATOM   580  N  N   . LYS A 1 75  ? 22.914 -18.182 30.331  1.00 12.46 ? 75   LYS A N   1 
ATOM   581  C  CA  A LYS A 1 75  ? 23.767 -18.552 31.447  0.50 13.37 ? 75   LYS A CA  1 
ATOM   582  C  CA  B LYS A 1 75  ? 23.681 -18.674 31.480  0.50 12.65 ? 75   LYS A CA  1 
ATOM   583  C  C   . LYS A 1 75  ? 24.659 -19.756 31.167  1.00 13.06 ? 75   LYS A C   1 
ATOM   584  O  O   . LYS A 1 75  ? 25.226 -20.292 32.083  1.00 16.18 ? 75   LYS A O   1 
ATOM   585  C  CB  A LYS A 1 75  ? 22.911 -18.688 32.717  0.50 16.04 ? 75   LYS A CB  1 
ATOM   586  C  CB  B LYS A 1 75  ? 22.743 -19.292 32.543  0.50 13.41 ? 75   LYS A CB  1 
ATOM   587  C  CG  A LYS A 1 75  ? 22.051 -17.415 32.931  0.50 18.25 ? 75   LYS A CG  1 
ATOM   588  C  CG  B LYS A 1 75  ? 21.774 -18.285 33.083  0.50 14.30 ? 75   LYS A CG  1 
ATOM   589  C  CD  A LYS A 1 75  ? 22.931 -16.175 33.026  0.50 22.33 ? 75   LYS A CD  1 
ATOM   590  C  CD  B LYS A 1 75  ? 21.192 -18.706 34.406  0.50 17.39 ? 75   LYS A CD  1 
ATOM   591  C  CE  A LYS A 1 75  ? 22.283 -14.957 32.451  0.50 21.31 ? 75   LYS A CE  1 
ATOM   592  C  CE  B LYS A 1 75  ? 20.125 -19.689 34.155  0.50 21.16 ? 75   LYS A CE  1 
ATOM   593  N  NZ  A LYS A 1 75  ? 22.887 -13.727 32.969  0.50 21.91 ? 75   LYS A NZ  1 
ATOM   594  N  NZ  B LYS A 1 75  ? 19.298 -19.951 35.358  0.50 25.43 ? 75   LYS A NZ  1 
ATOM   595  N  N   . ASP A 1 76  ? 24.788 -20.166 29.916  1.00 12.34 ? 76   ASP A N   1 
ATOM   596  C  CA  . ASP A 1 76  ? 25.674 -21.229 29.525  1.00 11.87 ? 76   ASP A CA  1 
ATOM   597  C  C   . ASP A 1 76  ? 27.015 -20.684 29.062  1.00 12.19 ? 76   ASP A C   1 
ATOM   598  O  O   . ASP A 1 76  ? 27.104 -19.602 28.409  1.00 14.38 ? 76   ASP A O   1 
ATOM   599  C  CB  . ASP A 1 76  ? 25.056 -22.074 28.416  1.00 14.68 ? 76   ASP A CB  1 
ATOM   600  C  CG  . ASP A 1 76  ? 23.773 -22.756 28.862  1.00 14.67 ? 76   ASP A CG  1 
ATOM   601  O  OD1 . ASP A 1 76  ? 23.597 -23.024 30.077  1.00 19.52 ? 76   ASP A OD1 1 
ATOM   602  O  OD2 . ASP A 1 76  ? 22.929 -22.989 27.993  1.00 15.91 ? 76   ASP A OD2 1 
ATOM   603  N  N   . GLU A 1 77  ? 28.097 -21.441 29.274  1.00 12.53 ? 77   GLU A N   1 
ATOM   604  C  CA  . GLU A 1 77  ? 29.380 -21.104 28.678  1.00 13.08 ? 77   GLU A CA  1 
ATOM   605  C  C   . GLU A 1 77  ? 29.352 -21.308 27.165  1.00 12.62 ? 77   GLU A C   1 
ATOM   606  O  O   . GLU A 1 77  ? 29.827 -20.462 26.399  1.00 14.35 ? 77   GLU A O   1 
ATOM   607  C  CB  . GLU A 1 77  ? 30.494 -21.966 29.293  1.00 13.82 ? 77   GLU A CB  1 
ATOM   608  C  CG  A GLU A 1 77  ? 31.841 -21.632 28.685  0.75 16.95 ? 77   GLU A CG  1 
ATOM   609  C  CG  B GLU A 1 77  ? 31.949 -21.544 28.927  0.25 13.70 ? 77   GLU A CG  1 
ATOM   610  C  CD  A GLU A 1 77  ? 33.013 -22.178 29.432  0.75 20.86 ? 77   GLU A CD  1 
ATOM   611  C  CD  B GLU A 1 77  ? 32.431 -21.990 27.548  0.25 13.19 ? 77   GLU A CD  1 
ATOM   612  O  OE1 A GLU A 1 77  ? 33.003 -23.338 29.874  0.75 21.24 ? 77   GLU A OE1 1 
ATOM   613  O  OE1 B GLU A 1 77  ? 31.961 -23.039 27.060  0.25 14.03 ? 77   GLU A OE1 1 
ATOM   614  O  OE2 A GLU A 1 77  ? 34.018 -21.453 29.479  0.75 23.76 ? 77   GLU A OE2 1 
ATOM   615  O  OE2 B GLU A 1 77  ? 33.289 -21.284 26.949  0.25 19.43 ? 77   GLU A OE2 1 
ATOM   616  N  N   . GLU A 1 78  ? 28.774 -22.419 26.743  1.00 12.62 ? 78   GLU A N   1 
ATOM   617  C  CA  . GLU A 1 78  ? 28.594 -22.728 25.357  1.00 12.97 ? 78   GLU A CA  1 
ATOM   618  C  C   . GLU A 1 78  ? 27.334 -22.052 24.811  1.00 12.63 ? 78   GLU A C   1 
ATOM   619  O  O   . GLU A 1 78  ? 26.227 -22.548 24.944  1.00 13.48 ? 78   GLU A O   1 
ATOM   620  C  CB  . GLU A 1 78  ? 28.574 -24.226 25.114  1.00 14.29 ? 78   GLU A CB  1 
ATOM   621  C  CG  . GLU A 1 78  ? 28.646 -24.574 23.610  1.00 17.89 ? 78   GLU A CG  1 
ATOM   622  C  CD  . GLU A 1 78  ? 30.004 -24.529 22.994  1.00 20.72 ? 78   GLU A CD  1 
ATOM   623  O  OE1 . GLU A 1 78  ? 31.032 -24.732 23.710  1.00 27.80 ? 78   GLU A OE1 1 
ATOM   624  O  OE2 . GLU A 1 78  ? 30.079 -24.349 21.752  1.00 22.43 ? 78   GLU A OE2 1 
ATOM   625  N  N   . ARG A 1 79  ? 27.555 -20.888 24.202  1.00 11.76 ? 79   ARG A N   1 
ATOM   626  C  CA  . ARG A 1 79  ? 26.459 -20.064 23.660  1.00 11.09 ? 79   ARG A CA  1 
ATOM   627  C  C   . ARG A 1 79  ? 27.055 -19.214 22.556  1.00 10.21 ? 79   ARG A C   1 
ATOM   628  O  O   . ARG A 1 79  ? 28.233 -18.949 22.531  1.00 11.88 ? 79   ARG A O   1 
ATOM   629  C  CB  . ARG A 1 79  ? 25.809 -19.202 24.747  1.00 11.05 ? 79   ARG A CB  1 
ATOM   630  C  CG  . ARG A 1 79  ? 26.803 -18.173 25.424  1.00 11.02 ? 79   ARG A CG  1 
ATOM   631  C  CD  . ARG A 1 79  ? 26.079 -17.234 26.297  1.00 10.85 ? 79   ARG A CD  1 
ATOM   632  N  NE  . ARG A 1 79  ? 25.686 -16.028 25.551  1.00 11.58 ? 79   ARG A NE  1 
ATOM   633  C  CZ  . ARG A 1 79  ? 25.237 -14.942 26.174  1.00 9.77  ? 79   ARG A CZ  1 
ATOM   634  N  NH1 . ARG A 1 79  ? 25.144 -14.930 27.489  1.00 10.61 ? 79   ARG A NH1 1 
ATOM   635  N  NH2 . ARG A 1 79  ? 24.988 -13.850 25.480  1.00 10.74 ? 79   ARG A NH2 1 
ATOM   636  N  N   . HIS A 1 80  ? 26.170 -18.758 21.692  1.00 11.26 ? 80   HIS A N   1 
ATOM   637  C  CA  . HIS A 1 80  ? 26.453 -17.649 20.831  1.00 10.83 ? 80   HIS A CA  1 
ATOM   638  C  C   . HIS A 1 80  ? 26.519 -16.323 21.607  1.00 9.63  ? 80   HIS A C   1 
ATOM   639  O  O   . HIS A 1 80  ? 25.741 -16.168 22.545  1.00 10.08 ? 80   HIS A O   1 
ATOM   640  C  CB  . HIS A 1 80  ? 25.375 -17.547 19.757  1.00 10.36 ? 80   HIS A CB  1 
ATOM   641  C  CG  . HIS A 1 80  ? 25.220 -18.782 18.953  1.00 11.61 ? 80   HIS A CG  1 
ATOM   642  N  ND1 . HIS A 1 80  ? 23.958 -19.190 18.536  1.00 12.57 ? 80   HIS A ND1 1 
ATOM   643  C  CD2 . HIS A 1 80  ? 26.113 -19.651 18.450  1.00 13.32 ? 80   HIS A CD2 1 
ATOM   644  C  CE1 . HIS A 1 80  ? 24.130 -20.235 17.727  1.00 11.59 ? 80   HIS A CE1 1 
ATOM   645  N  NE2 . HIS A 1 80  ? 25.417 -20.553 17.677  1.00 14.39 ? 80   HIS A NE2 1 
ATOM   646  N  N   . VAL A 1 81  ? 27.337 -15.361 21.167  1.00 9.49  ? 81   VAL A N   1 
ATOM   647  C  CA  . VAL A 1 81  ? 27.245 -14.059 21.809  1.00 9.95  ? 81   VAL A CA  1 
ATOM   648  C  C   . VAL A 1 81  ? 25.826 -13.562 21.828  1.00 8.97  ? 81   VAL A C   1 
ATOM   649  O  O   . VAL A 1 81  ? 25.429 -12.945 22.781  1.00 10.10 ? 81   VAL A O   1 
ATOM   650  C  CB  . VAL A 1 81  ? 28.230 -13.058 21.170  1.00 10.91 ? 81   VAL A CB  1 
ATOM   651  C  CG1 . VAL A 1 81  ? 28.024 -11.653 21.675  1.00 10.75 ? 81   VAL A CG1 1 
ATOM   652  C  CG2 . VAL A 1 81  ? 29.695 -13.494 21.462  1.00 10.96 ? 81   VAL A CG2 1 
ATOM   653  N  N   . GLY A 1 82  ? 25.130 -13.718 20.711  1.00 9.28  ? 82   GLY A N   1 
ATOM   654  C  CA  . GLY A 1 82  ? 23.784 -13.204 20.659  1.00 10.64 ? 82   GLY A CA  1 
ATOM   655  C  C   . GLY A 1 82  ? 22.681 -13.904 21.421  1.00 9.57  ? 82   GLY A C   1 
ATOM   656  O  O   . GLY A 1 82  ? 21.520 -13.513 21.354  1.00 9.68  ? 82   GLY A O   1 
ATOM   657  N  N   . ASP A 1 83  ? 22.971 -14.966 22.153  1.00 8.96  ? 83   ASP A N   1 
ATOM   658  C  CA  . ASP A 1 83  ? 21.943 -15.793 22.835  1.00 9.57  ? 83   ASP A CA  1 
ATOM   659  C  C   . ASP A 1 83  ? 21.496 -15.170 24.126  1.00 10.61 ? 83   ASP A C   1 
ATOM   660  O  O   . ASP A 1 83  ? 22.057 -15.419 25.201  1.00 12.10 ? 83   ASP A O   1 
ATOM   661  C  CB  . ASP A 1 83  ? 22.582 -17.206 23.046  1.00 10.51 ? 83   ASP A CB  1 
ATOM   662  C  CG  . ASP A 1 83  ? 22.687 -17.993 21.831  1.00 11.11 ? 83   ASP A CG  1 
ATOM   663  O  OD1 . ASP A 1 83  ? 22.091 -17.604 20.753  1.00 9.66  ? 83   ASP A OD1 1 
ATOM   664  O  OD2 . ASP A 1 83  ? 23.381 -19.038 21.825  1.00 11.23 ? 83   ASP A OD2 1 
ATOM   665  N  N   . LEU A 1 84  ? 20.312 -14.554 24.068  1.00 9.65  ? 84   LEU A N   1 
ATOM   666  C  CA  . LEU A 1 84  ? 19.699 -13.899 25.228  1.00 9.92  ? 84   LEU A CA  1 
ATOM   667  C  C   . LEU A 1 84  ? 18.469 -14.680 25.748  1.00 9.88  ? 84   LEU A C   1 
ATOM   668  O  O   . LEU A 1 84  ? 17.724 -14.171 26.554  1.00 12.31 ? 84   LEU A O   1 
ATOM   669  C  CB  . LEU A 1 84  ? 19.343 -12.450 24.933  1.00 10.51 ? 84   LEU A CB  1 
ATOM   670  C  CG  . LEU A 1 84  ? 20.599 -11.602 24.604  1.00 10.61 ? 84   LEU A CG  1 
ATOM   671  C  CD1 . LEU A 1 84  ? 20.144 -10.181 24.290  1.00 13.06 ? 84   LEU A CD1 1 
ATOM   672  C  CD2 . LEU A 1 84  ? 21.604 -11.586 25.739  1.00 13.49 ? 84   LEU A CD2 1 
ATOM   673  N  N   . GLY A 1 85  ? 18.312 -15.896 25.311  1.00 10.57 ? 85   GLY A N   1 
ATOM   674  C  CA  . GLY A 1 85  ? 17.323 -16.809 25.883  1.00 10.04 ? 85   GLY A CA  1 
ATOM   675  C  C   . GLY A 1 85  ? 15.905 -16.612 25.363  1.00 10.39 ? 85   GLY A C   1 
ATOM   676  O  O   . GLY A 1 85  ? 15.682 -16.594 24.144  1.00 11.26 ? 85   GLY A O   1 
ATOM   677  N  N   . ASN A 1 86  ? 15.013 -16.403 26.303  1.00 10.77 ? 86   ASN A N   1 
ATOM   678  C  CA  . ASN A 1 86  ? 13.601 -16.158 26.031  1.00 10.59 ? 86   ASN A CA  1 
ATOM   679  C  C   . ASN A 1 86  ? 13.062 -14.960 26.740  1.00 10.94 ? 86   ASN A C   1 
ATOM   680  O  O   . ASN A 1 86  ? 13.504 -14.702 27.871  1.00 12.43 ? 86   ASN A O   1 
ATOM   681  C  CB  . ASN A 1 86  ? 12.699 -17.314 26.505  1.00 11.84 ? 86   ASN A CB  1 
ATOM   682  C  CG  . ASN A 1 86  ? 12.980 -18.568 25.689  1.00 11.65 ? 86   ASN A CG  1 
ATOM   683  O  OD1 . ASN A 1 86  ? 12.495 -18.674 24.543  1.00 12.17 ? 86   ASN A OD1 1 
ATOM   684  N  ND2 . ASN A 1 86  ? 13.709 -19.504 26.216  1.00 13.41 ? 86   ASN A ND2 1 
ATOM   685  N  N   . VAL A 1 87  ? 12.071 -14.312 26.149  1.00 11.13 ? 87   VAL A N   1 
ATOM   686  C  CA  . VAL A 1 87  ? 11.183 -13.433 26.934  1.00 11.18 ? 87   VAL A CA  1 
ATOM   687  C  C   . VAL A 1 87  ? 9.895  -14.192 27.158  1.00 11.74 ? 87   VAL A C   1 
ATOM   688  O  O   . VAL A 1 87  ? 9.576  -15.082 26.407  1.00 12.04 ? 87   VAL A O   1 
ATOM   689  C  CB  . VAL A 1 87  ? 10.996 -12.087 26.255  1.00 11.53 ? 87   VAL A CB  1 
ATOM   690  C  CG1 . VAL A 1 87  ? 12.371 -11.377 26.122  1.00 14.84 ? 87   VAL A CG1 1 
ATOM   691  C  CG2 . VAL A 1 87  ? 10.341 -12.242 24.872  1.00 13.99 ? 87   VAL A CG2 1 
ATOM   692  N  N   . THR A 1 88  ? 9.178  -13.810 28.170  1.00 12.92 ? 88   THR A N   1 
ATOM   693  C  CA  . THR A 1 88  ? 7.949  -14.553 28.478  1.00 13.72 ? 88   THR A CA  1 
ATOM   694  C  C   . THR A 1 88  ? 6.736  -13.604 28.525  1.00 12.93 ? 88   THR A C   1 
ATOM   695  O  O   . THR A 1 88  ? 6.749  -12.608 29.241  1.00 18.35 ? 88   THR A O   1 
ATOM   696  C  CB  . THR A 1 88  ? 8.125  -15.326 29.853  1.00 15.78 ? 88   THR A CB  1 
ATOM   697  O  OG1 . THR A 1 88  ? 9.162  -16.314 29.758  1.00 21.11 ? 88   THR A OG1 1 
ATOM   698  C  CG2 . THR A 1 88  ? 6.777  -16.037 30.169  1.00 20.58 ? 88   THR A CG2 1 
ATOM   699  N  N   . ALA A 1 89  ? 5.754  -13.856 27.655  1.00 13.00 ? 89   ALA A N   1 
ATOM   700  C  CA  . ALA A 1 89  ? 4.543  -13.108 27.645  1.00 14.68 ? 89   ALA A CA  1 
ATOM   701  C  C   . ALA A 1 89  ? 3.440  -13.742 28.502  1.00 14.40 ? 89   ALA A C   1 
ATOM   702  O  O   . ALA A 1 89  ? 3.259  -14.946 28.567  1.00 14.44 ? 89   ALA A O   1 
ATOM   703  C  CB  . ALA A 1 89  ? 4.109  -12.986 26.211  1.00 13.40 ? 89   ALA A CB  1 
ATOM   704  N  N   . ASP A 1 90  ? 2.695  -12.865 29.083  1.00 15.73 ? 90   ASP A N   1 
ATOM   705  C  CA  . ASP A 1 90  ? 1.477  -13.224 29.839  1.00 16.85 ? 90   ASP A CA  1 
ATOM   706  C  C   . ASP A 1 90  ? 0.291  -13.378 28.925  1.00 16.17 ? 90   ASP A C   1 
ATOM   707  O  O   . ASP A 1 90  ? 0.375  -13.178 27.724  1.00 13.71 ? 90   ASP A O   1 
ATOM   708  C  CB  . ASP A 1 90  ? 1.340  -12.174 30.957  1.00 19.20 ? 90   ASP A CB  1 
ATOM   709  C  CG  A ASP A 1 90  ? 2.002  -12.646 32.289  0.60 19.14 ? 90   ASP A CG  1 
ATOM   710  C  CG  B ASP A 1 90  ? 1.001  -10.794 30.474  0.40 14.31 ? 90   ASP A CG  1 
ATOM   711  O  OD1 A ASP A 1 90  ? 2.755  -13.659 32.323  0.60 24.99 ? 90   ASP A OD1 1 
ATOM   712  O  OD1 B ASP A 1 90  ? 0.690  -10.499 29.300  0.40 12.96 ? 90   ASP A OD1 1 
ATOM   713  O  OD2 A ASP A 1 90  ? 1.827  -11.940 33.304  0.60 29.04 ? 90   ASP A OD2 1 
ATOM   714  O  OD2 B ASP A 1 90  ? 0.945  -9.893  31.340  0.40 19.95 ? 90   ASP A OD2 1 
ATOM   715  N  N   . LYS A 1 91  ? -0.851 -13.681 29.479  1.00 15.87 ? 91   LYS A N   1 
ATOM   716  C  CA  . LYS A 1 91  ? -2.125 -13.813 28.705  1.00 14.76 ? 91   LYS A CA  1 
ATOM   717  C  C   . LYS A 1 91  ? -2.469 -12.519 28.019  1.00 14.60 ? 91   LYS A C   1 
ATOM   718  O  O   . LYS A 1 91  ? -3.112 -12.522 26.996  1.00 19.45 ? 91   LYS A O   1 
ATOM   719  C  CB  . LYS A 1 91  ? -3.306 -14.198 29.584  1.00 13.61 ? 91   LYS A CB  1 
ATOM   720  C  CG  . LYS A 1 91  ? -3.433 -15.678 29.897  1.00 19.04 ? 91   LYS A CG  1 
ATOM   721  C  CD  . LYS A 1 91  ? -3.819 -16.360 28.612  1.00 22.12 ? 91   LYS A CD  1 
ATOM   722  C  CE  A LYS A 1 91  ? -4.754 -17.524 28.769  0.50 22.38 ? 91   LYS A CE  1 
ATOM   723  C  CE  B LYS A 1 91  ? -4.674 -17.628 28.813  0.50 23.54 ? 91   LYS A CE  1 
ATOM   724  N  NZ  A LYS A 1 91  ? -4.564 -18.322 27.507  0.50 20.90 ? 91   LYS A NZ  1 
ATOM   725  N  NZ  B LYS A 1 91  ? -3.830 -18.707 29.432  0.50 19.27 ? 91   LYS A NZ  1 
ATOM   726  N  N   . ASP A 1 92  ? -1.978 -11.426 28.626  1.00 16.45 ? 92   ASP A N   1 
ATOM   727  C  CA  A ASP A 1 92  ? -2.191 -10.077 28.068  0.70 17.53 ? 92   ASP A CA  1 
ATOM   728  C  CA  B ASP A 1 92  ? -2.072 -10.078 28.163  0.30 18.77 ? 92   ASP A CA  1 
ATOM   729  C  C   . ASP A 1 92  ? -1.303 -9.817  26.866  1.00 18.92 ? 92   ASP A C   1 
ATOM   730  O  O   . ASP A 1 92  ? -1.465 -8.774  26.231  1.00 23.29 ? 92   ASP A O   1 
ATOM   731  C  CB  A ASP A 1 92  ? -1.913 -8.936  29.035  0.70 21.97 ? 92   ASP A CB  1 
ATOM   732  C  CB  B ASP A 1 92  ? -1.457 -9.199  29.240  0.30 19.48 ? 92   ASP A CB  1 
ATOM   733  C  CG  A ASP A 1 92  ? -0.489 -8.839  29.511  0.70 28.44 ? 92   ASP A CG  1 
ATOM   734  C  CG  B ASP A 1 92  ? -2.178 -7.935  29.370  0.30 25.80 ? 92   ASP A CG  1 
ATOM   735  O  OD1 A ASP A 1 92  ? 0.361  -9.683  29.139  0.70 21.95 ? 92   ASP A OD1 1 
ATOM   736  O  OD1 B ASP A 1 92  ? -1.816 -6.968  28.649  0.30 28.82 ? 92   ASP A OD1 1 
ATOM   737  O  OD2 A ASP A 1 92  ? -0.229 -7.930  30.343  0.70 40.83 ? 92   ASP A OD2 1 
ATOM   738  O  OD2 B ASP A 1 92  ? -3.158 -7.954  30.143  0.30 20.42 ? 92   ASP A OD2 1 
ATOM   739  N  N   . GLY A 1 93  ? -0.419 -10.743 26.488  1.00 17.38 ? 93   GLY A N   1 
ATOM   740  C  CA  . GLY A 1 93  ? 0.402  -10.597 25.342  1.00 17.17 ? 93   GLY A CA  1 
ATOM   741  C  C   . GLY A 1 93  ? 1.661  -9.779  25.553  1.00 18.07 ? 93   GLY A C   1 
ATOM   742  O  O   . GLY A 1 93  ? 2.417  -9.509  24.584  1.00 16.50 ? 93   GLY A O   1 
ATOM   743  N  N   . VAL A 1 94  ? 1.955  -9.358  26.781  1.00 15.62 ? 94   VAL A N   1 
ATOM   744  C  CA  . VAL A 1 94  ? 3.109  -8.499  27.103  1.00 17.40 ? 94   VAL A CA  1 
ATOM   745  C  C   . VAL A 1 94  ? 4.184  -9.243  27.777  1.00 16.62 ? 94   VAL A C   1 
ATOM   746  O  O   . VAL A 1 94  ? 3.922  -9.997  28.766  1.00 17.95 ? 94   VAL A O   1 
ATOM   747  C  CB  . VAL A 1 94  ? 2.669  -7.354  28.088  1.00 17.05 ? 94   VAL A CB  1 
ATOM   748  C  CG1 . VAL A 1 94  ? 3.839  -6.460  28.429  1.00 21.68 ? 94   VAL A CG1 1 
ATOM   749  C  CG2 . VAL A 1 94  ? 1.504  -6.629  27.405  1.00 18.13 ? 94   VAL A CG2 1 
ATOM   750  N  N   . ALA A 1 95  ? 5.426  -8.990  27.324  1.00 14.86 ? 95   ALA A N   1 
ATOM   751  C  CA  . ALA A 1 95  ? 6.608  -9.513  27.984  1.00 16.79 ? 95   ALA A CA  1 
ATOM   752  C  C   . ALA A 1 95  ? 7.366  -8.332  28.477  1.00 17.05 ? 95   ALA A C   1 
ATOM   753  O  O   . ALA A 1 95  ? 7.675  -7.433  27.727  1.00 19.77 ? 95   ALA A O   1 
ATOM   754  C  CB  . ALA A 1 95  ? 7.398  -10.273 27.008  1.00 17.93 ? 95   ALA A CB  1 
ATOM   755  N  N   . ASP A 1 96  ? 7.549  -8.272  29.776  1.00 16.88 ? 96   ASP A N   1 
ATOM   756  C  CA  . ASP A 1 96  ? 8.390  -7.293  30.404  1.00 19.78 ? 96   ASP A CA  1 
ATOM   757  C  C   . ASP A 1 96  ? 9.795  -7.863  30.427  1.00 19.02 ? 96   ASP A C   1 
ATOM   758  O  O   . ASP A 1 96  ? 10.045 -8.963  30.941  1.00 23.96 ? 96   ASP A O   1 
ATOM   759  C  CB  . ASP A 1 96  ? 7.842  -6.957  31.775  1.00 22.61 ? 96   ASP A CB  1 
ATOM   760  C  CG  . ASP A 1 96  ? 6.536  -6.126  31.656  1.00 29.79 ? 96   ASP A CG  1 
ATOM   761  O  OD1 . ASP A 1 96  ? 6.438  -5.200  30.804  1.00 28.22 ? 96   ASP A OD1 1 
ATOM   762  O  OD2 . ASP A 1 96  ? 5.567  -6.412  32.361  1.00 37.09 ? 96   ASP A OD2 1 
ATOM   763  N  N   . VAL A 1 97  ? 10.741 -7.129  29.826  1.00 17.84 ? 97   VAL A N   1 
ATOM   764  C  CA  . VAL A 1 97  ? 12.069 -7.630  29.733  1.00 17.60 ? 97   VAL A CA  1 
ATOM   765  C  C   . VAL A 1 97  ? 12.935 -6.895  30.746  1.00 16.31 ? 97   VAL A C   1 
ATOM   766  O  O   . VAL A 1 97  ? 12.987 -5.653  30.745  1.00 16.30 ? 97   VAL A O   1 
ATOM   767  C  CB  . VAL A 1 97  ? 12.640 -7.409  28.305  1.00 17.64 ? 97   VAL A CB  1 
ATOM   768  C  CG1 . VAL A 1 97  ? 14.049 -7.948  28.177  1.00 20.34 ? 97   VAL A CG1 1 
ATOM   769  C  CG2 . VAL A 1 97  ? 11.668 -7.999  27.275  1.00 20.88 ? 97   VAL A CG2 1 
ATOM   770  N  N   A SER A 1 98  ? 13.640 -7.728  31.491  0.70 17.06 ? 98   SER A N   1 
ATOM   771  N  N   B SER A 1 98  ? 13.644 -7.559  31.683  0.20 14.31 ? 98   SER A N   1 
ATOM   772  C  CA  A SER A 1 98  ? 14.593 -7.291  32.405  0.70 17.24 ? 98   SER A CA  1 
ATOM   773  C  CA  B SER A 1 98  ? 14.620 -6.865  32.604  0.20 12.59 ? 98   SER A CA  1 
ATOM   774  C  C   A SER A 1 98  ? 15.718 -8.386  32.398  0.70 16.01 ? 98   SER A C   1 
ATOM   775  C  C   B SER A 1 98  ? 15.782 -7.789  33.064  0.20 10.36 ? 98   SER A C   1 
ATOM   776  O  O   A SER A 1 98  ? 15.574 -9.460  33.015  0.70 20.21 ? 98   SER A O   1 
ATOM   777  O  O   B SER A 1 98  ? 15.669 -8.576  34.017  0.20 8.58  ? 98   SER A O   1 
ATOM   778  C  CB  A SER A 1 98  ? 13.918 -7.129  33.781  0.70 16.54 ? 98   SER A CB  1 
ATOM   779  C  CB  B SER A 1 98  ? 13.943 -6.220  33.827  0.20 11.92 ? 98   SER A CB  1 
ATOM   780  O  OG  A SER A 1 98  ? 14.961 -6.635  34.542  0.70 23.03 ? 98   SER A OG  1 
ATOM   781  O  OG  B SER A 1 98  ? 14.919 -5.544  34.612  0.20 17.71 ? 98   SER A OG  1 
ATOM   782  N  N   A ILE A 1 99  ? 16.819 -8.130  31.721  0.70 15.49 ? 99   ILE A N   1 
ATOM   783  N  N   B ILE A 1 99  ? 16.900 -7.701  32.366  0.20 8.92  ? 99   ILE A N   1 
ATOM   784  C  CA  A ILE A 1 99  ? 17.981 -9.019  31.539  0.70 13.99 ? 99   ILE A CA  1 
ATOM   785  C  CA  B ILE A 1 99  ? 17.978 -8.673  32.478  0.20 8.41  ? 99   ILE A CA  1 
ATOM   786  C  C   A ILE A 1 99  ? 19.308 -8.238  31.938  0.70 13.74 ? 99   ILE A C   1 
ATOM   787  C  C   B ILE A 1 99  ? 19.299 -8.034  32.376  0.20 11.52 ? 99   ILE A C   1 
ATOM   788  O  O   A ILE A 1 99  ? 19.383 -7.050  31.674  0.70 14.38 ? 99   ILE A O   1 
ATOM   789  O  O   B ILE A 1 99  ? 19.455 -6.847  32.122  0.20 10.30 ? 99   ILE A O   1 
ATOM   790  C  CB  A ILE A 1 99  ? 18.008 -9.490  30.004  0.70 14.62 ? 99   ILE A CB  1 
ATOM   791  C  CB  B ILE A 1 99  ? 17.876 -9.786  31.377  0.20 8.05  ? 99   ILE A CB  1 
ATOM   792  C  CG1 A ILE A 1 99  ? 16.831 -10.466 29.675  0.70 14.60 ? 99   ILE A CG1 1 
ATOM   793  C  CG1 B ILE A 1 99  ? 18.270 -9.245  29.987  0.20 8.34  ? 99   ILE A CG1 1 
ATOM   794  C  CG2 A ILE A 1 99  ? 19.319 -10.105 29.588  0.70 21.54 ? 99   ILE A CG2 1 
ATOM   795  C  CG2 B ILE A 1 99  ? 16.441 -10.327 31.377  0.20 9.18  ? 99   ILE A CG2 1 
ATOM   796  C  CD1 A ILE A 1 99  ? 16.717 -10.724 28.158  0.70 16.71 ? 99   ILE A CD1 1 
ATOM   797  C  CD1 B ILE A 1 99  ? 19.602 -9.702  29.478  0.20 13.36 ? 99   ILE A CD1 1 
ATOM   798  N  N   . GLU A 1 100 ? 20.255 -8.884  32.619  1.00 13.77 ? 100  GLU A N   1 
ATOM   799  C  CA  A GLU A 1 100 ? 21.653 -8.469  32.565  0.70 14.70 ? 100  GLU A CA  1 
ATOM   800  C  CA  B GLU A 1 100 ? 21.628 -8.416  32.584  0.30 14.72 ? 100  GLU A CA  1 
ATOM   801  C  C   . GLU A 1 100 ? 22.447 -9.518  31.906  1.00 13.56 ? 100  GLU A C   1 
ATOM   802  O  O   . GLU A 1 100 ? 22.245 -10.697 32.199  1.00 14.93 ? 100  GLU A O   1 
ATOM   803  C  CB  A GLU A 1 100 ? 22.283 -8.208  33.956  0.70 16.65 ? 100  GLU A CB  1 
ATOM   804  C  CB  B GLU A 1 100 ? 22.192 -8.061  33.974  0.30 16.11 ? 100  GLU A CB  1 
ATOM   805  C  CG  A GLU A 1 100 ? 21.867 -6.885  34.565  0.70 23.66 ? 100  GLU A CG  1 
ATOM   806  C  CG  B GLU A 1 100 ? 23.707 -7.867  33.937  0.30 17.23 ? 100  GLU A CG  1 
ATOM   807  C  CD  A GLU A 1 100 ? 22.659 -6.459  35.784  0.70 23.08 ? 100  GLU A CD  1 
ATOM   808  C  CD  B GLU A 1 100 ? 24.352 -7.382  35.231  0.30 19.15 ? 100  GLU A CD  1 
ATOM   809  O  OE1 A GLU A 1 100 ? 23.552 -7.216  36.215  0.70 29.37 ? 100  GLU A OE1 1 
ATOM   810  O  OE1 B GLU A 1 100 ? 24.047 -6.229  35.617  0.30 17.35 ? 100  GLU A OE1 1 
ATOM   811  O  OE2 A GLU A 1 100 ? 22.373 -5.367  36.312  0.70 34.99 ? 100  GLU A OE2 1 
ATOM   812  O  OE2 B GLU A 1 100 ? 25.212 -8.127  35.805  0.30 16.11 ? 100  GLU A OE2 1 
ATOM   813  N  N   . ASP A 1 101 ? 23.380 -9.144  31.026  1.00 12.06 ? 101  ASP A N   1 
ATOM   814  C  CA  . ASP A 1 101 ? 24.154 -10.099 30.334  1.00 11.24 ? 101  ASP A CA  1 
ATOM   815  C  C   . ASP A 1 101 ? 25.628 -9.650  30.251  1.00 11.32 ? 101  ASP A C   1 
ATOM   816  O  O   . ASP A 1 101 ? 25.893 -8.478  30.011  1.00 12.74 ? 101  ASP A O   1 
ATOM   817  C  CB  . ASP A 1 101 ? 23.597 -10.349 28.910  1.00 11.26 ? 101  ASP A CB  1 
ATOM   818  C  CG  . ASP A 1 101 ? 24.252 -11.576 28.249  1.00 11.85 ? 101  ASP A CG  1 
ATOM   819  O  OD1 . ASP A 1 101 ? 23.817 -12.702 28.664  1.00 12.15 ? 101  ASP A OD1 1 
ATOM   820  O  OD2 . ASP A 1 101 ? 25.203 -11.477 27.408  1.00 11.85 ? 101  ASP A OD2 1 
ATOM   821  N  N   . SER A 1 102 ? 26.545 -10.557 30.532  1.00 12.50 ? 102  SER A N   1 
ATOM   822  C  CA  . SER A 1 102 ? 27.983 -10.208 30.511  1.00 13.69 ? 102  SER A CA  1 
ATOM   823  C  C   . SER A 1 102 ? 28.729 -10.678 29.321  1.00 11.62 ? 102  SER A C   1 
ATOM   824  O  O   . SER A 1 102 ? 29.938 -10.506 29.243  1.00 14.78 ? 102  SER A O   1 
ATOM   825  C  CB  . SER A 1 102 ? 28.616 -10.595 31.832  1.00 19.31 ? 102  SER A CB  1 
ATOM   826  O  OG  A SER A 1 102 ? 28.787 -9.331  32.456  0.50 17.36 ? 102  SER A OG  1 
ATOM   827  O  OG  B SER A 1 102 ? 28.438 -11.972 31.873  0.50 10.81 ? 102  SER A OG  1 
ATOM   828  N  N   . VAL A 1 103 ? 28.066 -11.227 28.321  1.00 11.96 ? 103  VAL A N   1 
ATOM   829  C  CA  . VAL A 1 103 ? 28.740 -11.686 27.096  1.00 11.65 ? 103  VAL A CA  1 
ATOM   830  C  C   . VAL A 1 103 ? 28.584 -10.695 25.910  1.00 10.82 ? 103  VAL A C   1 
ATOM   831  O  O   . VAL A 1 103 ? 29.525 -10.387 25.230  1.00 11.79 ? 103  VAL A O   1 
ATOM   832  C  CB  . VAL A 1 103 ? 28.234 -13.102 26.695  1.00 12.42 ? 103  VAL A CB  1 
ATOM   833  C  CG1 . VAL A 1 103 ? 28.775 -13.553 25.376  1.00 12.67 ? 103  VAL A CG1 1 
ATOM   834  C  CG2 . VAL A 1 103 ? 28.534 -14.113 27.840  1.00 12.72 ? 103  VAL A CG2 1 
ATOM   835  N  N   . ILE A 1 104 ? 27.391 -10.166 25.721  1.00 10.48 ? 104  ILE A N   1 
ATOM   836  C  CA  . ILE A 1 104 ? 27.193 -9.063  24.815  1.00 10.78 ? 104  ILE A CA  1 
ATOM   837  C  C   . ILE A 1 104 ? 27.968 -7.840  25.281  1.00 11.20 ? 104  ILE A C   1 
ATOM   838  O  O   . ILE A 1 104 ? 28.274 -7.695  26.446  1.00 12.37 ? 104  ILE A O   1 
ATOM   839  C  CB  . ILE A 1 104 ? 25.717 -8.726  24.551  1.00 10.65 ? 104  ILE A CB  1 
ATOM   840  C  CG1 . ILE A 1 104 ? 25.014 -8.270  25.877  1.00 11.12 ? 104  ILE A CG1 1 
ATOM   841  C  CG2 . ILE A 1 104 ? 24.934 -9.892  23.868  1.00 11.65 ? 104  ILE A CG2 1 
ATOM   842  C  CD1 . ILE A 1 104 ? 23.619 -7.728  25.684  1.00 10.32 ? 104  ILE A CD1 1 
ATOM   843  N  N   . SER A 1 105 ? 28.247 -6.940  24.349  1.00 11.72 ? 105  SER A N   1 
ATOM   844  C  CA  . SER A 1 105 ? 28.910 -5.687  24.694  1.00 12.78 ? 105  SER A CA  1 
ATOM   845  C  C   . SER A 1 105 ? 28.321 -4.605  23.771  1.00 11.84 ? 105  SER A C   1 
ATOM   846  O  O   . SER A 1 105 ? 27.772 -4.908  22.706  1.00 10.80 ? 105  SER A O   1 
ATOM   847  C  CB  . SER A 1 105 ? 30.435 -5.808  24.586  1.00 13.51 ? 105  SER A CB  1 
ATOM   848  O  OG  . SER A 1 105 ? 30.975 -4.636  25.118  1.00 14.24 ? 105  SER A OG  1 
ATOM   849  N  N   . LEU A 1 106 ? 28.556 -3.364  24.127  1.00 11.25 ? 106  LEU A N   1 
ATOM   850  C  CA  . LEU A 1 106 ? 28.272 -2.220  23.266  1.00 12.35 ? 106  LEU A CA  1 
ATOM   851  C  C   . LEU A 1 106 ? 29.524 -1.638  22.637  1.00 14.59 ? 106  LEU A C   1 
ATOM   852  O  O   . LEU A 1 106 ? 29.483 -0.579  22.051  1.00 16.07 ? 106  LEU A O   1 
ATOM   853  C  CB  . LEU A 1 106 ? 27.469 -1.164  24.039  1.00 13.46 ? 106  LEU A CB  1 
ATOM   854  C  CG  . LEU A 1 106 ? 26.171 -1.640  24.668  1.00 12.89 ? 106  LEU A CG  1 
ATOM   855  C  CD1 . LEU A 1 106 ? 25.448 -0.435  25.341  1.00 13.83 ? 106  LEU A CD1 1 
ATOM   856  C  CD2 . LEU A 1 106 ? 25.260 -2.304  23.681  1.00 12.91 ? 106  LEU A CD2 1 
ATOM   857  N  N   . SER A 1 107 ? 30.668 -2.332  22.713  1.00 14.43 ? 107  SER A N   1 
ATOM   858  C  CA  . SER A 1 107 ? 31.862 -1.957  22.004  1.00 16.76 ? 107  SER A CA  1 
ATOM   859  C  C   . SER A 1 107 ? 32.688 -3.222  21.791  1.00 13.97 ? 107  SER A C   1 
ATOM   860  O  O   . SER A 1 107 ? 32.473 -4.251  22.396  1.00 15.49 ? 107  SER A O   1 
ATOM   861  C  CB  . SER A 1 107 ? 32.594 -0.840  22.725  1.00 20.15 ? 107  SER A CB  1 
ATOM   862  O  OG  . SER A 1 107 ? 33.132 -1.358  23.906  1.00 24.89 ? 107  SER A OG  1 
ATOM   863  N  N   . GLY A 1 108 ? 33.663 -3.132  20.934  1.00 15.53 ? 108  GLY A N   1 
ATOM   864  C  CA  . GLY A 1 108 ? 34.584 -4.215  20.677  1.00 16.41 ? 108  GLY A CA  1 
ATOM   865  C  C   . GLY A 1 108 ? 34.033 -5.344  19.842  1.00 16.60 ? 108  GLY A C   1 
ATOM   866  O  O   . GLY A 1 108 ? 32.999 -5.212  19.173  1.00 16.23 ? 108  GLY A O   1 
ATOM   867  N  N   . ASP A 1 109 ? 34.741 -6.470  19.890  1.00 15.85 ? 109  ASP A N   1 
ATOM   868  C  CA  . ASP A 1 109 ? 34.417 -7.600  19.057  1.00 17.42 ? 109  ASP A CA  1 
ATOM   869  C  C   . ASP A 1 109 ? 33.074 -8.300  19.440  1.00 15.33 ? 109  ASP A C   1 
ATOM   870  O  O   . ASP A 1 109 ? 32.502 -8.975  18.614  1.00 17.43 ? 109  ASP A O   1 
ATOM   871  C  CB  . ASP A 1 109 ? 35.675 -8.426  18.952  1.00 20.41 ? 109  ASP A CB  1 
ATOM   872  C  CG  A ASP A 1 109 ? 35.449 -9.863  18.587  0.50 20.11 ? 109  ASP A CG  1 
ATOM   873  C  CG  B ASP A 1 109 ? 35.758 -9.514  19.932  0.50 19.46 ? 109  ASP A CG  1 
ATOM   874  O  OD1 A ASP A 1 109 ? 35.399 -10.068 17.350  0.50 24.04 ? 109  ASP A OD1 1 
ATOM   875  O  OD1 B ASP A 1 109 ? 35.564 -9.174  21.102  0.50 20.04 ? 109  ASP A OD1 1 
ATOM   876  O  OD2 A ASP A 1 109 ? 35.329 -10.742 19.468  0.50 35.19 ? 109  ASP A OD2 1 
ATOM   877  O  OD2 B ASP A 1 109 ? 36.180 -10.634 19.576  0.50 29.24 ? 109  ASP A OD2 1 
ATOM   878  N  N   . HIS A 1 110 ? 32.589 -8.106  20.649  1.00 13.94 ? 110  HIS A N   1 
ATOM   879  C  CA  . HIS A 1 110 ? 31.290 -8.625  21.068  1.00 11.86 ? 110  HIS A CA  1 
ATOM   880  C  C   . HIS A 1 110 ? 30.211 -7.576  20.915  1.00 11.72 ? 110  HIS A C   1 
ATOM   881  O  O   . HIS A 1 110 ? 29.094 -7.753  21.389  1.00 10.77 ? 110  HIS A O   1 
ATOM   882  C  CB  . HIS A 1 110 ? 31.373 -9.045  22.531  1.00 14.88 ? 110  HIS A CB  1 
ATOM   883  C  CG  . HIS A 1 110 ? 32.229 -10.227 22.765  1.00 19.32 ? 110  HIS A CG  1 
ATOM   884  N  ND1 . HIS A 1 110 ? 31.815 -11.289 23.537  1.00 19.25 ? 110  HIS A ND1 1 
ATOM   885  C  CD2 . HIS A 1 110 ? 33.501 -10.475 22.443  1.00 19.20 ? 110  HIS A CD2 1 
ATOM   886  C  CE1 . HIS A 1 110 ? 32.765 -12.205 23.556  1.00 21.48 ? 110  HIS A CE1 1 
ATOM   887  N  NE2 . HIS A 1 110 ? 33.824 -11.715 22.941  1.00 28.16 ? 110  HIS A NE2 1 
ATOM   888  N  N   . CYS A 1 111 ? 30.502 -6.441  20.209  1.00 11.88 ? 111  CYS A N   1 
ATOM   889  C  CA  . CYS A 1 111 ? 29.584 -5.336  20.089  1.00 11.86 ? 111  CYS A CA  1 
ATOM   890  C  C   . CYS A 1 111 ? 28.392 -5.867  19.347  1.00 10.69 ? 111  CYS A C   1 
ATOM   891  O  O   . CYS A 1 111 ? 28.408 -6.328  18.219  1.00 11.49 ? 111  CYS A O   1 
ATOM   892  C  CB  . CYS A 1 111 ? 30.220 -4.134  19.383  1.00 14.38 ? 111  CYS A CB  1 
ATOM   893  S  SG  . CYS A 1 111 ? 29.191 -2.709  19.405  1.00 14.96 ? 111  CYS A SG  1 
ATOM   894  N  N   . ILE A 1 112 ? 27.180 -5.376  19.794  1.00 9.86  ? 112  ILE A N   1 
ATOM   895  C  CA  . ILE A 1 112 ? 25.852 -5.674  19.176  1.00 9.83  ? 112  ILE A CA  1 
ATOM   896  C  C   . ILE A 1 112 ? 25.285 -4.487  18.456  1.00 10.14 ? 112  ILE A C   1 
ATOM   897  O  O   . ILE A 1 112 ? 24.243 -4.617  17.814  1.00 9.39  ? 112  ILE A O   1 
ATOM   898  C  CB  . ILE A 1 112 ? 24.919 -6.309  20.193  1.00 9.71  ? 112  ILE A CB  1 
ATOM   899  C  CG1 . ILE A 1 112 ? 24.573 -5.324  21.361  1.00 11.08 ? 112  ILE A CG1 1 
ATOM   900  C  CG2 . ILE A 1 112 ? 25.476 -7.657  20.681  1.00 11.52 ? 112  ILE A CG2 1 
ATOM   901  C  CD1 . ILE A 1 112 ? 23.486 -5.820  22.294  1.00 11.31 ? 112  ILE A CD1 1 
ATOM   902  N  N   . ILE A 1 113 ? 25.909 -3.336  18.588  1.00 11.20 ? 113  ILE A N   1 
ATOM   903  C  CA  . ILE A 1 113 ? 25.433 -2.135  17.846  1.00 10.53 ? 113  ILE A CA  1 
ATOM   904  C  C   . ILE A 1 113 ? 25.494 -2.385  16.375  1.00 9.56  ? 113  ILE A C   1 
ATOM   905  O  O   . ILE A 1 113 ? 26.477 -2.872  15.889  1.00 11.09 ? 113  ILE A O   1 
ATOM   906  C  CB  . ILE A 1 113 ? 26.064 -0.868  18.352  1.00 12.91 ? 113  ILE A CB  1 
ATOM   907  C  CG1 . ILE A 1 113 ? 25.545 -0.533  19.867  1.00 14.49 ? 113  ILE A CG1 1 
ATOM   908  C  CG2 . ILE A 1 113 ? 25.693 0.328   17.415  1.00 13.70 ? 113  ILE A CG2 1 
ATOM   909  C  CD1 . ILE A 1 113 ? 26.344 0.503   20.483  1.00 17.73 ? 113  ILE A CD1 1 
ATOM   910  N  N   . GLY A 1 114 ? 24.450 -2.077  15.625  1.00 8.87  ? 114  GLY A N   1 
ATOM   911  C  CA  . GLY A 1 114 ? 24.407 -2.309  14.206  1.00 9.37  ? 114  GLY A CA  1 
ATOM   912  C  C   . GLY A 1 114 ? 24.028 -3.713  13.804  1.00 8.63  ? 114  GLY A C   1 
ATOM   913  O  O   . GLY A 1 114 ? 23.985 -4.001  12.618  1.00 9.71  ? 114  GLY A O   1 
ATOM   914  N  N   . ARG A 1 115 ? 23.648 -4.535  14.757  1.00 8.81  ? 115  ARG A N   1 
ATOM   915  C  CA  . ARG A 1 115 ? 23.153 -5.846  14.514  1.00 9.66  ? 115  ARG A CA  1 
ATOM   916  C  C   . ARG A 1 115 ? 21.645 -5.849  14.813  1.00 9.44  ? 115  ARG A C   1 
ATOM   917  O  O   . ARG A 1 115 ? 21.088 -4.852  15.140  1.00 12.40 ? 115  ARG A O   1 
ATOM   918  C  CB  . ARG A 1 115 ? 23.987 -6.883  15.326  1.00 9.90  ? 115  ARG A CB  1 
ATOM   919  C  CG  . ARG A 1 115 ? 25.456 -6.738  15.025  1.00 11.56 ? 115  ARG A CG  1 
ATOM   920  C  CD  . ARG A 1 115 ? 26.289 -7.851  15.562  1.00 13.14 ? 115  ARG A CD  1 
ATOM   921  N  NE  . ARG A 1 115 ? 27.733 -7.585  15.352  1.00 14.00 ? 115  ARG A NE  1 
ATOM   922  C  CZ  . ARG A 1 115 ? 28.434 -7.905  14.274  1.00 13.37 ? 115  ARG A CZ  1 
ATOM   923  N  NH1 . ARG A 1 115 ? 27.914 -8.506  13.248  1.00 12.49 ? 115  ARG A NH1 1 
ATOM   924  N  NH2 . ARG A 1 115 ? 29.768 -7.652  14.224  1.00 15.42 ? 115  ARG A NH2 1 
ATOM   925  N  N   . THR A 1 116 ? 20.971 -6.985  14.644  1.00 8.96  ? 116  THR A N   1 
ATOM   926  C  CA  . THR A 1 116 ? 19.517 -7.047  14.751  1.00 8.51  ? 116  THR A CA  1 
ATOM   927  C  C   . THR A 1 116 ? 19.116 -7.834  15.986  1.00 9.41  ? 116  THR A C   1 
ATOM   928  O  O   . THR A 1 116 ? 19.503 -8.963  16.144  1.00 10.70 ? 116  THR A O   1 
ATOM   929  C  CB  . THR A 1 116 ? 18.905 -7.708  13.482  1.00 9.16  ? 116  THR A CB  1 
ATOM   930  O  OG1 . THR A 1 116 ? 19.184 -6.892  12.326  1.00 10.16 ? 116  THR A OG1 1 
ATOM   931  C  CG2 . THR A 1 116 ? 17.483 -7.849  13.573  1.00 9.72  ? 116  THR A CG2 1 
ATOM   932  N  N   . LEU A 1 117 ? 18.178 -7.262  16.778  1.00 8.57  ? 117  LEU A N   1 
ATOM   933  C  CA  . LEU A 1 117 ? 17.526 -8.024  17.832  1.00 9.27  ? 117  LEU A CA  1 
ATOM   934  C  C   . LEU A 1 117 ? 16.221 -8.600  17.289  1.00 9.36  ? 117  LEU A C   1 
ATOM   935  O  O   . LEU A 1 117 ? 15.499 -7.905  16.578  1.00 9.54  ? 117  LEU A O   1 
ATOM   936  C  CB  . LEU A 1 117 ? 17.234 -6.994  18.951  1.00 8.33  ? 117  LEU A CB  1 
ATOM   937  C  CG  . LEU A 1 117 ? 16.642 -7.602  20.281  1.00 10.15 ? 117  LEU A CG  1 
ATOM   938  C  CD1 . LEU A 1 117 ? 17.680 -8.525  20.932  1.00 11.23 ? 117  LEU A CD1 1 
ATOM   939  C  CD2 . LEU A 1 117 ? 16.252 -6.497  21.202  1.00 10.81 ? 117  LEU A CD2 1 
ATOM   940  N  N   . VAL A 1 118 ? 15.994 -9.860  17.614  1.00 8.77  ? 118  VAL A N   1 
ATOM   941  C  CA  . VAL A 1 118 ? 14.867 -10.611 17.071  1.00 9.67  ? 118  VAL A CA  1 
ATOM   942  C  C   . VAL A 1 118 ? 14.107 -11.286 18.163  1.00 8.34  ? 118  VAL A C   1 
ATOM   943  O  O   . VAL A 1 118 ? 14.681 -11.855 19.078  1.00 9.49  ? 118  VAL A O   1 
ATOM   944  C  CB  . VAL A 1 118 ? 15.333 -11.733 16.110  1.00 9.25  ? 118  VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 118 ? 14.134 -12.535 15.574  1.00 11.62 ? 118  VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 118 ? 16.130 -11.136 14.927  1.00 9.22  ? 118  VAL A CG2 1 
ATOM   947  N  N   . VAL A 1 119 ? 12.772 -11.197 18.110  1.00 8.31  ? 119  VAL A N   1 
ATOM   948  C  CA  . VAL A 1 119 ? 11.869 -11.947 18.987  1.00 9.44  ? 119  VAL A CA  1 
ATOM   949  C  C   . VAL A 1 119 ? 11.140 -12.974 18.106  1.00 10.46 ? 119  VAL A C   1 
ATOM   950  O  O   . VAL A 1 119 ? 10.615 -12.653 17.051  1.00 10.28 ? 119  VAL A O   1 
ATOM   951  C  CB  . VAL A 1 119 ? 10.968 -11.044 19.859  1.00 9.71  ? 119  VAL A CB  1 
ATOM   952  C  CG1 . VAL A 1 119 ? 10.024 -10.226 19.117  1.00 11.70 ? 119  VAL A CG1 1 
ATOM   953  C  CG2 . VAL A 1 119 ? 10.136 -11.948 20.841  1.00 11.94 ? 119  VAL A CG2 1 
ATOM   954  N  N   . HIS A 1 120 ? 11.089 -14.208 18.605  1.00 9.97  ? 120  HIS A N   1 
ATOM   955  C  CA  . HIS A 1 120 ? 10.658 -15.345 17.834  1.00 11.00 ? 120  HIS A CA  1 
ATOM   956  C  C   . HIS A 1 120 ? 9.235  -15.840 18.124  1.00 10.10 ? 120  HIS A C   1 
ATOM   957  O  O   . HIS A 1 120 ? 8.676  -15.584 19.189  1.00 11.65 ? 120  HIS A O   1 
ATOM   958  C  CB  . HIS A 1 120 ? 11.666 -16.529 18.018  1.00 10.80 ? 120  HIS A CB  1 
ATOM   959  C  CG  . HIS A 1 120 ? 12.968 -16.318 17.337  1.00 9.80  ? 120  HIS A CG  1 
ATOM   960  N  ND1 . HIS A 1 120 ? 13.197 -16.773 16.052  1.00 10.44 ? 120  HIS A ND1 1 
ATOM   961  C  CD2 . HIS A 1 120 ? 14.100 -15.664 17.720  1.00 10.74 ? 120  HIS A CD2 1 
ATOM   962  C  CE1 . HIS A 1 120 ? 14.437 -16.458 15.700  1.00 10.42 ? 120  HIS A CE1 1 
ATOM   963  N  NE2 . HIS A 1 120 ? 15.008 -15.749 16.684  1.00 11.48 ? 120  HIS A NE2 1 
ATOM   964  N  N   . GLU A 1 121 ? 8.791  -16.646 17.174  1.00 12.24 ? 121  GLU A N   1 
ATOM   965  C  CA  . GLU A 1 121 ? 7.446  -17.289 17.294  1.00 13.19 ? 121  GLU A CA  1 
ATOM   966  C  C   . GLU A 1 121 ? 7.308  -18.236 18.492  1.00 12.24 ? 121  GLU A C   1 
ATOM   967  O  O   . GLU A 1 121 ? 6.262  -18.241 19.134  1.00 12.78 ? 121  GLU A O   1 
ATOM   968  C  CB  . GLU A 1 121 ? 7.287  -18.130 16.032  1.00 16.18 ? 121  GLU A CB  1 
ATOM   969  C  CG  . GLU A 1 121 ? 6.030  -18.998 15.859  1.00 17.15 ? 121  GLU A CG  1 
ATOM   970  C  CD  . GLU A 1 121 ? 6.281  -20.144 14.807  1.00 21.39 ? 121  GLU A CD  1 
ATOM   971  O  OE1 . GLU A 1 121 ? 7.383  -20.301 14.141  1.00 20.91 ? 121  GLU A OE1 1 
ATOM   972  O  OE2 . GLU A 1 121 ? 5.307  -20.956 14.746  1.00 24.52 ? 121  GLU A OE2 1 
ATOM   973  N  N   . LYS A 1 122 ? 8.326  -19.064 18.702  1.00 14.79 ? 122  LYS A N   1 
ATOM   974  C  CA  . LYS A 1 122 ? 8.315  -20.192 19.602  1.00 16.81 ? 122  LYS A CA  1 
ATOM   975  C  C   . LYS A 1 122 ? 9.405  -20.011 20.705  1.00 14.74 ? 122  LYS A C   1 
ATOM   976  O  O   . LYS A 1 122 ? 10.225 -19.120 20.685  1.00 15.03 ? 122  LYS A O   1 
ATOM   977  C  CB  . LYS A 1 122 ? 8.591  -21.560 18.827  1.00 16.99 ? 122  LYS A CB  1 
ATOM   978  C  CG  . LYS A 1 122 ? 7.972  -21.807 17.439  1.00 22.43 ? 122  LYS A CG  1 
ATOM   979  C  CD  . LYS A 1 122 ? 8.324  -23.199 16.911  1.00 22.46 ? 122  LYS A CD  1 
ATOM   980  C  CE  . LYS A 1 122 ? 7.598  -23.405 15.583  1.00 29.75 ? 122  LYS A CE  1 
ATOM   981  N  NZ  . LYS A 1 122 ? 7.914  -24.707 15.022  1.00 35.59 ? 122  LYS A NZ  1 
ATOM   982  N  N   . ALA A 1 123 ? 9.408  -20.901 21.676  1.00 11.64 ? 123  ALA A N   1 
ATOM   983  C  CA  . ALA A 1 123 ? 10.373 -20.916 22.745  1.00 13.09 ? 123  ALA A CA  1 
ATOM   984  C  C   . ALA A 1 123 ? 11.691 -21.319 22.194  1.00 13.04 ? 123  ALA A C   1 
ATOM   985  O  O   . ALA A 1 123 ? 11.825 -22.190 21.291  1.00 14.31 ? 123  ALA A O   1 
ATOM   986  C  CB  . ALA A 1 123 ? 9.970  -21.890 23.788  1.00 13.98 ? 123  ALA A CB  1 
ATOM   987  N  N   . ASP A 1 124 ? 12.754 -20.801 22.826  1.00 10.74 ? 124  ASP A N   1 
ATOM   988  C  CA  . ASP A 1 124 ? 14.100 -21.270 22.612  1.00 10.90 ? 124  ASP A CA  1 
ATOM   989  C  C   . ASP A 1 124 ? 14.368 -22.347 23.702  1.00 11.72 ? 124  ASP A C   1 
ATOM   990  O  O   . ASP A 1 124 ? 14.143 -22.146 24.871  1.00 12.83 ? 124  ASP A O   1 
ATOM   991  C  CB  . ASP A 1 124 ? 15.034 -20.054 22.792  1.00 11.76 ? 124  ASP A CB  1 
ATOM   992  C  CG  . ASP A 1 124 ? 16.510 -20.335 22.555  1.00 11.83 ? 124  ASP A CG  1 
ATOM   993  O  OD1 . ASP A 1 124 ? 16.941 -21.491 22.534  1.00 11.67 ? 124  ASP A OD1 1 
ATOM   994  O  OD2 . ASP A 1 124 ? 17.231 -19.317 22.390  1.00 11.96 ? 124  ASP A OD2 1 
ATOM   995  N  N   . ASP A 1 125 ? 14.804 -23.469 23.208  1.00 13.02 ? 125  ASP A N   1 
ATOM   996  C  CA  . ASP A 1 125 ? 15.104 -24.611 24.114  1.00 12.62 ? 125  ASP A CA  1 
ATOM   997  C  C   . ASP A 1 125 ? 16.514 -24.560 24.707  1.00 12.17 ? 125  ASP A C   1 
ATOM   998  O  O   . ASP A 1 125 ? 16.940 -25.464 25.399  1.00 12.98 ? 125  ASP A O   1 
ATOM   999  C  CB  . ASP A 1 125 ? 14.869 -25.945 23.348  1.00 13.99 ? 125  ASP A CB  1 
ATOM   1000 C  CG  . ASP A 1 125 ? 15.799 -26.172 22.191  1.00 13.05 ? 125  ASP A CG  1 
ATOM   1001 O  OD1 . ASP A 1 125 ? 16.937 -25.663 22.188  1.00 14.39 ? 125  ASP A OD1 1 
ATOM   1002 O  OD2 . ASP A 1 125 ? 15.405 -27.009 21.338  1.00 15.18 ? 125  ASP A OD2 1 
ATOM   1003 N  N   . LEU A 1 126 ? 17.236 -23.466 24.458  1.00 12.71 ? 126  LEU A N   1 
ATOM   1004 C  CA  . LEU A 1 126 ? 18.525 -23.169 25.079  1.00 13.49 ? 126  LEU A CA  1 
ATOM   1005 C  C   . LEU A 1 126 ? 19.529 -24.212 24.766  1.00 14.84 ? 126  LEU A C   1 
ATOM   1006 O  O   . LEU A 1 126 ? 20.498 -24.386 25.481  1.00 14.54 ? 126  LEU A O   1 
ATOM   1007 C  CB  . LEU A 1 126 ? 18.380 -22.888 26.598  1.00 14.15 ? 126  LEU A CB  1 
ATOM   1008 C  CG  . LEU A 1 126 ? 17.311 -21.886 27.036  1.00 12.47 ? 126  LEU A CG  1 
ATOM   1009 C  CD1 . LEU A 1 126 ? 17.476 -21.563 28.498  1.00 15.04 ? 126  LEU A CD1 1 
ATOM   1010 C  CD2 . LEU A 1 126 ? 17.321 -20.548 26.177  1.00 13.21 ? 126  LEU A CD2 1 
ATOM   1011 N  N   . GLY A 1 127 ? 19.403 -24.831 23.590  1.00 13.03 ? 127  GLY A N   1 
ATOM   1012 C  CA  . GLY A 1 127 ? 20.315 -25.847 23.163  1.00 14.55 ? 127  GLY A CA  1 
ATOM   1013 C  C   . GLY A 1 127 ? 20.171 -27.225 23.805  1.00 14.69 ? 127  GLY A C   1 
ATOM   1014 O  O   . GLY A 1 127 ? 21.043 -28.082 23.626  1.00 17.02 ? 127  GLY A O   1 
ATOM   1015 N  N   . LYS A 1 128 ? 19.100 -27.434 24.535  1.00 14.05 ? 128  LYS A N   1 
ATOM   1016 C  CA  . LYS A 1 128 ? 18.884 -28.674 25.281  1.00 15.11 ? 128  LYS A CA  1 
ATOM   1017 C  C   . LYS A 1 128 ? 17.792 -29.482 24.697  1.00 15.95 ? 128  LYS A C   1 
ATOM   1018 O  O   . LYS A 1 128 ? 17.235 -30.369 25.360  1.00 16.81 ? 128  LYS A O   1 
ATOM   1019 C  CB  . LYS A 1 128 ? 18.500 -28.339 26.720  1.00 15.89 ? 128  LYS A CB  1 
ATOM   1020 C  CG  . LYS A 1 128 ? 19.552 -27.590 27.396  1.00 19.73 ? 128  LYS A CG  1 
ATOM   1021 C  CD  . LYS A 1 128 ? 20.626 -28.574 27.852  1.00 29.32 ? 128  LYS A CD  1 
ATOM   1022 C  CE  . LYS A 1 128 ? 21.653 -27.982 28.843  1.00 35.60 ? 128  LYS A CE  1 
ATOM   1023 N  NZ  . LYS A 1 128 ? 22.369 -29.093 29.578  1.00 41.37 ? 128  LYS A NZ  1 
ATOM   1024 N  N   . GLY A 1 129 ? 17.421 -29.202 23.468  0.70 12.77 ? 129  GLY A N   1 
ATOM   1025 C  CA  . GLY A 1 129 ? 16.354 -29.919 22.871  0.70 13.86 ? 129  GLY A CA  1 
ATOM   1026 C  C   . GLY A 1 129 ? 16.654 -31.286 22.264  0.70 13.33 ? 129  GLY A C   1 
ATOM   1027 O  O   . GLY A 1 129 ? 15.726 -31.972 21.869  0.70 16.10 ? 129  GLY A O   1 
ATOM   1028 N  N   . GLY A 1 130 ? 17.914 -31.642 22.192  0.70 13.17 ? 130  GLY A N   1 
ATOM   1029 C  CA  . GLY A 1 130 ? 18.322 -32.953 21.718  0.70 20.15 ? 130  GLY A CA  1 
ATOM   1030 C  C   . GLY A 1 130 ? 18.113 -33.256 20.231  0.70 22.61 ? 130  GLY A C   1 
ATOM   1031 O  O   . GLY A 1 130 ? 18.131 -34.416 19.877  0.70 25.12 ? 130  GLY A O   1 
ATOM   1032 N  N   . ASN A 1 131 ? 17.764 -32.286 19.384  1.00 25.12 ? 131  ASN A N   1 
ATOM   1033 C  CA  . ASN A 1 131 ? 17.911 -32.457 17.897  1.00 24.77 ? 131  ASN A CA  1 
ATOM   1034 C  C   . ASN A 1 131 ? 19.030 -31.545 17.448  1.00 23.83 ? 131  ASN A C   1 
ATOM   1035 O  O   . ASN A 1 131 ? 19.568 -30.703 18.192  1.00 24.29 ? 131  ASN A O   1 
ATOM   1036 C  CB  . ASN A 1 131 ? 16.567 -32.268 17.136  1.00 26.04 ? 131  ASN A CB  1 
ATOM   1037 C  CG  . ASN A 1 131 ? 16.016 -30.796 17.156  1.00 30.13 ? 131  ASN A CG  1 
ATOM   1038 O  OD1 . ASN A 1 131 ? 16.675 -29.911 17.645  1.00 19.65 ? 131  ASN A OD1 1 
ATOM   1039 N  ND2 . ASN A 1 131 ? 14.824 -30.551 16.543  1.00 28.87 ? 131  ASN A ND2 1 
ATOM   1040 N  N   . GLU A 1 132 ? 19.432 -31.692 16.199  1.00 21.65 ? 132  GLU A N   1 
ATOM   1041 C  CA  . GLU A 1 132 ? 20.499 -30.863 15.701  1.00 21.47 ? 132  GLU A CA  1 
ATOM   1042 C  C   . GLU A 1 132 ? 20.213 -29.365 15.688  1.00 18.93 ? 132  GLU A C   1 
ATOM   1043 O  O   . GLU A 1 132 ? 21.133 -28.539 15.941  1.00 23.06 ? 132  GLU A O   1 
ATOM   1044 C  CB  . GLU A 1 132 ? 20.774 -31.238 14.276  1.00 22.42 ? 132  GLU A CB  1 
ATOM   1045 C  CG  . GLU A 1 132 ? 22.085 -30.661 13.758  1.00 27.99 ? 132  GLU A CG  1 
ATOM   1046 C  CD  . GLU A 1 132 ? 23.318 -31.481 14.166  0.50 35.41 ? 132  GLU A CD  1 
ATOM   1047 O  OE1 . GLU A 1 132 ? 23.158 -32.545 14.809  0.50 39.47 ? 132  GLU A OE1 1 
ATOM   1048 O  OE2 . GLU A 1 132 ? 24.449 -31.063 13.829  0.50 39.72 ? 132  GLU A OE2 1 
ATOM   1049 N  N   . GLU A 1 133 ? 18.981 -29.009 15.336  1.00 17.48 ? 133  GLU A N   1 
ATOM   1050 C  CA  . GLU A 1 133 ? 18.614 -27.600 15.251  1.00 18.25 ? 133  GLU A CA  1 
ATOM   1051 C  C   . GLU A 1 133 ? 18.716 -26.938 16.600  1.00 16.98 ? 133  GLU A C   1 
ATOM   1052 O  O   . GLU A 1 133 ? 18.959 -25.739 16.687  1.00 16.43 ? 133  GLU A O   1 
ATOM   1053 C  CB  . GLU A 1 133 ? 17.207 -27.513 14.687  1.00 19.05 ? 133  GLU A CB  1 
ATOM   1054 C  CG  . GLU A 1 133 ? 16.695 -26.138 14.309  1.00 24.70 ? 133  GLU A CG  1 
ATOM   1055 C  CD  . GLU A 1 133 ? 16.778 -25.879 12.826  0.50 21.84 ? 133  GLU A CD  1 
ATOM   1056 O  OE1 . GLU A 1 133 ? 16.558 -26.812 12.036  0.50 33.25 ? 133  GLU A OE1 1 
ATOM   1057 O  OE2 . GLU A 1 133 ? 17.015 -24.701 12.440  0.50 28.25 ? 133  GLU A OE2 1 
ATOM   1058 N  N   . SER A 1 134 ? 18.565 -27.657 17.692  1.00 16.33 ? 134  SER A N   1 
ATOM   1059 C  CA  . SER A 1 134 ? 18.637 -27.073 19.011  1.00 15.53 ? 134  SER A CA  1 
ATOM   1060 C  C   . SER A 1 134 ? 19.957 -26.352 19.191  1.00 15.90 ? 134  SER A C   1 
ATOM   1061 O  O   . SER A 1 134 ? 19.958 -25.337 19.859  1.00 14.94 ? 134  SER A O   1 
ATOM   1062 C  CB  . SER A 1 134 ? 18.530 -28.159 20.048  1.00 14.87 ? 134  SER A CB  1 
ATOM   1063 O  OG  . SER A 1 134 ? 18.564 -27.593 21.371  1.00 15.97 ? 134  SER A OG  1 
ATOM   1064 N  N   . THR A 1 135 ? 21.014 -26.937 18.609  1.00 16.56 ? 135  THR A N   1 
ATOM   1065 C  CA  . THR A 1 135 ? 22.407 -26.524 18.687  1.00 19.24 ? 135  THR A CA  1 
ATOM   1066 C  C   . THR A 1 135 ? 22.711 -25.327 17.825  1.00 15.47 ? 135  THR A C   1 
ATOM   1067 O  O   . THR A 1 135 ? 23.834 -24.820 17.816  1.00 15.93 ? 135  THR A O   1 
ATOM   1068 C  CB  . THR A 1 135 ? 23.304 -27.817 18.199  1.00 22.46 ? 135  THR A CB  1 
ATOM   1069 O  OG1 A THR A 1 135 ? 23.622 -28.623 19.319  0.50 28.93 ? 135  THR A OG1 1 
ATOM   1070 O  OG1 B THR A 1 135 ? 23.665 -27.810 16.808  0.50 20.96 ? 135  THR A OG1 1 
ATOM   1071 C  CG2 A THR A 1 135 ? 24.529 -27.470 17.364  0.50 25.80 ? 135  THR A CG2 1 
ATOM   1072 C  CG2 B THR A 1 135 ? 22.909 -29.114 18.846  0.50 15.44 ? 135  THR A CG2 1 
ATOM   1073 N  N   . LYS A 1 136 ? 21.744 -24.903 17.034  1.00 14.45 ? 136  LYS A N   1 
ATOM   1074 C  CA  . LYS A 1 136 ? 21.986 -23.849 15.988  1.00 14.85 ? 136  LYS A CA  1 
ATOM   1075 C  C   . LYS A 1 136 ? 20.999 -22.664 16.309  1.00 14.34 ? 136  LYS A C   1 
ATOM   1076 O  O   . LYS A 1 136 ? 21.422 -21.512 16.402  1.00 14.65 ? 136  LYS A O   1 
ATOM   1077 C  CB  . LYS A 1 136 ? 21.743 -24.370 14.584  1.00 18.98 ? 136  LYS A CB  1 
ATOM   1078 C  CG  . LYS A 1 136 ? 22.732 -25.491 14.253  1.00 20.60 ? 136  LYS A CG  1 
ATOM   1079 C  CD  . LYS A 1 136 ? 22.701 -25.977 12.867  0.50 16.66 ? 136  LYS A CD  1 
ATOM   1080 C  CE  . LYS A 1 136 ? 22.737 -24.839 11.872  0.50 19.96 ? 136  LYS A CE  1 
ATOM   1081 N  NZ  . LYS A 1 136 ? 23.095 -25.159 10.479  0.50 18.39 ? 136  LYS A NZ  1 
ATOM   1082 N  N   . THR A 1 137 ? 19.700 -22.931 16.413  1.00 15.52 ? 137  THR A N   1 
ATOM   1083 C  CA  . THR A 1 137 ? 18.675 -21.906 16.568  1.00 13.56 ? 137  THR A CA  1 
ATOM   1084 C  C   . THR A 1 137 ? 17.896 -22.045 17.875  1.00 13.54 ? 137  THR A C   1 
ATOM   1085 O  O   . THR A 1 137 ? 17.040 -21.148 18.177  1.00 14.49 ? 137  THR A O   1 
ATOM   1086 C  CB  . THR A 1 137 ? 17.633 -21.980 15.456  1.00 16.08 ? 137  THR A CB  1 
ATOM   1087 O  OG1 . THR A 1 137 ? 16.940 -23.192 15.627  1.00 17.16 ? 137  THR A OG1 1 
ATOM   1088 C  CG2 . THR A 1 137 ? 18.278 -21.903 14.103  1.00 15.36 ? 137  THR A CG2 1 
ATOM   1089 N  N   . GLY A 1 138 ? 17.971 -23.174 18.618  1.00 13.20 ? 138  GLY A N   1 
ATOM   1090 C  CA  . GLY A 1 138 ? 17.132 -23.429 19.746  1.00 13.84 ? 138  GLY A CA  1 
ATOM   1091 C  C   . GLY A 1 138 ? 15.706 -23.757 19.398  1.00 11.16 ? 138  GLY A C   1 
ATOM   1092 O  O   . GLY A 1 138 ? 14.881 -23.780 20.281  1.00 13.93 ? 138  GLY A O   1 
ATOM   1093 N  N   . ASN A 1 139 ? 15.415 -24.001 18.159  1.00 12.94 ? 139  ASN A N   1 
ATOM   1094 C  CA  . ASN A 1 139 ? 14.057 -24.367 17.702  1.00 13.43 ? 139  ASN A CA  1 
ATOM   1095 C  C   . ASN A 1 139 ? 13.042 -23.272 17.969  1.00 14.53 ? 139  ASN A C   1 
ATOM   1096 O  O   . ASN A 1 139 ? 11.879 -23.525 18.169  1.00 14.88 ? 139  ASN A O   1 
ATOM   1097 C  CB  . ASN A 1 139 ? 13.614 -25.732 18.325  1.00 14.09 ? 139  ASN A CB  1 
ATOM   1098 C  CG  . ASN A 1 139 ? 14.407 -26.882 17.747  1.00 16.97 ? 139  ASN A CG  1 
ATOM   1099 O  OD1 . ASN A 1 139 ? 14.293 -27.138 16.530  1.00 19.14 ? 139  ASN A OD1 1 
ATOM   1100 N  ND2 . ASN A 1 139 ? 15.261 -27.488 18.512  1.00 17.52 ? 139  ASN A ND2 1 
ATOM   1101 N  N   . ALA A 1 140 ? 13.470 -22.008 17.897  1.00 13.36 ? 140  ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 140 ? 12.572 -20.905 18.233  1.00 13.53 ? 140  ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 140 ? 11.672 -20.444 17.066  1.00 14.31 ? 140  ALA A C   1 
ATOM   1104 O  O   . ALA A 1 140 ? 10.853 -19.574 17.262  1.00 14.62 ? 140  ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 140 ? 13.358 -19.718 18.776  1.00 13.58 ? 140  ALA A CB  1 
ATOM   1106 N  N   . GLY A 1 141 ? 11.846 -21.012 15.878  1.00 14.53 ? 141  GLY A N   1 
ATOM   1107 C  CA  . GLY A 1 141 ? 10.884 -20.751 14.843  1.00 15.94 ? 141  GLY A CA  1 
ATOM   1108 C  C   . GLY A 1 141 ? 11.095 -19.399 14.159  1.00 14.93 ? 141  GLY A C   1 
ATOM   1109 O  O   . GLY A 1 141 ? 12.184 -18.820 14.140  1.00 13.65 ? 141  GLY A O   1 
ATOM   1110 N  N   . SER A 1 142 ? 9.992  -18.912 13.587  1.00 14.25 ? 142  SER A N   1 
ATOM   1111 C  CA  . SER A 1 142 ? 10.037 -17.756 12.749  1.00 13.22 ? 142  SER A CA  1 
ATOM   1112 C  C   . SER A 1 142 ? 10.271 -16.465 13.547  1.00 12.16 ? 142  SER A C   1 
ATOM   1113 O  O   . SER A 1 142 ? 10.297 -16.450 14.777  1.00 12.63 ? 142  SER A O   1 
ATOM   1114 C  CB  . SER A 1 142 ? 8.718  -17.649 11.963  1.00 14.89 ? 142  SER A CB  1 
ATOM   1115 O  OG  . SER A 1 142 ? 7.673  -17.213 12.723  0.50 11.62 ? 142  SER A OG  1 
ATOM   1116 N  N   . ARG A 1 143 ? 10.499 -15.390 12.817  1.00 12.05 ? 143  ARG A N   1 
ATOM   1117 C  CA  . ARG A 1 143 ? 10.857 -14.109 13.404  1.00 12.79 ? 143  ARG A CA  1 
ATOM   1118 C  C   . ARG A 1 143 ? 9.657  -13.218 13.387  1.00 11.90 ? 143  ARG A C   1 
ATOM   1119 O  O   . ARG A 1 143 ? 9.179  -12.777 12.356  1.00 17.03 ? 143  ARG A O   1 
ATOM   1120 C  CB  . ARG A 1 143 ? 12.019 -13.534 12.612  1.00 11.17 ? 143  ARG A CB  1 
ATOM   1121 C  CG  . ARG A 1 143 ? 13.184 -14.494 12.581  1.00 11.57 ? 143  ARG A CG  1 
ATOM   1122 C  CD  . ARG A 1 143 ? 14.373 -14.061 11.700  1.00 11.91 ? 143  ARG A CD  1 
ATOM   1123 N  NE  . ARG A 1 143 ? 15.335 -15.150 11.598  1.00 12.81 ? 143  ARG A NE  1 
ATOM   1124 C  CZ  . ARG A 1 143 ? 16.563 -15.044 11.169  1.00 11.19 ? 143  ARG A CZ  1 
ATOM   1125 N  NH1 . ARG A 1 143 ? 17.000 -13.876 10.747  1.00 11.07 ? 143  ARG A NH1 1 
ATOM   1126 N  NH2 . ARG A 1 143 ? 17.338 -16.079 11.248  1.00 12.21 ? 143  ARG A NH2 1 
ATOM   1127 N  N   . LEU A 1 144 ? 9.170  -12.882 14.542  1.00 10.75 ? 144  LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 144 ? 7.903  -12.088 14.666  1.00 12.42 ? 144  LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 144 ? 8.137  -10.580 14.589  1.00 10.63 ? 144  LEU A C   1 
ATOM   1130 O  O   . LEU A 1 144 ? 7.352  -9.868  13.991  1.00 12.51 ? 144  LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 144 ? 7.121  -12.405 15.958  1.00 12.24 ? 144  LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 144 ? 6.778  -13.859 16.197  1.00 16.09 ? 144  LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 144 ? 5.861  -14.010 17.438  1.00 19.38 ? 144  LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 144 ? 6.067  -14.360 14.938  1.00 17.71 ? 144  LEU A CD2 1 
ATOM   1135 N  N   . ALA A 1 145 ? 9.256  -10.090 15.154  1.00 11.12 ? 145  ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 145 ? 9.610  -8.708  15.075  1.00 10.96 ? 145  ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 145 ? 11.124 -8.590  15.282  1.00 11.00 ? 145  ALA A C   1 
ATOM   1138 O  O   . ALA A 1 145 ? 11.732 -9.480  15.888  1.00 10.75 ? 145  ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 145 ? 8.822  -7.947  16.107  1.00 12.02 ? 145  ALA A CB  1 
ATOM   1140 N  N   . CYS A 1 146 ? 11.666 -7.490  14.775  1.00 10.15 ? 146  CYS A N   1 
ATOM   1141 C  CA  . CYS A 1 146 ? 13.064 -7.250  14.940  1.00 8.87  ? 146  CYS A CA  1 
ATOM   1142 C  C   . CYS A 1 146 ? 13.312 -5.784  14.733  1.00 9.34  ? 146  CYS A C   1 
ATOM   1143 O  O   . CYS A 1 146 ? 12.493 -5.053  14.286  1.00 10.41 ? 146  CYS A O   1 
ATOM   1144 C  CB  . CYS A 1 146 ? 13.777 -8.069  13.856  1.00 9.88  ? 146  CYS A CB  1 
ATOM   1145 S  SG  . CYS A 1 146 ? 13.414 -7.665  12.131  1.00 12.06 ? 146  CYS A SG  1 
ATOM   1146 N  N   . GLY A 1 147 ? 14.564 -5.405  14.963  1.00 9.91  ? 147  GLY A N   1 
ATOM   1147 C  CA  . GLY A 1 147 ? 15.052 -4.064  14.689  1.00 9.32  ? 147  GLY A CA  1 
ATOM   1148 C  C   . GLY A 1 147 ? 16.530 -4.041  14.798  1.00 9.15  ? 147  GLY A C   1 
ATOM   1149 O  O   . GLY A 1 147 ? 17.153 -4.912  15.363  1.00 9.65  ? 147  GLY A O   1 
ATOM   1150 N  N   . VAL A 1 148 ? 17.120 -3.015  14.174  1.00 9.13  ? 148  VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 148 ? 18.537 -2.778  14.260  1.00 8.74  ? 148  VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 148 ? 18.857 -2.078  15.576  1.00 9.12  ? 148  VAL A C   1 
ATOM   1153 O  O   . VAL A 1 148 ? 18.225 -1.110  15.916  1.00 11.13 ? 148  VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 148 ? 19.056 -1.960  13.017  1.00 9.79  ? 148  VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 148 ? 20.535 -1.888  13.087  1.00 11.21 ? 148  VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 148 ? 18.650 -2.599  11.705  1.00 11.91 ? 148  VAL A CG2 1 
ATOM   1157 N  N   . ILE A 1 149 ? 19.907 -2.490  16.240  1.00 9.66  ? 149  ILE A N   1 
ATOM   1158 C  CA  . ILE A 1 149 ? 20.346 -1.943  17.493  1.00 9.44  ? 149  ILE A CA  1 
ATOM   1159 C  C   . ILE A 1 149 ? 21.122 -0.694  17.222  1.00 10.07 ? 149  ILE A C   1 
ATOM   1160 O  O   . ILE A 1 149 ? 22.155 -0.726  16.557  1.00 10.70 ? 149  ILE A O   1 
ATOM   1161 C  CB  . ILE A 1 149 ? 21.120 -2.981  18.324  1.00 9.73  ? 149  ILE A CB  1 
ATOM   1162 C  CG1 . ILE A 1 149 ? 20.236 -4.192  18.572  1.00 10.27 ? 149  ILE A CG1 1 
ATOM   1163 C  CG2 . ILE A 1 149 ? 21.602 -2.350  19.596  1.00 10.37 ? 149  ILE A CG2 1 
ATOM   1164 C  CD1 . ILE A 1 149 ? 21.046 -5.428  19.092  1.00 11.49 ? 149  ILE A CD1 1 
ATOM   1165 N  N   . GLY A 1 150 ? 20.689 0.419   17.745  1.00 9.13  ? 150  GLY A N   1 
ATOM   1166 C  CA  . GLY A 1 150 ? 21.301 1.684   17.533  1.00 10.19 ? 150  GLY A CA  1 
ATOM   1167 C  C   . GLY A 1 150 ? 21.949 2.312   18.735  1.00 9.53  ? 150  GLY A C   1 
ATOM   1168 O  O   . GLY A 1 150 ? 21.539 2.051   19.883  1.00 10.01 ? 150  GLY A O   1 
ATOM   1169 N  N   . ILE A 1 151 ? 22.892 3.224   18.547  1.00 9.86  ? 151  ILE A N   1 
ATOM   1170 C  CA  . ILE A 1 151 ? 23.447 4.011   19.620  1.00 10.21 ? 151  ILE A CA  1 
ATOM   1171 C  C   . ILE A 1 151 ? 22.414 4.989   20.133  1.00 10.68 ? 151  ILE A C   1 
ATOM   1172 O  O   . ILE A 1 151 ? 21.722 5.662   19.367  1.00 11.08 ? 151  ILE A O   1 
ATOM   1173 C  CB  . ILE A 1 151 ? 24.674 4.779   19.133  1.00 10.44 ? 151  ILE A CB  1 
ATOM   1174 C  CG1 . ILE A 1 151 ? 25.757 3.897   18.563  1.00 13.37 ? 151  ILE A CG1 1 
ATOM   1175 C  CG2 . ILE A 1 151 ? 25.336 5.637   20.173  1.00 14.22 ? 151  ILE A CG2 1 
ATOM   1176 C  CD1 . ILE A 1 151 ? 26.815 4.595   17.732  1.00 16.09 ? 151  ILE A CD1 1 
ATOM   1177 N  N   . ALA A 1 152 ? 22.327 5.098   21.455  1.00 10.47 ? 152  ALA A N   1 
ATOM   1178 C  CA  . ALA A 1 152 ? 21.345 5.964   22.100  1.00 11.23 ? 152  ALA A CA  1 
ATOM   1179 C  C   . ALA A 1 152 ? 22.031 7.063   22.902  1.00 12.43 ? 152  ALA A C   1 
ATOM   1180 O  O   . ALA A 1 152 ? 23.210 6.957   23.280  1.00 14.30 ? 152  ALA A O   1 
ATOM   1181 C  CB  . ALA A 1 152 ? 20.412 5.128   23.067  1.00 12.43 ? 152  ALA A CB  1 
ATOM   1182 N  N   . GLN A 1 153 ? 21.261 8.114   23.148  1.00 13.14 ? 153  GLN A N   1 
ATOM   1183 C  CA  . GLN A 1 153 ? 21.682 9.313   23.877  1.00 15.51 ? 153  GLN A CA  1 
ATOM   1184 C  C   . GLN A 1 153 ? 21.895 8.990   25.345  1.00 17.03 ? 153  GLN A C   1 
ATOM   1185 O  O   . GLN A 1 153 ? 21.048 8.298   25.918  1.00 17.34 ? 153  GLN A O   1 
ATOM   1186 C  CB  . GLN A 1 153 ? 20.565 10.357  23.728  1.00 16.74 ? 153  GLN A CB  1 
ATOM   1187 C  CG  . GLN A 1 153 ? 20.786 11.696  24.336  1.00 16.57 ? 153  GLN A CG  1 
ATOM   1188 C  CD  . GLN A 1 153 ? 19.638 12.661  24.095  1.00 17.42 ? 153  GLN A CD  1 
ATOM   1189 O  OE1 . GLN A 1 153 ? 19.090 12.734  22.963  1.00 15.66 ? 153  GLN A OE1 1 
ATOM   1190 N  NE2 . GLN A 1 153 ? 19.400 13.487  25.050  1.00 19.86 ? 153  GLN A NE2 1 
ATOM   1191 O  OXT . GLN A 1 153 ? 22.841 9.434   25.919  1.00 21.12 ? 153  GLN A OXT 1 
ATOM   1192 N  N   A ALA B 1 1   ? 31.550 -2.846  9.330   0.50 20.25 ? 1    ALA F N   1 
ATOM   1193 N  N   B ALA B 1 1   ? 35.519 -4.137  2.061   0.50 24.63 ? 1    ALA F N   1 
ATOM   1194 C  CA  A ALA B 1 1   ? 32.610 -3.734  8.746   0.50 19.25 ? 1    ALA F CA  1 
ATOM   1195 C  CA  B ALA B 1 1   ? 35.805 -5.202  3.028   0.50 23.43 ? 1    ALA F CA  1 
ATOM   1196 C  C   A ALA B 1 1   ? 33.196 -3.186  7.460   0.50 17.36 ? 1    ALA F C   1 
ATOM   1197 C  C   B ALA B 1 1   ? 34.909 -5.026  4.246   0.50 21.07 ? 1    ALA F C   1 
ATOM   1198 O  O   A ALA B 1 1   ? 33.780 -2.116  7.423   0.50 17.25 ? 1    ALA F O   1 
ATOM   1199 O  O   B ALA B 1 1   ? 34.899 -5.869  5.114   0.50 22.80 ? 1    ALA F O   1 
ATOM   1200 C  CB  A ALA B 1 1   ? 32.020 -5.031  8.498   0.50 21.70 ? 1    ALA F CB  1 
ATOM   1201 C  CB  B ALA B 1 1   ? 37.288 -5.249  3.395   0.50 21.66 ? 1    ALA F CB  1 
ATOM   1202 N  N   A THR B 1 2   ? 32.970 -3.899  6.378   0.50 14.47 ? 2    THR F N   1 
ATOM   1203 N  N   B THR B 1 2   ? 34.118 -3.946  4.250   0.50 16.10 ? 2    THR F N   1 
ATOM   1204 C  CA  A THR B 1 2   ? 33.166 -3.251  5.074   0.50 15.35 ? 2    THR F CA  1 
ATOM   1205 C  CA  B THR B 1 2   ? 33.064 -3.658  5.201   0.50 15.97 ? 2    THR F CA  1 
ATOM   1206 C  C   A THR B 1 2   ? 31.851 -3.108  4.275   0.50 12.62 ? 2    THR F C   1 
ATOM   1207 C  C   B THR B 1 2   ? 31.884 -3.080  4.443   0.50 13.57 ? 2    THR F C   1 
ATOM   1208 O  O   A THR B 1 2   ? 31.838 -2.527  3.205   0.50 12.84 ? 2    THR F O   1 
ATOM   1209 O  O   B THR B 1 2   ? 32.024 -2.194  3.589   0.50 12.59 ? 2    THR F O   1 
ATOM   1210 C  CB  A THR B 1 2   ? 34.421 -3.671  4.246   0.50 19.95 ? 2    THR F CB  1 
ATOM   1211 C  CB  B THR B 1 2   ? 33.430 -2.583  6.305   0.50 18.97 ? 2    THR F CB  1 
ATOM   1212 O  OG1 A THR B 1 2   ? 34.044 -4.146  2.942   0.50 29.91 ? 2    THR F OG1 1 
ATOM   1213 O  OG1 B THR B 1 2   ? 34.702 -2.883  6.906   0.50 23.78 ? 2    THR F OG1 1 
ATOM   1214 C  CG2 A THR B 1 2   ? 35.360 -4.670  4.945   0.50 18.97 ? 2    THR F CG2 1 
ATOM   1215 C  CG2 B THR B 1 2   ? 32.324 -2.513  7.371   0.50 24.32 ? 2    THR F CG2 1 
ATOM   1216 N  N   . LYS B 1 3   ? 30.714 -3.551  4.831   1.00 11.88 ? 3    LYS F N   1 
ATOM   1217 C  CA  . LYS B 1 3   ? 29.405 -3.255  4.241   1.00 12.00 ? 3    LYS F CA  1 
ATOM   1218 C  C   . LYS B 1 3   ? 28.406 -2.913  5.273   1.00 11.16 ? 3    LYS F C   1 
ATOM   1219 O  O   . LYS B 1 3   ? 28.403 -3.483  6.373   1.00 12.47 ? 3    LYS F O   1 
ATOM   1220 C  CB  . LYS B 1 3   ? 28.911 -4.442  3.409   1.00 13.72 ? 3    LYS F CB  1 
ATOM   1221 C  CG  . LYS B 1 3   ? 29.890 -4.890  2.258   1.00 17.26 ? 3    LYS F CG  1 
ATOM   1222 C  CD  . LYS B 1 3   ? 29.190 -5.888  1.367   1.00 19.51 ? 3    LYS F CD  1 
ATOM   1223 C  CE  . LYS B 1 3   ? 30.098 -6.503  0.274   1.00 23.43 ? 3    LYS F CE  1 
ATOM   1224 N  NZ  . LYS B 1 3   ? 30.889 -5.501  -0.453  1.00 26.93 ? 3    LYS F NZ  1 
ATOM   1225 N  N   . ALA B 1 4   ? 27.497 -1.985  4.940   1.00 11.38 ? 4    ALA F N   1 
ATOM   1226 C  CA  . ALA B 1 4   ? 26.404 -1.608  5.801   1.00 10.21 ? 4    ALA F CA  1 
ATOM   1227 C  C   . ALA B 1 4   ? 25.183 -1.365  4.938   1.00 10.24 ? 4    ALA F C   1 
ATOM   1228 O  O   . ALA B 1 4   ? 25.272 -1.297  3.705   1.00 10.61 ? 4    ALA F O   1 
ATOM   1229 C  CB  . ALA B 1 4   ? 26.766 -0.409  6.623   1.00 10.79 ? 4    ALA F CB  1 
ATOM   1230 N  N   . VAL B 1 5   ? 24.008 -1.273  5.540   1.00 10.14 ? 5    VAL F N   1 
ATOM   1231 C  CA  . VAL B 1 5   ? 22.742 -1.138  4.867   1.00 9.82  ? 5    VAL F CA  1 
ATOM   1232 C  C   . VAL B 1 5   ? 21.811 -0.372  5.756   1.00 9.46  ? 5    VAL F C   1 
ATOM   1233 O  O   . VAL B 1 5   ? 21.904 -0.379  6.993   1.00 10.42 ? 5    VAL F O   1 
ATOM   1234 C  CB  . VAL B 1 5   ? 22.202 -2.535  4.506   1.00 11.07 ? 5    VAL F CB  1 
ATOM   1235 C  CG1 . VAL B 1 5   ? 21.884 -3.383  5.737   1.00 13.70 ? 5    VAL F CG1 1 
ATOM   1236 C  CG2 . VAL B 1 5   ? 21.073 -2.455  3.488   1.00 13.75 ? 5    VAL F CG2 1 
ATOM   1237 N  N   . CYS B 1 6   ? 20.865 0.278   5.119   1.00 10.01 ? 6    CYS F N   1 
ATOM   1238 C  CA  . CYS B 1 6   ? 19.831 1.010   5.789   1.00 9.94  ? 6    CYS F CA  1 
ATOM   1239 C  C   . CYS B 1 6   ? 18.517 0.979   5.054   1.00 9.10  ? 6    CYS F C   1 
ATOM   1240 O  O   . CYS B 1 6   ? 18.463 1.262   3.870   1.00 11.06 ? 6    CYS F O   1 
ATOM   1241 C  CB  . CYS B 1 6   ? 20.214 2.467   5.979   1.00 9.89  ? 6    CYS F CB  1 
ATOM   1242 S  SG  . CYS B 1 6   ? 19.098 3.479   7.001   1.00 11.78 ? 6    CYS F SG  1 
ATOM   1243 N  N   . VAL B 1 7   ? 17.454 0.618   5.753   1.00 10.16 ? 7    VAL F N   1 
ATOM   1244 C  CA  . VAL B 1 7   ? 16.066 0.606   5.224   1.00 11.47 ? 7    VAL F CA  1 
ATOM   1245 C  C   . VAL B 1 7   ? 15.422 1.863   5.697   1.00 10.65 ? 7    VAL F C   1 
ATOM   1246 O  O   . VAL B 1 7   ? 15.204 2.052   6.938   1.00 11.54 ? 7    VAL F O   1 
ATOM   1247 C  CB  . VAL B 1 7   ? 15.292 -0.616  5.738   1.00 12.92 ? 7    VAL F CB  1 
ATOM   1248 C  CG1 . VAL B 1 7   ? 13.895 -0.583  5.179   1.00 15.81 ? 7    VAL F CG1 1 
ATOM   1249 C  CG2 . VAL B 1 7   ? 15.959 -1.926  5.339   1.00 15.71 ? 7    VAL F CG2 1 
ATOM   1250 N  N   . LEU B 1 8   ? 15.095 2.744   4.769   1.00 12.52 ? 8    LEU F N   1 
ATOM   1251 C  CA  . LEU B 1 8   ? 14.418 3.986   5.139   1.00 12.16 ? 8    LEU F CA  1 
ATOM   1252 C  C   . LEU B 1 8   ? 12.909 3.829   5.062   1.00 13.80 ? 8    LEU F C   1 
ATOM   1253 O  O   . LEU B 1 8   ? 12.413 3.392   4.051   1.00 16.04 ? 8    LEU F O   1 
ATOM   1254 C  CB  . LEU B 1 8   ? 14.797 5.112   4.169   1.00 12.44 ? 8    LEU F CB  1 
ATOM   1255 C  CG  . LEU B 1 8   ? 16.264 5.507   4.081   1.00 13.83 ? 8    LEU F CG  1 
ATOM   1256 C  CD1 . LEU B 1 8   ? 16.637 6.384   2.833   1.00 16.16 ? 8    LEU F CD1 1 
ATOM   1257 C  CD2 . LEU B 1 8   ? 16.597 6.171   5.391   1.00 15.22 ? 8    LEU F CD2 1 
ATOM   1258 N  N   . LYS B 1 9   ? 12.222 4.223   6.127   1.00 14.13 ? 9    LYS F N   1 
ATOM   1259 C  CA  . LYS B 1 9   ? 10.744 4.207   6.195   1.00 17.33 ? 9    LYS F CA  1 
ATOM   1260 C  C   . LYS B 1 9   ? 10.221 5.427   6.938   1.00 18.27 ? 9    LYS F C   1 
ATOM   1261 O  O   . LYS B 1 9   ? 10.898 5.942   7.794   1.00 20.31 ? 9    LYS F O   1 
ATOM   1262 C  CB  . LYS B 1 9   ? 10.341 2.972   7.018   1.00 18.39 ? 9    LYS F CB  1 
ATOM   1263 C  CG  . LYS B 1 9   ? 10.559 1.631   6.318   1.00 20.55 ? 9    LYS F CG  1 
ATOM   1264 C  CD  . LYS B 1 9   ? 9.648  0.499   6.862   1.00 26.29 ? 9    LYS F CD  1 
ATOM   1265 C  CE  . LYS B 1 9   ? 9.587  -0.704  5.832   1.00 30.33 ? 9    LYS F CE  1 
ATOM   1266 N  NZ  . LYS B 1 9   ? 10.838 -1.495  5.848   1.00 37.04 ? 9    LYS F NZ  1 
ATOM   1267 N  N   A GLY B 1 10  ? 9.260  5.938   6.068   0.50 15.81 ? 10   GLY F N   1 
ATOM   1268 N  N   B GLY B 1 10  ? 8.943  5.654   7.147   0.50 15.33 ? 10   GLY F N   1 
ATOM   1269 C  CA  A GLY B 1 10  ? 8.335  7.052   6.292   0.50 12.82 ? 10   GLY F CA  1 
ATOM   1270 C  CA  B GLY B 1 10  ? 8.517  6.751   8.068   0.50 14.94 ? 10   GLY F CA  1 
ATOM   1271 C  C   A GLY B 1 10  ? 7.014  7.157   5.509   0.50 12.46 ? 10   GLY F C   1 
ATOM   1272 C  C   B GLY B 1 10  ? 7.025  6.703   8.285   0.50 15.84 ? 10   GLY F C   1 
ATOM   1273 O  O   A GLY B 1 10  ? 6.771  6.497   4.493   0.50 13.04 ? 10   GLY F O   1 
ATOM   1274 O  O   B GLY B 1 10  ? 6.386  5.665   8.094   0.50 18.06 ? 10   GLY F O   1 
ATOM   1275 N  N   A ASP B 1 11  ? 6.180  8.052   6.003   0.70 14.46 ? 11   ASP F N   1 
ATOM   1276 N  N   B ASP B 1 11  ? 6.485  7.844   8.679   0.30 13.17 ? 11   ASP F N   1 
ATOM   1277 C  CA  A ASP B 1 11  ? 4.805  8.261   5.475   0.70 16.41 ? 11   ASP F CA  1 
ATOM   1278 C  CA  B ASP B 1 11  ? 5.042  8.006   8.882   0.30 14.94 ? 11   ASP F CA  1 
ATOM   1279 C  C   A ASP B 1 11  ? 4.911  8.642   3.978   0.70 15.58 ? 11   ASP F C   1 
ATOM   1280 C  C   B ASP B 1 11  ? 4.220  7.950   7.563   0.30 16.71 ? 11   ASP F C   1 
ATOM   1281 O  O   A ASP B 1 11  ? 5.731  9.494   3.583   0.70 17.12 ? 11   ASP F O   1 
ATOM   1282 O  O   B ASP B 1 11  ? 3.188  7.321   7.526   0.30 18.35 ? 11   ASP F O   1 
ATOM   1283 C  CB  A ASP B 1 11  ? 4.130  9.380   6.245   0.70 15.78 ? 11   ASP F CB  1 
ATOM   1284 C  CB  B ASP B 1 11  ? 4.791  9.291   9.673   0.30 16.95 ? 11   ASP F CB  1 
ATOM   1285 C  CG  A ASP B 1 11  ? 2.872  8.964   6.919   0.70 24.52 ? 11   ASP F CG  1 
ATOM   1286 C  CG  B ASP B 1 11  ? 3.423  9.328   10.283  0.30 21.37 ? 11   ASP F CG  1 
ATOM   1287 O  OD1 A ASP B 1 11  ? 1.796  9.279   6.361   0.70 32.38 ? 11   ASP F OD1 1 
ATOM   1288 O  OD1 B ASP B 1 11  ? 2.422  9.239   9.536   0.30 31.36 ? 11   ASP F OD1 1 
ATOM   1289 O  OD2 A ASP B 1 11  ? 2.990  8.330   7.983   0.70 28.66 ? 11   ASP F OD2 1 
ATOM   1290 O  OD2 B ASP B 1 11  ? 3.320  9.450   11.518  0.30 27.45 ? 11   ASP F OD2 1 
ATOM   1291 N  N   A GLY B 1 12  ? 4.196  7.947   3.110   0.70 15.67 ? 12   GLY F N   1 
ATOM   1292 N  N   B GLY B 1 12  ? 4.677  8.525   6.460   0.30 16.28 ? 12   GLY F N   1 
ATOM   1293 C  CA  A GLY B 1 12  ? 4.038  8.340   1.714   0.70 16.78 ? 12   GLY F CA  1 
ATOM   1294 C  CA  B GLY B 1 12  ? 3.912  8.430   5.175   0.30 14.98 ? 12   GLY F CA  1 
ATOM   1295 C  C   A GLY B 1 12  ? 3.459  7.241   0.832   0.70 16.87 ? 12   GLY F C   1 
ATOM   1296 C  C   B GLY B 1 12  ? 4.732  7.619   4.180   0.30 13.60 ? 12   GLY F C   1 
ATOM   1297 O  O   A GLY B 1 12  ? 2.381  7.429   0.242   0.70 17.19 ? 12   GLY F O   1 
ATOM   1298 O  O   B GLY B 1 12  ? 4.983  6.469   4.457   0.30 12.69 ? 12   GLY F O   1 
ATOM   1299 N  N   A PRO B 1 13  ? 4.109  6.080   0.769   0.70 18.72 ? 13   PRO F N   1 
ATOM   1300 N  N   B PRO B 1 13  ? 4.820  8.006   2.893   0.30 15.62 ? 13   PRO F N   1 
ATOM   1301 C  CA  A PRO B 1 13  ? 5.348  5.731   1.468   0.70 17.83 ? 13   PRO F CA  1 
ATOM   1302 C  CA  B PRO B 1 13  ? 4.818  7.046   1.756   0.30 16.05 ? 13   PRO F CA  1 
ATOM   1303 C  C   A PRO B 1 13  ? 6.566  6.492   0.957   0.70 16.34 ? 13   PRO F C   1 
ATOM   1304 C  C   B PRO B 1 13  ? 6.289  6.699   1.188   0.30 17.20 ? 13   PRO F C   1 
ATOM   1305 O  O   A PRO B 1 13  ? 6.798  6.463   -0.277  0.70 18.18 ? 13   PRO F O   1 
ATOM   1306 O  O   B PRO B 1 13  ? 6.450  5.938   0.265   0.30 16.76 ? 13   PRO F O   1 
ATOM   1307 C  CB  A PRO B 1 13  ? 5.482  4.207   1.181   0.70 20.60 ? 13   PRO F CB  1 
ATOM   1308 C  CB  B PRO B 1 13  ? 3.998  7.765   0.709   0.30 14.63 ? 13   PRO F CB  1 
ATOM   1309 C  CG  A PRO B 1 13  ? 4.134  3.751   0.731   0.70 20.96 ? 13   PRO F CG  1 
ATOM   1310 C  CG  B PRO B 1 13  ? 4.278  9.211   0.970   0.30 13.33 ? 13   PRO F CG  1 
ATOM   1311 C  CD  A PRO B 1 13  ? 3.620  4.944   -0.027  0.70 20.32 ? 13   PRO F CD  1 
ATOM   1312 C  CD  B PRO B 1 13  ? 4.573  9.382   2.441   0.30 16.28 ? 13   PRO F CD  1 
ATOM   1313 N  N   . VAL B 1 14  ? 7.326  7.203   1.847   1.00 18.73 ? 14   VAL F N   1 
ATOM   1314 C  CA  . VAL B 1 14  ? 8.732  7.418   1.450   1.00 17.74 ? 14   VAL F CA  1 
ATOM   1315 C  C   . VAL B 1 14  ? 9.476  6.192   1.941   1.00 17.23 ? 14   VAL F C   1 
ATOM   1316 O  O   . VAL B 1 14  ? 9.431  5.890   3.144   1.00 22.12 ? 14   VAL F O   1 
ATOM   1317 C  CB  . VAL B 1 14  ? 9.318  8.744   1.996   1.00 15.87 ? 14   VAL F CB  1 
ATOM   1318 C  CG1 . VAL B 1 14  ? 10.792 8.805   1.674   1.00 13.59 ? 14   VAL F CG1 1 
ATOM   1319 C  CG2 . VAL B 1 14  ? 8.582  9.901   1.447   1.00 16.43 ? 14   VAL F CG2 1 
ATOM   1320 N  N   . GLN B 1 15  ? 10.064 5.463   0.997   1.00 19.71 ? 15   GLN F N   1 
ATOM   1321 C  CA  . GLN B 1 15  ? 10.734 4.197   1.329   1.00 23.87 ? 15   GLN F CA  1 
ATOM   1322 C  C   . GLN B 1 15  ? 11.991 4.066   0.532   1.00 21.64 ? 15   GLN F C   1 
ATOM   1323 O  O   . GLN B 1 15  ? 12.035 4.469   -0.651  1.00 21.59 ? 15   GLN F O   1 
ATOM   1324 C  CB  . GLN B 1 15  ? 9.823  3.011   0.980   1.00 23.71 ? 15   GLN F CB  1 
ATOM   1325 C  CG  . GLN B 1 15  ? 8.431  3.033   1.528   1.00 30.55 ? 15   GLN F CG  1 
ATOM   1326 C  CD  . GLN B 1 15  ? 7.730  1.682   1.393   1.00 31.90 ? 15   GLN F CD  1 
ATOM   1327 O  OE1 . GLN B 1 15  ? 7.385  1.229   0.276   1.00 41.64 ? 15   GLN F OE1 1 
ATOM   1328 N  NE2 . GLN B 1 15  ? 7.544  1.013   2.530   1.00 38.38 ? 15   GLN F NE2 1 
ATOM   1329 N  N   . GLY B 1 16  ? 13.030 3.512   1.125   1.00 17.38 ? 16   GLY F N   1 
ATOM   1330 C  CA  . GLY B 1 16  ? 14.214 3.337   0.357   1.00 20.88 ? 16   GLY F CA  1 
ATOM   1331 C  C   . GLY B 1 16  ? 15.140 2.331   0.973   1.00 16.27 ? 16   GLY F C   1 
ATOM   1332 O  O   . GLY B 1 16  ? 14.945 1.915   2.106   1.00 18.56 ? 16   GLY F O   1 
ATOM   1333 N  N   . ILE B 1 17  ? 16.072 1.868   0.195   1.00 14.75 ? 17   ILE F N   1 
ATOM   1334 C  CA  . ILE B 1 17  ? 17.157 1.026   0.648   1.00 14.41 ? 17   ILE F CA  1 
ATOM   1335 C  C   . ILE B 1 17  ? 18.461 1.645   0.205   1.00 12.47 ? 17   ILE F C   1 
ATOM   1336 O  O   . ILE B 1 17  ? 18.653 1.912   -0.976  1.00 14.49 ? 17   ILE F O   1 
ATOM   1337 C  CB  . ILE B 1 17  ? 17.034 -0.420  0.060   1.00 18.55 ? 17   ILE F CB  1 
ATOM   1338 C  CG1 . ILE B 1 17  ? 15.756 -1.081  0.436   1.00 26.08 ? 17   ILE F CG1 1 
ATOM   1339 C  CG2 . ILE B 1 17  ? 18.227 -1.283  0.338   1.00 19.43 ? 17   ILE F CG2 1 
ATOM   1340 C  CD1 . ILE B 1 17  ? 15.648 -1.433  1.897   1.00 29.56 ? 17   ILE F CD1 1 
ATOM   1341 N  N   . ILE B 1 18  ? 19.376 1.809   1.153   1.00 11.82 ? 18   ILE F N   1 
ATOM   1342 C  CA  . ILE B 1 18  ? 20.688 2.398   0.909   1.00 11.60 ? 18   ILE F CA  1 
ATOM   1343 C  C   . ILE B 1 18  ? 21.748 1.442   1.403   1.00 11.14 ? 18   ILE F C   1 
ATOM   1344 O  O   . ILE B 1 18  ? 21.690 0.967   2.540   1.00 12.13 ? 18   ILE F O   1 
ATOM   1345 C  CB  . ILE B 1 18  ? 20.779 3.764   1.621   1.00 11.02 ? 18   ILE F CB  1 
ATOM   1346 C  CG1 . ILE B 1 18  ? 19.632 4.713   1.157   1.00 13.71 ? 18   ILE F CG1 1 
ATOM   1347 C  CG2 . ILE B 1 18  ? 22.154 4.354   1.447   1.00 12.38 ? 18   ILE F CG2 1 
ATOM   1348 C  CD1 . ILE B 1 18  ? 19.650 5.121   -0.296  1.00 16.01 ? 18   ILE F CD1 1 
ATOM   1349 N  N   . ASN B 1 19  ? 22.684 1.171   0.518   1.00 11.63 ? 19   ASN F N   1 
ATOM   1350 C  CA  . ASN B 1 19  ? 23.829 0.336   0.760   1.00 10.61 ? 19   ASN F CA  1 
ATOM   1351 C  C   . ASN B 1 19  ? 25.084 1.141   0.876   1.00 10.32 ? 19   ASN F C   1 
ATOM   1352 O  O   . ASN B 1 19  ? 25.192 2.172   0.259   1.00 11.80 ? 19   ASN F O   1 
ATOM   1353 C  CB  . ASN B 1 19  ? 23.992 -0.621  -0.439  1.00 13.54 ? 19   ASN F CB  1 
ATOM   1354 C  CG  . ASN B 1 19  ? 22.728 -1.409  -0.720  1.00 17.13 ? 19   ASN F CG  1 
ATOM   1355 O  OD1 . ASN B 1 19  ? 22.312 -2.293  0.053   1.00 19.91 ? 19   ASN F OD1 1 
ATOM   1356 N  ND2 . ASN B 1 19  ? 22.074 -1.052  -1.799  1.00 22.03 ? 19   ASN F ND2 1 
ATOM   1357 N  N   . PHE B 1 20  ? 25.994 0.676   1.728   1.00 10.13 ? 20   PHE F N   1 
ATOM   1358 C  CA  . PHE B 1 20  ? 27.245 1.253   2.023   1.00 10.93 ? 20   PHE F CA  1 
ATOM   1359 C  C   . PHE B 1 20  ? 28.387 0.242   1.812   1.00 11.42 ? 20   PHE F C   1 
ATOM   1360 O  O   . PHE B 1 20  ? 28.227 -0.893  2.269   1.00 11.98 ? 20   PHE F O   1 
ATOM   1361 C  CB  . PHE B 1 20  ? 27.365 1.805   3.436   1.00 10.79 ? 20   PHE F CB  1 
ATOM   1362 C  CG  . PHE B 1 20  ? 26.284 2.846   3.832   1.00 10.86 ? 20   PHE F CG  1 
ATOM   1363 C  CD1 . PHE B 1 20  ? 25.026 2.456   4.185   1.00 10.64 ? 20   PHE F CD1 1 
ATOM   1364 C  CD2 . PHE B 1 20  ? 26.569 4.172   3.853   1.00 11.98 ? 20   PHE F CD2 1 
ATOM   1365 C  CE1 . PHE B 1 20  ? 24.095 3.380   4.601   1.00 11.45 ? 20   PHE F CE1 1 
ATOM   1366 C  CE2 . PHE B 1 20  ? 25.691 5.104   4.192   1.00 11.18 ? 20   PHE F CE2 1 
ATOM   1367 C  CZ  . PHE B 1 20  ? 24.447 4.728   4.559   1.00 11.74 ? 20   PHE F CZ  1 
ATOM   1368 N  N   . GLU B 1 21  ? 29.474 0.649   1.215   1.00 11.29 ? 21   GLU F N   1 
ATOM   1369 C  CA  . GLU B 1 21  ? 30.635 -0.214  1.061   1.00 12.90 ? 21   GLU F CA  1 
ATOM   1370 C  C   . GLU B 1 21  ? 31.913 0.535   1.222   1.00 12.46 ? 21   GLU F C   1 
ATOM   1371 O  O   . GLU B 1 21  ? 32.048 1.584   0.664   1.00 14.14 ? 21   GLU F O   1 
ATOM   1372 C  CB  . GLU B 1 21  ? 30.640 -0.928  -0.291  1.00 16.12 ? 21   GLU F CB  1 
ATOM   1373 C  CG  . GLU B 1 21  ? 31.880 -1.805  -0.480  0.70 20.56 ? 21   GLU F CG  1 
ATOM   1374 C  CD  . GLU B 1 21  ? 31.779 -2.796  -1.621  0.70 22.30 ? 21   GLU F CD  1 
ATOM   1375 O  OE1 . GLU B 1 21  ? 31.042 -2.506  -2.595  0.50 25.22 ? 21   GLU F OE1 1 
ATOM   1376 O  OE2 . GLU B 1 21  ? 32.429 -3.871  -1.488  0.50 26.94 ? 21   GLU F OE2 1 
ATOM   1377 N  N   . GLN B 1 22  ? 32.793 -0.002  2.034   1.00 12.70 ? 22   GLN F N   1 
ATOM   1378 C  CA  . GLN B 1 22  ? 34.092 0.601   2.334   1.00 13.57 ? 22   GLN F CA  1 
ATOM   1379 C  C   . GLN B 1 22  ? 35.155 -0.478  2.244   1.00 15.62 ? 22   GLN F C   1 
ATOM   1380 O  O   . GLN B 1 22  ? 35.264 -1.357  3.062   1.00 17.55 ? 22   GLN F O   1 
ATOM   1381 C  CB  . GLN B 1 22  ? 34.142 1.263   3.701   1.00 12.07 ? 22   GLN F CB  1 
ATOM   1382 C  CG  . GLN B 1 22  ? 35.391 2.015   3.983   1.00 13.55 ? 22   GLN F CG  1 
ATOM   1383 C  CD  . GLN B 1 22  ? 35.370 2.630   5.378   1.00 13.69 ? 22   GLN F CD  1 
ATOM   1384 O  OE1 . GLN B 1 22  ? 34.768 2.068   6.295   1.00 14.99 ? 22   GLN F OE1 1 
ATOM   1385 N  NE2 . GLN B 1 22  ? 36.020 3.760   5.575   1.00 13.93 ? 22   GLN F NE2 1 
ATOM   1386 N  N   . LYS B 1 23  ? 35.869 -0.422  1.142   1.00 19.77 ? 23   LYS F N   1 
ATOM   1387 C  CA  . LYS B 1 23  ? 36.860 -1.431  0.771   1.00 23.50 ? 23   LYS F CA  1 
ATOM   1388 C  C   . LYS B 1 23  ? 37.990 -1.572  1.756   1.00 24.19 ? 23   LYS F C   1 
ATOM   1389 O  O   . LYS B 1 23  ? 38.504 -2.687  1.916   1.00 26.37 ? 23   LYS F O   1 
ATOM   1390 C  CB  . LYS B 1 23  ? 37.355 -1.238  -0.665  1.00 26.50 ? 23   LYS F CB  1 
ATOM   1391 C  CG  . LYS B 1 23  ? 36.319 -1.761  -1.672  1.00 33.76 ? 23   LYS F CG  1 
ATOM   1392 C  CD  . LYS B 1 23  ? 36.927 -2.600  -2.777  0.10 30.22 ? 23   LYS F CD  1 
ATOM   1393 C  CE  . LYS B 1 23  ? 35.905 -3.596  -3.314  0.10 28.01 ? 23   LYS F CE  1 
ATOM   1394 N  NZ  . LYS B 1 23  ? 35.591 -4.669  -2.339  0.10 27.22 ? 23   LYS F NZ  1 
ATOM   1395 N  N   . GLU B 1 24  ? 38.411 -0.476  2.378   1.00 22.77 ? 24   GLU F N   1 
ATOM   1396 C  CA  . GLU B 1 24  ? 39.428 -0.507  3.473   1.00 23.82 ? 24   GLU F CA  1 
ATOM   1397 C  C   . GLU B 1 24  ? 39.194 0.596   4.476   1.00 22.85 ? 24   GLU F C   1 
ATOM   1398 O  O   . GLU B 1 24  ? 38.563 1.599   4.139   1.00 20.56 ? 24   GLU F O   1 
ATOM   1399 C  CB  . GLU B 1 24  ? 40.838 -0.427  2.937   1.00 25.68 ? 24   GLU F CB  1 
ATOM   1400 C  CG  . GLU B 1 24  ? 41.085 0.785   2.027   0.50 19.09 ? 24   GLU F CG  1 
ATOM   1401 C  CD  . GLU B 1 24  ? 41.975 0.444   0.835   0.50 28.26 ? 24   GLU F CD  1 
ATOM   1402 O  OE1 . GLU B 1 24  ? 42.957 -0.319  1.001   0.50 31.12 ? 24   GLU F OE1 1 
ATOM   1403 O  OE2 . GLU B 1 24  ? 41.697 0.933   -0.288  0.50 34.29 ? 24   GLU F OE2 1 
ATOM   1404 N  N   . SER B 1 25  ? 39.647 0.447   5.727   0.70 21.89 ? 25   SER F N   1 
ATOM   1405 C  CA  . SER B 1 25  ? 39.192 1.379   6.776   0.70 20.24 ? 25   SER F CA  1 
ATOM   1406 C  C   . SER B 1 25  ? 39.641 2.793   6.557   0.70 20.35 ? 25   SER F C   1 
ATOM   1407 O  O   . SER B 1 25  ? 39.021 3.721   7.037   0.70 23.89 ? 25   SER F O   1 
ATOM   1408 C  CB  . SER B 1 25  ? 39.593 0.931   8.181   0.70 22.00 ? 25   SER F CB  1 
ATOM   1409 O  OG  . SER B 1 25  ? 40.942 0.623   8.188   0.70 24.69 ? 25   SER F OG  1 
ATOM   1410 N  N   A ASN B 1 26  ? 40.746 2.928   5.830   0.50 20.28 ? 26   ASN F N   1 
ATOM   1411 N  N   B ASN B 1 26  ? 40.721 2.989   5.829   0.50 22.87 ? 26   ASN F N   1 
ATOM   1412 C  CA  A ASN B 1 26  ? 41.286 4.240   5.486   0.50 19.48 ? 26   ASN F CA  1 
ATOM   1413 C  CA  B ASN B 1 26  ? 41.140 4.357   5.559   0.50 24.16 ? 26   ASN F CA  1 
ATOM   1414 C  C   A ASN B 1 26  ? 40.709 4.798   4.174   0.50 15.04 ? 26   ASN F C   1 
ATOM   1415 C  C   B ASN B 1 26  ? 40.262 5.062   4.509   0.50 22.68 ? 26   ASN F C   1 
ATOM   1416 O  O   A ASN B 1 26  ? 41.179 5.818   3.686   0.50 17.31 ? 26   ASN F O   1 
ATOM   1417 O  O   B ASN B 1 26  ? 40.107 6.290   4.550   0.50 21.58 ? 26   ASN F O   1 
ATOM   1418 C  CB  A ASN B 1 26  ? 42.829 4.235   5.576   0.50 17.77 ? 26   ASN F CB  1 
ATOM   1419 C  CB  B ASN B 1 26  ? 42.633 4.368   5.248   0.50 24.92 ? 26   ASN F CB  1 
ATOM   1420 C  CG  A ASN B 1 26  ? 43.471 3.055   4.859   0.50 22.55 ? 26   ASN F CG  1 
ATOM   1421 C  CG  B ASN B 1 26  ? 43.455 4.227   6.501   0.50 24.64 ? 26   ASN F CG  1 
ATOM   1422 O  OD1 A ASN B 1 26  ? 42.780 2.135   4.380   0.50 25.25 ? 26   ASN F OD1 1 
ATOM   1423 O  OD1 B ASN B 1 26  ? 43.042 4.699   7.571   0.50 27.63 ? 26   ASN F OD1 1 
ATOM   1424 N  ND2 A ASN B 1 26  ? 44.806 3.052   4.804   0.50 25.89 ? 26   ASN F ND2 1 
ATOM   1425 N  ND2 B ASN B 1 26  ? 44.616 3.579   6.397   0.50 24.25 ? 26   ASN F ND2 1 
ATOM   1426 N  N   . GLY B 1 27  ? 39.560 4.246   3.731   1.00 18.07 ? 27   GLY F N   1 
ATOM   1427 C  CA  . GLY B 1 27  ? 39.124 4.549   2.387   1.00 16.62 ? 27   GLY F CA  1 
ATOM   1428 C  C   . GLY B 1 27  ? 37.814 5.169   2.258   1.00 15.57 ? 27   GLY F C   1 
ATOM   1429 O  O   . GLY B 1 27  ? 37.063 5.233   3.236   1.00 14.75 ? 27   GLY F O   1 
ATOM   1430 N  N   . PRO B 1 28  ? 37.390 5.561   1.093   1.00 13.93 ? 28   PRO F N   1 
ATOM   1431 C  CA  . PRO B 1 28  ? 36.061 6.132   0.975   1.00 16.25 ? 28   PRO F CA  1 
ATOM   1432 C  C   . PRO B 1 28  ? 34.963 5.113   1.080   1.00 14.80 ? 28   PRO F C   1 
ATOM   1433 O  O   . PRO B 1 28  ? 35.173 3.896   0.864   1.00 14.93 ? 28   PRO F O   1 
ATOM   1434 C  CB  . PRO B 1 28  ? 36.091 6.716   -0.437  1.00 18.83 ? 28   PRO F CB  1 
ATOM   1435 C  CG  . PRO B 1 28  ? 37.026 5.944   -1.130  1.00 19.48 ? 28   PRO F CG  1 
ATOM   1436 C  CD  . PRO B 1 28  ? 38.082 5.530   -0.193  1.00 17.14 ? 28   PRO F CD  1 
ATOM   1437 N  N   . VAL B 1 29  ? 33.758 5.611   1.317   1.00 14.19 ? 29   VAL F N   1 
ATOM   1438 C  CA  . VAL B 1 29  ? 32.563 4.817   1.442   1.00 12.91 ? 29   VAL F CA  1 
ATOM   1439 C  C   . VAL B 1 29  ? 31.712 5.116   0.211   1.00 13.66 ? 29   VAL F C   1 
ATOM   1440 O  O   . VAL B 1 29  ? 31.364 6.280   -0.027  1.00 14.42 ? 29   VAL F O   1 
ATOM   1441 C  CB  . VAL B 1 29  ? 31.804 5.129   2.712   1.00 13.63 ? 29   VAL F CB  1 
ATOM   1442 C  CG1 . VAL B 1 29  ? 30.549 4.178   2.829   1.00 13.79 ? 29   VAL F CG1 1 
ATOM   1443 C  CG2 . VAL B 1 29  ? 32.716 4.986   3.929   1.00 15.01 ? 29   VAL F CG2 1 
ATOM   1444 N  N   . LYS B 1 30  ? 31.314 4.064   -0.500  1.00 13.33 ? 30   LYS F N   1 
ATOM   1445 C  CA  . LYS B 1 30  ? 30.369 4.146   -1.594  1.00 14.69 ? 30   LYS F CA  1 
ATOM   1446 C  C   . LYS B 1 30  ? 29.000 3.996   -0.967  1.00 15.28 ? 30   LYS F C   1 
ATOM   1447 O  O   . LYS B 1 30  ? 28.779 3.096   -0.149  1.00 12.96 ? 30   LYS F O   1 
ATOM   1448 C  CB  . LYS B 1 30  ? 30.618 3.057   -2.621  1.00 17.12 ? 30   LYS F CB  1 
ATOM   1449 C  CG  . LYS B 1 30  ? 31.921 3.285   -3.393  0.50 15.74 ? 30   LYS F CG  1 
ATOM   1450 C  CD  . LYS B 1 30  ? 32.014 2.486   -4.680  0.50 19.60 ? 30   LYS F CD  1 
ATOM   1451 C  CE  . LYS B 1 30  ? 33.471 2.310   -5.088  0.50 18.01 ? 30   LYS F CE  1 
ATOM   1452 N  NZ  . LYS B 1 30  ? 33.701 1.828   -6.513  0.50 23.41 ? 30   LYS F NZ  1 
ATOM   1453 N  N   . VAL B 1 31  ? 28.060 4.860   -1.363  1.00 13.39 ? 31   VAL F N   1 
ATOM   1454 C  CA  . VAL B 1 31  ? 26.709 4.892   -0.876  1.00 13.44 ? 31   VAL F CA  1 
ATOM   1455 C  C   . VAL B 1 31  ? 25.787 4.819   -2.114  1.00 15.32 ? 31   VAL F C   1 
ATOM   1456 O  O   . VAL B 1 31  ? 25.882 5.634   -3.024  1.00 17.75 ? 31   VAL F O   1 
ATOM   1457 C  CB  . VAL B 1 31  ? 26.441 6.172   -0.080  1.00 14.27 ? 31   VAL F CB  1 
ATOM   1458 C  CG1 . VAL B 1 31  ? 25.034 6.196   0.514   1.00 14.25 ? 31   VAL F CG1 1 
ATOM   1459 C  CG2 . VAL B 1 31  ? 27.484 6.392   0.974   1.00 16.09 ? 31   VAL F CG2 1 
ATOM   1460 N  N   . TRP B 1 32  ? 24.887 3.856   -2.128  1.00 14.49 ? 32   TRP F N   1 
ATOM   1461 C  CA  . TRP B 1 32  ? 24.057 3.682   -3.311  1.00 15.57 ? 32   TRP F CA  1 
ATOM   1462 C  C   . TRP B 1 32  ? 22.756 3.004   -3.013  1.00 14.47 ? 32   TRP F C   1 
ATOM   1463 O  O   . TRP B 1 32  ? 22.656 2.179   -2.046  1.00 14.17 ? 32   TRP F O   1 
ATOM   1464 C  CB  . TRP B 1 32  ? 24.830 3.006   -4.450  1.00 16.79 ? 32   TRP F CB  1 
ATOM   1465 C  CG  . TRP B 1 32  ? 24.948 1.585   -4.264  1.00 18.88 ? 32   TRP F CG  1 
ATOM   1466 C  CD1 . TRP B 1 32  ? 24.170 0.620   -4.818  1.00 22.46 ? 32   TRP F CD1 1 
ATOM   1467 C  CD2 . TRP B 1 32  ? 25.984 0.894   -3.532  1.00 16.66 ? 32   TRP F CD2 1 
ATOM   1468 N  NE1 . TRP B 1 32  ? 24.605 -0.600  -4.435  1.00 22.63 ? 32   TRP F NE1 1 
ATOM   1469 C  CE2 . TRP B 1 32  ? 25.682 -0.465  -3.610  1.00 21.37 ? 32   TRP F CE2 1 
ATOM   1470 C  CE3 . TRP B 1 32  ? 27.028 1.316   -2.696  1.00 21.05 ? 32   TRP F CE3 1 
ATOM   1471 C  CZ2 . TRP B 1 32  ? 26.431 -1.410  -3.019  1.00 25.59 ? 32   TRP F CZ2 1 
ATOM   1472 C  CZ3 . TRP B 1 32  ? 27.759 0.362   -2.064  1.00 20.20 ? 32   TRP F CZ3 1 
ATOM   1473 C  CH2 . TRP B 1 32  ? 27.490 -0.984  -2.285  1.00 19.04 ? 32   TRP F CH2 1 
ATOM   1474 N  N   . GLY B 1 33  ? 21.751 3.349   -3.786  1.00 15.29 ? 33   GLY F N   1 
ATOM   1475 C  CA  . GLY B 1 33  ? 20.439 2.743   -3.600  1.00 14.78 ? 33   GLY F CA  1 
ATOM   1476 C  C   . GLY B 1 33  ? 19.377 3.582   -4.197  1.00 16.65 ? 33   GLY F C   1 
ATOM   1477 O  O   . GLY B 1 33  ? 19.684 4.315   -5.151  1.00 19.11 ? 33   GLY F O   1 
ATOM   1478 N  N   . SER B 1 34  ? 18.158 3.470   -3.672  1.00 18.49 ? 34   SER F N   1 
ATOM   1479 C  CA  . SER B 1 34  ? 16.959 4.112   -4.274  1.00 17.73 ? 34   SER F CA  1 
ATOM   1480 C  C   . SER B 1 34  ? 16.033 4.529   -3.181  1.00 17.63 ? 34   SER F C   1 
ATOM   1481 O  O   . SER B 1 34  ? 15.898 3.859   -2.120  1.00 19.86 ? 34   SER F O   1 
ATOM   1482 C  CB  . SER B 1 34  ? 16.241 3.149   -5.278  1.00 19.60 ? 34   SER F CB  1 
ATOM   1483 O  OG  . SER B 1 34  ? 15.011 3.659   -5.722  1.00 27.03 ? 34   SER F OG  1 
ATOM   1484 N  N   . ILE B 1 35  ? 15.408 5.673   -3.415  1.00 17.88 ? 35   ILE F N   1 
ATOM   1485 C  CA  . ILE B 1 35  ? 14.338 6.123   -2.512  1.00 16.03 ? 35   ILE F CA  1 
ATOM   1486 C  C   . ILE B 1 35  ? 13.164 6.502   -3.360  1.00 16.82 ? 35   ILE F C   1 
ATOM   1487 O  O   . ILE B 1 35  ? 13.311 7.241   -4.343  1.00 18.54 ? 35   ILE F O   1 
ATOM   1488 C  CB  . ILE B 1 35  ? 14.718 7.311   -1.640  1.00 16.75 ? 35   ILE F CB  1 
ATOM   1489 C  CG1 . ILE B 1 35  ? 16.054 7.044   -0.939  1.00 14.29 ? 35   ILE F CG1 1 
ATOM   1490 C  CG2 . ILE B 1 35  ? 13.688 7.611   -0.589  1.00 15.93 ? 35   ILE F CG2 1 
ATOM   1491 C  CD1 . ILE B 1 35  ? 16.673 8.274   -0.355  1.00 17.96 ? 35   ILE F CD1 1 
ATOM   1492 N  N   . LYS B 1 36  ? 11.979 6.048   -2.986  1.00 17.79 ? 36   LYS F N   1 
ATOM   1493 C  CA  . LYS B 1 36  ? 10.787 6.348   -3.740  1.00 18.79 ? 36   LYS F CA  1 
ATOM   1494 C  C   . LYS B 1 36  ? 9.793  7.097   -2.872  1.00 16.45 ? 36   LYS F C   1 
ATOM   1495 O  O   . LYS B 1 36  ? 9.910  7.187   -1.646  1.00 18.06 ? 36   LYS F O   1 
ATOM   1496 C  CB  . LYS B 1 36  ? 10.185 5.077   -4.335  1.00 19.87 ? 36   LYS F CB  1 
ATOM   1497 C  CG  . LYS B 1 36  ? 9.619  4.113   -3.347  1.00 22.32 ? 36   LYS F CG  1 
ATOM   1498 C  CD  . LYS B 1 36  ? 9.187  2.823   -4.115  1.00 24.40 ? 36   LYS F CD  1 
ATOM   1499 C  CE  . LYS B 1 36  ? 8.716  1.735   -3.208  0.50 23.88 ? 36   LYS F CE  1 
ATOM   1500 N  NZ  . LYS B 1 36  ? 8.410  0.503   -4.000  0.50 26.97 ? 36   LYS F NZ  1 
ATOM   1501 N  N   . GLY B 1 37  ? 8.773  7.601   -3.529  1.00 17.98 ? 37   GLY F N   1 
ATOM   1502 C  CA  . GLY B 1 37  ? 7.736  8.308   -2.862  1.00 16.20 ? 37   GLY F CA  1 
ATOM   1503 C  C   . GLY B 1 37  ? 7.997  9.761   -2.495  1.00 16.22 ? 37   GLY F C   1 
ATOM   1504 O  O   . GLY B 1 37  ? 7.196  10.373  -1.756  1.00 18.71 ? 37   GLY F O   1 
ATOM   1505 N  N   . LEU B 1 38  ? 9.063  10.344  -3.039  1.00 16.68 ? 38   LEU F N   1 
ATOM   1506 C  CA  . LEU B 1 38  ? 9.463  11.678  -2.769  1.00 15.88 ? 38   LEU F CA  1 
ATOM   1507 C  C   . LEU B 1 38  ? 8.844  12.703  -3.725  1.00 16.41 ? 38   LEU F C   1 
ATOM   1508 O  O   . LEU B 1 38  ? 8.574  12.416  -4.896  1.00 19.99 ? 38   LEU F O   1 
ATOM   1509 C  CB  . LEU B 1 38  ? 10.973 11.770  -2.941  1.00 16.40 ? 38   LEU F CB  1 
ATOM   1510 C  CG  . LEU B 1 38  ? 11.834 11.012  -1.916  1.00 15.23 ? 38   LEU F CG  1 
ATOM   1511 C  CD1 . LEU B 1 38  ? 13.282 10.908  -2.370  1.00 17.37 ? 38   LEU F CD1 1 
ATOM   1512 C  CD2 . LEU B 1 38  ? 11.738 11.787  -0.619  1.00 15.01 ? 38   LEU F CD2 1 
ATOM   1513 N  N   . THR B 1 39  ? 8.670  13.927  -3.271  1.00 15.44 ? 39   THR F N   1 
ATOM   1514 C  CA  . THR B 1 39  ? 8.359  15.011  -4.204  1.00 15.65 ? 39   THR F CA  1 
ATOM   1515 C  C   . THR B 1 39  ? 9.547  15.329  -5.088  1.00 15.99 ? 39   THR F C   1 
ATOM   1516 O  O   . THR B 1 39  ? 10.694 15.184  -4.705  1.00 15.90 ? 39   THR F O   1 
ATOM   1517 C  CB  . THR B 1 39  ? 7.892  16.269  -3.406  1.00 16.65 ? 39   THR F CB  1 
ATOM   1518 O  OG1 . THR B 1 39  ? 8.930  16.653  -2.511  1.00 17.52 ? 39   THR F OG1 1 
ATOM   1519 C  CG2 . THR B 1 39  ? 6.663  16.087  -2.686  1.00 17.26 ? 39   THR F CG2 1 
ATOM   1520 N  N   . GLU B 1 40  ? 9.276  15.797  -6.291  1.00 17.37 ? 40   GLU F N   1 
ATOM   1521 C  CA  . GLU B 1 40  ? 10.317 16.142  -7.222  1.00 17.95 ? 40   GLU F CA  1 
ATOM   1522 C  C   . GLU B 1 40  ? 11.228 17.193  -6.641  1.00 18.13 ? 40   GLU F C   1 
ATOM   1523 O  O   . GLU B 1 40  ? 10.797 18.188  -6.102  1.00 17.10 ? 40   GLU F O   1 
ATOM   1524 C  CB  . GLU B 1 40  ? 9.688  16.643  -8.537  1.00 19.28 ? 40   GLU F CB  1 
ATOM   1525 C  CG  . GLU B 1 40  ? 10.699 17.280  -9.551  1.00 19.83 ? 40   GLU F CG  1 
ATOM   1526 C  CD  . GLU B 1 40  ? 10.083 17.876  -10.738 1.00 20.39 ? 40   GLU F CD  1 
ATOM   1527 O  OE1 . GLU B 1 40  ? 8.930  18.412  -10.601 1.00 27.23 ? 40   GLU F OE1 1 
ATOM   1528 O  OE2 . GLU B 1 40  ? 10.745 17.798  -11.770 1.00 20.87 ? 40   GLU F OE2 1 
ATOM   1529 N  N   . GLY B 1 41  ? 12.524 17.006  -6.802  1.00 16.19 ? 41   GLY F N   1 
ATOM   1530 C  CA  . GLY B 1 41  ? 13.472 18.009  -6.335  1.00 15.40 ? 41   GLY F CA  1 
ATOM   1531 C  C   . GLY B 1 41  ? 14.444 17.446  -5.299  1.00 13.54 ? 41   GLY F C   1 
ATOM   1532 O  O   . GLY B 1 41  ? 14.562 16.271  -5.148  1.00 14.45 ? 41   GLY F O   1 
ATOM   1533 N  N   . LEU B 1 42  ? 15.168 18.374  -4.679  1.00 13.88 ? 42   LEU F N   1 
ATOM   1534 C  CA  . LEU B 1 42  ? 16.184 18.002  -3.751  1.00 12.18 ? 42   LEU F CA  1 
ATOM   1535 C  C   . LEU B 1 42  ? 15.624 17.708  -2.385  1.00 13.44 ? 42   LEU F C   1 
ATOM   1536 O  O   . LEU B 1 42  ? 14.702 18.349  -1.916  1.00 13.35 ? 42   LEU F O   1 
ATOM   1537 C  CB  . LEU B 1 42  ? 17.179 19.168  -3.585  1.00 13.90 ? 42   LEU F CB  1 
ATOM   1538 C  CG  A LEU B 1 42  ? 18.382 19.516  -4.418  0.80 17.59 ? 42   LEU F CG  1 
ATOM   1539 C  CG  B LEU B 1 42  ? 17.930 19.309  -4.939  0.20 8.37  ? 42   LEU F CG  1 
ATOM   1540 C  CD1 A LEU B 1 42  ? 17.892 19.808  -5.692  0.80 13.76 ? 42   LEU F CD1 1 
ATOM   1541 C  CD1 B LEU B 1 42  ? 18.651 20.646  -5.066  0.20 6.70  ? 42   LEU F CD1 1 
ATOM   1542 C  CD2 A LEU B 1 42  ? 19.206 20.713  -3.946  0.80 15.64 ? 42   LEU F CD2 1 
ATOM   1543 C  CD2 B LEU B 1 42  ? 18.901 18.196  -5.216  0.20 5.99  ? 42   LEU F CD2 1 
ATOM   1544 N  N   . HIS B 1 43  ? 16.168 16.719  -1.716  1.00 11.47 ? 43   HIS F N   1 
ATOM   1545 C  CA  . HIS B 1 43  ? 15.837 16.356  -0.328  1.00 11.36 ? 43   HIS F CA  1 
ATOM   1546 C  C   . HIS B 1 43  ? 17.153 16.133  0.424   1.00 11.48 ? 43   HIS F C   1 
ATOM   1547 O  O   . HIS B 1 43  ? 17.973 15.328  0.041   1.00 12.13 ? 43   HIS F O   1 
ATOM   1548 C  CB  . HIS B 1 43  ? 15.031 15.054  -0.347  1.00 11.86 ? 43   HIS F CB  1 
ATOM   1549 C  CG  . HIS B 1 43  ? 13.702 15.193  -0.975  1.00 10.56 ? 43   HIS F CG  1 
ATOM   1550 N  ND1 . HIS B 1 43  ? 12.609 15.578  -0.302  1.00 12.04 ? 43   HIS F ND1 1 
ATOM   1551 C  CD2 . HIS B 1 43  ? 13.350 15.141  -2.295  1.00 13.70 ? 43   HIS F CD2 1 
ATOM   1552 C  CE1 . HIS B 1 43  ? 11.619 15.749  -1.187  1.00 13.69 ? 43   HIS F CE1 1 
ATOM   1553 N  NE2 . HIS B 1 43  ? 12.021 15.427  -2.369  1.00 13.98 ? 43   HIS F NE2 1 
ATOM   1554 N  N   . GLY B 1 44  ? 17.267 16.811  1.545   1.00 11.20 ? 44   GLY F N   1 
ATOM   1555 C  CA  . GLY B 1 44  ? 18.449 16.678  2.371   1.00 11.06 ? 44   GLY F CA  1 
ATOM   1556 C  C   . GLY B 1 44  ? 18.633 15.234  2.827   1.00 10.38 ? 44   GLY F C   1 
ATOM   1557 O  O   . GLY B 1 44  ? 17.660 14.527  3.076   1.00 10.75 ? 44   GLY F O   1 
ATOM   1558 N  N   . PHE B 1 45  ? 19.893 14.894  3.030   1.00 10.77 ? 45   PHE F N   1 
ATOM   1559 C  CA  . PHE B 1 45  ? 20.279 13.488  3.220   1.00 10.87 ? 45   PHE F CA  1 
ATOM   1560 C  C   . PHE B 1 45  ? 21.456 13.404  4.146   1.00 9.95  ? 45   PHE F C   1 
ATOM   1561 O  O   . PHE B 1 45  ? 22.529 13.805  3.782   1.00 10.88 ? 45   PHE F O   1 
ATOM   1562 C  CB  . PHE B 1 45  ? 20.568 12.916  1.831   1.00 11.36 ? 45   PHE F CB  1 
ATOM   1563 C  CG  . PHE B 1 45  ? 20.834 11.417  1.760   1.00 11.15 ? 45   PHE F CG  1 
ATOM   1564 C  CD1 . PHE B 1 45  ? 19.830 10.488  2.084   1.00 13.62 ? 45   PHE F CD1 1 
ATOM   1565 C  CD2 . PHE B 1 45  ? 22.039 10.927  1.307   1.00 12.60 ? 45   PHE F CD2 1 
ATOM   1566 C  CE1 . PHE B 1 45  ? 20.070 9.130   1.942   1.00 14.25 ? 45   PHE F CE1 1 
ATOM   1567 C  CE2 . PHE B 1 45  ? 22.206 9.571   1.174   1.00 13.66 ? 45   PHE F CE2 1 
ATOM   1568 C  CZ  . PHE B 1 45  ? 21.273 8.717   1.472   1.00 13.11 ? 45   PHE F CZ  1 
ATOM   1569 N  N   . HIS B 1 46  ? 21.243 12.972  5.411   1.00 9.20  ? 46   HIS F N   1 
ATOM   1570 C  CA  . HIS B 1 46  ? 22.312 13.019  6.394   1.00 8.92  ? 46   HIS F CA  1 
ATOM   1571 C  C   . HIS B 1 46  ? 22.306 11.831  7.322   1.00 9.00  ? 46   HIS F C   1 
ATOM   1572 O  O   . HIS B 1 46  ? 21.264 11.237  7.561   1.00 9.15  ? 46   HIS F O   1 
ATOM   1573 C  CB  . HIS B 1 46  ? 22.219 14.249  7.331   1.00 10.92 ? 46   HIS F CB  1 
ATOM   1574 C  CG  . HIS B 1 46  ? 21.699 15.486  6.667   1.00 9.61  ? 46   HIS F CG  1 
ATOM   1575 N  ND1 . HIS B 1 46  ? 20.434 15.936  6.976   1.00 10.33 ? 46   HIS F ND1 1 
ATOM   1576 C  CD2 . HIS B 1 46  ? 22.218 16.326  5.720   1.00 12.10 ? 46   HIS F CD2 1 
ATOM   1577 C  CE1 . HIS B 1 46  ? 20.213 16.991  6.203   1.00 11.88 ? 46   HIS F CE1 1 
ATOM   1578 N  NE2 . HIS B 1 46  ? 21.271 17.265  5.459   1.00 12.60 ? 46   HIS F NE2 1 
ATOM   1579 N  N   . VAL B 1 47  ? 23.444 11.543  7.919   1.00 8.71  ? 47   VAL F N   1 
ATOM   1580 C  CA  . VAL B 1 47  ? 23.521 10.649  9.107   1.00 8.23  ? 47   VAL F CA  1 
ATOM   1581 C  C   . VAL B 1 47  ? 23.317 11.507  10.354  1.00 8.81  ? 47   VAL F C   1 
ATOM   1582 O  O   . VAL B 1 47  ? 24.081 12.491  10.559  1.00 9.33  ? 47   VAL F O   1 
ATOM   1583 C  CB  . VAL B 1 47  ? 24.876 9.913   9.130   1.00 8.35  ? 47   VAL F CB  1 
ATOM   1584 C  CG1 . VAL B 1 47  ? 24.876 8.969   10.333  1.00 9.97  ? 47   VAL F CG1 1 
ATOM   1585 C  CG2 . VAL B 1 47  ? 25.058 9.147   7.837   1.00 9.82  ? 47   VAL F CG2 1 
ATOM   1586 N  N   . HIS B 1 48  ? 22.367 11.111  11.168  1.00 9.35  ? 48   HIS F N   1 
ATOM   1587 C  CA  . HIS B 1 48  ? 22.092 11.739  12.481  1.00 9.13  ? 48   HIS F CA  1 
ATOM   1588 C  C   . HIS B 1 48  ? 22.722 10.942  13.575  1.00 11.90 ? 48   HIS F C   1 
ATOM   1589 O  O   . HIS B 1 48  ? 23.025 9.748   13.397  1.00 12.47 ? 48   HIS F O   1 
ATOM   1590 C  CB  . HIS B 1 48  ? 20.595 11.879  12.637  1.00 9.50  ? 48   HIS F CB  1 
ATOM   1591 C  CG  . HIS B 1 48  ? 20.028 12.955  11.758  1.00 10.30 ? 48   HIS F CG  1 
ATOM   1592 N  ND1 . HIS B 1 48  ? 19.318 14.019  12.268  1.00 9.87  ? 48   HIS F ND1 1 
ATOM   1593 C  CD2 . HIS B 1 48  ? 19.995 13.086  10.423  1.00 9.15  ? 48   HIS F CD2 1 
ATOM   1594 C  CE1 . HIS B 1 48  ? 18.941 14.782  11.245  1.00 10.97 ? 48   HIS F CE1 1 
ATOM   1595 N  NE2 . HIS B 1 48  ? 19.351 14.247  10.110  1.00 11.29 ? 48   HIS F NE2 1 
ATOM   1596 N  N   . GLU B 1 49  ? 22.894 11.559  14.701  1.00 10.06 ? 49   GLU F N   1 
ATOM   1597 C  CA  . GLU B 1 49  ? 23.752 11.052  15.718  1.00 11.04 ? 49   GLU F CA  1 
ATOM   1598 C  C   . GLU B 1 49  ? 23.291 9.712   16.357  1.00 12.32 ? 49   GLU F C   1 
ATOM   1599 O  O   . GLU B 1 49  ? 24.122 8.801   16.507  1.00 13.67 ? 49   GLU F O   1 
ATOM   1600 C  CB  . GLU B 1 49  ? 23.790 12.074  16.865  1.00 11.47 ? 49   GLU F CB  1 
ATOM   1601 C  CG  . GLU B 1 49  ? 24.847 11.698  17.901  0.70 10.87 ? 49   GLU F CG  1 
ATOM   1602 C  CD  . GLU B 1 49  ? 24.939 12.674  18.957  0.70 13.83 ? 49   GLU F CD  1 
ATOM   1603 O  OE1 . GLU B 1 49  ? 24.153 13.637  18.967  0.70 15.37 ? 49   GLU F OE1 1 
ATOM   1604 O  OE2 . GLU B 1 49  ? 25.801 12.447  19.847  0.70 18.61 ? 49   GLU F OE2 1 
ATOM   1605 N  N   . PHE B 1 50  ? 22.031 9.581   16.653  1.00 10.92 ? 50   PHE F N   1 
ATOM   1606 C  CA  . PHE B 1 50  ? 21.563 8.409   17.406  1.00 10.69 ? 50   PHE F CA  1 
ATOM   1607 C  C   . PHE B 1 50  ? 20.797 7.471   16.512  1.00 9.54  ? 50   PHE F C   1 
ATOM   1608 O  O   . PHE B 1 50  ? 19.959 7.902   15.698  1.00 11.05 ? 50   PHE F O   1 
ATOM   1609 C  CB  . PHE B 1 50  ? 20.655 8.840   18.566  1.00 12.90 ? 50   PHE F CB  1 
ATOM   1610 C  CG  . PHE B 1 50  ? 21.227 9.940   19.447  1.00 16.67 ? 50   PHE F CG  1 
ATOM   1611 C  CD1 . PHE B 1 50  ? 22.383 9.735   20.109  1.00 18.50 ? 50   PHE F CD1 1 
ATOM   1612 C  CD2 . PHE B 1 50  ? 20.584 11.164  19.578  1.00 19.46 ? 50   PHE F CD2 1 
ATOM   1613 C  CE1 . PHE B 1 50  ? 22.949 10.786  20.891  1.00 19.72 ? 50   PHE F CE1 1 
ATOM   1614 C  CE2 . PHE B 1 50  ? 21.117 12.197  20.379  1.00 17.49 ? 50   PHE F CE2 1 
ATOM   1615 C  CZ  . PHE B 1 50  ? 22.298 11.988  20.956  1.00 19.44 ? 50   PHE F CZ  1 
ATOM   1616 N  N   . GLY B 1 51  ? 21.002 6.182   16.709  1.00 9.32  ? 51   GLY F N   1 
ATOM   1617 C  CA  . GLY B 1 51  ? 20.234 5.108   16.060  1.00 9.24  ? 51   GLY F CA  1 
ATOM   1618 C  C   . GLY B 1 51  ? 19.000 4.766   16.833  1.00 9.90  ? 51   GLY F C   1 
ATOM   1619 O  O   . GLY B 1 51  ? 18.748 3.622   17.148  1.00 11.03 ? 51   GLY F O   1 
ATOM   1620 N  N   . ASP B 1 52  ? 18.281 5.811   17.215  1.00 11.86 ? 52   ASP F N   1 
ATOM   1621 C  CA  . ASP B 1 52  ? 17.110 5.743   18.090  1.00 11.20 ? 52   ASP F CA  1 
ATOM   1622 C  C   . ASP B 1 52  ? 15.882 6.181   17.349  1.00 11.41 ? 52   ASP F C   1 
ATOM   1623 O  O   . ASP B 1 52  ? 15.838 7.337   16.916  1.00 11.71 ? 52   ASP F O   1 
ATOM   1624 C  CB  . ASP B 1 52  ? 17.329 6.668   19.294  1.00 11.49 ? 52   ASP F CB  1 
ATOM   1625 C  CG  . ASP B 1 52  ? 16.272 6.507   20.366  1.00 14.02 ? 52   ASP F CG  1 
ATOM   1626 O  OD1 . ASP B 1 52  ? 15.189 5.938   20.096  1.00 13.77 ? 52   ASP F OD1 1 
ATOM   1627 O  OD2 . ASP B 1 52  ? 16.467 6.964   21.574  1.00 16.25 ? 52   ASP F OD2 1 
ATOM   1628 N  N   . ASN B 1 53  ? 14.977 5.259   17.113  1.00 11.08 ? 53   ASN F N   1 
ATOM   1629 C  CA  . ASN B 1 53  ? 13.691 5.522   16.459  1.00 12.57 ? 53   ASN F CA  1 
ATOM   1630 C  C   . ASN B 1 53  ? 12.508 5.301   17.371  1.00 10.85 ? 53   ASN F C   1 
ATOM   1631 O  O   . ASN B 1 53  ? 11.395 5.115   16.925  1.00 13.50 ? 53   ASN F O   1 
ATOM   1632 C  CB  . ASN B 1 53  ? 13.680 4.726   15.141  1.00 15.62 ? 53   ASN F CB  1 
ATOM   1633 C  CG  A ASN B 1 53  ? 14.810 5.333   14.005  0.50 14.92 ? 53   ASN F CG  1 
ATOM   1634 C  CG  B ASN B 1 53  ? 12.482 5.008   14.240  0.50 12.72 ? 53   ASN F CG  1 
ATOM   1635 O  OD1 A ASN B 1 53  ? 15.670 6.315   14.198  0.50 13.37 ? 53   ASN F OD1 1 
ATOM   1636 O  OD1 B ASN B 1 53  ? 12.335 6.116   13.832  0.50 13.47 ? 53   ASN F OD1 1 
ATOM   1637 N  ND2 A ASN B 1 53  ? 14.847 4.673   12.928  0.50 14.85 ? 53   ASN F ND2 1 
ATOM   1638 N  ND2 B ASN B 1 53  ? 11.590 3.999   14.001  0.50 15.67 ? 53   ASN F ND2 1 
ATOM   1639 N  N   . THR B 1 54  ? 12.782 5.415   18.686  1.00 12.18 ? 54   THR F N   1 
ATOM   1640 C  CA  . THR B 1 54  ? 11.764 5.237   19.690  1.00 13.47 ? 54   THR F CA  1 
ATOM   1641 C  C   . THR B 1 54  ? 10.454 5.939   19.355  1.00 13.87 ? 54   THR F C   1 
ATOM   1642 O  O   . THR B 1 54  ? 9.334  5.365   19.414  1.00 16.13 ? 54   THR F O   1 
ATOM   1643 C  CB  . THR B 1 54  ? 12.219 5.697   21.108  1.00 11.83 ? 54   THR F CB  1 
ATOM   1644 O  OG1 . THR B 1 54  ? 13.289 4.801   21.535  1.00 16.17 ? 54   THR F OG1 1 
ATOM   1645 C  CG2 . THR B 1 54  ? 11.076 5.563   22.135  1.00 14.57 ? 54   THR F CG2 1 
ATOM   1646 N  N   . ALA B 1 55  ? 10.574 7.203   18.999  1.00 13.66 ? 55   ALA F N   1 
ATOM   1647 C  CA  . ALA B 1 55  ? 9.333  8.002   18.834  1.00 14.72 ? 55   ALA F CA  1 
ATOM   1648 C  C   . ALA B 1 55  ? 9.302  8.474   17.395  1.00 14.03 ? 55   ALA F C   1 
ATOM   1649 O  O   . ALA B 1 55  ? 8.735  9.507   17.088  1.00 20.21 ? 55   ALA F O   1 
ATOM   1650 C  CB  . ALA B 1 55  ? 9.340  9.181   19.783  1.00 16.14 ? 55   ALA F CB  1 
ATOM   1651 N  N   . GLY B 1 56  ? 9.946  7.741   16.481  1.00 14.31 ? 56   GLY F N   1 
ATOM   1652 C  CA  . GLY B 1 56  ? 10.104 8.078   15.068  1.00 14.30 ? 56   GLY F CA  1 
ATOM   1653 C  C   . GLY B 1 56  ? 11.443 8.765   14.804  1.00 12.40 ? 56   GLY F C   1 
ATOM   1654 O  O   . GLY B 1 56  ? 12.364 8.699   15.627  1.00 11.91 ? 56   GLY F O   1 
ATOM   1655 N  N   . CYS B 1 57  ? 11.568 9.370   13.631  1.00 12.50 ? 57   CYS F N   1 
ATOM   1656 C  CA  . CYS B 1 57  ? 12.838 9.917   13.234  1.00 11.37 ? 57   CYS F CA  1 
ATOM   1657 C  C   . CYS B 1 57  ? 13.363 11.064  14.049  1.00 11.44 ? 57   CYS F C   1 
ATOM   1658 O  O   . CYS B 1 57  ? 14.528 11.373  14.003  1.00 11.54 ? 57   CYS F O   1 
ATOM   1659 C  CB  . CYS B 1 57  ? 12.736 10.379  11.779  1.00 11.70 ? 57   CYS F CB  1 
ATOM   1660 S  SG  . CYS B 1 57  ? 12.275 9.085   10.563  1.00 14.61 ? 57   CYS F SG  1 
ATOM   1661 N  N   . THR B 1 58  ? 12.484 11.742  14.763  1.00 12.36 ? 58   THR F N   1 
ATOM   1662 C  CA  . THR B 1 58  ? 12.848 12.795  15.692  1.00 13.66 ? 58   THR F CA  1 
ATOM   1663 C  C   . THR B 1 58  ? 13.835 12.291  16.734  1.00 11.81 ? 58   THR F C   1 
ATOM   1664 O  O   . THR B 1 58  ? 14.717 13.041  17.162  1.00 12.78 ? 58   THR F O   1 
ATOM   1665 C  CB  A THR B 1 58  ? 11.690 13.530  16.460  0.50 15.31 ? 58   THR F CB  1 
ATOM   1666 C  CB  B THR B 1 58  ? 11.577 13.404  16.310  0.50 14.47 ? 58   THR F CB  1 
ATOM   1667 O  OG1 A THR B 1 58  ? 12.206 14.668  17.161  0.50 17.87 ? 58   THR F OG1 1 
ATOM   1668 O  OG1 B THR B 1 58  ? 10.750 12.367  16.839  0.50 13.19 ? 58   THR F OG1 1 
ATOM   1669 C  CG2 A THR B 1 58  ? 11.128 12.693  17.520  0.50 13.24 ? 58   THR F CG2 1 
ATOM   1670 C  CG2 B THR B 1 58  ? 10.779 14.087  15.277  0.50 12.04 ? 58   THR F CG2 1 
ATOM   1671 N  N   . SER B 1 59  ? 13.705 11.014  17.134  1.00 11.51 ? 59   SER F N   1 
ATOM   1672 C  CA  . SER B 1 59  ? 14.522 10.481  18.194  1.00 11.46 ? 59   SER F CA  1 
ATOM   1673 C  C   . SER B 1 59  ? 15.993 10.359  17.833  1.00 10.42 ? 59   SER F C   1 
ATOM   1674 O  O   . SER B 1 59  ? 16.826 10.183  18.715  1.00 11.30 ? 59   SER F O   1 
ATOM   1675 C  CB  . SER B 1 59  ? 13.962 9.129   18.653  1.00 10.74 ? 59   SER F CB  1 
ATOM   1676 O  OG  . SER B 1 59  ? 12.654 9.242   19.172  1.00 13.72 ? 59   SER F OG  1 
ATOM   1677 N  N   . ALA B 1 60  ? 16.314 10.488  16.534  1.00 10.31 ? 60   ALA F N   1 
ATOM   1678 C  CA  . ALA B 1 60  ? 17.694 10.331  16.109  1.00 9.47  ? 60   ALA F CA  1 
ATOM   1679 C  C   . ALA B 1 60  ? 18.547 11.556  16.445  1.00 9.83  ? 60   ALA F C   1 
ATOM   1680 O  O   . ALA B 1 60  ? 19.783 11.492  16.293  1.00 10.36 ? 60   ALA F O   1 
ATOM   1681 C  CB  . ALA B 1 60  ? 17.656 10.170  14.580  1.00 9.86  ? 60   ALA F CB  1 
ATOM   1682 N  N   . GLY B 1 61  ? 17.974 12.664  16.857  1.00 9.57  ? 61   GLY F N   1 
ATOM   1683 C  CA  . GLY B 1 61  ? 18.768 13.824  17.277  1.00 10.99 ? 61   GLY F CA  1 
ATOM   1684 C  C   . GLY B 1 61  ? 19.364 14.556  16.105  1.00 9.76  ? 61   GLY F C   1 
ATOM   1685 O  O   . GLY B 1 61  ? 18.839 14.506  14.983  1.00 9.89  ? 61   GLY F O   1 
ATOM   1686 N  N   . PRO B 1 62  ? 20.422 15.347  16.341  1.00 9.86  ? 62   PRO F N   1 
ATOM   1687 C  CA  . PRO B 1 62  ? 20.991 16.232  15.346  1.00 10.50 ? 62   PRO F CA  1 
ATOM   1688 C  C   . PRO B 1 62  ? 21.884 15.484  14.388  1.00 9.74  ? 62   PRO F C   1 
ATOM   1689 O  O   . PRO B 1 62  ? 22.040 14.264  14.510  1.00 9.33  ? 62   PRO F O   1 
ATOM   1690 C  CB  . PRO B 1 62  ? 21.742 17.225  16.210  1.00 12.37 ? 62   PRO F CB  1 
ATOM   1691 C  CG  . PRO B 1 62  ? 22.179 16.410  17.410  1.00 10.97 ? 62   PRO F CG  1 
ATOM   1692 C  CD  . PRO B 1 62  ? 21.128 15.416  17.628  1.00 11.97 ? 62   PRO F CD  1 
ATOM   1693 N  N   . HIS B 1 63  ? 22.440 16.221  13.444  1.00 8.84  ? 63   HIS F N   1 
ATOM   1694 C  CA  . HIS B 1 63  ? 23.407 15.589  12.512  1.00 9.22  ? 63   HIS F CA  1 
ATOM   1695 C  C   . HIS B 1 63  ? 24.578 15.015  13.281  1.00 9.46  ? 63   HIS F C   1 
ATOM   1696 O  O   . HIS B 1 63  ? 25.032 15.597  14.269  1.00 10.17 ? 63   HIS F O   1 
ATOM   1697 C  CB  . HIS B 1 63  ? 23.890 16.604  11.486  1.00 9.63  ? 63   HIS F CB  1 
ATOM   1698 C  CG  . HIS B 1 63  ? 22.800 17.109  10.629  1.00 9.57  ? 63   HIS F CG  1 
ATOM   1699 N  ND1 . HIS B 1 63  ? 23.092 18.065  9.665   1.00 10.69 ? 63   HIS F ND1 1 
ATOM   1700 C  CD2 . HIS B 1 63  ? 21.458 16.946  10.628  1.00 12.18 ? 63   HIS F CD2 1 
ATOM   1701 C  CE1 . HIS B 1 63  ? 21.917 18.421  9.138   1.00 12.63 ? 63   HIS F CE1 1 
ATOM   1702 N  NE2 . HIS B 1 63  ? 20.940 17.693  9.614   1.00 12.20 ? 63   HIS F NE2 1 
ATOM   1703 N  N   . PHE B 1 64  ? 25.052 13.858  12.866  1.00 9.62  ? 64   PHE F N   1 
ATOM   1704 C  CA  . PHE B 1 64  ? 26.261 13.302  13.466  1.00 10.15 ? 64   PHE F CA  1 
ATOM   1705 C  C   . PHE B 1 64  ? 27.457 14.242  13.232  1.00 8.78  ? 64   PHE F C   1 
ATOM   1706 O  O   . PHE B 1 64  ? 27.836 14.580  12.104  1.00 9.15  ? 64   PHE F O   1 
ATOM   1707 C  CB  . PHE B 1 64  ? 26.522 11.932  12.865  1.00 9.73  ? 64   PHE F CB  1 
ATOM   1708 C  CG  . PHE B 1 64  ? 27.757 11.206  13.415  1.00 10.81 ? 64   PHE F CG  1 
ATOM   1709 C  CD1 . PHE B 1 64  ? 28.029 11.131  14.765  1.00 10.77 ? 64   PHE F CD1 1 
ATOM   1710 C  CD2 . PHE B 1 64  ? 28.656 10.570  12.539  1.00 12.17 ? 64   PHE F CD2 1 
ATOM   1711 C  CE1 . PHE B 1 64  ? 29.158 10.460  15.202  1.00 12.64 ? 64   PHE F CE1 1 
ATOM   1712 C  CE2 . PHE B 1 64  ? 29.769 9.883   12.990  1.00 13.13 ? 64   PHE F CE2 1 
ATOM   1713 C  CZ  . PHE B 1 64  ? 30.055 9.843   14.315  1.00 12.58 ? 64   PHE F CZ  1 
ATOM   1714 N  N   . ASN B 1 65  ? 28.015 14.656  14.324  1.00 9.07  ? 65   ASN F N   1 
ATOM   1715 C  CA  . ASN B 1 65  ? 28.963 15.774  14.343  1.00 10.35 ? 65   ASN F CA  1 
ATOM   1716 C  C   . ASN B 1 65  ? 30.035 15.555  15.402  1.00 11.18 ? 65   ASN F C   1 
ATOM   1717 O  O   . ASN B 1 65  ? 30.189 16.368  16.333  1.00 11.82 ? 65   ASN F O   1 
ATOM   1718 C  CB  . ASN B 1 65  ? 28.220 17.104  14.618  1.00 11.59 ? 65   ASN F CB  1 
ATOM   1719 C  CG  . ASN B 1 65  ? 29.108 18.338  14.475  1.00 10.74 ? 65   ASN F CG  1 
ATOM   1720 O  OD1 . ASN B 1 65  ? 30.148 18.323  13.791  1.00 11.61 ? 65   ASN F OD1 1 
ATOM   1721 N  ND2 . ASN B 1 65  ? 28.680 19.424  15.071  1.00 11.55 ? 65   ASN F ND2 1 
ATOM   1722 N  N   . PRO B 1 66  ? 30.851 14.492  15.279  1.00 11.47 ? 66   PRO F N   1 
ATOM   1723 C  CA  . PRO B 1 66  ? 31.824 14.150  16.331  1.00 11.23 ? 66   PRO F CA  1 
ATOM   1724 C  C   . PRO B 1 66  ? 32.939 15.223  16.452  1.00 12.60 ? 66   PRO F C   1 
ATOM   1725 O  O   . PRO B 1 66  ? 33.544 15.275  17.485  1.00 13.59 ? 66   PRO F O   1 
ATOM   1726 C  CB  . PRO B 1 66  ? 32.408 12.834  15.827  1.00 11.99 ? 66   PRO F CB  1 
ATOM   1727 C  CG  . PRO B 1 66  ? 32.221 12.854  14.260  1.00 11.77 ? 66   PRO F CG  1 
ATOM   1728 C  CD  . PRO B 1 66  ? 30.874 13.523  14.149  1.00 11.10 ? 66   PRO F CD  1 
ATOM   1729 N  N   . LEU B 1 67  ? 33.166 16.014  15.399  1.00 11.47 ? 67   LEU F N   1 
ATOM   1730 C  CA  . LEU B 1 67  ? 34.253 17.024  15.361  1.00 13.06 ? 67   LEU F CA  1 
ATOM   1731 C  C   . LEU B 1 67  ? 33.745 18.401  15.765  1.00 12.22 ? 67   LEU F C   1 
ATOM   1732 O  O   . LEU B 1 67  ? 34.497 19.343  15.747  1.00 13.28 ? 67   LEU F O   1 
ATOM   1733 C  CB  . LEU B 1 67  ? 34.959 17.093  14.014  1.00 13.40 ? 67   LEU F CB  1 
ATOM   1734 C  CG  . LEU B 1 67  ? 35.819 15.855  13.738  0.50 12.44 ? 67   LEU F CG  1 
ATOM   1735 C  CD1 . LEU B 1 67  ? 36.176 15.834  12.288  0.50 10.23 ? 67   LEU F CD1 1 
ATOM   1736 C  CD2 . LEU B 1 67  ? 37.120 15.911  14.500  0.50 15.45 ? 67   LEU F CD2 1 
ATOM   1737 N  N   . SER B 1 68  ? 32.464 18.562  16.138  1.00 12.04 ? 68   SER F N   1 
ATOM   1738 C  CA  . SER B 1 68  ? 31.950 19.860  16.549  1.00 11.72 ? 68   SER F CA  1 
ATOM   1739 C  C   . SER B 1 68  ? 32.075 21.006  15.529  1.00 12.88 ? 68   SER F C   1 
ATOM   1740 O  O   . SER B 1 68  ? 32.444 22.118  15.874  1.00 17.33 ? 68   SER F O   1 
ATOM   1741 C  CB  . SER B 1 68  ? 32.521 20.254  17.935  1.00 12.74 ? 68   SER F CB  1 
ATOM   1742 O  OG  . SER B 1 68  ? 32.254 19.283  18.919  1.00 14.04 ? 68   SER F OG  1 
ATOM   1743 N  N   . ARG B 1 69  ? 31.794 20.699  14.275  1.00 12.56 ? 69   ARG F N   1 
ATOM   1744 C  CA  . ARG B 1 69  ? 31.895 21.653  13.140  1.00 13.97 ? 69   ARG F CA  1 
ATOM   1745 C  C   . ARG B 1 69  ? 30.486 22.183  12.854  1.00 13.46 ? 69   ARG F C   1 
ATOM   1746 O  O   . ARG B 1 69  ? 29.457 21.733  13.435  1.00 14.52 ? 69   ARG F O   1 
ATOM   1747 C  CB  . ARG B 1 69  ? 32.499 20.976  11.920  1.00 15.02 ? 69   ARG F CB  1 
ATOM   1748 C  CG  A ARG B 1 69  ? 33.955 20.593  12.219  0.70 20.83 ? 69   ARG F CG  1 
ATOM   1749 C  CG  B ARG B 1 69  ? 33.857 20.341  12.101  0.30 16.16 ? 69   ARG F CG  1 
ATOM   1750 C  CD  A ARG B 1 69  ? 34.784 20.313  11.017  0.70 26.76 ? 69   ARG F CD  1 
ATOM   1751 C  CD  B ARG B 1 69  ? 34.989 21.326  12.058  0.30 15.31 ? 69   ARG F CD  1 
ATOM   1752 N  NE  A ARG B 1 69  ? 36.197 20.182  11.414  0.70 29.91 ? 69   ARG F NE  1 
ATOM   1753 N  NE  B ARG B 1 69  ? 36.256 20.618  11.892  0.30 14.70 ? 69   ARG F NE  1 
ATOM   1754 C  CZ  A ARG B 1 69  ? 37.138 19.566  10.704  0.70 28.06 ? 69   ARG F CZ  1 
ATOM   1755 C  CZ  B ARG B 1 69  ? 37.145 20.401  12.858  0.30 18.53 ? 69   ARG F CZ  1 
ATOM   1756 N  NH1 A ARG B 1 69  ? 36.847 19.005  9.543   0.70 31.76 ? 69   ARG F NH1 1 
ATOM   1757 N  NH1 B ARG B 1 69  ? 36.921 20.838  14.100  0.30 18.17 ? 69   ARG F NH1 1 
ATOM   1758 N  NH2 A ARG B 1 69  ? 38.383 19.478  11.181  0.70 29.44 ? 69   ARG F NH2 1 
ATOM   1759 N  NH2 B ARG B 1 69  ? 38.255 19.726  12.585  0.30 18.95 ? 69   ARG F NH2 1 
ATOM   1760 N  N   . LYS B 1 70  ? 30.409 23.163  11.955  1.00 14.30 ? 70   LYS F N   1 
ATOM   1761 C  CA  . LYS B 1 70  ? 29.149 23.631  11.442  1.00 14.25 ? 70   LYS F CA  1 
ATOM   1762 C  C   . LYS B 1 70  ? 28.701 22.816  10.235  1.00 13.97 ? 70   LYS F C   1 
ATOM   1763 O  O   . LYS B 1 70  ? 29.485 22.130  9.638   1.00 13.34 ? 70   LYS F O   1 
ATOM   1764 C  CB  . LYS B 1 70  ? 29.328 25.113  11.047  1.00 15.34 ? 70   LYS F CB  1 
ATOM   1765 C  CG  . LYS B 1 70  ? 29.500 26.042  12.266  1.00 20.50 ? 70   LYS F CG  1 
ATOM   1766 C  CD  . LYS B 1 70  ? 29.691 27.496  11.889  0.50 19.21 ? 70   LYS F CD  1 
ATOM   1767 C  CE  . LYS B 1 70  ? 29.886 28.327  13.151  0.50 23.13 ? 70   LYS F CE  1 
ATOM   1768 N  NZ  . LYS B 1 70  ? 29.469 29.732  12.949  0.50 26.61 ? 70   LYS F NZ  1 
ATOM   1769 N  N   . HIS B 1 71  ? 27.396 22.879  9.940   1.00 13.29 ? 71   HIS F N   1 
ATOM   1770 C  CA  . HIS B 1 71  ? 26.830 22.178  8.796   1.00 12.37 ? 71   HIS F CA  1 
ATOM   1771 C  C   . HIS B 1 71  ? 27.423 22.654  7.499   1.00 12.04 ? 71   HIS F C   1 
ATOM   1772 O  O   . HIS B 1 71  ? 27.627 23.865  7.259   1.00 13.13 ? 71   HIS F O   1 
ATOM   1773 C  CB  . HIS B 1 71  ? 25.317 22.388  8.823   1.00 11.70 ? 71   HIS F CB  1 
ATOM   1774 C  CG  . HIS B 1 71  ? 24.594 21.739  7.729   1.00 12.10 ? 71   HIS F CG  1 
ATOM   1775 N  ND1 . HIS B 1 71  ? 24.370 20.367  7.735   1.00 10.36 ? 71   HIS F ND1 1 
ATOM   1776 C  CD2 . HIS B 1 71  ? 24.097 22.202  6.566   1.00 12.18 ? 71   HIS F CD2 1 
ATOM   1777 C  CE1 . HIS B 1 71  ? 23.723 20.056  6.617   1.00 11.86 ? 71   HIS F CE1 1 
ATOM   1778 N  NE2 . HIS B 1 71  ? 23.599 21.138  5.870   1.00 12.13 ? 71   HIS F NE2 1 
ATOM   1779 N  N   . GLY B 1 72  ? 27.616 21.755  6.583   1.00 11.79 ? 72   GLY F N   1 
ATOM   1780 C  CA  . GLY B 1 72  ? 27.967 22.078  5.203   1.00 12.32 ? 72   GLY F CA  1 
ATOM   1781 C  C   . GLY B 1 72  ? 27.569 21.038  4.226   1.00 12.42 ? 72   GLY F C   1 
ATOM   1782 O  O   . GLY B 1 72  ? 26.731 20.189  4.536   1.00 13.38 ? 72   GLY F O   1 
ATOM   1783 N  N   . GLY B 1 73  ? 28.057 21.137  2.997   1.00 12.48 ? 73   GLY F N   1 
ATOM   1784 C  CA  . GLY B 1 73  ? 27.871 20.117  1.991   1.00 12.41 ? 73   GLY F CA  1 
ATOM   1785 C  C   . GLY B 1 73  ? 28.963 19.077  2.121   1.00 11.96 ? 73   GLY F C   1 
ATOM   1786 O  O   . GLY B 1 73  ? 30.072 19.342  2.690   1.00 13.79 ? 73   GLY F O   1 
ATOM   1787 N  N   . PRO B 1 74  ? 28.814 17.938  1.398   1.00 12.37 ? 74   PRO F N   1 
ATOM   1788 C  CA  . PRO B 1 74  ? 29.806 16.884  1.459   1.00 13.62 ? 74   PRO F CA  1 
ATOM   1789 C  C   . PRO B 1 74  ? 31.198 17.242  0.938   1.00 13.82 ? 74   PRO F C   1 
ATOM   1790 O  O   . PRO B 1 74  ? 32.163 16.694  1.437   1.00 15.64 ? 74   PRO F O   1 
ATOM   1791 C  CB  . PRO B 1 74  ? 29.118 15.740  0.675   1.00 14.17 ? 74   PRO F CB  1 
ATOM   1792 C  CG  . PRO B 1 74  ? 28.091 16.384  -0.154  1.00 15.93 ? 74   PRO F CG  1 
ATOM   1793 C  CD  . PRO B 1 74  ? 27.616 17.555  0.667   1.00 14.27 ? 74   PRO F CD  1 
ATOM   1794 N  N   . LYS B 1 75  ? 31.264 18.191  0.018   1.00 14.44 ? 75   LYS F N   1 
ATOM   1795 C  CA  . LYS B 1 75  ? 32.577 18.572  -0.527  1.00 16.38 ? 75   LYS F CA  1 
ATOM   1796 C  C   . LYS B 1 75  ? 33.311 19.610  0.302   1.00 15.40 ? 75   LYS F C   1 
ATOM   1797 O  O   . LYS B 1 75  ? 34.456 19.964  -0.031  1.00 24.14 ? 75   LYS F O   1 
ATOM   1798 C  CB  . LYS B 1 75  ? 32.432 19.154  -1.955  1.00 16.22 ? 75   LYS F CB  1 
ATOM   1799 C  CG  . LYS B 1 75  ? 31.727 18.352  -2.901  1.00 18.05 ? 75   LYS F CG  1 
ATOM   1800 C  CD  . LYS B 1 75  ? 31.707 18.965  -4.351  0.50 18.44 ? 75   LYS F CD  1 
ATOM   1801 C  CE  . LYS B 1 75  ? 32.643 18.202  -5.278  0.50 20.74 ? 75   LYS F CE  1 
ATOM   1802 N  NZ  . LYS B 1 75  ? 34.106 18.355  -4.909  0.50 22.85 ? 75   LYS F NZ  1 
ATOM   1803 N  N   . ASP B 1 76  ? 32.672 20.152  1.335   1.00 14.65 ? 76   ASP F N   1 
ATOM   1804 C  CA  . ASP B 1 76  ? 33.225 21.209  2.206   1.00 15.93 ? 76   ASP F CA  1 
ATOM   1805 C  C   . ASP B 1 76  ? 34.072 20.660  3.315   1.00 17.01 ? 76   ASP F C   1 
ATOM   1806 O  O   . ASP B 1 76  ? 33.768 19.645  3.904   1.00 17.44 ? 76   ASP F O   1 
ATOM   1807 C  CB  . ASP B 1 76  ? 32.135 22.087  2.805   1.00 17.77 ? 76   ASP F CB  1 
ATOM   1808 C  CG  . ASP B 1 76  ? 31.280 22.758  1.771   1.00 18.77 ? 76   ASP F CG  1 
ATOM   1809 O  OD1 . ASP B 1 76  ? 31.822 23.136  0.693   1.00 26.65 ? 76   ASP F OD1 1 
ATOM   1810 O  OD2 . ASP B 1 76  ? 30.062 22.960  2.093   1.00 18.93 ? 76   ASP F OD2 1 
ATOM   1811 N  N   . GLU B 1 77  ? 35.196 21.282  3.583   1.00 18.42 ? 77   GLU F N   1 
ATOM   1812 C  CA  . GLU B 1 77  ? 35.952 20.951  4.792   1.00 17.54 ? 77   GLU F CA  1 
ATOM   1813 C  C   . GLU B 1 77  ? 35.132 21.171  6.086   1.00 17.76 ? 77   GLU F C   1 
ATOM   1814 O  O   . GLU B 1 77  ? 35.128 20.312  7.001   1.00 19.57 ? 77   GLU F O   1 
ATOM   1815 C  CB  . GLU B 1 77  ? 37.310 21.673  4.820   1.00 19.95 ? 77   GLU F CB  1 
ATOM   1816 C  CG  . GLU B 1 77  ? 38.183 21.328  6.004   1.00 24.13 ? 77   GLU F CG  1 
ATOM   1817 C  CD  . GLU B 1 77  ? 39.565 21.935  5.884   0.50 23.48 ? 77   GLU F CD  1 
ATOM   1818 O  OE1 . GLU B 1 77  ? 39.695 23.044  5.310   0.50 29.15 ? 77   GLU F OE1 1 
ATOM   1819 O  OE2 . GLU B 1 77  ? 40.511 21.307  6.388   0.50 30.05 ? 77   GLU F OE2 1 
ATOM   1820 N  N   . GLU B 1 78  ? 34.444 22.308  6.149   1.00 17.03 ? 78   GLU F N   1 
ATOM   1821 C  CA  . GLU B 1 78  ? 33.592 22.632  7.277   1.00 16.54 ? 78   GLU F CA  1 
ATOM   1822 C  C   . GLU B 1 78  ? 32.256 21.966  7.011   1.00 15.57 ? 78   GLU F C   1 
ATOM   1823 O  O   . GLU B 1 78  ? 31.414 22.461  6.277   1.00 14.75 ? 78   GLU F O   1 
ATOM   1824 C  CB  . GLU B 1 78  ? 33.417 24.114  7.430   1.00 16.73 ? 78   GLU F CB  1 
ATOM   1825 C  CG  . GLU B 1 78  ? 32.735 24.536  8.696   1.00 17.35 ? 78   GLU F CG  1 
ATOM   1826 C  CD  . GLU B 1 78  ? 33.540 24.298  9.960   1.00 21.16 ? 78   GLU F CD  1 
ATOM   1827 O  OE1 . GLU B 1 78  ? 34.783 24.285  9.862   1.00 27.72 ? 78   GLU F OE1 1 
ATOM   1828 O  OE2 . GLU B 1 78  ? 32.986 24.186  11.049  1.00 24.54 ? 78   GLU F OE2 1 
ATOM   1829 N  N   . ARG B 1 79  ? 32.100 20.803  7.620   1.00 14.38 ? 79   ARG F N   1 
ATOM   1830 C  CA  . ARG B 1 79  ? 30.848 20.037  7.501   1.00 12.37 ? 79   ARG F CA  1 
ATOM   1831 C  C   . ARG B 1 79  ? 30.736 19.190  8.771   1.00 11.89 ? 79   ARG F C   1 
ATOM   1832 O  O   . ARG B 1 79  ? 31.738 18.956  9.476   1.00 12.92 ? 79   ARG F O   1 
ATOM   1833 C  CB  . ARG B 1 79  ? 30.838 19.130  6.272   1.00 12.26 ? 79   ARG F CB  1 
ATOM   1834 C  CG  . ARG B 1 79  ? 31.994 18.165  6.201   1.00 11.87 ? 79   ARG F CG  1 
ATOM   1835 C  CD  . ARG B 1 79  ? 31.892 17.177  5.078   1.00 13.22 ? 79   ARG F CD  1 
ATOM   1836 N  NE  . ARG B 1 79  ? 31.076 15.999  5.448   1.00 11.91 ? 79   ARG F NE  1 
ATOM   1837 C  CZ  . ARG B 1 79  ? 31.000 14.906  4.706   1.00 12.32 ? 79   ARG F CZ  1 
ATOM   1838 N  NH1 . ARG B 1 79  ? 31.648 14.862  3.581   1.00 12.09 ? 79   ARG F NH1 1 
ATOM   1839 N  NH2 . ARG B 1 79  ? 30.468 13.803  5.130   1.00 11.29 ? 79   ARG F NH2 1 
ATOM   1840 N  N   . HIS B 1 80  ? 29.538 18.719  9.066   1.00 11.65 ? 80   HIS F N   1 
ATOM   1841 C  CA  . HIS B 1 80  ? 29.349 17.589  9.958   1.00 10.49 ? 80   HIS F CA  1 
ATOM   1842 C  C   . HIS B 1 80  ? 29.776 16.305  9.287   1.00 9.55  ? 80   HIS F C   1 
ATOM   1843 O  O   . HIS B 1 80  ? 29.625 16.132  8.051   1.00 10.90 ? 80   HIS F O   1 
ATOM   1844 C  CB  . HIS B 1 80  ? 27.895 17.523  10.305  1.00 11.03 ? 80   HIS F CB  1 
ATOM   1845 C  CG  . HIS B 1 80  ? 27.351 18.753  10.935  1.00 11.09 ? 80   HIS F CG  1 
ATOM   1846 N  ND1 . HIS B 1 80  ? 26.045 19.118  10.680  1.00 10.69 ? 80   HIS F ND1 1 
ATOM   1847 C  CD2 . HIS B 1 80  ? 27.847 19.623  11.836  1.00 11.43 ? 80   HIS F CD2 1 
ATOM   1848 C  CE1 . HIS B 1 80  ? 25.791 20.192  11.413  1.00 10.74 ? 80   HIS F CE1 1 
ATOM   1849 N  NE2 . HIS B 1 80  ? 26.861 20.498  12.144  1.00 12.17 ? 80   HIS F NE2 1 
ATOM   1850 N  N   . VAL B 1 81  ? 30.272 15.320  10.085  1.00 10.11 ? 81   VAL F N   1 
ATOM   1851 C  CA  . VAL B 1 81  ? 30.643 14.027  9.446   1.00 10.13 ? 81   VAL F CA  1 
ATOM   1852 C  C   . VAL B 1 81  ? 29.380 13.471  8.721   1.00 9.87  ? 81   VAL F C   1 
ATOM   1853 O  O   . VAL B 1 81  ? 29.455 12.892  7.669   1.00 10.69 ? 81   VAL F O   1 
ATOM   1854 C  CB  . VAL B 1 81  ? 31.158 13.030  10.462  1.00 11.19 ? 81   VAL F CB  1 
ATOM   1855 C  CG1 . VAL B 1 81  ? 31.159 11.617  9.894   1.00 11.16 ? 81   VAL F CG1 1 
ATOM   1856 C  CG2 . VAL B 1 81  ? 32.535 13.470  10.934  1.00 10.69 ? 81   VAL F CG2 1 
ATOM   1857 N  N   . GLY B 1 82  ? 28.192 13.642  9.271   1.00 9.32  ? 82   GLY F N   1 
ATOM   1858 C  CA  . GLY B 1 82  ? 26.934 13.142  8.651   1.00 10.55 ? 82   GLY F CA  1 
ATOM   1859 C  C   . GLY B 1 82  ? 26.401 13.845  7.436   1.00 10.20 ? 82   GLY F C   1 
ATOM   1860 O  O   . GLY B 1 82  ? 25.375 13.445  6.939   1.00 10.29 ? 82   GLY F O   1 
ATOM   1861 N  N   . ASP B 1 83  ? 27.033 14.915  6.997   1.00 10.21 ? 83   ASP F N   1 
ATOM   1862 C  CA  . ASP B 1 83  ? 26.525 15.755  5.936   1.00 10.49 ? 83   ASP F CA  1 
ATOM   1863 C  C   . ASP B 1 83  ? 26.742 15.142  4.551   1.00 10.33 ? 83   ASP F C   1 
ATOM   1864 O  O   . ASP B 1 83  ? 27.776 15.335  3.957   1.00 13.26 ? 83   ASP F O   1 
ATOM   1865 C  CB  . ASP B 1 83  ? 27.114 17.150  6.002   1.00 11.07 ? 83   ASP F CB  1 
ATOM   1866 C  CG  . ASP B 1 83  ? 26.634 17.949  7.172   1.00 10.17 ? 83   ASP F CG  1 
ATOM   1867 O  OD1 . ASP B 1 83  ? 25.547 17.586  7.779   1.00 9.13  ? 83   ASP F OD1 1 
ATOM   1868 O  OD2 . ASP B 1 83  ? 27.224 18.969  7.500   1.00 11.14 ? 83   ASP F OD2 1 
ATOM   1869 N  N   . LEU B 1 84  ? 25.724 14.502  4.024   1.00 9.52  ? 84   LEU F N   1 
ATOM   1870 C  CA  . LEU B 1 84  ? 25.744 13.866  2.701   1.00 9.83  ? 84   LEU F CA  1 
ATOM   1871 C  C   . LEU B 1 84  ? 24.993 14.614  1.637   1.00 10.45 ? 84   LEU F C   1 
ATOM   1872 O  O   . LEU B 1 84  ? 24.784 14.112  0.540   1.00 13.17 ? 84   LEU F O   1 
ATOM   1873 C  CB  . LEU B 1 84  ? 25.367 12.409  2.759   1.00 12.07 ? 84   LEU F CB  1 
ATOM   1874 C  CG  . LEU B 1 84  ? 26.287 11.513  3.630   1.00 11.40 ? 84   LEU F CG  1 
ATOM   1875 C  CD1 . LEU B 1 84  ? 25.699 10.143  3.736   1.00 12.68 ? 84   LEU F CD1 1 
ATOM   1876 C  CD2 . LEU B 1 84  ? 27.668 11.499  3.181   1.00 12.80 ? 84   LEU F CD2 1 
ATOM   1877 N  N   . GLY B 1 85  ? 24.647 15.864  1.931   1.00 11.60 ? 85   GLY F N   1 
ATOM   1878 C  CA  . GLY B 1 85  ? 24.107 16.739  0.860   1.00 11.62 ? 85   GLY F CA  1 
ATOM   1879 C  C   . GLY B 1 85  ? 22.634 16.506  0.606   1.00 10.77 ? 85   GLY F C   1 
ATOM   1880 O  O   . GLY B 1 85  ? 21.821 16.520  1.545   1.00 11.87 ? 85   GLY F O   1 
ATOM   1881 N  N   . ASN B 1 86  ? 22.242 16.314  -0.632  1.00 11.87 ? 86   ASN F N   1 
ATOM   1882 C  CA  . ASN B 1 86  ? 20.889 16.039  -1.073  1.00 11.68 ? 86   ASN F CA  1 
ATOM   1883 C  C   . ASN B 1 86  ? 20.875 14.838  -2.009  1.00 12.54 ? 86   ASN F C   1 
ATOM   1884 O  O   . ASN B 1 86  ? 21.841 14.554  -2.678  1.00 14.62 ? 86   ASN F O   1 
ATOM   1885 C  CB  . ASN B 1 86  ? 20.375 17.233  -1.942  1.00 12.40 ? 86   ASN F CB  1 
ATOM   1886 C  CG  . ASN B 1 86  ? 20.162 18.473  -1.125  1.00 13.62 ? 86   ASN F CG  1 
ATOM   1887 O  OD1 . ASN B 1 86  ? 19.183 18.548  -0.348  1.00 13.54 ? 86   ASN F OD1 1 
ATOM   1888 N  ND2 . ASN B 1 86  ? 21.061 19.404  -1.248  1.00 14.50 ? 86   ASN F ND2 1 
ATOM   1889 N  N   . VAL B 1 87  ? 19.716 14.175  -2.010  1.00 12.00 ? 87   VAL F N   1 
ATOM   1890 C  CA  . VAL B 1 87  ? 19.323 13.263  -3.057  1.00 13.25 ? 87   VAL F CA  1 
ATOM   1891 C  C   . VAL B 1 87  ? 18.312 14.078  -3.877  1.00 12.32 ? 87   VAL F C   1 
ATOM   1892 O  O   . VAL B 1 87  ? 17.647 14.988  -3.413  1.00 13.67 ? 87   VAL F O   1 
ATOM   1893 C  CB  . VAL B 1 87  ? 18.857 11.892  -2.622  1.00 14.52 ? 87   VAL F CB  1 
ATOM   1894 C  CG1 . VAL B 1 87  ? 19.918 11.213  -1.800  1.00 18.15 ? 87   VAL F CG1 1 
ATOM   1895 C  CG2 . VAL B 1 87  ? 17.567 12.046  -1.767  1.00 14.21 ? 87   VAL F CG2 1 
ATOM   1896 N  N   . THR B 1 88  ? 18.166 13.691  -5.118  1.00 15.86 ? 88   THR F N   1 
ATOM   1897 C  CA  . THR B 1 88  ? 17.261 14.357  -6.070  1.00 17.76 ? 88   THR F CA  1 
ATOM   1898 C  C   . THR B 1 88  ? 16.247 13.372  -6.644  1.00 17.04 ? 88   THR F C   1 
ATOM   1899 O  O   . THR B 1 88  ? 16.569 12.326  -7.226  1.00 19.69 ? 88   THR F O   1 
ATOM   1900 C  CB  . THR B 1 88  ? 18.073 15.087  -7.186  1.00 20.71 ? 88   THR F CB  1 
ATOM   1901 O  OG1 . THR B 1 88  ? 18.898 16.085  -6.599  1.00 21.56 ? 88   THR F OG1 1 
ATOM   1902 C  CG2 . THR B 1 88  ? 17.058 15.776  -8.127  1.00 23.85 ? 88   THR F CG2 1 
ATOM   1903 N  N   . ALA B 1 89  ? 14.963 13.657  -6.423  1.00 15.55 ? 89   ALA F N   1 
ATOM   1904 C  CA  . ALA B 1 89  ? 13.893 12.856  -6.949  1.00 16.07 ? 89   ALA F CA  1 
ATOM   1905 C  C   . ALA B 1 89  ? 13.373 13.453  -8.278  1.00 16.31 ? 89   ALA F C   1 
ATOM   1906 O  O   . ALA B 1 89  ? 13.258 14.686  -8.445  1.00 18.32 ? 89   ALA F O   1 
ATOM   1907 C  CB  . ALA B 1 89  ? 12.765 12.844  -5.990  1.00 15.05 ? 89   ALA F CB  1 
ATOM   1908 N  N   . ASP B 1 90  ? 13.112 12.552  -9.194  1.00 20.04 ? 90   ASP F N   1 
ATOM   1909 C  CA  . ASP B 1 90  ? 12.471 12.757  -10.471 1.00 19.65 ? 90   ASP F CA  1 
ATOM   1910 C  C   . ASP B 1 90  ? 10.975 13.049  -10.243 1.00 17.74 ? 90   ASP F C   1 
ATOM   1911 O  O   . ASP B 1 90  ? 10.422 12.899  -9.170  1.00 18.60 ? 90   ASP F O   1 
ATOM   1912 C  CB  . ASP B 1 90  ? 12.718 11.404  -11.261 1.00 19.75 ? 90   ASP F CB  1 
ATOM   1913 C  CG  . ASP B 1 90  ? 12.343 11.399  -12.728 0.50 19.65 ? 90   ASP F CG  1 
ATOM   1914 O  OD1 . ASP B 1 90  ? 13.128 11.856  -13.581 0.50 19.24 ? 90   ASP F OD1 1 
ATOM   1915 O  OD2 . ASP B 1 90  ? 11.303 10.777  -13.027 0.50 23.32 ? 90   ASP F OD2 1 
ATOM   1916 N  N   . LYS B 1 91  ? 10.325 13.400  -11.348 1.00 17.91 ? 91   LYS F N   1 
ATOM   1917 C  CA  . LYS B 1 91  ? 8.831  13.530  -11.334 1.00 17.88 ? 91   LYS F CA  1 
ATOM   1918 C  C   . LYS B 1 91  ? 8.128  12.243  -10.916 1.00 18.54 ? 91   LYS F C   1 
ATOM   1919 O  O   . LYS B 1 91  ? 6.998  12.267  -10.425 1.00 20.29 ? 91   LYS F O   1 
ATOM   1920 C  CB  . LYS B 1 91  ? 8.313  13.886  -12.716 1.00 19.51 ? 91   LYS F CB  1 
ATOM   1921 C  CG  . LYS B 1 91  ? 8.436  15.301  -12.949 1.00 19.88 ? 91   LYS F CG  1 
ATOM   1922 C  CD  . LYS B 1 91  ? 7.329  16.041  -12.200 1.00 18.81 ? 91   LYS F CD  1 
ATOM   1923 C  CE  . LYS B 1 91  ? 7.132  17.417  -12.774 1.00 29.68 ? 91   LYS F CE  1 
ATOM   1924 N  NZ  . LYS B 1 91  ? 6.294  18.190  -11.890 1.00 27.99 ? 91   LYS F NZ  1 
ATOM   1925 N  N   . ASP B 1 92  ? 8.777  11.114  -11.178 1.00 20.57 ? 92   ASP F N   1 
ATOM   1926 C  CA  . ASP B 1 92  ? 8.239  9.826   -10.762 1.00 22.50 ? 92   ASP F CA  1 
ATOM   1927 C  C   . ASP B 1 92  ? 8.398  9.574   -9.245  1.00 22.72 ? 92   ASP F C   1 
ATOM   1928 O  O   . ASP B 1 92  ? 7.935  8.549   -8.749  1.00 24.64 ? 92   ASP F O   1 
ATOM   1929 C  CB  . ASP B 1 92  ? 8.862  8.673   -11.534 1.00 25.97 ? 92   ASP F CB  1 
ATOM   1930 C  CG  . ASP B 1 92  ? 10.386 8.574   -11.354 1.00 32.23 ? 92   ASP F CG  1 
ATOM   1931 O  OD1 . ASP B 1 92  ? 11.000 9.301   -10.490 1.00 26.17 ? 92   ASP F OD1 1 
ATOM   1932 O  OD2 . ASP B 1 92  ? 10.961 7.755   -12.137 1.00 35.74 ? 92   ASP F OD2 1 
ATOM   1933 N  N   . GLY B 1 93  ? 9.012  10.520  -8.541  1.00 20.42 ? 93   GLY F N   1 
ATOM   1934 C  CA  . GLY B 1 93  ? 9.193  10.419  -7.105  1.00 17.74 ? 93   GLY F CA  1 
ATOM   1935 C  C   . GLY B 1 93  ? 10.370 9.580   -6.641  1.00 18.45 ? 93   GLY F C   1 
ATOM   1936 O  O   . GLY B 1 93  ? 10.495 9.356   -5.419  1.00 19.73 ? 93   GLY F O   1 
ATOM   1937 N  N   . VAL B 1 94  ? 11.193 9.116   -7.574  1.00 18.64 ? 94   VAL F N   1 
ATOM   1938 C  CA  . VAL B 1 94  ? 12.350 8.300   -7.232  1.00 20.74 ? 94   VAL F CA  1 
ATOM   1939 C  C   . VAL B 1 94  ? 13.650 9.079   -7.309  1.00 18.26 ? 94   VAL F C   1 
ATOM   1940 O  O   . VAL B 1 94  ? 13.909 9.785   -8.290  1.00 18.22 ? 94   VAL F O   1 
ATOM   1941 C  CB  . VAL B 1 94  ? 12.439 7.083   -8.236  1.00 20.20 ? 94   VAL F CB  1 
ATOM   1942 C  CG1 . VAL B 1 94  ? 13.683 6.228   -8.001  1.00 20.63 ? 94   VAL F CG1 1 
ATOM   1943 C  CG2 . VAL B 1 94  ? 11.130 6.249   -8.189  1.00 21.97 ? 94   VAL F CG2 1 
ATOM   1944 N  N   . ALA B 1 95  ? 14.504 8.886   -6.294  1.00 16.07 ? 95   ALA F N   1 
ATOM   1945 C  CA  . ALA B 1 95  ? 15.887 9.389   -6.256  1.00 16.87 ? 95   ALA F CA  1 
ATOM   1946 C  C   . ALA B 1 95  ? 16.803 8.243   -6.354  1.00 18.47 ? 95   ALA F C   1 
ATOM   1947 O  O   . ALA B 1 95  ? 16.737 7.317   -5.555  1.00 18.76 ? 95   ALA F O   1 
ATOM   1948 C  CB  . ALA B 1 95  ? 16.148 10.151  -4.943  1.00 17.78 ? 95   ALA F CB  1 
ATOM   1949 N  N   . ASP B 1 96  ? 17.674 8.288   -7.356  1.00 19.39 ? 96   ASP F N   1 
ATOM   1950 C  CA  . ASP B 1 96  ? 18.753 7.388   -7.482  1.00 19.37 ? 96   ASP F CA  1 
ATOM   1951 C  C   . ASP B 1 96  ? 19.919 7.906   -6.746  1.00 19.64 ? 96   ASP F C   1 
ATOM   1952 O  O   . ASP B 1 96  ? 20.432 8.996   -7.021  1.00 26.33 ? 96   ASP F O   1 
ATOM   1953 C  CB  . ASP B 1 96  ? 19.084 7.296   -8.893  1.00 17.88 ? 96   ASP F CB  1 
ATOM   1954 C  CG  . ASP B 1 96  ? 18.023 6.539   -9.632  0.50 17.85 ? 96   ASP F CG  1 
ATOM   1955 O  OD1 . ASP B 1 96  ? 17.496 5.528   -9.133  0.50 20.44 ? 96   ASP F OD1 1 
ATOM   1956 O  OD2 . ASP B 1 96  ? 17.712 6.939   -10.748 0.50 27.85 ? 96   ASP F OD2 1 
ATOM   1957 N  N   . VAL B 1 97  ? 20.370 7.120   -5.772  1.00 19.54 ? 97   VAL F N   1 
ATOM   1958 C  CA  . VAL B 1 97  ? 21.414 7.552   -4.888  1.00 19.74 ? 97   VAL F CA  1 
ATOM   1959 C  C   . VAL B 1 97  ? 22.702 6.896   -5.326  1.00 17.96 ? 97   VAL F C   1 
ATOM   1960 O  O   . VAL B 1 97  ? 22.807 5.641   -5.456  1.00 17.30 ? 97   VAL F O   1 
ATOM   1961 C  CB  . VAL B 1 97  ? 21.107 7.221   -3.448  1.00 18.99 ? 97   VAL F CB  1 
ATOM   1962 C  CG1 . VAL B 1 97  ? 22.253 7.679   -2.552  1.00 18.85 ? 97   VAL F CG1 1 
ATOM   1963 C  CG2 . VAL B 1 97  ? 19.787 7.892   -3.041  1.00 19.76 ? 97   VAL F CG2 1 
ATOM   1964 N  N   . SER B 1 98  ? 23.700 7.731   -5.579  1.00 21.69 ? 98   SER F N   1 
ATOM   1965 C  CA  . SER B 1 98  ? 25.000 7.262   -5.962  1.00 20.19 ? 98   SER F CA  1 
ATOM   1966 C  C   . SER B 1 98  ? 26.024 8.312   -5.467  1.00 20.86 ? 98   SER F C   1 
ATOM   1967 O  O   . SER B 1 98  ? 26.208 9.396   -6.064  1.00 25.81 ? 98   SER F O   1 
ATOM   1968 C  CB  . SER B 1 98  ? 25.134 7.000   -7.481  1.00 19.31 ? 98   SER F CB  1 
ATOM   1969 O  OG  . SER B 1 98  ? 26.495 6.704   -7.642  1.00 25.65 ? 98   SER F OG  1 
ATOM   1970 N  N   . ILE B 1 99  ? 26.645 8.028   -4.332  1.00 19.52 ? 99   ILE F N   1 
ATOM   1971 C  CA  . ILE B 1 99  ? 27.514 8.980   -3.582  1.00 18.23 ? 99   ILE F CA  1 
ATOM   1972 C  C   . ILE B 1 99  ? 28.860 8.219   -3.298  1.00 17.15 ? 99   ILE F C   1 
ATOM   1973 O  O   . ILE B 1 99  ? 28.810 6.985   -3.009  1.00 18.01 ? 99   ILE F O   1 
ATOM   1974 C  CB  . ILE B 1 99  ? 26.806 9.415   -2.208  1.00 16.22 ? 99   ILE F CB  1 
ATOM   1975 C  CG1 . ILE B 1 99  ? 25.747 10.492  -2.497  1.00 18.94 ? 99   ILE F CG1 1 
ATOM   1976 C  CG2 . ILE B 1 99  ? 27.791 9.974   -1.190  1.00 21.43 ? 99   ILE F CG2 1 
ATOM   1977 C  CD1 . ILE B 1 99  ? 24.724 10.763  -1.314  1.00 21.84 ? 99   ILE F CD1 1 
ATOM   1978 N  N   . GLU B 1 100 ? 30.002 8.883   -3.308  1.00 16.34 ? 100  GLU F N   1 
ATOM   1979 C  CA  . GLU B 1 100 ? 31.203 8.384   -2.624  1.00 15.82 ? 100  GLU F CA  1 
ATOM   1980 C  C   . GLU B 1 100 ? 31.600 9.464   -1.670  1.00 13.25 ? 100  GLU F C   1 
ATOM   1981 O  O   . GLU B 1 100 ? 31.563 10.649  -1.990  1.00 15.48 ? 100  GLU F O   1 
ATOM   1982 C  CB  . GLU B 1 100 ? 32.343 8.122   -3.588  1.00 20.13 ? 100  GLU F CB  1 
ATOM   1983 C  CG  . GLU B 1 100 ? 33.446 7.357   -3.033  1.00 24.69 ? 100  GLU F CG  1 
ATOM   1984 C  CD  . GLU B 1 100 ? 34.072 6.413   -4.061  1.00 39.58 ? 100  GLU F CD  1 
ATOM   1985 O  OE1 . GLU B 1 100 ? 35.197 5.928   -3.818  1.00 45.46 ? 100  GLU F OE1 1 
ATOM   1986 O  OE2 . GLU B 1 100 ? 33.439 6.152   -5.112  1.00 44.42 ? 100  GLU F OE2 1 
ATOM   1987 N  N   . ASP B 1 101 ? 31.909 9.079   -0.440  1.00 13.19 ? 101  ASP F N   1 
ATOM   1988 C  CA  . ASP B 1 101 ? 32.292 10.044  0.577   1.00 12.27 ? 101  ASP F CA  1 
ATOM   1989 C  C   . ASP B 1 101 ? 33.482 9.582   1.392   1.00 12.88 ? 101  ASP F C   1 
ATOM   1990 O  O   . ASP B 1 101 ? 33.585 8.392   1.740   1.00 14.85 ? 101  ASP F O   1 
ATOM   1991 C  CB  . ASP B 1 101 ? 31.118 10.252  1.533   1.00 14.04 ? 101  ASP F CB  1 
ATOM   1992 C  CG  . ASP B 1 101 ? 31.258 11.509  2.405   1.00 11.76 ? 101  ASP F CG  1 
ATOM   1993 O  OD1 . ASP B 1 101 ? 31.203 12.677  1.827   1.00 13.86 ? 101  ASP F OD1 1 
ATOM   1994 O  OD2 . ASP B 1 101 ? 31.634 11.404  3.596   1.00 12.14 ? 101  ASP F OD2 1 
ATOM   1995 N  N   . SER B 1 102 ? 34.401 10.522  1.680   1.00 14.08 ? 102  SER F N   1 
ATOM   1996 C  CA  . SER B 1 102 ? 35.628 10.226  2.384   1.00 13.56 ? 102  SER F CA  1 
ATOM   1997 C  C   . SER B 1 102 ? 35.598 10.601  3.853   1.00 12.85 ? 102  SER F C   1 
ATOM   1998 O  O   . SER B 1 102 ? 36.592 10.390  4.526   1.00 16.23 ? 102  SER F O   1 
ATOM   1999 C  CB  . SER B 1 102 ? 36.777 10.986  1.671   1.00 17.53 ? 102  SER F CB  1 
ATOM   2000 O  OG  A SER B 1 102 ? 36.970 10.175  0.542   0.60 21.99 ? 102  SER F OG  1 
ATOM   2001 O  OG  B SER B 1 102 ? 36.675 12.300  2.269   0.40 21.01 ? 102  SER F OG  1 
ATOM   2002 N  N   . VAL B 1 103 ? 34.500 11.160  4.305   1.00 12.37 ? 103  VAL F N   1 
ATOM   2003 C  CA  . VAL B 1 103 ? 34.451 11.584  5.690   1.00 12.01 ? 103  VAL F CA  1 
ATOM   2004 C  C   . VAL B 1 103 ? 33.706 10.578  6.597   1.00 11.58 ? 103  VAL F C   1 
ATOM   2005 O  O   . VAL B 1 103 ? 34.164 10.249  7.706   1.00 12.57 ? 103  VAL F O   1 
ATOM   2006 C  CB  . VAL B 1 103 ? 33.927 13.009  5.774   1.00 13.13 ? 103  VAL F CB  1 
ATOM   2007 C  CG1 . VAL B 1 103 ? 33.716 13.485  7.200   1.00 12.79 ? 103  VAL F CG1 1 
ATOM   2008 C  CG2 . VAL B 1 103 ? 34.883 13.992  5.117   1.00 15.20 ? 103  VAL F CG2 1 
ATOM   2009 N  N   . ILE B 1 104 ? 32.552 10.105  6.166   1.00 11.41 ? 104  ILE F N   1 
ATOM   2010 C  CA  . ILE B 1 104 ? 31.926 8.960   6.862   1.00 11.61 ? 104  ILE F CA  1 
ATOM   2011 C  C   . ILE B 1 104 ? 32.871 7.753   6.815   1.00 12.34 ? 104  ILE F C   1 
ATOM   2012 O  O   . ILE B 1 104 ? 33.723 7.678   5.949   1.00 13.51 ? 104  ILE F O   1 
ATOM   2013 C  CB  . ILE B 1 104 ? 30.541 8.640   6.297   1.00 10.07 ? 104  ILE F CB  1 
ATOM   2014 C  CG1 . ILE B 1 104 ? 30.600 8.227   4.829   1.00 12.29 ? 104  ILE F CG1 1 
ATOM   2015 C  CG2 . ILE B 1 104 ? 29.572 9.807   6.544   1.00 11.63 ? 104  ILE F CG2 1 
ATOM   2016 C  CD1 . ILE B 1 104 ? 29.323 7.609   4.284   1.00 11.90 ? 104  ILE F CD1 1 
ATOM   2017 N  N   . SER B 1 105 ? 32.660 6.835   7.748   1.00 11.42 ? 105  SER F N   1 
ATOM   2018 C  CA  . SER B 1 105 ? 33.331 5.576   7.794   1.00 11.65 ? 105  SER F CA  1 
ATOM   2019 C  C   . SER B 1 105 ? 32.469 4.479   8.338   1.00 11.28 ? 105  SER F C   1 
ATOM   2020 O  O   . SER B 1 105 ? 31.474 4.766   8.949   1.00 11.68 ? 105  SER F O   1 
ATOM   2021 C  CB  . SER B 1 105 ? 34.599 5.698   8.632   1.00 13.49 ? 105  SER F CB  1 
ATOM   2022 O  OG  . SER B 1 105 ? 35.433 4.592   8.442   1.00 13.11 ? 105  SER F OG  1 
ATOM   2023 N  N   . LEU B 1 106 ? 32.824 3.243   8.092   1.00 11.68 ? 106  LEU F N   1 
ATOM   2024 C  CA  . LEU B 1 106 ? 32.213 2.074   8.661   1.00 12.79 ? 106  LEU F CA  1 
ATOM   2025 C  C   . LEU B 1 106 ? 32.987 1.470   9.813   1.00 14.03 ? 106  LEU F C   1 
ATOM   2026 O  O   . LEU B 1 106 ? 32.612 0.440   10.333  1.00 16.14 ? 106  LEU F O   1 
ATOM   2027 C  CB  . LEU B 1 106 ? 31.893 1.063   7.562   1.00 13.82 ? 106  LEU F CB  1 
ATOM   2028 C  CG  . LEU B 1 106 ? 31.047 1.518   6.359   1.00 12.79 ? 106  LEU F CG  1 
ATOM   2029 C  CD1 . LEU B 1 106 ? 30.707 0.300   5.463   1.00 15.39 ? 106  LEU F CD1 1 
ATOM   2030 C  CD2 . LEU B 1 106 ? 29.763 2.247   6.795   1.00 13.76 ? 106  LEU F CD2 1 
ATOM   2031 N  N   . SER B 1 107 ? 33.988 2.194   10.276  1.00 16.10 ? 107  SER F N   1 
ATOM   2032 C  CA  . SER B 1 107 ? 34.720 1.867   11.496  1.00 17.77 ? 107  SER F CA  1 
ATOM   2033 C  C   . SER B 1 107 ? 35.352 3.107   12.112  1.00 18.46 ? 107  SER F C   1 
ATOM   2034 O  O   . SER B 1 107 ? 35.399 4.195   11.483  1.00 16.55 ? 107  SER F O   1 
ATOM   2035 C  CB  . SER B 1 107 ? 35.724 0.749   11.277  1.00 21.32 ? 107  SER F CB  1 
ATOM   2036 O  OG  . SER B 1 107 ? 36.730 1.176   10.402  1.00 26.97 ? 107  SER F OG  1 
ATOM   2037 N  N   . GLY B 1 108 ? 35.774 3.013   13.370  1.00 18.63 ? 108  GLY F N   1 
ATOM   2038 C  CA  . GLY B 1 108 ? 36.470 4.172   13.958  1.00 21.08 ? 108  GLY F CA  1 
ATOM   2039 C  C   . GLY B 1 108 ? 35.568 5.253   14.502  1.00 21.71 ? 108  GLY F C   1 
ATOM   2040 O  O   . GLY B 1 108 ? 34.343 5.076   14.624  1.00 20.55 ? 108  GLY F O   1 
ATOM   2041 N  N   . ASP B 1 109 ? 36.163 6.413   14.801  1.00 23.14 ? 109  ASP F N   1 
ATOM   2042 C  CA  . ASP B 1 109 ? 35.460 7.511   15.451  1.00 22.55 ? 109  ASP F CA  1 
ATOM   2043 C  C   . ASP B 1 109 ? 34.385 8.168   14.606  1.00 19.98 ? 109  ASP F C   1 
ATOM   2044 O  O   . ASP B 1 109 ? 33.493 8.879   15.133  1.00 20.18 ? 109  ASP F O   1 
ATOM   2045 C  CB  . ASP B 1 109 ? 36.488 8.604   15.920  1.00 25.23 ? 109  ASP F CB  1 
ATOM   2046 C  CG  . ASP B 1 109 ? 35.940 9.433   17.045  1.00 26.99 ? 109  ASP F CG  1 
ATOM   2047 O  OD1 . ASP B 1 109 ? 35.233 8.831   17.906  1.00 37.18 ? 109  ASP F OD1 1 
ATOM   2048 O  OD2 . ASP B 1 109 ? 36.176 10.649  17.156  1.00 23.25 ? 109  ASP F OD2 1 
ATOM   2049 N  N   . HIS B 1 110 ? 34.561 8.021   13.283  1.00 15.43 ? 110  HIS F N   1 
ATOM   2050 C  CA  . HIS B 1 110 ? 33.599 8.523   12.319  1.00 13.35 ? 110  HIS F CA  1 
ATOM   2051 C  C   . HIS B 1 110 ? 32.668 7.452   11.814  1.00 13.21 ? 110  HIS F C   1 
ATOM   2052 O  O   . HIS B 1 110 ? 31.977 7.656   10.802  1.00 11.44 ? 110  HIS F O   1 
ATOM   2053 C  CB  . HIS B 1 110 ? 34.330 9.284   11.241  1.00 14.53 ? 110  HIS F CB  1 
ATOM   2054 C  CG  . HIS B 1 110 ? 35.097 10.444  11.776  1.00 15.40 ? 110  HIS F CG  1 
ATOM   2055 N  ND1 . HIS B 1 110 ? 36.001 11.168  11.028  1.00 20.95 ? 110  HIS F ND1 1 
ATOM   2056 C  CD2 . HIS B 1 110 ? 35.107 10.989  13.029  1.00 17.74 ? 110  HIS F CD2 1 
ATOM   2057 C  CE1 . HIS B 1 110 ? 36.542 12.100  11.795  1.00 20.12 ? 110  HIS F CE1 1 
ATOM   2058 N  NE2 . HIS B 1 110 ? 35.971 12.058  12.992  1.00 19.53 ? 110  HIS F NE2 1 
ATOM   2059 N  N   . CYS B 1 111 ? 32.613 6.287   12.550  1.00 13.23 ? 111  CYS F N   1 
ATOM   2060 C  CA  . CYS B 1 111 ? 31.763 5.180   12.093  1.00 13.13 ? 111  CYS F CA  1 
ATOM   2061 C  C   . CYS B 1 111 ? 30.336 5.644   12.180  1.00 11.49 ? 111  CYS F C   1 
ATOM   2062 O  O   . CYS B 1 111 ? 29.861 6.229   13.153  1.00 12.95 ? 111  CYS F O   1 
ATOM   2063 C  CB  . CYS B 1 111 ? 31.976 3.993   13.012  1.00 13.61 ? 111  CYS F CB  1 
ATOM   2064 S  SG  . CYS B 1 111 ? 31.098 2.591   12.457  1.00 14.77 ? 111  CYS F SG  1 
ATOM   2065 N  N   . ILE B 1 112 ? 29.533 5.238   11.159  1.00 10.42 ? 112  ILE F N   1 
ATOM   2066 C  CA  . ILE B 1 112 ? 28.076 5.586   11.116  1.00 9.61  ? 112  ILE F CA  1 
ATOM   2067 C  C   . ILE B 1 112 ? 27.199 4.384   11.384  1.00 10.39 ? 112  ILE F C   1 
ATOM   2068 O  O   . ILE B 1 112 ? 25.969 4.508   11.407  1.00 9.65  ? 112  ILE F O   1 
ATOM   2069 C  CB  . ILE B 1 112 ? 27.788 6.232   9.731   1.00 10.43 ? 112  ILE F CB  1 
ATOM   2070 C  CG1 . ILE B 1 112 ? 28.012 5.243   8.567   1.00 11.06 ? 112  ILE F CG1 1 
ATOM   2071 C  CG2 . ILE B 1 112 ? 28.515 7.562   9.611   1.00 11.80 ? 112  ILE F CG2 1 
ATOM   2072 C  CD1 . ILE B 1 112 ? 27.554 5.770   7.193   1.00 11.87 ? 112  ILE F CD1 1 
ATOM   2073 N  N   . ILE B 1 113 ? 27.785 3.205   11.556  1.00 10.41 ? 113  ILE F N   1 
ATOM   2074 C  CA  . ILE B 1 113 ? 26.964 2.033   11.917  1.00 11.07 ? 113  ILE F CA  1 
ATOM   2075 C  C   . ILE B 1 113 ? 26.336 2.310   13.269  1.00 10.13 ? 113  ILE F C   1 
ATOM   2076 O  O   . ILE B 1 113 ? 26.921 2.802   14.203  1.00 11.54 ? 113  ILE F O   1 
ATOM   2077 C  CB  . ILE B 1 113 ? 27.778 0.726   11.869  1.00 13.68 ? 113  ILE F CB  1 
ATOM   2078 C  CG1 . ILE B 1 113 ? 28.204 0.407   10.331  1.00 14.21 ? 113  ILE F CG1 1 
ATOM   2079 C  CG2 . ILE B 1 113 ? 27.012 -0.430  12.580  1.00 13.41 ? 113  ILE F CG2 1 
ATOM   2080 C  CD1 . ILE B 1 113 ? 29.217 -0.674  10.219  1.00 16.93 ? 113  ILE F CD1 1 
ATOM   2081 N  N   . GLY B 1 114 ? 25.047 1.960   13.401  1.00 8.75  ? 114  GLY F N   1 
ATOM   2082 C  CA  . GLY B 1 114 ? 24.317 2.201   14.650  1.00 9.73  ? 114  GLY F CA  1 
ATOM   2083 C  C   . GLY B 1 114 ? 23.751 3.582   14.746  1.00 9.49  ? 114  GLY F C   1 
ATOM   2084 O  O   . GLY B 1 114 ? 23.132 3.904   15.759  1.00 9.88  ? 114  GLY F O   1 
ATOM   2085 N  N   . ARG B 1 115 ? 23.926 4.429   13.715  1.00 8.96  ? 115  ARG F N   1 
ATOM   2086 C  CA  . ARG B 1 115 ? 23.369 5.786   13.641  1.00 9.61  ? 115  ARG F CA  1 
ATOM   2087 C  C   . ARG B 1 115 ? 22.207 5.762   12.658  1.00 9.43  ? 115  ARG F C   1 
ATOM   2088 O  O   . ARG B 1 115 ? 21.873 4.737   12.115  1.00 12.01 ? 115  ARG F O   1 
ATOM   2089 C  CB  . ARG B 1 115 ? 24.466 6.776   13.349  1.00 9.27  ? 115  ARG F CB  1 
ATOM   2090 C  CG  . ARG B 1 115 ? 25.582 6.645   14.381  1.00 12.71 ? 115  ARG F CG  1 
ATOM   2091 C  CD  . ARG B 1 115 ? 26.593 7.767   14.318  1.00 12.72 ? 115  ARG F CD  1 
ATOM   2092 N  NE  . ARG B 1 115 ? 27.743 7.494   15.221  1.00 13.15 ? 115  ARG F NE  1 
ATOM   2093 C  CZ  . ARG B 1 115 ? 27.817 7.802   16.520  1.00 12.78 ? 115  ARG F CZ  1 
ATOM   2094 N  NH1 . ARG B 1 115 ? 26.866 8.448   17.129  1.00 14.01 ? 115  ARG F NH1 1 
ATOM   2095 N  NH2 . ARG B 1 115 ? 28.909 7.559   17.184  1.00 14.03 ? 115  ARG F NH2 1 
ATOM   2096 N  N   . THR B 1 116 ? 21.538 6.909   12.506  1.00 9.26  ? 116  THR F N   1 
ATOM   2097 C  CA  . THR B 1 116 ? 20.291 6.933   11.700  1.00 8.39  ? 116  THR F CA  1 
ATOM   2098 C  C   . THR B 1 116 ? 20.558 7.730   10.404  1.00 8.86  ? 116  THR F C   1 
ATOM   2099 O  O   . THR B 1 116 ? 21.029 8.864   10.443  1.00 11.47 ? 116  THR F O   1 
ATOM   2100 C  CB  . THR B 1 116 ? 19.147 7.620   12.455  1.00 8.61  ? 116  THR F CB  1 
ATOM   2101 O  OG1 . THR B 1 116 ? 18.785 6.795   13.562  1.00 10.54 ? 116  THR F OG1 1 
ATOM   2102 C  CG2 . THR B 1 116 ? 17.941 7.803   11.632  1.00 9.47  ? 116  THR F CG2 1 
ATOM   2103 N  N   . LEU B 1 117 ? 20.207 7.148   9.276   1.00 8.46  ? 117  LEU F N   1 
ATOM   2104 C  CA  . LEU B 1 117 ? 20.172 7.899   7.999   1.00 8.61  ? 117  LEU F CA  1 
ATOM   2105 C  C   . LEU B 1 117 ? 18.770 8.543   7.823   1.00 9.52  ? 117  LEU F C   1 
ATOM   2106 O  O   . LEU B 1 117 ? 17.758 7.889   8.054   1.00 9.78  ? 117  LEU F O   1 
ATOM   2107 C  CB  . LEU B 1 117 ? 20.418 6.911   6.882   1.00 9.37  ? 117  LEU F CB  1 
ATOM   2108 C  CG  . LEU B 1 117 ? 20.635 7.503   5.476   1.00 9.37  ? 117  LEU F CG  1 
ATOM   2109 C  CD1 . LEU B 1 117 ? 21.853 8.383   5.405   1.00 10.40 ? 117  LEU F CD1 1 
ATOM   2110 C  CD2 . LEU B 1 117 ? 20.694 6.412   4.456   1.00 11.21 ? 117  LEU F CD2 1 
ATOM   2111 N  N   . VAL B 1 118 ? 18.737 9.826   7.401   1.00 9.36  ? 118  VAL F N   1 
ATOM   2112 C  CA  . VAL B 1 118 ? 17.459 10.559  7.305   1.00 9.61  ? 118  VAL F CA  1 
ATOM   2113 C  C   . VAL B 1 118 ? 17.424 11.175  5.890   1.00 8.90  ? 118  VAL F C   1 
ATOM   2114 O  O   . VAL B 1 118 ? 18.390 11.758  5.432   1.00 9.93  ? 118  VAL F O   1 
ATOM   2115 C  CB  . VAL B 1 118 ? 17.381 11.678  8.331   1.00 9.46  ? 118  VAL F CB  1 
ATOM   2116 C  CG1 . VAL B 1 118 ? 16.145 12.491  8.222   1.00 10.86 ? 118  VAL F CG1 1 
ATOM   2117 C  CG2 . VAL B 1 118 ? 17.481 11.086  9.774   1.00 9.69  ? 118  VAL F CG2 1 
ATOM   2118 N  N   . VAL B 1 119 ? 16.227 11.116  5.304   1.00 8.92  ? 119  VAL F N   1 
ATOM   2119 C  CA  . VAL B 1 119 ? 15.896 11.921  4.150   1.00 9.50  ? 119  VAL F CA  1 
ATOM   2120 C  C   . VAL B 1 119 ? 14.813 12.906  4.493   1.00 11.69 ? 119  VAL F C   1 
ATOM   2121 O  O   . VAL B 1 119 ? 13.843 12.561  5.130   1.00 11.06 ? 119  VAL F O   1 
ATOM   2122 C  CB  . VAL B 1 119 ? 15.560 11.025  2.899   1.00 11.70 ? 119  VAL F CB  1 
ATOM   2123 C  CG1 . VAL B 1 119 ? 14.337 10.167  3.112   1.00 11.94 ? 119  VAL F CG1 1 
ATOM   2124 C  CG2 . VAL B 1 119 ? 15.308 11.872  1.683   1.00 11.66 ? 119  VAL F CG2 1 
ATOM   2125 N  N   . HIS B 1 120 ? 15.032 14.152  4.076   1.00 11.10 ? 120  HIS F N   1 
ATOM   2126 C  CA  . HIS B 1 120 ? 14.255 15.280  4.571   1.00 11.24 ? 120  HIS F CA  1 
ATOM   2127 C  C   . HIS B 1 120 ? 13.227 15.789  3.573   1.00 11.77 ? 120  HIS F C   1 
ATOM   2128 O  O   . HIS B 1 120 ? 13.256 15.547  2.392   1.00 12.59 ? 120  HIS F O   1 
ATOM   2129 C  CB  . HIS B 1 120 ? 15.173 16.450  4.922   1.00 11.40 ? 120  HIS F CB  1 
ATOM   2130 C  CG  . HIS B 1 120 ? 15.962 16.243  6.123   1.00 9.66  ? 120  HIS F CG  1 
ATOM   2131 N  ND1 . HIS B 1 120 ? 15.516 16.669  7.369   1.00 10.64 ? 120  HIS F ND1 1 
ATOM   2132 C  CD2 . HIS B 1 120 ? 17.172 15.655  6.323   1.00 11.22 ? 120  HIS F CD2 1 
ATOM   2133 C  CE1 . HIS B 1 120 ? 16.424 16.327  8.294   1.00 11.26 ? 120  HIS F CE1 1 
ATOM   2134 N  NE2 . HIS B 1 120 ? 17.442 15.702  7.684   1.00 10.22 ? 120  HIS F NE2 1 
ATOM   2135 N  N   . GLU B 1 121 ? 12.301 16.556  4.124   1.00 12.20 ? 121  GLU F N   1 
ATOM   2136 C  CA  . GLU B 1 121 ? 11.217 17.239  3.371   1.00 14.28 ? 121  GLU F CA  1 
ATOM   2137 C  C   . GLU B 1 121 ? 11.706 18.162  2.282   1.00 14.06 ? 121  GLU F C   1 
ATOM   2138 O  O   . GLU B 1 121 ? 11.149 18.188  1.169   1.00 13.66 ? 121  GLU F O   1 
ATOM   2139 C  CB  . GLU B 1 121 ? 10.494 18.093  4.377   1.00 15.80 ? 121  GLU F CB  1 
ATOM   2140 C  CG  . GLU B 1 121 ? 9.287  18.969  3.948   1.00 18.66 ? 121  GLU F CG  1 
ATOM   2141 C  CD  . GLU B 1 121 ? 8.983  20.136  4.928   0.70 18.97 ? 121  GLU F CD  1 
ATOM   2142 O  OE1 . GLU B 1 121 ? 9.571  20.267  6.060   0.70 16.07 ? 121  GLU F OE1 1 
ATOM   2143 O  OE2 . GLU B 1 121 ? 8.074  20.942  4.557   0.70 22.37 ? 121  GLU F OE2 1 
ATOM   2144 N  N   . LYS B 1 122 ? 12.728 18.920  2.598   1.00 15.42 ? 122  LYS F N   1 
ATOM   2145 C  CA  . LYS B 1 122 ? 13.166 20.014  1.803   1.00 16.52 ? 122  LYS F CA  1 
ATOM   2146 C  C   . LYS B 1 122 ? 14.649 19.907  1.387   1.00 14.74 ? 122  LYS F C   1 
ATOM   2147 O  O   . LYS B 1 122 ? 15.405 19.019  1.844   1.00 15.58 ? 122  LYS F O   1 
ATOM   2148 C  CB  . LYS B 1 122 ? 12.988 21.362  2.605   1.00 16.01 ? 122  LYS F CB  1 
ATOM   2149 C  CG  A LYS B 1 122 ? 11.696 21.652  3.200   0.50 19.65 ? 122  LYS F CG  1 
ATOM   2150 C  CG  B LYS B 1 122 ? 11.716 21.572  3.372   0.50 19.42 ? 122  LYS F CG  1 
ATOM   2151 C  CD  A LYS B 1 122 ? 11.603 23.148  3.305   0.50 19.84 ? 122  LYS F CD  1 
ATOM   2152 C  CD  B LYS B 1 122 ? 11.781 22.910  4.067   0.50 19.51 ? 122  LYS F CD  1 
ATOM   2153 C  CE  A LYS B 1 122 ? 11.869 23.609  4.716   0.50 15.45 ? 122  LYS F CE  1 
ATOM   2154 C  CE  B LYS B 1 122 ? 10.404 23.430  4.442   0.50 18.86 ? 122  LYS F CE  1 
ATOM   2155 N  NZ  A LYS B 1 122 ? 10.626 23.382  5.508   0.50 19.39 ? 122  LYS F NZ  1 
ATOM   2156 N  NZ  B LYS B 1 122 ? 10.544 24.510  5.452   0.50 19.89 ? 122  LYS F NZ  1 
ATOM   2157 N  N   . ALA B 1 123 ? 15.077 20.808  0.532   1.00 13.33 ? 123  ALA F N   1 
ATOM   2158 C  CA  . ALA B 1 123 ? 16.470 20.841  0.147   1.00 14.60 ? 123  ALA F CA  1 
ATOM   2159 C  C   . ALA B 1 123 ? 17.372 21.261  1.284   1.00 14.11 ? 123  ALA F C   1 
ATOM   2160 O  O   . ALA B 1 123 ? 17.004 22.114  2.119   1.00 14.49 ? 123  ALA F O   1 
ATOM   2161 C  CB  . ALA B 1 123 ? 16.648 21.797  -1.007  1.00 14.70 ? 123  ALA F CB  1 
ATOM   2162 N  N   . ASP B 1 124 ? 18.575 20.709  1.329   1.00 12.54 ? 124  ASP F N   1 
ATOM   2163 C  CA  . ASP B 1 124 ? 19.654 21.152  2.170   1.00 12.77 ? 124  ASP F CA  1 
ATOM   2164 C  C   . ASP B 1 124 ? 20.403 22.224  1.336   1.00 13.24 ? 124  ASP F C   1 
ATOM   2165 O  O   . ASP B 1 124 ? 20.822 22.006  0.206   1.00 13.61 ? 124  ASP F O   1 
ATOM   2166 C  CB  . ASP B 1 124 ? 20.536 19.946  2.459   1.00 12.29 ? 124  ASP F CB  1 
ATOM   2167 C  CG  . ASP B 1 124 ? 21.705 20.217  3.387   1.00 12.30 ? 124  ASP F CG  1 
ATOM   2168 O  OD1 . ASP B 1 124 ? 22.074 21.382  3.606   1.00 12.82 ? 124  ASP F OD1 1 
ATOM   2169 O  OD2 . ASP B 1 124 ? 22.210 19.227  3.973   1.00 13.48 ? 124  ASP F OD2 1 
ATOM   2170 N  N   . ASP B 1 125 ? 20.509 23.360  1.940   1.00 12.61 ? 125  ASP F N   1 
ATOM   2171 C  CA  . ASP B 1 125 ? 21.258 24.500  1.351   1.00 13.70 ? 125  ASP F CA  1 
ATOM   2172 C  C   . ASP B 1 125 ? 22.746 24.424  1.526   1.00 13.58 ? 125  ASP F C   1 
ATOM   2173 O  O   . ASP B 1 125 ? 23.460 25.363  1.143   1.00 14.44 ? 125  ASP F O   1 
ATOM   2174 C  CB  . ASP B 1 125 ? 20.698 25.842  1.850   1.00 14.77 ? 125  ASP F CB  1 
ATOM   2175 C  CG  . ASP B 1 125 ? 20.900 26.114  3.322   1.00 12.87 ? 125  ASP F CG  1 
ATOM   2176 O  OD1 . ASP B 1 125 ? 21.844 25.601  3.962   1.00 13.33 ? 125  ASP F OD1 1 
ATOM   2177 O  OD2 . ASP B 1 125 ? 20.104 26.923  3.955   1.00 15.46 ? 125  ASP F OD2 1 
ATOM   2178 N  N   . LEU B 1 126 ? 23.251 23.345  2.110   1.00 12.74 ? 126  LEU F N   1 
ATOM   2179 C  CA  . LEU B 1 126 ? 24.689 23.048  2.174   1.00 14.30 ? 126  LEU F CA  1 
ATOM   2180 C  C   . LEU B 1 126 ? 25.376 24.085  2.970   1.00 14.73 ? 126  LEU F C   1 
ATOM   2181 O  O   . LEU B 1 126 ? 26.564 24.233  2.858   1.00 15.76 ? 126  LEU F O   1 
ATOM   2182 C  CB  . LEU B 1 126 ? 25.326 22.782  0.821   1.00 13.34 ? 126  LEU F CB  1 
ATOM   2183 C  CG  . LEU B 1 126 ? 24.595 21.784  -0.079  1.00 14.44 ? 126  LEU F CG  1 
ATOM   2184 C  CD1 . LEU B 1 126 ? 25.481 21.443  -1.318  1.00 15.69 ? 126  LEU F CD1 1 
ATOM   2185 C  CD2 . LEU B 1 126 ? 24.161 20.486  0.669   1.00 13.70 ? 126  LEU F CD2 1 
ATOM   2186 N  N   . GLY B 1 127 ? 24.710 24.708  3.930   1.00 14.21 ? 127  GLY F N   1 
ATOM   2187 C  CA  . GLY B 1 127 ? 25.306 25.714  4.823   1.00 15.80 ? 127  GLY F CA  1 
ATOM   2188 C  C   . GLY B 1 127 ? 25.465 27.119  4.190   1.00 15.81 ? 127  GLY F C   1 
ATOM   2189 O  O   . GLY B 1 127 ? 26.119 27.985  4.750   1.00 19.23 ? 127  GLY F O   1 
ATOM   2190 N  N   . LYS B 1 128 ? 24.926 27.296  2.995   1.00 15.26 ? 128  LYS F N   1 
ATOM   2191 C  CA  . LYS B 1 128 ? 25.106 28.514  2.146   1.00 15.52 ? 128  LYS F CA  1 
ATOM   2192 C  C   . LYS B 1 128 ? 23.876 29.369  2.150   1.00 16.57 ? 128  LYS F C   1 
ATOM   2193 O  O   . LYS B 1 128 ? 23.770 30.304  1.329   1.00 18.42 ? 128  LYS F O   1 
ATOM   2194 C  CB  . LYS B 1 128 ? 25.515 28.150  0.720   1.00 15.58 ? 128  LYS F CB  1 
ATOM   2195 C  CG  . LYS B 1 128 ? 26.843 27.427  0.667   1.00 20.89 ? 128  LYS F CG  1 
ATOM   2196 C  CD  . LYS B 1 128 ? 27.952 28.208  1.281   1.00 27.75 ? 128  LYS F CD  1 
ATOM   2197 C  CE  . LYS B 1 128 ? 29.349 27.729  0.862   1.00 31.88 ? 128  LYS F CE  1 
ATOM   2198 N  NZ  . LYS B 1 128 ? 29.852 26.760  1.851   1.00 34.40 ? 128  LYS F NZ  1 
ATOM   2199 N  N   . GLY B 1 129 ? 22.920 29.116  3.023   1.00 18.75 ? 129  GLY F N   1 
ATOM   2200 C  CA  . GLY B 1 129 ? 21.706 29.855  3.002   1.00 19.55 ? 129  GLY F CA  1 
ATOM   2201 C  C   . GLY B 1 129 ? 21.836 31.155  3.738   1.00 19.37 ? 129  GLY F C   1 
ATOM   2202 O  O   . GLY B 1 129 ? 22.846 31.465  4.392   1.00 20.41 ? 129  GLY F O   1 
ATOM   2203 N  N   A GLY B 1 130 ? 20.779 31.909  3.696   0.50 20.48 ? 130  GLY F N   1 
ATOM   2204 N  N   B GLY B 1 130 ? 20.781 31.925  3.734   0.50 20.52 ? 130  GLY F N   1 
ATOM   2205 C  CA  A GLY B 1 130 ? 20.832 33.223  4.323   0.50 22.90 ? 130  GLY F CA  1 
ATOM   2206 C  CA  B GLY B 1 130 ? 20.841 33.258  4.386   0.50 22.75 ? 130  GLY F CA  1 
ATOM   2207 C  C   A GLY B 1 130 ? 20.437 33.328  5.780   0.50 24.64 ? 130  GLY F C   1 
ATOM   2208 C  C   B GLY B 1 130 ? 21.029 33.348  5.899   0.50 24.73 ? 130  GLY F C   1 
ATOM   2209 O  O   A GLY B 1 130 ? 19.884 34.397  6.142   0.50 22.88 ? 130  GLY F O   1 
ATOM   2210 O  O   B GLY B 1 130 ? 21.547 34.341  6.411   0.50 24.06 ? 130  GLY F O   1 
ATOM   2211 N  N   . ASN B 1 131 ? 20.691 32.276  6.598   1.00 24.86 ? 131  ASN F N   1 
ATOM   2212 C  CA  . ASN B 1 131 ? 20.344 32.361  8.062   1.00 23.81 ? 131  ASN F CA  1 
ATOM   2213 C  C   . ASN B 1 131 ? 21.145 31.458  9.035   1.00 25.72 ? 131  ASN F C   1 
ATOM   2214 O  O   . ASN B 1 131 ? 21.983 30.627  8.643   1.00 24.78 ? 131  ASN F O   1 
ATOM   2215 C  CB  . ASN B 1 131 ? 18.862 32.103  8.116   1.00 25.72 ? 131  ASN F CB  1 
ATOM   2216 C  CG  . ASN B 1 131 ? 18.485 30.655  7.742   1.00 28.26 ? 131  ASN F CG  1 
ATOM   2217 O  OD1 . ASN B 1 131 ? 19.360 29.788  7.610   1.00 21.04 ? 131  ASN F OD1 1 
ATOM   2218 N  ND2 . ASN B 1 131 ? 17.171 30.383  7.623   1.00 24.80 ? 131  ASN F ND2 1 
ATOM   2219 N  N   . GLU B 1 132 ? 20.863 31.559  10.337  1.00 23.55 ? 132  GLU F N   1 
ATOM   2220 C  CA  . GLU B 1 132 ? 21.619 30.797  11.304  1.00 23.76 ? 132  GLU F CA  1 
ATOM   2221 C  C   . GLU B 1 132 ? 21.343 29.291  11.210  1.00 21.19 ? 132  GLU F C   1 
ATOM   2222 O  O   . GLU B 1 132 ? 22.223 28.448  11.405  1.00 23.33 ? 132  GLU F O   1 
ATOM   2223 C  CB  . GLU B 1 132 ? 21.263 31.257  12.715  1.00 25.69 ? 132  GLU F CB  1 
ATOM   2224 C  CG  . GLU B 1 132 ? 20.044 30.645  13.333  0.30 30.62 ? 132  GLU F CG  1 
ATOM   2225 C  CD  . GLU B 1 132 ? 20.307 29.270  13.899  0.30 32.38 ? 132  GLU F CD  1 
ATOM   2226 O  OE1 . GLU B 1 132 ? 21.458 29.032  14.312  0.30 37.38 ? 132  GLU F OE1 1 
ATOM   2227 O  OE2 . GLU B 1 132 ? 19.377 28.427  13.925  0.30 31.41 ? 132  GLU F OE2 1 
ATOM   2228 N  N   . GLU B 1 133 ? 20.116 28.951  10.858  1.00 17.98 ? 133  GLU F N   1 
ATOM   2229 C  CA  . GLU B 1 133 ? 19.787 27.540  10.777  1.00 16.02 ? 133  GLU F CA  1 
ATOM   2230 C  C   . GLU B 1 133 ? 20.570 26.855  9.683   1.00 15.79 ? 133  GLU F C   1 
ATOM   2231 O  O   . GLU B 1 133 ? 20.767 25.660  9.769   1.00 16.82 ? 133  GLU F O   1 
ATOM   2232 C  CB  . GLU B 1 133 ? 18.299 27.371  10.584  1.00 17.34 ? 133  GLU F CB  1 
ATOM   2233 C  CG  . GLU B 1 133 ? 17.764 25.890  10.782  0.70 22.58 ? 133  GLU F CG  1 
ATOM   2234 C  CD  . GLU B 1 133 ? 17.738 25.276  12.252  0.70 28.17 ? 133  GLU F CD  1 
ATOM   2235 O  OE1 . GLU B 1 133 ? 18.558 25.579  13.182  0.70 26.42 ? 133  GLU F OE1 1 
ATOM   2236 O  OE2 . GLU B 1 133 ? 16.856 24.373  12.459  0.70 28.58 ? 133  GLU F OE2 1 
ATOM   2237 N  N   . SER B 1 134 ? 20.965 27.549  8.622   1.00 15.17 ? 134  SER F N   1 
ATOM   2238 C  CA  . SER B 1 134 ? 21.648 26.940  7.522   1.00 15.76 ? 134  SER F CA  1 
ATOM   2239 C  C   . SER B 1 134 ? 22.912 26.212  8.011   1.00 15.11 ? 134  SER F C   1 
ATOM   2240 O  O   . SER B 1 134 ? 23.238 25.171  7.464   1.00 14.74 ? 134  SER F O   1 
ATOM   2241 C  CB  . SER B 1 134 ? 22.066 28.034  6.541   1.00 14.89 ? 134  SER F CB  1 
ATOM   2242 O  OG  . SER B 1 134 ? 22.795 27.481  5.419   1.00 16.44 ? 134  SER F OG  1 
ATOM   2243 N  N   . THR B 1 135 ? 23.596 26.815  8.992   1.00 14.59 ? 135  THR F N   1 
ATOM   2244 C  CA  . THR B 1 135 ? 24.864 26.290  9.511   1.00 16.30 ? 135  THR F CA  1 
ATOM   2245 C  C   . THR B 1 135 ? 24.624 25.229  10.625  1.00 13.94 ? 135  THR F C   1 
ATOM   2246 O  O   . THR B 1 135 ? 25.589 24.747  11.214  1.00 15.65 ? 135  THR F O   1 
ATOM   2247 C  CB  A THR B 1 135 ? 25.642 27.429  10.335  0.50 19.23 ? 135  THR F CB  1 
ATOM   2248 C  CB  B THR B 1 135 ? 25.963 27.364  9.718   0.50 15.99 ? 135  THR F CB  1 
ATOM   2249 O  OG1 A THR B 1 135 ? 24.944 27.707  11.566  0.50 19.52 ? 135  THR F OG1 1 
ATOM   2250 O  OG1 B THR B 1 135 ? 25.455 28.348  10.583  0.50 17.91 ? 135  THR F OG1 1 
ATOM   2251 C  CG2 A THR B 1 135 ? 25.740 28.700  9.592   0.50 18.30 ? 135  THR F CG2 1 
ATOM   2252 C  CG2 B THR B 1 135 ? 26.337 28.037  8.384   0.50 16.37 ? 135  THR F CG2 1 
ATOM   2253 N  N   . LYS B 1 136 ? 23.376 24.850  10.829  1.00 14.35 ? 136  LYS F N   1 
ATOM   2254 C  CA  . LYS B 1 136 ? 23.029 23.773  11.790  1.00 15.29 ? 136  LYS F CA  1 
ATOM   2255 C  C   . LYS B 1 136 ? 22.367 22.588  11.035  1.00 13.80 ? 136  LYS F C   1 
ATOM   2256 O  O   . LYS B 1 136 ? 22.753 21.426  11.196  1.00 13.99 ? 136  LYS F O   1 
ATOM   2257 C  CB  . LYS B 1 136 ? 22.153 24.330  12.932  1.00 16.95 ? 136  LYS F CB  1 
ATOM   2258 C  CG  . LYS B 1 136 ? 22.968 25.394  13.773  1.00 21.27 ? 136  LYS F CG  1 
ATOM   2259 C  CD  . LYS B 1 136 ? 22.183 26.005  14.929  1.00 22.12 ? 136  LYS F CD  1 
ATOM   2260 C  CE  . LYS B 1 136 ? 23.059 26.778  15.879  0.10 18.26 ? 136  LYS F CE  1 
ATOM   2261 N  NZ  . LYS B 1 136 ? 23.766 27.813  15.139  0.10 8.65  ? 136  LYS F NZ  1 
ATOM   2262 N  N   . THR B 1 137 ? 21.293 22.871  10.261  1.00 14.75 ? 137  THR F N   1 
ATOM   2263 C  CA  . THR B 1 137 ? 20.487 21.833  9.637   1.00 14.08 ? 137  THR F CA  1 
ATOM   2264 C  C   . THR B 1 137 ? 20.453 21.973  8.132   1.00 13.27 ? 137  THR F C   1 
ATOM   2265 O  O   . THR B 1 137 ? 19.895 21.085  7.452   1.00 14.91 ? 137  THR F O   1 
ATOM   2266 C  CB  . THR B 1 137 ? 19.019 21.849  10.085  1.00 15.15 ? 137  THR F CB  1 
ATOM   2267 O  OG1 . THR B 1 137 ? 18.471 23.052  9.638   1.00 17.62 ? 137  THR F OG1 1 
ATOM   2268 C  CG2 . THR B 1 137 ? 18.893 21.761  11.581  1.00 16.16 ? 137  THR F CG2 1 
ATOM   2269 N  N   . GLY B 1 138 ? 20.927 23.086  7.546   1.00 12.49 ? 138  GLY F N   1 
ATOM   2270 C  CA  . GLY B 1 138 ? 20.777 23.284  6.085   1.00 12.61 ? 138  GLY F CA  1 
ATOM   2271 C  C   . GLY B 1 138 ? 19.363 23.651  5.697   1.00 12.66 ? 138  GLY F C   1 
ATOM   2272 O  O   . GLY B 1 138 ? 19.125 23.672  4.459   1.00 14.91 ? 138  GLY F O   1 
ATOM   2273 N  N   . ASN B 1 139 ? 18.501 23.911  6.651   1.00 13.65 ? 139  ASN F N   1 
ATOM   2274 C  CA  . ASN B 1 139 ? 17.103 24.250  6.347   1.00 14.53 ? 139  ASN F CA  1 
ATOM   2275 C  C   . ASN B 1 139 ? 16.338 23.166  5.624   1.00 15.29 ? 139  ASN F C   1 
ATOM   2276 O  O   . ASN B 1 139 ? 15.447 23.442  4.848   1.00 16.45 ? 139  ASN F O   1 
ATOM   2277 C  CB  . ASN B 1 139 ? 17.022 25.606  5.585   1.00 15.93 ? 139  ASN F CB  1 
ATOM   2278 C  CG  . ASN B 1 139 ? 17.433 26.807  6.439   1.00 15.14 ? 139  ASN F CG  1 
ATOM   2279 O  OD1 . ASN B 1 139 ? 18.529 27.395  6.223   1.00 18.98 ? 139  ASN F OD1 1 
ATOM   2280 N  ND2 . ASN B 1 139 ? 16.715 27.048  7.473   1.00 16.08 ? 139  ASN F ND2 1 
ATOM   2281 N  N   . ALA B 1 140 ? 16.668 21.907  5.901   1.00 12.94 ? 140  ALA F N   1 
ATOM   2282 C  CA  . ALA B 1 140 ? 16.098 20.783  5.159   1.00 12.71 ? 140  ALA F CA  1 
ATOM   2283 C  C   . ALA B 1 140 ? 14.768 20.340  5.678   1.00 14.03 ? 140  ALA F C   1 
ATOM   2284 O  O   . ALA B 1 140 ? 14.139 19.480  5.094   1.00 14.49 ? 140  ALA F O   1 
ATOM   2285 C  CB  . ALA B 1 140 ? 17.082 19.589  5.178   1.00 13.83 ? 140  ALA F CB  1 
ATOM   2286 N  N   . GLY B 1 141 ? 14.307 20.911  6.788   1.00 15.12 ? 141  GLY F N   1 
ATOM   2287 C  CA  . GLY B 1 141 ? 12.947 20.660  7.167   1.00 14.99 ? 141  GLY F CA  1 
ATOM   2288 C  C   . GLY B 1 141 ? 12.759 19.313  7.872   1.00 14.25 ? 141  GLY F C   1 
ATOM   2289 O  O   . GLY B 1 141 ? 13.694 18.757  8.426   1.00 14.30 ? 141  GLY F O   1 
ATOM   2290 N  N   . SER B 1 142 ? 11.508 18.828  7.877   1.00 14.13 ? 142  SER F N   1 
ATOM   2291 C  CA  . SER B 1 142 ? 11.147 17.654  8.622   1.00 13.67 ? 142  SER F CA  1 
ATOM   2292 C  C   . SER B 1 142 ? 11.787 16.379  8.007   1.00 12.38 ? 142  SER F C   1 
ATOM   2293 O  O   . SER B 1 142 ? 12.403 16.377  6.937   1.00 12.16 ? 142  SER F O   1 
ATOM   2294 C  CB  . SER B 1 142 ? 9.622  17.564  8.628   1.00 15.61 ? 142  SER F CB  1 
ATOM   2295 O  OG  . SER B 1 142 ? 9.125  17.064  7.404   0.70 17.30 ? 142  SER F OG  1 
ATOM   2296 N  N   . ARG B 1 143 ? 11.585 15.291  8.762   1.00 12.62 ? 143  ARG F N   1 
ATOM   2297 C  CA  . ARG B 1 143 ? 12.223 14.003  8.439   1.00 12.18 ? 143  ARG F CA  1 
ATOM   2298 C  C   . ARG B 1 143 ? 11.219 13.068  7.806   1.00 11.74 ? 143  ARG F C   1 
ATOM   2299 O  O   . ARG B 1 143 ? 10.272 12.606  8.507   1.00 16.19 ? 143  ARG F O   1 
ATOM   2300 C  CB  . ARG B 1 143 ? 12.764 13.446  9.776   1.00 11.97 ? 143  ARG F CB  1 
ATOM   2301 C  CG  . ARG B 1 143 ? 13.761 14.389  10.372  1.00 11.99 ? 143  ARG F CG  1 
ATOM   2302 C  CD  . ARG B 1 143 ? 14.326 13.987  11.735  1.00 13.62 ? 143  ARG F CD  1 
ATOM   2303 N  NE  . ARG B 1 143 ? 15.125 15.079  12.272  1.00 13.22 ? 143  ARG F NE  1 
ATOM   2304 C  CZ  . ARG B 1 143 ? 15.991 14.969  13.245  1.00 11.16 ? 143  ARG F CZ  1 
ATOM   2305 N  NH1 . ARG B 1 143 ? 16.190 13.817  13.878  1.00 11.56 ? 143  ARG F NH1 1 
ATOM   2306 N  NH2 . ARG B 1 143 ? 16.698 16.028  13.600  1.00 11.88 ? 143  ARG F NH2 1 
ATOM   2307 N  N   . LEU B 1 144 ? 11.318 12.858  6.526   1.00 11.62 ? 144  LEU F N   1 
ATOM   2308 C  CA  . LEU B 1 144 ? 10.301 12.066  5.829   1.00 12.35 ? 144  LEU F CA  1 
ATOM   2309 C  C   . LEU B 1 144 ? 10.452 10.568  6.059   1.00 12.40 ? 144  LEU F C   1 
ATOM   2310 O  O   . LEU B 1 144 ? 9.476  9.847   6.155   1.00 13.32 ? 144  LEU F O   1 
ATOM   2311 C  CB  . LEU B 1 144 ? 10.339 12.335  4.353   1.00 13.64 ? 144  LEU F CB  1 
ATOM   2312 C  CG  . LEU B 1 144 ? 10.121 13.761  3.908   1.00 16.22 ? 144  LEU F CG  1 
ATOM   2313 C  CD1 . LEU B 1 144 ? 10.292 13.822  2.382   1.00 20.08 ? 144  LEU F CD1 1 
ATOM   2314 C  CD2 . LEU B 1 144 ? 8.750  14.246  4.435   1.00 19.89 ? 144  LEU F CD2 1 
ATOM   2315 N  N   . ALA B 1 145 ? 11.670 10.122  6.207   1.00 11.18 ? 145  ALA F N   1 
ATOM   2316 C  CA  . ALA B 1 145 ? 11.957 8.698   6.387   1.00 12.74 ? 145  ALA F CA  1 
ATOM   2317 C  C   . ALA B 1 145 ? 13.368 8.539   6.952   1.00 10.17 ? 145  ALA F C   1 
ATOM   2318 O  O   . ALA B 1 145 ? 14.219 9.399   6.756   1.00 10.59 ? 145  ALA F O   1 
ATOM   2319 C  CB  . ALA B 1 145 ? 11.832 7.911   5.107   1.00 12.85 ? 145  ALA F CB  1 
ATOM   2320 N  N   . CYS B 1 146 ? 13.532 7.454   7.683   1.00 10.66 ? 146  CYS F N   1 
ATOM   2321 C  CA  . CYS B 1 146 ? 14.810 7.177   8.292   1.00 10.39 ? 146  CYS F CA  1 
ATOM   2322 C  C   . CYS B 1 146 ? 14.937 5.698   8.599   1.00 9.21  ? 146  CYS F C   1 
ATOM   2323 O  O   . CYS B 1 146 ? 14.001 4.983   8.501   1.00 10.35 ? 146  CYS F O   1 
ATOM   2324 C  CB  . CYS B 1 146 ? 14.956 7.980   9.563   1.00 10.45 ? 146  CYS F CB  1 
ATOM   2325 S  SG  . CYS B 1 146 ? 13.709 7.600   10.872  1.00 12.82 ? 146  CYS F SG  1 
ATOM   2326 N  N   . GLY B 1 147 ? 16.153 5.293   8.948   1.00 9.60  ? 147  GLY F N   1 
ATOM   2327 C  CA  . GLY B 1 147 ? 16.407 3.948   9.429   1.00 9.71  ? 147  GLY F CA  1 
ATOM   2328 C  C   . GLY B 1 147 ? 17.755 3.936   10.109  1.00 8.59  ? 147  GLY F C   1 
ATOM   2329 O  O   . GLY B 1 147 ? 18.578 4.823   9.966   1.00 9.77  ? 147  GLY F O   1 
ATOM   2330 N  N   . VAL B 1 148 ? 17.957 2.912   10.928  1.00 9.69  ? 148  VAL F N   1 
ATOM   2331 C  CA  . VAL B 1 148 ? 19.198 2.675   11.589  1.00 10.01 ? 148  VAL F CA  1 
ATOM   2332 C  C   . VAL B 1 148 ? 20.153 1.950   10.630  1.00 9.62  ? 148  VAL F C   1 
ATOM   2333 O  O   . VAL B 1 148 ? 19.808 0.985   9.968   1.00 11.36 ? 148  VAL F O   1 
ATOM   2334 C  CB  . VAL B 1 148 ? 18.958 1.895   12.901  1.00 10.34 ? 148  VAL F CB  1 
ATOM   2335 C  CG1 . VAL B 1 148 ? 20.304 1.766   13.638  1.00 10.70 ? 148  VAL F CG1 1 
ATOM   2336 C  CG2 . VAL B 1 148 ? 17.979 2.600   13.768  1.00 13.08 ? 148  VAL F CG2 1 
ATOM   2337 N  N   . ILE B 1 149 ? 21.381 2.449   10.565  1.00 9.02  ? 149  ILE F N   1 
ATOM   2338 C  CA  . ILE B 1 149 ? 22.429 1.852   9.692   1.00 9.32  ? 149  ILE F CA  1 
ATOM   2339 C  C   . ILE B 1 149 ? 23.003 0.606   10.349  1.00 9.33  ? 149  ILE F C   1 
ATOM   2340 O  O   . ILE B 1 149 ? 23.523 0.663   11.474  1.00 10.31 ? 149  ILE F O   1 
ATOM   2341 C  CB  . ILE B 1 149 ? 23.530 2.867   9.358   1.00 9.62  ? 149  ILE F CB  1 
ATOM   2342 C  CG1 . ILE B 1 149 ? 22.943 4.089   8.678   1.00 11.33 ? 149  ILE F CG1 1 
ATOM   2343 C  CG2 . ILE B 1 149 ? 24.640 2.256   8.467   1.00 9.96  ? 149  ILE F CG2 1 
ATOM   2344 C  CD1 . ILE B 1 149 ? 23.866 5.290   8.692   1.00 11.27 ? 149  ILE F CD1 1 
ATOM   2345 N  N   . GLY B 1 150 ? 22.887 -0.511  9.667   1.00 8.63  ? 150  GLY F N   1 
ATOM   2346 C  CA  . GLY B 1 150 ? 23.329 -1.771  10.200  1.00 9.91  ? 150  GLY F CA  1 
ATOM   2347 C  C   . GLY B 1 150 ? 24.458 -2.405  9.439   1.00 9.44  ? 150  GLY F C   1 
ATOM   2348 O  O   . GLY B 1 150 ? 24.635 -2.153  8.240   1.00 10.08 ? 150  GLY F O   1 
ATOM   2349 N  N   . ILE B 1 151 ? 25.164 -3.332  10.034  1.00 10.21 ? 151  ILE F N   1 
ATOM   2350 C  CA  . ILE B 1 151 ? 26.201 -4.103  9.404   1.00 9.84  ? 151  ILE F CA  1 
ATOM   2351 C  C   . ILE B 1 151 ? 25.559 -5.114  8.463   1.00 10.13 ? 151  ILE F C   1 
ATOM   2352 O  O   . ILE B 1 151 ? 24.557 -5.770  8.782   1.00 10.98 ? 151  ILE F O   1 
ATOM   2353 C  CB  . ILE B 1 151 ? 27.025 -4.882  10.468  1.00 11.33 ? 151  ILE F CB  1 
ATOM   2354 C  CG1 . ILE B 1 151 ? 27.593 -3.936  11.506  1.00 16.22 ? 151  ILE F CG1 1 
ATOM   2355 C  CG2 . ILE B 1 151 ? 28.108 -5.736  9.834   1.00 15.72 ? 151  ILE F CG2 1 
ATOM   2356 C  CD1 . ILE B 1 151 ? 28.090 -4.584  12.760  1.00 17.19 ? 151  ILE F CD1 1 
ATOM   2357 N  N   . ALA B 1 152 ? 26.106 -5.189  7.272   1.00 10.41 ? 152  ALA F N   1 
ATOM   2358 C  CA  . ALA B 1 152 ? 25.646 -6.048  6.220   1.00 10.36 ? 152  ALA F CA  1 
ATOM   2359 C  C   . ALA B 1 152 ? 26.652 -7.113  5.898   1.00 12.15 ? 152  ALA F C   1 
ATOM   2360 O  O   . ALA B 1 152 ? 27.835 -7.003  6.152   1.00 12.49 ? 152  ALA F O   1 
ATOM   2361 C  CB  . ALA B 1 152 ? 25.345 -5.244  4.935   1.00 11.99 ? 152  ALA F CB  1 
ATOM   2362 N  N   . GLN B 1 153 ? 26.138 -8.171  5.308   1.00 12.28 ? 153  GLN F N   1 
ATOM   2363 C  CA  . GLN B 1 153 ? 26.871 -9.401  4.954   1.00 15.63 ? 153  GLN F CA  1 
ATOM   2364 C  C   . GLN B 1 153 ? 27.750 -9.089  3.769   1.00 15.96 ? 153  GLN F C   1 
ATOM   2365 O  O   . GLN B 1 153 ? 27.362 -8.401  2.797   1.00 17.43 ? 153  GLN F O   1 
ATOM   2366 C  CB  . GLN B 1 153 ? 25.845 -10.486 4.507   1.00 17.24 ? 153  GLN F CB  1 
ATOM   2367 C  CG  . GLN B 1 153 ? 26.390 -11.835 3.978   1.00 16.79 ? 153  GLN F CG  1 
ATOM   2368 C  CD  . GLN B 1 153 ? 25.256 -12.826 3.676   1.00 18.10 ? 153  GLN F CD  1 
ATOM   2369 O  OE1 . GLN B 1 153 ? 24.158 -12.822 4.327   1.00 18.85 ? 153  GLN F OE1 1 
ATOM   2370 N  NE2 . GLN B 1 153 ? 25.489 -13.699 2.750   1.00 21.11 ? 153  GLN F NE2 1 
ATOM   2371 O  OXT . GLN B 1 153 ? 28.893 -9.592  3.710   1.00 21.20 ? 153  GLN F OXT 1 
HETATM 2372 CU CU  A CU  C 2 .   ? 16.899 -15.145 17.026  0.88 10.83 ? 1154 CU  A CU  1 
HETATM 2373 CU CU  B CU  C 2 .   ? 17.245 -16.153 16.972  0.12 9.87  ? 1154 CU  A CU  1 
HETATM 2374 ZN ZN  . ZN  D 3 .   ? 22.123 -18.855 19.270  1.00 10.97 ? 1155 ZN  A ZN  1 
HETATM 2375 S  S   . SO4 E 4 .   ? 11.728 -15.846 9.155   0.50 27.77 ? 1157 SO4 A S   1 
HETATM 2376 O  O1  . SO4 E 4 .   ? 12.823 -14.882 9.004   0.50 25.82 ? 1157 SO4 A O1  1 
HETATM 2377 O  O2  . SO4 E 4 .   ? 11.309 -16.141 7.777   0.50 28.69 ? 1157 SO4 A O2  1 
HETATM 2378 O  O3  . SO4 E 4 .   ? 12.218 -17.066 9.789   0.50 24.78 ? 1157 SO4 A O3  1 
HETATM 2379 O  O4  . SO4 E 4 .   ? 10.647 -15.335 9.935   0.50 15.33 ? 1157 SO4 A O4  1 
HETATM 2380 S  S   . SO4 F 4 .   ? 13.935 -23.135 13.597  0.50 15.86 ? 1158 SO4 A S   1 
HETATM 2381 O  O1  . SO4 F 4 .   ? 14.764 -22.178 14.160  0.50 17.71 ? 1158 SO4 A O1  1 
HETATM 2382 O  O2  . SO4 F 4 .   ? 13.641 -22.466 12.345  0.50 24.43 ? 1158 SO4 A O2  1 
HETATM 2383 O  O3  . SO4 F 4 .   ? 12.886 -23.495 14.560  0.50 14.63 ? 1158 SO4 A O3  1 
HETATM 2384 O  O4  . SO4 F 4 .   ? 14.862 -24.274 13.475  0.50 20.66 ? 1158 SO4 A O4  1 
HETATM 2385 C  C   . ACT G 5 .   ? 11.091 15.636  12.540  0.50 21.34 ? 1154 ACT F C   1 
HETATM 2386 O  O   . ACT G 5 .   ? 11.620 14.895  13.423  0.50 23.04 ? 1154 ACT F O   1 
HETATM 2387 O  OXT . ACT G 5 .   ? 11.483 16.835  12.496  0.50 25.36 ? 1154 ACT F OXT 1 
HETATM 2388 C  CH3 . ACT G 5 .   ? 10.164 15.040  11.520  0.50 16.35 ? 1154 ACT F CH3 1 
HETATM 2389 CU CU  A CU  H 2 .   ? 19.212 15.140  8.394   0.80 9.95  ? 1156 CU  F CU  1 
HETATM 2390 CU CU  B CU  H 2 .   ? 19.420 16.097  8.562   0.20 9.77  ? 1156 CU  F CU  1 
HETATM 2391 ZN ZN  . ZN  I 3 .   ? 24.856 18.876  9.074   1.00 10.53 ? 1157 ZN  F ZN  1 
HETATM 2392 S  S   A SO4 J 4 .   ? 15.083 23.278  9.849   0.30 13.33 ? 1158 SO4 F S   1 
HETATM 2393 S  S   B SO4 J 4 .   ? 14.644 22.866  9.879   0.30 15.86 ? 1158 SO4 F S   1 
HETATM 2394 O  O1  A SO4 J 4 .   ? 15.916 22.372  9.066   0.30 13.79 ? 1158 SO4 F O1  1 
HETATM 2395 O  O1  B SO4 J 4 .   ? 15.884 22.171  10.140  0.30 11.95 ? 1158 SO4 F O1  1 
HETATM 2396 O  O2  A SO4 J 4 .   ? 14.448 22.703  10.992  0.30 13.42 ? 1158 SO4 F O2  1 
HETATM 2397 O  O2  B SO4 J 4 .   ? 13.455 22.100  10.251  0.30 16.94 ? 1158 SO4 F O2  1 
HETATM 2398 O  O3  A SO4 J 4 .   ? 14.057 23.697  8.903   0.30 20.44 ? 1158 SO4 F O3  1 
HETATM 2399 O  O3  B SO4 J 4 .   ? 14.679 23.240  8.430   0.30 13.96 ? 1158 SO4 F O3  1 
HETATM 2400 O  O4  A SO4 J 4 .   ? 15.993 24.324  10.292  0.30 11.85 ? 1158 SO4 F O4  1 
HETATM 2401 O  O4  B SO4 J 4 .   ? 14.769 24.023  10.762  0.30 16.81 ? 1158 SO4 F O4  1 
HETATM 2402 O  O   . HOH K 6 .   ? 13.932 -20.256 8.780   1.00 52.15 ? 2001 HOH A O   1 
HETATM 2403 O  O   . HOH K 6 .   ? 33.113 3.286   23.716  1.00 42.18 ? 2002 HOH A O   1 
HETATM 2404 O  O   . HOH K 6 .   ? 16.859 4.988   32.139  1.00 36.52 ? 2003 HOH A O   1 
HETATM 2405 O  O   . HOH K 6 .   ? 18.923 4.529   28.980  1.00 43.24 ? 2004 HOH A O   1 
HETATM 2406 O  O   . HOH K 6 .   ? 17.569 2.489   33.772  1.00 37.13 ? 2005 HOH A O   1 
HETATM 2407 O  O   . HOH K 6 .   ? 18.829 7.388   30.925  1.00 55.88 ? 2006 HOH A O   1 
HETATM 2408 O  O   . HOH K 6 .   ? 4.767  -12.665 11.389  1.00 38.90 ? 2007 HOH A O   1 
HETATM 2409 O  O   . HOH K 6 .   ? 12.554 -1.428  13.672  1.00 21.35 ? 2008 HOH A O   1 
HETATM 2410 O  O   . HOH K 6 .   ? 36.142 -3.749  23.743  1.00 41.38 ? 2009 HOH A O   1 
HETATM 2411 O  O   . HOH K 6 .   ? 40.198 -3.092  26.567  1.00 47.33 ? 2010 HOH A O   1 
HETATM 2412 O  O   . HOH K 6 .   ? 19.140 -15.927 32.544  1.00 30.42 ? 2011 HOH A O   1 
HETATM 2413 O  O   . HOH K 6 .   ? 36.400 -22.883 15.021  1.00 45.04 ? 2012 HOH A O   1 
HETATM 2414 O  O   . HOH K 6 .   ? 37.566 -24.203 12.247  1.00 42.03 ? 2013 HOH A O   1 
HETATM 2415 O  O   . HOH K 6 .   ? 6.621  -3.171  10.438  1.00 36.33 ? 2014 HOH A O   1 
HETATM 2416 O  O   . HOH K 6 .   ? 26.090 -2.822  35.586  1.00 36.49 ? 2015 HOH A O   1 
HETATM 2417 O  O   . HOH K 6 .   ? 29.039 -2.213  35.556  1.00 29.64 ? 2016 HOH A O   1 
HETATM 2418 O  O   . HOH K 6 .   ? 8.782  -8.869  6.638   1.00 39.75 ? 2017 HOH A O   1 
HETATM 2419 O  O   . HOH K 6 .   ? -0.935 -8.797  9.805   1.00 35.43 ? 2018 HOH A O   1 
HETATM 2420 O  O   . HOH K 6 .   ? 6.527  -10.389 11.370  0.50 15.15 ? 2019 HOH A O   1 
HETATM 2421 O  O   . HOH K 6 .   ? -0.317 -6.374  10.817  1.00 57.76 ? 2020 HOH A O   1 
HETATM 2422 O  O   . HOH K 6 .   ? 2.922  -4.560  11.687  1.00 43.72 ? 2021 HOH A O   1 
HETATM 2423 O  O   . HOH K 6 .   ? -1.643 -7.288  13.437  1.00 52.40 ? 2022 HOH A O   1 
HETATM 2424 O  O   . HOH K 6 .   ? -0.047 -5.422  19.347  1.00 31.64 ? 2023 HOH A O   1 
HETATM 2425 O  O   . HOH K 6 .   ? 4.951  -5.312  14.170  1.00 22.16 ? 2024 HOH A O   1 
HETATM 2426 O  O   . HOH K 6 .   ? 2.260  -13.331 15.500  1.00 25.96 ? 2025 HOH A O   1 
HETATM 2427 O  O   . HOH K 6 .   ? -0.859 -14.020 17.755  1.00 28.61 ? 2026 HOH A O   1 
HETATM 2428 O  O   . HOH K 6 .   ? 3.152  -3.506  14.597  1.00 39.48 ? 2027 HOH A O   1 
HETATM 2429 O  O   . HOH K 6 .   ? 5.987  -0.648  21.087  1.00 31.29 ? 2028 HOH A O   1 
HETATM 2430 O  O   . HOH K 6 .   ? 5.783  -2.182  23.466  1.00 37.23 ? 2029 HOH A O   1 
HETATM 2431 O  O   . HOH K 6 .   ? 0.609  -20.316 21.605  1.00 48.96 ? 2030 HOH A O   1 
HETATM 2432 O  O   . HOH K 6 .   ? 7.682  -0.749  18.428  1.00 28.66 ? 2031 HOH A O   1 
HETATM 2433 O  O   . HOH K 6 .   ? 15.860 4.514   28.360  1.00 40.26 ? 2032 HOH A O   1 
HETATM 2434 O  O   . HOH K 6 .   ? 13.709 4.062   24.309  1.00 17.66 ? 2033 HOH A O   1 
HETATM 2435 O  O   . HOH K 6 .   ? 17.789 3.368   25.407  1.00 27.67 ? 2034 HOH A O   1 
HETATM 2436 O  O   . HOH K 6 .   ? 31.959 -10.741 13.915  1.00 25.11 ? 2035 HOH A O   1 
HETATM 2437 O  O   . HOH K 6 .   ? 19.573 2.862   27.080  1.00 23.34 ? 2036 HOH A O   1 
HETATM 2438 O  O   . HOH K 6 .   ? 30.780 1.381   28.612  1.00 31.16 ? 2037 HOH A O   1 
HETATM 2439 O  O   . HOH K 6 .   ? 24.949 1.462   38.963  1.00 45.77 ? 2038 HOH A O   1 
HETATM 2440 O  O   . HOH K 6 .   ? 31.644 -2.227  38.567  1.00 50.32 ? 2039 HOH A O   1 
HETATM 2441 O  O   . HOH K 6 .   ? 38.086 -13.001 14.135  1.00 34.91 ? 2040 HOH A O   1 
HETATM 2442 O  O   . HOH K 6 .   ? 36.449 -18.555 22.219  1.00 46.34 ? 2041 HOH A O   1 
HETATM 2443 O  O   . HOH K 6 .   ? 37.176 -16.905 17.152  1.00 32.32 ? 2042 HOH A O   1 
HETATM 2444 O  O   . HOH K 6 .   ? 38.432 -20.229 19.042  1.00 39.18 ? 2043 HOH A O   1 
HETATM 2445 O  O   . HOH K 6 .   ? 37.506 -20.563 12.904  1.00 46.51 ? 2044 HOH A O   1 
HETATM 2446 O  O   . HOH K 6 .   ? 37.581 -0.382  25.697  1.00 52.19 ? 2045 HOH A O   1 
HETATM 2447 O  O   . HOH K 6 .   ? 37.899 -4.759  25.420  1.00 32.32 ? 2046 HOH A O   1 
HETATM 2448 O  O   . HOH K 6 .   ? 33.038 -2.416  26.797  1.00 45.50 ? 2047 HOH A O   1 
HETATM 2449 O  O   . HOH K 6 .   ? 19.732 -15.703 34.805  1.00 41.28 ? 2048 HOH A O   1 
HETATM 2450 O  O   . HOH K 6 .   ? 18.143 -18.844 31.341  1.00 24.01 ? 2049 HOH A O   1 
HETATM 2451 O  O   . HOH K 6 .   ? 19.306 -10.679 36.130  1.00 51.29 ? 2050 HOH A O   1 
HETATM 2452 O  O   . HOH K 6 .   ? 31.396 -16.665 24.632  1.00 21.22 ? 2051 HOH A O   1 
HETATM 2453 O  O   . HOH K 6 .   ? 26.151 -27.457 24.196  1.00 32.56 ? 2052 HOH A O   1 
HETATM 2454 O  O   . HOH K 6 .   ? 25.465 -1.853  33.007  1.00 26.62 ? 2053 HOH A O   1 
HETATM 2455 O  O   . HOH K 6 .   ? 28.790 -2.297  32.733  1.00 21.35 ? 2054 HOH A O   1 
HETATM 2456 O  O   . HOH K 6 .   ? 21.351 -1.077  40.127  1.00 50.79 ? 2055 HOH A O   1 
HETATM 2457 O  O   . HOH K 6 .   ? 19.218 -13.629 30.993  1.00 16.75 ? 2056 HOH A O   1 
HETATM 2458 O  O   . HOH K 6 .   ? 17.270 -2.336  36.946  1.00 48.06 ? 2057 HOH A O   1 
HETATM 2459 O  O   . HOH K 6 .   ? 11.100 -13.311 32.182  1.00 31.72 ? 2058 HOH A O   1 
HETATM 2460 O  O   . HOH K 6 .   ? 4.471  -2.498  29.087  1.00 46.49 ? 2059 HOH A O   1 
HETATM 2461 O  O   . HOH K 6 .   ? 10.457 -5.340  34.248  1.00 36.49 ? 2060 HOH A O   1 
HETATM 2462 O  O   . HOH K 6 .   ? 10.645 -1.448  31.308  1.00 40.61 ? 2061 HOH A O   1 
HETATM 2463 O  O   . HOH K 6 .   ? -1.546 -1.807  21.684  1.00 33.90 ? 2062 HOH A O   1 
HETATM 2464 O  O   . HOH K 6 .   ? 1.565  -12.772 18.085  1.00 20.74 ? 2063 HOH A O   1 
HETATM 2465 O  O   . HOH K 6 .   ? -1.883 -12.720 23.179  1.00 36.53 ? 2064 HOH A O   1 
HETATM 2466 O  O   . HOH K 6 .   ? 3.444  -14.393 19.310  1.00 18.75 ? 2065 HOH A O   1 
HETATM 2467 O  O   . HOH K 6 .   ? 3.224  -18.937 22.682  1.00 25.33 ? 2066 HOH A O   1 
HETATM 2468 O  O   . HOH K 6 .   ? 33.038 1.375   19.631  1.00 34.18 ? 2067 HOH A O   1 
HETATM 2469 O  O   . HOH K 6 .   ? 0.842  -20.647 25.605  1.00 37.28 ? 2068 HOH A O   1 
HETATM 2470 O  O   . HOH K 6 .   ? 0.310  -16.680 32.272  1.00 23.44 ? 2069 HOH A O   1 
HETATM 2471 O  O   . HOH K 6 .   ? -1.632 -19.891 31.615  0.60 12.79 ? 2070 HOH A O   1 
HETATM 2472 O  O   . HOH K 6 .   ? -2.630 -18.748 25.939  1.00 30.17 ? 2071 HOH A O   1 
HETATM 2473 O  O   . HOH K 6 .   ? -1.782 -16.354 23.828  1.00 24.04 ? 2072 HOH A O   1 
HETATM 2474 O  O   . HOH K 6 .   ? 36.528 -1.385  18.637  1.00 43.95 ? 2073 HOH A O   1 
HETATM 2475 O  O   . HOH K 6 .   ? 34.923 -7.001  15.244  1.00 42.63 ? 2074 HOH A O   1 
HETATM 2476 O  O   . HOH K 6 .   ? 2.751  -15.993 15.914  1.00 28.38 ? 2075 HOH A O   1 
HETATM 2477 O  O   . HOH K 6 .   ? 2.308  -19.353 18.078  1.00 34.11 ? 2076 HOH A O   1 
HETATM 2478 O  O   . HOH K 6 .   ? 1.519  -23.717 14.215  1.00 48.55 ? 2077 HOH A O   1 
HETATM 2479 O  O   . HOH K 6 .   ? 10.843 -27.406 19.926  1.00 32.86 ? 2078 HOH A O   1 
HETATM 2480 O  O   . HOH K 6 .   ? 11.520 -25.342 23.776  1.00 26.09 ? 2079 HOH A O   1 
HETATM 2481 O  O   . HOH K 6 .   ? 25.207 -30.486 23.452  1.00 48.95 ? 2080 HOH A O   1 
HETATM 2482 O  O   . HOH K 6 .   ? 30.518 -12.856 13.267  1.00 34.06 ? 2081 HOH A O   1 
HETATM 2483 O  O   . HOH K 6 .   ? 29.392 -9.850  11.030  1.00 24.11 ? 2082 HOH A O   1 
HETATM 2484 O  O   . HOH K 6 .   ? 16.456 -19.794 10.307  1.00 48.98 ? 2083 HOH A O   1 
HETATM 2485 O  O   . HOH K 6 .   ? 18.750 -2.713  7.584   1.00 11.24 ? 2084 HOH A O   1 
HETATM 2486 O  O   . HOH K 6 .   ? 3.583  -11.763 13.857  1.00 26.63 ? 2085 HOH A O   1 
HETATM 2487 O  O   . HOH K 6 .   ? 23.371 -8.401  5.106   1.00 23.32 ? 2086 HOH A O   1 
HETATM 2488 O  O   . HOH K 6 .   ? 20.442 -9.755  2.999   1.00 21.66 ? 2087 HOH A O   1 
HETATM 2489 O  O   . HOH K 6 .   ? 22.538 -6.050  2.243   1.00 27.99 ? 2088 HOH A O   1 
HETATM 2490 O  O   . HOH K 6 .   ? 13.829 -2.875  11.088  0.50 12.63 ? 2089 HOH A O   1 
HETATM 2491 O  O   . HOH K 6 .   ? 16.614 -5.317  11.563  0.50 16.32 ? 2090 HOH A O   1 
HETATM 2492 O  O   . HOH K 6 .   ? 10.771 -5.905  9.724   1.00 39.70 ? 2091 HOH A O   1 
HETATM 2493 O  O   . HOH K 6 .   ? 12.696 -1.166  8.910   1.00 26.28 ? 2092 HOH A O   1 
HETATM 2494 O  O   . HOH K 6 .   ? 14.988 -3.264  11.207  0.50 12.67 ? 2093 HOH A O   1 
HETATM 2495 O  O   . HOH K 6 .   ? 11.985 -4.312  7.004   0.50 23.59 ? 2094 HOH A O   1 
HETATM 2496 O  O   . HOH K 6 .   ? 16.171 -7.635  9.977   0.50 13.52 ? 2095 HOH A O   1 
HETATM 2497 O  O   . HOH K 6 .   ? 27.602 6.811   23.119  1.00 37.94 ? 2096 HOH A O   1 
HETATM 2498 O  O   . HOH K 6 .   ? 21.014 11.604  29.102  1.00 33.00 ? 2097 HOH A O   1 
HETATM 2499 O  O   . HOH K 6 .   ? 27.099 10.570  25.725  1.00 37.70 ? 2098 HOH A O   1 
HETATM 2500 O  O   . HOH K 6 .   ? 17.696 -1.859  2.244   0.30 16.55 ? 2099 HOH A O   1 
HETATM 2501 O  O   . HOH K 6 .   ? 11.137 -5.220  3.014   1.00 35.15 ? 2100 HOH A O   1 
HETATM 2502 O  O   . HOH K 6 .   ? 20.111 -4.262  0.437   1.00 20.59 ? 2101 HOH A O   1 
HETATM 2503 O  O   . HOH K 6 .   ? 11.262 -12.310 4.280   1.00 25.00 ? 2102 HOH A O   1 
HETATM 2504 O  O   . HOH K 6 .   ? 9.583  -7.867  3.563   1.00 30.67 ? 2103 HOH A O   1 
HETATM 2505 O  O   . HOH K 6 .   ? 10.097 -10.131 2.223   1.00 25.30 ? 2104 HOH A O   1 
HETATM 2506 O  O   . HOH K 6 .   ? 9.944  -8.930  8.900   1.00 22.37 ? 2105 HOH A O   1 
HETATM 2507 O  O   . HOH K 6 .   ? 15.440 -15.244 3.255   1.00 18.92 ? 2106 HOH A O   1 
HETATM 2508 O  O   . HOH K 6 .   ? 16.704 -15.802 7.761   1.00 19.30 ? 2107 HOH A O   1 
HETATM 2509 O  O   . HOH K 6 .   ? 10.635 -14.348 5.945   1.00 38.09 ? 2108 HOH A O   1 
HETATM 2510 O  O   . HOH K 6 .   ? 15.885 -12.594 3.789   1.00 20.54 ? 2109 HOH A O   1 
HETATM 2511 O  O   . HOH K 6 .   ? 15.904 -17.149 5.482   1.00 27.99 ? 2110 HOH A O   1 
HETATM 2512 O  O   . HOH K 6 .   ? 18.280 -15.724 8.192   1.00 21.61 ? 2111 HOH A O   1 
HETATM 2513 O  O   . HOH K 6 .   ? 22.410 -10.971 6.281   0.40 16.56 ? 2112 HOH A O   1 
HETATM 2514 O  O   . HOH K 6 .   ? 17.934 -10.744 2.331   1.00 19.87 ? 2113 HOH A O   1 
HETATM 2515 O  O   . HOH K 6 .   ? 17.145 -17.956 14.862  0.20 11.73 ? 2114 HOH A O   1 
HETATM 2516 O  O   . HOH K 6 .   ? 19.407 -18.358 13.304  1.00 19.32 ? 2115 HOH A O   1 
HETATM 2517 O  O   . HOH K 6 .   ? 29.882 -16.414 19.613  1.00 12.18 ? 2116 HOH A O   1 
HETATM 2518 O  O   . HOH K 6 .   ? 34.743 -13.749 14.380  1.00 36.67 ? 2117 HOH A O   1 
HETATM 2519 O  O   . HOH K 6 .   ? 36.528 -18.737 19.161  1.00 31.43 ? 2118 HOH A O   1 
HETATM 2520 O  O   . HOH K 6 .   ? 34.484 -20.707 12.350  1.00 31.95 ? 2119 HOH A O   1 
HETATM 2521 O  O   . HOH K 6 .   ? 35.101 -17.688 15.298  1.00 26.17 ? 2120 HOH A O   1 
HETATM 2522 O  O   . HOH K 6 .   ? 28.975 -22.709 15.469  1.00 43.19 ? 2121 HOH A O   1 
HETATM 2523 O  O   . HOH K 6 .   ? 31.002 -24.919 17.782  1.00 37.95 ? 2122 HOH A O   1 
HETATM 2524 O  O   . HOH K 6 .   ? 23.305 -26.751 21.761  0.50 16.39 ? 2123 HOH A O   1 
HETATM 2525 O  O   . HOH K 6 .   ? 27.103 -17.092 29.769  1.00 18.01 ? 2124 HOH A O   1 
HETATM 2526 O  O   . HOH K 6 .   ? 19.444 -19.042 29.015  0.30 12.16 ? 2125 HOH A O   1 
HETATM 2527 O  O   . HOH K 6 .   ? 17.572 -17.187 36.383  1.00 47.86 ? 2126 HOH A O   1 
HETATM 2528 O  O   . HOH K 6 .   ? 20.775 -12.621 35.189  1.00 38.00 ? 2127 HOH A O   1 
HETATM 2529 O  O   . HOH K 6 .   ? 24.174 -12.416 33.854  1.00 38.03 ? 2128 HOH A O   1 
HETATM 2530 O  O   . HOH K 6 .   ? 20.900 -19.312 37.448  1.00 58.52 ? 2129 HOH A O   1 
HETATM 2531 O  O   . HOH K 6 .   ? 21.883 -13.336 34.124  0.70 44.93 ? 2130 HOH A O   1 
HETATM 2532 O  O   . HOH K 6 .   ? 24.853 -21.344 34.562  1.00 26.64 ? 2131 HOH A O   1 
HETATM 2533 O  O   . HOH K 6 .   ? 20.924 -20.290 29.737  0.40 15.86 ? 2132 HOH A O   1 
HETATM 2534 O  O   . HOH K 6 .   ? 20.560 -19.863 30.285  0.60 10.58 ? 2133 HOH A O   1 
HETATM 2535 O  O   . HOH K 6 .   ? 20.949 -24.529 28.240  1.00 21.19 ? 2134 HOH A O   1 
HETATM 2536 O  O   . HOH K 6 .   ? 24.238 -25.975 30.610  1.00 40.33 ? 2135 HOH A O   1 
HETATM 2537 O  O   . HOH K 6 .   ? 24.954 -23.851 32.197  1.00 41.35 ? 2136 HOH A O   1 
HETATM 2538 O  O   . HOH K 6 .   ? 21.210 -22.414 31.304  1.00 21.55 ? 2137 HOH A O   1 
HETATM 2539 O  O   . HOH K 6 .   ? 30.578 -17.906 26.948  1.00 23.21 ? 2138 HOH A O   1 
HETATM 2540 O  O   . HOH K 6 .   ? 31.963 -25.102 30.917  0.80 26.11 ? 2139 HOH A O   1 
HETATM 2541 O  O   . HOH K 6 .   ? 35.265 -20.339 29.455  0.50 21.27 ? 2140 HOH A O   1 
HETATM 2542 O  O   . HOH K 6 .   ? 35.210 -22.368 26.195  1.00 40.13 ? 2141 HOH A O   1 
HETATM 2543 O  O   . HOH K 6 .   ? 34.612 -25.372 28.793  1.00 33.87 ? 2142 HOH A O   1 
HETATM 2544 O  O   . HOH K 6 .   ? 33.530 -23.857 22.599  1.00 45.58 ? 2143 HOH A O   1 
HETATM 2545 O  O   . HOH K 6 .   ? 25.108 -24.938 24.286  1.00 19.86 ? 2144 HOH A O   1 
HETATM 2546 O  O   . HOH K 6 .   ? 31.858 -25.002 20.249  1.00 37.47 ? 2145 HOH A O   1 
HETATM 2547 O  O   . HOH K 6 .   ? 30.139 -17.016 22.238  1.00 14.97 ? 2146 HOH A O   1 
HETATM 2548 O  O   . HOH K 6 .   ? 17.125 -14.070 29.178  1.00 20.69 ? 2147 HOH A O   1 
HETATM 2549 O  O   . HOH K 6 .   ? 14.688 -13.175 29.832  1.00 23.70 ? 2148 HOH A O   1 
HETATM 2550 O  O   . HOH K 6 .   ? 16.453 -17.166 29.333  1.00 20.90 ? 2149 HOH A O   1 
HETATM 2551 O  O   . HOH K 6 .   ? 9.444  -18.313 31.851  0.50 10.51 ? 2150 HOH A O   1 
HETATM 2552 O  O   . HOH K 6 .   ? 10.406 -11.659 29.757  1.00 18.97 ? 2151 HOH A O   1 
HETATM 2553 O  O   . HOH K 6 .   ? 7.402  -10.858 31.031  1.00 27.92 ? 2152 HOH A O   1 
HETATM 2554 O  O   . HOH K 6 .   ? 8.497  -17.330 32.180  0.50 15.30 ? 2153 HOH A O   1 
HETATM 2555 O  O   . HOH K 6 .   ? 11.632 -15.281 30.153  1.00 22.74 ? 2154 HOH A O   1 
HETATM 2556 O  O   . HOH K 6 .   ? 3.151  -9.501  31.319  1.00 31.16 ? 2155 HOH A O   1 
HETATM 2557 O  O   . HOH K 6 .   ? 5.481  -13.387 31.874  1.00 29.10 ? 2156 HOH A O   1 
HETATM 2558 O  O   . HOH K 6 .   ? -1.249 -8.870  33.197  1.00 27.63 ? 2157 HOH A O   1 
HETATM 2559 O  O   . HOH K 6 .   ? -0.626 -15.236 31.847  0.50 18.27 ? 2158 HOH A O   1 
HETATM 2560 O  O   . HOH K 6 .   ? -3.278 -10.641 25.041  1.00 32.66 ? 2159 HOH A O   1 
HETATM 2561 O  O   . HOH K 6 .   ? -2.153 -11.932 31.770  1.00 24.69 ? 2160 HOH A O   1 
HETATM 2562 O  O   . HOH K 6 .   ? -3.112 -14.326 25.028  1.00 35.16 ? 2161 HOH A O   1 
HETATM 2563 O  O   . HOH K 6 .   ? -0.149 -5.890  30.523  1.00 36.55 ? 2162 HOH A O   1 
HETATM 2564 O  O   . HOH K 6 .   ? -0.097 -7.207  24.208  0.50 16.51 ? 2163 HOH A O   1 
HETATM 2565 O  O   . HOH K 6 .   ? -4.393 -7.880  25.466  1.00 26.91 ? 2164 HOH A O   1 
HETATM 2566 O  O   . HOH K 6 .   ? -4.867 -9.237  29.574  1.00 40.90 ? 2165 HOH A O   1 
HETATM 2567 O  O   . HOH K 6 .   ? -3.778 -8.571  32.642  1.00 28.59 ? 2166 HOH A O   1 
HETATM 2568 O  O   . HOH K 6 .   ? 11.794 -10.371 33.365  0.50 28.25 ? 2167 HOH A O   1 
HETATM 2569 O  O   . HOH K 6 .   ? 10.561 -9.522  33.513  0.50 22.04 ? 2168 HOH A O   1 
HETATM 2570 O  O   . HOH K 6 .   ? 11.141 -4.027  32.170  1.00 26.01 ? 2169 HOH A O   1 
HETATM 2571 O  O   . HOH K 6 .   ? 16.403 -12.098 33.778  1.00 34.09 ? 2170 HOH A O   1 
HETATM 2572 O  O   . HOH K 6 .   ? 13.053 -10.145 32.531  0.50 17.60 ? 2171 HOH A O   1 
HETATM 2573 O  O   . HOH K 6 .   ? 13.060 -10.833 30.511  1.00 20.03 ? 2172 HOH A O   1 
HETATM 2574 O  O   . HOH K 6 .   ? 18.407 -6.405  35.219  1.00 41.39 ? 2173 HOH A O   1 
HETATM 2575 O  O   . HOH K 6 .   ? 17.861 -4.808  33.405  1.00 28.00 ? 2174 HOH A O   1 
HETATM 2576 O  O   . HOH K 6 .   ? 19.192 -11.732 33.219  1.00 25.88 ? 2175 HOH A O   1 
HETATM 2577 O  O   . HOH K 6 .   ? 25.287 -10.230 33.627  1.00 27.68 ? 2176 HOH A O   1 
HETATM 2578 O  O   . HOH K 6 .   ? 25.351 -13.212 31.049  1.00 16.63 ? 2177 HOH A O   1 
HETATM 2579 O  O   . HOH K 6 .   ? 21.822 -12.860 30.541  1.00 16.24 ? 2178 HOH A O   1 
HETATM 2580 O  O   . HOH K 6 .   ? 31.328 -8.296  30.817  1.00 28.89 ? 2179 HOH A O   1 
HETATM 2581 O  O   . HOH K 6 .   ? 32.534 -10.850 28.214  1.00 24.42 ? 2180 HOH A O   1 
HETATM 2582 O  O   . HOH K 6 .   ? 31.942 -9.041  26.401  1.00 32.01 ? 2181 HOH A O   1 
HETATM 2583 O  O   . HOH K 6 .   ? 30.248 -7.257  28.313  1.00 26.53 ? 2182 HOH A O   1 
HETATM 2584 O  O   . HOH K 6 .   ? 33.813 -4.509  25.259  1.00 26.14 ? 2183 HOH A O   1 
HETATM 2585 O  O   . HOH K 6 .   ? 30.606 1.482   20.668  1.00 27.29 ? 2184 HOH A O   1 
HETATM 2586 O  O   . HOH K 6 .   ? 33.697 -6.709  22.928  1.00 17.52 ? 2185 HOH A O   1 
HETATM 2587 O  O   . HOH K 6 .   ? 35.512 -0.251  24.340  1.00 41.27 ? 2186 HOH A O   1 
HETATM 2588 O  O   . HOH K 6 .   ? 31.495 -0.875  25.880  1.00 32.46 ? 2187 HOH A O   1 
HETATM 2589 O  O   . HOH K 6 .   ? 33.075 -3.913  16.545  1.00 39.06 ? 2188 HOH A O   1 
HETATM 2590 O  O   . HOH K 6 .   ? 34.084 -0.977  19.167  1.00 30.20 ? 2189 HOH A O   1 
HETATM 2591 O  O   . HOH K 6 .   ? 37.651 -8.382  23.029  0.50 16.52 ? 2190 HOH A O   1 
HETATM 2592 O  O   . HOH K 6 .   ? 35.350 -10.579 15.231  1.00 36.77 ? 2191 HOH A O   1 
HETATM 2593 O  O   . HOH K 6 .   ? 36.041 -5.308  16.958  1.00 36.38 ? 2192 HOH A O   1 
HETATM 2594 O  O   . HOH K 6 .   ? 32.659 -9.019  15.863  1.00 26.25 ? 2193 HOH A O   1 
HETATM 2595 O  O   . HOH K 6 .   ? 37.081 -6.202  21.732  1.00 33.69 ? 2194 HOH A O   1 
HETATM 2596 O  O   . HOH K 6 .   ? 30.814 -6.885  16.792  1.00 18.19 ? 2195 HOH A O   1 
HETATM 2597 O  O   . HOH K 6 .   ? 28.701 -4.581  15.988  1.00 23.75 ? 2196 HOH A O   1 
HETATM 2598 O  O   . HOH K 6 .   ? 31.330 -8.891  11.901  1.00 32.52 ? 2197 HOH A O   1 
HETATM 2599 O  O   . HOH K 6 .   ? 31.338 -6.516  11.639  1.00 33.90 ? 2198 HOH A O   1 
HETATM 2600 O  O   . HOH K 6 .   ? 8.096  -21.610 12.088  1.00 41.78 ? 2199 HOH A O   1 
HETATM 2601 O  O   . HOH K 6 .   ? 4.680  -20.173 20.755  1.00 26.08 ? 2200 HOH A O   1 
HETATM 2602 O  O   . HOH K 6 .   ? 3.866  -17.002 18.328  1.00 18.32 ? 2201 HOH A O   1 
HETATM 2603 O  O   . HOH K 6 .   ? 3.874  -21.848 16.909  1.00 30.76 ? 2202 HOH A O   1 
HETATM 2604 O  O   . HOH K 6 .   ? 2.832  -19.894 14.727  1.00 32.88 ? 2203 HOH A O   1 
HETATM 2605 O  O   . HOH K 6 .   ? 10.131 -23.869 13.280  1.00 38.12 ? 2204 HOH A O   1 
HETATM 2606 O  O   . HOH K 6 .   ? 7.915  -24.102 21.371  0.60 19.39 ? 2205 HOH A O   1 
HETATM 2607 O  O   . HOH K 6 .   ? 7.872  -23.522 21.987  0.40 14.46 ? 2206 HOH A O   1 
HETATM 2608 O  O   . HOH K 6 .   ? 10.658 -24.603 20.744  1.00 25.96 ? 2207 HOH A O   1 
HETATM 2609 O  O   . HOH K 6 .   ? 19.403 -18.203 23.794  1.00 12.25 ? 2208 HOH A O   1 
HETATM 2610 O  O   . HOH K 6 .   ? 13.032 -28.229 21.058  1.00 26.84 ? 2209 HOH A O   1 
HETATM 2611 O  O   . HOH K 6 .   ? 23.028 -25.843 26.111  1.00 29.72 ? 2210 HOH A O   1 
HETATM 2612 O  O   . HOH K 6 .   ? 20.475 -30.464 22.557  1.00 25.68 ? 2211 HOH A O   1 
HETATM 2613 O  O   . HOH K 6 .   ? 23.412 -28.612 24.511  1.00 34.71 ? 2212 HOH A O   1 
HETATM 2614 O  O   . HOH K 6 .   ? 16.329 -31.289 27.890  1.00 24.13 ? 2213 HOH A O   1 
HETATM 2615 O  O   . HOH K 6 .   ? 18.831 -31.850 27.062  1.00 34.99 ? 2214 HOH A O   1 
HETATM 2616 O  O   . HOH K 6 .   ? 21.212 -31.250 30.942  1.00 57.42 ? 2215 HOH A O   1 
HETATM 2617 O  O   . HOH K 6 .   ? 15.082 -34.622 21.702  1.00 34.72 ? 2216 HOH A O   1 
HETATM 2618 O  O   . HOH K 6 .   ? 13.253 -30.913 22.124  1.00 20.37 ? 2217 HOH A O   1 
HETATM 2619 O  O   . HOH K 6 .   ? 21.433 -34.007 18.424  1.00 42.58 ? 2218 HOH A O   1 
HETATM 2620 O  O   . HOH K 6 .   ? 15.915 -34.610 19.346  1.00 29.65 ? 2219 HOH A O   1 
HETATM 2621 O  O   . HOH K 6 .   ? 16.998 -36.458 17.650  1.00 31.19 ? 2220 HOH A O   1 
HETATM 2622 O  O   . HOH K 6 .   ? 21.790 -31.556 20.702  1.00 37.52 ? 2221 HOH A O   1 
HETATM 2623 O  O   . HOH K 6 .   ? 25.516 -29.237 11.174  1.00 40.62 ? 2222 HOH A O   1 
HETATM 2624 O  O   . HOH K 6 .   ? 18.200 -34.226 14.351  1.00 34.02 ? 2223 HOH A O   1 
HETATM 2625 O  O   . HOH K 6 .   ? 16.362 -26.463 9.593   1.00 37.16 ? 2224 HOH A O   1 
HETATM 2626 O  O   . HOH K 6 .   ? 17.873 -30.098 11.602  1.00 27.26 ? 2225 HOH A O   1 
HETATM 2627 O  O   . HOH K 6 .   ? 16.898 -24.060 11.482  1.00 33.48 ? 2226 HOH A O   1 
HETATM 2628 O  O   . HOH K 6 .   ? 19.259 -25.206 12.234  1.00 28.35 ? 2227 HOH A O   1 
HETATM 2629 O  O   . HOH K 6 .   ? 16.989 -30.719 13.957  1.00 25.12 ? 2228 HOH A O   1 
HETATM 2630 O  O   . HOH K 6 .   ? 23.455 -27.813 20.829  0.50 23.03 ? 2229 HOH A O   1 
HETATM 2631 O  O   . HOH K 6 .   ? 21.806 -19.320 14.456  1.00 15.98 ? 2230 HOH A O   1 
HETATM 2632 O  O   . HOH K 6 .   ? 16.390 -18.896 16.803  1.00 16.99 ? 2231 HOH A O   1 
HETATM 2633 O  O   . HOH K 6 .   ? 9.778  -25.540 18.470  1.00 39.25 ? 2232 HOH A O   1 
HETATM 2634 O  O   . HOH K 6 .   ? 5.097  -17.249 12.287  1.00 51.92 ? 2233 HOH A O   1 
HETATM 2635 O  O   . HOH K 6 .   ? 14.070 -17.757 12.021  0.80 21.30 ? 2234 HOH A O   1 
HETATM 2636 O  O   . HOH K 6 .   ? 8.311  -10.399 10.753  0.50 21.47 ? 2235 HOH A O   1 
HETATM 2637 O  O   . HOH K 6 .   ? 7.237  -14.672 11.069  0.30 16.92 ? 2236 HOH A O   1 
HETATM 2638 O  O   . HOH K 6 .   ? 19.238 -19.026 10.803  1.00 26.90 ? 2237 HOH A O   1 
HETATM 2639 O  O   . HOH K 6 .   ? 16.951 -17.990 13.700  0.80 18.32 ? 2238 HOH A O   1 
HETATM 2640 O  O   . HOH K 6 .   ? 4.562  -9.258  14.279  1.00 18.59 ? 2239 HOH A O   1 
HETATM 2641 O  O   . HOH K 6 .   ? 11.923 -3.687  11.904  1.00 26.75 ? 2240 HOH A O   1 
HETATM 2642 O  O   . HOH K 6 .   ? 15.369 -0.719  13.506  0.50 13.99 ? 2241 HOH A O   1 
HETATM 2643 O  O   . HOH K 6 .   ? 15.433 -1.287  12.569  0.50 12.87 ? 2242 HOH A O   1 
HETATM 2644 O  O   . HOH K 6 .   ? 15.778 0.107   16.131  1.00 10.71 ? 2243 HOH A O   1 
HETATM 2645 O  O   . HOH K 6 .   ? 25.461 8.662   22.323  1.00 26.28 ? 2244 HOH A O   1 
HETATM 2646 O  O   . HOH K 6 .   ? 25.662 5.919   24.282  1.00 19.09 ? 2245 HOH A O   1 
HETATM 2647 O  O   . HOH K 6 .   ? 21.506 13.268  23.191  1.00 31.34 ? 2246 HOH A O   1 
HETATM 2648 O  O   . HOH K 6 .   ? 19.767 13.429  20.773  0.50 16.74 ? 2247 HOH A O   1 
HETATM 2649 O  O   . HOH K 6 .   ? 25.251 7.915   26.158  1.00 28.24 ? 2248 HOH A O   1 
HETATM 2650 O  O   . HOH K 6 .   ? 18.231 8.087   25.136  1.00 30.85 ? 2249 HOH A O   1 
HETATM 2651 O  O   . HOH K 6 .   ? 25.024 11.087  24.183  1.00 29.63 ? 2250 HOH A O   1 
HETATM 2652 O  O   . HOH K 6 .   ? 23.042 9.741   28.587  1.00 34.06 ? 2251 HOH A O   1 
HETATM 2653 O  O   . HOH K 6 .   ? 19.661 9.666   28.163  0.50 20.58 ? 2252 HOH A O   1 
HETATM 2654 O  O   . HOH K 6 .   ? 19.415 15.394  26.854  1.00 26.37 ? 2253 HOH A O   1 
HETATM 2655 O  O   . HOH K 6 .   ? 18.660 11.733  26.988  0.50 19.71 ? 2254 HOH A O   1 
HETATM 2656 O  O   . HOH K 6 .   ? 18.852 8.300   21.869  1.00 20.39 ? 2255 HOH A O   1 
HETATM 2657 O  O   . HOH K 6 .   ? 8.958  -16.661 7.879   1.00 42.26 ? 2256 HOH A O   1 
HETATM 2658 O  O   . HOH K 6 .   ? 11.474 -19.400 9.459   1.00 44.32 ? 2257 HOH A O   1 
HETATM 2659 O  O   . HOH K 6 .   ? 13.299 -18.024 5.556   1.00 28.34 ? 2258 HOH A O   1 
HETATM 2660 O  O   . HOH K 6 .   ? 14.606 -16.800 8.689   1.00 39.38 ? 2259 HOH A O   1 
HETATM 2661 O  O   . HOH K 6 .   ? 10.703 -12.378 8.974   1.00 28.60 ? 2260 HOH A O   1 
HETATM 2662 O  O   . HOH K 6 .   ? 14.043 -18.825 11.082  0.20 8.20  ? 2261 HOH A O   1 
HETATM 2663 O  O   . HOH K 6 .   ? 8.313  -15.214 10.353  0.70 14.69 ? 2262 HOH A O   1 
HETATM 2664 O  O   . HOH K 6 .   ? 12.191 -26.038 14.978  1.00 32.53 ? 2263 HOH A O   1 
HETATM 2665 O  O   . HOH K 6 .   ? 10.907 -21.248 11.115  1.00 41.68 ? 2264 HOH A O   1 
HETATM 2666 O  O   . HOH K 6 .   ? 14.750 -19.643 14.704  1.00 17.60 ? 2265 HOH A O   1 
HETATM 2667 O  O   . HOH K 6 .   ? 14.597 -23.672 12.040  0.50 23.30 ? 2266 HOH A O   1 
HETATM 2668 O  O   . HOH K 6 .   ? 13.435 -23.948 10.124  1.00 33.39 ? 2267 HOH A O   1 
HETATM 2669 O  O   . HOH L 6 .   ? 10.424 25.103  10.682  1.00 53.86 ? 2001 HOH F O   1 
HETATM 2670 O  O   . HOH L 6 .   ? 31.941 -4.057  12.117  1.00 40.64 ? 2002 HOH F O   1 
HETATM 2671 O  O   . HOH L 6 .   ? 31.105 -4.110  14.595  1.00 31.22 ? 2003 HOH F O   1 
HETATM 2672 O  O   . HOH L 6 .   ? 30.653 -1.980  13.421  1.00 41.51 ? 2004 HOH F O   1 
HETATM 2673 O  O   . HOH L 6 .   ? 29.127 -0.081  15.684  1.00 28.75 ? 2005 HOH F O   1 
HETATM 2674 O  O   . HOH L 6 .   ? 4.121  16.309  1.083   1.00 38.73 ? 2006 HOH F O   1 
HETATM 2675 O  O   . HOH L 6 .   ? 37.351 7.967   -8.779  1.00 46.01 ? 2007 HOH F O   1 
HETATM 2676 O  O   . HOH L 6 .   ? 1.862  20.221  -3.785  1.00 47.96 ? 2008 HOH F O   1 
HETATM 2677 O  O   . HOH L 6 .   ? 35.248 -4.543  8.928   1.00 37.07 ? 2009 HOH F O   1 
HETATM 2678 O  O   . HOH L 6 .   ? 15.344 -1.051  9.735   1.00 19.67 ? 2010 HOH F O   1 
HETATM 2679 O  O   . HOH L 6 .   ? 9.681  -5.779  4.950   1.00 42.52 ? 2011 HOH F O   1 
HETATM 2680 O  O   . HOH L 6 .   ? 8.084  -3.746  4.406   1.00 45.70 ? 2012 HOH F O   1 
HETATM 2681 O  O   . HOH L 6 .   ? 29.335 -4.405  -1.826  1.00 32.15 ? 2013 HOH F O   1 
HETATM 2682 O  O   . HOH L 6 .   ? 2.130  12.008  1.945   1.00 39.82 ? 2014 HOH F O   1 
HETATM 2683 O  O   . HOH L 6 .   ? 5.349  14.744  3.595   1.00 36.46 ? 2015 HOH F O   1 
HETATM 2684 O  O   . HOH L 6 .   ? 6.250  13.145  6.734   1.00 31.34 ? 2016 HOH F O   1 
HETATM 2685 O  O   . HOH L 6 .   ? 35.312 7.351   -12.051 1.00 42.62 ? 2017 HOH F O   1 
HETATM 2686 O  O   . HOH L 6 .   ? 38.505 -3.445  -5.550  1.00 51.00 ? 2018 HOH F O   1 
HETATM 2687 O  O   . HOH L 6 .   ? 3.320  15.766  -0.966  1.00 44.76 ? 2019 HOH F O   1 
HETATM 2688 O  O   . HOH L 6 .   ? 3.923  18.542  -3.248  1.00 44.52 ? 2020 HOH F O   1 
HETATM 2689 O  O   . HOH L 6 .   ? 13.758 1.227   9.001   1.00 24.17 ? 2021 HOH F O   1 
HETATM 2690 O  O   . HOH L 6 .   ? 11.312 0.696   3.258   1.00 35.65 ? 2022 HOH F O   1 
HETATM 2691 O  O   . HOH L 6 .   ? 38.464 -3.660  5.963   1.00 53.51 ? 2023 HOH F O   1 
HETATM 2692 O  O   . HOH L 6 .   ? 11.915 -3.973  5.425   0.50 18.93 ? 2024 HOH F O   1 
HETATM 2693 O  O   . HOH L 6 .   ? 10.971 -1.867  3.352   1.00 36.23 ? 2025 HOH F O   1 
HETATM 2694 O  O   . HOH L 6 .   ? 36.848 2.296   -2.904  1.00 34.90 ? 2026 HOH F O   1 
HETATM 2695 O  O   . HOH L 6 .   ? 39.974 4.111   -3.014  1.00 40.44 ? 2027 HOH F O   1 
HETATM 2696 O  O   . HOH L 6 .   ? 7.248  3.425   9.192   1.00 38.76 ? 2028 HOH F O   1 
HETATM 2697 O  O   . HOH L 6 .   ? 7.340  5.026   4.990   1.00 30.57 ? 2029 HOH F O   1 
HETATM 2698 O  O   . HOH L 6 .   ? 7.157  11.158  5.291   1.00 28.33 ? 2030 HOH F O   1 
HETATM 2699 O  O   . HOH L 6 .   ? 2.021  11.018  4.406   1.00 36.05 ? 2031 HOH F O   1 
HETATM 2700 O  O   . HOH L 6 .   ? 5.424  12.471  2.177   1.00 31.78 ? 2032 HOH F O   1 
HETATM 2701 O  O   . HOH L 6 .   ? 7.084  9.781   8.343   1.00 30.76 ? 2033 HOH F O   1 
HETATM 2702 O  O   . HOH L 6 .   ? 1.451  11.532  9.703   1.00 45.17 ? 2034 HOH F O   1 
HETATM 2703 O  O   . HOH L 6 .   ? -0.992 8.039   9.588   1.00 28.96 ? 2035 HOH F O   1 
HETATM 2704 O  O   . HOH L 6 .   ? 29.738 2.469   -8.856  1.00 41.38 ? 2036 HOH F O   1 
HETATM 2705 O  O   . HOH L 6 .   ? 33.408 5.325   -10.515 1.00 58.77 ? 2037 HOH F O   1 
HETATM 2706 O  O   . HOH L 6 .   ? 36.067 -2.298  -5.709  1.00 44.22 ? 2038 HOH F O   1 
HETATM 2707 O  O   . HOH L 6 .   ? 1.852  7.151   -2.350  1.00 36.12 ? 2039 HOH F O   1 
HETATM 2708 O  O   . HOH L 6 .   ? 3.805  4.927   -6.582  1.00 52.05 ? 2040 HOH F O   1 
HETATM 2709 O  O   . HOH L 6 .   ? 6.310  5.147   -2.725  1.00 31.67 ? 2041 HOH F O   1 
HETATM 2710 O  O   . HOH L 6 .   ? 4.309  13.371  -1.542  1.00 29.66 ? 2042 HOH F O   1 
HETATM 2711 O  O   . HOH L 6 .   ? 4.318  13.523  -4.526  1.00 33.57 ? 2043 HOH F O   1 
HETATM 2712 O  O   . HOH L 6 .   ? 4.578  9.346   -4.978  1.00 46.14 ? 2044 HOH F O   1 
HETATM 2713 O  O   . HOH L 6 .   ? 12.830 2.337   -3.126  1.00 34.29 ? 2045 HOH F O   1 
HETATM 2714 O  O   . HOH L 6 .   ? 8.068  20.220  -2.846  1.00 41.56 ? 2046 HOH F O   1 
HETATM 2715 O  O   . HOH L 6 .   ? 4.492  16.097  -5.619  1.00 36.38 ? 2047 HOH F O   1 
HETATM 2716 O  O   . HOH L 6 .   ? 12.184 0.559   -0.426  1.00 35.88 ? 2048 HOH F O   1 
HETATM 2717 O  O   . HOH L 6 .   ? 12.701 -0.396  1.556   1.00 38.78 ? 2049 HOH F O   1 
HETATM 2718 O  O   . HOH L 6 .   ? 4.495  18.288  -0.769  1.00 48.85 ? 2050 HOH F O   1 
HETATM 2719 O  O   . HOH L 6 .   ? 31.415 31.372  5.918   1.00 46.36 ? 2051 HOH F O   1 
HETATM 2720 O  O   . HOH L 6 .   ? 24.175 -3.429  1.541   1.00 30.80 ? 2052 HOH F O   1 
HETATM 2721 O  O   . HOH L 6 .   ? 26.662 -2.853  0.959   1.00 25.45 ? 2053 HOH F O   1 
HETATM 2722 O  O   . HOH L 6 .   ? 14.215 1.024   13.864  1.00 19.88 ? 2054 HOH F O   1 
HETATM 2723 O  O   . HOH L 6 .   ? 7.157  5.484   15.029  1.00 37.60 ? 2055 HOH F O   1 
HETATM 2724 O  O   . HOH L 6 .   ? 6.997  9.458   13.044  1.00 49.02 ? 2056 HOH F O   1 
HETATM 2725 O  O   . HOH L 6 .   ? 10.345 17.716  16.139  1.00 38.08 ? 2057 HOH F O   1 
HETATM 2726 O  O   . HOH L 6 .   ? 36.938 -1.485  5.373   1.00 29.15 ? 2058 HOH F O   1 
HETATM 2727 O  O   . HOH L 6 .   ? 35.750 0.038   7.732   1.00 27.70 ? 2059 HOH F O   1 
HETATM 2728 O  O   . HOH L 6 .   ? 38.998 2.177   -1.381  1.00 35.77 ? 2060 HOH F O   1 
HETATM 2729 O  O   . HOH L 6 .   ? 31.053 19.533  23.315  1.00 21.01 ? 2061 HOH F O   1 
HETATM 2730 O  O   . HOH L 6 .   ? 37.125 14.264  9.145   1.00 27.86 ? 2062 HOH F O   1 
HETATM 2731 O  O   . HOH L 6 .   ? 37.684 17.021  4.670   1.00 45.35 ? 2063 HOH F O   1 
HETATM 2732 O  O   . HOH L 6 .   ? 41.046 15.276  7.317   1.00 50.05 ? 2064 HOH F O   1 
HETATM 2733 O  O   . HOH L 6 .   ? 40.777 -2.453  -1.751  1.00 37.31 ? 2065 HOH F O   1 
HETATM 2734 O  O   . HOH L 6 .   ? 31.205 27.187  6.784   1.00 36.48 ? 2066 HOH F O   1 
HETATM 2735 O  O   . HOH L 6 .   ? 38.810 8.419   3.812   1.00 23.80 ? 2067 HOH F O   1 
HETATM 2736 O  O   . HOH L 6 .   ? 44.923 1.171   8.129   1.00 49.72 ? 2068 HOH F O   1 
HETATM 2737 O  O   . HOH L 6 .   ? 29.055 15.913  -3.807  1.00 27.23 ? 2069 HOH F O   1 
HETATM 2738 O  O   . HOH L 6 .   ? 31.051 15.422  -5.083  1.00 36.50 ? 2070 HOH F O   1 
HETATM 2739 O  O   . HOH L 6 .   ? 27.567 18.707  -3.236  1.00 21.03 ? 2071 HOH F O   1 
HETATM 2740 O  O   . HOH L 6 .   ? 32.364 23.074  -3.251  1.00 40.75 ? 2072 HOH F O   1 
HETATM 2741 O  O   . HOH L 6 .   ? 37.921 18.835  2.799   1.00 42.94 ? 2073 HOH F O   1 
HETATM 2742 O  O   . HOH L 6 .   ? 31.548 27.842  9.171   1.00 50.24 ? 2074 HOH F O   1 
HETATM 2743 O  O   . HOH L 6 .   ? 34.644 1.505   -1.103  1.00 30.37 ? 2075 HOH F O   1 
HETATM 2744 O  O   . HOH L 6 .   ? 37.334 2.176   0.722   1.00 22.35 ? 2076 HOH F O   1 
HETATM 2745 O  O   . HOH L 6 .   ? 36.179 2.787   -7.104  1.00 33.93 ? 2077 HOH F O   1 
HETATM 2746 O  O   . HOH L 6 .   ? 36.734 1.217   -5.323  1.00 43.41 ? 2078 HOH F O   1 
HETATM 2747 O  O   . HOH L 6 .   ? 32.828 3.803   -7.908  1.00 43.83 ? 2079 HOH F O   1 
HETATM 2748 O  O   . HOH L 6 .   ? 28.338 13.621  -2.451  1.00 18.23 ? 2080 HOH F O   1 
HETATM 2749 O  O   . HOH L 6 .   ? 24.641 13.517  -6.370  1.00 41.20 ? 2081 HOH F O   1 
HETATM 2750 O  O   . HOH L 6 .   ? 21.841 -1.445  -4.790  1.00 35.83 ? 2082 HOH F O   1 
HETATM 2751 O  O   . HOH L 6 .   ? 22.221 13.736  -7.656  1.00 47.86 ? 2083 HOH F O   1 
HETATM 2752 O  O   . HOH L 6 .   ? 27.868 -2.381  -5.669  1.00 39.24 ? 2084 HOH F O   1 
HETATM 2753 O  O   . HOH L 6 .   ? 5.188  7.668   -12.771 1.00 50.86 ? 2085 HOH F O   1 
HETATM 2754 O  O   . HOH L 6 .   ? 3.787  14.614  -10.269 1.00 39.63 ? 2086 HOH F O   1 
HETATM 2755 O  O   . HOH L 6 .   ? 7.794  4.451   -7.025  1.00 44.02 ? 2087 HOH F O   1 
HETATM 2756 O  O   . HOH L 6 .   ? 12.549 2.711   -5.731  1.00 46.13 ? 2088 HOH F O   1 
HETATM 2757 O  O   . HOH L 6 .   ? 15.462 1.276   -2.838  1.00 33.39 ? 2089 HOH F O   1 
HETATM 2758 O  O   . HOH L 6 .   ? 24.358 2.913   -8.173  1.00 46.94 ? 2090 HOH F O   1 
HETATM 2759 O  O   . HOH L 6 .   ? 36.296 14.019  -3.269  1.00 50.82 ? 2091 HOH F O   1 
HETATM 2760 O  O   . HOH L 6 .   ? 35.150 10.303  -5.547  1.00 36.18 ? 2092 HOH F O   1 
HETATM 2761 O  O   . HOH L 6 .   ? 38.742 8.516   -3.730  1.00 33.76 ? 2093 HOH F O   1 
HETATM 2762 O  O   . HOH L 6 .   ? 27.036 3.960   -11.379 1.00 58.28 ? 2094 HOH F O   1 
HETATM 2763 O  O   . HOH L 6 .   ? 5.058  9.208   -1.335  1.00 30.67 ? 2095 HOH F O   1 
HETATM 2764 O  O   . HOH L 6 .   ? 6.510  12.600  -0.181  1.00 20.96 ? 2096 HOH F O   1 
HETATM 2765 O  O   . HOH L 6 .   ? 38.525 15.461  -3.520  1.00 50.90 ? 2097 HOH F O   1 
HETATM 2766 O  O   . HOH L 6 .   ? 37.798 12.595  7.554   1.00 35.16 ? 2098 HOH F O   1 
HETATM 2767 O  O   . HOH L 6 .   ? 5.993  11.960  -5.800  1.00 30.73 ? 2099 HOH F O   1 
HETATM 2768 O  O   . HOH L 6 .   ? 8.722  14.153  -0.434  1.00 16.71 ? 2100 HOH F O   1 
HETATM 2769 O  O   . HOH L 6 .   ? 10.173 18.705  -3.397  1.00 25.69 ? 2101 HOH F O   1 
HETATM 2770 O  O   . HOH L 6 .   ? 34.648 -1.430  14.283  1.00 35.56 ? 2102 HOH F O   1 
HETATM 2771 O  O   . HOH L 6 .   ? 6.511  16.384  -6.896  1.00 24.90 ? 2103 HOH F O   1 
HETATM 2772 O  O   . HOH L 6 .   ? 12.658 16.462  -13.096 1.00 19.54 ? 2104 HOH F O   1 
HETATM 2773 O  O   . HOH L 6 .   ? 6.586  18.236  -9.018  1.00 34.38 ? 2105 HOH F O   1 
HETATM 2774 O  O   . HOH L 6 .   ? 10.530 19.886  -13.584 1.00 15.18 ? 2106 HOH F O   1 
HETATM 2775 O  O   . HOH L 6 .   ? 7.912  18.610  -6.535  0.50 22.23 ? 2107 HOH F O   1 
HETATM 2776 O  O   . HOH L 6 .   ? 10.308 20.592  -6.321  1.00 33.44 ? 2108 HOH F O   1 
HETATM 2777 O  O   . HOH L 6 .   ? 38.277 7.883   20.633  1.00 30.90 ? 2109 HOH F O   1 
HETATM 2778 O  O   . HOH L 6 .   ? 40.002 4.308   14.438  1.00 49.55 ? 2110 HOH F O   1 
HETATM 2779 O  O   . HOH L 6 .   ? 29.279 1.900   18.461  1.00 39.47 ? 2111 HOH F O   1 
HETATM 2780 O  O   . HOH L 6 .   ? 29.911 7.024   21.669  1.00 36.89 ? 2112 HOH F O   1 
HETATM 2781 O  O   . HOH L 6 .   ? 15.103 20.125  -6.663  1.00 35.68 ? 2113 HOH F O   1 
HETATM 2782 O  O   . HOH L 6 .   ? 7.040  18.956  -0.335  1.00 39.05 ? 2114 HOH F O   1 
HETATM 2783 O  O   . HOH L 6 .   ? 6.390  16.749  2.156   1.00 34.64 ? 2115 HOH F O   1 
HETATM 2784 O  O   . HOH L 6 .   ? 9.756  22.228  -0.156  1.00 32.76 ? 2116 HOH F O   1 
HETATM 2785 O  O   . HOH L 6 .   ? 17.913 25.163  -0.174  1.00 28.66 ? 2117 HOH F O   1 
HETATM 2786 O  O   . HOH L 6 .   ? 15.314 28.114  3.791   1.00 34.74 ? 2118 HOH F O   1 
HETATM 2787 O  O   . HOH L 6 .   ? 28.863 30.634  7.102   1.00 39.66 ? 2119 HOH F O   1 
HETATM 2788 O  O   . HOH L 6 .   ? 27.311 31.523  3.268   1.00 49.85 ? 2120 HOH F O   1 
HETATM 2789 O  O   . HOH L 6 .   ? 16.048 33.848  8.352   1.00 45.08 ? 2121 HOH F O   1 
HETATM 2790 O  O   . HOH L 6 .   ? 18.205 31.951  15.584  1.00 39.03 ? 2122 HOH F O   1 
HETATM 2791 O  O   . HOH L 6 .   ? 26.888 9.631   19.939  1.00 25.30 ? 2123 HOH F O   1 
HETATM 2792 O  O   . HOH L 6 .   ? 27.661 11.714  18.434  1.00 31.80 ? 2124 HOH F O   1 
HETATM 2793 O  O   . HOH L 6 .   ? 15.875 19.912  14.389  1.00 37.03 ? 2125 HOH F O   1 
HETATM 2794 O  O   . HOH L 6 .   ? 16.094 2.603   17.407  1.00 11.24 ? 2126 HOH F O   1 
HETATM 2795 O  O   . HOH L 6 .   ? 16.676 5.860   24.021  1.00 27.62 ? 2127 HOH F O   1 
HETATM 2796 O  O   . HOH L 6 .   ? 15.321 9.494   22.417  1.00 19.31 ? 2128 HOH F O   1 
HETATM 2797 O  O   . HOH L 6 .   ? 16.105 5.237   12.896  0.50 15.92 ? 2129 HOH F O   1 
HETATM 2798 O  O   . HOH L 6 .   ? 8.969  3.876   16.089  1.00 30.22 ? 2130 HOH F O   1 
HETATM 2799 O  O   . HOH L 6 .   ? 14.081 2.928   12.170  1.00 24.31 ? 2131 HOH F O   1 
HETATM 2800 O  O   . HOH L 6 .   ? 11.576 1.097   13.355  1.00 23.66 ? 2132 HOH F O   1 
HETATM 2801 O  O   . HOH L 6 .   ? 10.046 3.248   10.780  1.00 36.37 ? 2133 HOH F O   1 
HETATM 2802 O  O   . HOH L 6 .   ? 10.453 6.049   11.836  1.00 29.86 ? 2134 HOH F O   1 
HETATM 2803 O  O   . HOH L 6 .   ? 14.938 7.389   14.099  0.50 13.83 ? 2135 HOH F O   1 
HETATM 2804 O  O   . HOH L 6 .   ? 31.495 -7.627  8.409   1.00 53.13 ? 2136 HOH F O   1 
HETATM 2805 O  O   . HOH L 6 .   ? 32.596 -10.308 6.154   1.00 39.26 ? 2137 HOH F O   1 
HETATM 2806 O  O   . HOH L 6 .   ? 7.783  3.435   19.071  1.00 40.63 ? 2138 HOH F O   1 
HETATM 2807 O  O   . HOH L 6 .   ? 7.125  5.383   17.749  1.00 35.84 ? 2139 HOH F O   1 
HETATM 2808 O  O   . HOH L 6 .   ? 6.012  9.836   17.974  1.00 21.02 ? 2140 HOH F O   1 
HETATM 2809 O  O   . HOH L 6 .   ? 6.148  7.416   16.670  1.00 39.26 ? 2141 HOH F O   1 
HETATM 2810 O  O   . HOH L 6 .   ? 9.026  10.096  12.221  0.60 21.57 ? 2142 HOH F O   1 
HETATM 2811 O  O   . HOH L 6 .   ? 9.048  8.697   11.939  0.40 15.24 ? 2143 HOH F O   1 
HETATM 2812 O  O   . HOH L 6 .   ? 11.690 12.485  19.286  0.50 14.28 ? 2144 HOH F O   1 
HETATM 2813 O  O   . HOH L 6 .   ? 12.567 16.840  17.941  1.00 28.64 ? 2145 HOH F O   1 
HETATM 2814 O  O   . HOH L 6 .   ? 14.480 15.551  16.276  0.50 13.93 ? 2146 HOH F O   1 
HETATM 2815 O  O   . HOH L 6 .   ? 13.560 16.745  15.520  0.50 30.93 ? 2147 HOH F O   1 
HETATM 2816 O  O   . HOH L 6 .   ? 7.967  12.178  16.483  1.00 28.69 ? 2148 HOH F O   1 
HETATM 2817 O  O   . HOH L 6 .   ? 9.576  11.728  14.067  0.40 19.90 ? 2149 HOH F O   1 
HETATM 2818 O  O   . HOH L 6 .   ? 11.008 15.207  19.457  1.00 24.50 ? 2150 HOH F O   1 
HETATM 2819 O  O   . HOH L 6 .   ? 18.536 10.981  20.607  0.40 17.17 ? 2151 HOH F O   1 
HETATM 2820 O  O   . HOH L 6 .   ? 17.527 10.751  21.448  0.60 10.69 ? 2152 HOH F O   1 
HETATM 2821 O  O   . HOH L 6 .   ? 12.804 10.524  21.605  1.00 18.50 ? 2153 HOH F O   1 
HETATM 2822 O  O   . HOH L 6 .   ? 18.277 17.993  10.876  0.50 16.22 ? 2154 HOH F O   1 
HETATM 2823 O  O   . HOH L 6 .   ? 19.489 18.286  12.939  1.00 18.25 ? 2155 HOH F O   1 
HETATM 2824 O  O   . HOH L 6 .   ? 24.899 18.488  14.347  0.50 14.24 ? 2156 HOH F O   1 
HETATM 2825 O  O   . HOH L 6 .   ? 31.705 16.321  12.658  1.00 11.44 ? 2157 HOH F O   1 
HETATM 2826 O  O   . HOH L 6 .   ? 27.081 13.539  16.860  0.40 15.83 ? 2158 HOH F O   1 
HETATM 2827 O  O   . HOH L 6 .   ? 26.057 19.920  16.036  0.50 14.55 ? 2159 HOH F O   1 
HETATM 2828 O  O   . HOH L 6 .   ? 34.136 17.270  19.164  1.00 13.78 ? 2160 HOH F O   1 
HETATM 2829 O  O   . HOH L 6 .   ? 37.170 18.777  16.591  1.00 19.72 ? 2161 HOH F O   1 
HETATM 2830 O  O   . HOH L 6 .   ? 32.206 24.963  15.223  1.00 33.50 ? 2162 HOH F O   1 
HETATM 2831 O  O   . HOH L 6 .   ? 30.228 23.247  17.339  1.00 27.98 ? 2163 HOH F O   1 
HETATM 2832 O  O   . HOH L 6 .   ? 31.817 20.747  21.251  1.00 18.29 ? 2164 HOH F O   1 
HETATM 2833 O  O   . HOH L 6 .   ? 39.120 18.070  7.759   1.00 50.38 ? 2165 HOH F O   1 
HETATM 2834 O  O   . HOH L 6 .   ? 39.076 18.417  14.561  1.00 33.71 ? 2166 HOH F O   1 
HETATM 2835 O  O   . HOH L 6 .   ? 40.028 16.632  12.486  1.00 29.82 ? 2167 HOH F O   1 
HETATM 2836 O  O   . HOH L 6 .   ? 37.991 20.110  13.784  0.50 41.19 ? 2168 HOH F O   1 
HETATM 2837 O  O   . HOH L 6 .   ? 36.932 21.736  14.163  0.50 25.37 ? 2169 HOH F O   1 
HETATM 2838 O  O   . HOH L 6 .   ? 35.278 16.297  8.980   1.00 27.00 ? 2170 HOH F O   1 
HETATM 2839 O  O   . HOH L 6 .   ? 29.011 30.286  15.335  1.00 40.75 ? 2171 HOH F O   1 
HETATM 2840 O  O   . HOH L 6 .   ? 29.908 24.982  6.233   1.00 25.53 ? 2172 HOH F O   1 
HETATM 2841 O  O   . HOH L 6 .   ? 27.414 26.485  7.745   1.00 33.60 ? 2173 HOH F O   1 
HETATM 2842 O  O   . HOH L 6 .   ? 34.862 15.657  1.393   1.00 28.28 ? 2174 HOH F O   1 
HETATM 2843 O  O   . HOH L 6 .   ? 37.058 20.973  0.490   1.00 43.08 ? 2175 HOH F O   1 
HETATM 2844 O  O   . HOH L 6 .   ? 34.700 21.951  -2.927  1.00 49.56 ? 2176 HOH F O   1 
HETATM 2845 O  O   . HOH L 6 .   ? 29.094 19.879  -1.078  1.00 16.95 ? 2177 HOH F O   1 
HETATM 2846 O  O   . HOH L 6 .   ? 32.004 15.416  -1.725  1.00 33.92 ? 2178 HOH F O   1 
HETATM 2847 O  O   . HOH L 6 .   ? 35.950 18.477  -1.814  1.00 34.74 ? 2179 HOH F O   1 
HETATM 2848 O  O   . HOH L 6 .   ? 30.467 22.263  -1.779  1.00 23.14 ? 2180 HOH F O   1 
HETATM 2849 O  O   . HOH L 6 .   ? 35.073 17.451  3.397   1.00 28.73 ? 2181 HOH F O   1 
HETATM 2850 O  O   . HOH L 6 .   ? 28.387 24.439  0.755   1.00 23.03 ? 2182 HOH F O   1 
HETATM 2851 O  O   . HOH L 6 .   ? 35.519 17.670  6.492   1.00 24.15 ? 2183 HOH F O   1 
HETATM 2852 O  O   . HOH L 6 .   ? 37.263 24.999  6.333   1.00 40.50 ? 2184 HOH F O   1 
HETATM 2853 O  O   . HOH L 6 .   ? 35.919 23.638  1.938   1.00 28.33 ? 2185 HOH F O   1 
HETATM 2854 O  O   . HOH L 6 .   ? 36.375 25.708  11.485  1.00 39.47 ? 2186 HOH F O   1 
HETATM 2855 O  O   . HOH L 6 .   ? 33.199 27.622  11.339  1.00 39.47 ? 2187 HOH F O   1 
HETATM 2856 O  O   . HOH L 6 .   ? 36.719 23.145  8.733   1.00 41.87 ? 2188 HOH F O   1 
HETATM 2857 O  O   . HOH L 6 .   ? 34.599 24.636  4.394   1.00 25.07 ? 2189 HOH F O   1 
HETATM 2858 O  O   . HOH L 6 .   ? 33.322 16.997  10.589  1.00 16.05 ? 2190 HOH F O   1 
HETATM 2859 O  O   . HOH L 6 .   ? 26.240 22.774  13.723  1.00 26.18 ? 2191 HOH F O   1 
HETATM 2860 O  O   . HOH L 6 .   ? 25.629 13.891  -2.005  1.00 20.35 ? 2192 HOH F O   1 
HETATM 2861 O  O   . HOH L 6 .   ? 23.844 13.181  -3.876  1.00 27.13 ? 2193 HOH F O   1 
HETATM 2862 O  O   . HOH L 6 .   ? 25.168 17.110  -2.486  1.00 16.13 ? 2194 HOH F O   1 
HETATM 2863 O  O   . HOH L 6 .   ? 16.964 13.311  -10.477 1.00 32.49 ? 2195 HOH F O   1 
HETATM 2864 O  O   . HOH L 6 .   ? 21.264 15.051  -5.701  1.00 25.12 ? 2196 HOH F O   1 
HETATM 2865 O  O   . HOH L 6 .   ? 19.529 17.130  -8.875  1.00 23.49 ? 2197 HOH F O   1 
HETATM 2866 O  O   . HOH L 6 .   ? 18.155 10.773  -8.587  1.00 29.01 ? 2198 HOH F O   1 
HETATM 2867 O  O   . HOH L 6 .   ? 11.856 14.118  -13.861 1.00 18.78 ? 2199 HOH F O   1 
HETATM 2868 O  O   . HOH L 6 .   ? 10.630 10.447  -13.944 0.50 20.62 ? 2200 HOH F O   1 
HETATM 2869 O  O   . HOH L 6 .   ? 14.935 13.405  -12.077 0.30 23.73 ? 2201 HOH F O   1 
HETATM 2870 O  O   . HOH L 6 .   ? 16.007 12.858  -12.727 0.70 26.90 ? 2202 HOH F O   1 
HETATM 2871 O  O   . HOH L 6 .   ? 12.878 11.171  -16.137 1.00 21.47 ? 2203 HOH F O   1 
HETATM 2872 O  O   . HOH L 6 .   ? 5.907  14.342  -8.790  1.00 37.44 ? 2204 HOH F O   1 
HETATM 2873 O  O   . HOH L 6 .   ? 5.597  10.725  -13.008 1.00 55.01 ? 2205 HOH F O   1 
HETATM 2874 O  O   . HOH L 6 .   ? 6.282  7.090   -10.129 1.00 42.10 ? 2206 HOH F O   1 
HETATM 2875 O  O   . HOH L 6 .   ? 7.810  7.079   -6.359  1.00 24.92 ? 2207 HOH F O   1 
HETATM 2876 O  O   . HOH L 6 .   ? 19.984 11.473  -5.886  1.00 21.32 ? 2208 HOH F O   1 
HETATM 2877 O  O   . HOH L 6 .   ? 15.669 3.634   -10.195 1.00 46.06 ? 2209 HOH F O   1 
HETATM 2878 O  O   . HOH L 6 .   ? 18.396 5.175   -12.356 1.00 36.64 ? 2210 HOH F O   1 
HETATM 2879 O  O   . HOH L 6 .   ? 16.720 4.734   -8.406  0.50 25.66 ? 2211 HOH F O   1 
HETATM 2880 O  O   . HOH L 6 .   ? 22.523 10.023  -8.589  1.00 33.04 ? 2212 HOH F O   1 
HETATM 2881 O  O   . HOH L 6 .   ? 21.944 3.890   -7.542  1.00 26.48 ? 2213 HOH F O   1 
HETATM 2882 O  O   . HOH L 6 .   ? 27.404 11.531  -6.425  1.00 38.70 ? 2214 HOH F O   1 
HETATM 2883 O  O   . HOH L 6 .   ? 22.758 10.824  -5.135  1.00 23.17 ? 2215 HOH F O   1 
HETATM 2884 O  O   . HOH L 6 .   ? 29.351 6.600   -6.418  1.00 42.44 ? 2216 HOH F O   1 
HETATM 2885 O  O   . HOH L 6 .   ? 26.830 4.430   -7.500  1.00 35.82 ? 2217 HOH F O   1 
HETATM 2886 O  O   . HOH L 6 .   ? 28.126 4.786   -5.298  1.00 36.37 ? 2218 HOH F O   1 
HETATM 2887 O  O   . HOH L 6 .   ? 32.408 12.306  -4.335  1.00 33.23 ? 2219 HOH F O   1 
HETATM 2888 O  O   . HOH L 6 .   ? 29.345 11.695  -4.321  1.00 27.63 ? 2220 HOH F O   1 
HETATM 2889 O  O   . HOH L 6 .   ? 36.028 8.625   -3.657  1.00 27.74 ? 2221 HOH F O   1 
HETATM 2890 O  O   . HOH L 6 .   ? 34.101 12.630  -2.220  1.00 29.93 ? 2222 HOH F O   1 
HETATM 2891 O  O   . HOH L 6 .   ? 36.747 4.403   -4.307  1.00 38.03 ? 2223 HOH F O   1 
HETATM 2892 O  O   . HOH L 6 .   ? 30.473 12.881  -0.790  1.00 18.31 ? 2224 HOH F O   1 
HETATM 2893 O  O   . HOH L 6 .   ? 33.850 13.273  0.753   1.00 20.72 ? 2225 HOH F O   1 
HETATM 2894 O  O   . HOH L 6 .   ? 38.261 13.778  4.241   1.00 37.50 ? 2226 HOH F O   1 
HETATM 2895 O  O   . HOH L 6 .   ? 35.105 9.997   -1.642  1.00 23.02 ? 2227 HOH F O   1 
HETATM 2896 O  O   . HOH L 6 .   ? 37.873 12.926  -1.316  1.00 47.94 ? 2228 HOH F O   1 
HETATM 2897 O  O   . HOH L 6 .   ? 38.909 8.817   1.138   1.00 34.01 ? 2229 HOH F O   1 
HETATM 2898 O  O   . HOH L 6 .   ? 36.495 10.535  8.614   1.00 25.58 ? 2230 HOH F O   1 
HETATM 2899 O  O   . HOH L 6 .   ? 36.341 7.080   5.284   1.00 23.18 ? 2231 HOH F O   1 
HETATM 2900 O  O   . HOH L 6 .   ? 37.920 4.904   9.655   1.00 26.94 ? 2232 HOH F O   1 
HETATM 2901 O  O   . HOH L 6 .   ? 32.953 -1.609  12.111  1.00 27.17 ? 2233 HOH F O   1 
HETATM 2902 O  O   . HOH L 6 .   ? 36.450 6.764   11.601  1.00 19.75 ? 2234 HOH F O   1 
HETATM 2903 O  O   . HOH L 6 .   ? 37.115 2.099   8.112   1.00 33.24 ? 2235 HOH F O   1 
HETATM 2904 O  O   . HOH L 6 .   ? 35.175 0.853   15.154  1.00 31.65 ? 2236 HOH F O   1 
HETATM 2905 O  O   . HOH L 6 .   ? 33.082 9.806   17.269  0.20 22.13 ? 2237 HOH F O   1 
HETATM 2906 O  O   . HOH L 6 .   ? 38.449 6.017   17.345  1.00 46.29 ? 2238 HOH F O   1 
HETATM 2907 O  O   . HOH L 6 .   ? 34.037 8.099   20.925  1.00 43.44 ? 2239 HOH F O   1 
HETATM 2908 O  O   . HOH L 6 .   ? 39.053 6.755   13.787  1.00 37.42 ? 2240 HOH F O   1 
HETATM 2909 O  O   . HOH L 6 .   ? 36.166 12.777  15.610  1.00 20.83 ? 2241 HOH F O   1 
HETATM 2910 O  O   . HOH L 6 .   ? 36.185 9.439   20.206  1.00 19.81 ? 2242 HOH F O   1 
HETATM 2911 O  O   . HOH L 6 .   ? 31.205 6.705   15.637  1.00 17.30 ? 2243 HOH F O   1 
HETATM 2912 O  O   . HOH L 6 .   ? 28.989 4.473   15.174  1.00 28.18 ? 2244 HOH F O   1 
HETATM 2913 O  O   . HOH L 6 .   ? 30.304 5.478   19.680  1.00 43.35 ? 2245 HOH F O   1 
HETATM 2914 O  O   . HOH L 6 .   ? 30.689 4.388   17.140  1.00 31.73 ? 2246 HOH F O   1 
HETATM 2915 O  O   . HOH L 6 .   ? 8.577  16.790  0.669   1.00 19.13 ? 2247 HOH F O   1 
HETATM 2916 O  O   . HOH L 6 .   ? 7.851  21.701  2.064   1.00 27.02 ? 2248 HOH F O   1 
HETATM 2917 O  O   . HOH L 6 .   ? 9.461  22.167  8.108   1.00 38.65 ? 2249 HOH F O   1 
HETATM 2918 O  O   . HOH L 6 .   ? 5.659  19.370  2.866   1.00 34.04 ? 2250 HOH F O   1 
HETATM 2919 O  O   . HOH L 6 .   ? 7.948  24.679  7.338   1.00 40.86 ? 2251 HOH F O   1 
HETATM 2920 O  O   . HOH L 6 .   ? 15.760 24.507  1.881   1.00 25.04 ? 2252 HOH F O   1 
HETATM 2921 O  O   . HOH L 6 .   ? 12.858 22.196  -0.554  0.50 15.57 ? 2253 HOH F O   1 
HETATM 2922 O  O   . HOH L 6 .   ? 13.769 23.776  -0.187  0.50 15.14 ? 2254 HOH F O   1 
HETATM 2923 O  O   . HOH L 6 .   ? 24.822 18.189  3.780   1.00 12.35 ? 2255 HOH F O   1 
HETATM 2924 O  O   . HOH L 6 .   ? 17.838 28.026  2.924   1.00 30.10 ? 2256 HOH F O   1 
HETATM 2925 O  O   . HOH L 6 .   ? 28.669 28.266  5.529   1.00 37.32 ? 2257 HOH F O   1 
HETATM 2926 O  O   . HOH L 6 .   ? 28.831 25.704  3.728   1.00 29.03 ? 2258 HOH F O   1 
HETATM 2927 O  O   . HOH L 6 .   ? 32.051 25.921  0.422   1.00 41.81 ? 2259 HOH F O   1 
HETATM 2928 O  O   . HOH L 6 .   ? 32.725 26.244  3.968   1.00 41.83 ? 2260 HOH F O   1 
HETATM 2929 O  O   . HOH L 6 .   ? 24.241 31.212  -1.260  1.00 24.12 ? 2261 HOH F O   1 
HETATM 2930 O  O   . HOH L 6 .   ? 26.058 31.778  0.740   1.00 31.18 ? 2262 HOH F O   1 
HETATM 2931 O  O   . HOH L 6 .   ? 25.007 30.431  5.360   1.00 30.50 ? 2263 HOH F O   1 
HETATM 2932 O  O   . HOH L 6 .   ? 17.501 35.530  7.130   1.00 36.83 ? 2264 HOH F O   1 
HETATM 2933 O  O   . HOH L 6 .   ? 18.595 30.778  2.020   1.00 25.05 ? 2265 HOH F O   1 
HETATM 2934 O  O   . HOH L 6 .   ? 19.398 36.543  7.872   1.00 33.60 ? 2266 HOH F O   1 
HETATM 2935 O  O   . HOH L 6 .   ? 14.596 31.965  8.099   1.00 47.56 ? 2267 HOH F O   1 
HETATM 2936 O  O   . HOH L 6 .   ? 24.710 31.122  8.193   1.00 45.17 ? 2268 HOH F O   1 
HETATM 2937 O  O   . HOH L 6 .   ? 15.216 31.057  5.786   1.00 49.70 ? 2269 HOH F O   1 
HETATM 2938 O  O   . HOH L 6 .   ? 17.468 30.017  13.514  1.00 26.11 ? 2270 HOH F O   1 
HETATM 2939 O  O   . HOH L 6 .   ? 18.856 33.929  11.349  1.00 33.48 ? 2271 HOH F O   1 
HETATM 2940 O  O   . HOH L 6 .   ? 17.682 30.521  10.991  1.00 23.61 ? 2272 HOH F O   1 
HETATM 2941 O  O   . HOH L 6 .   ? 14.800 26.664  13.752  1.00 41.62 ? 2273 HOH F O   1 
HETATM 2942 O  O   . HOH L 6 .   ? 26.111 27.730  13.758  1.00 37.34 ? 2274 HOH F O   1 
HETATM 2943 O  O   . HOH L 6 .   ? 22.276 19.292  13.200  1.00 16.36 ? 2275 HOH F O   1 
HETATM 2944 O  O   . HOH L 6 .   ? 18.682 18.789  8.300   1.00 14.94 ? 2276 HOH F O   1 
HETATM 2945 O  O   . HOH L 6 .   ? 13.823 25.847  3.731   1.00 37.22 ? 2277 HOH F O   1 
HETATM 2946 O  O   . HOH L 6 .   ? 8.546  15.212  9.782   0.50 13.47 ? 2278 HOH F O   1 
HETATM 2947 O  O   . HOH L 6 .   ? 7.882  14.651  8.156   0.50 21.29 ? 2279 HOH F O   1 
HETATM 2948 O  O   . HOH L 6 .   ? 6.927  17.513  6.207   1.00 40.32 ? 2280 HOH F O   1 
HETATM 2949 O  O   . HOH L 6 .   ? 17.402 17.828  11.410  0.50 14.74 ? 2281 HOH F O   1 
HETATM 2950 O  O   . HOH L 6 .   ? 9.016  10.248  9.542   1.00 24.26 ? 2282 HOH F O   1 
HETATM 2951 O  O   . HOH L 6 .   ? 18.162 18.912  15.132  1.00 24.90 ? 2283 HOH F O   1 
HETATM 2952 O  O   . HOH L 6 .   ? 14.347 17.703  11.244  0.70 18.70 ? 2284 HOH F O   1 
HETATM 2953 O  O   . HOH L 6 .   ? 12.443 3.613   10.207  1.00 28.57 ? 2285 HOH F O   1 
HETATM 2954 O  O   . HOH L 6 .   ? 15.998 0.708   10.827  0.50 16.34 ? 2286 HOH F O   1 
HETATM 2955 O  O   . HOH L 6 .   ? 15.659 1.167   11.466  0.50 14.93 ? 2287 HOH F O   1 
HETATM 2956 O  O   . HOH L 6 .   ? 17.822 -0.231  8.554   1.00 10.56 ? 2288 HOH F O   1 
HETATM 2957 O  O   . HOH L 6 .   ? 30.420 -6.008  6.591   1.00 18.30 ? 2289 HOH F O   1 
HETATM 2958 O  O   . HOH L 6 .   ? 29.317 -8.737  7.989   1.00 24.44 ? 2290 HOH F O   1 
HETATM 2959 O  O   . HOH L 6 .   ? 29.819 -11.241 6.150   1.00 28.21 ? 2291 HOH F O   1 
HETATM 2960 O  O   . HOH L 6 .   ? 23.067 -10.900 3.535   0.60 18.90 ? 2292 HOH F O   1 
HETATM 2961 O  O   . HOH L 6 .   ? 30.930 -8.151  4.768   1.00 27.25 ? 2293 HOH F O   1 
HETATM 2962 O  O   . HOH L 6 .   ? 24.262 -8.424  2.210   1.00 29.84 ? 2294 HOH F O   1 
HETATM 2963 O  O   . HOH L 6 .   ? 29.618 -9.536  1.098   1.00 41.76 ? 2295 HOH F O   1 
HETATM 2964 O  O   . HOH L 6 .   ? 26.497 -15.498 1.248   1.00 25.86 ? 2296 HOH F O   1 
HETATM 2965 O  O   . HOH L 6 .   ? 27.374 -9.791  0.335   1.00 29.43 ? 2297 HOH F O   1 
HETATM 2966 O  O   . HOH L 6 .   ? 22.082 -10.828 4.874   1.00 17.79 ? 2298 HOH F O   1 
HETATM 2967 O  O   . HOH L 6 .   ? 27.863 -14.144 1.135   0.50 16.71 ? 2299 HOH F O   1 
HETATM 2968 O  O   . HOH L 6 .   ? 25.670 -6.802  1.575   1.00 35.62 ? 2300 HOH F O   1 
HETATM 2969 O  O   . HOH L 6 .   ? 13.022 16.561  14.230  0.50 23.19 ? 2301 HOH F O   1 
HETATM 2970 O  O   . HOH L 6 .   ? 13.812 18.943  11.984  0.30 11.21 ? 2302 HOH F O   1 
HETATM 2971 O  O   . HOH L 6 .   ? 10.384 15.482  11.281  0.50 19.88 ? 2303 HOH F O   1 
HETATM 2972 O  O   . HOH L 6 .   ? 9.728  12.151  12.411  0.60 24.58 ? 2304 HOH F O   1 
HETATM 2973 O  O   . HOH L 6 .   ? 12.893 23.716  12.657  1.00 34.66 ? 2305 HOH F O   1 
HETATM 2974 O  O   . HOH L 6 .   ? 14.244 26.123  8.055   1.00 37.77 ? 2306 HOH F O   1 
HETATM 2975 O  O   . HOH L 6 .   ? 11.463 23.864  8.275   1.00 35.04 ? 2307 HOH F O   1 
HETATM 2976 O  O   . HOH L 6 .   ? 16.144 19.634  9.410   1.00 18.72 ? 2308 HOH F O   1 
HETATM 2977 O  O   . HOH L 6 .   ? 12.207 20.245  10.843  1.00 44.00 ? 2309 HOH F 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 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  CYS 57  57  57  CYS CYS F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  GLY 93  93  93  GLY GLY F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CYS 111 111 111 CYS CYS F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 ILE 113 113 113 ILE ILE F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 CYS 146 146 146 CYS CYS F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 GLN 153 153 153 GLN GLN F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU  1   1154 1154 CU  CU  A . 
D 3 ZN  1   1155 1155 ZN  ZN  A . 
E 4 SO4 1   1157 1157 SO4 SO4 A . 
F 4 SO4 1   1158 1158 SO4 SO4 A . 
G 5 ACT 1   1154 1154 ACT ACT F . 
H 2 CU  1   1156 1156 CU  CU  F . 
I 3 ZN  1   1157 1157 ZN  ZN  F . 
J 4 SO4 1   1158 1158 SO4 SO4 F . 
K 6 HOH 1   2001 2001 HOH HOH A . 
K 6 HOH 2   2002 2002 HOH HOH A . 
K 6 HOH 3   2003 2003 HOH HOH A . 
K 6 HOH 4   2004 2004 HOH HOH A . 
K 6 HOH 5   2005 2005 HOH HOH A . 
K 6 HOH 6   2006 2006 HOH HOH A . 
K 6 HOH 7   2007 2007 HOH HOH A . 
K 6 HOH 8   2008 2008 HOH HOH A . 
K 6 HOH 9   2009 2009 HOH HOH A . 
K 6 HOH 10  2010 2010 HOH HOH A . 
K 6 HOH 11  2011 2011 HOH HOH A . 
K 6 HOH 12  2012 2012 HOH HOH A . 
K 6 HOH 13  2013 2013 HOH HOH A . 
K 6 HOH 14  2014 2014 HOH HOH A . 
K 6 HOH 15  2015 2015 HOH HOH A . 
K 6 HOH 16  2016 2016 HOH HOH A . 
K 6 HOH 17  2017 2017 HOH HOH A . 
K 6 HOH 18  2018 2018 HOH HOH A . 
K 6 HOH 19  2019 2019 HOH HOH A . 
K 6 HOH 20  2020 2020 HOH HOH A . 
K 6 HOH 21  2021 2021 HOH HOH A . 
K 6 HOH 22  2022 2022 HOH HOH A . 
K 6 HOH 23  2023 2023 HOH HOH A . 
K 6 HOH 24  2024 2024 HOH HOH A . 
K 6 HOH 25  2025 2025 HOH HOH A . 
K 6 HOH 26  2026 2026 HOH HOH A . 
K 6 HOH 27  2027 2027 HOH HOH A . 
K 6 HOH 28  2028 2028 HOH HOH A . 
K 6 HOH 29  2029 2029 HOH HOH A . 
K 6 HOH 30  2030 2030 HOH HOH A . 
K 6 HOH 31  2031 2031 HOH HOH A . 
K 6 HOH 32  2032 2032 HOH HOH A . 
K 6 HOH 33  2033 2033 HOH HOH A . 
K 6 HOH 34  2034 2034 HOH HOH A . 
K 6 HOH 35  2035 2035 HOH HOH A . 
K 6 HOH 36  2036 2036 HOH HOH A . 
K 6 HOH 37  2037 2037 HOH HOH A . 
K 6 HOH 38  2038 2038 HOH HOH A . 
K 6 HOH 39  2039 2039 HOH HOH A . 
K 6 HOH 40  2040 2040 HOH HOH A . 
K 6 HOH 41  2041 2041 HOH HOH A . 
K 6 HOH 42  2042 2042 HOH HOH A . 
K 6 HOH 43  2043 2043 HOH HOH A . 
K 6 HOH 44  2044 2044 HOH HOH A . 
K 6 HOH 45  2045 2045 HOH HOH A . 
K 6 HOH 46  2046 2046 HOH HOH A . 
K 6 HOH 47  2047 2047 HOH HOH A . 
K 6 HOH 48  2048 2048 HOH HOH A . 
K 6 HOH 49  2049 2049 HOH HOH A . 
K 6 HOH 50  2050 2050 HOH HOH A . 
K 6 HOH 51  2051 2051 HOH HOH A . 
K 6 HOH 52  2052 2052 HOH HOH A . 
K 6 HOH 53  2053 2053 HOH HOH A . 
K 6 HOH 54  2054 2054 HOH HOH A . 
K 6 HOH 55  2055 2055 HOH HOH A . 
K 6 HOH 56  2056 2056 HOH HOH A . 
K 6 HOH 57  2057 2057 HOH HOH A . 
K 6 HOH 58  2058 2058 HOH HOH A . 
K 6 HOH 59  2059 2059 HOH HOH A . 
K 6 HOH 60  2060 2060 HOH HOH A . 
K 6 HOH 61  2061 2061 HOH HOH A . 
K 6 HOH 62  2062 2062 HOH HOH A . 
K 6 HOH 63  2063 2063 HOH HOH A . 
K 6 HOH 64  2064 2064 HOH HOH A . 
K 6 HOH 65  2065 2065 HOH HOH A . 
K 6 HOH 66  2066 2066 HOH HOH A . 
K 6 HOH 67  2067 2067 HOH HOH A . 
K 6 HOH 68  2068 2068 HOH HOH A . 
K 6 HOH 69  2069 2069 HOH HOH A . 
K 6 HOH 70  2070 2070 HOH HOH A . 
K 6 HOH 71  2071 2071 HOH HOH A . 
K 6 HOH 72  2072 2072 HOH HOH A . 
K 6 HOH 73  2073 2073 HOH HOH A . 
K 6 HOH 74  2074 2074 HOH HOH A . 
K 6 HOH 75  2075 2075 HOH HOH A . 
K 6 HOH 76  2076 2076 HOH HOH A . 
K 6 HOH 77  2077 2077 HOH HOH A . 
K 6 HOH 78  2078 2078 HOH HOH A . 
K 6 HOH 79  2079 2079 HOH HOH A . 
K 6 HOH 80  2080 2080 HOH HOH A . 
K 6 HOH 81  2081 2081 HOH HOH A . 
K 6 HOH 82  2082 2082 HOH HOH A . 
K 6 HOH 83  2083 2083 HOH HOH A . 
K 6 HOH 84  2084 2084 HOH HOH A . 
K 6 HOH 85  2085 2085 HOH HOH A . 
K 6 HOH 86  2086 2086 HOH HOH A . 
K 6 HOH 87  2087 2087 HOH HOH A . 
K 6 HOH 88  2088 2088 HOH HOH A . 
K 6 HOH 89  2089 2089 HOH HOH A . 
K 6 HOH 90  2090 2090 HOH HOH A . 
K 6 HOH 91  2091 2091 HOH HOH A . 
K 6 HOH 92  2092 2092 HOH HOH A . 
K 6 HOH 93  2093 2093 HOH HOH A . 
K 6 HOH 94  2094 2094 HOH HOH A . 
K 6 HOH 95  2095 2095 HOH HOH A . 
K 6 HOH 96  2096 2096 HOH HOH A . 
K 6 HOH 97  2097 2097 HOH HOH A . 
K 6 HOH 98  2098 2098 HOH HOH A . 
K 6 HOH 99  2099 2099 HOH HOH A . 
K 6 HOH 100 2100 2100 HOH HOH A . 
K 6 HOH 101 2101 2101 HOH HOH A . 
K 6 HOH 102 2102 2102 HOH HOH A . 
K 6 HOH 103 2103 2103 HOH HOH A . 
K 6 HOH 104 2104 2104 HOH HOH A . 
K 6 HOH 105 2105 2105 HOH HOH A . 
K 6 HOH 106 2106 2106 HOH HOH A . 
K 6 HOH 107 2107 2107 HOH HOH A . 
K 6 HOH 108 2108 2108 HOH HOH A . 
K 6 HOH 109 2109 2109 HOH HOH A . 
K 6 HOH 110 2110 2110 HOH HOH A . 
K 6 HOH 111 2111 2111 HOH HOH A . 
K 6 HOH 112 2112 2112 HOH HOH A . 
K 6 HOH 113 2113 2113 HOH HOH A . 
K 6 HOH 114 2114 2114 HOH HOH A . 
K 6 HOH 115 2115 2115 HOH HOH A . 
K 6 HOH 116 2116 2116 HOH HOH A . 
K 6 HOH 117 2117 2117 HOH HOH A . 
K 6 HOH 118 2118 2118 HOH HOH A . 
K 6 HOH 119 2119 2119 HOH HOH A . 
K 6 HOH 120 2120 2120 HOH HOH A . 
K 6 HOH 121 2121 2121 HOH HOH A . 
K 6 HOH 122 2122 2122 HOH HOH A . 
K 6 HOH 123 2123 2123 HOH HOH A . 
K 6 HOH 124 2124 2124 HOH HOH A . 
K 6 HOH 125 2125 2125 HOH HOH A . 
K 6 HOH 126 2126 2126 HOH HOH A . 
K 6 HOH 127 2127 2127 HOH HOH A . 
K 6 HOH 128 2128 2128 HOH HOH A . 
K 6 HOH 129 2129 2129 HOH HOH A . 
K 6 HOH 130 2130 2130 HOH HOH A . 
K 6 HOH 131 2131 2131 HOH HOH A . 
K 6 HOH 132 2132 2132 HOH HOH A . 
K 6 HOH 133 2133 2133 HOH HOH A . 
K 6 HOH 134 2134 2134 HOH HOH A . 
K 6 HOH 135 2135 2135 HOH HOH A . 
K 6 HOH 136 2136 2136 HOH HOH A . 
K 6 HOH 137 2137 2137 HOH HOH A . 
K 6 HOH 138 2138 2138 HOH HOH A . 
K 6 HOH 139 2139 2139 HOH HOH A . 
K 6 HOH 140 2140 2140 HOH HOH A . 
K 6 HOH 141 2141 2141 HOH HOH A . 
K 6 HOH 142 2142 2142 HOH HOH A . 
K 6 HOH 143 2143 2143 HOH HOH A . 
K 6 HOH 144 2144 2144 HOH HOH A . 
K 6 HOH 145 2145 2145 HOH HOH A . 
K 6 HOH 146 2146 2146 HOH HOH A . 
K 6 HOH 147 2147 2147 HOH HOH A . 
K 6 HOH 148 2148 2148 HOH HOH A . 
K 6 HOH 149 2149 2149 HOH HOH A . 
K 6 HOH 150 2150 2150 HOH HOH A . 
K 6 HOH 151 2151 2151 HOH HOH A . 
K 6 HOH 152 2152 2152 HOH HOH A . 
K 6 HOH 153 2153 2153 HOH HOH A . 
K 6 HOH 154 2154 2154 HOH HOH A . 
K 6 HOH 155 2155 2155 HOH HOH A . 
K 6 HOH 156 2156 2156 HOH HOH A . 
K 6 HOH 157 2157 2157 HOH HOH A . 
K 6 HOH 158 2158 2158 HOH HOH A . 
K 6 HOH 159 2159 2159 HOH HOH A . 
K 6 HOH 160 2160 2160 HOH HOH A . 
K 6 HOH 161 2161 2161 HOH HOH A . 
K 6 HOH 162 2162 2162 HOH HOH A . 
K 6 HOH 163 2163 2163 HOH HOH A . 
K 6 HOH 164 2164 2164 HOH HOH A . 
K 6 HOH 165 2165 2165 HOH HOH A . 
K 6 HOH 166 2166 2166 HOH HOH A . 
K 6 HOH 167 2167 2167 HOH HOH A . 
K 6 HOH 168 2168 2168 HOH HOH A . 
K 6 HOH 169 2169 2169 HOH HOH A . 
K 6 HOH 170 2170 2170 HOH HOH A . 
K 6 HOH 171 2171 2171 HOH HOH A . 
K 6 HOH 172 2172 2172 HOH HOH A . 
K 6 HOH 173 2173 2173 HOH HOH A . 
K 6 HOH 174 2174 2174 HOH HOH A . 
K 6 HOH 175 2175 2175 HOH HOH A . 
K 6 HOH 176 2176 2176 HOH HOH A . 
K 6 HOH 177 2177 2177 HOH HOH A . 
K 6 HOH 178 2178 2178 HOH HOH A . 
K 6 HOH 179 2179 2179 HOH HOH A . 
K 6 HOH 180 2180 2180 HOH HOH A . 
K 6 HOH 181 2181 2181 HOH HOH A . 
K 6 HOH 182 2182 2182 HOH HOH A . 
K 6 HOH 183 2183 2183 HOH HOH A . 
K 6 HOH 184 2184 2184 HOH HOH A . 
K 6 HOH 185 2185 2185 HOH HOH A . 
K 6 HOH 186 2186 2186 HOH HOH A . 
K 6 HOH 187 2187 2187 HOH HOH A . 
K 6 HOH 188 2188 2188 HOH HOH A . 
K 6 HOH 189 2189 2189 HOH HOH A . 
K 6 HOH 190 2190 2190 HOH HOH A . 
K 6 HOH 191 2191 2191 HOH HOH A . 
K 6 HOH 192 2192 2192 HOH HOH A . 
K 6 HOH 193 2193 2193 HOH HOH A . 
K 6 HOH 194 2194 2194 HOH HOH A . 
K 6 HOH 195 2195 2195 HOH HOH A . 
K 6 HOH 196 2196 2196 HOH HOH A . 
K 6 HOH 197 2197 2197 HOH HOH A . 
K 6 HOH 198 2198 2198 HOH HOH A . 
K 6 HOH 199 2199 2199 HOH HOH A . 
K 6 HOH 200 2200 2200 HOH HOH A . 
K 6 HOH 201 2201 2201 HOH HOH A . 
K 6 HOH 202 2202 2202 HOH HOH A . 
K 6 HOH 203 2203 2203 HOH HOH A . 
K 6 HOH 204 2204 2204 HOH HOH A . 
K 6 HOH 205 2205 2205 HOH HOH A . 
K 6 HOH 206 2206 2206 HOH HOH A . 
K 6 HOH 207 2207 2207 HOH HOH A . 
K 6 HOH 208 2208 2208 HOH HOH A . 
K 6 HOH 209 2209 2209 HOH HOH A . 
K 6 HOH 210 2210 2210 HOH HOH A . 
K 6 HOH 211 2211 2211 HOH HOH A . 
K 6 HOH 212 2212 2212 HOH HOH A . 
K 6 HOH 213 2213 2213 HOH HOH A . 
K 6 HOH 214 2214 2214 HOH HOH A . 
K 6 HOH 215 2215 2215 HOH HOH A . 
K 6 HOH 216 2216 2216 HOH HOH A . 
K 6 HOH 217 2217 2217 HOH HOH A . 
K 6 HOH 218 2218 2218 HOH HOH A . 
K 6 HOH 219 2219 2219 HOH HOH A . 
K 6 HOH 220 2220 2220 HOH HOH A . 
K 6 HOH 221 2221 2221 HOH HOH A . 
K 6 HOH 222 2222 2222 HOH HOH A . 
K 6 HOH 223 2223 2223 HOH HOH A . 
K 6 HOH 224 2224 2224 HOH HOH A . 
K 6 HOH 225 2225 2225 HOH HOH A . 
K 6 HOH 226 2226 2226 HOH HOH A . 
K 6 HOH 227 2227 2227 HOH HOH A . 
K 6 HOH 228 2228 2228 HOH HOH A . 
K 6 HOH 229 2229 2229 HOH HOH A . 
K 6 HOH 230 2230 2230 HOH HOH A . 
K 6 HOH 231 2231 2231 HOH HOH A . 
K 6 HOH 232 2232 2232 HOH HOH A . 
K 6 HOH 233 2233 2233 HOH HOH A . 
K 6 HOH 234 2234 2234 HOH HOH A . 
K 6 HOH 235 2235 2235 HOH HOH A . 
K 6 HOH 236 2236 2236 HOH HOH A . 
K 6 HOH 237 2237 2237 HOH HOH A . 
K 6 HOH 238 2238 2238 HOH HOH A . 
K 6 HOH 239 2239 2239 HOH HOH A . 
K 6 HOH 240 2240 2240 HOH HOH A . 
K 6 HOH 241 2241 2241 HOH HOH A . 
K 6 HOH 242 2242 2242 HOH HOH A . 
K 6 HOH 243 2243 2243 HOH HOH A . 
K 6 HOH 244 2244 2244 HOH HOH A . 
K 6 HOH 245 2245 2245 HOH HOH A . 
K 6 HOH 246 2246 2246 HOH HOH A . 
K 6 HOH 247 2247 2247 HOH HOH A . 
K 6 HOH 248 2248 2248 HOH HOH A . 
K 6 HOH 249 2249 2249 HOH HOH A . 
K 6 HOH 250 2250 2250 HOH HOH A . 
K 6 HOH 251 2251 2251 HOH HOH A . 
K 6 HOH 252 2252 2252 HOH HOH A . 
K 6 HOH 253 2253 2253 HOH HOH A . 
K 6 HOH 254 2254 2254 HOH HOH A . 
K 6 HOH 255 2255 2255 HOH HOH A . 
K 6 HOH 256 2256 2256 HOH HOH A . 
K 6 HOH 257 2257 2257 HOH HOH A . 
K 6 HOH 258 2258 2258 HOH HOH A . 
K 6 HOH 259 2259 2259 HOH HOH A . 
K 6 HOH 260 2260 2260 HOH HOH A . 
K 6 HOH 261 2261 2261 HOH HOH A . 
K 6 HOH 262 2262 2262 HOH HOH A . 
K 6 HOH 263 2263 2263 HOH HOH A . 
K 6 HOH 264 2264 2264 HOH HOH A . 
K 6 HOH 265 2265 2265 HOH HOH A . 
K 6 HOH 266 2266 2266 HOH HOH A . 
K 6 HOH 267 2267 2267 HOH HOH A . 
L 6 HOH 1   2001 2001 HOH HOH F . 
L 6 HOH 2   2002 2002 HOH HOH F . 
L 6 HOH 3   2003 2003 HOH HOH F . 
L 6 HOH 4   2004 2004 HOH HOH F . 
L 6 HOH 5   2005 2005 HOH HOH F . 
L 6 HOH 6   2006 2006 HOH HOH F . 
L 6 HOH 7   2007 2007 HOH HOH F . 
L 6 HOH 8   2008 2008 HOH HOH F . 
L 6 HOH 9   2009 2009 HOH HOH F . 
L 6 HOH 10  2010 2010 HOH HOH F . 
L 6 HOH 11  2011 2011 HOH HOH F . 
L 6 HOH 12  2012 2012 HOH HOH F . 
L 6 HOH 13  2013 2013 HOH HOH F . 
L 6 HOH 14  2014 2014 HOH HOH F . 
L 6 HOH 15  2015 2015 HOH HOH F . 
L 6 HOH 16  2016 2016 HOH HOH F . 
L 6 HOH 17  2017 2017 HOH HOH F . 
L 6 HOH 18  2018 2018 HOH HOH F . 
L 6 HOH 19  2019 2019 HOH HOH F . 
L 6 HOH 20  2020 2020 HOH HOH F . 
L 6 HOH 21  2021 2021 HOH HOH F . 
L 6 HOH 22  2022 2022 HOH HOH F . 
L 6 HOH 23  2023 2023 HOH HOH F . 
L 6 HOH 24  2024 2024 HOH HOH F . 
L 6 HOH 25  2025 2025 HOH HOH F . 
L 6 HOH 26  2026 2026 HOH HOH F . 
L 6 HOH 27  2027 2027 HOH HOH F . 
L 6 HOH 28  2028 2028 HOH HOH F . 
L 6 HOH 29  2029 2029 HOH HOH F . 
L 6 HOH 30  2030 2030 HOH HOH F . 
L 6 HOH 31  2031 2031 HOH HOH F . 
L 6 HOH 32  2032 2032 HOH HOH F . 
L 6 HOH 33  2033 2033 HOH HOH F . 
L 6 HOH 34  2034 2034 HOH HOH F . 
L 6 HOH 35  2035 2035 HOH HOH F . 
L 6 HOH 36  2036 2036 HOH HOH F . 
L 6 HOH 37  2037 2037 HOH HOH F . 
L 6 HOH 38  2038 2038 HOH HOH F . 
L 6 HOH 39  2039 2039 HOH HOH F . 
L 6 HOH 40  2040 2040 HOH HOH F . 
L 6 HOH 41  2041 2041 HOH HOH F . 
L 6 HOH 42  2042 2042 HOH HOH F . 
L 6 HOH 43  2043 2043 HOH HOH F . 
L 6 HOH 44  2044 2044 HOH HOH F . 
L 6 HOH 45  2045 2045 HOH HOH F . 
L 6 HOH 46  2046 2046 HOH HOH F . 
L 6 HOH 47  2047 2047 HOH HOH F . 
L 6 HOH 48  2048 2048 HOH HOH F . 
L 6 HOH 49  2049 2049 HOH HOH F . 
L 6 HOH 50  2050 2050 HOH HOH F . 
L 6 HOH 51  2051 2051 HOH HOH F . 
L 6 HOH 52  2052 2052 HOH HOH F . 
L 6 HOH 53  2053 2053 HOH HOH F . 
L 6 HOH 54  2054 2054 HOH HOH F . 
L 6 HOH 55  2055 2055 HOH HOH F . 
L 6 HOH 56  2056 2056 HOH HOH F . 
L 6 HOH 57  2057 2057 HOH HOH F . 
L 6 HOH 58  2058 2058 HOH HOH F . 
L 6 HOH 59  2059 2059 HOH HOH F . 
L 6 HOH 60  2060 2060 HOH HOH F . 
L 6 HOH 61  2061 2061 HOH HOH F . 
L 6 HOH 62  2062 2062 HOH HOH F . 
L 6 HOH 63  2063 2063 HOH HOH F . 
L 6 HOH 64  2064 2064 HOH HOH F . 
L 6 HOH 65  2065 2065 HOH HOH F . 
L 6 HOH 66  2066 2066 HOH HOH F . 
L 6 HOH 67  2067 2067 HOH HOH F . 
L 6 HOH 68  2068 2068 HOH HOH F . 
L 6 HOH 69  2069 2069 HOH HOH F . 
L 6 HOH 70  2070 2070 HOH HOH F . 
L 6 HOH 71  2071 2071 HOH HOH F . 
L 6 HOH 72  2072 2072 HOH HOH F . 
L 6 HOH 73  2073 2073 HOH HOH F . 
L 6 HOH 74  2074 2074 HOH HOH F . 
L 6 HOH 75  2075 2075 HOH HOH F . 
L 6 HOH 76  2076 2076 HOH HOH F . 
L 6 HOH 77  2077 2077 HOH HOH F . 
L 6 HOH 78  2078 2078 HOH HOH F . 
L 6 HOH 79  2079 2079 HOH HOH F . 
L 6 HOH 80  2080 2080 HOH HOH F . 
L 6 HOH 81  2081 2081 HOH HOH F . 
L 6 HOH 82  2082 2082 HOH HOH F . 
L 6 HOH 83  2083 2083 HOH HOH F . 
L 6 HOH 84  2084 2084 HOH HOH F . 
L 6 HOH 85  2085 2085 HOH HOH F . 
L 6 HOH 86  2086 2086 HOH HOH F . 
L 6 HOH 87  2087 2087 HOH HOH F . 
L 6 HOH 88  2088 2088 HOH HOH F . 
L 6 HOH 89  2089 2089 HOH HOH F . 
L 6 HOH 90  2090 2090 HOH HOH F . 
L 6 HOH 91  2091 2091 HOH HOH F . 
L 6 HOH 92  2092 2092 HOH HOH F . 
L 6 HOH 93  2093 2093 HOH HOH F . 
L 6 HOH 94  2094 2094 HOH HOH F . 
L 6 HOH 95  2095 2095 HOH HOH F . 
L 6 HOH 96  2096 2096 HOH HOH F . 
L 6 HOH 97  2097 2097 HOH HOH F . 
L 6 HOH 98  2098 2098 HOH HOH F . 
L 6 HOH 99  2099 2099 HOH HOH F . 
L 6 HOH 100 2100 2100 HOH HOH F . 
L 6 HOH 101 2101 2101 HOH HOH F . 
L 6 HOH 102 2102 2102 HOH HOH F . 
L 6 HOH 103 2103 2103 HOH HOH F . 
L 6 HOH 104 2104 2104 HOH HOH F . 
L 6 HOH 105 2105 2105 HOH HOH F . 
L 6 HOH 106 2106 2106 HOH HOH F . 
L 6 HOH 107 2107 2107 HOH HOH F . 
L 6 HOH 108 2108 2108 HOH HOH F . 
L 6 HOH 109 2109 2109 HOH HOH F . 
L 6 HOH 110 2110 2110 HOH HOH F . 
L 6 HOH 111 2111 2111 HOH HOH F . 
L 6 HOH 112 2112 2112 HOH HOH F . 
L 6 HOH 113 2113 2113 HOH HOH F . 
L 6 HOH 114 2114 2114 HOH HOH F . 
L 6 HOH 115 2115 2115 HOH HOH F . 
L 6 HOH 116 2116 2116 HOH HOH F . 
L 6 HOH 117 2117 2117 HOH HOH F . 
L 6 HOH 118 2118 2118 HOH HOH F . 
L 6 HOH 119 2119 2119 HOH HOH F . 
L 6 HOH 120 2120 2120 HOH HOH F . 
L 6 HOH 121 2121 2121 HOH HOH F . 
L 6 HOH 122 2122 2122 HOH HOH F . 
L 6 HOH 123 2123 2123 HOH HOH F . 
L 6 HOH 124 2124 2124 HOH HOH F . 
L 6 HOH 125 2125 2125 HOH HOH F . 
L 6 HOH 126 2126 2126 HOH HOH F . 
L 6 HOH 127 2127 2127 HOH HOH F . 
L 6 HOH 128 2128 2128 HOH HOH F . 
L 6 HOH 129 2129 2129 HOH HOH F . 
L 6 HOH 130 2130 2130 HOH HOH F . 
L 6 HOH 131 2131 2131 HOH HOH F . 
L 6 HOH 132 2132 2132 HOH HOH F . 
L 6 HOH 133 2133 2133 HOH HOH F . 
L 6 HOH 134 2134 2134 HOH HOH F . 
L 6 HOH 135 2135 2135 HOH HOH F . 
L 6 HOH 136 2136 2136 HOH HOH F . 
L 6 HOH 137 2137 2137 HOH HOH F . 
L 6 HOH 138 2138 2138 HOH HOH F . 
L 6 HOH 139 2139 2139 HOH HOH F . 
L 6 HOH 140 2140 2140 HOH HOH F . 
L 6 HOH 141 2141 2141 HOH HOH F . 
L 6 HOH 142 2142 2142 HOH HOH F . 
L 6 HOH 143 2143 2143 HOH HOH F . 
L 6 HOH 144 2144 2144 HOH HOH F . 
L 6 HOH 145 2145 2145 HOH HOH F . 
L 6 HOH 146 2146 2146 HOH HOH F . 
L 6 HOH 147 2147 2147 HOH HOH F . 
L 6 HOH 148 2148 2148 HOH HOH F . 
L 6 HOH 149 2149 2149 HOH HOH F . 
L 6 HOH 150 2150 2150 HOH HOH F . 
L 6 HOH 151 2151 2151 HOH HOH F . 
L 6 HOH 152 2152 2152 HOH HOH F . 
L 6 HOH 153 2153 2153 HOH HOH F . 
L 6 HOH 154 2154 2154 HOH HOH F . 
L 6 HOH 155 2155 2155 HOH HOH F . 
L 6 HOH 156 2156 2156 HOH HOH F . 
L 6 HOH 157 2157 2157 HOH HOH F . 
L 6 HOH 158 2158 2158 HOH HOH F . 
L 6 HOH 159 2159 2159 HOH HOH F . 
L 6 HOH 160 2160 2160 HOH HOH F . 
L 6 HOH 161 2161 2161 HOH HOH F . 
L 6 HOH 162 2162 2162 HOH HOH F . 
L 6 HOH 163 2163 2163 HOH HOH F . 
L 6 HOH 164 2164 2164 HOH HOH F . 
L 6 HOH 165 2165 2165 HOH HOH F . 
L 6 HOH 166 2166 2166 HOH HOH F . 
L 6 HOH 167 2167 2167 HOH HOH F . 
L 6 HOH 168 2168 2168 HOH HOH F . 
L 6 HOH 169 2169 2169 HOH HOH F . 
L 6 HOH 170 2170 2170 HOH HOH F . 
L 6 HOH 171 2171 2171 HOH HOH F . 
L 6 HOH 172 2172 2172 HOH HOH F . 
L 6 HOH 173 2173 2173 HOH HOH F . 
L 6 HOH 174 2174 2174 HOH HOH F . 
L 6 HOH 175 2175 2175 HOH HOH F . 
L 6 HOH 176 2176 2176 HOH HOH F . 
L 6 HOH 177 2177 2177 HOH HOH F . 
L 6 HOH 178 2178 2178 HOH HOH F . 
L 6 HOH 179 2179 2179 HOH HOH F . 
L 6 HOH 180 2180 2180 HOH HOH F . 
L 6 HOH 181 2181 2181 HOH HOH F . 
L 6 HOH 182 2182 2182 HOH HOH F . 
L 6 HOH 183 2183 2183 HOH HOH F . 
L 6 HOH 184 2184 2184 HOH HOH F . 
L 6 HOH 185 2185 2185 HOH HOH F . 
L 6 HOH 186 2186 2186 HOH HOH F . 
L 6 HOH 187 2187 2187 HOH HOH F . 
L 6 HOH 188 2188 2188 HOH HOH F . 
L 6 HOH 189 2189 2189 HOH HOH F . 
L 6 HOH 190 2190 2190 HOH HOH F . 
L 6 HOH 191 2191 2191 HOH HOH F . 
L 6 HOH 192 2192 2192 HOH HOH F . 
L 6 HOH 193 2193 2193 HOH HOH F . 
L 6 HOH 194 2194 2194 HOH HOH F . 
L 6 HOH 195 2195 2195 HOH HOH F . 
L 6 HOH 196 2196 2196 HOH HOH F . 
L 6 HOH 197 2197 2197 HOH HOH F . 
L 6 HOH 198 2198 2198 HOH HOH F . 
L 6 HOH 199 2199 2199 HOH HOH F . 
L 6 HOH 200 2200 2200 HOH HOH F . 
L 6 HOH 201 2201 2201 HOH HOH F . 
L 6 HOH 202 2202 2202 HOH HOH F . 
L 6 HOH 203 2203 2203 HOH HOH F . 
L 6 HOH 204 2204 2204 HOH HOH F . 
L 6 HOH 205 2205 2205 HOH HOH F . 
L 6 HOH 206 2206 2206 HOH HOH F . 
L 6 HOH 207 2207 2207 HOH HOH F . 
L 6 HOH 208 2208 2208 HOH HOH F . 
L 6 HOH 209 2209 2209 HOH HOH F . 
L 6 HOH 210 2210 2210 HOH HOH F . 
L 6 HOH 211 2211 2211 HOH HOH F . 
L 6 HOH 212 2212 2212 HOH HOH F . 
L 6 HOH 213 2213 2213 HOH HOH F . 
L 6 HOH 214 2214 2214 HOH HOH F . 
L 6 HOH 215 2215 2215 HOH HOH F . 
L 6 HOH 216 2216 2216 HOH HOH F . 
L 6 HOH 217 2217 2217 HOH HOH F . 
L 6 HOH 218 2218 2218 HOH HOH F . 
L 6 HOH 219 2219 2219 HOH HOH F . 
L 6 HOH 220 2220 2220 HOH HOH F . 
L 6 HOH 221 2221 2221 HOH HOH F . 
L 6 HOH 222 2222 2222 HOH HOH F . 
L 6 HOH 223 2223 2223 HOH HOH F . 
L 6 HOH 224 2224 2224 HOH HOH F . 
L 6 HOH 225 2225 2225 HOH HOH F . 
L 6 HOH 226 2226 2226 HOH HOH F . 
L 6 HOH 227 2227 2227 HOH HOH F . 
L 6 HOH 228 2228 2228 HOH HOH F . 
L 6 HOH 229 2229 2229 HOH HOH F . 
L 6 HOH 230 2230 2230 HOH HOH F . 
L 6 HOH 231 2231 2231 HOH HOH F . 
L 6 HOH 232 2232 2232 HOH HOH F . 
L 6 HOH 233 2233 2233 HOH HOH F . 
L 6 HOH 234 2234 2234 HOH HOH F . 
L 6 HOH 235 2235 2235 HOH HOH F . 
L 6 HOH 236 2236 2236 HOH HOH F . 
L 6 HOH 237 2237 2237 HOH HOH F . 
L 6 HOH 238 2238 2238 HOH HOH F . 
L 6 HOH 239 2239 2239 HOH HOH F . 
L 6 HOH 240 2240 2240 HOH HOH F . 
L 6 HOH 241 2241 2241 HOH HOH F . 
L 6 HOH 242 2242 2242 HOH HOH F . 
L 6 HOH 243 2243 2243 HOH HOH F . 
L 6 HOH 244 2244 2244 HOH HOH F . 
L 6 HOH 245 2245 2245 HOH HOH F . 
L 6 HOH 246 2246 2246 HOH HOH F . 
L 6 HOH 247 2247 2247 HOH HOH F . 
L 6 HOH 248 2248 2248 HOH HOH F . 
L 6 HOH 249 2249 2249 HOH HOH F . 
L 6 HOH 250 2250 2250 HOH HOH F . 
L 6 HOH 251 2251 2251 HOH HOH F . 
L 6 HOH 252 2252 2252 HOH HOH F . 
L 6 HOH 253 2253 2253 HOH HOH F . 
L 6 HOH 254 2254 2254 HOH HOH F . 
L 6 HOH 255 2255 2255 HOH HOH F . 
L 6 HOH 256 2256 2256 HOH HOH F . 
L 6 HOH 257 2257 2257 HOH HOH F . 
L 6 HOH 258 2258 2258 HOH HOH F . 
L 6 HOH 259 2259 2259 HOH HOH F . 
L 6 HOH 260 2260 2260 HOH HOH F . 
L 6 HOH 261 2261 2261 HOH HOH F . 
L 6 HOH 262 2262 2262 HOH HOH F . 
L 6 HOH 263 2263 2263 HOH HOH F . 
L 6 HOH 264 2264 2264 HOH HOH F . 
L 6 HOH 265 2265 2265 HOH HOH F . 
L 6 HOH 266 2266 2266 HOH HOH F . 
L 6 HOH 267 2267 2267 HOH HOH F . 
L 6 HOH 268 2268 2268 HOH HOH F . 
L 6 HOH 269 2269 2269 HOH HOH F . 
L 6 HOH 270 2270 2270 HOH HOH F . 
L 6 HOH 271 2271 2271 HOH HOH F . 
L 6 HOH 272 2272 2272 HOH HOH F . 
L 6 HOH 273 2273 2273 HOH HOH F . 
L 6 HOH 274 2274 2274 HOH HOH F . 
L 6 HOH 275 2275 2275 HOH HOH F . 
L 6 HOH 276 2276 2276 HOH HOH F . 
L 6 HOH 277 2277 2277 HOH HOH F . 
L 6 HOH 278 2278 2278 HOH HOH F . 
L 6 HOH 279 2279 2279 HOH HOH F . 
L 6 HOH 280 2280 2280 HOH HOH F . 
L 6 HOH 281 2281 2281 HOH HOH F . 
L 6 HOH 282 2282 2282 HOH HOH F . 
L 6 HOH 283 2283 2283 HOH HOH F . 
L 6 HOH 284 2284 2284 HOH HOH F . 
L 6 HOH 285 2285 2285 HOH HOH F . 
L 6 HOH 286 2286 2286 HOH HOH F . 
L 6 HOH 287 2287 2287 HOH HOH F . 
L 6 HOH 288 2288 2288 HOH HOH F . 
L 6 HOH 289 2289 2289 HOH HOH F . 
L 6 HOH 290 2290 2290 HOH HOH F . 
L 6 HOH 291 2291 2291 HOH HOH F . 
L 6 HOH 292 2292 2292 HOH HOH F . 
L 6 HOH 293 2293 2293 HOH HOH F . 
L 6 HOH 294 2294 2294 HOH HOH F . 
L 6 HOH 295 2295 2295 HOH HOH F . 
L 6 HOH 296 2296 2296 HOH HOH F . 
L 6 HOH 297 2297 2297 HOH HOH F . 
L 6 HOH 298 2298 2298 HOH HOH F . 
L 6 HOH 299 2299 2299 HOH HOH F . 
L 6 HOH 300 2300 2300 HOH HOH F . 
L 6 HOH 301 2301 2301 HOH HOH F . 
L 6 HOH 302 2302 2302 HOH HOH F . 
L 6 HOH 303 2303 2303 HOH HOH F . 
L 6 HOH 304 2304 2304 HOH HOH F . 
L 6 HOH 305 2305 2305 HOH HOH F . 
L 6 HOH 306 2306 2306 HOH HOH F . 
L 6 HOH 307 2307 2307 HOH HOH F . 
L 6 HOH 308 2308 2308 HOH HOH F . 
L 6 HOH 309 2309 2309 HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PQS 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU A C CU . ? A CU 1154 ? 1_555 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 100.4 ? 
2  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU A C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 119.5 ? 
3  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU A C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 138.5 ? 
4  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 96.0  ? 
5  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 144.9 ? 
6  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 97.4  ? 
7  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 94.2  ? 
8  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 121.6 ? 
9  NE2 ? A HIS 63  ? A HIS 63  ? 1_555 CU B C CU . ? A CU 1154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 105.8 ? 
10 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 113.7 ? 
11 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 98.6  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 119.6 ? 
13 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 108.0 ? 
14 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 111.8 ? 
15 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 1155 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 103.8 ? 
16 NE2 ? B HIS 63  ? F HIS 63  ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 148.1 ? 
17 NE2 ? B HIS 63  ? F HIS 63  ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 94.8  ? 
18 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 97.6  ? 
19 NE2 ? B HIS 63  ? F HIS 63  ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 104.0 ? 
20 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 95.3  ? 
21 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 CU B H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 119.2 ? 
22 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU A H CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 100.1 ? 
23 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU A H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 120.7 ? 
24 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 CU A H CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 138.9 ? 
25 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 124.8 ? 
26 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 97.5  ? 
27 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 113.5 ? 
28 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 105.9 ? 
29 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 109.2 ? 
30 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 ZN ? I ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 103.7 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-06-19 
2 'Structure model' 1 1 2011-05-08 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
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' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.2.0005 ? 1 
HKL-2000 'data reduction' .        ? 2 
HKL-2000 'data scaling'   .        ? 3 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE2 A GLU 133  ? ? O A HOH 2226 ? ? 1.16 
2  1 O   A HOH 2107 ? ? O A HOH 2111 ? ? 1.64 
3  1 O   F GLY 10   ? A O F HOH 2029 ? ? 1.65 
4  1 NZ  A LYS 23   ? ? O A HOH 2038 ? ? 1.98 
5  1 CG2 F THR 135  ? B O F HOH 2173 ? ? 1.99 
6  1 NZ  A LYS 75   ? A O A HOH 2128 ? ? 2.04 
7  1 OD2 A ASP 92   ? A O A HOH 2162 ? ? 2.05 
8  1 ND2 F ASN 53   ? A O F HOH 2131 ? ? 2.05 
9  1 N   F ASP 11   ? B O F HOH 2033 ? ? 2.06 
10 1 CG  A GLN 153  ? ? O A HOH 2246 ? ? 2.07 
11 1 CD  A GLN 153  ? ? O A HOH 2246 ? ? 2.16 
12 1 OD1 A ASP 109  ? A O A HOH 2191 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 2111 ? ? 1_555 O F HOH 2197 ? ? 2_645 1.61 
2 1 CD1 A ILE 17   ? A 1_555 O A HOH 2213 ? ? 2_656 1.93 
3 1 CD1 F ILE 17   ? ? 1_555 O F HOH 2261 ? ? 2_645 2.09 
4 1 O   A HOH 2213 ? ? 1_555 O F HOH 2138 ? ? 2_646 2.15 
5 1 O   A HOH 2200 ? ? 1_555 O A HOH 2253 ? ? 2_646 2.18 
6 1 O   A HOH 2060 ? ? 1_555 O F HOH 2273 ? ? 2_646 2.18 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A ASN 53 ? ? CG A ASN 53 ? B 1.674 1.506 0.168 0.023 N 
2 1 CB F ASN 53 ? ? CG F ASN 53 ? A 1.713 1.506 0.207 0.023 N 
# 
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 CB A PHE 64 ? ? CG A PHE 64 ? ? CD2 A PHE 64 ? ? 115.25 120.80 -5.55  0.70 N 
2 1 CB A PHE 64 ? ? CG A PHE 64 ? ? CD1 A PHE 64 ? ? 125.78 120.80 4.98   0.70 N 
3 1 CB A ASP 90 ? ? CG A ASP 90 ? B OD1 A ASP 90 ? B 125.14 118.30 6.84   0.90 N 
4 1 CA F LYS 9  ? ? C  F LYS 9  ? ? N   F GLY 10 ? A 103.08 116.20 -13.12 2.00 Y 
5 1 O  F LYS 9  ? ? C  F LYS 9  ? ? N   F GLY 10 ? B 111.03 123.20 -12.17 1.70 Y 
6 1 CA F LEU 42 ? ? CB F LEU 42 ? ? CG  F LEU 42 ? A 129.16 115.30 13.86  2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 65  ? ? -147.25 59.90  
2 1 LYS A 136 ? ? -121.76 -54.64 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    12 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    13 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   B 
_pdbx_validate_peptide_omega.omega            -141.51 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 CYS A 111 ? ? -11.28 
2 1 LYS F 9   ? ? 10.78  
3 1 LYS F 9   ? ? -16.36 
4 1 GLY F 12  ? B 11.11  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2013 ? 6.67 . 
2 1 O ? F HOH 2006 ? 6.01 . 
3 1 O ? F HOH 2008 ? 8.02 . 
4 1 O ? F HOH 2017 ? 7.29 . 
5 1 O ? F HOH 2019 ? 5.89 . 
6 1 O ? F HOH 2040 ? 5.91 . 
7 1 O ? F HOH 2051 ? 6.34 . 
8 1 O ? F HOH 2064 ? 6.04 . 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 'ZINC ION'        ZN  
4 'SULFATE ION'     SO4 
5 'ACETATE ION'     ACT 
6 water             HOH 
# 
